data_8YOX
# 
_entry.id   8YOX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YOX         pdb_00008yox 10.2210/pdb8yox/pdb 
WWPDB D_1300046053 ?            ?                   
# 
_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       2025-01-08 
# 
_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                        8YOX 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wfeng@bit.edu.cn 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9403-4337 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lan, H.Y.'   1 ? 
'Gao, Y.'     2 ? 
'Hong, T.'    3 ? 
'Zhao, Z.Z.'  4 ? 
'Chang, Z.H.' 5 ? 
'Wang, Y.F.'  6 ? 
'Wang, F.'    7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Discov' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2056-5968 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                88 
_citation.page_last                 88 
_citation.title                     'Structural insight into 6-OH-FAD-dependent activation of hFSP1 for ferroptosis suppression.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41421-024-00723-7 
_citation.pdbx_database_id_PubMed   39160155 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lan, H.'   1 0009-0009-6083-0704 
primary 'Gao, Y.'   2 ?                   
primary 'Hong, T.'  3 ?                   
primary 'Chang, Z.' 4 ?                   
primary 'Zhao, Z.'  5 ?                   
primary 'Wang, Y.'  6 ?                   
primary 'Wang, F.'  7 ?                   
# 
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 'Ferroptosis suppressor protein 1'      40035.066 1  1.6.5.- ? ? ? 
2 non-polymer syn '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE' 801.549   1  ?       ? ? ? 
3 non-polymer syn 'SULFATE ION'                           96.063    1  ?       ? ? ? 
4 water       nat water                                   18.015    33 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'FSP1,Apoptosis-inducing factor homologous mitochondrion-associated inducer of death,AMID,p53-responsive gene 3 protein' 
# 
_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       
;PHMGALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGID
LKNQMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYP
EKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIK
INSSAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGAL
TFLLSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PHMGALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGID
LKNQMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYP
EKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIK
INSSAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGAL
TFLLSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE' 6FA 
3 'SULFATE ION'                           SO4 
4 water                                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   HIS n 
1 3   MET n 
1 4   GLY n 
1 5   ALA n 
1 6   LEU n 
1 7   HIS n 
1 8   VAL n 
1 9   VAL n 
1 10  ILE n 
1 11  VAL n 
1 12  GLY n 
1 13  GLY n 
1 14  GLY n 
1 15  PHE n 
1 16  GLY n 
1 17  GLY n 
1 18  ILE n 
1 19  ALA n 
1 20  ALA n 
1 21  ALA n 
1 22  SER n 
1 23  GLN n 
1 24  LEU n 
1 25  GLN n 
1 26  ALA n 
1 27  LEU n 
1 28  ASN n 
1 29  VAL n 
1 30  PRO n 
1 31  PHE n 
1 32  MET n 
1 33  LEU n 
1 34  VAL n 
1 35  ASP n 
1 36  MET n 
1 37  LYS n 
1 38  ASP n 
1 39  SER n 
1 40  PHE n 
1 41  HIS n 
1 42  HIS n 
1 43  ASN n 
1 44  VAL n 
1 45  ALA n 
1 46  ALA n 
1 47  LEU n 
1 48  ARG n 
1 49  ALA n 
1 50  SER n 
1 51  VAL n 
1 52  GLU n 
1 53  THR n 
1 54  GLY n 
1 55  PHE n 
1 56  ALA n 
1 57  LYS n 
1 58  LYS n 
1 59  THR n 
1 60  PHE n 
1 61  ILE n 
1 62  SER n 
1 63  TYR n 
1 64  SER n 
1 65  VAL n 
1 66  THR n 
1 67  PHE n 
1 68  LYS n 
1 69  ASP n 
1 70  ASN n 
1 71  PHE n 
1 72  ARG n 
1 73  GLN n 
1 74  GLY n 
1 75  LEU n 
1 76  VAL n 
1 77  VAL n 
1 78  GLY n 
1 79  ILE n 
1 80  ASP n 
1 81  LEU n 
1 82  LYS n 
1 83  ASN n 
1 84  GLN n 
1 85  MET n 
1 86  VAL n 
1 87  LEU n 
1 88  LEU n 
1 89  GLN n 
1 90  GLY n 
1 91  GLY n 
1 92  GLU n 
1 93  ALA n 
1 94  LEU n 
1 95  PRO n 
1 96  PHE n 
1 97  SER n 
1 98  HIS n 
1 99  LEU n 
1 100 ILE n 
1 101 LEU n 
1 102 ALA n 
1 103 THR n 
1 104 GLY n 
1 105 SER n 
1 106 THR n 
1 107 GLY n 
1 108 PRO n 
1 109 PHE n 
1 110 PRO n 
1 111 GLY n 
1 112 LYS n 
1 113 PHE n 
1 114 ASN n 
1 115 GLU n 
1 116 VAL n 
1 117 SER n 
1 118 SER n 
1 119 GLN n 
1 120 GLN n 
1 121 ALA n 
1 122 ALA n 
1 123 ILE n 
1 124 GLN n 
1 125 ALA n 
1 126 TYR n 
1 127 GLU n 
1 128 ASP n 
1 129 MET n 
1 130 VAL n 
1 131 ARG n 
1 132 GLN n 
1 133 VAL n 
1 134 GLN n 
1 135 ARG n 
1 136 SER n 
1 137 ARG n 
1 138 PHE n 
1 139 ILE n 
1 140 VAL n 
1 141 VAL n 
1 142 VAL n 
1 143 GLY n 
1 144 GLY n 
1 145 GLY n 
1 146 SER n 
1 147 ALA n 
1 148 GLY n 
1 149 VAL n 
1 150 GLU n 
1 151 MET n 
1 152 ALA n 
1 153 ALA n 
1 154 GLU n 
1 155 ILE n 
1 156 LYS n 
1 157 THR n 
1 158 GLU n 
1 159 TYR n 
1 160 PRO n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 VAL n 
1 165 THR n 
1 166 LEU n 
1 167 ILE n 
1 168 HIS n 
1 169 SER n 
1 170 GLN n 
1 171 VAL n 
1 172 ALA n 
1 173 LEU n 
1 174 ALA n 
1 175 ASP n 
1 176 LYS n 
1 177 GLU n 
1 178 LEU n 
1 179 LEU n 
1 180 PRO n 
1 181 SER n 
1 182 VAL n 
1 183 ARG n 
1 184 GLN n 
1 185 GLU n 
1 186 VAL n 
1 187 LYS n 
1 188 GLU n 
1 189 ILE n 
1 190 LEU n 
1 191 LEU n 
1 192 ARG n 
1 193 LYS n 
1 194 GLY n 
1 195 VAL n 
1 196 GLN n 
1 197 LEU n 
1 198 LEU n 
1 199 LEU n 
1 200 SER n 
1 201 GLU n 
1 202 ARG n 
1 203 VAL n 
1 204 SER n 
1 205 ASN n 
1 206 LEU n 
1 207 GLU n 
1 208 GLU n 
1 209 LEU n 
1 210 PRO n 
1 211 LEU n 
1 212 ASN n 
1 213 GLU n 
1 214 TYR n 
1 215 ARG n 
1 216 GLU n 
1 217 TYR n 
1 218 ILE n 
1 219 LYS n 
1 220 VAL n 
1 221 GLN n 
1 222 THR n 
1 223 ASP n 
1 224 LYS n 
1 225 GLY n 
1 226 THR n 
1 227 GLU n 
1 228 VAL n 
1 229 ALA n 
1 230 THR n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ILE n 
1 235 LEU n 
1 236 CYS n 
1 237 THR n 
1 238 GLY n 
1 239 ILE n 
1 240 LYS n 
1 241 ILE n 
1 242 ASN n 
1 243 SER n 
1 244 SER n 
1 245 ALA n 
1 246 TYR n 
1 247 ARG n 
1 248 LYS n 
1 249 ALA n 
1 250 PHE n 
1 251 GLU n 
1 252 SER n 
1 253 ARG n 
1 254 LEU n 
1 255 ALA n 
1 256 SER n 
1 257 SER n 
1 258 GLY n 
1 259 ALA n 
1 260 LEU n 
1 261 ARG n 
1 262 VAL n 
1 263 ASN n 
1 264 GLU n 
1 265 HIS n 
1 266 LEU n 
1 267 GLN n 
1 268 VAL n 
1 269 GLU n 
1 270 GLY n 
1 271 HIS n 
1 272 SER n 
1 273 ASN n 
1 274 VAL n 
1 275 TYR n 
1 276 ALA n 
1 277 ILE n 
1 278 GLY n 
1 279 ASP n 
1 280 CYS n 
1 281 ALA n 
1 282 ASP n 
1 283 VAL n 
1 284 ARG n 
1 285 THR n 
1 286 PRO n 
1 287 LYS n 
1 288 MET n 
1 289 ALA n 
1 290 TYR n 
1 291 LEU n 
1 292 ALA n 
1 293 GLY n 
1 294 LEU n 
1 295 HIS n 
1 296 ALA n 
1 297 ASN n 
1 298 ILE n 
1 299 ALA n 
1 300 VAL n 
1 301 ALA n 
1 302 ASN n 
1 303 ILE n 
1 304 VAL n 
1 305 ASN n 
1 306 SER n 
1 307 VAL n 
1 308 LYS n 
1 309 GLN n 
1 310 ARG n 
1 311 PRO n 
1 312 LEU n 
1 313 GLN n 
1 314 ALA n 
1 315 TYR n 
1 316 LYS n 
1 317 PRO n 
1 318 GLY n 
1 319 ALA n 
1 320 LEU n 
1 321 THR n 
1 322 PHE n 
1 323 LEU n 
1 324 LEU n 
1 325 SER n 
1 326 MET n 
1 327 GLY n 
1 328 ARG n 
1 329 ASN n 
1 330 ASP n 
1 331 GLY n 
1 332 VAL n 
1 333 GLY n 
1 334 GLN n 
1 335 ILE n 
1 336 SER n 
1 337 GLY n 
1 338 PHE n 
1 339 TYR n 
1 340 VAL n 
1 341 GLY n 
1 342 ARG n 
1 343 LEU n 
1 344 MET n 
1 345 VAL n 
1 346 ARG n 
1 347 LEU n 
1 348 THR n 
1 349 LYS n 
1 350 SER n 
1 351 ARG n 
1 352 ASP n 
1 353 LEU n 
1 354 PHE n 
1 355 VAL n 
1 356 SER n 
1 357 THR n 
1 358 SER n 
1 359 TRP n 
1 360 LYS n 
1 361 THR n 
1 362 MET n 
1 363 ARG n 
1 364 GLN n 
1 365 SER n 
1 366 PRO n 
1 367 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                   367 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'AIFM2, AMID, PRG3' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
6FA non-polymer         . '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O16 P2' 801.549 
ALA 'L-peptide linking' y ALANINE                                 ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                              ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                         ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                               ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                         ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                 ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                               ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                   ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                              ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                 ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                  ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                              ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                           ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                 ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                  ? 'C3 H7 N O3'        105.093 
SO4 non-polymer         . 'SULFATE ION'                           ? 'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                               ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                              ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                  ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   PRO 1   7   7   PRO PRO A . n 
A 1 2   HIS 2   8   8   HIS HIS A . n 
A 1 3   MET 3   9   9   MET MET A . n 
A 1 4   GLY 4   10  10  GLY GLY A . n 
A 1 5   ALA 5   11  11  ALA ALA A . n 
A 1 6   LEU 6   12  12  LEU LEU A . n 
A 1 7   HIS 7   13  13  HIS HIS A . n 
A 1 8   VAL 8   14  14  VAL VAL A . n 
A 1 9   VAL 9   15  15  VAL VAL A . n 
A 1 10  ILE 10  16  16  ILE ILE A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  GLY 12  18  18  GLY GLY A . n 
A 1 13  GLY 13  19  19  GLY GLY A . n 
A 1 14  GLY 14  20  20  GLY GLY A . n 
A 1 15  PHE 15  21  21  PHE PHE A . n 
A 1 16  GLY 16  22  22  GLY GLY A . n 
A 1 17  GLY 17  23  23  GLY GLY A . n 
A 1 18  ILE 18  24  24  ILE ILE A . n 
A 1 19  ALA 19  25  25  ALA ALA A . n 
A 1 20  ALA 20  26  26  ALA ALA A . n 
A 1 21  ALA 21  27  27  ALA ALA A . n 
A 1 22  SER 22  28  28  SER SER A . n 
A 1 23  GLN 23  29  29  GLN GLN A . n 
A 1 24  LEU 24  30  30  LEU LEU A . n 
A 1 25  GLN 25  31  31  GLN GLN A . n 
A 1 26  ALA 26  32  32  ALA ALA A . n 
A 1 27  LEU 27  33  33  LEU LEU A . n 
A 1 28  ASN 28  34  34  ASN ASN A . n 
A 1 29  VAL 29  35  35  VAL VAL A . n 
A 1 30  PRO 30  36  36  PRO PRO A . n 
A 1 31  PHE 31  37  37  PHE PHE A . n 
A 1 32  MET 32  38  38  MET MET A . n 
A 1 33  LEU 33  39  39  LEU LEU A . n 
A 1 34  VAL 34  40  40  VAL VAL A . n 
A 1 35  ASP 35  41  41  ASP ASP A . n 
A 1 36  MET 36  42  42  MET MET A . n 
A 1 37  LYS 37  43  43  LYS LYS A . n 
A 1 38  ASP 38  44  44  ASP ASP A . n 
A 1 39  SER 39  45  45  SER SER A . n 
A 1 40  PHE 40  46  46  PHE PHE A . n 
A 1 41  HIS 41  47  47  HIS HIS A . n 
A 1 42  HIS 42  48  48  HIS HIS A . n 
A 1 43  ASN 43  49  49  ASN ASN A . n 
A 1 44  VAL 44  50  50  VAL VAL A . n 
A 1 45  ALA 45  51  51  ALA ALA A . n 
A 1 46  ALA 46  52  52  ALA ALA A . n 
A 1 47  LEU 47  53  53  LEU LEU A . n 
A 1 48  ARG 48  54  54  ARG ARG A . n 
A 1 49  ALA 49  55  55  ALA ALA A . n 
A 1 50  SER 50  56  56  SER SER A . n 
A 1 51  VAL 51  57  57  VAL VAL A . n 
A 1 52  GLU 52  58  58  GLU GLU A . n 
A 1 53  THR 53  59  59  THR THR A . n 
A 1 54  GLY 54  60  60  GLY GLY A . n 
A 1 55  PHE 55  61  61  PHE PHE A . n 
A 1 56  ALA 56  62  62  ALA ALA A . n 
A 1 57  LYS 57  63  63  LYS LYS A . n 
A 1 58  LYS 58  64  64  LYS LYS A . n 
A 1 59  THR 59  65  65  THR THR A . n 
A 1 60  PHE 60  66  66  PHE PHE A . n 
A 1 61  ILE 61  67  67  ILE ILE A . n 
A 1 62  SER 62  68  68  SER SER A . n 
A 1 63  TYR 63  69  69  TYR TYR A . n 
A 1 64  SER 64  70  70  SER SER A . n 
A 1 65  VAL 65  71  71  VAL VAL A . n 
A 1 66  THR 66  72  72  THR THR A . n 
A 1 67  PHE 67  73  73  PHE PHE A . n 
A 1 68  LYS 68  74  74  LYS LYS A . n 
A 1 69  ASP 69  75  75  ASP ASP A . n 
A 1 70  ASN 70  76  76  ASN ASN A . n 
A 1 71  PHE 71  77  77  PHE PHE A . n 
A 1 72  ARG 72  78  78  ARG ARG A . n 
A 1 73  GLN 73  79  79  GLN GLN A . n 
A 1 74  GLY 74  80  80  GLY GLY A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  VAL 76  82  82  VAL VAL A . n 
A 1 77  VAL 77  83  83  VAL VAL A . n 
A 1 78  GLY 78  84  84  GLY GLY A . n 
A 1 79  ILE 79  85  85  ILE ILE A . n 
A 1 80  ASP 80  86  86  ASP ASP A . n 
A 1 81  LEU 81  87  87  LEU LEU A . n 
A 1 82  LYS 82  88  88  LYS LYS A . n 
A 1 83  ASN 83  89  89  ASN ASN A . n 
A 1 84  GLN 84  90  90  GLN GLN A . n 
A 1 85  MET 85  91  91  MET MET A . n 
A 1 86  VAL 86  92  92  VAL VAL A . n 
A 1 87  LEU 87  93  93  LEU LEU A . n 
A 1 88  LEU 88  94  94  LEU LEU A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  GLY 90  96  96  GLY GLY A . n 
A 1 91  GLY 91  97  97  GLY GLY A . n 
A 1 92  GLU 92  98  98  GLU GLU A . n 
A 1 93  ALA 93  99  99  ALA ALA A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  PRO 95  101 101 PRO PRO A . n 
A 1 96  PHE 96  102 102 PHE PHE A . n 
A 1 97  SER 97  103 103 SER SER A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  LEU 99  105 105 LEU LEU A . n 
A 1 100 ILE 100 106 106 ILE ILE A . n 
A 1 101 LEU 101 107 107 LEU LEU A . n 
A 1 102 ALA 102 108 108 ALA ALA A . n 
A 1 103 THR 103 109 109 THR THR A . n 
A 1 104 GLY 104 110 110 GLY GLY A . n 
A 1 105 SER 105 111 111 SER SER A . n 
A 1 106 THR 106 112 112 THR THR A . n 
A 1 107 GLY 107 113 113 GLY GLY A . n 
A 1 108 PRO 108 114 114 PRO PRO A . n 
A 1 109 PHE 109 115 115 PHE PHE A . n 
A 1 110 PRO 110 116 116 PRO PRO A . n 
A 1 111 GLY 111 117 117 GLY GLY A . n 
A 1 112 LYS 112 118 118 LYS LYS A . n 
A 1 113 PHE 113 119 119 PHE PHE A . n 
A 1 114 ASN 114 120 120 ASN ASN A . n 
A 1 115 GLU 115 121 121 GLU GLU A . n 
A 1 116 VAL 116 122 122 VAL VAL A . n 
A 1 117 SER 117 123 123 SER SER A . n 
A 1 118 SER 118 124 124 SER SER A . n 
A 1 119 GLN 119 125 125 GLN GLN A . n 
A 1 120 GLN 120 126 126 GLN GLN A . n 
A 1 121 ALA 121 127 127 ALA ALA A . n 
A 1 122 ALA 122 128 128 ALA ALA A . n 
A 1 123 ILE 123 129 129 ILE ILE A . n 
A 1 124 GLN 124 130 130 GLN GLN A . n 
A 1 125 ALA 125 131 131 ALA ALA A . n 
A 1 126 TYR 126 132 132 TYR TYR A . n 
A 1 127 GLU 127 133 133 GLU GLU A . n 
A 1 128 ASP 128 134 134 ASP ASP A . n 
A 1 129 MET 129 135 135 MET MET A . n 
A 1 130 VAL 130 136 136 VAL VAL A . n 
A 1 131 ARG 131 137 137 ARG ARG A . n 
A 1 132 GLN 132 138 138 GLN GLN A . n 
A 1 133 VAL 133 139 139 VAL VAL A . n 
A 1 134 GLN 134 140 140 GLN GLN A . n 
A 1 135 ARG 135 141 141 ARG ARG A . n 
A 1 136 SER 136 142 142 SER SER A . n 
A 1 137 ARG 137 143 143 ARG ARG A . n 
A 1 138 PHE 138 144 144 PHE PHE A . n 
A 1 139 ILE 139 145 145 ILE ILE A . n 
A 1 140 VAL 140 146 146 VAL VAL A . n 
A 1 141 VAL 141 147 147 VAL VAL A . n 
A 1 142 VAL 142 148 148 VAL VAL A . n 
A 1 143 GLY 143 149 149 GLY GLY A . n 
A 1 144 GLY 144 150 150 GLY GLY A . n 
A 1 145 GLY 145 151 151 GLY GLY A . n 
A 1 146 SER 146 152 152 SER SER A . n 
A 1 147 ALA 147 153 153 ALA ALA A . n 
A 1 148 GLY 148 154 154 GLY GLY A . n 
A 1 149 VAL 149 155 155 VAL VAL A . n 
A 1 150 GLU 150 156 156 GLU GLU A . n 
A 1 151 MET 151 157 157 MET MET A . n 
A 1 152 ALA 152 158 158 ALA ALA A . n 
A 1 153 ALA 153 159 159 ALA ALA A . n 
A 1 154 GLU 154 160 160 GLU GLU A . n 
A 1 155 ILE 155 161 161 ILE ILE A . n 
A 1 156 LYS 156 162 162 LYS LYS A . n 
A 1 157 THR 157 163 163 THR THR A . n 
A 1 158 GLU 158 164 164 GLU GLU A . n 
A 1 159 TYR 159 165 165 TYR TYR A . n 
A 1 160 PRO 160 166 166 PRO PRO A . n 
A 1 161 GLU 161 167 167 GLU GLU A . n 
A 1 162 LYS 162 168 168 LYS LYS A . n 
A 1 163 GLU 163 169 169 GLU GLU A . n 
A 1 164 VAL 164 170 170 VAL VAL A . n 
A 1 165 THR 165 171 171 THR THR A . n 
A 1 166 LEU 166 172 172 LEU LEU A . n 
A 1 167 ILE 167 173 173 ILE ILE A . n 
A 1 168 HIS 168 174 174 HIS HIS A . n 
A 1 169 SER 169 175 175 SER SER A . n 
A 1 170 GLN 170 176 176 GLN GLN A . n 
A 1 171 VAL 171 177 177 VAL VAL A . n 
A 1 172 ALA 172 178 178 ALA ALA A . n 
A 1 173 LEU 173 179 179 LEU LEU A . n 
A 1 174 ALA 174 180 180 ALA ALA A . n 
A 1 175 ASP 175 181 181 ASP ASP A . n 
A 1 176 LYS 176 182 182 LYS LYS A . n 
A 1 177 GLU 177 183 183 GLU GLU A . n 
A 1 178 LEU 178 184 184 LEU LEU A . n 
A 1 179 LEU 179 185 185 LEU LEU A . n 
A 1 180 PRO 180 186 186 PRO PRO A . n 
A 1 181 SER 181 187 187 SER SER A . n 
A 1 182 VAL 182 188 188 VAL VAL A . n 
A 1 183 ARG 183 189 189 ARG ARG A . n 
A 1 184 GLN 184 190 190 GLN GLN A . n 
A 1 185 GLU 185 191 191 GLU GLU A . n 
A 1 186 VAL 186 192 192 VAL VAL A . n 
A 1 187 LYS 187 193 193 LYS LYS A . n 
A 1 188 GLU 188 194 194 GLU GLU A . n 
A 1 189 ILE 189 195 195 ILE ILE A . n 
A 1 190 LEU 190 196 196 LEU LEU A . n 
A 1 191 LEU 191 197 197 LEU LEU A . n 
A 1 192 ARG 192 198 198 ARG ARG A . n 
A 1 193 LYS 193 199 199 LYS LYS A . n 
A 1 194 GLY 194 200 200 GLY GLY A . n 
A 1 195 VAL 195 201 201 VAL VAL A . n 
A 1 196 GLN 196 202 202 GLN GLN A . n 
A 1 197 LEU 197 203 203 LEU LEU A . n 
A 1 198 LEU 198 204 204 LEU LEU A . n 
A 1 199 LEU 199 205 205 LEU LEU A . n 
A 1 200 SER 200 206 206 SER SER A . n 
A 1 201 GLU 201 207 207 GLU GLU A . n 
A 1 202 ARG 202 208 208 ARG ARG A . n 
A 1 203 VAL 203 209 209 VAL VAL A . n 
A 1 204 SER 204 210 210 SER SER A . n 
A 1 205 ASN 205 211 211 ASN ASN A . n 
A 1 206 LEU 206 212 212 LEU LEU A . n 
A 1 207 GLU 207 213 213 GLU GLU A . n 
A 1 208 GLU 208 214 214 GLU GLU A . n 
A 1 209 LEU 209 215 215 LEU LEU A . n 
A 1 210 PRO 210 216 216 PRO PRO A . n 
A 1 211 LEU 211 217 217 LEU LEU A . n 
A 1 212 ASN 212 218 218 ASN ASN A . n 
A 1 213 GLU 213 219 219 GLU GLU A . n 
A 1 214 TYR 214 220 220 TYR TYR A . n 
A 1 215 ARG 215 221 221 ARG ARG A . n 
A 1 216 GLU 216 222 222 GLU GLU A . n 
A 1 217 TYR 217 223 223 TYR TYR A . n 
A 1 218 ILE 218 224 224 ILE ILE A . n 
A 1 219 LYS 219 225 225 LYS LYS A . n 
A 1 220 VAL 220 226 226 VAL VAL A . n 
A 1 221 GLN 221 227 227 GLN GLN A . n 
A 1 222 THR 222 228 228 THR THR A . n 
A 1 223 ASP 223 229 229 ASP ASP A . n 
A 1 224 LYS 224 230 230 LYS LYS A . n 
A 1 225 GLY 225 231 231 GLY GLY A . n 
A 1 226 THR 226 232 232 THR THR A . n 
A 1 227 GLU 227 233 233 GLU GLU A . n 
A 1 228 VAL 228 234 234 VAL VAL A . n 
A 1 229 ALA 229 235 235 ALA ALA A . n 
A 1 230 THR 230 236 236 THR THR A . n 
A 1 231 ASN 231 237 237 ASN ASN A . n 
A 1 232 LEU 232 238 238 LEU LEU A . n 
A 1 233 VAL 233 239 239 VAL VAL A . n 
A 1 234 ILE 234 240 240 ILE ILE A . n 
A 1 235 LEU 235 241 241 LEU LEU A . n 
A 1 236 CYS 236 242 242 CYS CYS A . n 
A 1 237 THR 237 243 243 THR THR A . n 
A 1 238 GLY 238 244 244 GLY GLY A . n 
A 1 239 ILE 239 245 245 ILE ILE A . n 
A 1 240 LYS 240 246 246 LYS LYS A . n 
A 1 241 ILE 241 247 247 ILE ILE A . n 
A 1 242 ASN 242 248 248 ASN ASN A . n 
A 1 243 SER 243 249 249 SER SER A . n 
A 1 244 SER 244 250 250 SER SER A . n 
A 1 245 ALA 245 251 251 ALA ALA A . n 
A 1 246 TYR 246 252 252 TYR TYR A . n 
A 1 247 ARG 247 253 253 ARG ARG A . n 
A 1 248 LYS 248 254 254 LYS LYS A . n 
A 1 249 ALA 249 255 255 ALA ALA A . n 
A 1 250 PHE 250 256 256 PHE PHE A . n 
A 1 251 GLU 251 257 257 GLU GLU A . n 
A 1 252 SER 252 258 258 SER SER A . n 
A 1 253 ARG 253 259 259 ARG ARG A . n 
A 1 254 LEU 254 260 260 LEU LEU A . n 
A 1 255 ALA 255 261 261 ALA ALA A . n 
A 1 256 SER 256 262 262 SER SER A . n 
A 1 257 SER 257 263 263 SER SER A . n 
A 1 258 GLY 258 264 264 GLY GLY A . n 
A 1 259 ALA 259 265 265 ALA ALA A . n 
A 1 260 LEU 260 266 266 LEU LEU A . n 
A 1 261 ARG 261 267 267 ARG ARG A . n 
A 1 262 VAL 262 268 268 VAL VAL A . n 
A 1 263 ASN 263 269 269 ASN ASN A . n 
A 1 264 GLU 264 270 270 GLU GLU A . n 
A 1 265 HIS 265 271 271 HIS HIS A . n 
A 1 266 LEU 266 272 272 LEU LEU A . n 
A 1 267 GLN 267 273 273 GLN GLN A . n 
A 1 268 VAL 268 274 274 VAL VAL A . n 
A 1 269 GLU 269 275 275 GLU GLU A . n 
A 1 270 GLY 270 276 276 GLY GLY A . n 
A 1 271 HIS 271 277 277 HIS HIS A . n 
A 1 272 SER 272 278 278 SER SER A . n 
A 1 273 ASN 273 279 279 ASN ASN A . n 
A 1 274 VAL 274 280 280 VAL VAL A . n 
A 1 275 TYR 275 281 281 TYR TYR A . n 
A 1 276 ALA 276 282 282 ALA ALA A . n 
A 1 277 ILE 277 283 283 ILE ILE A . n 
A 1 278 GLY 278 284 284 GLY GLY A . n 
A 1 279 ASP 279 285 285 ASP ASP A . n 
A 1 280 CYS 280 286 286 CYS CYS A . n 
A 1 281 ALA 281 287 287 ALA ALA A . n 
A 1 282 ASP 282 288 288 ASP ASP A . n 
A 1 283 VAL 283 289 289 VAL VAL A . n 
A 1 284 ARG 284 290 290 ARG ARG A . n 
A 1 285 THR 285 291 291 THR THR A . n 
A 1 286 PRO 286 292 292 PRO PRO A . n 
A 1 287 LYS 287 293 293 LYS LYS A . n 
A 1 288 MET 288 294 294 MET MET A . n 
A 1 289 ALA 289 295 295 ALA ALA A . n 
A 1 290 TYR 290 296 296 TYR TYR A . n 
A 1 291 LEU 291 297 297 LEU LEU A . n 
A 1 292 ALA 292 298 298 ALA ALA A . n 
A 1 293 GLY 293 299 299 GLY GLY A . n 
A 1 294 LEU 294 300 300 LEU LEU A . n 
A 1 295 HIS 295 301 301 HIS HIS A . n 
A 1 296 ALA 296 302 302 ALA ALA A . n 
A 1 297 ASN 297 303 303 ASN ASN A . n 
A 1 298 ILE 298 304 304 ILE ILE A . n 
A 1 299 ALA 299 305 305 ALA ALA A . n 
A 1 300 VAL 300 306 306 VAL VAL A . n 
A 1 301 ALA 301 307 307 ALA ALA A . n 
A 1 302 ASN 302 308 308 ASN ASN A . n 
A 1 303 ILE 303 309 309 ILE ILE A . n 
A 1 304 VAL 304 310 310 VAL VAL A . n 
A 1 305 ASN 305 311 311 ASN ASN A . n 
A 1 306 SER 306 312 312 SER SER A . n 
A 1 307 VAL 307 313 313 VAL VAL A . n 
A 1 308 LYS 308 314 314 LYS LYS A . n 
A 1 309 GLN 309 315 315 GLN GLN A . n 
A 1 310 ARG 310 316 316 ARG ARG A . n 
A 1 311 PRO 311 317 317 PRO PRO A . n 
A 1 312 LEU 312 318 318 LEU LEU A . n 
A 1 313 GLN 313 319 319 GLN GLN A . n 
A 1 314 ALA 314 320 320 ALA ALA A . n 
A 1 315 TYR 315 321 321 TYR TYR A . n 
A 1 316 LYS 316 322 322 LYS LYS A . n 
A 1 317 PRO 317 323 323 PRO PRO A . n 
A 1 318 GLY 318 324 324 GLY GLY A . n 
A 1 319 ALA 319 325 325 ALA ALA A . n 
A 1 320 LEU 320 326 326 LEU LEU A . n 
A 1 321 THR 321 327 327 THR THR A . n 
A 1 322 PHE 322 328 328 PHE PHE A . n 
A 1 323 LEU 323 329 329 LEU LEU A . n 
A 1 324 LEU 324 330 330 LEU LEU A . n 
A 1 325 SER 325 331 331 SER SER A . n 
A 1 326 MET 326 332 332 MET MET A . n 
A 1 327 GLY 327 333 333 GLY GLY A . n 
A 1 328 ARG 328 334 334 ARG ARG A . n 
A 1 329 ASN 329 335 335 ASN ASN A . n 
A 1 330 ASP 330 336 336 ASP ASP A . n 
A 1 331 GLY 331 337 337 GLY GLY A . n 
A 1 332 VAL 332 338 338 VAL VAL A . n 
A 1 333 GLY 333 339 339 GLY GLY A . n 
A 1 334 GLN 334 340 340 GLN GLN A . n 
A 1 335 ILE 335 341 341 ILE ILE A . n 
A 1 336 SER 336 342 342 SER SER A . n 
A 1 337 GLY 337 343 343 GLY GLY A . n 
A 1 338 PHE 338 344 344 PHE PHE A . n 
A 1 339 TYR 339 345 345 TYR TYR A . n 
A 1 340 VAL 340 346 346 VAL VAL A . n 
A 1 341 GLY 341 347 347 GLY GLY A . n 
A 1 342 ARG 342 348 348 ARG ARG A . n 
A 1 343 LEU 343 349 349 LEU LEU A . n 
A 1 344 MET 344 350 350 MET MET A . n 
A 1 345 VAL 345 351 351 VAL VAL A . n 
A 1 346 ARG 346 352 352 ARG ARG A . n 
A 1 347 LEU 347 353 353 LEU LEU A . n 
A 1 348 THR 348 354 354 THR THR A . n 
A 1 349 LYS 349 355 355 LYS LYS A . n 
A 1 350 SER 350 356 356 SER SER A . n 
A 1 351 ARG 351 357 357 ARG ARG A . n 
A 1 352 ASP 352 358 358 ASP ASP A . n 
A 1 353 LEU 353 359 359 LEU LEU A . n 
A 1 354 PHE 354 360 360 PHE PHE A . n 
A 1 355 VAL 355 361 361 VAL VAL A . n 
A 1 356 SER 356 362 362 SER SER A . n 
A 1 357 THR 357 363 363 THR THR A . n 
A 1 358 SER 358 364 364 SER SER A . n 
A 1 359 TRP 359 365 365 TRP TRP A . n 
A 1 360 LYS 360 366 366 LYS LYS A . n 
A 1 361 THR 361 367 367 THR THR A . n 
A 1 362 MET 362 368 368 MET MET A . n 
A 1 363 ARG 363 369 369 ARG ARG A . n 
A 1 364 GLN 364 370 370 GLN GLN A . n 
A 1 365 SER 365 371 371 SER SER A . n 
A 1 366 PRO 366 372 372 PRO PRO A . n 
A 1 367 PRO 367 373 373 PRO PRO A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        6FA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   6FA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 6FA 1  401 401 6FA 6FA A . 
C 3 SO4 1  402 1   SO4 SO4 A . 
D 4 HOH 1  501 1   HOH HOH A . 
D 4 HOH 2  502 16  HOH HOH A . 
D 4 HOH 3  503 13  HOH HOH A . 
D 4 HOH 4  504 11  HOH HOH A . 
D 4 HOH 5  505 30  HOH HOH A . 
D 4 HOH 6  506 5   HOH HOH A . 
D 4 HOH 7  507 3   HOH HOH A . 
D 4 HOH 8  508 7   HOH HOH A . 
D 4 HOH 9  509 19  HOH HOH A . 
D 4 HOH 10 510 2   HOH HOH A . 
D 4 HOH 11 511 21  HOH HOH A . 
D 4 HOH 12 512 29  HOH HOH A . 
D 4 HOH 13 513 4   HOH HOH A . 
D 4 HOH 14 514 15  HOH HOH A . 
D 4 HOH 15 515 33  HOH HOH A . 
D 4 HOH 16 516 18  HOH HOH A . 
D 4 HOH 17 517 12  HOH HOH A . 
D 4 HOH 18 518 8   HOH HOH A . 
D 4 HOH 19 519 6   HOH HOH A . 
D 4 HOH 20 520 9   HOH HOH A . 
D 4 HOH 21 521 32  HOH HOH A . 
D 4 HOH 22 522 34  HOH HOH A . 
D 4 HOH 23 523 25  HOH HOH A . 
D 4 HOH 24 524 22  HOH HOH A . 
D 4 HOH 25 525 10  HOH HOH A . 
D 4 HOH 26 526 23  HOH HOH A . 
D 4 HOH 27 527 24  HOH HOH A . 
D 4 HOH 28 528 20  HOH HOH A . 
D 4 HOH 29 529 27  HOH HOH A . 
D 4 HOH 30 530 14  HOH HOH A . 
D 4 HOH 31 531 17  HOH HOH A . 
D 4 HOH 32 532 26  HOH HOH A . 
D 4 HOH 33 533 28  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 74  ? CE  ? A LYS 68  CE  
2  1 Y 1 A LYS 74  ? NZ  ? A LYS 68  NZ  
3  1 Y 1 A LYS 88  ? CG  ? A LYS 82  CG  
4  1 Y 1 A LYS 88  ? CD  ? A LYS 82  CD  
5  1 Y 1 A LYS 88  ? CE  ? A LYS 82  CE  
6  1 Y 1 A LYS 88  ? NZ  ? A LYS 82  NZ  
7  1 Y 1 A GLU 98  ? CG  ? A GLU 92  CG  
8  1 Y 1 A GLU 98  ? CD  ? A GLU 92  CD  
9  1 Y 1 A GLU 98  ? OE1 ? A GLU 92  OE1 
10 1 Y 1 A GLU 98  ? OE2 ? A GLU 92  OE2 
11 1 Y 1 A LYS 182 ? CD  ? A LYS 176 CD  
12 1 Y 1 A LYS 182 ? CE  ? A LYS 176 CE  
13 1 Y 1 A LYS 182 ? NZ  ? A LYS 176 NZ  
14 1 Y 1 A GLU 191 ? OE1 ? A GLU 185 OE1 
15 1 Y 1 A GLU 191 ? OE2 ? A GLU 185 OE2 
16 1 Y 1 A GLU 214 ? CG  ? A GLU 208 CG  
17 1 Y 1 A GLU 214 ? CD  ? A GLU 208 CD  
18 1 Y 1 A GLU 214 ? OE1 ? A GLU 208 OE1 
19 1 Y 1 A GLU 214 ? OE2 ? A GLU 208 OE2 
20 1 Y 1 A GLU 222 ? CG  ? A GLU 216 CG  
21 1 Y 1 A GLU 222 ? CD  ? A GLU 216 CD  
22 1 Y 1 A GLU 222 ? OE1 ? A GLU 216 OE1 
23 1 Y 1 A GLU 222 ? OE2 ? A GLU 216 OE2 
24 1 Y 1 A LYS 230 ? CG  ? A LYS 224 CG  
25 1 Y 1 A LYS 230 ? CD  ? A LYS 224 CD  
26 1 Y 1 A LYS 230 ? CE  ? A LYS 224 CE  
27 1 Y 1 A LYS 230 ? NZ  ? A LYS 224 NZ  
28 1 Y 1 A LYS 254 ? CD  ? A LYS 248 CD  
29 1 Y 1 A LYS 254 ? CE  ? A LYS 248 CE  
30 1 Y 1 A LYS 254 ? NZ  ? A LYS 248 NZ  
31 1 Y 1 A GLU 257 ? CG  ? A GLU 251 CG  
32 1 Y 1 A GLU 257 ? CD  ? A GLU 251 CD  
33 1 Y 1 A GLU 257 ? OE1 ? A GLU 251 OE1 
34 1 Y 1 A GLU 257 ? OE2 ? A GLU 251 OE2 
35 1 Y 1 A LEU 260 ? CG  ? A LEU 254 CG  
36 1 Y 1 A LEU 260 ? CD1 ? A LEU 254 CD1 
37 1 Y 1 A LEU 260 ? CD2 ? A LEU 254 CD2 
38 1 Y 1 A SER 262 ? OG  ? A SER 256 OG  
39 1 Y 1 A ASP 288 ? CG  ? A ASP 282 CG  
40 1 Y 1 A ASP 288 ? OD1 ? A ASP 282 OD1 
41 1 Y 1 A ASP 288 ? OD2 ? A ASP 282 OD2 
42 1 Y 1 A ARG 290 ? CG  ? A ARG 284 CG  
43 1 Y 1 A ARG 290 ? CD  ? A ARG 284 CD  
44 1 Y 1 A ARG 290 ? NE  ? A ARG 284 NE  
45 1 Y 1 A ARG 290 ? CZ  ? A ARG 284 CZ  
46 1 Y 1 A ARG 290 ? NH1 ? A ARG 284 NH1 
47 1 Y 1 A ARG 290 ? NH2 ? A ARG 284 NH2 
48 1 Y 1 A THR 291 ? OG1 ? A THR 285 OG1 
49 1 Y 1 A THR 291 ? CG2 ? A THR 285 CG2 
50 1 Y 1 A VAL 313 ? CG1 ? A VAL 307 CG1 
51 1 Y 1 A VAL 313 ? CG2 ? A VAL 307 CG2 
52 1 Y 1 A ARG 316 ? NE  ? A ARG 310 NE  
53 1 Y 1 A ARG 316 ? CZ  ? A ARG 310 CZ  
54 1 Y 1 A ARG 316 ? NH1 ? A ARG 310 NH1 
55 1 Y 1 A ARG 316 ? NH2 ? A ARG 310 NH2 
56 1 Y 1 A LYS 322 ? CG  ? A LYS 316 CG  
57 1 Y 1 A LYS 322 ? CD  ? A LYS 316 CD  
58 1 Y 1 A LYS 322 ? CE  ? A LYS 316 CE  
59 1 Y 1 A LYS 322 ? NZ  ? A LYS 316 NZ  
60 1 Y 1 A ASP 358 ? CG  ? A ASP 352 CG  
61 1 Y 1 A ASP 358 ? OD1 ? A ASP 352 OD1 
62 1 Y 1 A ASP 358 ? OD2 ? A ASP 352 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YOX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.360 
_cell.length_a_esd                 ? 
_cell.length_b                     60.360 
_cell.length_b_esd                 ? 
_cell.length_c                     194.380 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YOX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 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                   8YOX 
_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             2.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.83 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Sodium chloride, 0.12 M Lithium sulfate, 0.1 M Sodium HEPES, 16% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-09-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL17U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          52.84 
_reflns.entry_id                                       8YOX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.48 
_reflns.d_resolution_low                               35.59 
_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                                     15119 
_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                           98.41 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.48 
_reflns_shell.d_res_low                                     2.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1005 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.813 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 8YOX 
_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                            2.48 
_refine.ls_d_res_low                             27.54 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     15068 
_refine.ls_number_reflns_R_free                  1443 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.25 
_refine.ls_percent_reflns_R_free                 5.28 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1948 
_refine.ls_R_factor_R_free                       0.2674 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1910 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.19 
_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                 31.06 
_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                            0.40 
_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                       2.48 
_refine_hist.d_res_low                        27.54 
_refine_hist.number_atoms_solvent             33 
_refine_hist.number_atoms_total               2843 
_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        2751 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.922  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.979 ? 1053 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 452  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 495  ? 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.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' 2.48 2.57 . . 119 2207 83.00  . . . . 0.2829 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 2.57 2.67 . . 127 2508 94.00  . . . . 0.2682 . . . . . . . . . . . 0.3375 
'X-RAY DIFFRACTION' 2.67 2.79 . . 143 2626 98.00  . . . . 0.2622 . . . . . . . . . . . 0.3415 
'X-RAY DIFFRACTION' 2.79 2.94 . . 201 2577 100.00 . . . . 0.2636 . . . . . . . . . . . 0.3387 
'X-RAY DIFFRACTION' 2.94 3.12 . . 152 2630 100.00 . . . . 0.2660 . . . . . . . . . . . 0.3686 
'X-RAY DIFFRACTION' 3.12 3.36 . . 162 2692 100.00 . . . . 0.2313 . . . . . . . . . . . 0.2510 
'X-RAY DIFFRACTION' 3.37 3.70 . . 115 2645 99.00  . . . . 0.2034 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 3.70 4.23 . . 114 2684 100.00 . . . . 0.1654 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 4.24 5.33 . . 138 2660 100.00 . . . . 0.1455 . . . . . . . . . . . 0.1958 
# 
_struct.entry_id                     8YOX 
_struct.title                        'Crystal structure of hFSP1 with 6-OH-FAD (hFSP1-6-OH-FAD)' 
_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        8YOX 
_struct_keywords.text            'Flavoprotein, 6-OH-FAD, Redox, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FSP1_HUMAN 
_struct_ref.pdbx_db_accession          Q9BRQ8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGIDLKN
QMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYPEKE
VTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIKINS
SAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFL
LSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_struct_ref.pdbx_align_begin           10 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YOX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9BRQ8 
_struct_ref_seq.db_align_beg                  10 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  373 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       10 
_struct_ref_seq.pdbx_auth_seq_align_end       373 
# 
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 8YOX PRO A 1 ? UNP Q9BRQ8 ? ? 'expression tag'        7 1 
1 8YOX HIS A 2 ? UNP Q9BRQ8 ? ? 'expression tag'        8 2 
1 8YOX MET A 3 ? UNP Q9BRQ8 ? ? 'initiating methionine' 9 3 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly   ?    monomeric 1 
2 software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
2 'ABSA (A^2)' 4390  ? 
2 MORE         -49   ? 
2 'SSA (A^2)'  29220 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,C,D 
2 1,2 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 y,x,-z -0.5000000000 0.8660254038 0.0000000000 0.0000000000 0.8660254038 0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 14  ? ASN A 28  ? GLY A 20  ASN A 34  1 ? 15 
HELX_P HELX_P2  AA2 ALA A 45  ? SER A 50  ? ALA A 51  SER A 56  1 ? 6  
HELX_P HELX_P3  AA3 PHE A 55  ? LYS A 58  ? PHE A 61  LYS A 64  5 ? 4  
HELX_P HELX_P4  AA4 TYR A 63  ? LYS A 68  ? TYR A 69  LYS A 74  1 ? 6  
HELX_P HELX_P5  AA5 SER A 118 ? SER A 136 ? SER A 124 SER A 142 1 ? 19 
HELX_P HELX_P6  AA6 GLY A 145 ? TYR A 159 ? GLY A 151 TYR A 165 1 ? 15 
HELX_P HELX_P7  AA7 LEU A 179 ? LYS A 193 ? LEU A 185 LYS A 199 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 205 ? LEU A 209 ? ASN A 211 LEU A 215 5 ? 5  
HELX_P HELX_P9  AA9 TYR A 246 ? GLU A 251 ? TYR A 252 GLU A 257 1 ? 6  
HELX_P HELX_P10 AB1 MET A 288 ? LYS A 308 ? MET A 294 LYS A 314 1 ? 21 
HELX_P HELX_P11 AB2 GLY A 341 ? LYS A 349 ? GLY A 347 LYS A 355 1 ? 9  
HELX_P HELX_P12 AB3 PHE A 354 ? ARG A 363 ? PHE A 360 ARG A 369 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           109 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PHE 
_struct_mon_prot_cis.auth_seq_id            115 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    110 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     116 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 3 ? 
# 
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      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 71  ? GLN A 73  ? PHE A 77  GLN A 79  
AA1 2 PHE A 31  ? ASP A 35  ? PHE A 37  ASP A 41  
AA1 3 VAL A 8   ? VAL A 11  ? VAL A 14  VAL A 17  
AA1 4 HIS A 98  ? LEU A 101 ? HIS A 104 LEU A 107 
AA1 5 VAL A 274 ? ALA A 276 ? VAL A 280 ALA A 282 
AA2 1 SER A 39  ? HIS A 41  ? SER A 45  HIS A 47  
AA2 2 PHE A 60  ? SER A 62  ? PHE A 66  SER A 68  
AA3 1 VAL A 76  ? ASP A 80  ? VAL A 82  ASP A 86  
AA3 2 MET A 85  ? LEU A 88  ? MET A 91  LEU A 94  
AA4 1 SER A 105 ? THR A 106 ? SER A 111 THR A 112 
AA4 2 LYS A 240 ? ILE A 241 ? LYS A 246 ILE A 247 
AA5 1 GLN A 196 ? LEU A 199 ? GLN A 202 LEU A 205 
AA5 2 GLU A 163 ? HIS A 168 ? GLU A 169 HIS A 174 
AA5 3 PHE A 138 ? VAL A 142 ? PHE A 144 VAL A 148 
AA5 4 LEU A 232 ? LEU A 235 ? LEU A 238 LEU A 241 
AA6 1 ILE A 218 ? GLN A 221 ? ILE A 224 GLN A 227 
AA6 2 GLU A 227 ? THR A 230 ? GLU A 233 THR A 236 
AA7 1 LEU A 260 ? ARG A 261 ? LEU A 266 ARG A 267 
AA7 2 ALA A 281 ? ASP A 282 ? ALA A 287 ASP A 288 
AA8 1 PHE A 322 ? SER A 325 ? PHE A 328 SER A 331 
AA8 2 GLY A 331 ? ILE A 335 ? GLY A 337 ILE A 341 
AA8 3 PHE A 338 ? VAL A 340 ? PHE A 344 VAL A 346 
# 
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 O ARG A 72  ? O ARG A 78  N LEU A 33  ? N LEU A 39  
AA1 2 3 O VAL A 34  ? O VAL A 40  N ILE A 10  ? N ILE A 16  
AA1 3 4 N VAL A 9   ? N VAL A 15  O ILE A 100 ? O ILE A 106 
AA1 4 5 N LEU A 99  ? N LEU A 105 O TYR A 275 ? O TYR A 281 
AA2 1 2 N PHE A 40  ? N PHE A 46  O ILE A 61  ? O ILE A 67  
AA3 1 2 N GLY A 78  ? N GLY A 84  O LEU A 87  ? O LEU A 93  
AA4 1 2 N THR A 106 ? N THR A 112 O LYS A 240 ? O LYS A 246 
AA5 1 2 O LEU A 198 ? O LEU A 204 N LEU A 166 ? N LEU A 172 
AA5 2 3 O THR A 165 ? O THR A 171 N VAL A 141 ? N VAL A 147 
AA5 3 4 N VAL A 140 ? N VAL A 146 O ILE A 234 ? O ILE A 240 
AA6 1 2 N VAL A 220 ? N VAL A 226 O VAL A 228 ? O VAL A 234 
AA7 1 2 N LEU A 260 ? N LEU A 266 O ASP A 282 ? O ASP A 288 
AA8 1 2 N LEU A 324 ? N LEU A 330 O VAL A 332 ? O VAL A 338 
AA8 2 3 N GLY A 333 ? N GLY A 339 O VAL A 340 ? O VAL A 346 
# 
_pdbx_entry_details.entry_id                   8YOX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 74  ? ? 49.19   -132.49 
2 1 ALA A 108 ? ? -147.05 55.34   
3 1 ALA A 180 ? ? 63.56   -173.57 
4 1 SER A 263 ? ? -69.49  2.36    
5 1 ASN A 269 ? ? -79.91  -164.97 
6 1 GLU A 275 ? ? -38.91  131.32  
7 1 LYS A 293 ? ? 70.43   91.73   
8 1 GLN A 315 ? ? 38.24   81.32   
9 1 MET A 332 ? ? -106.38 68.94   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
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 32.7613 27.0443 30.1768 0.6697 ? -0.0281 ? -0.0445 ? 0.3737 ? -0.0539 ? 0.4648 ? 0.3130 ? 0.1919  
? -0.1919 ? 0.1350 ? -0.0534 ? 0.1989 ? -0.1782 ? 0.0411 ? -0.0196 ? 0.2616 ? 0.0633  ? -0.0179 ? -0.0372 ? 0.1539  ? 0.0001  ? 
2 'X-RAY DIFFRACTION' ? refined 31.6926 16.2795 16.7205 0.5114 ? -0.0325 ? 0.0169  ? 0.3737 ? -0.0796 ? 0.4710 ? 0.2549 ? -0.2003 
? 0.3133  ? 1.4206 ? 0.3532  ? 0.5944 ? 0.0518  ? 0.2867 ? 0.0358  ? 0.2080 ? 0.1221  ? -0.2770 ? 0.0321  ? 0.3152  ? 0.0109  ? 
3 'X-RAY DIFFRACTION' ? refined 11.8473 -0.4195 9.5999  0.6206 ? -0.0806 ? 0.0591  ? 0.4273 ? -0.0528 ? 0.5513 ? 0.5736 ? -0.1383 
? 0.1214  ? 0.6001 ? -0.0818 ? 0.6324 ? 0.0194  ? 0.0201 ? -0.0872 ? 0.2104 ? -0.0385 ? 0.1512  ? 0.1186  ? -0.0915 ? -0.0000 ? 
4 'X-RAY DIFFRACTION' ? refined 25.1137 4.1784  23.4184 1.0076 ? -0.0777 ? -0.0090 ? 0.2870 ? -0.0137 ? 0.4637 ? 0.5444 ? 0.2623  
? 0.1855  ? 0.4532 ? 0.1934  ? 0.3417 ? 0.1231  ? 0.0535 ? -0.1753 ? 0.8024 ? -0.1089 ? -0.0452 ? 0.3704  ? -0.2050 ? -0.0976 ? 
5 'X-RAY DIFFRACTION' ? refined 14.1263 20.5145 22.5354 0.6332 ? -0.0754 ? 0.1286  ? 0.3932 ? -0.0724 ? 0.4538 ? 0.5400 ? -0.0240 
? 0.6359  ? 0.4264 ? 0.0242  ? 0.6139 ? 0.0468  ? 0.0697 ? 0.1170  ? 0.2594 ? -0.1301 ? 0.2865  ? -0.1096 ? -0.1160 ? 0.0091  ? 
# 
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 7 through 41 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 42 through 141 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 142 through 214 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 215 through 294 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 295 through 373 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       533 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.98 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
6FA N1     N N N 1   
6FA C2     C N N 2   
6FA O2     O N N 3   
6FA N3     N N N 4   
6FA C4     C N N 5   
6FA O4     O N N 6   
6FA C4A    C N N 7   
6FA N5     N N N 8   
6FA C5A    C Y N 9   
6FA C6     C Y N 10  
6FA O6     O N N 11  
6FA C7     C Y N 12  
6FA C7M    C N N 13  
6FA C8     C Y N 14  
6FA C8M    C N N 15  
6FA C9     C Y N 16  
6FA C9A    C Y N 17  
6FA N10    N N N 18  
6FA C10    C N N 19  
6FA "C1'"  C N N 20  
6FA "C2'"  C N S 21  
6FA "O2'"  O N N 22  
6FA "C3'"  C N S 23  
6FA "O3'"  O N N 24  
6FA "C4'"  C N R 25  
6FA "O4'"  O N N 26  
6FA "C5'"  C N N 27  
6FA "O5'"  O N N 28  
6FA P      P N R 29  
6FA O1P    O N N 30  
6FA O2P    O N N 31  
6FA O3P    O N N 32  
6FA PA     P N S 33  
6FA O1A    O N N 34  
6FA O2A    O N N 35  
6FA O5B    O N N 36  
6FA C5B    C N N 37  
6FA C4B    C N R 38  
6FA O4B    O N N 39  
6FA C3B    C N S 40  
6FA O3B    O N N 41  
6FA C2B    C N R 42  
6FA O2B    O N N 43  
6FA C1B    C N R 44  
6FA N9A    N Y N 45  
6FA C8A    C Y N 46  
6FA N7A    N Y N 47  
6FA C5X    C Y N 48  
6FA C6A    C Y N 49  
6FA N6A    N N N 50  
6FA N1A    N Y N 51  
6FA C2A    C Y N 52  
6FA N3A    N Y N 53  
6FA C4X    C Y N 54  
6FA HN3    H N N 55  
6FA HO6    H N N 56  
6FA HM71   H N N 57  
6FA HM72   H N N 58  
6FA HM73   H N N 59  
6FA HM81   H N N 60  
6FA HM82   H N N 61  
6FA HM83   H N N 62  
6FA H9     H N N 63  
6FA "H1'1" H N N 64  
6FA "H1'2" H N N 65  
6FA "H2'"  H N N 66  
6FA "HO2'" H N N 67  
6FA "H3'"  H N N 68  
6FA "HO3'" H N N 69  
6FA "H4'"  H N N 70  
6FA "HO4'" H N N 71  
6FA "H5'1" H N N 72  
6FA "H5'2" H N N 73  
6FA HOP2   H N N 74  
6FA HOA2   H N N 75  
6FA H51A   H N N 76  
6FA H52A   H N N 77  
6FA H4B    H N N 78  
6FA H3B    H N N 79  
6FA HO3A   H N N 80  
6FA H2B    H N N 81  
6FA HO2A   H N N 82  
6FA H1B    H N N 83  
6FA H8A    H N N 84  
6FA H61A   H N N 85  
6FA H62A   H N N 86  
6FA H2A    H N N 87  
ALA N      N N N 88  
ALA CA     C N S 89  
ALA C      C N N 90  
ALA O      O N N 91  
ALA CB     C N N 92  
ALA OXT    O N N 93  
ALA H      H N N 94  
ALA H2     H N N 95  
ALA HA     H N N 96  
ALA HB1    H N N 97  
ALA HB2    H N N 98  
ALA HB3    H N N 99  
ALA HXT    H N N 100 
ARG N      N N N 101 
ARG CA     C N S 102 
ARG C      C N N 103 
ARG O      O N N 104 
ARG CB     C N N 105 
ARG CG     C N N 106 
ARG CD     C N N 107 
ARG NE     N N N 108 
ARG CZ     C N N 109 
ARG NH1    N N N 110 
ARG NH2    N N N 111 
ARG OXT    O N N 112 
ARG H      H N N 113 
ARG H2     H N N 114 
ARG HA     H N N 115 
ARG HB2    H N N 116 
ARG HB3    H N N 117 
ARG HG2    H N N 118 
ARG HG3    H N N 119 
ARG HD2    H N N 120 
ARG HD3    H N N 121 
ARG HE     H N N 122 
ARG HH11   H N N 123 
ARG HH12   H N N 124 
ARG HH21   H N N 125 
ARG HH22   H N N 126 
ARG HXT    H N N 127 
ASN N      N N N 128 
ASN CA     C N S 129 
ASN C      C N N 130 
ASN O      O N N 131 
ASN CB     C N N 132 
ASN CG     C N N 133 
ASN OD1    O N N 134 
ASN ND2    N N N 135 
ASN OXT    O N N 136 
ASN H      H N N 137 
ASN H2     H N N 138 
ASN HA     H N N 139 
ASN HB2    H N N 140 
ASN HB3    H N N 141 
ASN HD21   H N N 142 
ASN HD22   H N N 143 
ASN HXT    H N N 144 
ASP N      N N N 145 
ASP CA     C N S 146 
ASP C      C N N 147 
ASP O      O N N 148 
ASP CB     C N N 149 
ASP CG     C N N 150 
ASP OD1    O N N 151 
ASP OD2    O N N 152 
ASP OXT    O N N 153 
ASP H      H N N 154 
ASP H2     H N N 155 
ASP HA     H N N 156 
ASP HB2    H N N 157 
ASP HB3    H N N 158 
ASP HD2    H N N 159 
ASP HXT    H N N 160 
CYS N      N N N 161 
CYS CA     C N R 162 
CYS C      C N N 163 
CYS O      O N N 164 
CYS CB     C N N 165 
CYS SG     S N N 166 
CYS OXT    O N N 167 
CYS H      H N N 168 
CYS H2     H N N 169 
CYS HA     H N N 170 
CYS HB2    H N N 171 
CYS HB3    H N N 172 
CYS HG     H N N 173 
CYS HXT    H N N 174 
GLN N      N N N 175 
GLN CA     C N S 176 
GLN C      C N N 177 
GLN O      O N N 178 
GLN CB     C N N 179 
GLN CG     C N N 180 
GLN CD     C N N 181 
GLN OE1    O N N 182 
GLN NE2    N N N 183 
GLN OXT    O N N 184 
GLN H      H N N 185 
GLN H2     H N N 186 
GLN HA     H N N 187 
GLN HB2    H N N 188 
GLN HB3    H N N 189 
GLN HG2    H N N 190 
GLN HG3    H N N 191 
GLN HE21   H N N 192 
GLN HE22   H N N 193 
GLN HXT    H N N 194 
GLU N      N N N 195 
GLU CA     C N S 196 
GLU C      C N N 197 
GLU O      O N N 198 
GLU CB     C N N 199 
GLU CG     C N N 200 
GLU CD     C N N 201 
GLU OE1    O N N 202 
GLU OE2    O N N 203 
GLU OXT    O N N 204 
GLU H      H N N 205 
GLU H2     H N N 206 
GLU HA     H N N 207 
GLU HB2    H N N 208 
GLU HB3    H N N 209 
GLU HG2    H N N 210 
GLU HG3    H N N 211 
GLU HE2    H N N 212 
GLU HXT    H N N 213 
GLY N      N N N 214 
GLY CA     C N N 215 
GLY C      C N N 216 
GLY O      O N N 217 
GLY OXT    O N N 218 
GLY H      H N N 219 
GLY H2     H N N 220 
GLY HA2    H N N 221 
GLY HA3    H N N 222 
GLY HXT    H N N 223 
HIS N      N N N 224 
HIS CA     C N S 225 
HIS C      C N N 226 
HIS O      O N N 227 
HIS CB     C N N 228 
HIS CG     C Y N 229 
HIS ND1    N Y N 230 
HIS CD2    C Y N 231 
HIS CE1    C Y N 232 
HIS NE2    N Y N 233 
HIS OXT    O N N 234 
HIS H      H N N 235 
HIS H2     H N N 236 
HIS HA     H N N 237 
HIS HB2    H N N 238 
HIS HB3    H N N 239 
HIS HD1    H N N 240 
HIS HD2    H N N 241 
HIS HE1    H N N 242 
HIS HE2    H N N 243 
HIS HXT    H N N 244 
HOH O      O N N 245 
HOH H1     H N N 246 
HOH H2     H N N 247 
ILE N      N N N 248 
ILE CA     C N S 249 
ILE C      C N N 250 
ILE O      O N N 251 
ILE CB     C N S 252 
ILE CG1    C N N 253 
ILE CG2    C N N 254 
ILE CD1    C N N 255 
ILE OXT    O N N 256 
ILE H      H N N 257 
ILE H2     H N N 258 
ILE HA     H N N 259 
ILE HB     H N N 260 
ILE HG12   H N N 261 
ILE HG13   H N N 262 
ILE HG21   H N N 263 
ILE HG22   H N N 264 
ILE HG23   H N N 265 
ILE HD11   H N N 266 
ILE HD12   H N N 267 
ILE HD13   H N N 268 
ILE HXT    H N N 269 
LEU N      N N N 270 
LEU CA     C N S 271 
LEU C      C N N 272 
LEU O      O N N 273 
LEU CB     C N N 274 
LEU CG     C N N 275 
LEU CD1    C N N 276 
LEU CD2    C N N 277 
LEU OXT    O N N 278 
LEU H      H N N 279 
LEU H2     H N N 280 
LEU HA     H N N 281 
LEU HB2    H N N 282 
LEU HB3    H N N 283 
LEU HG     H N N 284 
LEU HD11   H N N 285 
LEU HD12   H N N 286 
LEU HD13   H N N 287 
LEU HD21   H N N 288 
LEU HD22   H N N 289 
LEU HD23   H N N 290 
LEU HXT    H N N 291 
LYS N      N N N 292 
LYS CA     C N S 293 
LYS C      C N N 294 
LYS O      O N N 295 
LYS CB     C N N 296 
LYS CG     C N N 297 
LYS CD     C N N 298 
LYS CE     C N N 299 
LYS NZ     N N N 300 
LYS OXT    O N N 301 
LYS H      H N N 302 
LYS H2     H N N 303 
LYS HA     H N N 304 
LYS HB2    H N N 305 
LYS HB3    H N N 306 
LYS HG2    H N N 307 
LYS HG3    H N N 308 
LYS HD2    H N N 309 
LYS HD3    H N N 310 
LYS HE2    H N N 311 
LYS HE3    H N N 312 
LYS HZ1    H N N 313 
LYS HZ2    H N N 314 
LYS HZ3    H N N 315 
LYS HXT    H N N 316 
MET N      N N N 317 
MET CA     C N S 318 
MET C      C N N 319 
MET O      O N N 320 
MET CB     C N N 321 
MET CG     C N N 322 
MET SD     S N N 323 
MET CE     C N N 324 
MET OXT    O N N 325 
MET H      H N N 326 
MET H2     H N N 327 
MET HA     H N N 328 
MET HB2    H N N 329 
MET HB3    H N N 330 
MET HG2    H N N 331 
MET HG3    H N N 332 
MET HE1    H N N 333 
MET HE2    H N N 334 
MET HE3    H N N 335 
MET HXT    H N N 336 
PHE N      N N N 337 
PHE CA     C N S 338 
PHE C      C N N 339 
PHE O      O N N 340 
PHE CB     C N N 341 
PHE CG     C Y N 342 
PHE CD1    C Y N 343 
PHE CD2    C Y N 344 
PHE CE1    C Y N 345 
PHE CE2    C Y N 346 
PHE CZ     C Y N 347 
PHE OXT    O N N 348 
PHE H      H N N 349 
PHE H2     H N N 350 
PHE HA     H N N 351 
PHE HB2    H N N 352 
PHE HB3    H N N 353 
PHE HD1    H N N 354 
PHE HD2    H N N 355 
PHE HE1    H N N 356 
PHE HE2    H N N 357 
PHE HZ     H N N 358 
PHE HXT    H N N 359 
PRO N      N N N 360 
PRO CA     C N S 361 
PRO C      C N N 362 
PRO O      O N N 363 
PRO CB     C N N 364 
PRO CG     C N N 365 
PRO CD     C N N 366 
PRO OXT    O N N 367 
PRO H      H N N 368 
PRO HA     H N N 369 
PRO HB2    H N N 370 
PRO HB3    H N N 371 
PRO HG2    H N N 372 
PRO HG3    H N N 373 
PRO HD2    H N N 374 
PRO HD3    H N N 375 
PRO HXT    H N N 376 
SER N      N N N 377 
SER CA     C N S 378 
SER C      C N N 379 
SER O      O N N 380 
SER CB     C N N 381 
SER OG     O N N 382 
SER OXT    O N N 383 
SER H      H N N 384 
SER H2     H N N 385 
SER HA     H N N 386 
SER HB2    H N N 387 
SER HB3    H N N 388 
SER HG     H N N 389 
SER HXT    H N N 390 
SO4 S      S N N 391 
SO4 O1     O N N 392 
SO4 O2     O N N 393 
SO4 O3     O N N 394 
SO4 O4     O N N 395 
THR N      N N N 396 
THR CA     C N S 397 
THR C      C N N 398 
THR O      O N N 399 
THR CB     C N R 400 
THR OG1    O N N 401 
THR CG2    C N N 402 
THR OXT    O N N 403 
THR H      H N N 404 
THR H2     H N N 405 
THR HA     H N N 406 
THR HB     H N N 407 
THR HG1    H N N 408 
THR HG21   H N N 409 
THR HG22   H N N 410 
THR HG23   H N N 411 
THR HXT    H N N 412 
TRP N      N N N 413 
TRP CA     C N S 414 
TRP C      C N N 415 
TRP O      O N N 416 
TRP CB     C N N 417 
TRP CG     C Y N 418 
TRP CD1    C Y N 419 
TRP CD2    C Y N 420 
TRP NE1    N Y N 421 
TRP CE2    C Y N 422 
TRP CE3    C Y N 423 
TRP CZ2    C Y N 424 
TRP CZ3    C Y N 425 
TRP CH2    C Y N 426 
TRP OXT    O N N 427 
TRP H      H N N 428 
TRP H2     H N N 429 
TRP HA     H N N 430 
TRP HB2    H N N 431 
TRP HB3    H N N 432 
TRP HD1    H N N 433 
TRP HE1    H N N 434 
TRP HE3    H N N 435 
TRP HZ2    H N N 436 
TRP HZ3    H N N 437 
TRP HH2    H N N 438 
TRP HXT    H N N 439 
TYR N      N N N 440 
TYR CA     C N S 441 
TYR C      C N N 442 
TYR O      O N N 443 
TYR CB     C N N 444 
TYR CG     C Y N 445 
TYR CD1    C Y N 446 
TYR CD2    C Y N 447 
TYR CE1    C Y N 448 
TYR CE2    C Y N 449 
TYR CZ     C Y N 450 
TYR OH     O N N 451 
TYR OXT    O N N 452 
TYR H      H N N 453 
TYR H2     H N N 454 
TYR HA     H N N 455 
TYR HB2    H N N 456 
TYR HB3    H N N 457 
TYR HD1    H N N 458 
TYR HD2    H N N 459 
TYR HE1    H N N 460 
TYR HE2    H N N 461 
TYR HH     H N N 462 
TYR HXT    H N N 463 
VAL N      N N N 464 
VAL CA     C N S 465 
VAL C      C N N 466 
VAL O      O N N 467 
VAL CB     C N N 468 
VAL CG1    C N N 469 
VAL CG2    C N N 470 
VAL OXT    O N N 471 
VAL H      H N N 472 
VAL H2     H N N 473 
VAL HA     H N N 474 
VAL HB     H N N 475 
VAL HG11   H N N 476 
VAL HG12   H N N 477 
VAL HG13   H N N 478 
VAL HG21   H N N 479 
VAL HG22   H N N 480 
VAL HG23   H N N 481 
VAL HXT    H N N 482 
# 
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 
6FA N1    C2     sing N N 1   
6FA N1    C10    doub N N 2   
6FA C2    O2     doub N N 3   
6FA C2    N3     sing N N 4   
6FA N3    C4     sing N N 5   
6FA N3    HN3    sing N N 6   
6FA C4    O4     doub N N 7   
6FA C4    C4A    sing N N 8   
6FA C4A   N5     doub N N 9   
6FA C4A   C10    sing N N 10  
6FA N5    C5A    sing N N 11  
6FA C5A   C6     doub Y N 12  
6FA C5A   C9A    sing Y N 13  
6FA C6    O6     sing N N 14  
6FA C6    C7     sing Y N 15  
6FA O6    HO6    sing N N 16  
6FA C7    C7M    sing N N 17  
6FA C7    C8     doub Y N 18  
6FA C7M   HM71   sing N N 19  
6FA C7M   HM72   sing N N 20  
6FA C7M   HM73   sing N N 21  
6FA C8    C8M    sing N N 22  
6FA C8    C9     sing Y N 23  
6FA C8M   HM81   sing N N 24  
6FA C8M   HM82   sing N N 25  
6FA C8M   HM83   sing N N 26  
6FA C9    C9A    doub Y N 27  
6FA C9    H9     sing N N 28  
6FA C9A   N10    sing N N 29  
6FA N10   C10    sing N N 30  
6FA N10   "C1'"  sing N N 31  
6FA "C1'" "C2'"  sing N N 32  
6FA "C1'" "H1'1" sing N N 33  
6FA "C1'" "H1'2" sing N N 34  
6FA "C2'" "O2'"  sing N N 35  
6FA "C2'" "C3'"  sing N N 36  
6FA "C2'" "H2'"  sing N N 37  
6FA "O2'" "HO2'" sing N N 38  
6FA "C3'" "O3'"  sing N N 39  
6FA "C3'" "C4'"  sing N N 40  
6FA "C3'" "H3'"  sing N N 41  
6FA "O3'" "HO3'" sing N N 42  
6FA "C4'" "O4'"  sing N N 43  
6FA "C4'" "C5'"  sing N N 44  
6FA "C4'" "H4'"  sing N N 45  
6FA "O4'" "HO4'" sing N N 46  
6FA "C5'" "O5'"  sing N N 47  
6FA "C5'" "H5'1" sing N N 48  
6FA "C5'" "H5'2" sing N N 49  
6FA "O5'" P      sing N N 50  
6FA P     O1P    doub N N 51  
6FA P     O2P    sing N N 52  
6FA P     O3P    sing N N 53  
6FA O2P   HOP2   sing N N 54  
6FA O3P   PA     sing N N 55  
6FA PA    O1A    doub N N 56  
6FA PA    O2A    sing N N 57  
6FA PA    O5B    sing N N 58  
6FA O2A   HOA2   sing N N 59  
6FA O5B   C5B    sing N N 60  
6FA C5B   C4B    sing N N 61  
6FA C5B   H51A   sing N N 62  
6FA C5B   H52A   sing N N 63  
6FA C4B   O4B    sing N N 64  
6FA C4B   C3B    sing N N 65  
6FA C4B   H4B    sing N N 66  
6FA O4B   C1B    sing N N 67  
6FA C3B   O3B    sing N N 68  
6FA C3B   C2B    sing N N 69  
6FA C3B   H3B    sing N N 70  
6FA O3B   HO3A   sing N N 71  
6FA C2B   O2B    sing N N 72  
6FA C2B   C1B    sing N N 73  
6FA C2B   H2B    sing N N 74  
6FA O2B   HO2A   sing N N 75  
6FA C1B   N9A    sing N N 76  
6FA C1B   H1B    sing N N 77  
6FA N9A   C8A    sing Y N 78  
6FA N9A   C4X    sing Y N 79  
6FA C8A   N7A    doub Y N 80  
6FA C8A   H8A    sing N N 81  
6FA N7A   C5X    sing Y N 82  
6FA C5X   C6A    sing Y N 83  
6FA C5X   C4X    doub Y N 84  
6FA C6A   N6A    sing N N 85  
6FA C6A   N1A    doub Y N 86  
6FA N6A   H61A   sing N N 87  
6FA N6A   H62A   sing N N 88  
6FA N1A   C2A    sing Y N 89  
6FA C2A   N3A    doub Y N 90  
6FA C2A   H2A    sing N N 91  
6FA N3A   C4X    sing Y N 92  
ALA N     CA     sing N N 93  
ALA N     H      sing N N 94  
ALA N     H2     sing N N 95  
ALA CA    C      sing N N 96  
ALA CA    CB     sing N N 97  
ALA CA    HA     sing N N 98  
ALA C     O      doub N N 99  
ALA C     OXT    sing N N 100 
ALA CB    HB1    sing N N 101 
ALA CB    HB2    sing N N 102 
ALA CB    HB3    sing N N 103 
ALA OXT   HXT    sing N N 104 
ARG N     CA     sing N N 105 
ARG N     H      sing N N 106 
ARG N     H2     sing N N 107 
ARG CA    C      sing N N 108 
ARG CA    CB     sing N N 109 
ARG CA    HA     sing N N 110 
ARG C     O      doub N N 111 
ARG C     OXT    sing N N 112 
ARG CB    CG     sing N N 113 
ARG CB    HB2    sing N N 114 
ARG CB    HB3    sing N N 115 
ARG CG    CD     sing N N 116 
ARG CG    HG2    sing N N 117 
ARG CG    HG3    sing N N 118 
ARG CD    NE     sing N N 119 
ARG CD    HD2    sing N N 120 
ARG CD    HD3    sing N N 121 
ARG NE    CZ     sing N N 122 
ARG NE    HE     sing N N 123 
ARG CZ    NH1    sing N N 124 
ARG CZ    NH2    doub N N 125 
ARG NH1   HH11   sing N N 126 
ARG NH1   HH12   sing N N 127 
ARG NH2   HH21   sing N N 128 
ARG NH2   HH22   sing N N 129 
ARG OXT   HXT    sing N N 130 
ASN N     CA     sing N N 131 
ASN N     H      sing N N 132 
ASN N     H2     sing N N 133 
ASN CA    C      sing N N 134 
ASN CA    CB     sing N N 135 
ASN CA    HA     sing N N 136 
ASN C     O      doub N N 137 
ASN C     OXT    sing N N 138 
ASN CB    CG     sing N N 139 
ASN CB    HB2    sing N N 140 
ASN CB    HB3    sing N N 141 
ASN CG    OD1    doub N N 142 
ASN CG    ND2    sing N N 143 
ASN ND2   HD21   sing N N 144 
ASN ND2   HD22   sing N N 145 
ASN OXT   HXT    sing N N 146 
ASP N     CA     sing N N 147 
ASP N     H      sing N N 148 
ASP N     H2     sing N N 149 
ASP CA    C      sing N N 150 
ASP CA    CB     sing N N 151 
ASP CA    HA     sing N N 152 
ASP C     O      doub N N 153 
ASP C     OXT    sing N N 154 
ASP CB    CG     sing N N 155 
ASP CB    HB2    sing N N 156 
ASP CB    HB3    sing N N 157 
ASP CG    OD1    doub N N 158 
ASP CG    OD2    sing N N 159 
ASP OD2   HD2    sing N N 160 
ASP OXT   HXT    sing N N 161 
CYS N     CA     sing N N 162 
CYS N     H      sing N N 163 
CYS N     H2     sing N N 164 
CYS CA    C      sing N N 165 
CYS CA    CB     sing N N 166 
CYS CA    HA     sing N N 167 
CYS C     O      doub N N 168 
CYS C     OXT    sing N N 169 
CYS CB    SG     sing N N 170 
CYS CB    HB2    sing N N 171 
CYS CB    HB3    sing N N 172 
CYS SG    HG     sing N N 173 
CYS OXT   HXT    sing N N 174 
GLN N     CA     sing N N 175 
GLN N     H      sing N N 176 
GLN N     H2     sing N N 177 
GLN CA    C      sing N N 178 
GLN CA    CB     sing N N 179 
GLN CA    HA     sing N N 180 
GLN C     O      doub N N 181 
GLN C     OXT    sing N N 182 
GLN CB    CG     sing N N 183 
GLN CB    HB2    sing N N 184 
GLN CB    HB3    sing N N 185 
GLN CG    CD     sing N N 186 
GLN CG    HG2    sing N N 187 
GLN CG    HG3    sing N N 188 
GLN CD    OE1    doub N N 189 
GLN CD    NE2    sing N N 190 
GLN NE2   HE21   sing N N 191 
GLN NE2   HE22   sing N N 192 
GLN OXT   HXT    sing N N 193 
GLU N     CA     sing N N 194 
GLU N     H      sing N N 195 
GLU N     H2     sing N N 196 
GLU CA    C      sing N N 197 
GLU CA    CB     sing N N 198 
GLU CA    HA     sing N N 199 
GLU C     O      doub N N 200 
GLU C     OXT    sing N N 201 
GLU CB    CG     sing N N 202 
GLU CB    HB2    sing N N 203 
GLU CB    HB3    sing N N 204 
GLU CG    CD     sing N N 205 
GLU CG    HG2    sing N N 206 
GLU CG    HG3    sing N N 207 
GLU CD    OE1    doub N N 208 
GLU CD    OE2    sing N N 209 
GLU OE2   HE2    sing N N 210 
GLU OXT   HXT    sing N N 211 
GLY N     CA     sing N N 212 
GLY N     H      sing N N 213 
GLY N     H2     sing N N 214 
GLY CA    C      sing N N 215 
GLY CA    HA2    sing N N 216 
GLY CA    HA3    sing N N 217 
GLY C     O      doub N N 218 
GLY C     OXT    sing N N 219 
GLY OXT   HXT    sing N N 220 
HIS N     CA     sing N N 221 
HIS N     H      sing N N 222 
HIS N     H2     sing N N 223 
HIS CA    C      sing N N 224 
HIS CA    CB     sing N N 225 
HIS CA    HA     sing N N 226 
HIS C     O      doub N N 227 
HIS C     OXT    sing N N 228 
HIS CB    CG     sing N N 229 
HIS CB    HB2    sing N N 230 
HIS CB    HB3    sing N N 231 
HIS CG    ND1    sing Y N 232 
HIS CG    CD2    doub Y N 233 
HIS ND1   CE1    doub Y N 234 
HIS ND1   HD1    sing N N 235 
HIS CD2   NE2    sing Y N 236 
HIS CD2   HD2    sing N N 237 
HIS CE1   NE2    sing Y N 238 
HIS CE1   HE1    sing N N 239 
HIS NE2   HE2    sing N N 240 
HIS OXT   HXT    sing N N 241 
HOH O     H1     sing N N 242 
HOH O     H2     sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
SO4 S     O1     doub N N 382 
SO4 S     O2     doub N N 383 
SO4 S     O3     sing N N 384 
SO4 S     O4     sing N N 385 
THR N     CA     sing N N 386 
THR N     H      sing N N 387 
THR N     H2     sing N N 388 
THR CA    C      sing N N 389 
THR CA    CB     sing N N 390 
THR CA    HA     sing N N 391 
THR C     O      doub N N 392 
THR C     OXT    sing N N 393 
THR CB    OG1    sing N N 394 
THR CB    CG2    sing N N 395 
THR CB    HB     sing N N 396 
THR OG1   HG1    sing N N 397 
THR CG2   HG21   sing N N 398 
THR CG2   HG22   sing N N 399 
THR CG2   HG23   sing N N 400 
THR OXT   HXT    sing N N 401 
TRP N     CA     sing N N 402 
TRP N     H      sing N N 403 
TRP N     H2     sing N N 404 
TRP CA    C      sing N N 405 
TRP CA    CB     sing N N 406 
TRP CA    HA     sing N N 407 
TRP C     O      doub N N 408 
TRP C     OXT    sing N N 409 
TRP CB    CG     sing N N 410 
TRP CB    HB2    sing N N 411 
TRP CB    HB3    sing N N 412 
TRP CG    CD1    doub Y N 413 
TRP CG    CD2    sing Y N 414 
TRP CD1   NE1    sing Y N 415 
TRP CD1   HD1    sing N N 416 
TRP CD2   CE2    doub Y N 417 
TRP CD2   CE3    sing Y N 418 
TRP NE1   CE2    sing Y N 419 
TRP NE1   HE1    sing N N 420 
TRP CE2   CZ2    sing Y N 421 
TRP CE3   CZ3    doub Y N 422 
TRP CE3   HE3    sing N N 423 
TRP CZ2   CH2    doub Y N 424 
TRP CZ2   HZ2    sing N N 425 
TRP CZ3   CH2    sing Y N 426 
TRP CZ3   HZ3    sing N N 427 
TRP CH2   HH2    sing N N 428 
TRP OXT   HXT    sing N N 429 
TYR N     CA     sing N N 430 
TYR N     H      sing N N 431 
TYR N     H2     sing N N 432 
TYR CA    C      sing N N 433 
TYR CA    CB     sing N N 434 
TYR CA    HA     sing N N 435 
TYR C     O      doub N N 436 
TYR C     OXT    sing N N 437 
TYR CB    CG     sing N N 438 
TYR CB    HB2    sing N N 439 
TYR CB    HB3    sing N N 440 
TYR CG    CD1    doub Y N 441 
TYR CG    CD2    sing Y N 442 
TYR CD1   CE1    sing Y N 443 
TYR CD1   HD1    sing N N 444 
TYR CD2   CE2    doub Y N 445 
TYR CD2   HD2    sing N N 446 
TYR CE1   CZ     doub Y N 447 
TYR CE1   HE1    sing N N 448 
TYR CE2   CZ     sing Y N 449 
TYR CE2   HE2    sing N N 450 
TYR CZ    OH     sing N N 451 
TYR OH    HH     sing N N 452 
TYR OXT   HXT    sing N N 453 
VAL N     CA     sing N N 454 
VAL N     H      sing N N 455 
VAL N     H2     sing N N 456 
VAL CA    C      sing N N 457 
VAL CA    CB     sing N N 458 
VAL CA    HA     sing N N 459 
VAL C     O      doub N N 460 
VAL C     OXT    sing N N 461 
VAL CB    CG1    sing N N 462 
VAL CB    CG2    sing N N 463 
VAL CB    HB     sing N N 464 
VAL CG1   HG11   sing N N 465 
VAL CG1   HG12   sing N N 466 
VAL CG1   HG13   sing N N 467 
VAL CG2   HG21   sing N N 468 
VAL CG2   HG22   sing N N 469 
VAL CG2   HG23   sing N N 470 
VAL OXT   HXT    sing N N 471 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32071269 1 
'National Natural Science Foundation of China (NSFC)' China 31770827 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   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YOX 
_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]   0.016567 
_atom_sites.fract_transf_matrix[1][2]   0.009565 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019130 
_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]   0.005145 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . PRO A 1 1   ? 45.250 25.552  41.514  1.00 65.18  ?  7   PRO A N     1 
ATOM   2    C CA    . PRO A 1 1   ? 45.146 26.559  42.590  1.00 59.51  ?  7   PRO A CA    1 
ATOM   3    C C     . PRO A 1 1   ? 44.365 27.758  42.087  1.00 56.60  ?  7   PRO A C     1 
ATOM   4    O O     . PRO A 1 1   ? 44.965 28.657  41.502  1.00 59.62  ?  7   PRO A O     1 
ATOM   5    C CB    . PRO A 1 1   ? 46.608 26.944  42.890  1.00 51.54  ?  7   PRO A CB    1 
ATOM   6    C CG    . PRO A 1 1   ? 47.449 25.903  42.192  1.00 59.71  ?  7   PRO A CG    1 
ATOM   7    C CD    . PRO A 1 1   ? 46.627 25.398  41.023  1.00 59.25  ?  7   PRO A CD    1 
ATOM   8    N N     . HIS A 1 2   ? 43.048 27.776  42.268  1.00 52.97  ?  8   HIS A N     1 
ATOM   9    C CA    . HIS A 1 2   ? 42.262 28.819  41.624  1.00 53.38  ?  8   HIS A CA    1 
ATOM   10   C C     . HIS A 1 2   ? 41.948 30.012  42.519  1.00 54.90  ?  8   HIS A C     1 
ATOM   11   O O     . HIS A 1 2   ? 41.489 31.034  41.996  1.00 53.13  ?  8   HIS A O     1 
ATOM   12   C CB    . HIS A 1 2   ? 40.981 28.225  41.048  1.00 55.08  ?  8   HIS A CB    1 
ATOM   13   C CG    . HIS A 1 2   ? 41.191 27.624  39.696  1.00 60.77  ?  8   HIS A CG    1 
ATOM   14   N ND1   . HIS A 1 2   ? 41.568 26.309  39.519  1.00 62.77  ?  8   HIS A ND1   1 
ATOM   15   C CD2   . HIS A 1 2   ? 41.162 28.181  38.461  1.00 58.47  ?  8   HIS A CD2   1 
ATOM   16   C CE1   . HIS A 1 2   ? 41.729 26.072  38.228  1.00 64.98  ?  8   HIS A CE1   1 
ATOM   17   N NE2   . HIS A 1 2   ? 41.491 27.191  37.564  1.00 63.64  ?  8   HIS A NE2   1 
ATOM   18   N N     . MET A 1 3   ? 42.186 29.912  43.832  1.00 50.52  ?  9   MET A N     1 
ATOM   19   C CA    . MET A 1 3   ? 42.125 31.047  44.750  1.00 48.74  ?  9   MET A CA    1 
ATOM   20   C C     . MET A 1 3   ? 40.834 31.840  44.599  1.00 46.58  ?  9   MET A C     1 
ATOM   21   O O     . MET A 1 3   ? 40.846 33.071  44.512  1.00 45.94  ?  9   MET A O     1 
ATOM   22   C CB    . MET A 1 3   ? 43.332 31.960  44.568  1.00 45.87  ?  9   MET A CB    1 
ATOM   23   C CG    . MET A 1 3   ? 44.638 31.209  44.643  1.00 48.56  ?  9   MET A CG    1 
ATOM   24   S SD    . MET A 1 3   ? 46.075 32.272  44.944  1.00 61.78  ?  9   MET A SD    1 
ATOM   25   C CE    . MET A 1 3   ? 47.379 31.065  44.698  1.00 55.77  ?  9   MET A CE    1 
ATOM   26   N N     . GLY A 1 4   ? 39.711 31.119  44.571  1.00 45.02  ?  10  GLY A N     1 
ATOM   27   C CA    . GLY A 1 4   ? 38.395 31.709  44.496  1.00 45.05  ?  10  GLY A CA    1 
ATOM   28   C C     . GLY A 1 4   ? 37.822 31.866  43.098  1.00 54.22  ?  10  GLY A C     1 
ATOM   29   O O     . GLY A 1 4   ? 36.602 31.838  42.940  1.00 57.95  ?  10  GLY A O     1 
ATOM   30   N N     . ALA A 1 5   ? 38.669 32.034  42.082  1.00 54.01  ?  11  ALA A N     1 
ATOM   31   C CA    . ALA A 1 5   ? 38.188 32.328  40.736  1.00 55.25  ?  11  ALA A CA    1 
ATOM   32   C C     . ALA A 1 5   ? 37.510 31.109  40.114  1.00 60.96  ?  11  ALA A C     1 
ATOM   33   O O     . ALA A 1 5   ? 37.634 29.973  40.591  1.00 63.45  ?  11  ALA A O     1 
ATOM   34   C CB    . ALA A 1 5   ? 39.333 32.792  39.831  1.00 52.61  ?  11  ALA A CB    1 
ATOM   35   N N     . LEU A 1 6   ? 36.772 31.365  39.042  1.00 59.48  ?  12  LEU A N     1 
ATOM   36   C CA    . LEU A 1 6   ? 36.070 30.323  38.322  1.00 57.79  ?  12  LEU A CA    1 
ATOM   37   C C     . LEU A 1 6   ? 36.873 29.954  37.093  1.00 59.62  ?  12  LEU A C     1 
ATOM   38   O O     . LEU A 1 6   ? 37.487 30.811  36.451  1.00 58.36  ?  12  LEU A O     1 
ATOM   39   C CB    . LEU A 1 6   ? 34.671 30.762  37.896  1.00 56.80  ?  12  LEU A CB    1 
ATOM   40   C CG    . LEU A 1 6   ? 33.598 31.015  38.946  1.00 57.46  ?  12  LEU A CG    1 
ATOM   41   C CD1   . LEU A 1 6   ? 32.256 31.261  38.281  1.00 52.88  ?  12  LEU A CD1   1 
ATOM   42   C CD2   . LEU A 1 6   ? 33.502 29.872  39.914  1.00 60.62  ?  12  LEU A CD2   1 
ATOM   43   N N     . HIS A 1 7   ? 36.893 28.668  36.792  1.00 59.26  ?  13  HIS A N     1 
ATOM   44   C CA    . HIS A 1 7   ? 37.297 28.217  35.472  1.00 59.31  ?  13  HIS A CA    1 
ATOM   45   C C     . HIS A 1 7   ? 36.462 26.977  35.213  1.00 59.86  ?  13  HIS A C     1 
ATOM   46   O O     . HIS A 1 7   ? 36.653 25.959  35.882  1.00 59.71  ?  13  HIS A O     1 
ATOM   47   C CB    . HIS A 1 7   ? 38.790 27.939  35.390  1.00 57.24  ?  13  HIS A CB    1 
ATOM   48   C CG    . HIS A 1 7   ? 39.279 27.789  33.987  1.00 68.11  ?  13  HIS A CG    1 
ATOM   49   N ND1   . HIS A 1 7   ? 38.418 27.628  32.918  1.00 70.78  ?  13  HIS A ND1   1 
ATOM   50   C CD2   . HIS A 1 7   ? 40.529 27.790  33.466  1.00 73.65  ?  13  HIS A CD2   1 
ATOM   51   C CE1   . HIS A 1 7   ? 39.116 27.528  31.800  1.00 64.55  ?  13  HIS A CE1   1 
ATOM   52   N NE2   . HIS A 1 7   ? 40.400 27.617  32.105  1.00 78.35  ?  13  HIS A NE2   1 
ATOM   53   N N     . VAL A 1 8   ? 35.488 27.092  34.317  1.00 56.04  ?  14  VAL A N     1 
ATOM   54   C CA    . VAL A 1 8   ? 34.579 25.993  34.026  1.00 55.57  ?  14  VAL A CA    1 
ATOM   55   C C     . VAL A 1 8   ? 35.076 25.279  32.786  1.00 54.57  ?  14  VAL A C     1 
ATOM   56   O O     . VAL A 1 8   ? 35.461 25.911  31.801  1.00 55.07  ?  14  VAL A O     1 
ATOM   57   C CB    . VAL A 1 8   ? 33.134 26.481  33.841  1.00 51.25  ?  14  VAL A CB    1 
ATOM   58   C CG1   . VAL A 1 8   ? 32.215 25.307  33.522  1.00 48.16  ?  14  VAL A CG1   1 
ATOM   59   C CG2   . VAL A 1 8   ? 32.672 27.167  35.096  1.00 51.08  ?  14  VAL A CG2   1 
ATOM   60   N N     . VAL A 1 9   ? 35.101 23.958  32.847  1.00 51.32  ?  15  VAL A N     1 
ATOM   61   C CA    . VAL A 1 9   ? 35.476 23.129  31.719  1.00 53.24  ?  15  VAL A CA    1 
ATOM   62   C C     . VAL A 1 9   ? 34.253 22.333  31.310  1.00 52.85  ?  15  VAL A C     1 
ATOM   63   O O     . VAL A 1 9   ? 33.631 21.671  32.152  1.00 49.82  ?  15  VAL A O     1 
ATOM   64   C CB    . VAL A 1 9   ? 36.653 22.202  32.051  1.00 53.37  ?  15  VAL A CB    1 
ATOM   65   C CG1   . VAL A 1 9   ? 36.857 21.215  30.908  1.00 50.26  ?  15  VAL A CG1   1 
ATOM   66   C CG2   . VAL A 1 9   ? 37.896 23.030  32.283  1.00 53.76  ?  15  VAL A CG2   1 
ATOM   67   N N     . ILE A 1 10  ? 33.894 22.435  30.032  1.00 48.55  ?  16  ILE A N     1 
ATOM   68   C CA    . ILE A 1 10  ? 32.789 21.686  29.453  1.00 47.67  ?  16  ILE A CA    1 
ATOM   69   C C     . ILE A 1 10  ? 33.400 20.563  28.646  1.00 49.00  ?  16  ILE A C     1 
ATOM   70   O O     . ILE A 1 10  ? 34.109 20.812  27.661  1.00 52.64  ?  16  ILE A O     1 
ATOM   71   C CB    . ILE A 1 10  ? 31.905 22.582  28.586  1.00 47.86  ?  16  ILE A CB    1 
ATOM   72   C CG1   . ILE A 1 10  ? 31.479 23.788  29.417  1.00 47.04  ?  16  ILE A CG1   1 
ATOM   73   C CG2   . ILE A 1 10  ? 30.722 21.807  28.076  1.00 42.11  ?  16  ILE A CG2   1 
ATOM   74   C CD1   . ILE A 1 10  ? 30.669 24.766  28.683  1.00 47.37  ?  16  ILE A CD1   1 
ATOM   75   N N     . VAL A 1 11  ? 33.167 19.326  29.062  1.00 50.35  ?  17  VAL A N     1 
ATOM   76   C CA    . VAL A 1 11  ? 33.629 18.176  28.292  1.00 52.39  ?  17  VAL A CA    1 
ATOM   77   C C     . VAL A 1 11  ? 32.461 17.674  27.464  1.00 44.96  ?  17  VAL A C     1 
ATOM   78   O O     . VAL A 1 11  ? 31.472 17.170  28.009  1.00 45.19  ?  17  VAL A O     1 
ATOM   79   C CB    . VAL A 1 11  ? 34.202 17.069  29.177  1.00 55.30  ?  17  VAL A CB    1 
ATOM   80   C CG1   . VAL A 1 11  ? 34.446 15.862  28.324  1.00 54.11  ?  17  VAL A CG1   1 
ATOM   81   C CG2   . VAL A 1 11  ? 35.513 17.539  29.812  1.00 54.58  ?  17  VAL A CG2   1 
ATOM   82   N N     . GLY A 1 12  ? 32.580 17.842  26.144  1.00 49.25  ?  18  GLY A N     1 
ATOM   83   C CA    . GLY A 1 12  ? 31.560 17.455  25.182  1.00 49.10  ?  18  GLY A CA    1 
ATOM   84   C C     . GLY A 1 12  ? 30.856 18.649  24.565  1.00 48.60  ?  18  GLY A C     1 
ATOM   85   O O     . GLY A 1 12  ? 30.270 19.465  25.287  1.00 48.70  ?  18  GLY A O     1 
ATOM   86   N N     . GLY A 1 13  ? 30.896 18.764  23.235  1.00 45.33  ?  19  GLY A N     1 
ATOM   87   C CA    . GLY A 1 13  ? 30.304 19.908  22.568  1.00 40.64  ?  19  GLY A CA    1 
ATOM   88   C C     . GLY A 1 13  ? 29.053 19.555  21.797  1.00 43.19  ?  19  GLY A C     1 
ATOM   89   O O     . GLY A 1 13  ? 28.932 19.899  20.615  1.00 51.73  ?  19  GLY A O     1 
ATOM   90   N N     . GLY A 1 14  ? 28.138 18.835  22.431  1.00 39.13  ?  20  GLY A N     1 
ATOM   91   C CA    . GLY A 1 14  ? 26.846 18.518  21.861  1.00 37.63  ?  20  GLY A CA    1 
ATOM   92   C C     . GLY A 1 14  ? 25.802 19.562  22.185  1.00 37.96  ?  20  GLY A C     1 
ATOM   93   O O     . GLY A 1 14  ? 26.113 20.722  22.465  1.00 38.71  ?  20  GLY A O     1 
ATOM   94   N N     . PHE A 1 15  ? 24.537 19.135  22.144  1.00 37.81  ?  21  PHE A N     1 
ATOM   95   C CA    . PHE A 1 15  ? 23.436 20.039  22.469  1.00 40.66  ?  21  PHE A CA    1 
ATOM   96   C C     . PHE A 1 15  ? 23.602 20.669  23.853  1.00 41.41  ?  21  PHE A C     1 
ATOM   97   O O     . PHE A 1 15  ? 23.408 21.881  24.015  1.00 42.12  ?  21  PHE A O     1 
ATOM   98   C CB    . PHE A 1 15  ? 22.105 19.301  22.369  1.00 41.35  ?  21  PHE A CB    1 
ATOM   99   C CG    . PHE A 1 15  ? 21.696 18.999  20.976  1.00 40.97  ?  21  PHE A CG    1 
ATOM   100  C CD1   . PHE A 1 15  ? 22.079 17.824  20.370  1.00 44.43  ?  21  PHE A CD1   1 
ATOM   101  C CD2   . PHE A 1 15  ? 20.956 19.908  20.250  1.00 46.42  ?  21  PHE A CD2   1 
ATOM   102  C CE1   . PHE A 1 15  ? 21.693 17.546  19.052  1.00 45.36  ?  21  PHE A CE1   1 
ATOM   103  C CE2   . PHE A 1 15  ? 20.585 19.644  18.932  1.00 45.28  ?  21  PHE A CE2   1 
ATOM   104  C CZ    . PHE A 1 15  ? 20.944 18.453  18.344  1.00 40.03  ?  21  PHE A CZ    1 
ATOM   105  N N     . GLY A 1 16  ? 23.985 19.877  24.857  1.00 39.22  ?  22  GLY A N     1 
ATOM   106  C CA    . GLY A 1 16  ? 24.193 20.448  26.178  1.00 39.72  ?  22  GLY A CA    1 
ATOM   107  C C     . GLY A 1 16  ? 25.416 21.342  26.247  1.00 39.30  ?  22  GLY A C     1 
ATOM   108  O O     . GLY A 1 16  ? 25.339 22.499  26.674  1.00 44.13  ?  22  GLY A O     1 
ATOM   109  N N     . GLY A 1 17  ? 26.559 20.818  25.829  1.00 39.84  ?  23  GLY A N     1 
ATOM   110  C CA    . GLY A 1 17  ? 27.787 21.590  25.883  1.00 40.68  ?  23  GLY A CA    1 
ATOM   111  C C     . GLY A 1 17  ? 27.708 22.950  25.208  1.00 43.52  ?  23  GLY A C     1 
ATOM   112  O O     . GLY A 1 17  ? 28.219 23.935  25.742  1.00 49.63  ?  23  GLY A O     1 
ATOM   113  N N     . ILE A 1 18  ? 27.087 23.030  24.022  1.00 39.12  ?  24  ILE A N     1 
ATOM   114  C CA    . ILE A 1 18  ? 27.036 24.336  23.361  1.00 40.75  ?  24  ILE A CA    1 
ATOM   115  C C     . ILE A 1 18  ? 26.026 25.218  24.057  1.00 38.35  ?  24  ILE A C     1 
ATOM   116  O O     . ILE A 1 18  ? 26.164 26.441  24.047  1.00 41.10  ?  24  ILE A O     1 
ATOM   117  C CB    . ILE A 1 18  ? 26.714 24.265  21.842  1.00 40.77  ?  24  ILE A CB    1 
ATOM   118  C CG1   . ILE A 1 18  ? 25.396 23.540  21.572  1.00 40.79  ?  24  ILE A CG1   1 
ATOM   119  C CG2   . ILE A 1 18  ? 27.815 23.595  21.077  1.00 40.24  ?  24  ILE A CG2   1 
ATOM   120  C CD1   . ILE A 1 18  ? 24.628 24.072  20.451  1.00 43.03  ?  24  ILE A CD1   1 
ATOM   121  N N     . ALA A 1 19  ? 24.984 24.638  24.639  1.00 39.29  ?  25  ALA A N     1 
ATOM   122  C CA    . ALA A 1 19  ? 24.090 25.427  25.479  1.00 39.92  ?  25  ALA A CA    1 
ATOM   123  C C     . ALA A 1 19  ? 24.830 25.990  26.693  1.00 45.03  ?  25  ALA A C     1 
ATOM   124  O O     . ALA A 1 19  ? 24.663 27.166  27.042  1.00 48.59  ?  25  ALA A O     1 
ATOM   125  C CB    . ALA A 1 19  ? 22.905 24.578  25.919  1.00 39.17  ?  25  ALA A CB    1 
ATOM   126  N N     . ALA A 1 20  ? 25.676 25.179  27.333  1.00 43.16  ?  26  ALA A N     1 
ATOM   127  C CA    . ALA A 1 20  ? 26.404 25.660  28.506  1.00 45.48  ?  26  ALA A CA    1 
ATOM   128  C C     . ALA A 1 20  ? 27.504 26.645  28.120  1.00 47.20  ?  26  ALA A C     1 
ATOM   129  O O     . ALA A 1 20  ? 27.709 27.665  28.794  1.00 45.70  ?  26  ALA A O     1 
ATOM   130  C CB    . ALA A 1 20  ? 26.981 24.474  29.286  1.00 44.59  ?  26  ALA A CB    1 
ATOM   131  N N     . ALA A 1 21  ? 28.222 26.359  27.036  1.00 48.24  ?  27  ALA A N     1 
ATOM   132  C CA    . ALA A 1 21  ? 29.266 27.275  26.597  1.00 46.85  ?  27  ALA A CA    1 
ATOM   133  C C     . ALA A 1 21  ? 28.684 28.646  26.261  1.00 48.86  ?  27  ALA A C     1 
ATOM   134  O O     . ALA A 1 21  ? 29.294 29.676  26.563  1.00 51.56  ?  27  ALA A O     1 
ATOM   135  C CB    . ALA A 1 21  ? 30.008 26.673  25.408  1.00 45.83  ?  27  ALA A CB    1 
ATOM   136  N N     . SER A 1 22  ? 27.483 28.679  25.673  1.00 48.31  ?  28  SER A N     1 
ATOM   137  C CA    . SER A 1 22  ? 26.884 29.950  25.285  1.00 49.24  ?  28  SER A CA    1 
ATOM   138  C C     . SER A 1 22  ? 26.425 30.736  26.492  1.00 47.85  ?  28  SER A C     1 
ATOM   139  O O     . SER A 1 22  ? 26.511 31.969  26.497  1.00 49.96  ?  28  SER A O     1 
ATOM   140  C CB    . SER A 1 22  ? 25.710 29.730  24.332  1.00 51.74  ?  28  SER A CB    1 
ATOM   141  O OG    . SER A 1 22  ? 26.098 30.051  23.005  1.00 61.22  ?  28  SER A OG    1 
ATOM   142  N N     . GLN A 1 23  ? 25.907 30.048  27.510  1.00 51.91  ?  29  GLN A N     1 
ATOM   143  C CA    . GLN A 1 23  ? 25.520 30.730  28.738  1.00 50.11  ?  29  GLN A CA    1 
ATOM   144  C C     . GLN A 1 23  ? 26.735 31.346  29.430  1.00 51.56  ?  29  GLN A C     1 
ATOM   145  O O     . GLN A 1 23  ? 26.745 32.543  29.748  1.00 50.11  ?  29  GLN A O     1 
ATOM   146  C CB    . GLN A 1 23  ? 24.823 29.750  29.657  1.00 50.88  ?  29  GLN A CB    1 
ATOM   147  C CG    . GLN A 1 23  ? 24.076 30.440  30.752  1.00 61.89  ?  29  GLN A CG    1 
ATOM   148  C CD    . GLN A 1 23  ? 22.656 30.732  30.348  1.00 69.27  ?  29  GLN A CD    1 
ATOM   149  O OE1   . GLN A 1 23  ? 21.936 29.844  29.863  1.00 68.48  ?  29  GLN A OE1   1 
ATOM   150  N NE2   . GLN A 1 23  ? 22.239 31.980  30.531  1.00 65.84  ?  29  GLN A NE2   1 
ATOM   151  N N     . LEU A 1 24  ? 27.774 30.533  29.659  1.00 50.52  ?  30  LEU A N     1 
ATOM   152  C CA    . LEU A 1 24  ? 29.022 31.011  30.246  1.00 47.99  ?  30  LEU A CA    1 
ATOM   153  C C     . LEU A 1 24  ? 29.628 32.132  29.427  1.00 47.65  ?  30  LEU A C     1 
ATOM   154  O O     . LEU A 1 24  ? 30.237 33.057  29.975  1.00 51.66  ?  30  LEU A O     1 
ATOM   155  C CB    . LEU A 1 24  ? 30.018 29.856  30.361  1.00 46.00  ?  30  LEU A CB    1 
ATOM   156  C CG    . LEU A 1 24  ? 29.606 28.767  31.342  1.00 49.50  ?  30  LEU A CG    1 
ATOM   157  C CD1   . LEU A 1 24  ? 30.350 27.488  31.080  1.00 50.29  ?  30  LEU A CD1   1 
ATOM   158  C CD2   . LEU A 1 24  ? 29.839 29.243  32.792  1.00 48.19  ?  30  LEU A CD2   1 
ATOM   159  N N     . GLN A 1 25  ? 29.497 32.062  28.105  1.00 48.53  ?  31  GLN A N     1 
ATOM   160  C CA    . GLN A 1 25  ? 30.030 33.144  27.295  1.00 49.61  ?  31  GLN A CA    1 
ATOM   161  C C     . GLN A 1 25  ? 29.239 34.432  27.498  1.00 50.35  ?  31  GLN A C     1 
ATOM   162  O O     . GLN A 1 25  ? 29.821 35.519  27.457  1.00 57.30  ?  31  GLN A O     1 
ATOM   163  C CB    . GLN A 1 25  ? 30.057 32.737  25.830  1.00 49.22  ?  31  GLN A CB    1 
ATOM   164  C CG    . GLN A 1 25  ? 30.874 33.685  24.984  1.00 52.55  ?  31  GLN A CG    1 
ATOM   165  C CD    . GLN A 1 25  ? 31.279 33.090  23.645  1.00 59.65  ?  31  GLN A CD    1 
ATOM   166  O OE1   . GLN A 1 25  ? 30.444 32.944  22.745  1.00 54.47  ?  31  GLN A OE1   1 
ATOM   167  N NE2   . GLN A 1 25  ? 32.571 32.750  23.500  1.00 58.42  ?  31  GLN A NE2   1 
ATOM   168  N N     . ALA A 1 26  ? 27.929 34.336  27.757  1.00 49.10  ?  32  ALA A N     1 
ATOM   169  C CA    . ALA A 1 26  ? 27.119 35.530  27.983  1.00 46.04  ?  32  ALA A CA    1 
ATOM   170  C C     . ALA A 1 26  ? 27.412 36.187  29.328  1.00 48.80  ?  32  ALA A C     1 
ATOM   171  O O     . ALA A 1 26  ? 27.275 37.404  29.459  1.00 50.38  ?  32  ALA A O     1 
ATOM   172  C CB    . ALA A 1 26  ? 25.632 35.194  27.893  1.00 40.56  ?  32  ALA A CB    1 
ATOM   173  N N     . LEU A 1 27  ? 27.783 35.409  30.339  1.00 52.17  ?  33  LEU A N     1 
ATOM   174  C CA    . LEU A 1 27  ? 28.120 35.933  31.656  1.00 53.25  ?  33  LEU A CA    1 
ATOM   175  C C     . LEU A 1 27  ? 29.586 36.319  31.789  1.00 54.71  ?  33  LEU A C     1 
ATOM   176  O O     . LEU A 1 27  ? 29.986 36.801  32.853  1.00 59.39  ?  33  LEU A O     1 
ATOM   177  C CB    . LEU A 1 27  ? 27.787 34.901  32.732  1.00 53.25  ?  33  LEU A CB    1 
ATOM   178  C CG    . LEU A 1 27  ? 26.436 34.210  32.613  1.00 50.96  ?  33  LEU A CG    1 
ATOM   179  C CD1   . LEU A 1 27  ? 26.531 32.847  33.272  1.00 51.02  ?  33  LEU A CD1   1 
ATOM   180  C CD2   . LEU A 1 27  ? 25.338 35.057  33.233  1.00 44.22  ?  33  LEU A CD2   1 
ATOM   181  N N     . ASN A 1 28  ? 30.393 36.098  30.753  1.00 56.56  ?  34  ASN A N     1 
ATOM   182  C CA    . ASN A 1 28  ? 31.819 36.417  30.769  1.00 59.35  ?  34  ASN A CA    1 
ATOM   183  C C     . ASN A 1 28  ? 32.577 35.617  31.829  1.00 58.57  ?  34  ASN A C     1 
ATOM   184  O O     . ASN A 1 28  ? 33.578 36.088  32.378  1.00 59.55  ?  34  ASN A O     1 
ATOM   185  C CB    . ASN A 1 28  ? 32.050 37.918  30.952  1.00 60.28  ?  34  ASN A CB    1 
ATOM   186  C CG    . ASN A 1 28  ? 33.434 38.337  30.523  1.00 70.82  ?  34  ASN A CG    1 
ATOM   187  O OD1   . ASN A 1 28  ? 34.148 37.575  29.852  1.00 69.50  ?  34  ASN A OD1   1 
ATOM   188  N ND2   . ASN A 1 28  ? 33.840 39.543  30.921  1.00 77.53  ?  34  ASN A ND2   1 
ATOM   189  N N     . VAL A 1 29  ? 32.105 34.405  32.104  1.00 52.70  ?  35  VAL A N     1 
ATOM   190  C CA    . VAL A 1 29  ? 32.794 33.476  33.005  1.00 51.19  ?  35  VAL A CA    1 
ATOM   191  C C     . VAL A 1 29  ? 33.890 32.750  32.225  1.00 57.13  ?  35  VAL A C     1 
ATOM   192  O O     . VAL A 1 29  ? 33.626 32.257  31.115  1.00 55.60  ?  35  VAL A O     1 
ATOM   193  C CB    . VAL A 1 29  ? 31.810 32.479  33.591  1.00 51.99  ?  35  VAL A CB    1 
ATOM   194  C CG1   . VAL A 1 29  ? 32.551 31.430  34.378  1.00 50.76  ?  35  VAL A CG1   1 
ATOM   195  C CG2   . VAL A 1 29  ? 30.771 33.179  34.441  1.00 48.88  ?  35  VAL A CG2   1 
ATOM   196  N N     . PRO A 1 30  ? 35.109 32.655  32.751  1.00 58.63  ?  36  PRO A N     1 
ATOM   197  C CA    . PRO A 1 30  ? 36.152 31.912  32.032  1.00 57.86  ?  36  PRO A CA    1 
ATOM   198  C C     . PRO A 1 30  ? 35.757 30.456  31.863  1.00 54.69  ?  36  PRO A C     1 
ATOM   199  O O     . PRO A 1 30  ? 35.294 29.803  32.799  1.00 53.88  ?  36  PRO A O     1 
ATOM   200  C CB    . PRO A 1 30  ? 37.385 32.054  32.933  1.00 58.13  ?  36  PRO A CB    1 
ATOM   201  C CG    . PRO A 1 30  ? 37.101 33.209  33.798  1.00 62.74  ?  36  PRO A CG    1 
ATOM   202  C CD    . PRO A 1 30  ? 35.618 33.254  33.993  1.00 56.58  ?  36  PRO A CD    1 
ATOM   203  N N     . PHE A 1 31  ? 35.949 29.941  30.659  1.00 54.48  ?  37  PHE A N     1 
ATOM   204  C CA    . PHE A 1 31  ? 35.575 28.561  30.423  1.00 53.85  ?  37  PHE A CA    1 
ATOM   205  C C     . PHE A 1 31  ? 36.330 28.055  29.218  1.00 52.11  ?  37  PHE A C     1 
ATOM   206  O O     . PHE A 1 31  ? 36.765 28.828  28.368  1.00 54.54  ?  37  PHE A O     1 
ATOM   207  C CB    . PHE A 1 31  ? 34.064 28.404  30.212  1.00 53.90  ?  37  PHE A CB    1 
ATOM   208  C CG    . PHE A 1 31  ? 33.589 28.871  28.872  1.00 51.12  ?  37  PHE A CG    1 
ATOM   209  C CD1   . PHE A 1 31  ? 33.391 30.219  28.624  1.00 48.63  ?  37  PHE A CD1   1 
ATOM   210  C CD2   . PHE A 1 31  ? 33.334 27.955  27.852  1.00 52.10  ?  37  PHE A CD2   1 
ATOM   211  C CE1   . PHE A 1 31  ? 32.947 30.650  27.386  1.00 50.59  ?  37  PHE A CE1   1 
ATOM   212  C CE2   . PHE A 1 31  ? 32.887 28.380  26.599  1.00 49.11  ?  37  PHE A CE2   1 
ATOM   213  C CZ    . PHE A 1 31  ? 32.695 29.722  26.368  1.00 51.89  ?  37  PHE A CZ    1 
ATOM   214  N N     . MET A 1 32  ? 36.478 26.743  29.169  1.00 53.60  ?  38  MET A N     1 
ATOM   215  C CA    . MET A 1 32  ? 37.057 26.035  28.042  1.00 54.95  ?  38  MET A CA    1 
ATOM   216  C C     . MET A 1 32  ? 36.109 24.902  27.670  1.00 54.82  ?  38  MET A C     1 
ATOM   217  O O     . MET A 1 32  ? 35.706 24.120  28.538  1.00 53.78  ?  38  MET A O     1 
ATOM   218  C CB    . MET A 1 32  ? 38.448 25.494  28.397  1.00 55.63  ?  38  MET A CB    1 
ATOM   219  C CG    . MET A 1 32  ? 39.266 25.065  27.198  1.00 63.15  ?  38  MET A CG    1 
ATOM   220  S SD    . MET A 1 32  ? 39.412 26.429  26.017  1.00 71.24  ?  38  MET A SD    1 
ATOM   221  C CE    . MET A 1 32  ? 41.113 26.275  25.472  1.00 73.35  ?  38  MET A CE    1 
ATOM   222  N N     . LEU A 1 33  ? 35.714 24.847  26.403  1.00 51.29  ?  39  LEU A N     1 
ATOM   223  C CA    . LEU A 1 33  ? 34.858 23.784  25.893  1.00 51.04  ?  39  LEU A CA    1 
ATOM   224  C C     . LEU A 1 33  ? 35.716 22.811  25.104  1.00 49.38  ?  39  LEU A C     1 
ATOM   225  O O     . LEU A 1 33  ? 36.505 23.232  24.253  1.00 50.44  ?  39  LEU A O     1 
ATOM   226  C CB    . LEU A 1 33  ? 33.746 24.353  25.008  1.00 49.46  ?  39  LEU A CB    1 
ATOM   227  C CG    . LEU A 1 33  ? 32.968 23.416  24.069  1.00 45.32  ?  39  LEU A CG    1 
ATOM   228  C CD1   . LEU A 1 33  ? 31.958 22.581  24.838  1.00 44.31  ?  39  LEU A CD1   1 
ATOM   229  C CD2   . LEU A 1 33  ? 32.264 24.204  22.966  1.00 44.50  ?  39  LEU A CD2   1 
ATOM   230  N N     . VAL A 1 34  ? 35.572 21.517  25.391  1.00 51.00  ?  40  VAL A N     1 
ATOM   231  C CA    . VAL A 1 34  ? 36.357 20.481  24.723  1.00 50.60  ?  40  VAL A CA    1 
ATOM   232  C C     . VAL A 1 34  ? 35.430 19.528  23.985  1.00 50.80  ?  40  VAL A C     1 
ATOM   233  O O     . VAL A 1 34  ? 34.419 19.071  24.534  1.00 51.43  ?  40  VAL A O     1 
ATOM   234  C CB    . VAL A 1 34  ? 37.240 19.678  25.695  1.00 51.79  ?  40  VAL A CB    1 
ATOM   235  C CG1   . VAL A 1 34  ? 38.469 19.189  24.979  1.00 51.92  ?  40  VAL A CG1   1 
ATOM   236  C CG2   . VAL A 1 34  ? 37.582 20.499  26.935  1.00 56.11  ?  40  VAL A CG2   1 
ATOM   237  N N     . ASP A 1 35  ? 35.797 19.221  22.746  1.00 48.17  ?  41  ASP A N     1 
ATOM   238  C CA    . ASP A 1 35  ? 35.127 18.231  21.923  1.00 49.89  ?  41  ASP A CA    1 
ATOM   239  C C     . ASP A 1 35  ? 36.188 17.579  21.048  1.00 53.03  ?  41  ASP A C     1 
ATOM   240  O O     . ASP A 1 35  ? 37.192 18.208  20.711  1.00 53.26  ?  41  ASP A O     1 
ATOM   241  C CB    . ASP A 1 35  ? 34.036 18.874  21.059  1.00 48.13  ?  41  ASP A CB    1 
ATOM   242  C CG    . ASP A 1 35  ? 33.029 17.869  20.544  1.00 50.18  ?  41  ASP A CG    1 
ATOM   243  O OD1   . ASP A 1 35  ? 33.245 17.302  19.448  1.00 52.65  -1 41  ASP A OD1   1 
ATOM   244  O OD2   . ASP A 1 35  ? 32.019 17.637  21.238  1.00 49.65  ?  41  ASP A OD2   1 
ATOM   245  N N     . MET A 1 36  ? 35.974 16.309  20.692  1.00 53.01  ?  42  MET A N     1 
ATOM   246  C CA    . MET A 1 36  ? 36.923 15.648  19.797  1.00 53.32  ?  42  MET A CA    1 
ATOM   247  C C     . MET A 1 36  ? 36.776 16.125  18.351  1.00 51.90  ?  42  MET A C     1 
ATOM   248  O O     . MET A 1 36  ? 37.750 16.107  17.597  1.00 55.40  ?  42  MET A O     1 
ATOM   249  C CB    . MET A 1 36  ? 36.764 14.128  19.892  1.00 56.32  ?  42  MET A CB    1 
ATOM   250  C CG    . MET A 1 36  ? 35.453 13.600  19.361  1.00 55.58  ?  42  MET A CG    1 
ATOM   251  S SD    . MET A 1 36  ? 35.230 11.825  19.589  1.00 65.83  ?  42  MET A SD    1 
ATOM   252  C CE    . MET A 1 36  ? 34.412 11.722  21.173  1.00 54.55  ?  42  MET A CE    1 
ATOM   253  N N     . LYS A 1 37  ? 35.590 16.557  17.941  1.00 49.65  ?  43  LYS A N     1 
ATOM   254  C CA    . LYS A 1 37  ? 35.419 17.113  16.610  1.00 48.82  ?  43  LYS A CA    1 
ATOM   255  C C     . LYS A 1 37  ? 35.710 18.609  16.625  1.00 49.96  ?  43  LYS A C     1 
ATOM   256  O O     . LYS A 1 37  ? 35.817 19.237  17.676  1.00 50.57  ?  43  LYS A O     1 
ATOM   257  C CB    . LYS A 1 37  ? 34.009 16.850  16.099  1.00 44.34  ?  43  LYS A CB    1 
ATOM   258  C CG    . LYS A 1 37  ? 33.534 15.473  16.437  1.00 46.49  ?  43  LYS A CG    1 
ATOM   259  C CD    . LYS A 1 37  ? 32.200 15.168  15.773  1.00 50.19  ?  43  LYS A CD    1 
ATOM   260  C CE    . LYS A 1 37  ? 31.140 16.191  16.133  1.00 50.00  ?  43  LYS A CE    1 
ATOM   261  N NZ    . LYS A 1 37  ? 30.915 16.371  17.599  1.00 44.97  ?  43  LYS A NZ    1 
ATOM   262  N N     . ASP A 1 38  ? 35.832 19.193  15.441  1.00 47.69  ?  44  ASP A N     1 
ATOM   263  C CA    . ASP A 1 38  ? 35.971 20.636  15.354  1.00 45.86  ?  44  ASP A CA    1 
ATOM   264  C C     . ASP A 1 38  ? 34.651 21.330  15.082  1.00 45.84  ?  44  ASP A C     1 
ATOM   265  O O     . ASP A 1 38  ? 34.628 22.557  14.951  1.00 47.95  ?  44  ASP A O     1 
ATOM   266  C CB    . ASP A 1 38  ? 36.964 21.027  14.273  1.00 48.28  ?  44  ASP A CB    1 
ATOM   267  C CG    . ASP A 1 38  ? 36.419 20.759  12.868  1.00 58.55  ?  44  ASP A CG    1 
ATOM   268  O OD1   . ASP A 1 38  ? 35.825 19.667  12.675  1.00 58.64  ?  44  ASP A OD1   1 
ATOM   269  O OD2   . ASP A 1 38  ? 36.570 21.636  11.968  1.00 62.81  -1 44  ASP A OD2   1 
ATOM   270  N N     . SER A 1 39  ? 33.548 20.592  14.996  1.00 43.76  ?  45  SER A N     1 
ATOM   271  C CA    . SER A 1 39  ? 32.281 21.260  14.762  1.00 45.50  ?  45  SER A CA    1 
ATOM   272  C C     . SER A 1 39  ? 31.160 20.506  15.457  1.00 44.21  ?  45  SER A C     1 
ATOM   273  O O     . SER A 1 39  ? 31.237 19.298  15.677  1.00 46.84  ?  45  SER A O     1 
ATOM   274  C CB    . SER A 1 39  ? 31.978 21.423  13.260  1.00 45.89  ?  45  SER A CB    1 
ATOM   275  O OG    . SER A 1 39  ? 32.620 20.438  12.482  1.00 46.29  ?  45  SER A OG    1 
ATOM   276  N N     . PHE A 1 40  ? 30.129 21.253  15.826  1.00 42.10  ?  46  PHE A N     1 
ATOM   277  C CA    . PHE A 1 40  ? 28.959 20.672  16.451  1.00 39.53  ?  46  PHE A CA    1 
ATOM   278  C C     . PHE A 1 40  ? 28.156 19.904  15.410  1.00 44.65  ?  46  PHE A C     1 
ATOM   279  O O     . PHE A 1 40  ? 28.092 20.290  14.235  1.00 42.75  ?  46  PHE A O     1 
ATOM   280  C CB    . PHE A 1 40  ? 28.122 21.781  17.099  1.00 43.17  ?  46  PHE A CB    1 
ATOM   281  C CG    . PHE A 1 40  ? 26.728 21.372  17.422  1.00 40.58  ?  46  PHE A CG    1 
ATOM   282  C CD1   . PHE A 1 40  ? 26.451 20.708  18.600  1.00 40.20  ?  46  PHE A CD1   1 
ATOM   283  C CD2   . PHE A 1 40  ? 25.693 21.634  16.537  1.00 40.61  ?  46  PHE A CD2   1 
ATOM   284  C CE1   . PHE A 1 40  ? 25.178 20.306  18.895  1.00 38.97  ?  46  PHE A CE1   1 
ATOM   285  C CE2   . PHE A 1 40  ? 24.419 21.242  16.823  1.00 43.37  ?  46  PHE A CE2   1 
ATOM   286  C CZ    . PHE A 1 40  ? 24.161 20.575  18.015  1.00 44.11  ?  46  PHE A CZ    1 
ATOM   287  N N     . HIS A 1 41  ? 27.549 18.801  15.844  1.00 44.36  ?  47  HIS A N     1 
ATOM   288  C CA    . HIS A 1 41  ? 26.859 17.882  14.950  1.00 39.17  ?  47  HIS A CA    1 
ATOM   289  C C     . HIS A 1 41  ? 25.404 17.838  15.359  1.00 41.87  ?  47  HIS A C     1 
ATOM   290  O O     . HIS A 1 41  ? 25.077 17.336  16.436  1.00 44.88  ?  47  HIS A O     1 
ATOM   291  C CB    . HIS A 1 41  ? 27.474 16.492  15.007  1.00 36.77  ?  47  HIS A CB    1 
ATOM   292  C CG    . HIS A 1 41  ? 26.771 15.492  14.139  1.00 44.41  ?  47  HIS A CG    1 
ATOM   293  N ND1   . HIS A 1 41  ? 26.043 15.852  13.023  1.00 41.22  ?  47  HIS A ND1   1 
ATOM   294  C CD2   . HIS A 1 41  ? 26.692 14.144  14.219  1.00 41.05  ?  47  HIS A CD2   1 
ATOM   295  C CE1   . HIS A 1 41  ? 25.544 14.774  12.457  1.00 39.24  ?  47  HIS A CE1   1 
ATOM   296  N NE2   . HIS A 1 41  ? 25.921 13.725  13.163  1.00 45.31  ?  47  HIS A NE2   1 
ATOM   297  N N     . HIS A 1 42  ? 24.525 18.359  14.512  1.00 40.72  ?  48  HIS A N     1 
ATOM   298  C CA    . HIS A 1 42  ? 23.105 18.340  14.835  1.00 38.89  ?  48  HIS A CA    1 
ATOM   299  C C     . HIS A 1 42  ? 22.577 16.942  14.537  1.00 41.59  ?  48  HIS A C     1 
ATOM   300  O O     . HIS A 1 42  ? 21.897 16.701  13.537  1.00 47.56  ?  48  HIS A O     1 
ATOM   301  C CB    . HIS A 1 42  ? 22.373 19.397  14.044  1.00 38.92  ?  48  HIS A CB    1 
ATOM   302  C CG    . HIS A 1 42  ? 20.944 19.557  14.434  1.00 40.48  ?  48  HIS A CG    1 
ATOM   303  N ND1   . HIS A 1 42  ? 20.510 20.572  15.252  1.00 43.23  ?  48  HIS A ND1   1 
ATOM   304  C CD2   . HIS A 1 42  ? 19.842 18.850  14.095  1.00 45.45  ?  48  HIS A CD2   1 
ATOM   305  C CE1   . HIS A 1 42  ? 19.202 20.478  15.410  1.00 44.51  ?  48  HIS A CE1   1 
ATOM   306  N NE2   . HIS A 1 42  ? 18.772 19.442  14.716  1.00 42.64  ?  48  HIS A NE2   1 
ATOM   307  N N     . ASN A 1 43  ? 22.904 15.993  15.423  1.00 40.92  ?  49  ASN A N     1 
ATOM   308  C CA    . ASN A 1 43  ? 22.706 14.593  15.076  1.00 38.23  ?  49  ASN A CA    1 
ATOM   309  C C     . ASN A 1 43  ? 21.239 14.230  14.891  1.00 42.00  ?  49  ASN A C     1 
ATOM   310  O O     . ASN A 1 43  ? 20.949 13.172  14.321  1.00 42.24  ?  49  ASN A O     1 
ATOM   311  C CB    . ASN A 1 43  ? 23.369 13.677  16.107  1.00 39.29  ?  49  ASN A CB    1 
ATOM   312  C CG    . ASN A 1 43  ? 22.861 13.896  17.533  1.00 44.95  ?  49  ASN A CG    1 
ATOM   313  O OD1   . ASN A 1 43  ? 21.824 14.539  17.769  1.00 46.01  ?  49  ASN A OD1   1 
ATOM   314  N ND2   . ASN A 1 43  ? 23.599 13.349  18.495  1.00 39.78  ?  49  ASN A ND2   1 
ATOM   315  N N     . VAL A 1 44  ? 20.307 15.086  15.313  1.00 43.52  ?  50  VAL A N     1 
ATOM   316  C CA    . VAL A 1 44  ? 18.897 14.790  15.075  1.00 46.37  ?  50  VAL A CA    1 
ATOM   317  C C     . VAL A 1 44  ? 18.576 14.812  13.573  1.00 46.11  ?  50  VAL A C     1 
ATOM   318  O O     . VAL A 1 44  ? 17.605 14.176  13.139  1.00 50.27  ?  50  VAL A O     1 
ATOM   319  C CB    . VAL A 1 44  ? 18.018 15.765  15.897  1.00 44.33  ?  50  VAL A CB    1 
ATOM   320  C CG1   . VAL A 1 44  ? 16.533 15.541  15.635  1.00 48.28  ?  50  VAL A CG1   1 
ATOM   321  C CG2   . VAL A 1 44  ? 18.295 15.596  17.386  1.00 47.83  ?  50  VAL A CG2   1 
ATOM   322  N N     . ALA A 1 45  ? 19.373 15.503  12.755  1.00 39.17  ?  51  ALA A N     1 
ATOM   323  C CA    . ALA A 1 45  ? 19.173 15.463  11.309  1.00 44.97  ?  51  ALA A CA    1 
ATOM   324  C C     . ALA A 1 45  ? 20.118 14.505  10.600  1.00 42.72  ?  51  ALA A C     1 
ATOM   325  O O     . ALA A 1 45  ? 20.179 14.531  9.374   1.00 38.52  ?  51  ALA A O     1 
ATOM   326  C CB    . ALA A 1 45  ? 19.318 16.852  10.694  1.00 42.64  ?  51  ALA A CB    1 
ATOM   327  N N     . ALA A 1 46  ? 20.841 13.655  11.337  1.00 40.91  ?  52  ALA A N     1 
ATOM   328  C CA    . ALA A 1 46  ? 21.819 12.779  10.702  1.00 39.79  ?  52  ALA A CA    1 
ATOM   329  C C     . ALA A 1 46  ? 21.188 11.838  9.678   1.00 43.79  ?  52  ALA A C     1 
ATOM   330  O O     . ALA A 1 46  ? 21.831 11.492  8.684   1.00 43.83  ?  52  ALA A O     1 
ATOM   331  C CB    . ALA A 1 46  ? 22.576 11.974  11.752  1.00 35.69  ?  52  ALA A CB    1 
ATOM   332  N N     . LEU A 1 47  ? 19.947 11.400  9.890   1.00 44.70  ?  53  LEU A N     1 
ATOM   333  C CA    . LEU A 1 47  ? 19.395 10.428  8.952   1.00 44.18  ?  53  LEU A CA    1 
ATOM   334  C C     . LEU A 1 47  ? 18.955 11.101  7.655   1.00 44.94  ?  53  LEU A C     1 
ATOM   335  O O     . LEU A 1 47  ? 19.169 10.559  6.567   1.00 46.27  ?  53  LEU A O     1 
ATOM   336  C CB    . LEU A 1 47  ? 18.236 9.662   9.591   1.00 44.05  ?  53  LEU A CB    1 
ATOM   337  C CG    . LEU A 1 47  ? 18.508 9.068   10.975  1.00 46.92  ?  53  LEU A CG    1 
ATOM   338  C CD1   . LEU A 1 47  ? 17.284 8.318   11.484  1.00 43.63  ?  53  LEU A CD1   1 
ATOM   339  C CD2   . LEU A 1 47  ? 19.749 8.166   10.967  1.00 46.44  ?  53  LEU A CD2   1 
ATOM   340  N N     . ARG A 1 48  ? 18.345 12.283  7.741   1.00 45.12  ?  54  ARG A N     1 
ATOM   341  C CA    . ARG A 1 48  ? 18.060 13.015  6.520   1.00 45.18  ?  54  ARG A CA    1 
ATOM   342  C C     . ARG A 1 48  ? 19.349 13.346  5.771   1.00 45.89  ?  54  ARG A C     1 
ATOM   343  O O     . ARG A 1 48  ? 19.383 13.301  4.539   1.00 48.85  ?  54  ARG A O     1 
ATOM   344  C CB    . ARG A 1 48  ? 17.274 14.286  6.821   1.00 44.13  ?  54  ARG A CB    1 
ATOM   345  C CG    . ARG A 1 48  ? 17.047 15.092  5.555   1.00 47.29  ?  54  ARG A CG    1 
ATOM   346  C CD    . ARG A 1 48  ? 15.712 15.757  5.518   1.00 52.63  ?  54  ARG A CD    1 
ATOM   347  N NE    . ARG A 1 48  ? 14.647 14.894  6.013   1.00 50.40  ?  54  ARG A NE    1 
ATOM   348  C CZ    . ARG A 1 48  ? 13.544 15.360  6.577   1.00 46.68  ?  54  ARG A CZ    1 
ATOM   349  N NH1   . ARG A 1 48  ? 13.322 16.660  6.676   1.00 44.10  ?  54  ARG A NH1   1 
ATOM   350  N NH2   . ARG A 1 48  ? 12.666 14.505  7.090   1.00 47.67  ?  54  ARG A NH2   1 
ATOM   351  N N     . ALA A 1 49  ? 20.421 13.684  6.495   1.00 46.45  ?  55  ALA A N     1 
ATOM   352  C CA    . ALA A 1 49  ? 21.697 13.936  5.841   1.00 42.67  ?  55  ALA A CA    1 
ATOM   353  C C     . ALA A 1 49  ? 22.269 12.676  5.209   1.00 44.80  ?  55  ALA A C     1 
ATOM   354  O O     . ALA A 1 49  ? 23.157 12.770  4.360   1.00 45.54  ?  55  ALA A O     1 
ATOM   355  C CB    . ALA A 1 49  ? 22.700 14.525  6.819   1.00 34.57  ?  55  ALA A CB    1 
ATOM   356  N N     . SER A 1 50  ? 21.773 11.505  5.595   1.00 48.60  ?  56  SER A N     1 
ATOM   357  C CA    . SER A 1 50  ? 22.184 10.257  4.965   1.00 49.33  ?  56  SER A CA    1 
ATOM   358  C C     . SER A 1 50  ? 21.490 9.986   3.645   1.00 47.88  ?  56  SER A C     1 
ATOM   359  O O     . SER A 1 50  ? 21.840 9.003   2.995   1.00 48.83  ?  56  SER A O     1 
ATOM   360  C CB    . SER A 1 50  ? 21.896 9.070   5.875   1.00 43.60  ?  56  SER A CB    1 
ATOM   361  O OG    . SER A 1 50  ? 22.769 9.089   6.950   1.00 46.86  ?  56  SER A OG    1 
ATOM   362  N N     . VAL A 1 51  ? 20.496 10.785  3.258   1.00 47.11  ?  57  VAL A N     1 
ATOM   363  C CA    . VAL A 1 51  ? 19.683 10.452  2.095   1.00 48.93  ?  57  VAL A CA    1 
ATOM   364  C C     . VAL A 1 51  ? 19.436 11.656  1.186   1.00 51.39  ?  57  VAL A C     1 
ATOM   365  O O     . VAL A 1 51  ? 19.036 11.486  0.028   1.00 51.38  ?  57  VAL A O     1 
ATOM   366  C CB    . VAL A 1 51  ? 18.345 9.838   2.537   1.00 46.36  ?  57  VAL A CB    1 
ATOM   367  C CG1   . VAL A 1 51  ? 18.567 8.545   3.294   1.00 46.57  ?  57  VAL A CG1   1 
ATOM   368  C CG2   . VAL A 1 51  ? 17.594 10.829  3.389   1.00 45.97  ?  57  VAL A CG2   1 
ATOM   369  N N     . GLU A 1 52  ? 19.648 12.877  1.680   1.00 48.09  ?  58  GLU A N     1 
ATOM   370  C CA    . GLU A 1 52  ? 19.384 14.074  0.884   1.00 48.32  ?  58  GLU A CA    1 
ATOM   371  C C     . GLU A 1 52  ? 20.691 14.748  0.461   1.00 47.73  ?  58  GLU A C     1 
ATOM   372  O O     . GLU A 1 52  ? 21.476 15.171  1.312   1.00 46.56  ?  58  GLU A O     1 
ATOM   373  C CB    . GLU A 1 52  ? 18.502 15.059  1.645   1.00 49.39  ?  58  GLU A CB    1 
ATOM   374  C CG    . GLU A 1 52  ? 18.138 16.264  0.783   1.00 54.63  ?  58  GLU A CG    1 
ATOM   375  C CD    . GLU A 1 52  ? 17.521 17.419  1.566   1.00 54.29  ?  58  GLU A CD    1 
ATOM   376  O OE1   . GLU A 1 52  ? 16.640 17.168  2.415   1.00 58.98  ?  58  GLU A OE1   1 
ATOM   377  O OE2   . GLU A 1 52  ? 17.913 18.585  1.319   1.00 58.11  -1 58  GLU A OE2   1 
ATOM   378  N N     . THR A 1 53  ? 20.904 14.866  -0.856  1.00 48.68  ?  59  THR A N     1 
ATOM   379  C CA    . THR A 1 53  ? 22.107 15.505  -1.387  1.00 47.96  ?  59  THR A CA    1 
ATOM   380  C C     . THR A 1 53  ? 22.241 16.935  -0.871  1.00 49.62  ?  59  THR A C     1 
ATOM   381  O O     . THR A 1 53  ? 21.280 17.712  -0.889  1.00 48.65  ?  59  THR A O     1 
ATOM   382  C CB    . THR A 1 53  ? 22.069 15.518  -2.923  1.00 49.80  ?  59  THR A CB    1 
ATOM   383  O OG1   . THR A 1 53  ? 22.051 14.174  -3.414  1.00 54.40  ?  59  THR A OG1   1 
ATOM   384  C CG2   . THR A 1 53  ? 23.302 16.216  -3.507  1.00 40.02  ?  59  THR A CG2   1 
ATOM   385  N N     . GLY A 1 54  ? 23.442 17.290  -0.427  1.00 43.23  ?  60  GLY A N     1 
ATOM   386  C CA    . GLY A 1 54  ? 23.682 18.649  0.022   1.00 44.82  ?  60  GLY A CA    1 
ATOM   387  C C     . GLY A 1 54  ? 23.051 19.036  1.346   1.00 50.22  ?  60  GLY A C     1 
ATOM   388  O O     . GLY A 1 54  ? 23.147 20.205  1.740   1.00 53.91  ?  60  GLY A O     1 
ATOM   389  N N     . PHE A 1 55  ? 22.396 18.106  2.047   1.00 42.89  ?  61  PHE A N     1 
ATOM   390  C CA    . PHE A 1 55  ? 21.837 18.474  3.338   1.00 44.34  ?  61  PHE A CA    1 
ATOM   391  C C     . PHE A 1 55  ? 22.898 18.492  4.422   1.00 45.09  ?  61  PHE A C     1 
ATOM   392  O O     . PHE A 1 55  ? 22.840 19.331  5.315   1.00 45.30  ?  61  PHE A O     1 
ATOM   393  C CB    . PHE A 1 55  ? 20.722 17.521  3.737   1.00 42.44  ?  61  PHE A CB    1 
ATOM   394  C CG    . PHE A 1 55  ? 19.953 17.965  4.939   1.00 46.94  ?  61  PHE A CG    1 
ATOM   395  C CD1   . PHE A 1 55  ? 19.184 19.105  4.893   1.00 51.87  ?  61  PHE A CD1   1 
ATOM   396  C CD2   . PHE A 1 55  ? 19.982 17.242  6.116   1.00 44.47  ?  61  PHE A CD2   1 
ATOM   397  C CE1   . PHE A 1 55  ? 18.467 19.528  6.013   1.00 49.60  ?  61  PHE A CE1   1 
ATOM   398  C CE2   . PHE A 1 55  ? 19.273 17.670  7.215   1.00 45.68  ?  61  PHE A CE2   1 
ATOM   399  C CZ    . PHE A 1 55  ? 18.515 18.807  7.166   1.00 44.81  ?  61  PHE A CZ    1 
ATOM   400  N N     . ALA A 1 56  ? 23.902 17.626  4.333   1.00 45.06  ?  62  ALA A N     1 
ATOM   401  C CA    . ALA A 1 56  ? 24.803 17.430  5.462   1.00 40.92  ?  62  ALA A CA    1 
ATOM   402  C C     . ALA A 1 56  ? 25.519 18.711  5.865   1.00 42.00  ?  62  ALA A C     1 
ATOM   403  O O     . ALA A 1 56  ? 25.865 18.875  7.037   1.00 44.28  ?  62  ALA A O     1 
ATOM   404  C CB    . ALA A 1 56  ? 25.816 16.338  5.139   1.00 42.63  ?  62  ALA A CB    1 
ATOM   405  N N     . LYS A 1 57  ? 25.738 19.639  4.933   1.00 46.06  ?  63  LYS A N     1 
ATOM   406  C CA    . LYS A 1 57  ? 26.391 20.883  5.328   1.00 43.48  ?  63  LYS A CA    1 
ATOM   407  C C     . LYS A 1 57  ? 25.492 21.773  6.183   1.00 46.77  ?  63  LYS A C     1 
ATOM   408  O O     . LYS A 1 57  ? 25.986 22.757  6.734   1.00 48.21  ?  63  LYS A O     1 
ATOM   409  C CB    . LYS A 1 57  ? 26.879 21.651  4.106   1.00 40.68  ?  63  LYS A CB    1 
ATOM   410  C CG    . LYS A 1 57  ? 25.781 22.171  3.207   1.00 47.14  ?  63  LYS A CG    1 
ATOM   411  C CD    . LYS A 1 57  ? 26.298 22.288  1.788   1.00 53.33  ?  63  LYS A CD    1 
ATOM   412  C CE    . LYS A 1 57  ? 26.045 23.645  1.221   1.00 60.29  ?  63  LYS A CE    1 
ATOM   413  N NZ    . LYS A 1 57  ? 24.584 23.879  1.214   1.00 67.29  ?  63  LYS A NZ    1 
ATOM   414  N N     . LYS A 1 58  ? 24.200 21.450  6.311   1.00 46.82  ?  64  LYS A N     1 
ATOM   415  C CA    . LYS A 1 58  ? 23.310 22.095  7.270   1.00 46.08  ?  64  LYS A CA    1 
ATOM   416  C C     . LYS A 1 58  ? 23.435 21.525  8.684   1.00 43.15  ?  64  LYS A C     1 
ATOM   417  O O     . LYS A 1 58  ? 22.827 22.071  9.612   1.00 42.75  ?  64  LYS A O     1 
ATOM   418  C CB    . LYS A 1 58  ? 21.845 21.981  6.825   1.00 44.04  ?  64  LYS A CB    1 
ATOM   419  C CG    . LYS A 1 58  ? 21.550 22.386  5.383   1.00 51.81  ?  64  LYS A CG    1 
ATOM   420  C CD    . LYS A 1 58  ? 21.915 23.842  5.118   1.00 58.52  ?  64  LYS A CD    1 
ATOM   421  C CE    . LYS A 1 58  ? 21.368 24.314  3.772   1.00 63.66  ?  64  LYS A CE    1 
ATOM   422  N NZ    . LYS A 1 58  ? 21.863 23.467  2.635   1.00 68.87  ?  64  LYS A NZ    1 
ATOM   423  N N     . THR A 1 59  ? 24.213 20.469  8.881   1.00 39.12  ?  65  THR A N     1 
ATOM   424  C CA    . THR A 1 59  ? 24.200 19.739  10.140  1.00 42.11  ?  65  THR A CA    1 
ATOM   425  C C     . THR A 1 59  ? 25.525 19.777  10.896  1.00 40.65  ?  65  THR A C     1 
ATOM   426  O O     . THR A 1 59  ? 25.651 19.082  11.898  1.00 42.85  ?  65  THR A O     1 
ATOM   427  C CB    . THR A 1 59  ? 23.815 18.277  9.901   1.00 41.52  ?  65  THR A CB    1 
ATOM   428  O OG1   . THR A 1 59  ? 24.815 17.659  9.082   1.00 42.33  ?  65  THR A OG1   1 
ATOM   429  C CG2   . THR A 1 59  ? 22.467 18.173  9.201   1.00 38.40  ?  65  THR A CG2   1 
ATOM   430  N N     . PHE A 1 60  ? 26.524 20.536  10.442  1.00 42.93  ?  66  PHE A N     1 
ATOM   431  C CA    . PHE A 1 60  ? 27.780 20.713  11.174  1.00 42.66  ?  66  PHE A CA    1 
ATOM   432  C C     . PHE A 1 60  ? 28.081 22.195  11.334  1.00 43.07  ?  66  PHE A C     1 
ATOM   433  O O     . PHE A 1 60  ? 28.012 22.944  10.358  1.00 42.69  ?  66  PHE A O     1 
ATOM   434  C CB    . PHE A 1 60  ? 28.955 20.021  10.474  1.00 37.06  ?  66  PHE A CB    1 
ATOM   435  C CG    . PHE A 1 60  ? 28.924 18.527  10.591  1.00 37.92  ?  66  PHE A CG    1 
ATOM   436  C CD1   . PHE A 1 60  ? 29.390 17.897  11.732  1.00 42.05  ?  66  PHE A CD1   1 
ATOM   437  C CD2   . PHE A 1 60  ? 28.422 17.749  9.571   1.00 41.24  ?  66  PHE A CD2   1 
ATOM   438  C CE1   . PHE A 1 60  ? 29.366 16.522  11.848  1.00 41.52  ?  66  PHE A CE1   1 
ATOM   439  C CE2   . PHE A 1 60  ? 28.397 16.365  9.681   1.00 40.34  ?  66  PHE A CE2   1 
ATOM   440  C CZ    . PHE A 1 60  ? 28.869 15.758  10.823  1.00 44.07  ?  66  PHE A CZ    1 
ATOM   441  N N     . ILE A 1 61  ? 28.391 22.629  12.561  1.00 41.61  ?  67  ILE A N     1 
ATOM   442  C CA    . ILE A 1 61  ? 28.651 24.042  12.821  1.00 42.95  ?  67  ILE A CA    1 
ATOM   443  C C     . ILE A 1 61  ? 29.989 24.209  13.527  1.00 43.30  ?  67  ILE A C     1 
ATOM   444  O O     . ILE A 1 61  ? 30.204 23.646  14.606  1.00 44.14  ?  67  ILE A O     1 
ATOM   445  C CB    . ILE A 1 61  ? 27.528 24.693  13.639  1.00 42.83  ?  67  ILE A CB    1 
ATOM   446  C CG1   . ILE A 1 61  ? 26.179 24.172  13.155  1.00 42.62  ?  67  ILE A CG1   1 
ATOM   447  C CG2   . ILE A 1 61  ? 27.624 26.176  13.508  1.00 41.32  ?  67  ILE A CG2   1 
ATOM   448  C CD1   . ILE A 1 61  ? 24.996 24.738  13.866  1.00 41.43  ?  67  ILE A CD1   1 
ATOM   449  N N     . SER A 1 62  ? 30.868 25.000  12.921  1.00 42.05  ?  68  SER A N     1 
ATOM   450  C CA    . SER A 1 62  ? 32.196 25.272  13.459  1.00 44.01  ?  68  SER A CA    1 
ATOM   451  C C     . SER A 1 62  ? 32.146 25.774  14.908  1.00 45.02  ?  68  SER A C     1 
ATOM   452  O O     . SER A 1 62  ? 31.467 26.760  15.221  1.00 43.94  ?  68  SER A O     1 
ATOM   453  C CB    . SER A 1 62  ? 32.872 26.312  12.569  1.00 41.33  ?  68  SER A CB    1 
ATOM   454  O OG    . SER A 1 62  ? 34.073 26.789  13.142  1.00 49.40  ?  68  SER A OG    1 
ATOM   455  N N     . TYR A 1 63  ? 32.895 25.116  15.792  1.00 45.13  ?  69  TYR A N     1 
ATOM   456  C CA    . TYR A 1 63  ? 32.978 25.617  17.162  1.00 44.05  ?  69  TYR A CA    1 
ATOM   457  C C     . TYR A 1 63  ? 33.734 26.936  17.215  1.00 46.22  ?  69  TYR A C     1 
ATOM   458  O O     . TYR A 1 63  ? 33.291 27.895  17.863  1.00 46.02  ?  69  TYR A O     1 
ATOM   459  C CB    . TYR A 1 63  ? 33.657 24.598  18.079  1.00 43.21  ?  69  TYR A CB    1 
ATOM   460  C CG    . TYR A 1 63  ? 32.874 23.342  18.373  1.00 42.36  ?  69  TYR A CG    1 
ATOM   461  C CD1   . TYR A 1 63  ? 31.646 23.395  19.016  1.00 42.07  ?  69  TYR A CD1   1 
ATOM   462  C CD2   . TYR A 1 63  ? 33.388 22.096  18.041  1.00 44.72  ?  69  TYR A CD2   1 
ATOM   463  C CE1   . TYR A 1 63  ? 30.939 22.238  19.287  1.00 43.35  ?  69  TYR A CE1   1 
ATOM   464  C CE2   . TYR A 1 63  ? 32.697 20.937  18.304  1.00 41.51  ?  69  TYR A CE2   1 
ATOM   465  C CZ    . TYR A 1 63  ? 31.478 21.010  18.920  1.00 42.64  ?  69  TYR A CZ    1 
ATOM   466  O OH    . TYR A 1 63  ? 30.805 19.852  19.198  1.00 42.63  ?  69  TYR A OH    1 
ATOM   467  N N     . SER A 1 64  ? 34.874 27.004  16.528  1.00 46.00  ?  70  SER A N     1 
ATOM   468  C CA    . SER A 1 64  ? 35.778 28.132  16.707  1.00 46.20  ?  70  SER A CA    1 
ATOM   469  C C     . SER A 1 64  ? 35.163 29.434  16.233  1.00 49.56  ?  70  SER A C     1 
ATOM   470  O O     . SER A 1 64  ? 35.517 30.504  16.742  1.00 49.65  ?  70  SER A O     1 
ATOM   471  C CB    . SER A 1 64  ? 37.054 27.874  15.947  1.00 48.61  ?  70  SER A CB    1 
ATOM   472  O OG    . SER A 1 64  ? 36.676 27.504  14.636  1.00 54.64  ?  70  SER A OG    1 
ATOM   473  N N     . VAL A 1 65  ? 34.258 29.373  15.255  1.00 48.25  ?  71  VAL A N     1 
ATOM   474  C CA    . VAL A 1 65  ? 33.587 30.590  14.813  1.00 44.49  ?  71  VAL A CA    1 
ATOM   475  C C     . VAL A 1 65  ? 32.744 31.164  15.950  1.00 46.77  ?  71  VAL A C     1 
ATOM   476  O O     . VAL A 1 65  ? 32.682 32.381  16.156  1.00 49.54  ?  71  VAL A O     1 
ATOM   477  C CB    . VAL A 1 65  ? 32.759 30.300  13.545  1.00 46.82  ?  71  VAL A CB    1 
ATOM   478  C CG1   . VAL A 1 65  ? 31.786 31.436  13.244  1.00 40.84  ?  71  VAL A CG1   1 
ATOM   479  C CG2   . VAL A 1 65  ? 33.688 30.022  12.355  1.00 39.21  ?  71  VAL A CG2   1 
ATOM   480  N N     . THR A 1 66  ? 32.118 30.301  16.729  1.00 44.93  ?  72  THR A N     1 
ATOM   481  C CA    . THR A 1 66  ? 31.266 30.802  17.794  1.00 49.25  ?  72  THR A CA    1 
ATOM   482  C C     . THR A 1 66  ? 32.045 31.092  19.059  1.00 46.69  ?  72  THR A C     1 
ATOM   483  O O     . THR A 1 66  ? 31.813 32.113  19.706  1.00 46.98  ?  72  THR A O     1 
ATOM   484  C CB    . THR A 1 66  ? 30.165 29.787  18.114  1.00 51.42  ?  72  THR A CB    1 
ATOM   485  O OG1   . THR A 1 66  ? 29.332 29.593  16.958  1.00 53.90  ?  72  THR A OG1   1 
ATOM   486  C CG2   . THR A 1 66  ? 29.328 30.269  19.283  1.00 45.40  ?  72  THR A CG2   1 
ATOM   487  N N     . PHE A 1 67  ? 32.962 30.203  19.421  1.00 46.14  ?  73  PHE A N     1 
ATOM   488  C CA    . PHE A 1 67  ? 33.581 30.241  20.726  1.00 47.89  ?  73  PHE A CA    1 
ATOM   489  C C     . PHE A 1 67  ? 35.025 30.719  20.715  1.00 50.49  ?  73  PHE A C     1 
ATOM   490  O O     . PHE A 1 67  ? 35.560 31.020  21.787  1.00 53.42  ?  73  PHE A O     1 
ATOM   491  C CB    . PHE A 1 67  ? 33.481 28.856  21.377  1.00 46.90  ?  73  PHE A CB    1 
ATOM   492  C CG    . PHE A 1 67  ? 32.067 28.400  21.592  1.00 43.67  ?  73  PHE A CG    1 
ATOM   493  C CD1   . PHE A 1 67  ? 31.220 29.101  22.448  1.00 45.22  ?  73  PHE A CD1   1 
ATOM   494  C CD2   . PHE A 1 67  ? 31.580 27.274  20.957  1.00 45.48  ?  73  PHE A CD2   1 
ATOM   495  C CE1   . PHE A 1 67  ? 29.915 28.697  22.656  1.00 43.99  ?  73  PHE A CE1   1 
ATOM   496  C CE2   . PHE A 1 67  ? 30.268 26.856  21.157  1.00 44.58  ?  73  PHE A CE2   1 
ATOM   497  C CZ    . PHE A 1 67  ? 29.441 27.562  22.013  1.00 45.42  ?  73  PHE A CZ    1 
ATOM   498  N N     . LYS A 1 68  ? 35.649 30.830  19.546  1.00 50.25  ?  74  LYS A N     1 
ATOM   499  C CA    . LYS A 1 68  ? 37.013 31.346  19.382  1.00 51.06  ?  74  LYS A CA    1 
ATOM   500  C C     . LYS A 1 68  ? 37.906 30.620  20.388  1.00 55.65  ?  74  LYS A C     1 
ATOM   501  O O     . LYS A 1 68  ? 37.809 29.392  20.510  1.00 58.86  ?  74  LYS A O     1 
ATOM   502  C CB    . LYS A 1 68  ? 37.010 32.870  19.483  1.00 55.49  ?  74  LYS A CB    1 
ATOM   503  C CG    . LYS A 1 68  ? 36.390 33.625  18.289  1.00 51.91  ?  74  LYS A CG    1 
ATOM   504  C CD    . LYS A 1 68  ? 34.926 33.998  18.547  1.00 54.01  ?  74  LYS A CD    1 
ATOM   505  N N     . ASP A 1 69  ? 38.744 31.321  21.141  1.00 58.57  ?  75  ASP A N     1 
ATOM   506  C CA    . ASP A 1 69  ? 39.752 30.717  22.003  1.00 61.30  ?  75  ASP A CA    1 
ATOM   507  C C     . ASP A 1 69  ? 39.178 30.035  23.238  1.00 59.77  ?  75  ASP A C     1 
ATOM   508  O O     . ASP A 1 69  ? 39.967 29.457  23.991  1.00 61.52  ?  75  ASP A O     1 
ATOM   509  C CB    . ASP A 1 69  ? 40.763 31.786  22.420  1.00 72.17  ?  75  ASP A CB    1 
ATOM   510  C CG    . ASP A 1 69  ? 40.280 33.201  22.094  1.00 79.10  ?  75  ASP A CG    1 
ATOM   511  O OD1   . ASP A 1 69  ? 39.145 33.568  22.491  1.00 77.75  ?  75  ASP A OD1   1 
ATOM   512  O OD2   . ASP A 1 69  ? 41.033 33.950  21.434  1.00 88.71  -1 75  ASP A OD2   1 
ATOM   513  N N     . ASN A 1 70  ? 37.859 30.085  23.469  1.00 56.51  ?  76  ASN A N     1 
ATOM   514  C CA    . ASN A 1 70  ? 37.198 29.313  24.525  1.00 55.47  ?  76  ASN A CA    1 
ATOM   515  C C     . ASN A 1 70  ? 36.916 27.870  24.129  1.00 55.12  ?  76  ASN A C     1 
ATOM   516  O O     . ASN A 1 70  ? 36.305 27.132  24.912  1.00 52.71  ?  76  ASN A O     1 
ATOM   517  C CB    . ASN A 1 70  ? 35.876 29.966  24.931  1.00 54.96  ?  76  ASN A CB    1 
ATOM   518  C CG    . ASN A 1 70  ? 36.073 31.293  25.619  1.00 58.27  ?  76  ASN A CG    1 
ATOM   519  O OD1   . ASN A 1 70  ? 35.418 32.283  25.287  1.00 54.93  ?  76  ASN A OD1   1 
ATOM   520  N ND2   . ASN A 1 70  ? 36.992 31.324  26.579  1.00 57.36  ?  76  ASN A ND2   1 
ATOM   521  N N     . PHE A 1 71  ? 37.322 27.457  22.937  1.00 55.13  ?  77  PHE A N     1 
ATOM   522  C CA    . PHE A 1 71  ? 37.136 26.093  22.482  1.00 52.06  ?  77  PHE A CA    1 
ATOM   523  C C     . PHE A 1 71  ? 38.492 25.444  22.282  1.00 54.21  ?  77  PHE A C     1 
ATOM   524  O O     . PHE A 1 71  ? 39.483 26.109  21.982  1.00 59.14  ?  77  PHE A O     1 
ATOM   525  C CB    . PHE A 1 71  ? 36.344 26.049  21.187  1.00 51.03  ?  77  PHE A CB    1 
ATOM   526  C CG    . PHE A 1 71  ? 36.385 24.725  20.516  1.00 52.12  ?  77  PHE A CG    1 
ATOM   527  C CD1   . PHE A 1 71  ? 35.621 23.669  20.993  1.00 47.78  ?  77  PHE A CD1   1 
ATOM   528  C CD2   . PHE A 1 71  ? 37.214 24.520  19.418  1.00 51.42  ?  77  PHE A CD2   1 
ATOM   529  C CE1   . PHE A 1 71  ? 35.675 22.434  20.385  1.00 47.77  ?  77  PHE A CE1   1 
ATOM   530  C CE2   . PHE A 1 71  ? 37.272 23.288  18.806  1.00 49.24  ?  77  PHE A CE2   1 
ATOM   531  C CZ    . PHE A 1 71  ? 36.497 22.244  19.291  1.00 48.66  ?  77  PHE A CZ    1 
ATOM   532  N N     . ARG A 1 72  ? 38.544 24.139  22.461  1.00 54.12  ?  78  ARG A N     1 
ATOM   533  C CA    . ARG A 1 72  ? 39.800 23.439  22.249  1.00 56.56  ?  78  ARG A CA    1 
ATOM   534  C C     . ARG A 1 72  ? 39.438 22.043  21.784  1.00 57.19  ?  78  ARG A C     1 
ATOM   535  O O     . ARG A 1 72  ? 38.799 21.301  22.532  1.00 55.85  ?  78  ARG A O     1 
ATOM   536  C CB    . ARG A 1 72  ? 40.642 23.402  23.514  1.00 59.78  ?  78  ARG A CB    1 
ATOM   537  C CG    . ARG A 1 72  ? 42.094 23.059  23.273  1.00 65.39  ?  78  ARG A CG    1 
ATOM   538  C CD    . ARG A 1 72  ? 42.462 21.751  23.942  1.00 65.28  ?  78  ARG A CD    1 
ATOM   539  N NE    . ARG A 1 72  ? 43.898 21.487  23.890  1.00 73.86  ?  78  ARG A NE    1 
ATOM   540  C CZ    . ARG A 1 72  ? 44.810 22.090  24.646  1.00 79.28  ?  78  ARG A CZ    1 
ATOM   541  N NH1   . ARG A 1 72  ? 44.483 23.051  25.502  1.00 75.54  ?  78  ARG A NH1   1 
ATOM   542  N NH2   . ARG A 1 72  ? 46.085 21.721  24.542  1.00 77.94  ?  78  ARG A NH2   1 
ATOM   543  N N     . GLN A 1 73  ? 39.817 21.712  20.547  1.00 56.64  ?  79  GLN A N     1 
ATOM   544  C CA    . GLN A 1 73  ? 39.639 20.360  20.039  1.00 52.97  ?  79  GLN A CA    1 
ATOM   545  C C     . GLN A 1 73  ? 40.574 19.415  20.770  1.00 55.48  ?  79  GLN A C     1 
ATOM   546  O O     . GLN A 1 73  ? 41.769 19.698  20.932  1.00 60.41  ?  79  GLN A O     1 
ATOM   547  C CB    . GLN A 1 73  ? 39.909 20.308  18.543  1.00 51.51  ?  79  GLN A CB    1 
ATOM   548  C CG    . GLN A 1 73  ? 39.594 18.973  17.895  1.00 52.00  ?  79  GLN A CG    1 
ATOM   549  C CD    . GLN A 1 73  ? 39.552 19.095  16.383  1.00 58.92  ?  79  GLN A CD    1 
ATOM   550  O OE1   . GLN A 1 73  ? 39.689 20.197  15.850  1.00 56.04  ?  79  GLN A OE1   1 
ATOM   551  N NE2   . GLN A 1 73  ? 39.366 17.968  15.683  1.00 57.73  ?  79  GLN A NE2   1 
ATOM   552  N N     . GLY A 1 74  ? 40.028 18.296  21.211  1.00 51.97  ?  80  GLY A N     1 
ATOM   553  C CA    . GLY A 1 74  ? 40.828 17.304  21.897  1.00 54.22  ?  80  GLY A CA    1 
ATOM   554  C C     . GLY A 1 74  ? 39.928 16.172  22.336  1.00 59.86  ?  80  GLY A C     1 
ATOM   555  O O     . GLY A 1 74  ? 38.711 16.339  22.480  1.00 59.05  ?  80  GLY A O     1 
ATOM   556  N N     . LEU A 1 75  ? 40.547 15.009  22.520  1.00 57.87  ?  81  LEU A N     1 
ATOM   557  C CA    . LEU A 1 75  ? 39.868 13.834  23.040  1.00 58.97  ?  81  LEU A CA    1 
ATOM   558  C C     . LEU A 1 75  ? 40.190 13.717  24.520  1.00 61.57  ?  81  LEU A C     1 
ATOM   559  O O     . LEU A 1 75  ? 41.362 13.722  24.905  1.00 67.37  ?  81  LEU A O     1 
ATOM   560  C CB    . LEU A 1 75  ? 40.310 12.570  22.304  1.00 62.01  ?  81  LEU A CB    1 
ATOM   561  C CG    . LEU A 1 75  ? 39.533 11.325  22.721  1.00 60.12  ?  81  LEU A CG    1 
ATOM   562  C CD1   . LEU A 1 75  ? 38.239 11.292  21.937  1.00 61.88  ?  81  LEU A CD1   1 
ATOM   563  C CD2   . LEU A 1 75  ? 40.340 10.062  22.514  1.00 62.82  ?  81  LEU A CD2   1 
ATOM   564  N N     . VAL A 1 76  ? 39.166 13.622  25.346  1.00 58.37  ?  82  VAL A N     1 
ATOM   565  C CA    . VAL A 1 76  ? 39.382 13.561  26.781  1.00 65.55  ?  82  VAL A CA    1 
ATOM   566  C C     . VAL A 1 76  ? 39.562 12.103  27.168  1.00 67.36  ?  82  VAL A C     1 
ATOM   567  O O     . VAL A 1 76  ? 38.666 11.285  26.944  1.00 67.90  ?  82  VAL A O     1 
ATOM   568  C CB    . VAL A 1 76  ? 38.219 14.201  27.546  1.00 63.03  ?  82  VAL A CB    1 
ATOM   569  C CG1   . VAL A 1 76  ? 38.508 14.179  29.037  1.00 66.02  ?  82  VAL A CG1   1 
ATOM   570  C CG2   . VAL A 1 76  ? 37.997 15.613  27.064  1.00 61.20  ?  82  VAL A CG2   1 
ATOM   571  N N     . VAL A 1 77  ? 40.712 11.780  27.757  1.00 69.36  ?  83  VAL A N     1 
ATOM   572  C CA    . VAL A 1 77  ? 41.004 10.403  28.147  1.00 70.68  ?  83  VAL A CA    1 
ATOM   573  C C     . VAL A 1 77  ? 40.676 10.146  29.616  1.00 70.26  ?  83  VAL A C     1 
ATOM   574  O O     . VAL A 1 77  ? 40.181 9.075   29.962  1.00 75.09  ?  83  VAL A O     1 
ATOM   575  C CB    . VAL A 1 77  ? 42.471 10.055  27.826  1.00 70.61  ?  83  VAL A CB    1 
ATOM   576  C CG1   . VAL A 1 77  ? 42.715 10.113  26.327  1.00 69.24  ?  83  VAL A CG1   1 
ATOM   577  C CG2   . VAL A 1 77  ? 43.409 10.984  28.553  1.00 72.75  ?  83  VAL A CG2   1 
ATOM   578  N N     . GLY A 1 78  ? 40.921 11.093  30.510  1.00 71.94  ?  84  GLY A N     1 
ATOM   579  C CA    . GLY A 1 78  ? 40.616 10.859  31.909  1.00 73.93  ?  84  GLY A CA    1 
ATOM   580  C C     . GLY A 1 78  ? 40.461 12.136  32.704  1.00 73.51  ?  84  GLY A C     1 
ATOM   581  O O     . GLY A 1 78  ? 40.921 13.210  32.305  1.00 71.18  ?  84  GLY A O     1 
ATOM   582  N N     . ILE A 1 79  ? 39.797 12.003  33.848  1.00 73.19  ?  85  ILE A N     1 
ATOM   583  C CA    . ILE A 1 79  ? 39.654 13.086  34.811  1.00 74.30  ?  85  ILE A CA    1 
ATOM   584  C C     . ILE A 1 79  ? 40.561 12.780  35.993  1.00 77.09  ?  85  ILE A C     1 
ATOM   585  O O     . ILE A 1 79  ? 40.541 11.662  36.523  1.00 79.25  ?  85  ILE A O     1 
ATOM   586  C CB    . ILE A 1 79  ? 38.195 13.250  35.273  1.00 73.34  ?  85  ILE A CB    1 
ATOM   587  C CG1   . ILE A 1 79  ? 37.232 13.280  34.087  1.00 73.27  ?  85  ILE A CG1   1 
ATOM   588  C CG2   . ILE A 1 79  ? 38.037 14.523  36.079  1.00 75.44  ?  85  ILE A CG2   1 
ATOM   589  C CD1   . ILE A 1 79  ? 37.489 14.395  33.139  1.00 70.01  ?  85  ILE A CD1   1 
ATOM   590  N N     . ASP A 1 80  ? 41.361 13.763  36.395  1.00 74.32  ?  86  ASP A N     1 
ATOM   591  C CA    . ASP A 1 80  ? 42.156 13.691  37.620  1.00 78.86  ?  86  ASP A CA    1 
ATOM   592  C C     . ASP A 1 80  ? 41.409 14.445  38.710  1.00 79.24  ?  86  ASP A C     1 
ATOM   593  O O     . ASP A 1 80  ? 41.526 15.663  38.823  1.00 78.03  ?  86  ASP A O     1 
ATOM   594  C CB    . ASP A 1 80  ? 43.542 14.273  37.382  1.00 81.32  ?  86  ASP A CB    1 
ATOM   595  C CG    . ASP A 1 80  ? 44.467 14.085  38.549  1.00 93.21  ?  86  ASP A CG    1 
ATOM   596  O OD1   . ASP A 1 80  ? 43.988 13.985  39.707  1.00 96.89  ?  86  ASP A OD1   1 
ATOM   597  O OD2   . ASP A 1 80  ? 45.685 14.065  38.302  1.00 103.10 -1 86  ASP A OD2   1 
ATOM   598  N N     . LEU A 1 81  ? 40.658 13.712  39.525  1.00 82.01  ?  87  LEU A N     1 
ATOM   599  C CA    . LEU A 1 81  ? 39.802 14.353  40.516  1.00 80.21  ?  87  LEU A CA    1 
ATOM   600  C C     . LEU A 1 81  ? 40.614 15.038  41.609  1.00 84.46  ?  87  LEU A C     1 
ATOM   601  O O     . LEU A 1 81  ? 40.247 16.130  42.061  1.00 81.68  ?  87  LEU A O     1 
ATOM   602  C CB    . LEU A 1 81  ? 38.853 13.326  41.126  1.00 80.35  ?  87  LEU A CB    1 
ATOM   603  C CG    . LEU A 1 81  ? 37.651 12.980  40.255  1.00 80.25  ?  87  LEU A CG    1 
ATOM   604  C CD1   . LEU A 1 81  ? 36.755 11.954  40.928  1.00 81.06  ?  87  LEU A CD1   1 
ATOM   605  C CD2   . LEU A 1 81  ? 36.881 14.248  39.954  1.00 79.60  ?  87  LEU A CD2   1 
ATOM   606  N N     . LYS A 1 82  ? 41.717 14.423  42.047  1.00 91.60  ?  88  LYS A N     1 
ATOM   607  C CA    . LYS A 1 82  ? 42.473 14.978  43.170  1.00 96.46  ?  88  LYS A CA    1 
ATOM   608  C C     . LYS A 1 82  ? 43.048 16.350  42.823  1.00 95.41  ?  88  LYS A C     1 
ATOM   609  O O     . LYS A 1 82  ? 42.960 17.295  43.617  1.00 92.34  ?  88  LYS A O     1 
ATOM   610  C CB    . LYS A 1 82  ? 43.583 14.011  43.594  1.00 92.09  ?  88  LYS A CB    1 
ATOM   611  N N     . ASN A 1 83  ? 43.621 16.485  41.630  1.00 90.68  ?  89  ASN A N     1 
ATOM   612  C CA    . ASN A 1 83  ? 44.255 17.729  41.223  1.00 89.81  ?  89  ASN A CA    1 
ATOM   613  C C     . ASN A 1 83  ? 43.368 18.574  40.324  1.00 82.83  ?  89  ASN A C     1 
ATOM   614  O O     . ASN A 1 83  ? 43.866 19.513  39.699  1.00 84.02  ?  89  ASN A O     1 
ATOM   615  C CB    . ASN A 1 83  ? 45.583 17.430  40.535  1.00 93.90  ?  89  ASN A CB    1 
ATOM   616  C CG    . ASN A 1 83  ? 46.463 16.540  41.374  1.00 103.66 ?  89  ASN A CG    1 
ATOM   617  O OD1   . ASN A 1 83  ? 46.298 15.317  41.375  1.00 106.78 ?  89  ASN A OD1   1 
ATOM   618  N ND2   . ASN A 1 83  ? 47.392 17.147  42.119  1.00 108.08 ?  89  ASN A ND2   1 
ATOM   619  N N     . GLN A 1 84  ? 42.073 18.257  40.248  1.00 78.24  ?  90  GLN A N     1 
ATOM   620  C CA    . GLN A 1 84  ? 41.100 19.007  39.455  1.00 78.33  ?  90  GLN A CA    1 
ATOM   621  C C     . GLN A 1 84  ? 41.633 19.336  38.063  1.00 73.27  ?  90  GLN A C     1 
ATOM   622  O O     . GLN A 1 84  ? 41.794 20.503  37.693  1.00 73.78  ?  90  GLN A O     1 
ATOM   623  C CB    . GLN A 1 84  ? 40.692 20.283  40.188  1.00 75.15  ?  90  GLN A CB    1 
ATOM   624  C CG    . GLN A 1 84  ? 40.249 20.038  41.613  1.00 79.19  ?  90  GLN A CG    1 
ATOM   625  C CD    . GLN A 1 84  ? 38.782 19.693  41.731  1.00 73.77  ?  90  GLN A CD    1 
ATOM   626  O OE1   . GLN A 1 84  ? 37.929 20.585  41.770  1.00 72.09  ?  90  GLN A OE1   1 
ATOM   627  N NE2   . GLN A 1 84  ? 38.478 18.395  41.814  1.00 68.27  ?  90  GLN A NE2   1 
ATOM   628  N N     . MET A 1 85  ? 41.933 18.301  37.299  1.00 73.83  ?  91  MET A N     1 
ATOM   629  C CA    . MET A 1 85  ? 42.467 18.445  35.961  1.00 75.30  ?  91  MET A CA    1 
ATOM   630  C C     . MET A 1 85  ? 41.580 17.676  34.995  1.00 72.01  ?  91  MET A C     1 
ATOM   631  O O     . MET A 1 85  ? 40.706 16.907  35.395  1.00 74.17  ?  91  MET A O     1 
ATOM   632  C CB    . MET A 1 85  ? 43.915 17.941  35.882  1.00 78.01  ?  91  MET A CB    1 
ATOM   633  C CG    . MET A 1 85  ? 44.926 18.854  36.528  1.00 77.48  ?  91  MET A CG    1 
ATOM   634  S SD    . MET A 1 85  ? 44.908 20.482  35.752  1.00 86.36  ?  91  MET A SD    1 
ATOM   635  C CE    . MET A 1 85  ? 46.613 20.628  35.217  1.00 82.79  ?  91  MET A CE    1 
ATOM   636  N N     . VAL A 1 86  ? 41.804 17.894  33.706  1.00 72.10  ?  92  VAL A N     1 
ATOM   637  C CA    . VAL A 1 86  ? 41.125 17.141  32.665  1.00 68.70  ?  92  VAL A CA    1 
ATOM   638  C C     . VAL A 1 86  ? 42.190 16.710  31.674  1.00 71.09  ?  92  VAL A C     1 
ATOM   639  O O     . VAL A 1 86  ? 42.869 17.559  31.085  1.00 70.07  ?  92  VAL A O     1 
ATOM   640  C CB    . VAL A 1 86  ? 40.007 17.955  31.992  1.00 64.68  ?  92  VAL A CB    1 
ATOM   641  C CG1   . VAL A 1 86  ? 39.754 17.470  30.582  1.00 66.68  ?  92  VAL A CG1   1 
ATOM   642  C CG2   . VAL A 1 86  ? 38.727 17.836  32.809  1.00 58.67  ?  92  VAL A CG2   1 
ATOM   643  N N     . LEU A 1 87  ? 42.355 15.395  31.517  1.00 72.89  ?  93  LEU A N     1 
ATOM   644  C CA    . LEU A 1 87  ? 43.492 14.817  30.809  1.00 73.51  ?  93  LEU A CA    1 
ATOM   645  C C     . LEU A 1 87  ? 43.137 14.641  29.336  1.00 69.80  ?  93  LEU A C     1 
ATOM   646  O O     . LEU A 1 87  ? 42.146 13.987  29.003  1.00 68.44  ?  93  LEU A O     1 
ATOM   647  C CB    . LEU A 1 87  ? 43.902 13.482  31.441  1.00 75.10  ?  93  LEU A CB    1 
ATOM   648  C CG    . LEU A 1 87  ? 44.694 13.471  32.771  1.00 75.26  ?  93  LEU A CG    1 
ATOM   649  C CD1   . LEU A 1 87  ? 43.927 14.103  33.926  1.00 74.42  ?  93  LEU A CD1   1 
ATOM   650  C CD2   . LEU A 1 87  ? 45.149 12.060  33.156  1.00 76.22  ?  93  LEU A CD2   1 
ATOM   651  N N     . LEU A 1 88  ? 43.933 15.241  28.464  1.00 70.51  ?  94  LEU A N     1 
ATOM   652  C CA    . LEU A 1 88  ? 43.700 15.205  27.032  1.00 71.62  ?  94  LEU A CA    1 
ATOM   653  C C     . LEU A 1 88  ? 44.688 14.252  26.387  1.00 79.47  ?  94  LEU A C     1 
ATOM   654  O O     . LEU A 1 88  ? 45.864 14.217  26.771  1.00 83.47  ?  94  LEU A O     1 
ATOM   655  C CB    . LEU A 1 88  ? 43.852 16.591  26.412  1.00 72.33  ?  94  LEU A CB    1 
ATOM   656  C CG    . LEU A 1 88  ? 42.859 17.647  26.875  1.00 67.75  ?  94  LEU A CG    1 
ATOM   657  C CD1   . LEU A 1 88  ? 43.007 18.915  26.058  1.00 61.45  ?  94  LEU A CD1   1 
ATOM   658  C CD2   . LEU A 1 88  ? 41.454 17.109  26.789  1.00 62.72  ?  94  LEU A CD2   1 
ATOM   659  N N     . GLN A 1 89  ? 44.204 13.480  25.412  1.00 76.31  ?  95  GLN A N     1 
ATOM   660  C CA    . GLN A 1 89  ? 45.082 12.597  24.657  1.00 79.32  ?  95  GLN A CA    1 
ATOM   661  C C     . GLN A 1 89  ? 46.217 13.407  24.044  1.00 81.67  ?  95  GLN A C     1 
ATOM   662  O O     . GLN A 1 89  ? 45.983 14.377  23.315  1.00 76.52  ?  95  GLN A O     1 
ATOM   663  C CB    . GLN A 1 89  ? 44.310 11.859  23.568  1.00 76.13  ?  95  GLN A CB    1 
ATOM   664  C CG    . GLN A 1 89  ? 45.141 10.764  22.916  1.00 81.06  ?  95  GLN A CG    1 
ATOM   665  C CD    . GLN A 1 89  ? 44.574 10.307  21.586  1.00 86.93  ?  95  GLN A CD    1 
ATOM   666  O OE1   . GLN A 1 89  ? 43.372 10.061  21.455  1.00 80.95  ?  95  GLN A OE1   1 
ATOM   667  N NE2   . GLN A 1 89  ? 45.440 10.202  20.583  1.00 90.68  ?  95  GLN A NE2   1 
ATOM   668  N N     . GLY A 1 90  ? 47.446 13.019  24.361  1.00 83.86  ?  96  GLY A N     1 
ATOM   669  C CA    . GLY A 1 90  ? 48.622 13.777  23.994  1.00 85.38  ?  96  GLY A CA    1 
ATOM   670  C C     . GLY A 1 90  ? 49.331 14.417  25.166  1.00 85.28  ?  96  GLY A C     1 
ATOM   671  O O     . GLY A 1 90  ? 50.470 14.873  25.004  1.00 90.06  ?  96  GLY A O     1 
ATOM   672  N N     . GLY A 1 91  ? 48.703 14.475  26.335  1.00 81.36  ?  97  GLY A N     1 
ATOM   673  C CA    . GLY A 1 91  ? 49.395 14.972  27.504  1.00 85.04  ?  97  GLY A CA    1 
ATOM   674  C C     . GLY A 1 91  ? 48.722 16.136  28.195  1.00 84.12  ?  97  GLY A C     1 
ATOM   675  O O     . GLY A 1 91  ? 48.707 16.189  29.428  1.00 84.28  ?  97  GLY A O     1 
ATOM   676  N N     . GLU A 1 92  ? 48.157 17.064  27.419  1.00 83.04  ?  98  GLU A N     1 
ATOM   677  C CA    . GLU A 1 92  ? 47.656 18.315  27.980  1.00 80.95  ?  98  GLU A CA    1 
ATOM   678  C C     . GLU A 1 92  ? 46.601 18.060  29.048  1.00 80.78  ?  98  GLU A C     1 
ATOM   679  O O     . GLU A 1 92  ? 45.799 17.126  28.953  1.00 78.68  ?  98  GLU A O     1 
ATOM   680  C CB    . GLU A 1 92  ? 47.076 19.209  26.882  1.00 75.06  ?  98  GLU A CB    1 
ATOM   681  N N     . ALA A 1 93  ? 46.630 18.892  30.085  1.00 85.60  ?  99  ALA A N     1 
ATOM   682  C CA    . ALA A 1 93  ? 45.631 18.887  31.140  1.00 81.97  ?  99  ALA A CA    1 
ATOM   683  C C     . ALA A 1 93  ? 45.010 20.272  31.251  1.00 78.33  ?  99  ALA A C     1 
ATOM   684  O O     . ALA A 1 93  ? 45.692 21.290  31.103  1.00 78.55  ?  99  ALA A O     1 
ATOM   685  C CB    . ALA A 1 93  ? 46.231 18.468  32.483  1.00 78.92  ?  99  ALA A CB    1 
ATOM   686  N N     . LEU A 1 94  ? 43.711 20.300  31.491  1.00 75.86  ?  100 LEU A N     1 
ATOM   687  C CA    . LEU A 1 94  ? 42.967 21.550  31.604  1.00 72.29  ?  100 LEU A CA    1 
ATOM   688  C C     . LEU A 1 94  ? 42.470 21.701  33.031  1.00 70.13  ?  100 LEU A C     1 
ATOM   689  O O     . LEU A 1 94  ? 41.650 20.883  33.491  1.00 63.21  ?  100 LEU A O     1 
ATOM   690  C CB    . LEU A 1 94  ? 41.806 21.571  30.610  1.00 68.20  ?  100 LEU A CB    1 
ATOM   691  C CG    . LEU A 1 94  ? 42.252 21.641  29.147  1.00 71.75  ?  100 LEU A CG    1 
ATOM   692  C CD1   . LEU A 1 94  ? 41.076 21.453  28.222  1.00 71.30  ?  100 LEU A CD1   1 
ATOM   693  C CD2   . LEU A 1 94  ? 42.946 22.962  28.837  1.00 74.23  ?  100 LEU A CD2   1 
ATOM   694  N N     . PRO A 1 95  ? 42.941 22.697  33.775  1.00 71.78  ?  101 PRO A N     1 
ATOM   695  C CA    . PRO A 1 95  ? 42.489 22.859  35.161  1.00 67.93  ?  101 PRO A CA    1 
ATOM   696  C C     . PRO A 1 95  ? 41.106 23.478  35.229  1.00 64.96  ?  101 PRO A C     1 
ATOM   697  O O     . PRO A 1 95  ? 40.775 24.393  34.477  1.00 65.08  ?  101 PRO A O     1 
ATOM   698  C CB    . PRO A 1 95  ? 43.541 23.794  35.762  1.00 66.86  ?  101 PRO A CB    1 
ATOM   699  C CG    . PRO A 1 95  ? 44.065 24.556  34.588  1.00 69.67  ?  101 PRO A CG    1 
ATOM   700  C CD    . PRO A 1 95  ? 44.042 23.613  33.433  1.00 68.61  ?  101 PRO A CD    1 
ATOM   701  N N     . PHE A 1 96  ? 40.296 22.984  36.152  1.00 64.14  ?  102 PHE A N     1 
ATOM   702  C CA    . PHE A 1 96  ? 38.961 23.525  36.320  1.00 64.13  ?  102 PHE A CA    1 
ATOM   703  C C     . PHE A 1 96  ? 38.667 23.811  37.784  1.00 64.01  ?  102 PHE A C     1 
ATOM   704  O O     . PHE A 1 96  ? 39.124 23.096  38.677  1.00 70.64  ?  102 PHE A O     1 
ATOM   705  C CB    . PHE A 1 96  ? 37.911 22.571  35.786  1.00 61.87  ?  102 PHE A CB    1 
ATOM   706  C CG    . PHE A 1 96  ? 37.931 21.227  36.437  1.00 64.98  ?  102 PHE A CG    1 
ATOM   707  C CD1   . PHE A 1 96  ? 37.188 20.984  37.582  1.00 65.94  ?  102 PHE A CD1   1 
ATOM   708  C CD2   . PHE A 1 96  ? 38.668 20.188  35.888  1.00 66.97  ?  102 PHE A CD2   1 
ATOM   709  C CE1   . PHE A 1 96  ? 37.193 19.732  38.178  1.00 65.95  ?  102 PHE A CE1   1 
ATOM   710  C CE2   . PHE A 1 96  ? 38.681 18.945  36.483  1.00 65.85  ?  102 PHE A CE2   1 
ATOM   711  C CZ    . PHE A 1 96  ? 37.943 18.719  37.634  1.00 64.78  ?  102 PHE A CZ    1 
ATOM   712  N N     . SER A 1 97  ? 37.884 24.862  38.014  1.00 55.72  ?  103 SER A N     1 
ATOM   713  C CA    . SER A 1 97  ? 37.221 25.013  39.297  1.00 55.56  ?  103 SER A CA    1 
ATOM   714  C C     . SER A 1 97  ? 35.920 24.226  39.316  1.00 61.31  ?  103 SER A C     1 
ATOM   715  O O     . SER A 1 97  ? 35.576 23.615  40.335  1.00 59.78  ?  103 SER A O     1 
ATOM   716  C CB    . SER A 1 97  ? 36.964 26.495  39.591  1.00 61.15  ?  103 SER A CB    1 
ATOM   717  O OG    . SER A 1 97  ? 35.694 26.947  39.133  1.00 60.27  ?  103 SER A OG    1 
ATOM   718  N N     . HIS A 1 98  ? 35.202 24.215  38.186  1.00 60.43  ?  104 HIS A N     1 
ATOM   719  C CA    . HIS A 1 98  ? 33.971 23.452  38.007  1.00 61.27  ?  104 HIS A CA    1 
ATOM   720  C C     . HIS A 1 98  ? 34.014 22.661  36.703  1.00 61.46  ?  104 HIS A C     1 
ATOM   721  O O     . HIS A 1 98  ? 34.610 23.099  35.713  1.00 56.22  ?  104 HIS A O     1 
ATOM   722  C CB    . HIS A 1 98  ? 32.752 24.359  37.980  1.00 59.80  ?  104 HIS A CB    1 
ATOM   723  C CG    . HIS A 1 98  ? 32.560 25.137  39.233  1.00 62.83  ?  104 HIS A CG    1 
ATOM   724  N ND1   . HIS A 1 98  ? 33.464 26.085  39.664  1.00 62.00  ?  104 HIS A ND1   1 
ATOM   725  C CD2   . HIS A 1 98  ? 31.567 25.113  40.149  1.00 60.56  ?  104 HIS A CD2   1 
ATOM   726  C CE1   . HIS A 1 98  ? 33.028 26.620  40.787  1.00 59.30  ?  104 HIS A CE1   1 
ATOM   727  N NE2   . HIS A 1 98  ? 31.879 26.050  41.102  1.00 61.09  ?  104 HIS A NE2   1 
ATOM   728  N N     . LEU A 1 99  ? 33.330 21.510  36.700  1.00 59.86  ?  105 LEU A N     1 
ATOM   729  C CA    . LEU A 1 99  ? 33.358 20.571  35.580  1.00 58.23  ?  105 LEU A CA    1 
ATOM   730  C C     . LEU A 1 99  ? 31.940 20.220  35.145  1.00 58.78  ?  105 LEU A C     1 
ATOM   731  O O     . LEU A 1 99  ? 31.126 19.771  35.961  1.00 60.22  ?  105 LEU A O     1 
ATOM   732  C CB    . LEU A 1 99  ? 34.124 19.303  35.949  1.00 55.87  ?  105 LEU A CB    1 
ATOM   733  C CG    . LEU A 1 99  ? 34.183 18.253  34.836  1.00 59.33  ?  105 LEU A CG    1 
ATOM   734  C CD1   . LEU A 1 99  ? 35.134 18.663  33.702  1.00 54.37  ?  105 LEU A CD1   1 
ATOM   735  C CD2   . LEU A 1 99  ? 34.582 16.914  35.413  1.00 58.16  ?  105 LEU A CD2   1 
ATOM   736  N N     . ILE A 1 100 ? 31.655 20.403  33.856  1.00 54.52  ?  106 ILE A N     1 
ATOM   737  C CA    . ILE A 1 100 ? 30.384 20.021  33.255  1.00 51.91  ?  106 ILE A CA    1 
ATOM   738  C C     . ILE A 1 100 ? 30.643 18.851  32.323  1.00 51.30  ?  106 ILE A C     1 
ATOM   739  O O     . ILE A 1 100 ? 31.421 18.966  31.371  1.00 56.20  ?  106 ILE A O     1 
ATOM   740  C CB    . ILE A 1 100 ? 29.743 21.187  32.493  1.00 54.58  ?  106 ILE A CB    1 
ATOM   741  C CG1   . ILE A 1 100 ? 29.435 22.347  33.437  1.00 47.73  ?  106 ILE A CG1   1 
ATOM   742  C CG2   . ILE A 1 100 ? 28.492 20.713  31.757  1.00 51.40  ?  106 ILE A CG2   1 
ATOM   743  C CD1   . ILE A 1 100 ? 28.684 23.478  32.753  1.00 48.35  ?  106 ILE A CD1   1 
ATOM   744  N N     . LEU A 1 101 ? 30.007 17.724  32.589  1.00 54.38  ?  107 LEU A N     1 
ATOM   745  C CA    . LEU A 1 101 ? 30.184 16.531  31.780  1.00 49.93  ?  107 LEU A CA    1 
ATOM   746  C C     . LEU A 1 101 ? 28.959 16.379  30.890  1.00 55.00  ?  107 LEU A C     1 
ATOM   747  O O     . LEU A 1 101 ? 27.825 16.325  31.384  1.00 53.54  ?  107 LEU A O     1 
ATOM   748  C CB    . LEU A 1 101 ? 30.409 15.300  32.651  1.00 51.78  ?  107 LEU A CB    1 
ATOM   749  C CG    . LEU A 1 101 ? 31.797 15.305  33.279  1.00 54.37  ?  107 LEU A CG    1 
ATOM   750  C CD1   . LEU A 1 101 ? 31.992 14.126  34.202  1.00 62.34  ?  107 LEU A CD1   1 
ATOM   751  C CD2   . LEU A 1 101 ? 32.865 15.331  32.214  1.00 54.82  ?  107 LEU A CD2   1 
ATOM   752  N N     . ALA A 1 102 ? 29.194 16.332  29.583  1.00 51.78  ?  108 ALA A N     1 
ATOM   753  C CA    . ALA A 1 102 ? 28.124 16.435  28.598  1.00 49.78  ?  108 ALA A CA    1 
ATOM   754  C C     . ALA A 1 102 ? 28.492 15.586  27.391  1.00 46.94  ?  108 ALA A C     1 
ATOM   755  O O     . ALA A 1 102 ? 28.546 16.064  26.260  1.00 49.13  ?  108 ALA A O     1 
ATOM   756  C CB    . ALA A 1 102 ? 27.895 17.892  28.197  1.00 42.88  ?  108 ALA A CB    1 
ATOM   757  N N     . THR A 1 103 ? 28.765 14.314  27.632  1.00 50.60  ?  109 THR A N     1 
ATOM   758  C CA    . THR A 1 103 ? 29.506 13.493  26.691  1.00 50.22  ?  109 THR A CA    1 
ATOM   759  C C     . THR A 1 103 ? 28.612 12.694  25.759  1.00 47.64  ?  109 THR A C     1 
ATOM   760  O O     . THR A 1 103 ? 29.130 11.943  24.938  1.00 46.93  ?  109 THR A O     1 
ATOM   761  C CB    . THR A 1 103 ? 30.423 12.537  27.443  1.00 50.71  ?  109 THR A CB    1 
ATOM   762  O OG1   . THR A 1 103 ? 29.618 11.726  28.302  1.00 55.38  ?  109 THR A OG1   1 
ATOM   763  C CG2   . THR A 1 103 ? 31.430 13.309  28.262  1.00 51.75  ?  109 THR A CG2   1 
ATOM   764  N N     . GLY A 1 104 ? 27.302 12.811  25.894  1.00 51.21  ?  110 GLY A N     1 
ATOM   765  C CA    . GLY A 1 104 ? 26.349 12.284  24.951  1.00 49.58  ?  110 GLY A CA    1 
ATOM   766  C C     . GLY A 1 104 ? 26.407 10.782  24.746  1.00 53.50  ?  110 GLY A C     1 
ATOM   767  O O     . GLY A 1 104 ? 26.906 10.016  25.573  1.00 54.54  ?  110 GLY A O     1 
ATOM   768  N N     . SER A 1 105 ? 25.872 10.363  23.604  1.00 52.71  ?  111 SER A N     1 
ATOM   769  C CA    . SER A 1 105 ? 25.727 8.950   23.316  1.00 54.54  ?  111 SER A CA    1 
ATOM   770  C C     . SER A 1 105 ? 26.574 8.564   22.115  1.00 58.08  ?  111 SER A C     1 
ATOM   771  O O     . SER A 1 105 ? 26.885 9.383   21.243  1.00 60.50  ?  111 SER A O     1 
ATOM   772  C CB    . SER A 1 105 ? 24.272 8.574   23.036  1.00 57.32  ?  111 SER A CB    1 
ATOM   773  O OG    . SER A 1 105 ? 23.457 8.758   24.180  1.00 58.77  ?  111 SER A OG    1 
ATOM   774  N N     . THR A 1 106 ? 26.915 7.291   22.079  1.00 60.29  ?  112 THR A N     1 
ATOM   775  C CA    . THR A 1 106 ? 27.739 6.702   21.048  1.00 52.16  ?  112 THR A CA    1 
ATOM   776  C C     . THR A 1 106 ? 26.907 5.669   20.300  1.00 56.41  ?  112 THR A C     1 
ATOM   777  O O     . THR A 1 106 ? 26.018 5.037   20.875  1.00 54.46  ?  112 THR A O     1 
ATOM   778  C CB    . THR A 1 106 ? 28.981 6.092   21.698  1.00 55.17  ?  112 THR A CB    1 
ATOM   779  O OG1   . THR A 1 106 ? 30.153 6.554   21.021  1.00 63.35  ?  112 THR A OG1   1 
ATOM   780  C CG2   . THR A 1 106 ? 28.937 4.593   21.702  1.00 55.33  ?  112 THR A CG2   1 
ATOM   781  N N     . GLY A 1 107 ? 27.163 5.533   19.000  1.00 57.16  ?  113 GLY A N     1 
ATOM   782  C CA    . GLY A 1 107 ? 26.381 4.642   18.180  1.00 52.09  ?  113 GLY A CA    1 
ATOM   783  C C     . GLY A 1 107 ? 27.006 4.421   16.822  1.00 53.31  ?  113 GLY A C     1 
ATOM   784  O O     . GLY A 1 107 ? 28.064 4.968   16.506  1.00 55.82  ?  113 GLY A O     1 
ATOM   785  N N     . PRO A 1 108 ? 26.366 3.593   16.001  1.00 52.28  ?  114 PRO A N     1 
ATOM   786  C CA    . PRO A 1 108 ? 26.853 3.378   14.630  1.00 51.58  ?  114 PRO A CA    1 
ATOM   787  C C     . PRO A 1 108 ? 26.547 4.552   13.708  1.00 49.17  ?  114 PRO A C     1 
ATOM   788  O O     . PRO A 1 108 ? 25.518 5.219   13.833  1.00 48.85  ?  114 PRO A O     1 
ATOM   789  C CB    . PRO A 1 108 ? 26.096 2.122   14.172  1.00 48.60  ?  114 PRO A CB    1 
ATOM   790  C CG    . PRO A 1 108 ? 25.331 1.639   15.369  1.00 56.55  ?  114 PRO A CG    1 
ATOM   791  C CD    . PRO A 1 108 ? 25.184 2.779   16.305  1.00 55.04  ?  114 PRO A CD    1 
ATOM   792  N N     . PHE A 1 109 ? 27.462 4.788   12.774  1.00 50.69  ?  115 PHE A N     1 
ATOM   793  C CA    . PHE A 1 109 ? 27.187 5.653   11.630  1.00 50.72  ?  115 PHE A CA    1 
ATOM   794  C C     . PHE A 1 109 ? 26.054 5.060   10.786  1.00 45.84  ?  115 PHE A C     1 
ATOM   795  O O     . PHE A 1 109 ? 25.981 3.841   10.616  1.00 46.69  ?  115 PHE A O     1 
ATOM   796  C CB    . PHE A 1 109 ? 28.458 5.797   10.786  1.00 48.78  ?  115 PHE A CB    1 
ATOM   797  C CG    . PHE A 1 109 ? 28.394 6.876   9.770   1.00 46.03  ?  115 PHE A CG    1 
ATOM   798  C CD1   . PHE A 1 109 ? 28.606 8.191   10.123  1.00 49.23  ?  115 PHE A CD1   1 
ATOM   799  C CD2   . PHE A 1 109 ? 28.122 6.576   8.445   1.00 49.22  ?  115 PHE A CD2   1 
ATOM   800  C CE1   . PHE A 1 109 ? 28.544 9.192   9.156   1.00 49.03  ?  115 PHE A CE1   1 
ATOM   801  C CE2   . PHE A 1 109 ? 28.066 7.571   7.475   1.00 45.98  ?  115 PHE A CE2   1 
ATOM   802  C CZ    . PHE A 1 109 ? 28.278 8.874   7.827   1.00 42.86  ?  115 PHE A CZ    1 
ATOM   803  N N     . PRO A 1 110 ? 25.143 5.877   10.248  1.00 48.04  ?  116 PRO A N     1 
ATOM   804  C CA    . PRO A 1 110 ? 25.035 7.343   10.294  1.00 45.94  ?  116 PRO A CA    1 
ATOM   805  C C     . PRO A 1 110 ? 24.308 7.957   11.467  1.00 47.36  ?  116 PRO A C     1 
ATOM   806  O O     . PRO A 1 110 ? 24.301 9.176   11.541  1.00 50.02  ?  116 PRO A O     1 
ATOM   807  C CB    . PRO A 1 110 ? 24.231 7.656   9.032   1.00 47.58  ?  116 PRO A CB    1 
ATOM   808  C CG    . PRO A 1 110 ? 23.291 6.494   8.911   1.00 45.85  ?  116 PRO A CG    1 
ATOM   809  C CD    . PRO A 1 110 ? 24.131 5.295   9.339   1.00 46.43  ?  116 PRO A CD    1 
ATOM   810  N N     . GLY A 1 111 ? 23.677 7.192   12.361  1.00 47.86  ?  117 GLY A N     1 
ATOM   811  C CA    . GLY A 1 111 ? 22.915 7.805   13.445  1.00 45.83  ?  117 GLY A CA    1 
ATOM   812  C C     . GLY A 1 111 ? 23.751 8.700   14.349  1.00 51.31  ?  117 GLY A C     1 
ATOM   813  O O     . GLY A 1 111 ? 23.290 9.764   14.781  1.00 44.91  ?  117 GLY A O     1 
ATOM   814  N N     . LYS A 1 112 ? 24.979 8.274   14.667  1.00 49.16  ?  118 LYS A N     1 
ATOM   815  C CA    . LYS A 1 112 ? 25.930 9.097   15.399  1.00 47.05  ?  118 LYS A CA    1 
ATOM   816  C C     . LYS A 1 112 ? 27.232 9.165   14.616  1.00 50.38  ?  118 LYS A C     1 
ATOM   817  O O     . LYS A 1 112 ? 27.521 8.319   13.766  1.00 52.52  ?  118 LYS A O     1 
ATOM   818  C CB    . LYS A 1 112 ? 26.250 8.565   16.811  1.00 49.37  ?  118 LYS A CB    1 
ATOM   819  C CG    . LYS A 1 112 ? 25.074 8.328   17.743  1.00 48.87  ?  118 LYS A CG    1 
ATOM   820  C CD    . LYS A 1 112 ? 24.363 9.596   18.197  1.00 50.16  ?  118 LYS A CD    1 
ATOM   821  C CE    . LYS A 1 112 ? 23.361 9.251   19.324  1.00 54.10  ?  118 LYS A CE    1 
ATOM   822  N NZ    . LYS A 1 112 ? 22.325 10.307  19.592  1.00 51.66  ?  118 LYS A NZ    1 
ATOM   823  N N     . PHE A 1 113 ? 28.036 10.169  14.960  1.00 52.17  ?  119 PHE A N     1 
ATOM   824  C CA    . PHE A 1 113 ? 29.321 10.409  14.318  1.00 47.43  ?  119 PHE A CA    1 
ATOM   825  C C     . PHE A 1 113 ? 30.249 10.987  15.390  1.00 51.03  ?  119 PHE A C     1 
ATOM   826  O O     . PHE A 1 113 ? 30.163 12.174  15.715  1.00 50.13  ?  119 PHE A O     1 
ATOM   827  C CB    . PHE A 1 113 ? 29.139 11.355  13.145  1.00 43.73  ?  119 PHE A CB    1 
ATOM   828  C CG    . PHE A 1 113 ? 30.418 11.796  12.513  1.00 45.27  ?  119 PHE A CG    1 
ATOM   829  C CD1   . PHE A 1 113 ? 31.083 12.931  12.969  1.00 49.90  ?  119 PHE A CD1   1 
ATOM   830  C CD2   . PHE A 1 113 ? 30.936 11.107  11.433  1.00 48.91  ?  119 PHE A CD2   1 
ATOM   831  C CE1   . PHE A 1 113 ? 32.267 13.343  12.379  1.00 51.50  ?  119 PHE A CE1   1 
ATOM   832  C CE2   . PHE A 1 113 ? 32.115 11.509  10.838  1.00 50.76  ?  119 PHE A CE2   1 
ATOM   833  C CZ    . PHE A 1 113 ? 32.780 12.625  11.302  1.00 51.95  ?  119 PHE A CZ    1 
ATOM   834  N N     . ASN A 1 114 ? 31.113 10.150  15.950  1.00 52.28  ?  120 ASN A N     1 
ATOM   835  C CA    . ASN A 1 114 ? 32.073 10.581  16.969  1.00 59.36  ?  120 ASN A CA    1 
ATOM   836  C C     . ASN A 1 114 ? 33.473 10.244  16.470  1.00 60.40  ?  120 ASN A C     1 
ATOM   837  O O     . ASN A 1 114 ? 34.132 9.324   16.950  1.00 62.82  ?  120 ASN A O     1 
ATOM   838  C CB    . ASN A 1 114 ? 31.776 9.924   18.347  1.00 61.81  ?  120 ASN A CB    1 
ATOM   839  C CG    . ASN A 1 114 ? 30.303 10.027  18.744  1.00 59.81  ?  120 ASN A CG    1 
ATOM   840  O OD1   . ASN A 1 114 ? 29.528 9.081   18.544  1.00 61.56  ?  120 ASN A OD1   1 
ATOM   841  N ND2   . ASN A 1 114 ? 29.910 11.180  19.298  1.00 54.98  ?  120 ASN A ND2   1 
ATOM   842  N N     . GLU A 1 115 ? 33.906 10.980  15.463  1.00 58.97  ?  121 GLU A N     1 
ATOM   843  C CA    . GLU A 1 115 ? 35.195 10.783  14.831  1.00 57.77  ?  121 GLU A CA    1 
ATOM   844  C C     . GLU A 1 115 ? 35.964 12.082  14.938  1.00 59.75  ?  121 GLU A C     1 
ATOM   845  O O     . GLU A 1 115 ? 35.412 13.158  14.688  1.00 58.58  ?  121 GLU A O     1 
ATOM   846  C CB    . GLU A 1 115 ? 35.056 10.411  13.359  1.00 57.77  ?  121 GLU A CB    1 
ATOM   847  C CG    . GLU A 1 115 ? 34.721 8.976   13.030  1.00 65.24  ?  121 GLU A CG    1 
ATOM   848  C CD    . GLU A 1 115 ? 34.853 8.717   11.519  1.00 79.44  ?  121 GLU A CD    1 
ATOM   849  O OE1   . GLU A 1 115 ? 35.504 9.550   10.839  1.00 82.38  ?  121 GLU A OE1   1 
ATOM   850  O OE2   . GLU A 1 115 ? 34.318 7.701   11.004  1.00 83.04  -1 121 GLU A OE2   1 
ATOM   851  N N     . VAL A 1 116 ? 37.230 11.992  15.309  1.00 60.63  ?  122 VAL A N     1 
ATOM   852  C CA    . VAL A 1 116 ? 38.101 13.135  15.114  1.00 59.83  ?  122 VAL A CA    1 
ATOM   853  C C     . VAL A 1 116 ? 38.252 13.366  13.615  1.00 61.77  ?  122 VAL A C     1 
ATOM   854  O O     . VAL A 1 116 ? 38.510 12.427  12.847  1.00 60.39  ?  122 VAL A O     1 
ATOM   855  C CB    . VAL A 1 116 ? 39.439 12.893  15.820  1.00 60.56  ?  122 VAL A CB    1 
ATOM   856  C CG1   . VAL A 1 116 ? 40.359 14.099  15.670  1.00 60.30  ?  122 VAL A CG1   1 
ATOM   857  C CG2   . VAL A 1 116 ? 39.173 12.581  17.299  1.00 61.34  ?  122 VAL A CG2   1 
ATOM   858  N N     . SER A 1 117 ? 38.050 14.610  13.181  1.00 59.76  ?  123 SER A N     1 
ATOM   859  C CA    . SER A 1 117 ? 37.915 14.914  11.759  1.00 59.90  ?  123 SER A CA    1 
ATOM   860  C C     . SER A 1 117 ? 37.813 16.425  11.591  1.00 59.13  ?  123 SER A C     1 
ATOM   861  O O     . SER A 1 117 ? 37.541 17.161  12.548  1.00 58.95  ?  123 SER A O     1 
ATOM   862  C CB    . SER A 1 117 ? 36.667 14.270  11.168  1.00 58.74  ?  123 SER A CB    1 
ATOM   863  O OG    . SER A 1 117 ? 35.527 14.732  11.889  1.00 60.41  ?  123 SER A OG    1 
ATOM   864  N N     . SER A 1 118 ? 37.981 16.874  10.350  1.00 52.46  ?  124 SER A N     1 
ATOM   865  C CA    . SER A 1 118 ? 37.627 18.240  9.990   1.00 50.86  ?  124 SER A CA    1 
ATOM   866  C C     . SER A 1 118 ? 36.133 18.336  9.666   1.00 46.46  ?  124 SER A C     1 
ATOM   867  O O     . SER A 1 118 ? 35.449 17.328  9.472   1.00 44.83  ?  124 SER A O     1 
ATOM   868  C CB    . SER A 1 118 ? 38.462 18.726  8.803   1.00 50.43  ?  124 SER A CB    1 
ATOM   869  O OG    . SER A 1 118 ? 38.289 17.892  7.670   1.00 53.48  ?  124 SER A OG    1 
ATOM   870  N N     . GLN A 1 119 ? 35.632 19.575  9.637   1.00 41.97  ?  125 GLN A N     1 
ATOM   871  C CA    . GLN A 1 119 ? 34.262 19.817  9.198   1.00 43.24  ?  125 GLN A CA    1 
ATOM   872  C C     . GLN A 1 119 ? 34.022 19.270  7.791   1.00 47.52  ?  125 GLN A C     1 
ATOM   873  O O     . GLN A 1 119 ? 33.021 18.588  7.544   1.00 47.63  ?  125 GLN A O     1 
ATOM   874  C CB    . GLN A 1 119 ? 33.955 21.309  9.247   1.00 45.93  ?  125 GLN A CB    1 
ATOM   875  C CG    . GLN A 1 119 ? 32.522 21.661  8.830   1.00 50.22  ?  125 GLN A CG    1 
ATOM   876  C CD    . GLN A 1 119 ? 32.119 23.102  9.184   1.00 51.01  ?  125 GLN A CD    1 
ATOM   877  O OE1   . GLN A 1 119 ? 31.732 23.387  10.317  1.00 48.84  ?  125 GLN A OE1   1 
ATOM   878  N NE2   . GLN A 1 119 ? 32.211 24.008  8.209   1.00 55.64  ?  125 GLN A NE2   1 
ATOM   879  N N     . GLN A 1 120 ? 34.938 19.548  6.855   1.00 43.39  ?  126 GLN A N     1 
ATOM   880  C CA    . GLN A 1 120 ? 34.718 19.100  5.490   1.00 43.90  ?  126 GLN A CA    1 
ATOM   881  C C     . GLN A 1 120 ? 34.808 17.582  5.378   1.00 47.58  ?  126 GLN A C     1 
ATOM   882  O O     . GLN A 1 120 ? 34.092 16.980  4.575   1.00 49.64  ?  126 GLN A O     1 
ATOM   883  C CB    . GLN A 1 120 ? 35.697 19.776  4.528   1.00 44.36  ?  126 GLN A CB    1 
ATOM   884  C CG    . GLN A 1 120 ? 35.350 21.222  4.187   1.00 48.58  ?  126 GLN A CG    1 
ATOM   885  C CD    . GLN A 1 120 ? 33.832 21.510  4.123   1.00 58.16  ?  126 GLN A CD    1 
ATOM   886  O OE1   . GLN A 1 120 ? 33.303 22.324  4.904   1.00 57.12  ?  126 GLN A OE1   1 
ATOM   887  N NE2   . GLN A 1 120 ? 33.136 20.865  3.174   1.00 52.16  ?  126 GLN A NE2   1 
ATOM   888  N N     . ALA A 1 121 ? 35.669 16.936  6.170   1.00 48.51  ?  127 ALA A N     1 
ATOM   889  C CA    . ALA A 1 121 ? 35.707 15.473  6.147   1.00 47.65  ?  127 ALA A CA    1 
ATOM   890  C C     . ALA A 1 121 ? 34.425 14.884  6.720   1.00 47.07  ?  127 ALA A C     1 
ATOM   891  O O     . ALA A 1 121 ? 33.914 13.882  6.209   1.00 49.79  ?  127 ALA A O     1 
ATOM   892  C CB    . ALA A 1 121 ? 36.914 14.948  6.923   1.00 45.07  ?  127 ALA A CB    1 
ATOM   893  N N     . ALA A 1 122 ? 33.899 15.486  7.792   1.00 47.30  ?  128 ALA A N     1 
ATOM   894  C CA    . ALA A 1 122 ? 32.660 15.000  8.390   1.00 47.73  ?  128 ALA A CA    1 
ATOM   895  C C     . ALA A 1 122 ? 31.502 15.114  7.411   1.00 46.16  ?  128 ALA A C     1 
ATOM   896  O O     . ALA A 1 122 ? 30.738 14.164  7.226   1.00 47.19  ?  128 ALA A O     1 
ATOM   897  C CB    . ALA A 1 122 ? 32.355 15.780  9.665   1.00 41.67  ?  128 ALA A CB    1 
ATOM   898  N N     . ILE A 1 123 ? 31.348 16.289  6.799   1.00 44.92  ?  129 ILE A N     1 
ATOM   899  C CA    . ILE A 1 123 ? 30.329 16.498  5.775   1.00 45.73  ?  129 ILE A CA    1 
ATOM   900  C C     . ILE A 1 123 ? 30.453 15.449  4.678   1.00 48.17  ?  129 ILE A C     1 
ATOM   901  O O     . ILE A 1 123 ? 29.469 14.821  4.266   1.00 48.53  ?  129 ILE A O     1 
ATOM   902  C CB    . ILE A 1 123 ? 30.456 17.916  5.194   1.00 44.77  ?  129 ILE A CB    1 
ATOM   903  C CG1   . ILE A 1 123 ? 30.165 18.975  6.266   1.00 45.84  ?  129 ILE A CG1   1 
ATOM   904  C CG2   . ILE A 1 123 ? 29.535 18.079  4.027   1.00 40.64  ?  129 ILE A CG2   1 
ATOM   905  C CD1   . ILE A 1 123 ? 30.304 20.395  5.746   1.00 44.13  ?  129 ILE A CD1   1 
ATOM   906  N N     . GLN A 1 124 ? 31.676 15.240  4.198   1.00 45.90  ?  130 GLN A N     1 
ATOM   907  C CA    . GLN A 1 124 ? 31.898 14.290  3.121   1.00 49.47  ?  130 GLN A CA    1 
ATOM   908  C C     . GLN A 1 124 ? 31.479 12.880  3.515   1.00 53.17  ?  130 GLN A C     1 
ATOM   909  O O     . GLN A 1 124 ? 30.999 12.119  2.658   1.00 52.05  ?  130 GLN A O     1 
ATOM   910  C CB    . GLN A 1 124 ? 33.363 14.314  2.697   1.00 47.15  ?  130 GLN A CB    1 
ATOM   911  C CG    . GLN A 1 124 ? 33.582 13.619  1.363   1.00 56.75  ?  130 GLN A CG    1 
ATOM   912  C CD    . GLN A 1 124 ? 32.700 14.218  0.270   1.00 61.86  ?  130 GLN A CD    1 
ATOM   913  O OE1   . GLN A 1 124 ? 31.973 13.505  -0.406  1.00 64.66  ?  130 GLN A OE1   1 
ATOM   914  N NE2   . GLN A 1 124 ? 32.751 15.535  0.114   1.00 59.18  ?  130 GLN A NE2   1 
ATOM   915  N N     . ALA A 1 125 ? 31.647 12.519  4.793   1.00 42.17  ?  131 ALA A N     1 
ATOM   916  C CA    . ALA A 1 125 ? 31.211 11.209  5.252   1.00 43.80  ?  131 ALA A CA    1 
ATOM   917  C C     . ALA A 1 125 ? 29.722 10.991  4.991   1.00 45.18  ?  131 ALA A C     1 
ATOM   918  O O     . ALA A 1 125 ? 29.308 9.891   4.614   1.00 45.24  ?  131 ALA A O     1 
ATOM   919  C CB    . ALA A 1 125 ? 31.523 11.045  6.743   1.00 43.30  ?  131 ALA A CB    1 
ATOM   920  N N     . TYR A 1 126 ? 28.898 12.026  5.181   1.00 40.38  ?  132 TYR A N     1 
ATOM   921  C CA    . TYR A 1 126 ? 27.469 11.847  4.960   1.00 41.73  ?  132 TYR A CA    1 
ATOM   922  C C     . TYR A 1 126 ? 27.115 11.923  3.482   1.00 50.55  ?  132 TYR A C     1 
ATOM   923  O O     . TYR A 1 126 ? 26.237 11.186  3.016   1.00 50.18  ?  132 TYR A O     1 
ATOM   924  C CB    . TYR A 1 126 ? 26.666 12.867  5.768   1.00 40.02  ?  132 TYR A CB    1 
ATOM   925  C CG    . TYR A 1 126 ? 26.541 12.457  7.220   1.00 39.54  ?  132 TYR A CG    1 
ATOM   926  C CD1   . TYR A 1 126 ? 27.522 12.767  8.131   1.00 39.81  ?  132 TYR A CD1   1 
ATOM   927  C CD2   . TYR A 1 126 ? 25.470 11.705  7.653   1.00 40.66  ?  132 TYR A CD2   1 
ATOM   928  C CE1   . TYR A 1 126 ? 27.415 12.366  9.454   1.00 43.38  ?  132 TYR A CE1   1 
ATOM   929  C CE2   . TYR A 1 126 ? 25.365 11.286  8.955   1.00 41.49  ?  132 TYR A CE2   1 
ATOM   930  C CZ    . TYR A 1 126 ? 26.333 11.621  9.856   1.00 44.11  ?  132 TYR A CZ    1 
ATOM   931  O OH    . TYR A 1 126 ? 26.221 11.215  11.167  1.00 47.04  ?  132 TYR A OH    1 
ATOM   932  N N     . GLU A 1 127 ? 27.779 12.804  2.728   1.00 47.99  ?  133 GLU A N     1 
ATOM   933  C CA    . GLU A 1 127 ? 27.560 12.828  1.291   1.00 51.75  ?  133 GLU A CA    1 
ATOM   934  C C     . GLU A 1 127 ? 27.929 11.492  0.663   1.00 53.47  ?  133 GLU A C     1 
ATOM   935  O O     . GLU A 1 127 ? 27.257 11.033  -0.268  1.00 53.15  ?  133 GLU A O     1 
ATOM   936  C CB    . GLU A 1 127 ? 28.356 13.965  0.655   1.00 55.22  ?  133 GLU A CB    1 
ATOM   937  C CG    . GLU A 1 127 ? 27.857 15.344  1.027   1.00 55.48  ?  133 GLU A CG    1 
ATOM   938  C CD    . GLU A 1 127 ? 26.448 15.636  0.492   1.00 62.18  ?  133 GLU A CD    1 
ATOM   939  O OE1   . GLU A 1 127 ? 25.967 14.926  -0.441  1.00 62.16  ?  133 GLU A OE1   1 
ATOM   940  O OE2   . GLU A 1 127 ? 25.828 16.597  1.008   1.00 57.80  -1 133 GLU A OE2   1 
ATOM   941  N N     . ASP A 1 128 ? 28.995 10.854  1.166   1.00 52.72  ?  134 ASP A N     1 
ATOM   942  C CA    . ASP A 1 128 ? 29.360 9.516   0.710   1.00 50.52  ?  134 ASP A CA    1 
ATOM   943  C C     . ASP A 1 128 ? 28.230 8.528   0.954   1.00 52.09  ?  134 ASP A C     1 
ATOM   944  O O     . ASP A 1 128 ? 27.866 7.750   0.065   1.00 51.88  ?  134 ASP A O     1 
ATOM   945  C CB    . ASP A 1 128 ? 30.625 9.047   1.417   1.00 50.72  ?  134 ASP A CB    1 
ATOM   946  C CG    . ASP A 1 128 ? 31.868 9.768   0.933   1.00 62.20  ?  134 ASP A CG    1 
ATOM   947  O OD1   . ASP A 1 128 ? 31.733 10.663  0.066   1.00 65.44  ?  134 ASP A OD1   1 
ATOM   948  O OD2   . ASP A 1 128 ? 32.982 9.435   1.411   1.00 67.55  -1 134 ASP A OD2   1 
ATOM   949  N N     . MET A 1 129 ? 27.672 8.543   2.169   1.00 50.01  ?  135 MET A N     1 
ATOM   950  C CA    . MET A 1 129 ? 26.531 7.700   2.491   1.00 47.82  ?  135 MET A CA    1 
ATOM   951  C C     . MET A 1 129 ? 25.397 7.887   1.490   1.00 48.54  ?  135 MET A C     1 
ATOM   952  O O     . MET A 1 129 ? 24.807 6.912   1.020   1.00 51.89  ?  135 MET A O     1 
ATOM   953  C CB    . MET A 1 129 ? 26.059 8.010   3.909   1.00 47.55  ?  135 MET A CB    1 
ATOM   954  C CG    . MET A 1 129 ? 24.936 7.118   4.393   1.00 51.55  ?  135 MET A CG    1 
ATOM   955  S SD    . MET A 1 129 ? 25.522 5.516   4.993   1.00 57.75  ?  135 MET A SD    1 
ATOM   956  C CE    . MET A 1 129 ? 24.635 4.405   3.925   1.00 45.99  ?  135 MET A CE    1 
ATOM   957  N N     . VAL A 1 130 ? 25.070 9.138   1.165   1.00 48.59  ?  136 VAL A N     1 
ATOM   958  C CA    . VAL A 1 130 ? 23.990 9.420   0.218   1.00 46.05  ?  136 VAL A CA    1 
ATOM   959  C C     . VAL A 1 130 ? 24.259 8.738   -1.117  1.00 49.02  ?  136 VAL A C     1 
ATOM   960  O O     . VAL A 1 130 ? 23.343 8.213   -1.761  1.00 50.10  ?  136 VAL A O     1 
ATOM   961  C CB    . VAL A 1 130 ? 23.824 10.945  0.046   1.00 49.42  ?  136 VAL A CB    1 
ATOM   962  C CG1   . VAL A 1 130 ? 22.821 11.292  -1.064  1.00 43.68  ?  136 VAL A CG1   1 
ATOM   963  C CG2   . VAL A 1 130 ? 23.444 11.605  1.368   1.00 47.46  ?  136 VAL A CG2   1 
ATOM   964  N N     . ARG A 1 131 ? 25.516 8.741   -1.562  1.00 49.83  ?  137 ARG A N     1 
ATOM   965  C CA    . ARG A 1 131 ? 25.823 8.076   -2.819  1.00 49.91  ?  137 ARG A CA    1 
ATOM   966  C C     . ARG A 1 131 ? 25.690 6.569   -2.681  1.00 49.74  ?  137 ARG A C     1 
ATOM   967  O O     . ARG A 1 131 ? 25.286 5.900   -3.633  1.00 51.45  ?  137 ARG A O     1 
ATOM   968  C CB    . ARG A 1 131 ? 27.217 8.455   -3.305  1.00 49.64  ?  137 ARG A CB    1 
ATOM   969  C CG    . ARG A 1 131 ? 27.335 9.896   -3.712  1.00 58.60  ?  137 ARG A CG    1 
ATOM   970  C CD    . ARG A 1 131 ? 28.760 10.382  -3.508  1.00 68.62  ?  137 ARG A CD    1 
ATOM   971  N NE    . ARG A 1 131 ? 28.818 11.799  -3.154  1.00 75.03  ?  137 ARG A NE    1 
ATOM   972  C CZ    . ARG A 1 131 ? 29.936 12.434  -2.820  1.00 76.43  ?  137 ARG A CZ    1 
ATOM   973  N NH1   . ARG A 1 131 ? 31.094 11.792  -2.748  1.00 82.19  ?  137 ARG A NH1   1 
ATOM   974  N NH2   . ARG A 1 131 ? 29.896 13.744  -2.562  1.00 68.27  ?  137 ARG A NH2   1 
ATOM   975  N N     . GLN A 1 132 ? 26.015 6.015   -1.508  1.00 48.55  ?  138 GLN A N     1 
ATOM   976  C CA    . GLN A 1 132 ? 25.783 4.589   -1.293  1.00 48.07  ?  138 GLN A CA    1 
ATOM   977  C C     . GLN A 1 132 ? 24.303 4.268   -1.435  1.00 49.47  ?  138 GLN A C     1 
ATOM   978  O O     . GLN A 1 132 ? 23.924 3.217   -1.962  1.00 47.60  ?  138 GLN A O     1 
ATOM   979  C CB    . GLN A 1 132 ? 26.284 4.159   0.093   1.00 46.90  ?  138 GLN A CB    1 
ATOM   980  C CG    . GLN A 1 132 ? 27.753 4.449   0.387   1.00 45.94  ?  138 GLN A CG    1 
ATOM   981  C CD    . GLN A 1 132 ? 28.677 3.933   -0.694  1.00 52.73  ?  138 GLN A CD    1 
ATOM   982  O OE1   . GLN A 1 132 ? 28.619 2.769   -1.075  1.00 51.31  ?  138 GLN A OE1   1 
ATOM   983  N NE2   . GLN A 1 132 ? 29.518 4.811   -1.216  1.00 59.45  ?  138 GLN A NE2   1 
ATOM   984  N N     . VAL A 1 133 ? 23.449 5.169   -0.962  1.00 50.41  ?  139 VAL A N     1 
ATOM   985  C CA    . VAL A 1 133 ? 22.021 4.916   -0.998  1.00 46.25  ?  139 VAL A CA    1 
ATOM   986  C C     . VAL A 1 133 ? 21.489 5.127   -2.398  1.00 45.58  ?  139 VAL A C     1 
ATOM   987  O O     . VAL A 1 133 ? 20.700 4.317   -2.897  1.00 49.80  ?  139 VAL A O     1 
ATOM   988  C CB    . VAL A 1 133 ? 21.320 5.801   0.040   1.00 46.55  ?  139 VAL A CB    1 
ATOM   989  C CG1   . VAL A 1 133 ? 19.846 5.926   -0.269  1.00 48.06  ?  139 VAL A CG1   1 
ATOM   990  C CG2   . VAL A 1 133 ? 21.525 5.217   1.381   1.00 42.98  ?  139 VAL A CG2   1 
ATOM   991  N N     . GLN A 1 134 ? 21.947 6.189   -3.069  1.00 47.87  ?  140 GLN A N     1 
ATOM   992  C CA    . GLN A 1 134 ? 21.587 6.402   -4.473  1.00 45.53  ?  140 GLN A CA    1 
ATOM   993  C C     . GLN A 1 134 ? 21.969 5.198   -5.330  1.00 42.48  ?  140 GLN A C     1 
ATOM   994  O O     . GLN A 1 134 ? 21.155 4.706   -6.113  1.00 42.46  ?  140 GLN A O     1 
ATOM   995  C CB    . GLN A 1 134 ? 22.232 7.689   -4.987  1.00 44.87  ?  140 GLN A CB    1 
ATOM   996  C CG    . GLN A 1 134 ? 21.304 8.879   -4.813  1.00 47.18  ?  140 GLN A CG    1 
ATOM   997  C CD    . GLN A 1 134 ? 22.002 10.161  -4.434  1.00 48.82  ?  140 GLN A CD    1 
ATOM   998  O OE1   . GLN A 1 134 ? 23.237 10.268  -4.476  1.00 52.80  ?  140 GLN A OE1   1 
ATOM   999  N NE2   . GLN A 1 134 ? 21.207 11.159  -4.055  1.00 46.95  ?  140 GLN A NE2   1 
ATOM   1000 N N     . ARG A 1 135 ? 23.178 4.665   -5.130  1.00 43.84  ?  141 ARG A N     1 
ATOM   1001 C CA    . ARG A 1 135 ? 23.644 3.512   -5.892  1.00 48.59  ?  141 ARG A CA    1 
ATOM   1002 C C     . ARG A 1 135 ? 22.773 2.283   -5.685  1.00 46.75  ?  141 ARG A C     1 
ATOM   1003 O O     . ARG A 1 135 ? 22.696 1.430   -6.569  1.00 47.64  ?  141 ARG A O     1 
ATOM   1004 C CB    . ARG A 1 135 ? 25.083 3.151   -5.503  1.00 49.43  ?  141 ARG A CB    1 
ATOM   1005 C CG    . ARG A 1 135 ? 26.162 4.142   -5.877  1.00 52.18  ?  141 ARG A CG    1 
ATOM   1006 C CD    . ARG A 1 135 ? 27.491 3.422   -6.065  1.00 55.00  ?  141 ARG A CD    1 
ATOM   1007 N NE    . ARG A 1 135 ? 27.436 2.581   -7.260  1.00 67.88  ?  141 ARG A NE    1 
ATOM   1008 C CZ    . ARG A 1 135 ? 28.400 1.753   -7.642  1.00 66.04  ?  141 ARG A CZ    1 
ATOM   1009 N NH1   . ARG A 1 135 ? 29.530 1.647   -6.953  1.00 65.08  ?  141 ARG A NH1   1 
ATOM   1010 N NH2   . ARG A 1 135 ? 28.222 1.009   -8.733  1.00 62.41  ?  141 ARG A NH2   1 
ATOM   1011 N N     . SER A 1 136 ? 22.158 2.145   -4.520  1.00 47.47  ?  142 SER A N     1 
ATOM   1012 C CA    . SER A 1 136 ? 21.578 0.876   -4.100  1.00 45.28  ?  142 SER A CA    1 
ATOM   1013 C C     . SER A 1 136 ? 20.116 0.783   -4.501  1.00 45.97  ?  142 SER A C     1 
ATOM   1014 O O     . SER A 1 136 ? 19.367 1.754   -4.379  1.00 54.43  ?  142 SER A O     1 
ATOM   1015 C CB    . SER A 1 136 ? 21.705 0.725   -2.586  1.00 44.67  ?  142 SER A CB    1 
ATOM   1016 O OG    . SER A 1 136 ? 23.056 0.844   -2.192  1.00 43.88  ?  142 SER A OG    1 
ATOM   1017 N N     . ARG A 1 137 ? 19.704 -0.390  -4.965  1.00 42.26  ?  143 ARG A N     1 
ATOM   1018 C CA    . ARG A 1 137 ? 18.283 -0.631  -5.187  1.00 47.29  ?  143 ARG A CA    1 
ATOM   1019 C C     . ARG A 1 137 ? 17.618 -1.329  -4.008  1.00 46.31  ?  143 ARG A C     1 
ATOM   1020 O O     . ARG A 1 137 ? 16.450 -1.065  -3.705  1.00 45.49  ?  143 ARG A O     1 
ATOM   1021 C CB    . ARG A 1 137 ? 18.060 -1.471  -6.446  1.00 46.82  ?  143 ARG A CB    1 
ATOM   1022 C CG    . ARG A 1 137 ? 16.625 -2.001  -6.582  1.00 49.90  ?  143 ARG A CG    1 
ATOM   1023 C CD    . ARG A 1 137 ? 15.645 -0.916  -6.987  1.00 55.51  ?  143 ARG A CD    1 
ATOM   1024 N NE    . ARG A 1 137 ? 16.087 -0.272  -8.223  1.00 61.32  ?  143 ARG A NE    1 
ATOM   1025 C CZ    . ARG A 1 137 ? 15.332 0.496   -8.998  1.00 61.30  ?  143 ARG A CZ    1 
ATOM   1026 N NH1   . ARG A 1 137 ? 14.059 0.741   -8.712  1.00 58.30  ?  143 ARG A NH1   1 
ATOM   1027 N NH2   . ARG A 1 137 ? 15.864 1.024   -10.097 1.00 63.10  ?  143 ARG A NH2   1 
ATOM   1028 N N     . PHE A 1 138 ? 18.338 -2.238  -3.363  1.00 45.71  ?  144 PHE A N     1 
ATOM   1029 C CA    . PHE A 1 138 ? 17.872 -2.951  -2.191  1.00 45.05  ?  144 PHE A CA    1 
ATOM   1030 C C     . PHE A 1 138 ? 18.684 -2.504  -0.984  1.00 46.67  ?  144 PHE A C     1 
ATOM   1031 O O     . PHE A 1 138 ? 19.918 -2.468  -1.037  1.00 46.57  ?  144 PHE A O     1 
ATOM   1032 C CB    . PHE A 1 138 ? 17.984 -4.453  -2.414  1.00 43.88  ?  144 PHE A CB    1 
ATOM   1033 C CG    . PHE A 1 138 ? 17.173 -4.944  -3.586  1.00 44.53  ?  144 PHE A CG    1 
ATOM   1034 C CD1   . PHE A 1 138 ? 17.675 -4.868  -4.876  1.00 47.25  ?  144 PHE A CD1   1 
ATOM   1035 C CD2   . PHE A 1 138 ? 15.905 -5.470  -3.396  1.00 45.24  ?  144 PHE A CD2   1 
ATOM   1036 C CE1   . PHE A 1 138 ? 16.932 -5.310  -5.947  1.00 44.70  ?  144 PHE A CE1   1 
ATOM   1037 C CE2   . PHE A 1 138 ? 15.168 -5.914  -4.461  1.00 50.60  ?  144 PHE A CE2   1 
ATOM   1038 C CZ    . PHE A 1 138 ? 15.685 -5.839  -5.740  1.00 42.40  ?  144 PHE A CZ    1 
ATOM   1039 N N     . ILE A 1 139 ? 17.985 -2.134  0.083   1.00 43.78  ?  145 ILE A N     1 
ATOM   1040 C CA    . ILE A 1 139 ? 18.589 -1.640  1.313   1.00 43.13  ?  145 ILE A CA    1 
ATOM   1041 C C     . ILE A 1 139 ? 17.952 -2.360  2.494   1.00 42.90  ?  145 ILE A C     1 
ATOM   1042 O O     . ILE A 1 139 ? 16.727 -2.523  2.547   1.00 42.56  ?  145 ILE A O     1 
ATOM   1043 C CB    . ILE A 1 139 ? 18.412 -0.116  1.444   1.00 42.83  ?  145 ILE A CB    1 
ATOM   1044 C CG1   . ILE A 1 139 ? 18.950 0.551   0.173   1.00 44.37  ?  145 ILE A CG1   1 
ATOM   1045 C CG2   . ILE A 1 139 ? 19.095 0.389   2.684   1.00 40.19  ?  145 ILE A CG2   1 
ATOM   1046 C CD1   . ILE A 1 139 ? 18.922 2.073   0.153   1.00 42.32  ?  145 ILE A CD1   1 
ATOM   1047 N N     . VAL A 1 140 ? 18.779 -2.794  3.437   1.00 44.13  ?  146 VAL A N     1 
ATOM   1048 C CA    . VAL A 1 140 ? 18.310 -3.383  4.683   1.00 43.52  ?  146 VAL A CA    1 
ATOM   1049 C C     . VAL A 1 140 ? 18.680 -2.443  5.821   1.00 43.09  ?  146 VAL A C     1 
ATOM   1050 O O     . VAL A 1 140 ? 19.847 -2.067  5.968   1.00 44.35  ?  146 VAL A O     1 
ATOM   1051 C CB    . VAL A 1 140 ? 18.909 -4.776  4.912   1.00 46.50  ?  146 VAL A CB    1 
ATOM   1052 C CG1   . VAL A 1 140 ? 18.639 -5.226  6.349   1.00 45.40  ?  146 VAL A CG1   1 
ATOM   1053 C CG2   . VAL A 1 140 ? 18.333 -5.753  3.931   1.00 45.69  ?  146 VAL A CG2   1 
ATOM   1054 N N     . VAL A 1 141 ? 17.691 -2.045  6.608   1.00 44.48  ?  147 VAL A N     1 
ATOM   1055 C CA    . VAL A 1 141 ? 17.922 -1.345  7.868   1.00 43.74  ?  147 VAL A CA    1 
ATOM   1056 C C     . VAL A 1 141 ? 17.819 -2.366  8.996   1.00 45.29  ?  147 VAL A C     1 
ATOM   1057 O O     . VAL A 1 141 ? 16.804 -3.063  9.128   1.00 46.41  ?  147 VAL A O     1 
ATOM   1058 C CB    . VAL A 1 141 ? 16.924 -0.196  8.068   1.00 44.49  ?  147 VAL A CB    1 
ATOM   1059 C CG1   . VAL A 1 141 ? 17.139 0.461   9.444   1.00 44.71  ?  147 VAL A CG1   1 
ATOM   1060 C CG2   . VAL A 1 141 ? 17.042 0.829   6.930   1.00 40.80  ?  147 VAL A CG2   1 
ATOM   1061 N N     . VAL A 1 142 ? 18.872 -2.480  9.792   1.00 42.34  ?  148 VAL A N     1 
ATOM   1062 C CA    . VAL A 1 142 ? 18.925 -3.460  10.869  1.00 46.63  ?  148 VAL A CA    1 
ATOM   1063 C C     . VAL A 1 142 ? 18.593 -2.747  12.173  1.00 51.48  ?  148 VAL A C     1 
ATOM   1064 O O     . VAL A 1 142 ? 19.391 -1.949  12.678  1.00 49.59  ?  148 VAL A O     1 
ATOM   1065 C CB    . VAL A 1 142 ? 20.297 -4.133  10.963  1.00 51.00  ?  148 VAL A CB    1 
ATOM   1066 C CG1   . VAL A 1 142 ? 20.318 -5.068  12.152  1.00 43.98  ?  148 VAL A CG1   1 
ATOM   1067 C CG2   . VAL A 1 142 ? 20.627 -4.865  9.685   1.00 49.30  ?  148 VAL A CG2   1 
ATOM   1068 N N     . GLY A 1 143 ? 17.418 -3.034  12.727  1.00 49.37  ?  149 GLY A N     1 
ATOM   1069 C CA    . GLY A 1 143 ? 17.043 -2.440  13.989  1.00 46.61  ?  149 GLY A CA    1 
ATOM   1070 C C     . GLY A 1 143 ? 15.824 -1.558  13.873  1.00 51.45  ?  149 GLY A C     1 
ATOM   1071 O O     . GLY A 1 143 ? 15.835 -0.561  13.149  1.00 51.60  ?  149 GLY A O     1 
ATOM   1072 N N     . GLY A 1 144 ? 14.760 -1.935  14.568  1.00 53.20  ?  150 GLY A N     1 
ATOM   1073 C CA    . GLY A 1 144 ? 13.542 -1.157  14.626  1.00 53.23  ?  150 GLY A CA    1 
ATOM   1074 C C     . GLY A 1 144 ? 13.402 -0.340  15.898  1.00 56.36  ?  150 GLY A C     1 
ATOM   1075 O O     . GLY A 1 144 ? 12.301 -0.210  16.440  1.00 56.32  ?  150 GLY A O     1 
ATOM   1076 N N     . GLY A 1 145 ? 14.510 0.206   16.395  1.00 57.82  ?  151 GLY A N     1 
ATOM   1077 C CA    . GLY A 1 145 ? 14.442 1.260   17.382  1.00 55.59  ?  151 GLY A CA    1 
ATOM   1078 C C     . GLY A 1 145 ? 14.011 2.540   16.700  1.00 57.88  ?  151 GLY A C     1 
ATOM   1079 O O     . GLY A 1 145 ? 13.789 2.591   15.490  1.00 57.92  ?  151 GLY A O     1 
ATOM   1080 N N     . SER A 1 146 ? 13.893 3.606   17.492  1.00 58.10  ?  152 SER A N     1 
ATOM   1081 C CA    . SER A 1 146 ? 13.472 4.883   16.919  1.00 57.62  ?  152 SER A CA    1 
ATOM   1082 C C     . SER A 1 146 ? 14.335 5.283   15.732  1.00 53.20  ?  152 SER A C     1 
ATOM   1083 O O     . SER A 1 146 ? 13.836 5.892   14.780  1.00 51.57  ?  152 SER A O     1 
ATOM   1084 C CB    . SER A 1 146 ? 13.504 5.981   17.984  1.00 60.08  ?  152 SER A CB    1 
ATOM   1085 O OG    . SER A 1 146 ? 12.557 5.698   18.998  1.00 64.40  ?  152 SER A OG    1 
ATOM   1086 N N     . ALA A 1 147 ? 15.618 4.929   15.765  1.00 51.25  ?  153 ALA A N     1 
ATOM   1087 C CA    . ALA A 1 147 ? 16.544 5.326   14.719  1.00 47.48  ?  153 ALA A CA    1 
ATOM   1088 C C     . ALA A 1 147 ? 16.323 4.539   13.427  1.00 51.45  ?  153 ALA A C     1 
ATOM   1089 O O     . ALA A 1 147 ? 16.286 5.119   12.332  1.00 48.48  ?  153 ALA A O     1 
ATOM   1090 C CB    . ALA A 1 147 ? 17.969 5.146   15.222  1.00 46.76  ?  153 ALA A CB    1 
ATOM   1091 N N     . GLY A 1 148 ? 16.176 3.221   13.523  1.00 47.90  ?  154 GLY A N     1 
ATOM   1092 C CA    . GLY A 1 148 ? 15.964 2.439   12.321  1.00 49.66  ?  154 GLY A CA    1 
ATOM   1093 C C     . GLY A 1 148 ? 14.641 2.756   11.655  1.00 52.88  ?  154 GLY A C     1 
ATOM   1094 O O     . GLY A 1 148 ? 14.558 2.875   10.424  1.00 48.56  ?  154 GLY A O     1 
ATOM   1095 N N     . VAL A 1 149 ? 13.589 2.891   12.460  1.00 49.25  ?  155 VAL A N     1 
ATOM   1096 C CA    . VAL A 1 149 ? 12.267 3.231   11.943  1.00 49.42  ?  155 VAL A CA    1 
ATOM   1097 C C     . VAL A 1 149 ? 12.315 4.518   11.120  1.00 49.25  ?  155 VAL A C     1 
ATOM   1098 O O     . VAL A 1 149 ? 11.766 4.592   10.017  1.00 48.42  ?  155 VAL A O     1 
ATOM   1099 C CB    . VAL A 1 149 ? 11.274 3.341   13.108  1.00 53.27  ?  155 VAL A CB    1 
ATOM   1100 C CG1   . VAL A 1 149 ? 10.110 4.125   12.696  1.00 59.03  ?  155 VAL A CG1   1 
ATOM   1101 C CG2   . VAL A 1 149 ? 10.853 1.966   13.546  1.00 53.48  ?  155 VAL A CG2   1 
ATOM   1102 N N     . GLU A 1 150 ? 12.981 5.548   11.637  1.00 46.24  ?  156 GLU A N     1 
ATOM   1103 C CA    . GLU A 1 150 ? 13.063 6.797   10.890  1.00 47.16  ?  156 GLU A CA    1 
ATOM   1104 C C     . GLU A 1 150 ? 13.989 6.688   9.677   1.00 49.66  ?  156 GLU A C     1 
ATOM   1105 O O     . GLU A 1 150 ? 13.751 7.338   8.653   1.00 45.41  ?  156 GLU A O     1 
ATOM   1106 C CB    . GLU A 1 150 ? 13.543 7.915   11.798  1.00 49.45  ?  156 GLU A CB    1 
ATOM   1107 C CG    . GLU A 1 150 ? 12.547 8.323   12.875  1.00 58.34  ?  156 GLU A CG    1 
ATOM   1108 C CD    . GLU A 1 150 ? 13.163 9.318   13.834  1.00 62.99  ?  156 GLU A CD    1 
ATOM   1109 O OE1   . GLU A 1 150 ? 14.348 9.089   14.167  1.00 67.55  ?  156 GLU A OE1   1 
ATOM   1110 O OE2   . GLU A 1 150 ? 12.495 10.316  14.223  1.00 59.96  -1 156 GLU A OE2   1 
ATOM   1111 N N     . MET A 1 151 ? 15.057 5.899   9.793   1.00 47.32  ?  157 MET A N     1 
ATOM   1112 C CA    . MET A 1 151 ? 15.988 5.715   8.695   1.00 44.62  ?  157 MET A CA    1 
ATOM   1113 C C     . MET A 1 151 ? 15.299 5.047   7.510   1.00 48.72  ?  157 MET A C     1 
ATOM   1114 O O     . MET A 1 151 ? 15.453 5.479   6.358   1.00 48.22  ?  157 MET A O     1 
ATOM   1115 C CB    . MET A 1 151 ? 17.176 4.887   9.184   1.00 45.94  ?  157 MET A CB    1 
ATOM   1116 C CG    . MET A 1 151 ? 18.208 4.539   8.137   1.00 41.98  ?  157 MET A CG    1 
ATOM   1117 S SD    . MET A 1 151 ? 19.358 5.899   7.856   1.00 59.31  ?  157 MET A SD    1 
ATOM   1118 C CE    . MET A 1 151 ? 18.514 6.817   6.583   1.00 48.39  ?  157 MET A CE    1 
ATOM   1119 N N     . ALA A 1 152 ? 14.507 4.006   7.783   1.00 44.70  ?  158 ALA A N     1 
ATOM   1120 C CA    . ALA A 1 152 ? 13.775 3.323   6.725   1.00 43.91  ?  158 ALA A CA    1 
ATOM   1121 C C     . ALA A 1 152 ? 12.729 4.229   6.104   1.00 43.81  ?  158 ALA A C     1 
ATOM   1122 O O     . ALA A 1 152 ? 12.527 4.211   4.890   1.00 52.12  ?  158 ALA A O     1 
ATOM   1123 C CB    . ALA A 1 152 ? 13.116 2.058   7.265   1.00 42.99  ?  158 ALA A CB    1 
ATOM   1124 N N     . ALA A 1 153 ? 12.039 5.013   6.918   1.00 47.28  ?  159 ALA A N     1 
ATOM   1125 C CA    . ALA A 1 153 ? 11.040 5.935   6.393   1.00 49.31  ?  159 ALA A CA    1 
ATOM   1126 C C     . ALA A 1 153 ? 11.681 7.056   5.590   1.00 45.46  ?  159 ALA A C     1 
ATOM   1127 O O     . ALA A 1 153 ? 11.092 7.555   4.628   1.00 44.84  ?  159 ALA A O     1 
ATOM   1128 C CB    . ALA A 1 153 ? 10.232 6.524   7.553   1.00 47.48  ?  159 ALA A CB    1 
ATOM   1129 N N     . GLU A 1 154 ? 12.870 7.476   6.002   1.00 44.84  ?  160 GLU A N     1 
ATOM   1130 C CA    . GLU A 1 154 ? 13.584 8.546   5.334   1.00 44.14  ?  160 GLU A CA    1 
ATOM   1131 C C     . GLU A 1 154 ? 14.002 8.114   3.934   1.00 46.20  ?  160 GLU A C     1 
ATOM   1132 O O     . GLU A 1 154 ? 13.819 8.858   2.962   1.00 46.94  ?  160 GLU A O     1 
ATOM   1133 C CB    . GLU A 1 154 ? 14.787 8.919   6.197   1.00 45.33  ?  160 GLU A CB    1 
ATOM   1134 C CG    . GLU A 1 154 ? 15.298 10.331  6.095   1.00 50.94  ?  160 GLU A CG    1 
ATOM   1135 C CD    . GLU A 1 154 ? 14.266 11.400  6.403   1.00 54.29  ?  160 GLU A CD    1 
ATOM   1136 O OE1   . GLU A 1 154 ? 13.960 11.664  7.608   1.00 52.06  ?  160 GLU A OE1   1 
ATOM   1137 O OE2   . GLU A 1 154 ? 13.777 11.990  5.405   1.00 57.70  -1 160 GLU A OE2   1 
ATOM   1138 N N     . ILE A 1 155 ? 14.529 6.893   3.811   1.00 44.56  ?  161 ILE A N     1 
ATOM   1139 C CA    . ILE A 1 155 ? 14.921 6.367   2.510   1.00 43.26  ?  161 ILE A CA    1 
ATOM   1140 C C     . ILE A 1 155 ? 13.709 6.199   1.602   1.00 47.43  ?  161 ILE A C     1 
ATOM   1141 O O     . ILE A 1 155 ? 13.748 6.572   0.421   1.00 47.77  ?  161 ILE A O     1 
ATOM   1142 C CB    . ILE A 1 155 ? 15.678 5.042   2.684   1.00 45.63  ?  161 ILE A CB    1 
ATOM   1143 C CG1   . ILE A 1 155 ? 16.978 5.275   3.431   1.00 44.14  ?  161 ILE A CG1   1 
ATOM   1144 C CG2   . ILE A 1 155 ? 15.963 4.377   1.329   1.00 41.26  ?  161 ILE A CG2   1 
ATOM   1145 C CD1   . ILE A 1 155 ? 17.522 4.006   4.008   1.00 46.13  ?  161 ILE A CD1   1 
ATOM   1146 N N     . LYS A 1 156 ? 12.621 5.617   2.119   1.00 43.81  ?  162 LYS A N     1 
ATOM   1147 C CA    . LYS A 1 156 ? 11.462 5.379   1.261   1.00 45.11  ?  162 LYS A CA    1 
ATOM   1148 C C     . LYS A 1 156 ? 10.780 6.673   0.848   1.00 44.94  ?  162 LYS A C     1 
ATOM   1149 O O     . LYS A 1 156 ? 10.183 6.735   -0.228  1.00 45.70  ?  162 LYS A O     1 
ATOM   1150 C CB    . LYS A 1 156 ? 10.452 4.475   1.953   1.00 43.03  ?  162 LYS A CB    1 
ATOM   1151 C CG    . LYS A 1 156 ? 10.499 3.071   1.475   1.00 47.79  ?  162 LYS A CG    1 
ATOM   1152 C CD    . LYS A 1 156 ? 9.907  2.944   0.093   1.00 45.08  ?  162 LYS A CD    1 
ATOM   1153 C CE    . LYS A 1 156 ? 9.944  1.491   -0.350  1.00 47.55  ?  162 LYS A CE    1 
ATOM   1154 N NZ    . LYS A 1 156 ? 9.108  1.202   -1.550  1.00 51.45  ?  162 LYS A NZ    1 
ATOM   1155 N N     . THR A 1 157 ? 10.815 7.707   1.686   1.00 45.84  ?  163 THR A N     1 
ATOM   1156 C CA    . THR A 1 157 ? 10.136 8.932   1.282   1.00 46.14  ?  163 THR A CA    1 
ATOM   1157 C C     . THR A 1 157 ? 10.895 9.621   0.166   1.00 44.71  ?  163 THR A C     1 
ATOM   1158 O O     . THR A 1 157 ? 10.276 10.158  -0.757  1.00 43.78  ?  163 THR A O     1 
ATOM   1159 C CB    . THR A 1 157 ? 9.961  9.883   2.465   1.00 45.07  ?  163 THR A CB    1 
ATOM   1160 O OG1   . THR A 1 157 ? 9.263  9.203   3.508   1.00 48.77  ?  163 THR A OG1   1 
ATOM   1161 C CG2   . THR A 1 157 ? 9.146  11.103  2.053   1.00 40.86  ?  163 THR A CG2   1 
ATOM   1162 N N     . GLU A 1 158 ? 12.239 9.628   0.249   1.00 44.11  ?  164 GLU A N     1 
ATOM   1163 C CA    . GLU A 1 158 ? 13.082 10.268  -0.757  1.00 42.42  ?  164 GLU A CA    1 
ATOM   1164 C C     . GLU A 1 158 ? 13.233 9.411   -2.010  1.00 46.56  ?  164 GLU A C     1 
ATOM   1165 O O     . GLU A 1 158 ? 13.450 9.949   -3.106  1.00 43.91  ?  164 GLU A O     1 
ATOM   1166 C CB    . GLU A 1 158 ? 14.461 10.576  -0.181  1.00 40.81  ?  164 GLU A CB    1 
ATOM   1167 C CG    . GLU A 1 158 ? 14.427 11.527  1.019   1.00 49.07  ?  164 GLU A CG    1 
ATOM   1168 C CD    . GLU A 1 158 ? 13.821 12.889  0.676   1.00 51.01  ?  164 GLU A CD    1 
ATOM   1169 O OE1   . GLU A 1 158 ? 14.411 13.601  -0.169  1.00 56.19  ?  164 GLU A OE1   1 
ATOM   1170 O OE2   . GLU A 1 158 ? 12.759 13.248  1.249   1.00 49.32  -1 164 GLU A OE2   1 
ATOM   1171 N N     . TYR A 1 159 ? 13.109 8.092   -1.874  1.00 46.54  ?  165 TYR A N     1 
ATOM   1172 C CA    . TYR A 1 159 ? 13.349 7.156   -2.969  1.00 43.49  ?  165 TYR A CA    1 
ATOM   1173 C C     . TYR A 1 159 ? 12.261 6.096   -2.957  1.00 44.68  ?  165 TYR A C     1 
ATOM   1174 O O     . TYR A 1 159 ? 12.507 4.933   -2.619  1.00 45.45  ?  165 TYR A O     1 
ATOM   1175 C CB    . TYR A 1 159 ? 14.736 6.537   -2.836  1.00 41.94  ?  165 TYR A CB    1 
ATOM   1176 C CG    . TYR A 1 159 ? 15.847 7.557   -2.779  1.00 41.52  ?  165 TYR A CG    1 
ATOM   1177 C CD1   . TYR A 1 159 ? 16.323 8.168   -3.935  1.00 44.97  ?  165 TYR A CD1   1 
ATOM   1178 C CD2   . TYR A 1 159 ? 16.431 7.901   -1.585  1.00 42.62  ?  165 TYR A CD2   1 
ATOM   1179 C CE1   . TYR A 1 159 ? 17.345 9.106   -3.883  1.00 45.81  ?  165 TYR A CE1   1 
ATOM   1180 C CE2   . TYR A 1 159 ? 17.463 8.840   -1.521  1.00 44.39  ?  165 TYR A CE2   1 
ATOM   1181 C CZ    . TYR A 1 159 ? 17.911 9.435   -2.663  1.00 47.15  ?  165 TYR A CZ    1 
ATOM   1182 O OH    . TYR A 1 159 ? 18.927 10.349  -2.569  1.00 48.70  ?  165 TYR A OH    1 
ATOM   1183 N N     . PRO A 1 160 ? 11.029 6.472   -3.313  1.00 45.34  ?  166 PRO A N     1 
ATOM   1184 C CA    . PRO A 1 160 ? 9.927  5.488   -3.361  1.00 49.28  ?  166 PRO A CA    1 
ATOM   1185 C C     . PRO A 1 160 ? 10.269 4.220   -4.131  1.00 49.79  ?  166 PRO A C     1 
ATOM   1186 O O     . PRO A 1 160 ? 9.768  3.139   -3.794  1.00 49.12  ?  166 PRO A O     1 
ATOM   1187 C CB    . PRO A 1 160 ? 8.796  6.265   -4.056  1.00 51.22  ?  166 PRO A CB    1 
ATOM   1188 C CG    . PRO A 1 160 ? 9.119  7.715   -3.842  1.00 46.44  ?  166 PRO A CG    1 
ATOM   1189 C CD    . PRO A 1 160 ? 10.602 7.826   -3.707  1.00 43.93  ?  166 PRO A CD    1 
ATOM   1190 N N     . GLU A 1 161 ? 11.131 4.318   -5.141  1.00 48.04  ?  167 GLU A N     1 
ATOM   1191 C CA    . GLU A 1 161 ? 11.460 3.199   -6.019  1.00 48.95  ?  167 GLU A CA    1 
ATOM   1192 C C     . GLU A 1 161 ? 12.510 2.255   -5.446  1.00 47.64  ?  167 GLU A C     1 
ATOM   1193 O O     . GLU A 1 161 ? 12.851 1.259   -6.096  1.00 48.83  ?  167 GLU A O     1 
ATOM   1194 C CB    . GLU A 1 161 ? 11.959 3.731   -7.357  1.00 50.51  ?  167 GLU A CB    1 
ATOM   1195 C CG    . GLU A 1 161 ? 13.371 4.293   -7.270  1.00 54.35  ?  167 GLU A CG    1 
ATOM   1196 C CD    . GLU A 1 161 ? 13.443 5.716   -6.701  1.00 50.67  ?  167 GLU A CD    1 
ATOM   1197 O OE1   . GLU A 1 161 ? 12.422 6.237   -6.189  1.00 48.47  ?  167 GLU A OE1   1 
ATOM   1198 O OE2   . GLU A 1 161 ? 14.541 6.311   -6.789  1.00 52.90  -1 167 GLU A OE2   1 
ATOM   1199 N N     . LYS A 1 162 ? 13.045 2.529   -4.271  1.00 45.22  ?  168 LYS A N     1 
ATOM   1200 C CA    . LYS A 1 162 ? 13.957 1.567   -3.691  1.00 44.04  ?  168 LYS A CA    1 
ATOM   1201 C C     . LYS A 1 162 ? 13.159 0.514   -2.939  1.00 43.35  ?  168 LYS A C     1 
ATOM   1202 O O     . LYS A 1 162 ? 11.963 0.658   -2.704  1.00 46.67  ?  168 LYS A O     1 
ATOM   1203 C CB    . LYS A 1 162 ? 14.982 2.272   -2.808  1.00 40.89  ?  168 LYS A CB    1 
ATOM   1204 C CG    . LYS A 1 162 ? 15.854 3.180   -3.623  1.00 41.65  ?  168 LYS A CG    1 
ATOM   1205 C CD    . LYS A 1 162 ? 17.001 3.803   -2.861  1.00 44.86  ?  168 LYS A CD    1 
ATOM   1206 C CE    . LYS A 1 162 ? 17.785 4.725   -3.806  1.00 47.01  ?  168 LYS A CE    1 
ATOM   1207 N NZ    . LYS A 1 162 ? 18.426 3.959   -4.935  1.00 47.42  ?  168 LYS A NZ    1 
ATOM   1208 N N     . GLU A 1 163 ? 13.819 -0.586  -2.628  1.00 43.52  ?  169 GLU A N     1 
ATOM   1209 C CA    . GLU A 1 163 ? 13.239 -1.679  -1.860  1.00 48.50  ?  169 GLU A CA    1 
ATOM   1210 C C     . GLU A 1 163 ? 13.916 -1.643  -0.503  1.00 46.22  ?  169 GLU A C     1 
ATOM   1211 O O     . GLU A 1 163 ? 15.109 -1.939  -0.403  1.00 45.57  ?  169 GLU A O     1 
ATOM   1212 C CB    . GLU A 1 163 ? 13.456 -3.034  -2.543  1.00 49.87  ?  169 GLU A CB    1 
ATOM   1213 C CG    . GLU A 1 163 ? 12.686 -3.257  -3.842  1.00 57.74  ?  169 GLU A CG    1 
ATOM   1214 C CD    . GLU A 1 163 ? 11.188 -3.507  -3.631  1.00 68.04  ?  169 GLU A CD    1 
ATOM   1215 O OE1   . GLU A 1 163 ? 10.729 -3.500  -2.456  1.00 62.93  ?  169 GLU A OE1   1 
ATOM   1216 O OE2   . GLU A 1 163 ? 10.474 -3.717  -4.651  1.00 73.43  -1 169 GLU A OE2   1 
ATOM   1217 N N     . VAL A 1 164 ? 13.164 -1.284  0.532   1.00 48.98  ?  170 VAL A N     1 
ATOM   1218 C CA    . VAL A 1 164 ? 13.695 -1.113  1.886   1.00 47.32  ?  170 VAL A CA    1 
ATOM   1219 C C     . VAL A 1 164 ? 13.110 -2.193  2.785   1.00 45.12  ?  170 VAL A C     1 
ATOM   1220 O O     . VAL A 1 164 ? 11.886 -2.303  2.924   1.00 47.83  ?  170 VAL A O     1 
ATOM   1221 C CB    . VAL A 1 164 ? 13.379 0.283   2.443   1.00 46.17  ?  170 VAL A CB    1 
ATOM   1222 C CG1   . VAL A 1 164 ? 14.052 0.498   3.805   1.00 44.49  ?  170 VAL A CG1   1 
ATOM   1223 C CG2   . VAL A 1 164 ? 13.808 1.351   1.454   1.00 46.55  ?  170 VAL A CG2   1 
ATOM   1224 N N     . THR A 1 165 ? 13.980 -2.981  3.400   1.00 43.38  ?  171 THR A N     1 
ATOM   1225 C CA    . THR A 1 165 ? 13.572 -3.971  4.388   1.00 49.92  ?  171 THR A CA    1 
ATOM   1226 C C     . THR A 1 165 ? 14.120 -3.577  5.759   1.00 46.65  ?  171 THR A C     1 
ATOM   1227 O O     . THR A 1 165 ? 15.310 -3.271  5.896   1.00 47.94  ?  171 THR A O     1 
ATOM   1228 C CB    . THR A 1 165 ? 14.052 -5.375  3.994   1.00 47.18  ?  171 THR A CB    1 
ATOM   1229 O OG1   . THR A 1 165 ? 13.353 -5.801  2.822   1.00 50.15  ?  171 THR A OG1   1 
ATOM   1230 C CG2   . THR A 1 165 ? 13.766 -6.366  5.112   1.00 47.06  ?  171 THR A CG2   1 
ATOM   1231 N N     . LEU A 1 166 ? 13.257 -3.581  6.767   1.00 47.94  ?  172 LEU A N     1 
ATOM   1232 C CA    . LEU A 1 166 ? 13.643 -3.287  8.144   1.00 48.16  ?  172 LEU A CA    1 
ATOM   1233 C C     . LEU A 1 166 ? 13.539 -4.557  8.971   1.00 47.10  ?  172 LEU A C     1 
ATOM   1234 O O     . LEU A 1 166 ? 12.502 -5.221  8.962   1.00 48.26  ?  172 LEU A O     1 
ATOM   1235 C CB    . LEU A 1 166 ? 12.751 -2.202  8.743   1.00 48.18  ?  172 LEU A CB    1 
ATOM   1236 C CG    . LEU A 1 166 ? 12.917 -1.929  10.236  1.00 45.18  ?  172 LEU A CG    1 
ATOM   1237 C CD1   . LEU A 1 166 ? 14.263 -1.326  10.491  1.00 48.17  ?  172 LEU A CD1   1 
ATOM   1238 C CD2   . LEU A 1 166 ? 11.844 -0.992  10.703  1.00 49.19  ?  172 LEU A CD2   1 
ATOM   1239 N N     . ILE A 1 167 ? 14.605 -4.891  9.685   1.00 47.26  ?  173 ILE A N     1 
ATOM   1240 C CA    . ILE A 1 167 ? 14.675 -6.129  10.446  1.00 53.07  ?  173 ILE A CA    1 
ATOM   1241 C C     . ILE A 1 167 ? 14.852 -5.778  11.911  1.00 51.45  ?  173 ILE A C     1 
ATOM   1242 O O     . ILE A 1 167 ? 15.768 -5.029  12.266  1.00 50.99  ?  173 ILE A O     1 
ATOM   1243 C CB    . ILE A 1 167 ? 15.823 -7.027  9.966   1.00 54.08  ?  173 ILE A CB    1 
ATOM   1244 C CG1   . ILE A 1 167 ? 15.593 -7.437  8.509   1.00 51.49  ?  173 ILE A CG1   1 
ATOM   1245 C CG2   . ILE A 1 167 ? 15.951 -8.223  10.891  1.00 51.40  ?  173 ILE A CG2   1 
ATOM   1246 C CD1   . ILE A 1 167 ? 16.810 -8.037  7.849   1.00 49.17  ?  173 ILE A CD1   1 
ATOM   1247 N N     . HIS A 1 168 ? 13.998 -6.339  12.759  1.00 54.86  ?  174 HIS A N     1 
ATOM   1248 C CA    . HIS A 1 168 ? 13.913 -5.909  14.145  1.00 56.93  ?  174 HIS A CA    1 
ATOM   1249 C C     . HIS A 1 168 ? 13.615 -7.088  15.053  1.00 57.47  ?  174 HIS A C     1 
ATOM   1250 O O     . HIS A 1 168 ? 12.772 -7.927  14.733  1.00 57.87  ?  174 HIS A O     1 
ATOM   1251 C CB    . HIS A 1 168 ? 12.836 -4.854  14.337  1.00 51.43  ?  174 HIS A CB    1 
ATOM   1252 C CG    . HIS A 1 168 ? 12.785 -4.336  15.731  1.00 58.65  ?  174 HIS A CG    1 
ATOM   1253 N ND1   . HIS A 1 168 ? 13.926 -4.099  16.467  1.00 57.94  ?  174 HIS A ND1   1 
ATOM   1254 C CD2   . HIS A 1 168 ? 11.742 -4.048  16.542  1.00 59.02  ?  174 HIS A CD2   1 
ATOM   1255 C CE1   . HIS A 1 168 ? 13.586 -3.663  17.663  1.00 55.22  ?  174 HIS A CE1   1 
ATOM   1256 N NE2   . HIS A 1 168 ? 12.267 -3.634  17.737  1.00 59.50  ?  174 HIS A NE2   1 
ATOM   1257 N N     . SER A 1 169 ? 14.288 -7.119  16.208  1.00 59.25  ?  175 SER A N     1 
ATOM   1258 C CA    . SER A 1 169 ? 14.252 -8.301  17.067  1.00 58.20  ?  175 SER A CA    1 
ATOM   1259 C C     . SER A 1 169 ? 12.930 -8.450  17.822  1.00 60.78  ?  175 SER A C     1 
ATOM   1260 O O     . SER A 1 169 ? 12.526 -9.578  18.107  1.00 63.34  ?  175 SER A O     1 
ATOM   1261 C CB    . SER A 1 169 ? 15.429 -8.281  18.040  1.00 56.89  ?  175 SER A CB    1 
ATOM   1262 O OG    . SER A 1 169 ? 15.417 -7.105  18.827  1.00 61.59  ?  175 SER A OG    1 
ATOM   1263 N N     . GLN A 1 170 ? 12.241 -7.357  18.159  1.00 62.93  ?  176 GLN A N     1 
ATOM   1264 C CA    . GLN A 1 170 ? 10.960 -7.468  18.847  1.00 63.87  ?  176 GLN A CA    1 
ATOM   1265 C C     . GLN A 1 170 ? 9.812  -7.448  17.847  1.00 64.65  ?  176 GLN A C     1 
ATOM   1266 O O     . GLN A 1 170 ? 10.010 -7.463  16.630  1.00 64.01  ?  176 GLN A O     1 
ATOM   1267 C CB    . GLN A 1 170 ? 10.770 -6.352  19.874  1.00 68.71  ?  176 GLN A CB    1 
ATOM   1268 C CG    . GLN A 1 170 ? 11.268 -6.694  21.240  1.00 72.04  ?  176 GLN A CG    1 
ATOM   1269 C CD    . GLN A 1 170 ? 12.763 -6.865  21.244  1.00 75.21  ?  176 GLN A CD    1 
ATOM   1270 O OE1   . GLN A 1 170 ? 13.491 -6.038  20.685  1.00 79.27  ?  176 GLN A OE1   1 
ATOM   1271 N NE2   . GLN A 1 170 ? 13.236 -7.949  21.853  1.00 76.90  ?  176 GLN A NE2   1 
ATOM   1272 N N     . VAL A 1 171 ? 8.588  -7.396  18.374  1.00 67.12  ?  177 VAL A N     1 
ATOM   1273 C CA    . VAL A 1 171 ? 7.382  -7.411  17.562  1.00 67.29  ?  177 VAL A CA    1 
ATOM   1274 C C     . VAL A 1 171 ? 6.768  -6.011  17.439  1.00 67.53  ?  177 VAL A C     1 
ATOM   1275 O O     . VAL A 1 171 ? 6.098  -5.721  16.437  1.00 66.05  ?  177 VAL A O     1 
ATOM   1276 C CB    . VAL A 1 171 ? 6.354  -8.446  18.120  1.00 69.54  ?  177 VAL A CB    1 
ATOM   1277 C CG1   . VAL A 1 171 ? 6.294  -8.400  19.656  1.00 63.03  ?  177 VAL A CG1   1 
ATOM   1278 C CG2   . VAL A 1 171 ? 4.956  -8.286  17.493  1.00 65.92  ?  177 VAL A CG2   1 
ATOM   1279 N N     . ALA A 1 172 ? 7.029  -5.117  18.396  1.00 67.52  ?  178 ALA A N     1 
ATOM   1280 C CA    . ALA A 1 172 ? 6.647  -3.712  18.304  1.00 64.62  ?  178 ALA A CA    1 
ATOM   1281 C C     . ALA A 1 172 ? 7.859  -2.845  17.980  1.00 65.91  ?  178 ALA A C     1 
ATOM   1282 O O     . ALA A 1 172 ? 8.989  -3.147  18.377  1.00 64.44  ?  178 ALA A O     1 
ATOM   1283 C CB    . ALA A 1 172 ? 6.009  -3.225  19.604  1.00 58.07  ?  178 ALA A CB    1 
ATOM   1284 N N     . LEU A 1 173 ? 7.615  -1.744  17.278  1.00 62.22  ?  179 LEU A N     1 
ATOM   1285 C CA    . LEU A 1 173 ? 8.708  -0.892  16.832  1.00 62.15  ?  179 LEU A CA    1 
ATOM   1286 C C     . LEU A 1 173 ? 8.861  0.357   17.712  1.00 63.14  ?  179 LEU A C     1 
ATOM   1287 O O     . LEU A 1 173 ? 7.954  0.734   18.460  1.00 64.54  ?  179 LEU A O     1 
ATOM   1288 C CB    . LEU A 1 173 ? 8.497  -0.502  15.374  1.00 58.60  ?  179 LEU A CB    1 
ATOM   1289 C CG    . LEU A 1 173 ? 8.377  -1.739  14.484  1.00 61.72  ?  179 LEU A CG    1 
ATOM   1290 C CD1   . LEU A 1 173 ? 7.796  -1.372  13.148  1.00 58.36  ?  179 LEU A CD1   1 
ATOM   1291 C CD2   . LEU A 1 173 ? 9.726  -2.427  14.302  1.00 59.76  ?  179 LEU A CD2   1 
ATOM   1292 N N     . ALA A 1 174 ? 10.052 0.977   17.631  1.00 58.32  ?  180 ALA A N     1 
ATOM   1293 C CA    . ALA A 1 174 ? 10.433 2.175   18.388  1.00 61.79  ?  180 ALA A CA    1 
ATOM   1294 C C     . ALA A 1 174 ? 10.464 1.935   19.894  1.00 61.65  ?  180 ALA A C     1 
ATOM   1295 O O     . ALA A 1 174 ? 10.270 0.806   20.354  1.00 62.19  ?  180 ALA A O     1 
ATOM   1296 C CB    . ALA A 1 174 ? 9.503  3.355   18.083  1.00 59.85  ?  180 ALA A CB    1 
ATOM   1297 N N     . ASP A 1 175 ? 10.671 3.003   20.661  1.00 61.94  ?  181 ASP A N     1 
ATOM   1298 C CA    . ASP A 1 175 ? 10.995 2.883   22.082  1.00 66.94  ?  181 ASP A CA    1 
ATOM   1299 C C     . ASP A 1 175 ? 9.855  2.281   22.894  1.00 68.38  ?  181 ASP A C     1 
ATOM   1300 O O     . ASP A 1 175 ? 8.688  2.661   22.752  1.00 67.51  ?  181 ASP A O     1 
ATOM   1301 C CB    . ASP A 1 175 ? 11.364 4.249   22.652  1.00 70.70  ?  181 ASP A CB    1 
ATOM   1302 C CG    . ASP A 1 175 ? 12.751 4.686   22.241  1.00 76.31  ?  181 ASP A CG    1 
ATOM   1303 O OD1   . ASP A 1 175 ? 13.675 3.848   22.342  1.00 79.05  ?  181 ASP A OD1   1 
ATOM   1304 O OD2   . ASP A 1 175 ? 12.913 5.848   21.795  1.00 77.04  -1 181 ASP A OD2   1 
ATOM   1305 N N     . LYS A 1 176 ? 10.216 1.348   23.775  1.00 69.71  ?  182 LYS A N     1 
ATOM   1306 C CA    . LYS A 1 176 ? 9.215  0.646   24.569  1.00 71.74  ?  182 LYS A CA    1 
ATOM   1307 C C     . LYS A 1 176 ? 8.406  1.595   25.450  1.00 71.93  ?  182 LYS A C     1 
ATOM   1308 O O     . LYS A 1 176 ? 7.224  1.335   25.710  1.00 71.67  ?  182 LYS A O     1 
ATOM   1309 C CB    . LYS A 1 176 ? 9.895  -0.433  25.412  1.00 72.07  ?  182 LYS A CB    1 
ATOM   1310 C CG    . LYS A 1 176 ? 11.329 -0.109  25.805  1.00 72.83  ?  182 LYS A CG    1 
ATOM   1311 N N     . GLU A 1 177 ? 9.003  2.704   25.896  1.00 69.57  ?  183 GLU A N     1 
ATOM   1312 C CA    . GLU A 1 177 ? 8.304  3.636   26.774  1.00 70.14  ?  183 GLU A CA    1 
ATOM   1313 C C     . GLU A 1 177 ? 7.293  4.509   26.050  1.00 65.24  ?  183 GLU A C     1 
ATOM   1314 O O     . GLU A 1 177 ? 6.685  5.375   26.684  1.00 70.54  ?  183 GLU A O     1 
ATOM   1315 C CB    . GLU A 1 177 ? 9.293  4.549   27.503  1.00 74.53  ?  183 GLU A CB    1 
ATOM   1316 C CG    . GLU A 1 177 ? 10.459 3.843   28.175  1.00 76.83  ?  183 GLU A CG    1 
ATOM   1317 C CD    . GLU A 1 177 ? 11.591 3.558   27.202  1.00 85.47  ?  183 GLU A CD    1 
ATOM   1318 O OE1   . GLU A 1 177 ? 11.357 3.676   25.970  1.00 77.20  ?  183 GLU A OE1   1 
ATOM   1319 O OE2   . GLU A 1 177 ? 12.706 3.215   27.668  1.00 89.27  -1 183 GLU A OE2   1 
ATOM   1320 N N     . LEU A 1 178 ? 7.102  4.330   24.754  1.00 62.79  ?  184 LEU A N     1 
ATOM   1321 C CA    . LEU A 1 178 ? 6.123  5.141   24.061  1.00 59.49  ?  184 LEU A CA    1 
ATOM   1322 C C     . LEU A 1 178 ? 4.728  4.562   24.261  1.00 61.79  ?  184 LEU A C     1 
ATOM   1323 O O     . LEU A 1 178 ? 4.553  3.378   24.574  1.00 59.70  ?  184 LEU A O     1 
ATOM   1324 C CB    . LEU A 1 178 ? 6.458  5.228   22.573  1.00 62.70  ?  184 LEU A CB    1 
ATOM   1325 C CG    . LEU A 1 178 ? 7.667  6.081   22.144  1.00 66.06  ?  184 LEU A CG    1 
ATOM   1326 C CD1   . LEU A 1 178 ? 7.943  5.905   20.666  1.00 62.31  ?  184 LEU A CD1   1 
ATOM   1327 C CD2   . LEU A 1 178 ? 7.481  7.576   22.448  1.00 61.33  ?  184 LEU A CD2   1 
ATOM   1328 N N     . LEU A 1 179 ? 3.733  5.423   24.091  1.00 56.41  ?  185 LEU A N     1 
ATOM   1329 C CA    . LEU A 1 179 ? 2.349  4.979   24.036  1.00 59.20  ?  185 LEU A CA    1 
ATOM   1330 C C     . LEU A 1 179 ? 2.187  3.846   23.023  1.00 61.11  ?  185 LEU A C     1 
ATOM   1331 O O     . LEU A 1 179 ? 2.624  3.985   21.872  1.00 63.53  ?  185 LEU A O     1 
ATOM   1332 C CB    . LEU A 1 179 ? 1.445  6.143   23.638  1.00 57.40  ?  185 LEU A CB    1 
ATOM   1333 C CG    . LEU A 1 179 ? 1.265  7.228   24.688  1.00 58.55  ?  185 LEU A CG    1 
ATOM   1334 C CD1   . LEU A 1 179 ? 0.620  8.424   24.049  1.00 58.34  ?  185 LEU A CD1   1 
ATOM   1335 C CD2   . LEU A 1 179 ? 0.405  6.676   25.821  1.00 56.73  ?  185 LEU A CD2   1 
ATOM   1336 N N     . PRO A 1 180 ? 1.556  2.732   23.396  1.00 60.65  ?  186 PRO A N     1 
ATOM   1337 C CA    . PRO A 1 180 ? 1.231  1.704   22.388  1.00 60.21  ?  186 PRO A CA    1 
ATOM   1338 C C     . PRO A 1 180 ? 0.521  2.259   21.152  1.00 65.78  ?  186 PRO A C     1 
ATOM   1339 O O     . PRO A 1 180 ? 0.686  1.722   20.044  1.00 65.84  ?  186 PRO A O     1 
ATOM   1340 C CB    . PRO A 1 180 ? 0.338  0.731   23.167  1.00 61.09  ?  186 PRO A CB    1 
ATOM   1341 C CG    . PRO A 1 180 ? 0.763  0.910   24.613  1.00 64.23  ?  186 PRO A CG    1 
ATOM   1342 C CD    . PRO A 1 180 ? 1.131  2.356   24.755  1.00 59.48  ?  186 PRO A CD    1 
ATOM   1343 N N     . SER A 1 181 ? -0.273 3.322   21.310  1.00 66.04  ?  187 SER A N     1 
ATOM   1344 C CA    . SER A 1 181 ? -0.900 3.943   20.148  1.00 62.53  ?  187 SER A CA    1 
ATOM   1345 C C     . SER A 1 181 ? 0.146  4.550   19.237  1.00 64.11  ?  187 SER A C     1 
ATOM   1346 O O     . SER A 1 181 ? -0.000 4.529   18.008  1.00 64.41  ?  187 SER A O     1 
ATOM   1347 C CB    . SER A 1 181 ? -1.904 5.012   20.580  1.00 63.37  ?  187 SER A CB    1 
ATOM   1348 O OG    . SER A 1 181 ? -1.324 5.916   21.503  1.00 63.60  ?  187 SER A OG    1 
ATOM   1349 N N     . VAL A 1 182 ? 1.205  5.103   19.826  1.00 63.92  ?  188 VAL A N     1 
ATOM   1350 C CA    . VAL A 1 182 ? 2.301  5.637   19.031  1.00 61.15  ?  188 VAL A CA    1 
ATOM   1351 C C     . VAL A 1 182 ? 3.020  4.507   18.308  1.00 59.77  ?  188 VAL A C     1 
ATOM   1352 O O     . VAL A 1 182 ? 3.262  4.577   17.100  1.00 56.37  ?  188 VAL A O     1 
ATOM   1353 C CB    . VAL A 1 182 ? 3.254  6.457   19.920  1.00 59.56  ?  188 VAL A CB    1 
ATOM   1354 C CG1   . VAL A 1 182 ? 4.573  6.762   19.205  1.00 57.54  ?  188 VAL A CG1   1 
ATOM   1355 C CG2   . VAL A 1 182 ? 2.580  7.749   20.337  1.00 60.28  ?  188 VAL A CG2   1 
ATOM   1356 N N     . ARG A 1 183 ? 3.346  3.433   19.028  1.00 61.73  ?  189 ARG A N     1 
ATOM   1357 C CA    . ARG A 1 183 ? 4.122  2.363   18.413  1.00 60.04  ?  189 ARG A CA    1 
ATOM   1358 C C     . ARG A 1 183 ? 3.361  1.725   17.253  1.00 60.32  ?  189 ARG A C     1 
ATOM   1359 O O     . ARG A 1 183 ? 3.950  1.415   16.212  1.00 59.56  ?  189 ARG A O     1 
ATOM   1360 C CB    . ARG A 1 183 ? 4.515  1.334   19.474  1.00 60.82  ?  189 ARG A CB    1 
ATOM   1361 C CG    . ARG A 1 183 ? 5.301  1.945   20.636  1.00 62.50  ?  189 ARG A CG    1 
ATOM   1362 C CD    . ARG A 1 183 ? 5.826  0.898   21.598  1.00 64.23  ?  189 ARG A CD    1 
ATOM   1363 N NE    . ARG A 1 183 ? 7.003  0.206   21.085  1.00 63.62  ?  189 ARG A NE    1 
ATOM   1364 C CZ    . ARG A 1 183 ? 7.590  -0.822  21.684  1.00 65.53  ?  189 ARG A CZ    1 
ATOM   1365 N NH1   . ARG A 1 183 ? 7.128  -1.318  22.821  1.00 68.32  ?  189 ARG A NH1   1 
ATOM   1366 N NH2   . ARG A 1 183 ? 8.666  -1.368  21.131  1.00 66.59  ?  189 ARG A NH2   1 
ATOM   1367 N N     . GLN A 1 184 ? 2.043  1.572   17.393  1.00 61.59  ?  190 GLN A N     1 
ATOM   1368 C CA    . GLN A 1 184 ? 1.247  0.973   16.327  1.00 63.12  ?  190 GLN A CA    1 
ATOM   1369 C C     . GLN A 1 184 ? 1.211  1.851   15.076  1.00 63.36  ?  190 GLN A C     1 
ATOM   1370 O O     . GLN A 1 184 ? 1.341  1.344   13.955  1.00 64.34  ?  190 GLN A O     1 
ATOM   1371 C CB    . GLN A 1 184 ? -0.167 0.700   16.828  1.00 59.07  ?  190 GLN A CB    1 
ATOM   1372 C CG    . GLN A 1 184 ? -0.520 -0.766  16.842  1.00 65.18  ?  190 GLN A CG    1 
ATOM   1373 C CD    . GLN A 1 184 ? -0.283 -1.439  15.497  1.00 67.84  ?  190 GLN A CD    1 
ATOM   1374 O OE1   . GLN A 1 184 ? -1.076 -1.293  14.558  1.00 65.55  ?  190 GLN A OE1   1 
ATOM   1375 N NE2   . GLN A 1 184 ? 0.816  -2.185  15.399  1.00 70.45  ?  190 GLN A NE2   1 
ATOM   1376 N N     . GLU A 1 185 ? 1.014  3.163   15.235  1.00 58.30  ?  191 GLU A N     1 
ATOM   1377 C CA    . GLU A 1 185 ? 0.893  4.013   14.057  1.00 61.68  ?  191 GLU A CA    1 
ATOM   1378 C C     . GLU A 1 185 ? 2.210  4.089   13.299  1.00 64.02  ?  191 GLU A C     1 
ATOM   1379 O O     . GLU A 1 185 ? 2.213  4.272   12.078  1.00 61.42  ?  191 GLU A O     1 
ATOM   1380 C CB    . GLU A 1 185 ? 0.419  5.411   14.441  1.00 59.32  ?  191 GLU A CB    1 
ATOM   1381 C CG    . GLU A 1 185 ? -0.106 6.228   13.280  1.00 64.86  ?  191 GLU A CG    1 
ATOM   1382 C CD    . GLU A 1 185 ? -1.253 5.544   12.568  1.00 68.65  ?  191 GLU A CD    1 
ATOM   1383 N N     . VAL A 1 186 ? 3.333  3.938   14.001  1.00 59.77  ?  192 VAL A N     1 
ATOM   1384 C CA    . VAL A 1 186 ? 4.616  3.835   13.325  1.00 56.75  ?  192 VAL A CA    1 
ATOM   1385 C C     . VAL A 1 186 ? 4.638  2.618   12.406  1.00 60.38  ?  192 VAL A C     1 
ATOM   1386 O O     . VAL A 1 186 ? 5.186  2.673   11.296  1.00 62.40  ?  192 VAL A O     1 
ATOM   1387 C CB    . VAL A 1 186 ? 5.754  3.800   14.358  1.00 55.81  ?  192 VAL A CB    1 
ATOM   1388 C CG1   . VAL A 1 186 ? 6.978  3.204   13.750  1.00 56.59  ?  192 VAL A CG1   1 
ATOM   1389 C CG2   . VAL A 1 186 ? 6.057  5.187   14.822  1.00 54.40  ?  192 VAL A CG2   1 
ATOM   1390 N N     . LYS A 1 187 ? 4.026  1.507   12.831  1.00 59.65  ?  193 LYS A N     1 
ATOM   1391 C CA    . LYS A 1 187 ? 3.987  0.338   11.959  1.00 59.94  ?  193 LYS A CA    1 
ATOM   1392 C C     . LYS A 1 187 ? 3.087  0.588   10.753  1.00 59.01  ?  193 LYS A C     1 
ATOM   1393 O O     . LYS A 1 187 ? 3.481  0.318   9.614   1.00 56.91  ?  193 LYS A O     1 
ATOM   1394 C CB    . LYS A 1 187 ? 3.532  -0.898  12.731  1.00 61.83  ?  193 LYS A CB    1 
ATOM   1395 C CG    . LYS A 1 187 ? 3.979  -2.205  12.080  1.00 62.05  ?  193 LYS A CG    1 
ATOM   1396 C CD    . LYS A 1 187 ? 3.003  -3.359  12.294  1.00 61.69  ?  193 LYS A CD    1 
ATOM   1397 C CE    . LYS A 1 187 ? 3.153  -3.985  13.674  1.00 68.15  ?  193 LYS A CE    1 
ATOM   1398 N NZ    . LYS A 1 187 ? 2.466  -5.325  13.748  1.00 74.78  ?  193 LYS A NZ    1 
ATOM   1399 N N     . GLU A 1 188 ? 1.876  1.113   10.988  1.00 63.27  ?  194 GLU A N     1 
ATOM   1400 C CA    . GLU A 1 188 ? 0.964  1.468   9.894   1.00 64.26  ?  194 GLU A CA    1 
ATOM   1401 C C     . GLU A 1 188 ? 1.678  2.270   8.815   1.00 59.05  ?  194 GLU A C     1 
ATOM   1402 O O     . GLU A 1 188 ? 1.611  1.948   7.626   1.00 58.23  ?  194 GLU A O     1 
ATOM   1403 C CB    . GLU A 1 188 ? -0.208 2.305   10.421  1.00 71.80  ?  194 GLU A CB    1 
ATOM   1404 C CG    . GLU A 1 188 ? -1.402 1.616   11.097  1.00 78.20  ?  194 GLU A CG    1 
ATOM   1405 C CD    . GLU A 1 188 ? -2.477 2.650   11.512  1.00 88.80  ?  194 GLU A CD    1 
ATOM   1406 O OE1   . GLU A 1 188 ? -2.888 3.483   10.664  1.00 92.70  ?  194 GLU A OE1   1 
ATOM   1407 O OE2   . GLU A 1 188 ? -2.888 2.659   12.694  1.00 92.80  -1 194 GLU A OE2   1 
ATOM   1408 N N     . ILE A 1 189 ? 2.369  3.327   9.230   1.00 59.21  ?  195 ILE A N     1 
ATOM   1409 C CA    . ILE A 1 189 ? 2.992  4.257   8.301   1.00 57.87  ?  195 ILE A CA    1 
ATOM   1410 C C     . ILE A 1 189 ? 4.112  3.582   7.514   1.00 56.60  ?  195 ILE A C     1 
ATOM   1411 O O     . ILE A 1 189 ? 4.227  3.759   6.295   1.00 56.83  ?  195 ILE A O     1 
ATOM   1412 C CB    . ILE A 1 189 ? 3.496  5.484   9.078   1.00 57.94  ?  195 ILE A CB    1 
ATOM   1413 C CG1   . ILE A 1 189 ? 2.309  6.238   9.674   1.00 58.35  ?  195 ILE A CG1   1 
ATOM   1414 C CG2   . ILE A 1 189 ? 4.344  6.383   8.194   1.00 54.43  ?  195 ILE A CG2   1 
ATOM   1415 C CD1   . ILE A 1 189 ? 2.728  7.328   10.656  1.00 59.95  ?  195 ILE A CD1   1 
ATOM   1416 N N     . LEU A 1 190 ? 4.968  2.818   8.198   1.00 53.58  ?  196 LEU A N     1 
ATOM   1417 C CA    . LEU A 1 190 ? 6.041  2.126   7.498   1.00 49.68  ?  196 LEU A CA    1 
ATOM   1418 C C     . LEU A 1 190 ? 5.482  1.193   6.439   1.00 53.74  ?  196 LEU A C     1 
ATOM   1419 O O     . LEU A 1 190 ? 6.030  1.104   5.331   1.00 53.99  ?  196 LEU A O     1 
ATOM   1420 C CB    . LEU A 1 190 ? 6.911  1.356   8.485   1.00 51.09  ?  196 LEU A CB    1 
ATOM   1421 C CG    . LEU A 1 190 ? 7.915  2.190   9.287   1.00 52.54  ?  196 LEU A CG    1 
ATOM   1422 C CD1   . LEU A 1 190 ? 8.687  1.333   10.273  1.00 52.62  ?  196 LEU A CD1   1 
ATOM   1423 C CD2   . LEU A 1 190 ? 8.890  2.940   8.351   1.00 49.44  ?  196 LEU A CD2   1 
ATOM   1424 N N     . LEU A 1 191 ? 4.368  0.516   6.744   1.00 54.18  ?  197 LEU A N     1 
ATOM   1425 C CA    . LEU A 1 191 ? 3.796  -0.425  5.784   1.00 50.99  ?  197 LEU A CA    1 
ATOM   1426 C C     . LEU A 1 191 ? 3.156  0.300   4.611   1.00 54.66  ?  197 LEU A C     1 
ATOM   1427 O O     . LEU A 1 191 ? 3.330  -0.104  3.454   1.00 52.73  ?  197 LEU A O     1 
ATOM   1428 C CB    . LEU A 1 191 ? 2.798  -1.339  6.476   1.00 51.57  ?  197 LEU A CB    1 
ATOM   1429 C CG    . LEU A 1 191 ? 3.491  -2.315  7.436   1.00 53.21  ?  197 LEU A CG    1 
ATOM   1430 C CD1   . LEU A 1 191 ? 2.513  -2.830  8.468   1.00 47.79  ?  197 LEU A CD1   1 
ATOM   1431 C CD2   . LEU A 1 191 ? 4.159  -3.473  6.682   1.00 44.64  ?  197 LEU A CD2   1 
ATOM   1432 N N     . ARG A 1 192 ? 2.449  1.394   4.878   1.00 53.26  ?  198 ARG A N     1 
ATOM   1433 C CA    . ARG A 1 192 ? 1.888  2.165   3.778   1.00 52.30  ?  198 ARG A CA    1 
ATOM   1434 C C     . ARG A 1 192 ? 2.953  2.807   2.896   1.00 53.35  ?  198 ARG A C     1 
ATOM   1435 O O     . ARG A 1 192 ? 2.689  3.058   1.717   1.00 51.92  ?  198 ARG A O     1 
ATOM   1436 C CB    . ARG A 1 192 ? 0.929  3.212   4.318   1.00 51.49  ?  198 ARG A CB    1 
ATOM   1437 C CG    . ARG A 1 192 ? -0.342 2.576   4.805   1.00 59.28  ?  198 ARG A CG    1 
ATOM   1438 C CD    . ARG A 1 192 ? -0.766 3.138   6.126   1.00 67.49  ?  198 ARG A CD    1 
ATOM   1439 N NE    . ARG A 1 192 ? -1.530 4.366   5.974   1.00 70.96  ?  198 ARG A NE    1 
ATOM   1440 C CZ    . ARG A 1 192 ? -1.953 5.111   6.984   1.00 75.14  ?  198 ARG A CZ    1 
ATOM   1441 N NH1   . ARG A 1 192 ? -1.638 4.821   8.241   1.00 66.26  ?  198 ARG A NH1   1 
ATOM   1442 N NH2   . ARG A 1 192 ? -2.719 6.170   6.729   1.00 78.10  ?  198 ARG A NH2   1 
ATOM   1443 N N     . LYS A 1 193 ? 4.154  3.051   3.413   1.00 54.01  ?  199 LYS A N     1 
ATOM   1444 C CA    . LYS A 1 193 ? 5.236  3.535   2.555   1.00 50.75  ?  199 LYS A CA    1 
ATOM   1445 C C     . LYS A 1 193 ? 5.927  2.421   1.766   1.00 51.51  ?  199 LYS A C     1 
ATOM   1446 O O     . LYS A 1 193 ? 6.865  2.714   1.013   1.00 51.99  ?  199 LYS A O     1 
ATOM   1447 C CB    . LYS A 1 193 ? 6.277  4.302   3.383   1.00 49.28  ?  199 LYS A CB    1 
ATOM   1448 C CG    . LYS A 1 193 ? 5.859  5.704   3.757   1.00 46.55  ?  199 LYS A CG    1 
ATOM   1449 C CD    . LYS A 1 193 ? 6.906  6.413   4.593   1.00 46.07  ?  199 LYS A CD    1 
ATOM   1450 C CE    . LYS A 1 193 ? 6.357  7.737   5.152   1.00 43.52  ?  199 LYS A CE    1 
ATOM   1451 N NZ    . LYS A 1 193 ? 6.489  8.873   4.194   1.00 42.93  ?  199 LYS A NZ    1 
ATOM   1452 N N     . GLY A 1 194 ? 5.490  1.165   1.900   1.00 53.21  ?  200 GLY A N     1 
ATOM   1453 C CA    . GLY A 1 194 ? 6.073  0.063   1.155   1.00 47.71  ?  200 GLY A CA    1 
ATOM   1454 C C     . GLY A 1 194 ? 7.300  -0.566  1.779   1.00 50.61  ?  200 GLY A C     1 
ATOM   1455 O O     . GLY A 1 194 ? 7.974  -1.361  1.113   1.00 52.10  ?  200 GLY A O     1 
ATOM   1456 N N     . VAL A 1 195 ? 7.629  -0.223  3.025   1.00 47.83  ?  201 VAL A N     1 
ATOM   1457 C CA    . VAL A 1 195 ? 8.745  -0.862  3.701   1.00 46.99  ?  201 VAL A CA    1 
ATOM   1458 C C     . VAL A 1 195 ? 8.344  -2.279  4.072   1.00 49.80  ?  201 VAL A C     1 
ATOM   1459 O O     . VAL A 1 195 ? 7.247  -2.522  4.585   1.00 52.24  ?  201 VAL A O     1 
ATOM   1460 C CB    . VAL A 1 195 ? 9.161  -0.066  4.953   1.00 46.55  ?  201 VAL A CB    1 
ATOM   1461 C CG1   . VAL A 1 195 ? 10.410 -0.655  5.586   1.00 45.73  ?  201 VAL A CG1   1 
ATOM   1462 C CG2   . VAL A 1 195 ? 9.370  1.392   4.627   1.00 43.82  ?  201 VAL A CG2   1 
ATOM   1463 N N     . GLN A 1 196 ? 9.234  -3.221  3.824   1.00 52.01  ?  202 GLN A N     1 
ATOM   1464 C CA    . GLN A 1 196 ? 8.995  -4.615  4.170   1.00 52.87  ?  202 GLN A CA    1 
ATOM   1465 C C     . GLN A 1 196 ? 9.575  -4.860  5.553   1.00 54.26  ?  202 GLN A C     1 
ATOM   1466 O O     . GLN A 1 196 ? 10.784 -4.701  5.757   1.00 56.40  ?  202 GLN A O     1 
ATOM   1467 C CB    . GLN A 1 196 ? 9.616  -5.530  3.118   1.00 51.17  ?  202 GLN A CB    1 
ATOM   1468 C CG    . GLN A 1 196 ? 9.246  -5.104  1.709   1.00 56.54  ?  202 GLN A CG    1 
ATOM   1469 C CD    . GLN A 1 196 ? 9.090  -6.278  0.763   1.00 73.05  ?  202 GLN A CD    1 
ATOM   1470 O OE1   . GLN A 1 196 ? 9.307  -7.436  1.148   1.00 75.24  ?  202 GLN A OE1   1 
ATOM   1471 N NE2   . GLN A 1 196 ? 8.700  -5.992  -0.485  1.00 68.62  ?  202 GLN A NE2   1 
ATOM   1472 N N     . LEU A 1 197 ? 8.716  -5.234  6.506   1.00 56.24  ?  203 LEU A N     1 
ATOM   1473 C CA    . LEU A 1 197 ? 9.129  -5.442  7.890   1.00 52.35  ?  203 LEU A CA    1 
ATOM   1474 C C     . LEU A 1 197 ? 9.363  -6.921  8.173   1.00 54.55  ?  203 LEU A C     1 
ATOM   1475 O O     . LEU A 1 197 ? 8.532  -7.772  7.845   1.00 55.77  ?  203 LEU A O     1 
ATOM   1476 C CB    . LEU A 1 197 ? 8.080  -4.902  8.856   1.00 52.06  ?  203 LEU A CB    1 
ATOM   1477 C CG    . LEU A 1 197 ? 7.673  -3.455  8.639   1.00 55.41  ?  203 LEU A CG    1 
ATOM   1478 C CD1   . LEU A 1 197 ? 6.738  -3.015  9.751   1.00 54.34  ?  203 LEU A CD1   1 
ATOM   1479 C CD2   . LEU A 1 197 ? 8.920  -2.580  8.592   1.00 56.15  ?  203 LEU A CD2   1 
ATOM   1480 N N     . LEU A 1 198 ? 10.494 -7.214  8.792   1.00 56.06  ?  204 LEU A N     1 
ATOM   1481 C CA    . LEU A 1 198 ? 10.851 -8.546  9.259   1.00 58.06  ?  204 LEU A CA    1 
ATOM   1482 C C     . LEU A 1 198 ? 10.918 -8.456  10.771  1.00 61.38  ?  204 LEU A C     1 
ATOM   1483 O O     . LEU A 1 198 ? 11.988 -8.219  11.337  1.00 57.77  ?  204 LEU A O     1 
ATOM   1484 C CB    . LEU A 1 198 ? 12.148 -8.982  8.685   1.00 56.52  ?  204 LEU A CB    1 
ATOM   1485 C CG    . LEU A 1 198 ? 11.999 -9.908  7.510   1.00 61.11  ?  204 LEU A CG    1 
ATOM   1486 C CD1   . LEU A 1 198 ? 13.374 -10.349 7.116   1.00 64.86  ?  204 LEU A CD1   1 
ATOM   1487 C CD2   . LEU A 1 198 ? 11.145 -11.076 7.946   1.00 64.81  ?  204 LEU A CD2   1 
ATOM   1488 N N     . LEU A 1 199 ? 9.773  -8.645  11.419  1.00 63.58  ?  205 LEU A N     1 
ATOM   1489 C CA    . LEU A 1 199 ? 9.683  -8.504  12.862  1.00 57.72  ?  205 LEU A CA    1 
ATOM   1490 C C     . LEU A 1 199 ? 10.029 -9.815  13.561  1.00 62.14  ?  205 LEU A C     1 
ATOM   1491 O O     . LEU A 1 199 ? 9.865  -10.904 13.006  1.00 63.32  ?  205 LEU A O     1 
ATOM   1492 C CB    . LEU A 1 199 ? 8.282  -8.053  13.262  1.00 61.80  ?  205 LEU A CB    1 
ATOM   1493 C CG    . LEU A 1 199 ? 7.796  -6.721  12.689  1.00 57.55  ?  205 LEU A CG    1 
ATOM   1494 C CD1   . LEU A 1 199 ? 6.429  -6.369  13.263  1.00 58.24  ?  205 LEU A CD1   1 
ATOM   1495 C CD2   . LEU A 1 199 ? 8.806  -5.632  12.957  1.00 54.56  ?  205 LEU A CD2   1 
ATOM   1496 N N     . SER A 1 200 ? 10.529 -9.690  14.793  1.00 61.64  ?  206 SER A N     1 
ATOM   1497 C CA    . SER A 1 200 ? 10.860 -10.830 15.650  1.00 62.67  ?  206 SER A CA    1 
ATOM   1498 C C     . SER A 1 200 ? 11.971 -11.694 15.052  1.00 64.73  ?  206 SER A C     1 
ATOM   1499 O O     . SER A 1 200 ? 11.956 -12.917 15.179  1.00 64.36  ?  206 SER A O     1 
ATOM   1500 C CB    . SER A 1 200 ? 9.621  -11.675 15.955  1.00 65.55  ?  206 SER A CB    1 
ATOM   1501 O OG    . SER A 1 200 ? 8.574  -10.887 16.511  1.00 69.77  ?  206 SER A OG    1 
ATOM   1502 N N     . GLU A 1 201 ? 12.948 -11.056 14.410  1.00 65.46  ?  207 GLU A N     1 
ATOM   1503 C CA    . GLU A 1 201 ? 14.103 -11.742 13.848  1.00 66.10  ?  207 GLU A CA    1 
ATOM   1504 C C     . GLU A 1 201 ? 15.366 -11.001 14.250  1.00 61.34  ?  207 GLU A C     1 
ATOM   1505 O O     . GLU A 1 201 ? 15.352 -9.787  14.447  1.00 57.14  ?  207 GLU A O     1 
ATOM   1506 C CB    . GLU A 1 201 ? 14.022 -11.835 12.310  1.00 65.53  ?  207 GLU A CB    1 
ATOM   1507 C CG    . GLU A 1 201 ? 12.633 -12.214 11.803  1.00 69.09  ?  207 GLU A CG    1 
ATOM   1508 C CD    . GLU A 1 201 ? 12.631 -13.393 10.830  1.00 75.12  ?  207 GLU A CD    1 
ATOM   1509 O OE1   . GLU A 1 201 ? 13.724 -13.821 10.384  1.00 74.92  ?  207 GLU A OE1   1 
ATOM   1510 O OE2   . GLU A 1 201 ? 11.522 -13.889 10.515  1.00 78.28  -1 207 GLU A OE2   1 
ATOM   1511 N N     . ARG A 1 202 ? 16.465 -11.736 14.348  1.00 64.99  ?  208 ARG A N     1 
ATOM   1512 C CA    . ARG A 1 202 ? 17.752 -11.184 14.748  1.00 66.72  ?  208 ARG A CA    1 
ATOM   1513 C C     . ARG A 1 202 ? 18.787 -11.500 13.675  1.00 62.38  ?  208 ARG A C     1 
ATOM   1514 O O     . ARG A 1 202 ? 18.887 -12.642 13.223  1.00 64.69  ?  208 ARG A O     1 
ATOM   1515 C CB    . ARG A 1 202 ? 18.161 -11.749 16.115  1.00 72.13  ?  208 ARG A CB    1 
ATOM   1516 C CG    . ARG A 1 202 ? 19.489 -11.266 16.635  1.00 76.22  ?  208 ARG A CG    1 
ATOM   1517 C CD    . ARG A 1 202 ? 19.652 -11.587 18.114  1.00 82.60  ?  208 ARG A CD    1 
ATOM   1518 N NE    . ARG A 1 202 ? 18.860 -10.702 18.966  1.00 91.07  ?  208 ARG A NE    1 
ATOM   1519 C CZ    . ARG A 1 202 ? 19.179 -9.443  19.257  1.00 89.40  ?  208 ARG A CZ    1 
ATOM   1520 N NH1   . ARG A 1 202 ? 20.257 -8.864  18.746  1.00 84.47  ?  208 ARG A NH1   1 
ATOM   1521 N NH2   . ARG A 1 202 ? 18.395 -8.746  20.078  1.00 88.85  ?  208 ARG A NH2   1 
ATOM   1522 N N     . VAL A 1 203 ? 19.544 -10.494 13.246  1.00 60.83  ?  209 VAL A N     1 
ATOM   1523 C CA    . VAL A 1 203 ? 20.526 -10.734 12.196  1.00 65.10  ?  209 VAL A CA    1 
ATOM   1524 C C     . VAL A 1 203 ? 21.673 -11.556 12.764  1.00 66.59  ?  209 VAL A C     1 
ATOM   1525 O O     . VAL A 1 203 ? 22.326 -11.152 13.735  1.00 60.13  ?  209 VAL A O     1 
ATOM   1526 C CB    . VAL A 1 203 ? 21.035 -9.426  11.589  1.00 59.55  ?  209 VAL A CB    1 
ATOM   1527 C CG1   . VAL A 1 203 ? 22.314 -9.688  10.825  1.00 61.44  ?  209 VAL A CG1   1 
ATOM   1528 C CG2   . VAL A 1 203 ? 20.002 -8.857  10.653  1.00 58.08  ?  209 VAL A CG2   1 
ATOM   1529 N N     . SER A 1 204 ? 21.953 -12.688 12.120  1.00 65.38  ?  210 SER A N     1 
ATOM   1530 C CA    . SER A 1 204 ? 22.865 -13.702 12.632  1.00 65.78  ?  210 SER A CA    1 
ATOM   1531 C C     . SER A 1 204 ? 24.271 -13.650 12.042  1.00 68.50  ?  210 SER A C     1 
ATOM   1532 O O     . SER A 1 204 ? 25.206 -14.134 12.687  1.00 73.88  ?  210 SER A O     1 
ATOM   1533 C CB    . SER A 1 204 ? 22.279 -15.091 12.379  1.00 61.97  ?  210 SER A CB    1 
ATOM   1534 O OG    . SER A 1 204 ? 22.094 -15.302 10.999  1.00 66.94  ?  210 SER A OG    1 
ATOM   1535 N N     . ASN A 1 205 ? 24.462 -13.099 10.842  1.00 64.60  ?  211 ASN A N     1 
ATOM   1536 C CA    . ASN A 1 205 ? 25.779 -13.062 10.213  1.00 66.98  ?  211 ASN A CA    1 
ATOM   1537 C C     . ASN A 1 205 ? 26.334 -11.642 10.145  1.00 67.18  ?  211 ASN A C     1 
ATOM   1538 O O     . ASN A 1 205 ? 26.963 -11.253 9.160   1.00 69.61  ?  211 ASN A O     1 
ATOM   1539 C CB    . ASN A 1 205 ? 25.751 -13.703 8.821   1.00 66.98  ?  211 ASN A CB    1 
ATOM   1540 C CG    . ASN A 1 205 ? 24.962 -12.897 7.795   1.00 64.21  ?  211 ASN A CG    1 
ATOM   1541 O OD1   . ASN A 1 205 ? 23.959 -12.259 8.107   1.00 62.02  ?  211 ASN A OD1   1 
ATOM   1542 N ND2   . ASN A 1 205 ? 25.418 -12.943 6.553   1.00 66.04  ?  211 ASN A ND2   1 
ATOM   1543 N N     . LEU A 1 206 ? 26.163 -10.882 11.230  1.00 65.61  ?  212 LEU A N     1 
ATOM   1544 C CA    . LEU A 1 206 ? 26.390 -9.440  11.186  1.00 67.89  ?  212 LEU A CA    1 
ATOM   1545 C C     . LEU A 1 206 ? 27.873 -9.087  11.095  1.00 70.35  ?  212 LEU A C     1 
ATOM   1546 O O     . LEU A 1 206 ? 28.253 -8.163  10.364  1.00 70.54  ?  212 LEU A O     1 
ATOM   1547 C CB    . LEU A 1 206 ? 25.757 -8.791  12.410  1.00 62.74  ?  212 LEU A CB    1 
ATOM   1548 C CG    . LEU A 1 206 ? 25.696 -7.274  12.394  1.00 62.93  ?  212 LEU A CG    1 
ATOM   1549 C CD1   . LEU A 1 206 ? 24.957 -6.792  11.174  1.00 63.19  ?  212 LEU A CD1   1 
ATOM   1550 C CD2   . LEU A 1 206 ? 25.000 -6.801  13.650  1.00 68.72  ?  212 LEU A CD2   1 
ATOM   1551 N N     . GLU A 1 207 ? 28.726 -9.800  11.828  1.00 73.28  ?  213 GLU A N     1 
ATOM   1552 C CA    . GLU A 1 207 ? 30.157 -9.520  11.770  1.00 74.63  ?  213 GLU A CA    1 
ATOM   1553 C C     . GLU A 1 207 ? 30.717 -9.663  10.361  1.00 72.26  ?  213 GLU A C     1 
ATOM   1554 O O     . GLU A 1 207 ? 31.794 -9.128  10.080  1.00 76.09  ?  213 GLU A O     1 
ATOM   1555 C CB    . GLU A 1 207 ? 30.918 -10.453 12.715  1.00 81.52  ?  213 GLU A CB    1 
ATOM   1556 C CG    . GLU A 1 207 ? 30.109 -10.946 13.917  1.00 83.19  ?  213 GLU A CG    1 
ATOM   1557 C CD    . GLU A 1 207 ? 30.206 -10.034 15.128  1.00 89.59  ?  213 GLU A CD    1 
ATOM   1558 O OE1   . GLU A 1 207 ? 30.096 -8.796  14.976  1.00 93.91  ?  213 GLU A OE1   1 
ATOM   1559 O OE2   . GLU A 1 207 ? 30.397 -10.563 16.241  1.00 91.56  -1 213 GLU A OE2   1 
ATOM   1560 N N     . GLU A 1 208 ? 30.009 -10.360 9.473   1.00 70.69  ?  214 GLU A N     1 
ATOM   1561 C CA    . GLU A 1 208 ? 30.457 -10.632 8.115   1.00 65.87  ?  214 GLU A CA    1 
ATOM   1562 C C     . GLU A 1 208 ? 29.864 -9.683  7.082   1.00 67.74  ?  214 GLU A C     1 
ATOM   1563 O O     . GLU A 1 208 ? 30.177 -9.813  5.896   1.00 72.00  ?  214 GLU A O     1 
ATOM   1564 C CB    . GLU A 1 208 ? 30.106 -12.074 7.731   1.00 64.38  ?  214 GLU A CB    1 
ATOM   1565 N N     . LEU A 1 209 ? 28.991 -8.739  7.493   1.00 67.58  ?  215 LEU A N     1 
ATOM   1566 C CA    . LEU A 1 209 ? 28.374 -7.897  6.475   1.00 65.23  ?  215 LEU A CA    1 
ATOM   1567 C C     . LEU A 1 209 ? 29.139 -6.592  6.319   1.00 63.15  ?  215 LEU A C     1 
ATOM   1568 O O     . LEU A 1 209 ? 29.660 -6.047  7.297   1.00 61.54  ?  215 LEU A O     1 
ATOM   1569 C CB    . LEU A 1 209 ? 26.930 -7.563  6.835   1.00 60.11  ?  215 LEU A CB    1 
ATOM   1570 C CG    . LEU A 1 209 ? 25.948 -8.700  7.057   1.00 60.42  ?  215 LEU A CG    1 
ATOM   1571 C CD1   . LEU A 1 209 ? 24.678 -8.137  7.627   1.00 60.78  ?  215 LEU A CD1   1 
ATOM   1572 C CD2   . LEU A 1 209 ? 25.681 -9.415  5.769   1.00 61.63  ?  215 LEU A CD2   1 
ATOM   1573 N N     . PRO A 1 210 ? 29.201 -6.093  5.086   1.00 60.82  ?  216 PRO A N     1 
ATOM   1574 C CA    . PRO A 1 210 ? 29.727 -4.746  4.848   1.00 58.14  ?  216 PRO A CA    1 
ATOM   1575 C C     . PRO A 1 210 ? 28.679 -3.714  5.231   1.00 59.78  ?  216 PRO A C     1 
ATOM   1576 O O     . PRO A 1 210 ? 27.533 -3.776  4.777   1.00 56.88  ?  216 PRO A O     1 
ATOM   1577 C CB    . PRO A 1 210 ? 29.997 -4.727  3.338   1.00 59.40  ?  216 PRO A CB    1 
ATOM   1578 C CG    . PRO A 1 210 ? 29.799 -6.120  2.875   1.00 58.38  ?  216 PRO A CG    1 
ATOM   1579 C CD    . PRO A 1 210 ? 28.883 -6.785  3.833   1.00 54.61  ?  216 PRO A CD    1 
ATOM   1580 N N     . LEU A 1 211 ? 29.076 -2.762  6.063   1.00 57.09  ?  217 LEU A N     1 
ATOM   1581 C CA    . LEU A 1 211 ? 28.166 -1.739  6.538   1.00 53.31  ?  217 LEU A CA    1 
ATOM   1582 C C     . LEU A 1 211 ? 28.387 -0.440  5.782   1.00 53.78  ?  217 LEU A C     1 
ATOM   1583 O O     . LEU A 1 211 ? 29.523 -0.071  5.474   1.00 55.70  ?  217 LEU A O     1 
ATOM   1584 C CB    . LEU A 1 211 ? 28.355 -1.515  8.034   1.00 56.65  ?  217 LEU A CB    1 
ATOM   1585 C CG    . LEU A 1 211 ? 28.074 -2.751  8.871   1.00 55.83  ?  217 LEU A CG    1 
ATOM   1586 C CD1   . LEU A 1 211 ? 28.230 -2.396  10.332  1.00 55.12  ?  217 LEU A CD1   1 
ATOM   1587 C CD2   . LEU A 1 211 ? 26.678 -3.278  8.569   1.00 54.34  ?  217 LEU A CD2   1 
ATOM   1588 N N     . ASN A 1 212 ? 27.287 0.231   5.467   1.00 51.92  ?  218 ASN A N     1 
ATOM   1589 C CA    . ASN A 1 212 ? 27.306 1.569   4.882   1.00 52.31  ?  218 ASN A CA    1 
ATOM   1590 C C     . ASN A 1 212 ? 28.054 1.629   3.552   1.00 51.75  ?  218 ASN A C     1 
ATOM   1591 O O     . ASN A 1 212 ? 28.689 2.631   3.222   1.00 52.88  ?  218 ASN A O     1 
ATOM   1592 C CB    . ASN A 1 212 ? 27.899 2.567   5.867   1.00 53.00  ?  218 ASN A CB    1 
ATOM   1593 C CG    . ASN A 1 212 ? 27.181 2.564   7.173   1.00 52.69  ?  218 ASN A CG    1 
ATOM   1594 O OD1   . ASN A 1 212 ? 25.954 2.440   7.221   1.00 53.22  ?  218 ASN A OD1   1 
ATOM   1595 N ND2   . ASN A 1 212 ? 27.936 2.687   8.252   1.00 51.34  ?  218 ASN A ND2   1 
ATOM   1596 N N     . GLU A 1 213 ? 27.962 0.573   2.761   1.00 52.49  ?  219 GLU A N     1 
ATOM   1597 C CA    . GLU A 1 213 ? 28.752 0.513   1.537   1.00 53.36  ?  219 GLU A CA    1 
ATOM   1598 C C     . GLU A 1 213 ? 28.019 -0.332  0.506   1.00 49.03  ?  219 GLU A C     1 
ATOM   1599 O O     . GLU A 1 213 ? 27.683 -1.486  0.778   1.00 54.65  ?  219 GLU A O     1 
ATOM   1600 C CB    . GLU A 1 213 ? 30.145 -0.040  1.864   1.00 56.23  ?  219 GLU A CB    1 
ATOM   1601 C CG    . GLU A 1 213 ? 30.780 -0.995  0.871   1.00 59.14  ?  219 GLU A CG    1 
ATOM   1602 C CD    . GLU A 1 213 ? 31.850 -1.877  1.536   1.00 67.15  ?  219 GLU A CD    1 
ATOM   1603 O OE1   . GLU A 1 213 ? 32.190 -1.629  2.733   1.00 67.75  ?  219 GLU A OE1   1 
ATOM   1604 O OE2   . GLU A 1 213 ? 32.329 -2.832  0.868   1.00 62.31  -1 219 GLU A OE2   1 
ATOM   1605 N N     . TYR A 1 214 ? 27.740 0.254   -0.656  1.00 47.38  ?  220 TYR A N     1 
ATOM   1606 C CA    . TYR A 1 214 ? 27.081 -0.476  -1.735  1.00 48.51  ?  220 TYR A CA    1 
ATOM   1607 C C     . TYR A 1 214 ? 27.903 -1.685  -2.182  1.00 50.77  ?  220 TYR A C     1 
ATOM   1608 O O     . TYR A 1 214 ? 29.121 -1.599  -2.369  1.00 52.27  ?  220 TYR A O     1 
ATOM   1609 C CB    . TYR A 1 214 ? 26.840 0.444   -2.931  1.00 47.68  ?  220 TYR A CB    1 
ATOM   1610 C CG    . TYR A 1 214 ? 26.465 -0.305  -4.195  1.00 48.06  ?  220 TYR A CG    1 
ATOM   1611 C CD1   . TYR A 1 214 ? 25.139 -0.609  -4.475  1.00 47.80  ?  220 TYR A CD1   1 
ATOM   1612 C CD2   . TYR A 1 214 ? 27.430 -0.713  -5.107  1.00 50.33  ?  220 TYR A CD2   1 
ATOM   1613 C CE1   . TYR A 1 214 ? 24.788 -1.287  -5.615  1.00 46.45  ?  220 TYR A CE1   1 
ATOM   1614 C CE2   . TYR A 1 214 ? 27.079 -1.412  -6.256  1.00 45.80  ?  220 TYR A CE2   1 
ATOM   1615 C CZ    . TYR A 1 214 ? 25.766 -1.691  -6.500  1.00 45.27  ?  220 TYR A CZ    1 
ATOM   1616 O OH    . TYR A 1 214 ? 25.400 -2.378  -7.625  1.00 50.70  ?  220 TYR A OH    1 
ATOM   1617 N N     . ARG A 1 215 ? 27.222 -2.808  -2.365  1.00 46.71  ?  221 ARG A N     1 
ATOM   1618 C CA    . ARG A 1 215 ? 27.782 -3.999  -2.979  1.00 48.99  ?  221 ARG A CA    1 
ATOM   1619 C C     . ARG A 1 215 ? 26.774 -4.520  -3.985  1.00 52.08  ?  221 ARG A C     1 
ATOM   1620 O O     . ARG A 1 215 ? 25.560 -4.319  -3.838  1.00 51.20  ?  221 ARG A O     1 
ATOM   1621 C CB    . ARG A 1 215 ? 28.093 -5.107  -1.959  1.00 51.28  ?  221 ARG A CB    1 
ATOM   1622 C CG    . ARG A 1 215 ? 29.143 -4.746  -0.928  1.00 53.10  ?  221 ARG A CG    1 
ATOM   1623 C CD    . ARG A 1 215 ? 30.505 -4.687  -1.566  1.00 57.07  ?  221 ARG A CD    1 
ATOM   1624 N NE    . ARG A 1 215 ? 31.568 -4.530  -0.581  1.00 63.16  ?  221 ARG A NE    1 
ATOM   1625 C CZ    . ARG A 1 215 ? 32.077 -5.521  0.141   1.00 66.53  ?  221 ARG A CZ    1 
ATOM   1626 N NH1   . ARG A 1 215 ? 31.625 -6.765  0.030   1.00 62.48  ?  221 ARG A NH1   1 
ATOM   1627 N NH2   . ARG A 1 215 ? 33.055 -5.254  1.008   1.00 67.70  ?  221 ARG A NH2   1 
ATOM   1628 N N     . GLU A 1 216 ? 27.279 -5.192  -5.016  1.00 50.26  ?  222 GLU A N     1 
ATOM   1629 C CA    . GLU A 1 216 ? 26.360 -5.755  -5.994  1.00 50.15  ?  222 GLU A CA    1 
ATOM   1630 C C     . GLU A 1 216 ? 25.491 -6.833  -5.347  1.00 49.11  ?  222 GLU A C     1 
ATOM   1631 O O     . GLU A 1 216 ? 24.300 -6.964  -5.669  1.00 44.70  ?  222 GLU A O     1 
ATOM   1632 C CB    . GLU A 1 216 ? 27.144 -6.296  -7.193  1.00 44.86  ?  222 GLU A CB    1 
ATOM   1633 N N     . TYR A 1 217 ? 26.059 -7.582  -4.396  1.00 47.94  ?  223 TYR A N     1 
ATOM   1634 C CA    . TYR A 1 217 ? 25.338 -8.660  -3.728  1.00 46.23  ?  223 TYR A CA    1 
ATOM   1635 C C     . TYR A 1 217 ? 25.772 -8.782  -2.275  1.00 49.28  ?  223 TYR A C     1 
ATOM   1636 O O     . TYR A 1 217 ? 26.954 -9.006  -1.993  1.00 49.61  ?  223 TYR A O     1 
ATOM   1637 C CB    . TYR A 1 217 ? 25.554 -9.990  -4.438  1.00 46.39  ?  223 TYR A CB    1 
ATOM   1638 C CG    . TYR A 1 217 ? 24.707 -11.047 -3.796  1.00 49.24  ?  223 TYR A CG    1 
ATOM   1639 C CD1   . TYR A 1 217 ? 23.394 -11.236 -4.197  1.00 46.84  ?  223 TYR A CD1   1 
ATOM   1640 C CD2   . TYR A 1 217 ? 25.194 -11.806 -2.738  1.00 49.47  ?  223 TYR A CD2   1 
ATOM   1641 C CE1   . TYR A 1 217 ? 22.599 -12.174 -3.591  1.00 50.72  ?  223 TYR A CE1   1 
ATOM   1642 C CE2   . TYR A 1 217 ? 24.410 -12.742 -2.128  1.00 49.91  ?  223 TYR A CE2   1 
ATOM   1643 C CZ    . TYR A 1 217 ? 23.118 -12.927 -2.565  1.00 52.85  ?  223 TYR A CZ    1 
ATOM   1644 O OH    . TYR A 1 217 ? 22.328 -13.867 -1.966  1.00 63.65  ?  223 TYR A OH    1 
ATOM   1645 N N     . ILE A 1 218 ? 24.807 -8.702  -1.362  1.00 48.10  ?  224 ILE A N     1 
ATOM   1646 C CA    . ILE A 1 218 ? 25.024 -8.961  0.060   1.00 44.62  ?  224 ILE A CA    1 
ATOM   1647 C C     . ILE A 1 218 ? 23.860 -9.809  0.549   1.00 47.77  ?  224 ILE A C     1 
ATOM   1648 O O     . ILE A 1 218 ? 22.702 -9.517  0.233   1.00 45.89  ?  224 ILE A O     1 
ATOM   1649 C CB    . ILE A 1 218 ? 25.110 -7.661  0.886   1.00 47.45  ?  224 ILE A CB    1 
ATOM   1650 C CG1   . ILE A 1 218 ? 26.372 -6.879  0.590   1.00 46.83  ?  224 ILE A CG1   1 
ATOM   1651 C CG2   . ILE A 1 218 ? 25.031 -7.947  2.401   1.00 51.34  ?  224 ILE A CG2   1 
ATOM   1652 C CD1   . ILE A 1 218 ? 26.273 -5.460  1.117   1.00 43.71  ?  224 ILE A CD1   1 
ATOM   1653 N N     . LYS A 1 219 ? 24.152 -10.852 1.312   1.00 49.36  ?  225 LYS A N     1 
ATOM   1654 C CA    . LYS A 1 219 ? 23.098 -11.699 1.867   1.00 56.13  ?  225 LYS A CA    1 
ATOM   1655 C C     . LYS A 1 219 ? 23.062 -11.537 3.375   1.00 58.39  ?  225 LYS A C     1 
ATOM   1656 O O     . LYS A 1 219 ? 24.022 -11.892 4.067   1.00 57.93  ?  225 LYS A O     1 
ATOM   1657 C CB    . LYS A 1 219 ? 23.277 -13.170 1.507   1.00 59.90  ?  225 LYS A CB    1 
ATOM   1658 C CG    . LYS A 1 219 ? 22.016 -13.978 1.795   1.00 61.40  ?  225 LYS A CG    1 
ATOM   1659 C CD    . LYS A 1 219 ? 22.136 -15.440 1.373   1.00 71.81  ?  225 LYS A CD    1 
ATOM   1660 C CE    . LYS A 1 219 ? 22.820 -16.260 2.470   1.00 78.50  ?  225 LYS A CE    1 
ATOM   1661 N NZ    . LYS A 1 219 ? 22.553 -17.726 2.326   1.00 78.05  ?  225 LYS A NZ    1 
ATOM   1662 N N     . VAL A 1 220 ? 21.956 -11.014 3.870   1.00 60.00  ?  226 VAL A N     1 
ATOM   1663 C CA    . VAL A 1 220 ? 21.708 -10.880 5.297   1.00 55.92  ?  226 VAL A CA    1 
ATOM   1664 C C     . VAL A 1 220 ? 20.969 -12.120 5.760   1.00 59.94  ?  226 VAL A C     1 
ATOM   1665 O O     . VAL A 1 220 ? 20.047 -12.594 5.085   1.00 57.87  ?  226 VAL A O     1 
ATOM   1666 C CB    . VAL A 1 220 ? 20.908 -9.597  5.582   1.00 53.89  ?  226 VAL A CB    1 
ATOM   1667 C CG1   . VAL A 1 220 ? 20.616 -9.454  7.061   1.00 55.51  ?  226 VAL A CG1   1 
ATOM   1668 C CG2   . VAL A 1 220 ? 21.669 -8.410  5.090   1.00 51.61  ?  226 VAL A CG2   1 
ATOM   1669 N N     . GLN A 1 221 ? 21.387 -12.662 6.900   1.00 61.97  ?  227 GLN A N     1 
ATOM   1670 C CA    . GLN A 1 221 ? 20.816 -13.880 7.456   1.00 64.32  ?  227 GLN A CA    1 
ATOM   1671 C C     . GLN A 1 221 ? 20.257 -13.618 8.846   1.00 63.97  ?  227 GLN A C     1 
ATOM   1672 O O     . GLN A 1 221 ? 20.808 -12.818 9.607   1.00 65.28  ?  227 GLN A O     1 
ATOM   1673 C CB    . GLN A 1 221 ? 21.856 -14.986 7.538   1.00 64.07  ?  227 GLN A CB    1 
ATOM   1674 C CG    . GLN A 1 221 ? 21.972 -15.825 6.310   1.00 65.73  ?  227 GLN A CG    1 
ATOM   1675 C CD    . GLN A 1 221 ? 23.079 -16.833 6.457   1.00 73.67  ?  227 GLN A CD    1 
ATOM   1676 O OE1   . GLN A 1 221 ? 24.017 -16.623 7.232   1.00 73.27  ?  227 GLN A OE1   1 
ATOM   1677 N NE2   . GLN A 1 221 ? 22.979 -17.943 5.728   1.00 75.80  ?  227 GLN A NE2   1 
ATOM   1678 N N     . THR A 1 222 ? 19.165 -14.301 9.173   1.00 64.45  ?  228 THR A N     1 
ATOM   1679 C CA    . THR A 1 222 ? 18.550 -14.203 10.482  1.00 68.74  ?  228 THR A CA    1 
ATOM   1680 C C     . THR A 1 222 ? 18.556 -15.557 11.177  1.00 74.54  ?  228 THR A C     1 
ATOM   1681 O O     . THR A 1 222 ? 18.598 -16.618 10.538  1.00 74.40  ?  228 THR A O     1 
ATOM   1682 C CB    . THR A 1 222 ? 17.100 -13.698 10.414  1.00 71.63  ?  228 THR A CB    1 
ATOM   1683 O OG1   . THR A 1 222 ? 16.237 -14.770 9.999   1.00 71.63  ?  228 THR A OG1   1 
ATOM   1684 C CG2   . THR A 1 222 ? 16.975 -12.510 9.462   1.00 66.98  ?  228 THR A CG2   1 
ATOM   1685 N N     . ASP A 1 223 ? 18.474 -15.489 12.509  1.00 70.43  ?  229 ASP A N     1 
ATOM   1686 C CA    . ASP A 1 223 ? 18.438 -16.682 13.345  1.00 74.82  ?  229 ASP A CA    1 
ATOM   1687 C C     . ASP A 1 223 ? 17.255 -17.592 13.024  1.00 74.01  ?  229 ASP A C     1 
ATOM   1688 O O     . ASP A 1 223 ? 17.292 -18.781 13.358  1.00 73.50  ?  229 ASP A O     1 
ATOM   1689 C CB    . ASP A 1 223 ? 18.412 -16.266 14.824  1.00 77.26  ?  229 ASP A CB    1 
ATOM   1690 C CG    . ASP A 1 223 ? 17.315 -15.240 15.137  1.00 80.19  ?  229 ASP A CG    1 
ATOM   1691 O OD1   . ASP A 1 223 ? 16.528 -14.888 14.224  1.00 80.95  ?  229 ASP A OD1   1 
ATOM   1692 O OD2   . ASP A 1 223 ? 17.240 -14.784 16.302  1.00 85.09  -1 229 ASP A OD2   1 
ATOM   1693 N N     . LYS A 1 224 ? 16.209 -17.060 12.398  1.00 73.38  ?  230 LYS A N     1 
ATOM   1694 C CA    . LYS A 1 224 ? 15.071 -17.850 11.962  1.00 70.05  ?  230 LYS A CA    1 
ATOM   1695 C C     . LYS A 1 224 ? 15.265 -18.414 10.564  1.00 74.52  ?  230 LYS A C     1 
ATOM   1696 O O     . LYS A 1 224 ? 14.343 -19.041 10.026  1.00 77.53  ?  230 LYS A O     1 
ATOM   1697 C CB    . LYS A 1 224 ? 13.792 -17.010 12.017  1.00 71.39  ?  230 LYS A CB    1 
ATOM   1698 N N     . GLY A 1 225 ? 16.438 -18.202 9.962   1.00 75.08  ?  231 GLY A N     1 
ATOM   1699 C CA    . GLY A 1 225 ? 16.732 -18.742 8.645   1.00 71.13  ?  231 GLY A CA    1 
ATOM   1700 C C     . GLY A 1 225 ? 16.260 -17.912 7.473   1.00 67.39  ?  231 GLY A C     1 
ATOM   1701 O O     . GLY A 1 225 ? 16.346 -18.380 6.334   1.00 66.00  ?  231 GLY A O     1 
ATOM   1702 N N     . THR A 1 226 ? 15.756 -16.703 7.713   1.00 68.87  ?  232 THR A N     1 
ATOM   1703 C CA    . THR A 1 226 ? 15.326 -15.822 6.639   1.00 63.17  ?  232 THR A CA    1 
ATOM   1704 C C     . THR A 1 226 ? 16.551 -15.202 5.993   1.00 66.30  ?  232 THR A C     1 
ATOM   1705 O O     . THR A 1 226 ? 17.388 -14.608 6.679   1.00 64.57  ?  232 THR A O     1 
ATOM   1706 C CB    . THR A 1 226 ? 14.406 -14.719 7.166   1.00 62.52  ?  232 THR A CB    1 
ATOM   1707 O OG1   . THR A 1 226 ? 13.320 -15.292 7.894   1.00 66.00  ?  232 THR A OG1   1 
ATOM   1708 C CG2   . THR A 1 226 ? 13.846 -13.902 6.025   1.00 62.66  ?  232 THR A CG2   1 
ATOM   1709 N N     . GLU A 1 227 ? 16.656 -15.331 4.674   1.00 65.54  ?  233 GLU A N     1 
ATOM   1710 C CA    . GLU A 1 227 ? 17.768 -14.766 3.929   1.00 62.11  ?  233 GLU A CA    1 
ATOM   1711 C C     . GLU A 1 227 ? 17.257 -13.629 3.064   1.00 59.41  ?  233 GLU A C     1 
ATOM   1712 O O     . GLU A 1 227 ? 16.280 -13.787 2.328   1.00 62.66  ?  233 GLU A O     1 
ATOM   1713 C CB    . GLU A 1 227 ? 18.475 -15.839 3.099   1.00 68.64  ?  233 GLU A CB    1 
ATOM   1714 C CG    . GLU A 1 227 ? 19.277 -16.804 3.978   1.00 70.94  ?  233 GLU A CG    1 
ATOM   1715 C CD    . GLU A 1 227 ? 19.550 -18.149 3.322   1.00 80.40  ?  233 GLU A CD    1 
ATOM   1716 O OE1   . GLU A 1 227 ? 20.117 -18.166 2.206   1.00 79.95  ?  233 GLU A OE1   1 
ATOM   1717 O OE2   . GLU A 1 227 ? 19.198 -19.192 3.929   1.00 83.34  -1 233 GLU A OE2   1 
ATOM   1718 N N     . VAL A 1 228 ? 17.893 -12.476 3.200   1.00 59.83  ?  234 VAL A N     1 
ATOM   1719 C CA    . VAL A 1 228 ? 17.511 -11.262 2.506   1.00 54.03  ?  234 VAL A CA    1 
ATOM   1720 C C     . VAL A 1 228 ? 18.728 -10.814 1.714   1.00 52.15  ?  234 VAL A C     1 
ATOM   1721 O O     . VAL A 1 228 ? 19.762 -10.449 2.291   1.00 50.62  ?  234 VAL A O     1 
ATOM   1722 C CB    . VAL A 1 228 ? 17.033 -10.172 3.477   1.00 53.35  ?  234 VAL A CB    1 
ATOM   1723 C CG1   . VAL A 1 228 ? 16.420 -9.002  2.730   1.00 48.77  ?  234 VAL A CG1   1 
ATOM   1724 C CG2   . VAL A 1 228 ? 16.032 -10.762 4.490   1.00 53.18  ?  234 VAL A CG2   1 
ATOM   1725 N N     . ALA A 1 229 ? 18.616 -10.882 0.395   1.00 50.07  ?  235 ALA A N     1 
ATOM   1726 C CA    . ALA A 1 229 ? 19.624 -10.334 -0.495  1.00 49.59  ?  235 ALA A CA    1 
ATOM   1727 C C     . ALA A 1 229 ? 19.441 -8.819  -0.629  1.00 46.16  ?  235 ALA A C     1 
ATOM   1728 O O     . ALA A 1 229 ? 18.313 -8.321  -0.717  1.00 45.93  ?  235 ALA A O     1 
ATOM   1729 C CB    . ALA A 1 229 ? 19.524 -11.026 -1.858  1.00 45.55  ?  235 ALA A CB    1 
ATOM   1730 N N     . THR A 1 230 ? 20.553 -8.081  -0.641  1.00 41.01  ?  236 THR A N     1 
ATOM   1731 C CA    . THR A 1 230 ? 20.477 -6.629  -0.565  1.00 41.72  ?  236 THR A CA    1 
ATOM   1732 C C     . THR A 1 230 ? 21.699 -6.006  -1.231  1.00 39.46  ?  236 THR A C     1 
ATOM   1733 O O     . THR A 1 230 ? 22.691 -6.677  -1.490  1.00 40.52  ?  236 THR A O     1 
ATOM   1734 C CB    . THR A 1 230 ? 20.367 -6.179  0.902   1.00 42.79  ?  236 THR A CB    1 
ATOM   1735 O OG1   . THR A 1 230 ? 19.935 -4.817  0.963   1.00 45.19  ?  236 THR A OG1   1 
ATOM   1736 C CG2   . THR A 1 230 ? 21.703 -6.267  1.559   1.00 44.00  ?  236 THR A CG2   1 
ATOM   1737 N N     . ASN A 1 231 ? 21.627 -4.699  -1.497  1.00 43.72  ?  237 ASN A N     1 
ATOM   1738 C CA    . ASN A 1 231 ? 22.797 -3.938  -1.941  1.00 43.94  ?  237 ASN A CA    1 
ATOM   1739 C C     . ASN A 1 231 ? 23.463 -3.142  -0.836  1.00 44.07  ?  237 ASN A C     1 
ATOM   1740 O O     . ASN A 1 231 ? 24.636 -2.788  -0.978  1.00 45.06  ?  237 ASN A O     1 
ATOM   1741 C CB    . ASN A 1 231 ? 22.440 -2.941  -3.045  1.00 44.12  ?  237 ASN A CB    1 
ATOM   1742 C CG    . ASN A 1 231 ? 21.842 -3.602  -4.228  1.00 47.79  ?  237 ASN A CG    1 
ATOM   1743 O OD1   . ASN A 1 231 ? 20.756 -3.237  -4.693  1.00 48.03  ?  237 ASN A OD1   1 
ATOM   1744 N ND2   . ASN A 1 231 ? 22.545 -4.597  -4.740  1.00 49.36  ?  237 ASN A ND2   1 
ATOM   1745 N N     . LEU A 1 232 ? 22.747 -2.824  0.241   1.00 47.95  ?  238 LEU A N     1 
ATOM   1746 C CA    . LEU A 1 232 ? 23.265 -1.934  1.273   1.00 45.60  ?  238 LEU A CA    1 
ATOM   1747 C C     . LEU A 1 232 ? 22.717 -2.387  2.613   1.00 44.33  ?  238 LEU A C     1 
ATOM   1748 O O     . LEU A 1 232 ? 21.526 -2.679  2.727   1.00 45.99  ?  238 LEU A O     1 
ATOM   1749 C CB    . LEU A 1 232 ? 22.857 -0.483  0.998   1.00 43.78  ?  238 LEU A CB    1 
ATOM   1750 C CG    . LEU A 1 232 ? 23.470 0.607   1.870   1.00 44.88  ?  238 LEU A CG    1 
ATOM   1751 C CD1   . LEU A 1 232 ? 24.952 0.650   1.645   1.00 46.73  ?  238 LEU A CD1   1 
ATOM   1752 C CD2   . LEU A 1 232 ? 22.865 1.957   1.566   1.00 42.30  ?  238 LEU A CD2   1 
ATOM   1753 N N     . VAL A 1 233 ? 23.580 -2.432  3.623   1.00 46.30  ?  239 VAL A N     1 
ATOM   1754 C CA    . VAL A 1 233 ? 23.178 -2.740  4.993   1.00 43.04  ?  239 VAL A CA    1 
ATOM   1755 C C     . VAL A 1 233 ? 23.487 -1.541  5.885   1.00 46.49  ?  239 VAL A C     1 
ATOM   1756 O O     . VAL A 1 233 ? 24.653 -1.152  6.040   1.00 46.76  ?  239 VAL A O     1 
ATOM   1757 C CB    . VAL A 1 233 ? 23.878 -3.998  5.522   1.00 48.21  ?  239 VAL A CB    1 
ATOM   1758 C CG1   . VAL A 1 233 ? 23.546 -4.197  6.983   1.00 47.87  ?  239 VAL A CG1   1 
ATOM   1759 C CG2   . VAL A 1 233 ? 23.467 -5.207  4.724   1.00 49.93  ?  239 VAL A CG2   1 
ATOM   1760 N N     . ILE A 1 234 ? 22.447 -0.975  6.491   1.00 45.76  ?  240 ILE A N     1 
ATOM   1761 C CA    . ILE A 1 234 ? 22.570 0.132   7.430   1.00 44.61  ?  240 ILE A CA    1 
ATOM   1762 C C     . ILE A 1 234 ? 22.247 -0.365  8.832   1.00 47.81  ?  240 ILE A C     1 
ATOM   1763 O O     . ILE A 1 234 ? 21.179 -0.942  9.080   1.00 45.12  ?  240 ILE A O     1 
ATOM   1764 C CB    . ILE A 1 234 ? 21.654 1.306   7.060   1.00 42.20  ?  240 ILE A CB    1 
ATOM   1765 C CG1   . ILE A 1 234 ? 21.877 1.726   5.597   1.00 40.73  ?  240 ILE A CG1   1 
ATOM   1766 C CG2   . ILE A 1 234 ? 21.890 2.455   8.035   1.00 38.76  ?  240 ILE A CG2   1 
ATOM   1767 C CD1   . ILE A 1 234 ? 20.938 2.813   5.109   1.00 37.46  ?  240 ILE A CD1   1 
ATOM   1768 N N     . LEU A 1 235 ? 23.149 -0.101  9.753   1.00 46.33  ?  241 LEU A N     1 
ATOM   1769 C CA    . LEU A 1 235 ? 23.007 -0.570  11.110  1.00 45.72  ?  241 LEU A CA    1 
ATOM   1770 C C     . LEU A 1 235 ? 22.423 0.551   11.960  1.00 51.26  ?  241 LEU A C     1 
ATOM   1771 O O     . LEU A 1 235 ? 22.913 1.683   11.935  1.00 52.56  ?  241 LEU A O     1 
ATOM   1772 C CB    . LEU A 1 235 ? 24.363 -1.033  11.628  1.00 47.44  ?  241 LEU A CB    1 
ATOM   1773 C CG    . LEU A 1 235 ? 24.345 -1.657  13.004  1.00 55.95  ?  241 LEU A CG    1 
ATOM   1774 C CD1   . LEU A 1 235 ? 23.331 -2.797  13.030  1.00 54.79  ?  241 LEU A CD1   1 
ATOM   1775 C CD2   . LEU A 1 235 ? 25.738 -2.140  13.344  1.00 57.59  ?  241 LEU A CD2   1 
ATOM   1776 N N     . CYS A 1 236 ? 21.360 0.242   12.690  1.00 55.23  ?  242 CYS A N     1 
ATOM   1777 C CA    . CYS A 1 236 ? 20.671 1.218   13.511  1.00 50.46  ?  242 CYS A CA    1 
ATOM   1778 C C     . CYS A 1 236 ? 20.345 0.606   14.865  1.00 58.46  ?  242 CYS A C     1 
ATOM   1779 O O     . CYS A 1 236 ? 19.200 0.567   15.300  1.00 64.93  ?  242 CYS A O     1 
ATOM   1780 C CB    . CYS A 1 236 ? 19.396 1.699   12.836  1.00 48.22  ?  242 CYS A CB    1 
ATOM   1781 S SG    . CYS A 1 236 ? 19.739 2.784   11.490  1.00 53.45  ?  242 CYS A SG    1 
ATOM   1782 N N     . THR A 1 237 ? 21.365 0.105   15.547  1.00 62.31  ?  243 THR A N     1 
ATOM   1783 C CA    . THR A 1 237 ? 21.152 -0.360  16.905  1.00 66.81  ?  243 THR A CA    1 
ATOM   1784 C C     . THR A 1 237 ? 22.461 -0.241  17.667  1.00 68.52  ?  243 THR A C     1 
ATOM   1785 O O     . THR A 1 237 ? 23.539 -0.498  17.117  1.00 69.45  ?  243 THR A O     1 
ATOM   1786 C CB    . THR A 1 237 ? 20.619 -1.803  16.916  1.00 67.98  ?  243 THR A CB    1 
ATOM   1787 O OG1   . THR A 1 237 ? 20.325 -2.194  18.262  1.00 81.03  ?  243 THR A OG1   1 
ATOM   1788 C CG2   . THR A 1 237 ? 21.622 -2.765  16.305  1.00 61.11  ?  243 THR A CG2   1 
ATOM   1789 N N     . GLY A 1 238 ? 22.364 0.169   18.926  1.00 68.18  ?  244 GLY A N     1 
ATOM   1790 C CA    . GLY A 1 238 ? 23.540 0.193   19.767  1.00 65.71  ?  244 GLY A CA    1 
ATOM   1791 C C     . GLY A 1 238 ? 23.915 1.552   20.318  1.00 67.34  ?  244 GLY A C     1 
ATOM   1792 O O     . GLY A 1 238 ? 25.103 1.824   20.531  1.00 68.09  ?  244 GLY A O     1 
ATOM   1793 N N     . ILE A 1 239 ? 22.923 2.412   20.570  1.00 64.80  ?  245 ILE A N     1 
ATOM   1794 C CA    . ILE A 1 239 ? 23.203 3.682   21.230  1.00 60.46  ?  245 ILE A CA    1 
ATOM   1795 C C     . ILE A 1 239 ? 23.546 3.412   22.687  1.00 63.68  ?  245 ILE A C     1 
ATOM   1796 O O     . ILE A 1 239 ? 22.835 2.672   23.381  1.00 66.23  ?  245 ILE A O     1 
ATOM   1797 C CB    . ILE A 1 239 ? 22.013 4.644   21.102  1.00 59.59  ?  245 ILE A CB    1 
ATOM   1798 C CG1   . ILE A 1 239 ? 21.542 4.714   19.651  1.00 62.06  ?  245 ILE A CG1   1 
ATOM   1799 C CG2   . ILE A 1 239 ? 22.412 6.034   21.525  1.00 57.58  ?  245 ILE A CG2   1 
ATOM   1800 C CD1   . ILE A 1 239 ? 22.645 5.041   18.708  1.00 61.14  ?  245 ILE A CD1   1 
ATOM   1801 N N     . LYS A 1 240 ? 24.651 3.991   23.155  1.00 61.90  ?  246 LYS A N     1 
ATOM   1802 C CA    . LYS A 1 240 ? 25.050 3.845   24.548  1.00 57.65  ?  246 LYS A CA    1 
ATOM   1803 C C     . LYS A 1 240 ? 25.833 5.076   24.984  1.00 60.81  ?  246 LYS A C     1 
ATOM   1804 O O     . LYS A 1 240 ? 26.319 5.853   24.153  1.00 58.74  ?  246 LYS A O     1 
ATOM   1805 C CB    . LYS A 1 240 ? 25.866 2.560   24.768  1.00 63.04  ?  246 LYS A CB    1 
ATOM   1806 C CG    . LYS A 1 240 ? 27.197 2.492   24.043  1.00 65.31  ?  246 LYS A CG    1 
ATOM   1807 C CD    . LYS A 1 240 ? 28.139 1.460   24.662  1.00 68.48  ?  246 LYS A CD    1 
ATOM   1808 C CE    . LYS A 1 240 ? 27.485 0.087   24.784  1.00 76.16  ?  246 LYS A CE    1 
ATOM   1809 N NZ    . LYS A 1 240 ? 27.360 -0.605  23.462  1.00 90.17  ?  246 LYS A NZ    1 
ATOM   1810 N N     . ILE A 1 241 ? 25.939 5.249   26.309  1.00 59.06  ?  247 ILE A N     1 
ATOM   1811 C CA    . ILE A 1 241 ? 26.574 6.434   26.881  1.00 57.82  ?  247 ILE A CA    1 
ATOM   1812 C C     . ILE A 1 241 ? 28.061 6.456   26.540  1.00 58.48  ?  247 ILE A C     1 
ATOM   1813 O O     . ILE A 1 241 ? 28.729 5.414   26.505  1.00 61.34  ?  247 ILE A O     1 
ATOM   1814 C CB    . ILE A 1 241 ? 26.363 6.468   28.405  1.00 63.92  ?  247 ILE A CB    1 
ATOM   1815 C CG1   . ILE A 1 241 ? 24.897 6.228   28.759  1.00 65.94  ?  247 ILE A CG1   1 
ATOM   1816 C CG2   . ILE A 1 241 ? 26.832 7.776   28.988  1.00 61.46  ?  247 ILE A CG2   1 
ATOM   1817 C CD1   . ILE A 1 241 ? 23.983 7.326   28.393  1.00 60.20  ?  247 ILE A CD1   1 
ATOM   1818 N N     . ASN A 1 242 ? 28.593 7.650   26.288  1.00 55.81  ?  248 ASN A N     1 
ATOM   1819 C CA    . ASN A 1 242 ? 30.001 7.806   25.936  1.00 57.82  ?  248 ASN A CA    1 
ATOM   1820 C C     . ASN A 1 242 ? 30.792 8.214   27.179  1.00 61.69  ?  248 ASN A C     1 
ATOM   1821 O O     . ASN A 1 242 ? 31.094 9.392   27.410  1.00 62.09  ?  248 ASN A O     1 
ATOM   1822 C CB    . ASN A 1 242 ? 30.147 8.822   24.812  1.00 55.42  ?  248 ASN A CB    1 
ATOM   1823 C CG    . ASN A 1 242 ? 31.536 8.855   24.249  1.00 57.36  ?  248 ASN A CG    1 
ATOM   1824 O OD1   . ASN A 1 242 ? 32.480 8.383   24.882  1.00 54.11  ?  248 ASN A OD1   1 
ATOM   1825 N ND2   . ASN A 1 242 ? 31.680 9.409   23.046  1.00 63.66  ?  248 ASN A ND2   1 
ATOM   1826 N N     . SER A 1 243 ? 31.170 7.208   27.961  1.00 55.15  ?  249 SER A N     1 
ATOM   1827 C CA    . SER A 1 243 ? 31.922 7.376   29.198  1.00 62.46  ?  249 SER A CA    1 
ATOM   1828 C C     . SER A 1 243 ? 33.427 7.365   28.999  1.00 66.00  ?  249 SER A C     1 
ATOM   1829 O O     . SER A 1 243 ? 34.162 7.272   29.985  1.00 66.77  ?  249 SER A O     1 
ATOM   1830 C CB    . SER A 1 243 ? 31.568 6.274   30.178  1.00 67.05  ?  249 SER A CB    1 
ATOM   1831 O OG    . SER A 1 243 ? 30.229 5.896   30.008  1.00 73.51  ?  249 SER A OG    1 
ATOM   1832 N N     . SER A 1 244 ? 33.900 7.426   27.758  1.00 62.90  ?  250 SER A N     1 
ATOM   1833 C CA    . SER A 1 244 ? 35.337 7.407   27.516  1.00 64.42  ?  250 SER A CA    1 
ATOM   1834 C C     . SER A 1 244 ? 36.066 8.345   28.468  1.00 70.68  ?  250 SER A C     1 
ATOM   1835 O O     . SER A 1 244 ? 37.004 7.943   29.164  1.00 71.57  ?  250 SER A O     1 
ATOM   1836 C CB    . SER A 1 244 ? 35.614 7.814   26.076  1.00 61.24  ?  250 SER A CB    1 
ATOM   1837 O OG    . SER A 1 244 ? 34.852 8.970   25.771  1.00 67.16  ?  250 SER A OG    1 
ATOM   1838 N N     . ALA A 1 245 ? 35.599 9.595   28.544  1.00 70.19  ?  251 ALA A N     1 
ATOM   1839 C CA    . ALA A 1 245 ? 36.337 10.656  29.220  1.00 69.65  ?  251 ALA A CA    1 
ATOM   1840 C C     . ALA A 1 245 ? 36.401 10.483  30.736  1.00 75.84  ?  251 ALA A C     1 
ATOM   1841 O O     . ALA A 1 245 ? 37.357 10.959  31.362  1.00 78.54  ?  251 ALA A O     1 
ATOM   1842 C CB    . ALA A 1 245 ? 35.708 12.005  28.893  1.00 67.86  ?  251 ALA A CB    1 
ATOM   1843 N N     . TYR A 1 246 ? 35.409 9.839   31.356  1.00 69.10  ?  252 TYR A N     1 
ATOM   1844 C CA    . TYR A 1 246 ? 35.283 9.960   32.797  1.00 72.29  ?  252 TYR A CA    1 
ATOM   1845 C C     . TYR A 1 246 ? 35.139 8.654   33.563  1.00 77.11  ?  252 TYR A C     1 
ATOM   1846 O O     . TYR A 1 246 ? 35.041 8.698   34.792  1.00 77.41  ?  252 TYR A O     1 
ATOM   1847 C CB    . TYR A 1 246 ? 34.095 10.873  33.136  1.00 72.26  ?  252 TYR A CB    1 
ATOM   1848 C CG    . TYR A 1 246 ? 32.743 10.373  32.685  1.00 68.24  ?  252 TYR A CG    1 
ATOM   1849 C CD1   . TYR A 1 246 ? 32.071 9.392   33.398  1.00 70.51  ?  252 TYR A CD1   1 
ATOM   1850 C CD2   . TYR A 1 246 ? 32.121 10.905  31.569  1.00 64.10  ?  252 TYR A CD2   1 
ATOM   1851 C CE1   . TYR A 1 246 ? 30.831 8.943   33.000  1.00 68.65  ?  252 TYR A CE1   1 
ATOM   1852 C CE2   . TYR A 1 246 ? 30.874 10.461  31.163  1.00 61.59  ?  252 TYR A CE2   1 
ATOM   1853 C CZ    . TYR A 1 246 ? 30.242 9.481   31.882  1.00 68.37  ?  252 TYR A CZ    1 
ATOM   1854 O OH    . TYR A 1 246 ? 29.007 9.043   31.499  1.00 66.99  ?  252 TYR A OH    1 
ATOM   1855 N N     . ARG A 1 247 ? 35.139 7.501   32.890  1.00 82.93  ?  253 ARG A N     1 
ATOM   1856 C CA    . ARG A 1 247 ? 34.749 6.254   33.549  1.00 80.71  ?  253 ARG A CA    1 
ATOM   1857 C C     . ARG A 1 247 ? 35.776 5.815   34.591  1.00 83.22  ?  253 ARG A C     1 
ATOM   1858 O O     . ARG A 1 247 ? 35.415 5.461   35.719  1.00 85.50  ?  253 ARG A O     1 
ATOM   1859 C CB    . ARG A 1 247 ? 34.543 5.154   32.508  1.00 78.48  ?  253 ARG A CB    1 
ATOM   1860 C CG    . ARG A 1 247 ? 33.795 3.949   33.044  1.00 86.51  ?  253 ARG A CG    1 
ATOM   1861 C CD    . ARG A 1 247 ? 34.155 2.671   32.318  1.00 87.35  ?  253 ARG A CD    1 
ATOM   1862 N NE    . ARG A 1 247 ? 33.917 1.509   33.168  1.00 97.07  ?  253 ARG A NE    1 
ATOM   1863 C CZ    . ARG A 1 247 ? 34.834 0.948   33.946  1.00 99.37  ?  253 ARG A CZ    1 
ATOM   1864 N NH1   . ARG A 1 247 ? 36.084 1.385   33.969  1.00 98.93  ?  253 ARG A NH1   1 
ATOM   1865 N NH2   . ARG A 1 247 ? 34.489 -0.075  34.723  1.00 101.21 ?  253 ARG A NH2   1 
ATOM   1866 N N     . LYS A 1 248 ? 37.063 5.814   34.223  1.00 86.18  ?  254 LYS A N     1 
ATOM   1867 C CA    . LYS A 1 248 ? 38.118 5.389   35.140  1.00 86.53  ?  254 LYS A CA    1 
ATOM   1868 C C     . LYS A 1 248 ? 38.082 6.165   36.452  1.00 88.16  ?  254 LYS A C     1 
ATOM   1869 O O     . LYS A 1 248 ? 38.360 5.600   37.514  1.00 98.82  ?  254 LYS A O     1 
ATOM   1870 C CB    . LYS A 1 248 ? 39.486 5.543   34.465  1.00 86.31  ?  254 LYS A CB    1 
ATOM   1871 C CG    . LYS A 1 248 ? 40.675 5.171   35.339  1.00 92.21  ?  254 LYS A CG    1 
ATOM   1872 N N     . ALA A 1 249 ? 37.712 7.442   36.407  1.00 87.07  ?  255 ALA A N     1 
ATOM   1873 C CA    . ALA A 1 249 ? 37.777 8.300   37.580  1.00 81.78  ?  255 ALA A CA    1 
ATOM   1874 C C     . ALA A 1 249 ? 36.501 8.303   38.405  1.00 84.26  ?  255 ALA A C     1 
ATOM   1875 O O     . ALA A 1 249 ? 36.557 8.582   39.610  1.00 89.14  ?  255 ALA A O     1 
ATOM   1876 C CB    . ALA A 1 249 ? 38.102 9.734   37.163  1.00 83.95  ?  255 ALA A CB    1 
ATOM   1877 N N     . PHE A 1 250 ? 35.353 8.021   37.794  1.00 80.97  ?  256 PHE A N     1 
ATOM   1878 C CA    . PHE A 1 250 ? 34.080 8.029   38.501  1.00 78.36  ?  256 PHE A CA    1 
ATOM   1879 C C     . PHE A 1 250 ? 33.452 6.649   38.568  1.00 83.07  ?  256 PHE A C     1 
ATOM   1880 O O     . PHE A 1 250 ? 32.232 6.554   38.715  1.00 81.87  ?  256 PHE A O     1 
ATOM   1881 C CB    . PHE A 1 250 ? 33.075 8.977   37.847  1.00 80.11  ?  256 PHE A CB    1 
ATOM   1882 C CG    . PHE A 1 250 ? 33.443 10.435  37.898  1.00 81.27  ?  256 PHE A CG    1 
ATOM   1883 C CD1   . PHE A 1 250 ? 34.366 10.968  37.011  1.00 78.31  ?  256 PHE A CD1   1 
ATOM   1884 C CD2   . PHE A 1 250 ? 32.799 11.292  38.780  1.00 84.66  ?  256 PHE A CD2   1 
ATOM   1885 C CE1   . PHE A 1 250 ? 34.677 12.313  37.033  1.00 75.32  ?  256 PHE A CE1   1 
ATOM   1886 C CE2   . PHE A 1 250 ? 33.107 12.644  38.804  1.00 82.49  ?  256 PHE A CE2   1 
ATOM   1887 C CZ    . PHE A 1 250 ? 34.049 13.152  37.926  1.00 75.49  ?  256 PHE A CZ    1 
ATOM   1888 N N     . GLU A 1 251 ? 34.247 5.581   38.431  1.00 84.74  ?  257 GLU A N     1 
ATOM   1889 C CA    . GLU A 1 251 ? 33.688 4.229   38.484  1.00 86.32  ?  257 GLU A CA    1 
ATOM   1890 C C     . GLU A 1 251 ? 32.754 4.071   39.679  1.00 92.80  ?  257 GLU A C     1 
ATOM   1891 O O     . GLU A 1 251 ? 31.651 3.524   39.555  1.00 87.07  ?  257 GLU A O     1 
ATOM   1892 C CB    . GLU A 1 251 ? 34.810 3.185   38.531  1.00 81.67  ?  257 GLU A CB    1 
ATOM   1893 N N     . SER A 1 252 ? 33.174 4.592   40.841  1.00 92.43  ?  258 SER A N     1 
ATOM   1894 C CA    . SER A 1 252 ? 32.336 4.563   42.034  1.00 91.84  ?  258 SER A CA    1 
ATOM   1895 C C     . SER A 1 252 ? 30.993 5.236   41.796  1.00 91.95  ?  258 SER A C     1 
ATOM   1896 O O     . SER A 1 252 ? 29.987 4.858   42.407  1.00 89.27  ?  258 SER A O     1 
ATOM   1897 C CB    . SER A 1 252 ? 33.061 5.248   43.192  1.00 87.11  ?  258 SER A CB    1 
ATOM   1898 O OG    . SER A 1 252 ? 32.240 6.247   43.772  1.00 91.49  ?  258 SER A OG    1 
ATOM   1899 N N     . ARG A 1 253 ? 30.954 6.218   40.898  1.00 94.60  ?  259 ARG A N     1 
ATOM   1900 C CA    . ARG A 1 253 ? 29.778 7.055   40.717  1.00 92.89  ?  259 ARG A CA    1 
ATOM   1901 C C     . ARG A 1 253 ? 28.924 6.667   39.527  1.00 91.11  ?  259 ARG A C     1 
ATOM   1902 O O     . ARG A 1 253 ? 27.720 6.939   39.545  1.00 88.63  ?  259 ARG A O     1 
ATOM   1903 C CB    . ARG A 1 253 ? 30.197 8.519   40.573  1.00 91.74  ?  259 ARG A CB    1 
ATOM   1904 C CG    . ARG A 1 253 ? 30.770 9.077   41.840  1.00 90.05  ?  259 ARG A CG    1 
ATOM   1905 C CD    . ARG A 1 253 ? 29.833 8.759   42.974  1.00 93.39  ?  259 ARG A CD    1 
ATOM   1906 N NE    . ARG A 1 253 ? 30.419 9.069   44.266  1.00 96.37  ?  259 ARG A NE    1 
ATOM   1907 C CZ    . ARG A 1 253 ? 29.760 8.977   45.409  1.00 95.58  ?  259 ARG A CZ    1 
ATOM   1908 N NH1   . ARG A 1 253 ? 28.496 8.589   45.445  1.00 90.75  ?  259 ARG A NH1   1 
ATOM   1909 N NH2   . ARG A 1 253 ? 30.384 9.282   46.541  1.00 98.33  ?  259 ARG A NH2   1 
ATOM   1910 N N     . LEU A 1 254 ? 29.506 6.049   38.498  1.00 94.83  ?  260 LEU A N     1 
ATOM   1911 C CA    . LEU A 1 254 ? 28.737 5.703   37.309  1.00 85.23  ?  260 LEU A CA    1 
ATOM   1912 C C     . LEU A 1 254 ? 27.652 4.706   37.675  1.00 87.13  ?  260 LEU A C     1 
ATOM   1913 O O     . LEU A 1 254 ? 27.930 3.681   38.303  1.00 89.86  ?  260 LEU A O     1 
ATOM   1914 C CB    . LEU A 1 254 ? 29.653 5.132   36.233  1.00 79.22  ?  260 LEU A CB    1 
ATOM   1915 N N     . ALA A 1 255 ? 26.407 5.035   37.328  1.00 84.74  ?  261 ALA A N     1 
ATOM   1916 C CA    . ALA A 1 255 ? 25.333 4.059   37.385  1.00 84.78  ?  261 ALA A CA    1 
ATOM   1917 C C     . ALA A 1 255 ? 25.646 2.950   36.389  1.00 88.88  ?  261 ALA A C     1 
ATOM   1918 O O     . ALA A 1 255 ? 26.592 3.038   35.603  1.00 86.70  ?  261 ALA A O     1 
ATOM   1919 C CB    . ALA A 1 255 ? 23.982 4.695   37.065  1.00 78.35  ?  261 ALA A CB    1 
ATOM   1920 N N     . SER A 1 256 ? 24.850 1.883   36.432  1.00 89.10  ?  262 SER A N     1 
ATOM   1921 C CA    . SER A 1 256 ? 25.202 0.718   35.636  1.00 89.05  ?  262 SER A CA    1 
ATOM   1922 C C     . SER A 1 256 ? 25.185 1.050   34.148  1.00 94.10  ?  262 SER A C     1 
ATOM   1923 O O     . SER A 1 256 ? 26.069 0.616   33.402  1.00 92.33  ?  262 SER A O     1 
ATOM   1924 C CB    . SER A 1 256 ? 24.256 -0.437  35.957  1.00 90.40  ?  262 SER A CB    1 
ATOM   1925 N N     . SER A 1 257 ? 24.218 1.865   33.711  1.00 93.38  ?  263 SER A N     1 
ATOM   1926 C CA    . SER A 1 257 ? 24.036 2.225   32.306  1.00 85.55  ?  263 SER A CA    1 
ATOM   1927 C C     . SER A 1 257 ? 25.138 3.128   31.751  1.00 78.77  ?  263 SER A C     1 
ATOM   1928 O O     . SER A 1 257 ? 25.045 3.511   30.590  1.00 84.22  ?  263 SER A O     1 
ATOM   1929 C CB    . SER A 1 257 ? 22.686 2.932   32.113  1.00 82.44  ?  263 SER A CB    1 
ATOM   1930 O OG    . SER A 1 257 ? 22.815 4.339   32.268  1.00 76.95  ?  263 SER A OG    1 
ATOM   1931 N N     . GLY A 1 258 ? 26.177 3.484   32.512  1.00 80.95  ?  264 GLY A N     1 
ATOM   1932 C CA    . GLY A 1 258 ? 27.190 4.414   32.056  1.00 75.52  ?  264 GLY A CA    1 
ATOM   1933 C C     . GLY A 1 258 ? 26.986 5.857   32.498  1.00 75.04  ?  264 GLY A C     1 
ATOM   1934 O O     . GLY A 1 258 ? 27.958 6.632   32.533  1.00 72.25  ?  264 GLY A O     1 
ATOM   1935 N N     . ALA A 1 259 ? 25.761 6.239   32.842  1.00 73.27  ?  265 ALA A N     1 
ATOM   1936 C CA    . ALA A 1 259 ? 25.505 7.614   33.241  1.00 73.93  ?  265 ALA A CA    1 
ATOM   1937 C C     . ALA A 1 259 ? 26.007 7.879   34.660  1.00 75.69  ?  265 ALA A C     1 
ATOM   1938 O O     . ALA A 1 259 ? 26.170 6.974   35.482  1.00 75.90  ?  265 ALA A O     1 
ATOM   1939 C CB    . ALA A 1 259 ? 24.011 7.929   33.152  1.00 73.45  ?  265 ALA A CB    1 
ATOM   1940 N N     . LEU A 1 260 ? 26.278 9.150   34.927  1.00 72.64  ?  266 LEU A N     1 
ATOM   1941 C CA    . LEU A 1 260 ? 26.630 9.589   36.264  1.00 70.97  ?  266 LEU A CA    1 
ATOM   1942 C C     . LEU A 1 260 ? 25.354 9.833   37.055  1.00 71.84  ?  266 LEU A C     1 
ATOM   1943 O O     . LEU A 1 260 ? 24.450 10.525  36.581  1.00 74.28  ?  266 LEU A O     1 
ATOM   1944 C CB    . LEU A 1 260 ? 27.462 10.862  36.191  1.00 64.92  ?  266 LEU A CB    1 
ATOM   1945 C CG    . LEU A 1 260 ? 28.687 10.775  35.287  1.00 67.14  ?  266 LEU A CG    1 
ATOM   1946 C CD1   . LEU A 1 260 ? 28.669 11.842  34.191  1.00 63.43  ?  266 LEU A CD1   1 
ATOM   1947 C CD2   . LEU A 1 260 ? 29.942 10.904  36.110  1.00 71.78  ?  266 LEU A CD2   1 
ATOM   1948 N N     . ARG A 1 261 ? 25.263 9.243   38.243  1.00 78.30  ?  267 ARG A N     1 
ATOM   1949 C CA    . ARG A 1 261 ? 24.173 9.586   39.149  1.00 83.57  ?  267 ARG A CA    1 
ATOM   1950 C C     . ARG A 1 261 ? 24.311 11.037  39.612  1.00 79.81  ?  267 ARG A C     1 
ATOM   1951 O O     . ARG A 1 261 ? 25.420 11.533  39.843  1.00 75.94  ?  267 ARG A O     1 
ATOM   1952 C CB    . ARG A 1 261 ? 24.157 8.654   40.361  1.00 84.65  ?  267 ARG A CB    1 
ATOM   1953 C CG    . ARG A 1 261 ? 24.805 7.293   40.156  1.00 87.78  ?  267 ARG A CG    1 
ATOM   1954 C CD    . ARG A 1 261 ? 24.967 6.563   41.507  1.00 96.70  ?  267 ARG A CD    1 
ATOM   1955 N NE    . ARG A 1 261 ? 26.309 6.025   41.713  1.00 93.05  ?  267 ARG A NE    1 
ATOM   1956 C CZ    . ARG A 1 261 ? 26.600 4.733   41.743  1.00 100.36 ?  267 ARG A CZ    1 
ATOM   1957 N NH1   . ARG A 1 261 ? 25.658 3.810   41.626  1.00 108.17 ?  267 ARG A NH1   1 
ATOM   1958 N NH2   . ARG A 1 261 ? 27.868 4.356   41.893  1.00 104.95 ?  267 ARG A NH2   1 
ATOM   1959 N N     . VAL A 1 262 ? 23.174 11.727  39.737  1.00 78.09  ?  268 VAL A N     1 
ATOM   1960 C CA    . VAL A 1 262 ? 23.154 13.140  40.091  1.00 81.05  ?  268 VAL A CA    1 
ATOM   1961 C C     . VAL A 1 262 ? 21.931 13.444  40.950  1.00 79.72  ?  268 VAL A C     1 
ATOM   1962 O O     . VAL A 1 262 ? 20.923 12.738  40.904  1.00 77.71  ?  268 VAL A O     1 
ATOM   1963 C CB    . VAL A 1 262 ? 23.150 14.035  38.831  1.00 78.38  ?  268 VAL A CB    1 
ATOM   1964 C CG1   . VAL A 1 262 ? 24.507 14.027  38.151  1.00 72.86  ?  268 VAL A CG1   1 
ATOM   1965 C CG2   . VAL A 1 262 ? 22.064 13.573  37.864  1.00 74.07  ?  268 VAL A CG2   1 
ATOM   1966 N N     . ASN A 1 263 ? 22.011 14.533  41.723  1.00 82.93  ?  269 ASN A N     1 
ATOM   1967 C CA    . ASN A 1 263 ? 20.852 14.989  42.492  1.00 82.35  ?  269 ASN A CA    1 
ATOM   1968 C C     . ASN A 1 263 ? 19.898 15.761  41.592  1.00 85.57  ?  269 ASN A C     1 
ATOM   1969 O O     . ASN A 1 263 ? 20.008 15.688  40.366  1.00 77.32  ?  269 ASN A O     1 
ATOM   1970 C CB    . ASN A 1 263 ? 21.270 15.853  43.678  1.00 84.63  ?  269 ASN A CB    1 
ATOM   1971 C CG    . ASN A 1 263 ? 22.424 16.760  43.354  1.00 85.11  ?  269 ASN A CG    1 
ATOM   1972 O OD1   . ASN A 1 263 ? 22.270 17.758  42.648  1.00 85.26  ?  269 ASN A OD1   1 
ATOM   1973 N ND2   . ASN A 1 263 ? 23.602 16.417  43.870  1.00 87.38  ?  269 ASN A ND2   1 
ATOM   1974 N N     . GLU A 1 264 ? 18.959 16.500  42.176  1.00 85.95  ?  270 GLU A N     1 
ATOM   1975 C CA    . GLU A 1 264 ? 18.035 17.292  41.370  1.00 82.60  ?  270 GLU A CA    1 
ATOM   1976 C C     . GLU A 1 264 ? 18.654 18.594  40.882  1.00 83.55  ?  270 GLU A C     1 
ATOM   1977 O O     . GLU A 1 264 ? 18.009 19.337  40.132  1.00 79.34  ?  270 GLU A O     1 
ATOM   1978 C CB    . GLU A 1 264 ? 16.761 17.578  42.162  1.00 88.64  ?  270 GLU A CB    1 
ATOM   1979 C CG    . GLU A 1 264 ? 17.013 17.848  43.653  1.00 94.22  ?  270 GLU A CG    1 
ATOM   1980 C CD    . GLU A 1 264 ? 15.745 18.198  44.409  1.00 97.92  ?  270 GLU A CD    1 
ATOM   1981 O OE1   . GLU A 1 264 ? 14.641 17.913  43.895  1.00 101.90 ?  270 GLU A OE1   1 
ATOM   1982 O OE2   . GLU A 1 264 ? 15.853 18.759  45.519  1.00 102.09 -1 270 GLU A OE2   1 
ATOM   1983 N N     . HIS A 1 265 ? 19.888 18.881  41.285  1.00 84.39  ?  271 HIS A N     1 
ATOM   1984 C CA    . HIS A 1 265 ? 20.642 20.018  40.781  1.00 82.57  ?  271 HIS A CA    1 
ATOM   1985 C C     . HIS A 1 265 ? 21.687 19.602  39.754  1.00 74.14  ?  271 HIS A C     1 
ATOM   1986 O O     . HIS A 1 265 ? 22.561 20.403  39.409  1.00 67.06  ?  271 HIS A O     1 
ATOM   1987 C CB    . HIS A 1 265 ? 21.299 20.754  41.947  1.00 80.46  ?  271 HIS A CB    1 
ATOM   1988 C CG    . HIS A 1 265 ? 20.401 20.899  43.131  1.00 83.60  ?  271 HIS A CG    1 
ATOM   1989 N ND1   . HIS A 1 265 ? 19.162 21.496  43.053  1.00 85.59  ?  271 HIS A ND1   1 
ATOM   1990 C CD2   . HIS A 1 265 ? 20.551 20.509  44.418  1.00 81.45  ?  271 HIS A CD2   1 
ATOM   1991 C CE1   . HIS A 1 265 ? 18.589 21.472  44.243  1.00 83.00  ?  271 HIS A CE1   1 
ATOM   1992 N NE2   . HIS A 1 265 ? 19.412 20.881  45.088  1.00 83.07  ?  271 HIS A NE2   1 
ATOM   1993 N N     . LEU A 1 266 ? 21.619 18.356  39.289  1.00 75.86  ?  272 LEU A N     1 
ATOM   1994 C CA    . LEU A 1 266 ? 22.527 17.789  38.292  1.00 72.26  ?  272 LEU A CA    1 
ATOM   1995 C C     . LEU A 1 266 ? 23.968 17.753  38.783  1.00 71.50  ?  272 LEU A C     1 
ATOM   1996 O O     . LEU A 1 266 ? 24.904 17.782  37.988  1.00 69.03  ?  272 LEU A O     1 
ATOM   1997 C CB    . LEU A 1 266 ? 22.421 18.530  36.963  1.00 65.43  ?  272 LEU A CB    1 
ATOM   1998 C CG    . LEU A 1 266 ? 21.054 18.373  36.295  1.00 69.96  ?  272 LEU A CG    1 
ATOM   1999 C CD1   . LEU A 1 266 ? 20.904 19.339  35.133  1.00 66.08  ?  272 LEU A CD1   1 
ATOM   2000 C CD2   . LEU A 1 266 ? 20.868 16.947  35.802  1.00 74.60  ?  272 LEU A CD2   1 
ATOM   2001 N N     . GLN A 1 267 ? 24.164 17.651  40.092  1.00 74.84  ?  273 GLN A N     1 
ATOM   2002 C CA    . GLN A 1 267 ? 25.501 17.518  40.642  1.00 74.42  ?  273 GLN A CA    1 
ATOM   2003 C C     . GLN A 1 267 ? 25.869 16.054  40.725  1.00 73.54  ?  273 GLN A C     1 
ATOM   2004 O O     . GLN A 1 267 ? 25.055 15.222  41.121  1.00 75.03  ?  273 GLN A O     1 
ATOM   2005 C CB    . GLN A 1 267 ? 25.592 18.143  42.028  1.00 73.03  ?  273 GLN A CB    1 
ATOM   2006 C CG    . GLN A 1 267 ? 25.196 19.589  42.054  1.00 74.26  ?  273 GLN A CG    1 
ATOM   2007 C CD    . GLN A 1 267 ? 25.445 20.210  43.392  1.00 79.33  ?  273 GLN A CD    1 
ATOM   2008 O OE1   . GLN A 1 267 ? 26.587 20.488  43.759  1.00 78.90  ?  273 GLN A OE1   1 
ATOM   2009 N NE2   . GLN A 1 267 ? 24.379 20.417  44.147  1.00 84.77  ?  273 GLN A NE2   1 
ATOM   2010 N N     . VAL A 1 268 ? 27.108 15.746  40.361  1.00 72.66  ?  274 VAL A N     1 
ATOM   2011 C CA    . VAL A 1 268 ? 27.551 14.361  40.382  1.00 77.62  ?  274 VAL A CA    1 
ATOM   2012 C C     . VAL A 1 268 ? 27.799 13.958  41.829  1.00 81.14  ?  274 VAL A C     1 
ATOM   2013 O O     . VAL A 1 268 ? 28.612 14.580  42.526  1.00 82.03  ?  274 VAL A O     1 
ATOM   2014 C CB    . VAL A 1 268 ? 28.798 14.165  39.507  1.00 77.05  ?  274 VAL A CB    1 
ATOM   2015 C CG1   . VAL A 1 268 ? 29.315 12.731  39.622  1.00 76.51  ?  274 VAL A CG1   1 
ATOM   2016 C CG2   . VAL A 1 268 ? 28.472 14.495  38.055  1.00 68.59  ?  274 VAL A CG2   1 
ATOM   2017 N N     . GLU A 1 269 ? 27.069 12.938  42.284  1.00 83.24  ?  275 GLU A N     1 
ATOM   2018 C CA    . GLU A 1 269 ? 27.206 12.375  43.621  1.00 88.58  ?  275 GLU A CA    1 
ATOM   2019 C C     . GLU A 1 269 ? 28.662 12.317  44.053  1.00 91.53  ?  275 GLU A C     1 
ATOM   2020 O O     . GLU A 1 269 ? 29.525 11.846  43.306  1.00 82.94  ?  275 GLU A O     1 
ATOM   2021 C CB    . GLU A 1 269 ? 26.612 10.972  43.652  1.00 89.27  ?  275 GLU A CB    1 
ATOM   2022 C CG    . GLU A 1 269 ? 25.114 10.905  43.812  1.00 91.31  ?  275 GLU A CG    1 
ATOM   2023 C CD    . GLU A 1 269 ? 24.649 9.482   44.117  1.00 95.63  ?  275 GLU A CD    1 
ATOM   2024 O OE1   . GLU A 1 269 ? 25.506 8.568   44.172  1.00 92.31  ?  275 GLU A OE1   1 
ATOM   2025 O OE2   . GLU A 1 269 ? 23.433 9.274   44.308  1.00 96.95  -1 275 GLU A OE2   1 
ATOM   2026 N N     . GLY A 1 270 ? 28.926 12.804  45.267  1.00 83.60  ?  276 GLY A N     1 
ATOM   2027 C CA    . GLY A 1 270 ? 30.272 12.867  45.785  1.00 85.21  ?  276 GLY A CA    1 
ATOM   2028 C C     . GLY A 1 270 ? 31.027 14.120  45.423  1.00 89.50  ?  276 GLY A C     1 
ATOM   2029 O O     . GLY A 1 270 ? 32.171 14.284  45.869  1.00 91.04  ?  276 GLY A O     1 
ATOM   2030 N N     . HIS A 1 271 ? 30.430 15.004  44.626  1.00 87.85  ?  277 HIS A N     1 
ATOM   2031 C CA    . HIS A 1 271 ? 31.054 16.261  44.244  1.00 84.50  ?  277 HIS A CA    1 
ATOM   2032 C C     . HIS A 1 271 ? 30.021 17.373  44.299  1.00 82.33  ?  277 HIS A C     1 
ATOM   2033 O O     . HIS A 1 271 ? 28.829 17.149  44.073  1.00 83.92  ?  277 HIS A O     1 
ATOM   2034 C CB    . HIS A 1 271 ? 31.674 16.174  42.853  1.00 79.88  ?  277 HIS A CB    1 
ATOM   2035 C CG    . HIS A 1 271 ? 32.650 15.055  42.718  1.00 81.07  ?  277 HIS A CG    1 
ATOM   2036 N ND1   . HIS A 1 271 ? 32.258 13.737  42.649  1.00 85.12  ?  277 HIS A ND1   1 
ATOM   2037 C CD2   . HIS A 1 271 ? 34.002 15.050  42.679  1.00 82.44  ?  277 HIS A CD2   1 
ATOM   2038 C CE1   . HIS A 1 271 ? 33.326 12.967  42.552  1.00 87.01  ?  277 HIS A CE1   1 
ATOM   2039 N NE2   . HIS A 1 271 ? 34.398 13.739  42.571  1.00 88.48  ?  277 HIS A NE2   1 
ATOM   2040 N N     . SER A 1 272 ? 30.491 18.572  44.642  1.00 76.02  ?  278 SER A N     1 
ATOM   2041 C CA    . SER A 1 272 ? 29.660 19.764  44.594  1.00 77.60  ?  278 SER A CA    1 
ATOM   2042 C C     . SER A 1 272 ? 29.927 20.628  43.369  1.00 71.57  ?  278 SER A C     1 
ATOM   2043 O O     . SER A 1 272 ? 29.051 21.411  42.985  1.00 70.29  ?  278 SER A O     1 
ATOM   2044 C CB    . SER A 1 272 ? 29.878 20.608  45.850  1.00 78.59  ?  278 SER A CB    1 
ATOM   2045 O OG    . SER A 1 272 ? 31.221 21.050  45.906  1.00 80.99  ?  278 SER A OG    1 
ATOM   2046 N N     . ASN A 1 273 ? 31.100 20.493  42.746  1.00 66.65  ?  279 ASN A N     1 
ATOM   2047 C CA    . ASN A 1 273 ? 31.521 21.326  41.627  1.00 63.41  ?  279 ASN A CA    1 
ATOM   2048 C C     . ASN A 1 273 ? 31.553 20.581  40.293  1.00 64.96  ?  279 ASN A C     1 
ATOM   2049 O O     . ASN A 1 273 ? 32.134 21.087  39.325  1.00 62.20  ?  279 ASN A O     1 
ATOM   2050 C CB    . ASN A 1 273 ? 32.907 21.894  41.909  1.00 62.12  ?  279 ASN A CB    1 
ATOM   2051 C CG    . ASN A 1 273 ? 33.962 20.825  41.903  1.00 63.77  ?  279 ASN A CG    1 
ATOM   2052 O OD1   . ASN A 1 273 ? 33.685 19.672  42.241  1.00 66.12  ?  279 ASN A OD1   1 
ATOM   2053 N ND2   . ASN A 1 273 ? 35.178 21.188  41.500  1.00 65.33  ?  279 ASN A ND2   1 
ATOM   2054 N N     . VAL A 1 274 ? 30.974 19.386  40.221  1.00 69.78  ?  280 VAL A N     1 
ATOM   2055 C CA    . VAL A 1 274 ? 30.989 18.570  39.013  1.00 63.15  ?  280 VAL A CA    1 
ATOM   2056 C C     . VAL A 1 274 ? 29.554 18.282  38.615  1.00 63.75  ?  280 VAL A C     1 
ATOM   2057 O O     . VAL A 1 274 ? 28.787 17.704  39.397  1.00 66.27  ?  280 VAL A O     1 
ATOM   2058 C CB    . VAL A 1 274 ? 31.773 17.269  39.210  1.00 67.23  ?  280 VAL A CB    1 
ATOM   2059 C CG1   . VAL A 1 274 ? 31.505 16.331  38.062  1.00 68.68  ?  280 VAL A CG1   1 
ATOM   2060 C CG2   . VAL A 1 274 ? 33.258 17.583  39.314  1.00 64.93  ?  280 VAL A CG2   1 
ATOM   2061 N N     . TYR A 1 275 ? 29.194 18.681  37.399  1.00 64.14  ?  281 TYR A N     1 
ATOM   2062 C CA    . TYR A 1 275 ? 27.847 18.514  36.883  1.00 64.76  ?  281 TYR A CA    1 
ATOM   2063 C C     . TYR A 1 275 ? 27.838 17.540  35.711  1.00 60.33  ?  281 TYR A C     1 
ATOM   2064 O O     . TYR A 1 275 ? 28.854 17.305  35.054  1.00 58.10  ?  281 TYR A O     1 
ATOM   2065 C CB    . TYR A 1 275 ? 27.265 19.865  36.471  1.00 58.77  ?  281 TYR A CB    1 
ATOM   2066 C CG    . TYR A 1 275 ? 27.066 20.818  37.628  1.00 61.66  ?  281 TYR A CG    1 
ATOM   2067 C CD1   . TYR A 1 275 ? 28.149 21.468  38.218  1.00 64.82  ?  281 TYR A CD1   1 
ATOM   2068 C CD2   . TYR A 1 275 ? 25.799 21.080  38.124  1.00 62.97  ?  281 TYR A CD2   1 
ATOM   2069 C CE1   . TYR A 1 275 ? 27.979 22.337  39.273  1.00 57.45  ?  281 TYR A CE1   1 
ATOM   2070 C CE2   . TYR A 1 275 ? 25.616 21.956  39.183  1.00 65.92  ?  281 TYR A CE2   1 
ATOM   2071 C CZ    . TYR A 1 275 ? 26.710 22.581  39.746  1.00 62.53  ?  281 TYR A CZ    1 
ATOM   2072 O OH    . TYR A 1 275 ? 26.523 23.450  40.793  1.00 66.62  ?  281 TYR A OH    1 
ATOM   2073 N N     . ALA A 1 276 ? 26.677 16.941  35.485  1.00 61.82  ?  282 ALA A N     1 
ATOM   2074 C CA    . ALA A 1 276 ? 26.453 16.086  34.331  1.00 58.59  ?  282 ALA A CA    1 
ATOM   2075 C C     . ALA A 1 276 ? 25.116 16.457  33.715  1.00 62.27  ?  282 ALA A C     1 
ATOM   2076 O O     . ALA A 1 276 ? 24.144 16.703  34.441  1.00 58.00  ?  282 ALA A O     1 
ATOM   2077 C CB    . ALA A 1 276 ? 26.470 14.607  34.708  1.00 56.81  ?  282 ALA A CB    1 
ATOM   2078 N N     . ILE A 1 277 ? 25.070 16.505  32.376  1.00 54.65  ?  283 ILE A N     1 
ATOM   2079 C CA    . ILE A 1 277 ? 23.912 17.022  31.663  1.00 52.92  ?  283 ILE A CA    1 
ATOM   2080 C C     . ILE A 1 277 ? 23.645 16.185  30.419  1.00 58.13  ?  283 ILE A C     1 
ATOM   2081 O O     . ILE A 1 277 ? 24.519 15.487  29.902  1.00 59.91  ?  283 ILE A O     1 
ATOM   2082 C CB    . ILE A 1 277 ? 24.088 18.503  31.265  1.00 52.96  ?  283 ILE A CB    1 
ATOM   2083 C CG1   . ILE A 1 277 ? 25.239 18.660  30.281  1.00 48.68  ?  283 ILE A CG1   1 
ATOM   2084 C CG2   . ILE A 1 277 ? 24.313 19.384  32.494  1.00 51.13  ?  283 ILE A CG2   1 
ATOM   2085 C CD1   . ILE A 1 277 ? 25.355 20.065  29.713  1.00 48.24  ?  283 ILE A CD1   1 
ATOM   2086 N N     . GLY A 1 278 ? 22.408 16.270  29.944  1.00 54.96  ?  284 GLY A N     1 
ATOM   2087 C CA    . GLY A 1 278 ? 22.031 15.566  28.746  1.00 58.22  ?  284 GLY A CA    1 
ATOM   2088 C C     . GLY A 1 278 ? 22.110 14.068  28.929  1.00 60.21  ?  284 GLY A C     1 
ATOM   2089 O O     . GLY A 1 278 ? 21.624 13.515  29.917  1.00 63.00  ?  284 GLY A O     1 
ATOM   2090 N N     . ASP A 1 279 ? 22.740 13.398  27.963  1.00 59.70  ?  285 ASP A N     1 
ATOM   2091 C CA    . ASP A 1 279 ? 22.639 11.944  27.890  1.00 61.62  ?  285 ASP A CA    1 
ATOM   2092 C C     . ASP A 1 279 ? 23.457 11.239  28.958  1.00 61.41  ?  285 ASP A C     1 
ATOM   2093 O O     . ASP A 1 279 ? 23.098 10.134  29.365  1.00 62.62  ?  285 ASP A O     1 
ATOM   2094 C CB    . ASP A 1 279 ? 23.067 11.442  26.509  1.00 59.15  ?  285 ASP A CB    1 
ATOM   2095 C CG    . ASP A 1 279 ? 21.992 11.668  25.448  1.00 61.68  ?  285 ASP A CG    1 
ATOM   2096 O OD1   . ASP A 1 279 ? 20.973 12.318  25.781  1.00 63.74  ?  285 ASP A OD1   1 
ATOM   2097 O OD2   . ASP A 1 279 ? 22.159 11.189  24.295  1.00 58.89  -1 285 ASP A OD2   1 
ATOM   2098 N N     . CYS A 1 280 ? 24.541 11.841  29.424  1.00 61.27  ?  286 CYS A N     1 
ATOM   2099 C CA    . CYS A 1 280 ? 25.399 11.145  30.369  1.00 65.09  ?  286 CYS A CA    1 
ATOM   2100 C C     . CYS A 1 280 ? 24.918 11.266  31.822  1.00 68.13  ?  286 CYS A C     1 
ATOM   2101 O O     . CYS A 1 280 ? 25.584 10.747  32.719  1.00 68.50  ?  286 CYS A O     1 
ATOM   2102 C CB    . CYS A 1 280 ? 26.834 11.655  30.239  1.00 61.52  ?  286 CYS A CB    1 
ATOM   2103 S SG    . CYS A 1 280 ? 26.998 13.358  30.693  1.00 56.43  ?  286 CYS A SG    1 
ATOM   2104 N N     . ALA A 1 281 ? 23.779 11.910  32.062  1.00 64.62  ?  287 ALA A N     1 
ATOM   2105 C CA    . ALA A 1 281 ? 23.233 12.090  33.396  1.00 69.24  ?  287 ALA A CA    1 
ATOM   2106 C C     . ALA A 1 281 ? 22.196 11.010  33.670  1.00 77.85  ?  287 ALA A C     1 
ATOM   2107 O O     . ALA A 1 281 ? 21.321 10.771  32.828  1.00 79.40  ?  287 ALA A O     1 
ATOM   2108 C CB    . ALA A 1 281 ? 22.595 13.472  33.525  1.00 69.07  ?  287 ALA A CB    1 
ATOM   2109 N N     . ASP A 1 282 ? 22.286 10.372  34.848  1.00 76.67  ?  288 ASP A N     1 
ATOM   2110 C CA    . ASP A 1 282 ? 21.372 9.294   35.239  1.00 78.38  ?  288 ASP A CA    1 
ATOM   2111 C C     . ASP A 1 282 ? 20.066 9.923   35.690  1.00 85.12  ?  288 ASP A C     1 
ATOM   2112 O O     . ASP A 1 282 ? 19.871 10.237  36.863  1.00 92.00  ?  288 ASP A O     1 
ATOM   2113 C CB    . ASP A 1 282 ? 21.975 8.423   36.336  1.00 80.68  ?  288 ASP A CB    1 
ATOM   2114 N N     . VAL A 1 283 ? 19.147 10.095  34.745  1.00 88.54  ?  289 VAL A N     1 
ATOM   2115 C CA    . VAL A 1 283 ? 17.932 10.859  34.977  1.00 94.69  ?  289 VAL A CA    1 
ATOM   2116 C C     . VAL A 1 283 ? 16.666 10.055  34.747  1.00 105.90 ?  289 VAL A C     1 
ATOM   2117 O O     . VAL A 1 283 ? 15.571 10.581  34.979  1.00 113.34 ?  289 VAL A O     1 
ATOM   2118 C CB    . VAL A 1 283 ? 17.903 12.131  34.112  1.00 94.57  ?  289 VAL A CB    1 
ATOM   2119 C CG1   . VAL A 1 283 ? 18.977 13.088  34.569  1.00 90.30  ?  289 VAL A CG1   1 
ATOM   2120 C CG2   . VAL A 1 283 ? 18.101 11.762  32.651  1.00 93.32  ?  289 VAL A CG2   1 
ATOM   2121 N N     . ARG A 1 284 ? 16.770 8.803   34.293  1.00 105.13 ?  290 ARG A N     1 
ATOM   2122 C CA    . ARG A 1 284 ? 15.597 7.969   34.008  1.00 106.34 ?  290 ARG A CA    1 
ATOM   2123 C C     . ARG A 1 284 ? 14.655 8.644   33.005  1.00 109.53 ?  290 ARG A C     1 
ATOM   2124 O O     . ARG A 1 284 ? 13.448 8.385   32.988  1.00 113.64 ?  290 ARG A O     1 
ATOM   2125 C CB    . ARG A 1 284 ? 14.847 7.599   35.295  1.00 102.65 ?  290 ARG A CB    1 
ATOM   2126 N N     . THR A 1 285 ? 15.200 9.521   32.175  1.00 103.51 ?  291 THR A N     1 
ATOM   2127 C CA    . THR A 1 285 ? 14.509 10.156  31.066  1.00 99.03  ?  291 THR A CA    1 
ATOM   2128 C C     . THR A 1 285 ? 14.752 9.355   29.795  1.00 96.86  ?  291 THR A C     1 
ATOM   2129 O O     . THR A 1 285 ? 15.506 8.377   29.798  1.00 96.58  ?  291 THR A O     1 
ATOM   2130 C CB    . THR A 1 285 ? 15.001 11.601  30.911  1.00 95.62  ?  291 THR A CB    1 
ATOM   2131 N N     . PRO A 1 286 ? 14.108 9.717   28.680  1.00 100.36 ?  292 PRO A N     1 
ATOM   2132 C CA    . PRO A 1 286 ? 14.401 9.044   27.405  1.00 94.40  ?  292 PRO A CA    1 
ATOM   2133 C C     . PRO A 1 286 ? 15.605 9.596   26.654  1.00 81.78  ?  292 PRO A C     1 
ATOM   2134 O O     . PRO A 1 286 ? 15.891 9.097   25.561  1.00 81.18  ?  292 PRO A O     1 
ATOM   2135 C CB    . PRO A 1 286 ? 13.123 9.291   26.601  1.00 92.16  ?  292 PRO A CB    1 
ATOM   2136 C CG    . PRO A 1 286 ? 12.762 10.667  27.034  1.00 89.87  ?  292 PRO A CG    1 
ATOM   2137 C CD    . PRO A 1 286 ? 12.952 10.621  28.532  1.00 97.94  ?  292 PRO A CD    1 
ATOM   2138 N N     . LYS A 1 287 ? 16.292 10.608  27.191  1.00 75.14  ?  293 LYS A N     1 
ATOM   2139 C CA    . LYS A 1 287 ? 17.495 11.184  26.597  1.00 70.73  ?  293 LYS A CA    1 
ATOM   2140 C C     . LYS A 1 287 ? 17.172 11.969  25.328  1.00 59.91  ?  293 LYS A C     1 
ATOM   2141 O O     . LYS A 1 287 ? 17.160 11.412  24.238  1.00 58.01  ?  293 LYS A O     1 
ATOM   2142 C CB    . LYS A 1 287 ? 18.545 10.098  26.316  1.00 68.48  ?  293 LYS A CB    1 
ATOM   2143 C CG    . LYS A 1 287 ? 19.020 9.358   27.551  1.00 73.50  ?  293 LYS A CG    1 
ATOM   2144 C CD    . LYS A 1 287 ? 19.119 10.308  28.749  1.00 78.88  ?  293 LYS A CD    1 
ATOM   2145 C CE    . LYS A 1 287 ? 19.330 9.563   30.061  1.00 76.65  ?  293 LYS A CE    1 
ATOM   2146 N NZ    . LYS A 1 287 ? 20.660 8.905   30.103  1.00 73.15  ?  293 LYS A NZ    1 
ATOM   2147 N N     . MET A 1 288 ? 16.928 13.267  25.466  1.00 61.95  ?  294 MET A N     1 
ATOM   2148 C CA    . MET A 1 288 ? 16.539 14.141  24.374  1.00 54.72  ?  294 MET A CA    1 
ATOM   2149 C C     . MET A 1 288 ? 17.507 15.307  24.285  1.00 54.51  ?  294 MET A C     1 
ATOM   2150 O O     . MET A 1 288 ? 18.052 15.759  25.296  1.00 55.44  ?  294 MET A O     1 
ATOM   2151 C CB    . MET A 1 288 ? 15.132 14.709  24.574  1.00 57.80  ?  294 MET A CB    1 
ATOM   2152 C CG    . MET A 1 288 ? 14.048 13.686  24.745  1.00 59.76  ?  294 MET A CG    1 
ATOM   2153 S SD    . MET A 1 288 ? 13.824 12.741  23.256  1.00 68.55  ?  294 MET A SD    1 
ATOM   2154 C CE    . MET A 1 288 ? 12.922 13.907  22.234  1.00 57.31  ?  294 MET A CE    1 
ATOM   2155 N N     . ALA A 1 289 ? 17.677 15.815  23.061  1.00 51.16  ?  295 ALA A N     1 
ATOM   2156 C CA    . ALA A 1 289 ? 18.500 16.996  22.847  1.00 45.85  ?  295 ALA A CA    1 
ATOM   2157 C C     . ALA A 1 289 ? 17.937 18.203  23.572  1.00 48.53  ?  295 ALA A C     1 
ATOM   2158 O O     . ALA A 1 289 ? 18.695 18.988  24.143  1.00 51.41  ?  295 ALA A O     1 
ATOM   2159 C CB    . ALA A 1 289 ? 18.621 17.307  21.357  1.00 50.26  ?  295 ALA A CB    1 
ATOM   2160 N N     . TYR A 1 290 ? 16.619 18.395  23.544  1.00 49.78  ?  296 TYR A N     1 
ATOM   2161 C CA    . TYR A 1 290 ? 16.079 19.584  24.187  1.00 46.52  ?  296 TYR A CA    1 
ATOM   2162 C C     . TYR A 1 290 ? 16.313 19.527  25.691  1.00 49.93  ?  296 TYR A C     1 
ATOM   2163 O O     . TYR A 1 290 ? 16.664 20.538  26.315  1.00 51.60  ?  296 TYR A O     1 
ATOM   2164 C CB    . TYR A 1 290 ? 14.603 19.758  23.836  1.00 48.18  ?  296 TYR A CB    1 
ATOM   2165 C CG    . TYR A 1 290 ? 13.616 18.911  24.611  1.00 54.96  ?  296 TYR A CG    1 
ATOM   2166 C CD1   . TYR A 1 290 ? 13.042 19.371  25.793  1.00 52.11  ?  296 TYR A CD1   1 
ATOM   2167 C CD2   . TYR A 1 290 ? 13.228 17.665  24.143  1.00 53.54  ?  296 TYR A CD2   1 
ATOM   2168 C CE1   . TYR A 1 290 ? 12.129 18.605  26.488  1.00 51.68  ?  296 TYR A CE1   1 
ATOM   2169 C CE2   . TYR A 1 290 ? 12.315 16.896  24.834  1.00 55.24  ?  296 TYR A CE2   1 
ATOM   2170 C CZ    . TYR A 1 290 ? 11.765 17.370  26.003  1.00 55.00  ?  296 TYR A CZ    1 
ATOM   2171 O OH    . TYR A 1 290 ? 10.853 16.590  26.674  1.00 58.44  ?  296 TYR A OH    1 
ATOM   2172 N N     . LEU A 1 291 ? 16.200 18.336  26.275  1.00 53.46  ?  297 LEU A N     1 
ATOM   2173 C CA    . LEU A 1 291 ? 16.525 18.163  27.682  1.00 50.69  ?  297 LEU A CA    1 
ATOM   2174 C C     . LEU A 1 291 ? 17.979 18.501  27.960  1.00 54.17  ?  297 LEU A C     1 
ATOM   2175 O O     . LEU A 1 291 ? 18.297 19.091  28.998  1.00 52.63  ?  297 LEU A O     1 
ATOM   2176 C CB    . LEU A 1 291 ? 16.226 16.732  28.103  1.00 54.34  ?  297 LEU A CB    1 
ATOM   2177 C CG    . LEU A 1 291 ? 14.733 16.419  28.181  1.00 59.18  ?  297 LEU A CG    1 
ATOM   2178 C CD1   . LEU A 1 291 ? 14.502 14.955  28.552  1.00 61.18  ?  297 LEU A CD1   1 
ATOM   2179 C CD2   . LEU A 1 291 ? 14.055 17.376  29.165  1.00 56.57  ?  297 LEU A CD2   1 
ATOM   2180 N N     . ALA A 1 292 ? 18.879 18.123  27.049  1.00 51.96  ?  298 ALA A N     1 
ATOM   2181 C CA    . ALA A 1 292 ? 20.289 18.415  27.258  1.00 49.07  ?  298 ALA A CA    1 
ATOM   2182 C C     . ALA A 1 292 ? 20.507 19.916  27.424  1.00 52.90  ?  298 ALA A C     1 
ATOM   2183 O O     . ALA A 1 292 ? 21.307 20.345  28.265  1.00 49.74  ?  298 ALA A O     1 
ATOM   2184 C CB    . ALA A 1 292 ? 21.109 17.852  26.100  1.00 44.35  ?  298 ALA A CB    1 
ATOM   2185 N N     . GLY A 1 293 ? 19.761 20.727  26.668  1.00 48.51  ?  299 GLY A N     1 
ATOM   2186 C CA    . GLY A 1 293 ? 19.856 22.170  26.825  1.00 49.11  ?  299 GLY A CA    1 
ATOM   2187 C C     . GLY A 1 293 ? 19.310 22.660  28.156  1.00 52.01  ?  299 GLY A C     1 
ATOM   2188 O O     . GLY A 1 293 ? 19.955 23.454  28.838  1.00 58.47  ?  299 GLY A O     1 
ATOM   2189 N N     . LEU A 1 294 ? 18.111 22.205  28.537  1.00 52.88  ?  300 LEU A N     1 
ATOM   2190 C CA    . LEU A 1 294 ? 17.538 22.579  29.824  1.00 53.03  ?  300 LEU A CA    1 
ATOM   2191 C C     . LEU A 1 294 ? 18.485 22.240  30.965  1.00 55.53  ?  300 LEU A C     1 
ATOM   2192 O O     . LEU A 1 294 ? 18.744 23.071  31.838  1.00 57.96  ?  300 LEU A O     1 
ATOM   2193 C CB    . LEU A 1 294 ? 16.194 21.882  30.030  1.00 56.18  ?  300 LEU A CB    1 
ATOM   2194 C CG    . LEU A 1 294 ? 15.029 22.222  29.089  1.00 60.67  ?  300 LEU A CG    1 
ATOM   2195 C CD1   . LEU A 1 294 ? 13.734 21.538  29.539  1.00 61.81  ?  300 LEU A CD1   1 
ATOM   2196 C CD2   . LEU A 1 294 ? 14.817 23.741  28.946  1.00 60.30  ?  300 LEU A CD2   1 
ATOM   2197 N N     . HIS A 1 295 ? 19.013 21.016  30.967  1.00 57.03  ?  301 HIS A N     1 
ATOM   2198 C CA    . HIS A 1 295 ? 20.050 20.631  31.917  1.00 56.67  ?  301 HIS A CA    1 
ATOM   2199 C C     . HIS A 1 295 ? 21.201 21.627  31.931  1.00 55.07  ?  301 HIS A C     1 
ATOM   2200 O O     . HIS A 1 295 ? 21.825 21.854  32.970  1.00 57.82  ?  301 HIS A O     1 
ATOM   2201 C CB    . HIS A 1 295 ? 20.590 19.242  31.568  1.00 54.25  ?  301 HIS A CB    1 
ATOM   2202 C CG    . HIS A 1 295 ? 19.575 18.144  31.666  1.00 61.70  ?  301 HIS A CG    1 
ATOM   2203 N ND1   . HIS A 1 295 ? 19.847 16.845  31.283  1.00 61.94  ?  301 HIS A ND1   1 
ATOM   2204 C CD2   . HIS A 1 295 ? 18.296 18.146  32.115  1.00 65.20  ?  301 HIS A CD2   1 
ATOM   2205 C CE1   . HIS A 1 295 ? 18.777 16.097  31.486  1.00 64.91  ?  301 HIS A CE1   1 
ATOM   2206 N NE2   . HIS A 1 295 ? 17.820 16.863  31.984  1.00 70.11  ?  301 HIS A NE2   1 
ATOM   2207 N N     . ALA A 1 296 ? 21.507 22.222  30.787  1.00 56.67  ?  302 ALA A N     1 
ATOM   2208 C CA    . ALA A 1 296 ? 22.682 23.072  30.714  1.00 55.44  ?  302 ALA A CA    1 
ATOM   2209 C C     . ALA A 1 296 ? 22.431 24.400  31.400  1.00 56.71  ?  302 ALA A C     1 
ATOM   2210 O O     . ALA A 1 296 ? 23.297 24.902  32.118  1.00 57.53  ?  302 ALA A O     1 
ATOM   2211 C CB    . ALA A 1 296 ? 23.090 23.275  29.258  1.00 49.15  ?  302 ALA A CB    1 
ATOM   2212 N N     . ASN A 1 297 ? 21.252 24.985  31.192  1.00 58.25  ?  303 ASN A N     1 
ATOM   2213 C CA    . ASN A 1 297 ? 20.904 26.196  31.925  1.00 58.19  ?  303 ASN A CA    1 
ATOM   2214 C C     . ASN A 1 297 ? 20.857 25.935  33.421  1.00 59.14  ?  303 ASN A C     1 
ATOM   2215 O O     . ASN A 1 297 ? 21.281 26.782  34.212  1.00 58.98  ?  303 ASN A O     1 
ATOM   2216 C CB    . ASN A 1 297 ? 19.566 26.733  31.440  1.00 59.11  ?  303 ASN A CB    1 
ATOM   2217 C CG    . ASN A 1 297 ? 19.679 27.395  30.104  1.00 70.87  ?  303 ASN A CG    1 
ATOM   2218 O OD1   . ASN A 1 297 ? 20.772 27.475  29.529  1.00 68.96  ?  303 ASN A OD1   1 
ATOM   2219 N ND2   . ASN A 1 297 ? 18.550 27.876  29.586  1.00 77.28  ?  303 ASN A ND2   1 
ATOM   2220 N N     . ILE A 1 298 ? 20.335 24.769  33.815  1.00 57.49  ?  304 ILE A N     1 
ATOM   2221 C CA    . ILE A 1 298 ? 20.332 24.357  35.211  1.00 57.17  ?  304 ILE A CA    1 
ATOM   2222 C C     . ILE A 1 298 ? 21.754 24.325  35.759  1.00 60.19  ?  304 ILE A C     1 
ATOM   2223 O O     . ILE A 1 298 ? 22.038 24.871  36.832  1.00 58.86  ?  304 ILE A O     1 
ATOM   2224 C CB    . ILE A 1 298 ? 19.649 22.984  35.353  1.00 61.65  ?  304 ILE A CB    1 
ATOM   2225 C CG1   . ILE A 1 298 ? 18.178 23.036  34.908  1.00 64.85  ?  304 ILE A CG1   1 
ATOM   2226 C CG2   . ILE A 1 298 ? 19.795 22.459  36.765  1.00 58.49  ?  304 ILE A CG2   1 
ATOM   2227 C CD1   . ILE A 1 298 ? 17.226 23.632  35.914  1.00 69.01  ?  304 ILE A CD1   1 
ATOM   2228 N N     . ALA A 1 299 ? 22.674 23.691  35.026  1.00 57.21  ?  305 ALA A N     1 
ATOM   2229 C CA    . ALA A 1 299 ? 24.011 23.486  35.572  1.00 55.66  ?  305 ALA A CA    1 
ATOM   2230 C C     . ALA A 1 299 ? 24.782 24.792  35.674  1.00 58.39  ?  305 ALA A C     1 
ATOM   2231 O O     . ALA A 1 299 ? 25.487 25.019  36.664  1.00 59.76  ?  305 ALA A O     1 
ATOM   2232 C CB    . ALA A 1 299 ? 24.787 22.478  34.732  1.00 51.81  ?  305 ALA A CB    1 
ATOM   2233 N N     . VAL A 1 300 ? 24.680 25.655  34.660  1.00 57.13  ?  306 VAL A N     1 
ATOM   2234 C CA    . VAL A 1 300 ? 25.390 26.931  34.701  1.00 53.67  ?  306 VAL A CA    1 
ATOM   2235 C C     . VAL A 1 300 ? 24.822 27.814  35.804  1.00 58.51  ?  306 VAL A C     1 
ATOM   2236 O O     . VAL A 1 300 ? 25.567 28.447  36.563  1.00 58.30  ?  306 VAL A O     1 
ATOM   2237 C CB    . VAL A 1 300 ? 25.334 27.629  33.325  1.00 53.26  ?  306 VAL A CB    1 
ATOM   2238 C CG1   . VAL A 1 300 ? 26.082 28.953  33.367  1.00 50.93  ?  306 VAL A CG1   1 
ATOM   2239 C CG2   . VAL A 1 300 ? 25.942 26.753  32.264  1.00 48.61  ?  306 VAL A CG2   1 
ATOM   2240 N N     . ALA A 1 301 ? 23.496 27.866  35.913  1.00 57.13  ?  307 ALA A N     1 
ATOM   2241 C CA    . ALA A 1 301 ? 22.871 28.641  36.973  1.00 56.88  ?  307 ALA A CA    1 
ATOM   2242 C C     . ALA A 1 301 ? 23.370 28.189  38.346  1.00 65.55  ?  307 ALA A C     1 
ATOM   2243 O O     . ALA A 1 301 ? 23.720 29.017  39.200  1.00 61.88  ?  307 ALA A O     1 
ATOM   2244 C CB    . ALA A 1 301 ? 21.351 28.520  36.868  1.00 56.92  ?  307 ALA A CB    1 
ATOM   2245 N N     . ASN A 1 302 ? 23.436 26.870  38.562  1.00 63.87  ?  308 ASN A N     1 
ATOM   2246 C CA    . ASN A 1 302 ? 23.849 26.326  39.850  1.00 63.61  ?  308 ASN A CA    1 
ATOM   2247 C C     . ASN A 1 302 ? 25.336 26.500  40.105  1.00 64.05  ?  308 ASN A C     1 
ATOM   2248 O O     . ASN A 1 302 ? 25.760 26.407  41.262  1.00 66.85  ?  308 ASN A O     1 
ATOM   2249 C CB    . ASN A 1 302 ? 23.478 24.843  39.951  1.00 62.76  ?  308 ASN A CB    1 
ATOM   2250 C CG    . ASN A 1 302 ? 21.990 24.627  40.061  1.00 67.74  ?  308 ASN A CG    1 
ATOM   2251 O OD1   . ASN A 1 302 ? 21.227 25.577  40.245  1.00 70.48  ?  308 ASN A OD1   1 
ATOM   2252 N ND2   . ASN A 1 302 ? 21.562 23.375  39.963  1.00 68.95  ?  308 ASN A ND2   1 
ATOM   2253 N N     . ILE A 1 303 ? 26.140 26.728  39.061  1.00 60.61  ?  309 ILE A N     1 
ATOM   2254 C CA    . ILE A 1 303 ? 27.524 27.116  39.298  1.00 61.20  ?  309 ILE A CA    1 
ATOM   2255 C C     . ILE A 1 303 ? 27.581 28.564  39.759  1.00 67.71  ?  309 ILE A C     1 
ATOM   2256 O O     . ILE A 1 303 ? 28.265 28.889  40.734  1.00 73.45  ?  309 ILE A O     1 
ATOM   2257 C CB    . ILE A 1 303 ? 28.397 26.882  38.054  1.00 58.59  ?  309 ILE A CB    1 
ATOM   2258 C CG1   . ILE A 1 303 ? 28.481 25.398  37.701  1.00 60.36  ?  309 ILE A CG1   1 
ATOM   2259 C CG2   . ILE A 1 303 ? 29.793 27.390  38.294  1.00 57.54  ?  309 ILE A CG2   1 
ATOM   2260 C CD1   . ILE A 1 303 ? 29.441 25.076  36.512  1.00 48.69  ?  309 ILE A CD1   1 
ATOM   2261 N N     . VAL A 1 304 ? 26.834 29.450  39.100  1.00 65.67  ?  310 VAL A N     1 
ATOM   2262 C CA    . VAL A 1 304 ? 26.798 30.844  39.528  1.00 67.30  ?  310 VAL A CA    1 
ATOM   2263 C C     . VAL A 1 304 ? 26.120 30.973  40.887  1.00 67.82  ?  310 VAL A C     1 
ATOM   2264 O O     . VAL A 1 304 ? 26.584 31.712  41.759  1.00 67.92  ?  310 VAL A O     1 
ATOM   2265 C CB    . VAL A 1 304 ? 26.101 31.718  38.474  1.00 64.78  ?  310 VAL A CB    1 
ATOM   2266 C CG1   . VAL A 1 304 ? 26.104 33.176  38.941  1.00 66.58  ?  310 VAL A CG1   1 
ATOM   2267 C CG2   . VAL A 1 304 ? 26.791 31.572  37.141  1.00 63.64  ?  310 VAL A CG2   1 
ATOM   2268 N N     . ASN A 1 305 ? 24.999 30.280  41.077  1.00 66.33  ?  311 ASN A N     1 
ATOM   2269 C CA    . ASN A 1 305 ? 24.315 30.334  42.363  1.00 70.94  ?  311 ASN A CA    1 
ATOM   2270 C C     . ASN A 1 305 ? 25.191 29.792  43.485  1.00 75.81  ?  311 ASN A C     1 
ATOM   2271 O O     . ASN A 1 305 ? 25.154 30.312  44.603  1.00 80.80  ?  311 ASN A O     1 
ATOM   2272 C CB    . ASN A 1 305 ? 22.998 29.560  42.294  1.00 72.83  ?  311 ASN A CB    1 
ATOM   2273 C CG    . ASN A 1 305 ? 21.882 30.378  41.688  1.00 71.84  ?  311 ASN A CG    1 
ATOM   2274 O OD1   . ASN A 1 305 ? 21.957 31.604  41.662  1.00 69.03  ?  311 ASN A OD1   1 
ATOM   2275 N ND2   . ASN A 1 305 ? 20.836 29.709  41.211  1.00 73.17  ?  311 ASN A ND2   1 
ATOM   2276 N N     . SER A 1 306 ? 25.998 28.767  43.209  1.00 72.85  ?  312 SER A N     1 
ATOM   2277 C CA    . SER A 1 306 ? 26.884 28.252  44.241  1.00 74.04  ?  312 SER A CA    1 
ATOM   2278 C C     . SER A 1 306 ? 27.959 29.269  44.626  1.00 76.01  ?  312 SER A C     1 
ATOM   2279 O O     . SER A 1 306 ? 28.448 29.248  45.758  1.00 83.66  ?  312 SER A O     1 
ATOM   2280 C CB    . SER A 1 306 ? 27.514 26.933  43.787  1.00 74.43  ?  312 SER A CB    1 
ATOM   2281 O OG    . SER A 1 306 ? 28.897 27.082  43.507  1.00 85.38  ?  312 SER A OG    1 
ATOM   2282 N N     . VAL A 1 307 ? 28.337 30.172  43.724  1.00 76.98  ?  313 VAL A N     1 
ATOM   2283 C CA    . VAL A 1 307 ? 29.290 31.214  44.106  1.00 79.47  ?  313 VAL A CA    1 
ATOM   2284 C C     . VAL A 1 307 ? 28.578 32.364  44.819  1.00 78.47  ?  313 VAL A C     1 
ATOM   2285 O O     . VAL A 1 307 ? 29.043 32.836  45.856  1.00 80.25  ?  313 VAL A O     1 
ATOM   2286 C CB    . VAL A 1 307 ? 30.076 31.703  42.874  1.00 72.19  ?  313 VAL A CB    1 
ATOM   2287 N N     . LYS A 1 308 ? 27.446 32.834  44.277  1.00 79.72  ?  314 LYS A N     1 
ATOM   2288 C CA    . LYS A 1 308 ? 26.615 33.898  44.839  1.00 71.87  ?  314 LYS A CA    1 
ATOM   2289 C C     . LYS A 1 308 ? 25.794 33.452  46.049  1.00 82.48  ?  314 LYS A C     1 
ATOM   2290 O O     . LYS A 1 308 ? 24.872 34.180  46.438  1.00 80.66  ?  314 LYS A O     1 
ATOM   2291 C CB    . LYS A 1 308 ? 25.647 34.436  43.780  1.00 70.16  ?  314 LYS A CB    1 
ATOM   2292 C CG    . LYS A 1 308 ? 26.259 35.292  42.693  1.00 65.58  ?  314 LYS A CG    1 
ATOM   2293 C CD    . LYS A 1 308 ? 25.155 35.871  41.831  1.00 66.70  ?  314 LYS A CD    1 
ATOM   2294 C CE    . LYS A 1 308 ? 25.704 36.590  40.616  1.00 68.66  ?  314 LYS A CE    1 
ATOM   2295 N NZ    . LYS A 1 308 ? 24.642 36.985  39.666  1.00 70.27  ?  314 LYS A NZ    1 
ATOM   2296 N N     . GLN A 1 309 ? 26.096 32.284  46.628  1.00 86.26  ?  315 GLN A N     1 
ATOM   2297 C CA    . GLN A 1 309 ? 25.352 31.699  47.743  1.00 87.99  ?  315 GLN A CA    1 
ATOM   2298 C C     . GLN A 1 309 ? 23.848 31.923  47.613  1.00 85.17  ?  315 GLN A C     1 
ATOM   2299 O O     . GLN A 1 309 ? 23.286 32.837  48.222  1.00 90.44  ?  315 GLN A O     1 
ATOM   2300 C CB    . GLN A 1 309 ? 25.885 32.244  49.075  1.00 86.70  ?  315 GLN A CB    1 
ATOM   2301 C CG    . GLN A 1 309 ? 26.844 31.293  49.814  1.00 86.62  ?  315 GLN A CG    1 
ATOM   2302 C CD    . GLN A 1 309 ? 27.990 30.784  48.948  1.00 94.26  ?  315 GLN A CD    1 
ATOM   2303 O OE1   . GLN A 1 309 ? 28.389 31.430  47.980  1.00 96.82  ?  315 GLN A OE1   1 
ATOM   2304 N NE2   . GLN A 1 309 ? 28.521 29.611  49.294  1.00 98.23  ?  315 GLN A NE2   1 
ATOM   2305 N N     . ARG A 1 310 ? 23.199 31.091  46.816  1.00 82.38  ?  316 ARG A N     1 
ATOM   2306 C CA    . ARG A 1 310 ? 21.783 31.184  46.510  1.00 82.38  ?  316 ARG A CA    1 
ATOM   2307 C C     . ARG A 1 310 ? 21.245 29.764  46.433  1.00 86.05  ?  316 ARG A C     1 
ATOM   2308 O O     . ARG A 1 310 ? 22.013 28.814  46.240  1.00 81.55  ?  316 ARG A O     1 
ATOM   2309 C CB    . ARG A 1 310 ? 21.548 31.928  45.184  1.00 80.92  ?  316 ARG A CB    1 
ATOM   2310 C CG    . ARG A 1 310 ? 20.742 33.209  45.289  1.00 77.60  ?  316 ARG A CG    1 
ATOM   2311 C CD    . ARG A 1 310 ? 20.806 34.026  44.002  1.00 74.12  ?  316 ARG A CD    1 
ATOM   2312 N N     . PRO A 1 311 ? 19.935 29.582  46.598  1.00 87.33  ?  317 PRO A N     1 
ATOM   2313 C CA    . PRO A 1 311 ? 19.372 28.232  46.470  1.00 86.55  ?  317 PRO A CA    1 
ATOM   2314 C C     . PRO A 1 311 ? 19.511 27.739  45.038  1.00 79.72  ?  317 PRO A C     1 
ATOM   2315 O O     . PRO A 1 311 ? 19.092 28.415  44.095  1.00 80.06  ?  317 PRO A O     1 
ATOM   2316 C CB    . PRO A 1 311 ? 17.898 28.411  46.864  1.00 86.41  ?  317 PRO A CB    1 
ATOM   2317 C CG    . PRO A 1 311 ? 17.793 29.765  47.458  1.00 77.13  ?  317 PRO A CG    1 
ATOM   2318 C CD    . PRO A 1 311 ? 18.897 30.584  46.888  1.00 80.66  ?  317 PRO A CD    1 
ATOM   2319 N N     . LEU A 1 312 ? 20.120 26.564  44.879  1.00 77.44  ?  318 LEU A N     1 
ATOM   2320 C CA    . LEU A 1 312 ? 20.174 25.939  43.563  1.00 76.00  ?  318 LEU A CA    1 
ATOM   2321 C C     . LEU A 1 312 ? 18.762 25.644  43.070  1.00 76.59  ?  318 LEU A C     1 
ATOM   2322 O O     . LEU A 1 312 ? 17.822 25.504  43.856  1.00 80.72  ?  318 LEU A O     1 
ATOM   2323 C CB    . LEU A 1 312 ? 20.990 24.645  43.594  1.00 72.82  ?  318 LEU A CB    1 
ATOM   2324 C CG    . LEU A 1 312 ? 22.353 24.652  44.290  1.00 73.29  ?  318 LEU A CG    1 
ATOM   2325 C CD1   . LEU A 1 312 ? 23.108 23.396  43.954  1.00 70.84  ?  318 LEU A CD1   1 
ATOM   2326 C CD2   . LEU A 1 312 ? 23.183 25.864  43.935  1.00 75.39  ?  318 LEU A CD2   1 
ATOM   2327 N N     . GLN A 1 313 ? 18.608 25.582  41.754  1.00 78.79  ?  319 GLN A N     1 
ATOM   2328 C CA    . GLN A 1 313 ? 17.333 25.193  41.173  1.00 79.70  ?  319 GLN A CA    1 
ATOM   2329 C C     . GLN A 1 313 ? 17.392 23.743  40.712  1.00 77.78  ?  319 GLN A C     1 
ATOM   2330 O O     . GLN A 1 313 ? 18.464 23.179  40.467  1.00 73.96  ?  319 GLN A O     1 
ATOM   2331 C CB    . GLN A 1 313 ? 16.940 26.114  40.017  1.00 77.47  ?  319 GLN A CB    1 
ATOM   2332 C CG    . GLN A 1 313 ? 17.990 26.308  38.952  1.00 76.63  ?  319 GLN A CG    1 
ATOM   2333 C CD    . GLN A 1 313 ? 17.720 27.552  38.119  1.00 80.74  ?  319 GLN A CD    1 
ATOM   2334 O OE1   . GLN A 1 313 ? 17.638 27.493  36.891  1.00 75.58  ?  319 GLN A OE1   1 
ATOM   2335 N NE2   . GLN A 1 313 ? 17.573 28.687  38.791  1.00 84.23  ?  319 GLN A NE2   1 
ATOM   2336 N N     . ALA A 1 314 ? 16.216 23.139  40.617  1.00 78.16  ?  320 ALA A N     1 
ATOM   2337 C CA    . ALA A 1 314 ? 16.100 21.708  40.407  1.00 80.23  ?  320 ALA A CA    1 
ATOM   2338 C C     . ALA A 1 314 ? 15.509 21.418  39.039  1.00 76.40  ?  320 ALA A C     1 
ATOM   2339 O O     . ALA A 1 314 ? 14.952 22.296  38.378  1.00 75.99  ?  320 ALA A O     1 
ATOM   2340 C CB    . ALA A 1 314 ? 15.243 21.067  41.503  1.00 82.12  ?  320 ALA A CB    1 
ATOM   2341 N N     . TYR A 1 315 ? 15.634 20.157  38.635  1.00 77.51  ?  321 TYR A N     1 
ATOM   2342 C CA    . TYR A 1 315 ? 15.111 19.655  37.372  1.00 78.32  ?  321 TYR A CA    1 
ATOM   2343 C C     . TYR A 1 315 ? 13.901 18.774  37.660  1.00 81.38  ?  321 TYR A C     1 
ATOM   2344 O O     . TYR A 1 315 ? 14.033 17.743  38.327  1.00 83.69  ?  321 TYR A O     1 
ATOM   2345 C CB    . TYR A 1 315 ? 16.196 18.879  36.622  1.00 78.47  ?  321 TYR A CB    1 
ATOM   2346 C CG    . TYR A 1 315 ? 15.673 17.918  35.577  1.00 84.22  ?  321 TYR A CG    1 
ATOM   2347 C CD1   . TYR A 1 315 ? 14.868 18.364  34.529  1.00 84.26  ?  321 TYR A CD1   1 
ATOM   2348 C CD2   . TYR A 1 315 ? 15.996 16.563  35.626  1.00 84.48  ?  321 TYR A CD2   1 
ATOM   2349 C CE1   . TYR A 1 315 ? 14.384 17.485  33.563  1.00 84.40  ?  321 TYR A CE1   1 
ATOM   2350 C CE2   . TYR A 1 315 ? 15.522 15.675  34.664  1.00 86.26  ?  321 TYR A CE2   1 
ATOM   2351 C CZ    . TYR A 1 315 ? 14.715 16.142  33.634  1.00 86.77  ?  321 TYR A CZ    1 
ATOM   2352 O OH    . TYR A 1 315 ? 14.236 15.265  32.677  1.00 89.25  ?  321 TYR A OH    1 
ATOM   2353 N N     . LYS A 1 316 ? 12.728 19.175  37.153  1.00 80.98  ?  322 LYS A N     1 
ATOM   2354 C CA    . LYS A 1 316 ? 11.458 18.498  37.427  1.00 81.35  ?  322 LYS A CA    1 
ATOM   2355 C C     . LYS A 1 316 ? 10.945 17.753  36.198  1.00 84.15  ?  322 LYS A C     1 
ATOM   2356 O O     . LYS A 1 316 ? 10.186 18.317  35.397  1.00 83.78  ?  322 LYS A O     1 
ATOM   2357 C CB    . LYS A 1 316 ? 10.413 19.505  37.907  1.00 77.55  ?  322 LYS A CB    1 
ATOM   2358 N N     . PRO A 1 317 ? 11.279 16.473  36.031  1.00 85.85  ?  323 PRO A N     1 
ATOM   2359 C CA    . PRO A 1 317 ? 10.827 15.741  34.840  1.00 82.35  ?  323 PRO A CA    1 
ATOM   2360 C C     . PRO A 1 317 ? 9.309  15.718  34.724  1.00 83.62  ?  323 PRO A C     1 
ATOM   2361 O O     . PRO A 1 317 ? 8.590  15.621  35.720  1.00 83.11  ?  323 PRO A O     1 
ATOM   2362 C CB    . PRO A 1 317 ? 11.381 14.328  35.059  1.00 81.90  ?  323 PRO A CB    1 
ATOM   2363 C CG    . PRO A 1 317 ? 12.416 14.464  36.126  1.00 87.10  ?  323 PRO A CG    1 
ATOM   2364 C CD    . PRO A 1 317 ? 11.991 15.606  36.983  1.00 86.40  ?  323 PRO A CD    1 
ATOM   2365 N N     . GLY A 1 318 ? 8.825  15.802  33.482  1.00 83.84  ?  324 GLY A N     1 
ATOM   2366 C CA    . GLY A 1 318 ? 7.424  15.659  33.170  1.00 75.01  ?  324 GLY A CA    1 
ATOM   2367 C C     . GLY A 1 318 ? 7.128  14.426  32.333  1.00 74.13  ?  324 GLY A C     1 
ATOM   2368 O O     . GLY A 1 318 ? 7.925  13.483  32.241  1.00 69.94  ?  324 GLY A O     1 
ATOM   2369 N N     . ALA A 1 319 ? 5.950  14.428  31.716  1.00 71.83  ?  325 ALA A N     1 
ATOM   2370 C CA    . ALA A 1 319 ? 5.546  13.300  30.897  1.00 69.93  ?  325 ALA A CA    1 
ATOM   2371 C C     . ALA A 1 319 ? 6.385  13.237  29.619  1.00 70.91  ?  325 ALA A C     1 
ATOM   2372 O O     . ALA A 1 319 ? 7.086  14.186  29.245  1.00 67.61  ?  325 ALA A O     1 
ATOM   2373 C CB    . ALA A 1 319 ? 4.059  13.387  30.554  1.00 70.61  ?  325 ALA A CB    1 
ATOM   2374 N N     . LEU A 1 320 ? 6.277  12.102  28.931  1.00 69.52  ?  326 LEU A N     1 
ATOM   2375 C CA    . LEU A 1 320 ? 7.187  11.768  27.839  1.00 68.29  ?  326 LEU A CA    1 
ATOM   2376 C C     . LEU A 1 320 ? 6.892  12.582  26.581  1.00 62.68  ?  326 LEU A C     1 
ATOM   2377 O O     . LEU A 1 320 ? 5.780  12.533  26.046  1.00 62.54  ?  326 LEU A O     1 
ATOM   2378 C CB    . LEU A 1 320 ? 7.076  10.281  27.532  1.00 68.53  ?  326 LEU A CB    1 
ATOM   2379 C CG    . LEU A 1 320 ? 8.197  9.682   26.690  1.00 68.89  ?  326 LEU A CG    1 
ATOM   2380 C CD1   . LEU A 1 320 ? 7.964  9.880   25.214  1.00 67.65  ?  326 LEU A CD1   1 
ATOM   2381 C CD2   . LEU A 1 320 ? 9.474  10.333  27.095  1.00 70.69  ?  326 LEU A CD2   1 
ATOM   2382 N N     . THR A 1 321 ? 7.901  13.291  26.081  1.00 61.43  ?  327 THR A N     1 
ATOM   2383 C CA    . THR A 1 321 ? 7.835  13.920  24.767  1.00 61.71  ?  327 THR A CA    1 
ATOM   2384 C C     . THR A 1 321 ? 8.862  13.272  23.843  1.00 57.26  ?  327 THR A C     1 
ATOM   2385 O O     . THR A 1 321 ? 10.057 13.262  24.143  1.00 53.13  ?  327 THR A O     1 
ATOM   2386 C CB    . THR A 1 321 ? 8.061  15.427  24.843  1.00 56.52  ?  327 THR A CB    1 
ATOM   2387 O OG1   . THR A 1 321 ? 6.966  16.022  25.537  1.00 64.55  ?  327 THR A OG1   1 
ATOM   2388 C CG2   . THR A 1 321 ? 8.104  16.007  23.442  1.00 55.06  ?  327 THR A CG2   1 
ATOM   2389 N N     . PHE A 1 322 ? 8.386  12.710  22.737  1.00 58.92  ?  328 PHE A N     1 
ATOM   2390 C CA    . PHE A 1 322 ? 9.263  12.220  21.683  1.00 57.45  ?  328 PHE A CA    1 
ATOM   2391 C C     . PHE A 1 322 ? 8.444  12.108  20.412  1.00 53.42  ?  328 PHE A C     1 
ATOM   2392 O O     . PHE A 1 322 ? 7.383  11.475  20.413  1.00 52.21  ?  328 PHE A O     1 
ATOM   2393 C CB    . PHE A 1 322 ? 9.897  10.866  22.032  1.00 58.85  ?  328 PHE A CB    1 
ATOM   2394 C CG    . PHE A 1 322 ? 10.795 10.341  20.956  1.00 61.52  ?  328 PHE A CG    1 
ATOM   2395 C CD1   . PHE A 1 322 ? 11.688 11.190  20.300  1.00 63.60  ?  328 PHE A CD1   1 
ATOM   2396 C CD2   . PHE A 1 322 ? 10.740 9.016   20.572  1.00 64.78  ?  328 PHE A CD2   1 
ATOM   2397 C CE1   . PHE A 1 322 ? 12.522 10.720  19.268  1.00 57.59  ?  328 PHE A CE1   1 
ATOM   2398 C CE2   . PHE A 1 322 ? 11.562 8.542   19.556  1.00 62.04  ?  328 PHE A CE2   1 
ATOM   2399 C CZ    . PHE A 1 322 ? 12.457 9.395   18.911  1.00 61.42  ?  328 PHE A CZ    1 
ATOM   2400 N N     . LEU A 1 323 ? 8.932  12.740  19.347  1.00 52.18  ?  329 LEU A N     1 
ATOM   2401 C CA    . LEU A 1 323 ? 8.284  12.761  18.045  1.00 49.32  ?  329 LEU A CA    1 
ATOM   2402 C C     . LEU A 1 323 ? 9.117  11.952  17.074  1.00 48.27  ?  329 LEU A C     1 
ATOM   2403 O O     . LEU A 1 323 ? 10.330 12.161  16.979  1.00 48.83  ?  329 LEU A O     1 
ATOM   2404 C CB    . LEU A 1 323 ? 8.153  14.189  17.533  1.00 47.99  ?  329 LEU A CB    1 
ATOM   2405 C CG    . LEU A 1 323 ? 7.534  15.130  18.554  1.00 46.24  ?  329 LEU A CG    1 
ATOM   2406 C CD1   . LEU A 1 323 ? 7.855  16.560  18.216  1.00 47.01  ?  329 LEU A CD1   1 
ATOM   2407 C CD2   . LEU A 1 323 ? 6.056  14.916  18.552  1.00 49.13  ?  329 LEU A CD2   1 
ATOM   2408 N N     . LEU A 1 324 ? 8.478  11.031  16.362  1.00 47.88  ?  330 LEU A N     1 
ATOM   2409 C CA    . LEU A 1 324 ? 9.149  10.257  15.326  1.00 48.93  ?  330 LEU A CA    1 
ATOM   2410 C C     . LEU A 1 324 ? 8.877  10.876  13.967  1.00 51.16  ?  330 LEU A C     1 
ATOM   2411 O O     . LEU A 1 324 ? 7.718  11.082  13.593  1.00 51.68  ?  330 LEU A O     1 
ATOM   2412 C CB    . LEU A 1 324 ? 8.701  8.803   15.328  1.00 48.27  ?  330 LEU A CB    1 
ATOM   2413 C CG    . LEU A 1 324 ? 9.306  8.030   16.483  1.00 55.13  ?  330 LEU A CG    1 
ATOM   2414 C CD1   . LEU A 1 324 ? 8.418  6.882   16.837  1.00 58.51  ?  330 LEU A CD1   1 
ATOM   2415 C CD2   . LEU A 1 324 ? 10.699 7.544   16.131  1.00 55.85  ?  330 LEU A CD2   1 
ATOM   2416 N N     . SER A 1 325 ? 9.955  11.175  13.247  1.00 53.64  ?  331 SER A N     1 
ATOM   2417 C CA    . SER A 1 325 ? 9.913  11.636  11.864  1.00 51.77  ?  331 SER A CA    1 
ATOM   2418 C C     . SER A 1 325 ? 9.729  10.438  10.933  1.00 53.94  ?  331 SER A C     1 
ATOM   2419 O O     . SER A 1 325 ? 10.554 9.520   10.936  1.00 58.89  ?  331 SER A O     1 
ATOM   2420 C CB    . SER A 1 325 ? 11.220 12.367  11.555  1.00 50.63  ?  331 SER A CB    1 
ATOM   2421 O OG    . SER A 1 325 ? 11.185 13.027  10.308  1.00 55.79  ?  331 SER A OG    1 
ATOM   2422 N N     . MET A 1 326 ? 8.665  10.428  10.137  1.00 51.78  ?  332 MET A N     1 
ATOM   2423 C CA    . MET A 1 326 ? 8.465  9.372   9.137   1.00 49.33  ?  332 MET A CA    1 
ATOM   2424 C C     . MET A 1 326 ? 8.737  9.927   7.736   1.00 51.86  ?  332 MET A C     1 
ATOM   2425 O O     . MET A 1 326 ? 7.839  10.071  6.898   1.00 50.01  ?  332 MET A O     1 
ATOM   2426 C CB    . MET A 1 326 ? 7.040  8.797   9.250   1.00 54.31  ?  332 MET A CB    1 
ATOM   2427 C CG    . MET A 1 326 ? 6.695  8.058   10.567  1.00 56.78  ?  332 MET A CG    1 
ATOM   2428 S SD    . MET A 1 326 ? 7.692  6.583   10.862  1.00 64.85  ?  332 MET A SD    1 
ATOM   2429 C CE    . MET A 1 326 ? 8.826  7.269   12.057  1.00 54.98  ?  332 MET A CE    1 
ATOM   2430 N N     . GLY A 1 327 ? 9.996  10.229  7.469   1.00 53.67  ?  333 GLY A N     1 
ATOM   2431 C CA    . GLY A 1 327 ? 10.304 10.984  6.274   1.00 48.31  ?  333 GLY A CA    1 
ATOM   2432 C C     . GLY A 1 327 ? 9.976  12.450  6.494   1.00 50.43  ?  333 GLY A C     1 
ATOM   2433 O O     . GLY A 1 327 ? 9.707  12.894  7.615   1.00 49.30  ?  333 GLY A O     1 
ATOM   2434 N N     . ARG A 1 328 ? 9.977  13.214  5.405   1.00 47.06  ?  334 ARG A N     1 
ATOM   2435 C CA    . ARG A 1 328 ? 9.715  14.638  5.543   1.00 45.47  ?  334 ARG A CA    1 
ATOM   2436 C C     . ARG A 1 328 ? 8.223  14.981  5.532   1.00 48.69  ?  334 ARG A C     1 
ATOM   2437 O O     . ARG A 1 328 ? 7.844  16.071  5.980   1.00 46.21  ?  334 ARG A O     1 
ATOM   2438 C CB    . ARG A 1 328 ? 10.459 15.421  4.449   1.00 44.90  ?  334 ARG A CB    1 
ATOM   2439 C CG    . ARG A 1 328 ? 9.824  15.313  3.084   1.00 43.94  ?  334 ARG A CG    1 
ATOM   2440 C CD    . ARG A 1 328 ? 10.566 16.115  2.030   1.00 41.51  ?  334 ARG A CD    1 
ATOM   2441 N NE    . ARG A 1 328 ? 11.906 15.606  1.774   1.00 46.38  ?  334 ARG A NE    1 
ATOM   2442 C CZ    . ARG A 1 328 ? 13.019 16.189  2.195   1.00 48.82  ?  334 ARG A CZ    1 
ATOM   2443 N NH1   . ARG A 1 328 ? 12.988 17.290  2.919   1.00 48.60  ?  334 ARG A NH1   1 
ATOM   2444 N NH2   . ARG A 1 328 ? 14.193 15.662  1.866   1.00 47.21  ?  334 ARG A NH2   1 
ATOM   2445 N N     . ASN A 1 329 ? 7.362  14.083  5.063   1.00 47.22  ?  335 ASN A N     1 
ATOM   2446 C CA    . ASN A 1 329 ? 5.946  14.392  4.928   1.00 42.77  ?  335 ASN A CA    1 
ATOM   2447 C C     . ASN A 1 329 ? 5.072  13.697  5.966   1.00 44.94  ?  335 ASN A C     1 
ATOM   2448 O O     . ASN A 1 329 ? 3.847  13.744  5.851   1.00 48.92  ?  335 ASN A O     1 
ATOM   2449 C CB    . ASN A 1 329 ? 5.469  14.036  3.518   1.00 43.90  ?  335 ASN A CB    1 
ATOM   2450 C CG    . ASN A 1 329 ? 5.656  12.561  3.180   1.00 44.96  ?  335 ASN A CG    1 
ATOM   2451 O OD1   . ASN A 1 329 ? 6.335  11.820  3.897   1.00 44.58  ?  335 ASN A OD1   1 
ATOM   2452 N ND2   . ASN A 1 329 ? 5.054  12.131  2.069   1.00 43.07  ?  335 ASN A ND2   1 
ATOM   2453 N N     . ASP A 1 330 ? 5.649  13.075  6.988   1.00 47.63  ?  336 ASP A N     1 
ATOM   2454 C CA    . ASP A 1 330 ? 4.843  12.272  7.898   1.00 48.48  ?  336 ASP A CA    1 
ATOM   2455 C C     . ASP A 1 330 ? 5.537  12.142  9.251   1.00 50.73  ?  336 ASP A C     1 
ATOM   2456 O O     . ASP A 1 330 ? 6.730  12.417  9.407   1.00 49.56  ?  336 ASP A O     1 
ATOM   2457 C CB    . ASP A 1 330 ? 4.578  10.877  7.303   1.00 51.78  ?  336 ASP A CB    1 
ATOM   2458 C CG    . ASP A 1 330 ? 3.139  10.368  7.555   1.00 59.86  ?  336 ASP A CG    1 
ATOM   2459 O OD1   . ASP A 1 330 ? 2.513  10.752  8.581   1.00 52.61  ?  336 ASP A OD1   1 
ATOM   2460 O OD2   . ASP A 1 330 ? 2.649  9.562   6.709   1.00 60.30  -1 336 ASP A OD2   1 
ATOM   2461 N N     . GLY A 1 331 ? 4.772  11.694  10.233  1.00 50.82  ?  337 GLY A N     1 
ATOM   2462 C CA    . GLY A 1 331 ? 5.347  11.401  11.525  1.00 51.52  ?  337 GLY A CA    1 
ATOM   2463 C C     . GLY A 1 331 ? 4.246  11.085  12.505  1.00 50.04  ?  337 GLY A C     1 
ATOM   2464 O O     . GLY A 1 331 ? 3.064  11.054  12.149  1.00 52.00  ?  337 GLY A O     1 
ATOM   2465 N N     . VAL A 1 332 ? 4.662  10.859  13.746  1.00 49.37  ?  338 VAL A N     1 
ATOM   2466 C CA    . VAL A 1 332 ? 3.741  10.652  14.859  1.00 48.96  ?  338 VAL A CA    1 
ATOM   2467 C C     . VAL A 1 332 ? 4.561  10.684  16.139  1.00 48.72  ?  338 VAL A C     1 
ATOM   2468 O O     . VAL A 1 332 ? 5.790  10.588  16.098  1.00 50.88  ?  338 VAL A O     1 
ATOM   2469 C CB    . VAL A 1 332 ? 2.968  9.330   14.696  1.00 50.67  ?  338 VAL A CB    1 
ATOM   2470 C CG1   . VAL A 1 332 ? 3.920  8.143   14.760  1.00 52.08  ?  338 VAL A CG1   1 
ATOM   2471 C CG2   . VAL A 1 332 ? 1.858  9.216   15.722  1.00 55.75  ?  338 VAL A CG2   1 
ATOM   2472 N N     . GLY A 1 333 ? 3.901  10.833  17.279  1.00 53.09  ?  339 GLY A N     1 
ATOM   2473 C CA    . GLY A 1 333 ? 4.610  10.837  18.539  1.00 53.00  ?  339 GLY A CA    1 
ATOM   2474 C C     . GLY A 1 333 ? 3.720  11.349  19.649  1.00 53.21  ?  339 GLY A C     1 
ATOM   2475 O O     . GLY A 1 333 ? 2.502  11.448  19.506  1.00 54.21  ?  339 GLY A O     1 
ATOM   2476 N N     . GLN A 1 334 ? 4.357  11.677  20.755  1.00 54.56  ?  340 GLN A N     1 
ATOM   2477 C CA    . GLN A 1 334 ? 3.635  12.145  21.922  1.00 59.75  ?  340 GLN A CA    1 
ATOM   2478 C C     . GLN A 1 334 ? 4.339  13.355  22.514  1.00 59.83  ?  340 GLN A C     1 
ATOM   2479 O O     . GLN A 1 334 ? 5.568  13.398  22.592  1.00 59.85  ?  340 GLN A O     1 
ATOM   2480 C CB    . GLN A 1 334 ? 3.510  11.041  22.965  1.00 58.35  ?  340 GLN A CB    1 
ATOM   2481 C CG    . GLN A 1 334 ? 4.825  10.461  23.324  1.00 56.68  ?  340 GLN A CG    1 
ATOM   2482 C CD    . GLN A 1 334 ? 4.700  9.328   24.280  1.00 61.58  ?  340 GLN A CD    1 
ATOM   2483 O OE1   . GLN A 1 334 ? 4.779  8.156   23.887  1.00 64.23  ?  340 GLN A OE1   1 
ATOM   2484 N NE2   . GLN A 1 334 ? 4.511  9.655   25.561  1.00 61.33  ?  340 GLN A NE2   1 
ATOM   2485 N N     . ILE A 1 335 ? 3.545  14.345  22.906  1.00 63.05  ?  341 ILE A N     1 
ATOM   2486 C CA    . ILE A 1 335 ? 4.025  15.548  23.576  1.00 63.20  ?  341 ILE A CA    1 
ATOM   2487 C C     . ILE A 1 335 ? 3.445  15.541  24.972  1.00 62.19  ?  341 ILE A C     1 
ATOM   2488 O O     . ILE A 1 335 ? 2.224  15.620  25.134  1.00 70.03  ?  341 ILE A O     1 
ATOM   2489 C CB    . ILE A 1 335 ? 3.611  16.820  22.829  1.00 62.17  ?  341 ILE A CB    1 
ATOM   2490 C CG1   . ILE A 1 335 ? 4.436  16.987  21.558  1.00 57.64  ?  341 ILE A CG1   1 
ATOM   2491 C CG2   . ILE A 1 335 ? 3.778  18.021  23.727  1.00 65.46  ?  341 ILE A CG2   1 
ATOM   2492 C CD1   . ILE A 1 335 ? 3.838  17.988  20.604  1.00 59.39  ?  341 ILE A CD1   1 
ATOM   2493 N N     . SER A 1 336 ? 4.303  15.435  25.976  1.00 62.27  ?  342 SER A N     1 
ATOM   2494 C CA    . SER A 1 336 ? 3.856  15.337  27.369  1.00 66.88  ?  342 SER A CA    1 
ATOM   2495 C C     . SER A 1 336 ? 2.793  14.254  27.525  1.00 62.12  ?  342 SER A C     1 
ATOM   2496 O O     . SER A 1 336 ? 1.669  14.507  27.956  1.00 66.10  ?  342 SER A O     1 
ATOM   2497 C CB    . SER A 1 336 ? 3.337  16.682  27.891  1.00 65.36  ?  342 SER A CB    1 
ATOM   2498 O OG    . SER A 1 336 ? 4.317  17.706  27.758  1.00 68.38  ?  342 SER A OG    1 
ATOM   2499 N N     . GLY A 1 337 ? 3.149  13.041  27.119  1.00 61.64  ?  343 GLY A N     1 
ATOM   2500 C CA    . GLY A 1 337 ? 2.413  11.854  27.479  1.00 60.41  ?  343 GLY A CA    1 
ATOM   2501 C C     . GLY A 1 337 ? 1.090  11.650  26.788  1.00 58.68  ?  343 GLY A C     1 
ATOM   2502 O O     . GLY A 1 337 ? 0.393  10.680  27.108  1.00 59.10  ?  343 GLY A O     1 
ATOM   2503 N N     . PHE A 1 338 ? 0.713  12.512  25.857  1.00 60.86  ?  344 PHE A N     1 
ATOM   2504 C CA    . PHE A 1 338 ? -0.447 12.243  25.025  1.00 65.12  ?  344 PHE A CA    1 
ATOM   2505 C C     . PHE A 1 338 ? -0.079 12.246  23.540  1.00 63.55  ?  344 PHE A C     1 
ATOM   2506 O O     . PHE A 1 338 ? 0.917  12.830  23.112  1.00 59.03  ?  344 PHE A O     1 
ATOM   2507 C CB    . PHE A 1 338 ? -1.575 13.244  25.287  1.00 63.79  ?  344 PHE A CB    1 
ATOM   2508 C CG    . PHE A 1 338 ? -1.166 14.684  25.155  1.00 65.54  ?  344 PHE A CG    1 
ATOM   2509 C CD1   . PHE A 1 338 ? -1.046 15.276  23.910  1.00 67.71  ?  344 PHE A CD1   1 
ATOM   2510 C CD2   . PHE A 1 338 ? -0.942 15.455  26.281  1.00 67.09  ?  344 PHE A CD2   1 
ATOM   2511 C CE1   . PHE A 1 338 ? -0.687 16.608  23.791  1.00 70.89  ?  344 PHE A CE1   1 
ATOM   2512 C CE2   . PHE A 1 338 ? -0.583 16.786  26.169  1.00 68.75  ?  344 PHE A CE2   1 
ATOM   2513 C CZ    . PHE A 1 338 ? -0.457 17.365  24.922  1.00 66.01  ?  344 PHE A CZ    1 
ATOM   2514 N N     . TYR A 1 339 ? -0.939 11.601  22.764  1.00 60.76  ?  345 TYR A N     1 
ATOM   2515 C CA    . TYR A 1 339 ? -0.692 11.357  21.357  1.00 57.85  ?  345 TYR A CA    1 
ATOM   2516 C C     . TYR A 1 339 ? -0.822 12.640  20.550  1.00 60.10  ?  345 TYR A C     1 
ATOM   2517 O O     . TYR A 1 339 ? -1.790 13.393  20.702  1.00 58.91  ?  345 TYR A O     1 
ATOM   2518 C CB    . TYR A 1 339 ? -1.687 10.314  20.866  1.00 55.34  ?  345 TYR A CB    1 
ATOM   2519 C CG    . TYR A 1 339 ? -1.624 9.922   19.408  1.00 61.01  ?  345 TYR A CG    1 
ATOM   2520 C CD1   . TYR A 1 339 ? -2.294 10.657  18.433  1.00 57.91  ?  345 TYR A CD1   1 
ATOM   2521 C CD2   . TYR A 1 339 ? -0.950 8.776   19.011  1.00 62.85  ?  345 TYR A CD2   1 
ATOM   2522 C CE1   . TYR A 1 339 ? -2.264 10.281  17.107  1.00 57.30  ?  345 TYR A CE1   1 
ATOM   2523 C CE2   . TYR A 1 339 ? -0.917 8.394   17.683  1.00 64.51  ?  345 TYR A CE2   1 
ATOM   2524 C CZ    . TYR A 1 339 ? -1.575 9.148   16.733  1.00 58.75  ?  345 TYR A CZ    1 
ATOM   2525 O OH    . TYR A 1 339 ? -1.547 8.750   15.409  1.00 63.03  ?  345 TYR A OH    1 
ATOM   2526 N N     . VAL A 1 340 ? 0.151  12.880  19.678  1.00 57.52  ?  346 VAL A N     1 
ATOM   2527 C CA    . VAL A 1 340 ? 0.060  13.930  18.675  1.00 57.41  ?  346 VAL A CA    1 
ATOM   2528 C C     . VAL A 1 340 ? 0.205  13.280  17.305  1.00 55.12  ?  346 VAL A C     1 
ATOM   2529 O O     . VAL A 1 340 ? 0.931  12.292  17.144  1.00 56.72  ?  346 VAL A O     1 
ATOM   2530 C CB    . VAL A 1 340 ? 1.100  15.043  18.919  1.00 56.03  ?  346 VAL A CB    1 
ATOM   2531 C CG1   . VAL A 1 340 ? 0.950  15.584  20.339  1.00 59.19  ?  346 VAL A CG1   1 
ATOM   2532 C CG2   . VAL A 1 340 ? 2.476  14.532  18.715  1.00 56.09  ?  346 VAL A CG2   1 
ATOM   2533 N N     . GLY A 1 341 ? -0.525 13.805  16.329  1.00 54.22  ?  347 GLY A N     1 
ATOM   2534 C CA    . GLY A 1 341 ? -0.717 13.129  15.064  1.00 54.24  ?  347 GLY A CA    1 
ATOM   2535 C C     . GLY A 1 341 ? 0.259  13.543  13.980  1.00 51.82  ?  347 GLY A C     1 
ATOM   2536 O O     . GLY A 1 341 ? 1.255  14.235  14.206  1.00 52.93  ?  347 GLY A O     1 
ATOM   2537 N N     . ARG A 1 342 ? -0.069 13.125  12.762  1.00 52.96  ?  348 ARG A N     1 
ATOM   2538 C CA    . ARG A 1 342 ? 0.871  13.231  11.651  1.00 50.41  ?  348 ARG A CA    1 
ATOM   2539 C C     . ARG A 1 342 ? 1.077  14.684  11.229  1.00 49.40  ?  348 ARG A C     1 
ATOM   2540 O O     . ARG A 1 342 ? 2.215  15.110  11.002  1.00 50.03  ?  348 ARG A O     1 
ATOM   2541 C CB    . ARG A 1 342 ? 0.382  12.366  10.484  1.00 51.68  ?  348 ARG A CB    1 
ATOM   2542 C CG    . ARG A 1 342 ? -0.052 10.960  10.935  1.00 51.49  ?  348 ARG A CG    1 
ATOM   2543 C CD    . ARG A 1 342 ? -0.879 10.231  9.889   1.00 55.72  ?  348 ARG A CD    1 
ATOM   2544 N NE    . ARG A 1 342 ? -0.034 9.622   8.866   1.00 54.34  ?  348 ARG A NE    1 
ATOM   2545 C CZ    . ARG A 1 342 ? -0.489 8.965   7.807   1.00 53.45  ?  348 ARG A CZ    1 
ATOM   2546 N NH1   . ARG A 1 342 ? -1.782 8.829   7.585   1.00 61.81  ?  348 ARG A NH1   1 
ATOM   2547 N NH2   . ARG A 1 342 ? 0.377  8.426   6.951   1.00 54.56  ?  348 ARG A NH2   1 
ATOM   2548 N N     . LEU A 1 343 ? -0.007 15.465  11.112  1.00 49.31  ?  349 LEU A N     1 
ATOM   2549 C CA    . LEU A 1 343 ? 0.145  16.872  10.747  1.00 47.05  ?  349 LEU A CA    1 
ATOM   2550 C C     . LEU A 1 343 ? 1.045  17.584  11.745  1.00 51.25  ?  349 LEU A C     1 
ATOM   2551 O O     . LEU A 1 343 ? 1.979  18.300  11.359  1.00 49.69  ?  349 LEU A O     1 
ATOM   2552 C CB    . LEU A 1 343 ? -1.219 17.555  10.663  1.00 45.40  ?  349 LEU A CB    1 
ATOM   2553 C CG    . LEU A 1 343 ? -1.354 18.905  9.936   1.00 49.53  ?  349 LEU A CG    1 
ATOM   2554 C CD1   . LEU A 1 343 ? -2.806 19.253  9.758   1.00 44.19  ?  349 LEU A CD1   1 
ATOM   2555 C CD2   . LEU A 1 343 ? -0.704 20.029  10.696  1.00 55.16  ?  349 LEU A CD2   1 
ATOM   2556 N N     . MET A 1 344 ? 0.788  17.371  13.039  1.00 51.52  ?  350 MET A N     1 
ATOM   2557 C CA    . MET A 1 344 ? 1.558  18.023  14.086  1.00 48.43  ?  350 MET A CA    1 
ATOM   2558 C C     . MET A 1 344 ? 3.039  17.667  14.000  1.00 47.65  ?  350 MET A C     1 
ATOM   2559 O O     . MET A 1 344 ? 3.905  18.540  14.101  1.00 47.40  ?  350 MET A O     1 
ATOM   2560 C CB    . MET A 1 344 ? 0.997  17.621  15.450  1.00 59.71  ?  350 MET A CB    1 
ATOM   2561 C CG    . MET A 1 344 ? 0.604  18.781  16.321  1.00 66.08  ?  350 MET A CG    1 
ATOM   2562 S SD    . MET A 1 344 ? 2.021  19.839  16.592  1.00 79.82  ?  350 MET A SD    1 
ATOM   2563 C CE    . MET A 1 344 ? 3.162  18.578  17.206  1.00 69.35  ?  350 MET A CE    1 
ATOM   2564 N N     . VAL A 1 345 ? 3.353  16.378  13.871  1.00 47.36  ?  351 VAL A N     1 
ATOM   2565 C CA    . VAL A 1 345 ? 4.757  15.988  13.879  1.00 46.10  ?  351 VAL A CA    1 
ATOM   2566 C C     . VAL A 1 345 ? 5.465  16.486  12.624  1.00 49.54  ?  351 VAL A C     1 
ATOM   2567 O O     . VAL A 1 345 ? 6.657  16.825  12.662  1.00 47.29  ?  351 VAL A O     1 
ATOM   2568 C CB    . VAL A 1 345 ? 4.882  14.465  14.027  1.00 49.68  ?  351 VAL A CB    1 
ATOM   2569 C CG1   . VAL A 1 345 ? 6.330  14.032  13.812  1.00 47.00  ?  351 VAL A CG1   1 
ATOM   2570 C CG2   . VAL A 1 345 ? 4.371  14.017  15.399  1.00 50.64  ?  351 VAL A CG2   1 
ATOM   2571 N N     . ARG A 1 346 ? 4.746  16.543  11.498  1.00 49.09  ?  352 ARG A N     1 
ATOM   2572 C CA    . ARG A 1 346 ? 5.341  17.022  10.260  1.00 45.49  ?  352 ARG A CA    1 
ATOM   2573 C C     . ARG A 1 346 ? 5.756  18.472  10.393  1.00 46.19  ?  352 ARG A C     1 
ATOM   2574 O O     . ARG A 1 346 ? 6.855  18.839  9.966   1.00 49.92  ?  352 ARG A O     1 
ATOM   2575 C CB    . ARG A 1 346 ? 4.363  16.832  9.093   1.00 49.65  ?  352 ARG A CB    1 
ATOM   2576 C CG    . ARG A 1 346 ? 4.837  17.395  7.760   1.00 45.66  ?  352 ARG A CG    1 
ATOM   2577 C CD    . ARG A 1 346 ? 3.896  17.007  6.646   1.00 40.56  ?  352 ARG A CD    1 
ATOM   2578 N NE    . ARG A 1 346 ? 2.582  17.588  6.866   1.00 48.23  ?  352 ARG A NE    1 
ATOM   2579 C CZ    . ARG A 1 346 ? 1.443  16.911  6.951   1.00 49.30  ?  352 ARG A CZ    1 
ATOM   2580 N NH1   . ARG A 1 346 ? 1.395  15.599  6.759   1.00 47.18  ?  352 ARG A NH1   1 
ATOM   2581 N NH2   . ARG A 1 346 ? 0.322  17.571  7.232   1.00 48.04  ?  352 ARG A NH2   1 
ATOM   2582 N N     . LEU A 1 347 ? 4.904  19.308  11.015  1.00 47.08  ?  353 LEU A N     1 
ATOM   2583 C CA    . LEU A 1 347 ? 5.240  20.722  11.193  1.00 45.75  ?  353 LEU A CA    1 
ATOM   2584 C C     . LEU A 1 347 ? 6.282  20.931  12.283  1.00 49.06  ?  353 LEU A C     1 
ATOM   2585 O O     . LEU A 1 347 ? 7.109  21.843  12.180  1.00 51.42  ?  353 LEU A O     1 
ATOM   2586 C CB    . LEU A 1 347 ? 3.999  21.547  11.515  1.00 48.33  ?  353 LEU A CB    1 
ATOM   2587 C CG    . LEU A 1 347 ? 2.945  21.763  10.413  1.00 55.59  ?  353 LEU A CG    1 
ATOM   2588 C CD1   . LEU A 1 347 ? 1.846  22.699  10.916  1.00 56.36  ?  353 LEU A CD1   1 
ATOM   2589 C CD2   . LEU A 1 347 ? 3.538  22.284  9.101   1.00 48.59  ?  353 LEU A CD2   1 
ATOM   2590 N N     . THR A 1 348 ? 6.282  20.098  13.320  1.00 46.37  ?  354 THR A N     1 
ATOM   2591 C CA    . THR A 1 348 ? 7.215  20.331  14.414  1.00 44.93  ?  354 THR A CA    1 
ATOM   2592 C C     . THR A 1 348 ? 8.596  19.758  14.112  1.00 47.54  ?  354 THR A C     1 
ATOM   2593 O O     . THR A 1 348 ? 9.595  20.474  14.180  1.00 55.33  ?  354 THR A O     1 
ATOM   2594 C CB    . THR A 1 348 ? 6.645  19.752  15.703  1.00 49.50  ?  354 THR A CB    1 
ATOM   2595 O OG1   . THR A 1 348 ? 5.340  20.287  15.906  1.00 47.27  ?  354 THR A OG1   1 
ATOM   2596 C CG2   . THR A 1 348 ? 7.504  20.144  16.878  1.00 49.23  ?  354 THR A CG2   1 
ATOM   2597 N N     . LYS A 1 349 ? 8.682  18.483  13.763  1.00 46.87  ?  355 LYS A N     1 
ATOM   2598 C CA    . LYS A 1 349 ? 9.972  17.835  13.548  1.00 46.83  ?  355 LYS A CA    1 
ATOM   2599 C C     . LYS A 1 349 ? 10.308 17.546  12.082  1.00 48.05  ?  355 LYS A C     1 
ATOM   2600 O O     . LYS A 1 349 ? 11.427 17.812  11.658  1.00 45.98  ?  355 LYS A O     1 
ATOM   2601 C CB    . LYS A 1 349 ? 10.025 16.525  14.343  1.00 43.47  ?  355 LYS A CB    1 
ATOM   2602 C CG    . LYS A 1 349 ? 11.415 15.960  14.454  1.00 44.37  ?  355 LYS A CG    1 
ATOM   2603 C CD    . LYS A 1 349 ? 11.421 14.675  15.229  1.00 44.86  ?  355 LYS A CD    1 
ATOM   2604 C CE    . LYS A 1 349 ? 12.708 13.944  15.004  1.00 47.69  ?  355 LYS A CE    1 
ATOM   2605 N NZ    . LYS A 1 349 ? 13.008 13.058  16.144  1.00 54.65  ?  355 LYS A NZ    1 
ATOM   2606 N N     . SER A 1 350 ? 9.370  17.025  11.284  1.00 45.00  ?  356 SER A N     1 
ATOM   2607 C CA    . SER A 1 350 ? 9.730  16.331  10.047  1.00 49.36  ?  356 SER A CA    1 
ATOM   2608 C C     . SER A 1 350 ? 10.171 17.264  8.919   1.00 48.26  ?  356 SER A C     1 
ATOM   2609 O O     . SER A 1 350 ? 10.989 16.875  8.086   1.00 45.68  ?  356 SER A O     1 
ATOM   2610 C CB    . SER A 1 350 ? 8.560  15.471  9.576   1.00 50.84  ?  356 SER A CB    1 
ATOM   2611 O OG    . SER A 1 350 ? 8.299  14.428  10.505  1.00 47.02  ?  356 SER A OG    1 
ATOM   2612 N N     . ARG A 1 351 ? 9.672  18.490  8.874   1.00 50.75  ?  357 ARG A N     1 
ATOM   2613 C CA    . ARG A 1 351 ? 10.106 19.393  7.822   1.00 50.06  ?  357 ARG A CA    1 
ATOM   2614 C C     . ARG A 1 351 ? 11.559 19.811  8.012   1.00 52.02  ?  357 ARG A C     1 
ATOM   2615 O O     . ARG A 1 351 ? 12.387 19.614  7.114   1.00 51.52  ?  357 ARG A O     1 
ATOM   2616 C CB    . ARG A 1 351 ? 9.180  20.603  7.757   1.00 55.10  ?  357 ARG A CB    1 
ATOM   2617 C CG    . ARG A 1 351 ? 7.858  20.295  7.047   1.00 58.17  ?  357 ARG A CG    1 
ATOM   2618 C CD    . ARG A 1 351 ? 7.187  21.536  6.475   1.00 61.35  ?  357 ARG A CD    1 
ATOM   2619 N NE    . ARG A 1 351 ? 8.062  22.311  5.597   1.00 71.55  ?  357 ARG A NE    1 
ATOM   2620 C CZ    . ARG A 1 351 ? 8.847  23.315  5.981   1.00 74.14  ?  357 ARG A CZ    1 
ATOM   2621 N NH1   . ARG A 1 351 ? 8.954  23.669  7.255   1.00 69.02  ?  357 ARG A NH1   1 
ATOM   2622 N NH2   . ARG A 1 351 ? 9.543  23.984  5.063   1.00 77.67  ?  357 ARG A NH2   1 
ATOM   2623 N N     . ASP A 1 352 ? 11.900 20.363  9.186   1.00 51.66  ?  358 ASP A N     1 
ATOM   2624 C CA    . ASP A 1 352 ? 13.212 20.969  9.393   1.00 47.37  ?  358 ASP A CA    1 
ATOM   2625 C C     . ASP A 1 352 ? 14.090 20.238  10.399  1.00 44.85  ?  358 ASP A C     1 
ATOM   2626 O O     . ASP A 1 352 ? 15.238 20.645  10.595  1.00 44.70  ?  358 ASP A O     1 
ATOM   2627 C CB    . ASP A 1 352 ? 13.059 22.433  9.822   1.00 48.04  ?  358 ASP A CB    1 
ATOM   2628 N N     . LEU A 1 353 ? 13.588 19.190  11.050  1.00 44.47  ?  359 LEU A N     1 
ATOM   2629 C CA    . LEU A 1 353 ? 14.354 18.413  12.048  1.00 43.87  ?  359 LEU A CA    1 
ATOM   2630 C C     . LEU A 1 353 ? 15.091 19.308  13.051  1.00 42.23  ?  359 LEU A C     1 
ATOM   2631 O O     . LEU A 1 353 ? 16.188 18.985  13.507  1.00 46.09  ?  359 LEU A O     1 
ATOM   2632 C CB    . LEU A 1 353 ? 15.318 17.442  11.352  1.00 44.04  ?  359 LEU A CB    1 
ATOM   2633 C CG    . LEU A 1 353 ? 14.580 16.350  10.555  1.00 45.42  ?  359 LEU A CG    1 
ATOM   2634 C CD1   . LEU A 1 353 ? 15.403 15.844  9.421   1.00 42.46  ?  359 LEU A CD1   1 
ATOM   2635 C CD2   . LEU A 1 353 ? 14.177 15.189  11.444  1.00 44.27  ?  359 LEU A CD2   1 
ATOM   2636 N N     . PHE A 1 354 ? 14.492 20.441  13.399  1.00 42.40  ?  360 PHE A N     1 
ATOM   2637 C CA    . PHE A 1 354 ? 15.003 21.393  14.392  1.00 43.19  ?  360 PHE A CA    1 
ATOM   2638 C C     . PHE A 1 354 ? 16.361 21.971  14.017  1.00 43.84  ?  360 PHE A C     1 
ATOM   2639 O O     . PHE A 1 354 ? 17.064 22.495  14.884  1.00 45.97  ?  360 PHE A O     1 
ATOM   2640 C CB    . PHE A 1 354 ? 15.093 20.787  15.809  1.00 42.76  ?  360 PHE A CB    1 
ATOM   2641 C CG    . PHE A 1 354 ? 13.853 20.077  16.260  1.00 38.64  ?  360 PHE A CG    1 
ATOM   2642 C CD1   . PHE A 1 354 ? 12.670 20.760  16.445  1.00 40.60  ?  360 PHE A CD1   1 
ATOM   2643 C CD2   . PHE A 1 354 ? 13.885 18.720  16.529  1.00 42.41  ?  360 PHE A CD2   1 
ATOM   2644 C CE1   . PHE A 1 354 ? 11.525 20.099  16.864  1.00 42.27  ?  360 PHE A CE1   1 
ATOM   2645 C CE2   . PHE A 1 354 ? 12.745 18.042  16.956  1.00 44.11  ?  360 PHE A CE2   1 
ATOM   2646 C CZ    . PHE A 1 354 ? 11.563 18.733  17.117  1.00 44.90  ?  360 PHE A CZ    1 
ATOM   2647 N N     . VAL A 1 355 ? 16.737 21.920  12.738  1.00 45.92  ?  361 VAL A N     1 
ATOM   2648 C CA    . VAL A 1 355 ? 18.090 22.309  12.344  1.00 44.18  ?  361 VAL A CA    1 
ATOM   2649 C C     . VAL A 1 355 ? 18.350 23.780  12.663  1.00 43.92  ?  361 VAL A C     1 
ATOM   2650 O O     . VAL A 1 355 ? 19.404 24.133  13.198  1.00 45.73  ?  361 VAL A O     1 
ATOM   2651 C CB    . VAL A 1 355 ? 18.329 21.989  10.853  1.00 45.50  ?  361 VAL A CB    1 
ATOM   2652 C CG1   . VAL A 1 355 ? 19.576 22.668  10.353  1.00 38.53  ?  361 VAL A CG1   1 
ATOM   2653 C CG2   . VAL A 1 355 ? 18.480 20.497  10.669  1.00 45.70  ?  361 VAL A CG2   1 
ATOM   2654 N N     . SER A 1 356 ? 17.393 24.659  12.354  1.00 44.62  ?  362 SER A N     1 
ATOM   2655 C CA    . SER A 1 356 ? 17.610 26.098  12.541  1.00 42.27  ?  362 SER A CA    1 
ATOM   2656 C C     . SER A 1 356 ? 17.916 26.463  13.999  1.00 46.01  ?  362 SER A C     1 
ATOM   2657 O O     . SER A 1 356 ? 18.575 27.477  14.267  1.00 45.68  ?  362 SER A O     1 
ATOM   2658 C CB    . SER A 1 356 ? 16.380 26.856  12.067  1.00 43.41  ?  362 SER A CB    1 
ATOM   2659 O OG    . SER A 1 356 ? 15.263 26.465  12.859  1.00 51.42  ?  362 SER A OG    1 
ATOM   2660 N N     . THR A 1 357 ? 17.447 25.644  14.943  1.00 47.74  ?  363 THR A N     1 
ATOM   2661 C CA    . THR A 1 357 ? 17.654 25.883  16.371  1.00 42.83  ?  363 THR A CA    1 
ATOM   2662 C C     . THR A 1 357 ? 19.131 25.909  16.739  1.00 45.35  ?  363 THR A C     1 
ATOM   2663 O O     . THR A 1 357 ? 19.577 26.772  17.499  1.00 47.39  ?  363 THR A O     1 
ATOM   2664 C CB    . THR A 1 357 ? 16.941 24.789  17.146  1.00 46.26  ?  363 THR A CB    1 
ATOM   2665 O OG1   . THR A 1 357 ? 15.538 24.875  16.879  1.00 47.05  ?  363 THR A OG1   1 
ATOM   2666 C CG2   . THR A 1 357 ? 17.176 24.946  18.612  1.00 59.90  ?  363 THR A CG2   1 
ATOM   2667 N N     . SER A 1 358 ? 19.909 24.961  16.215  1.00 49.37  ?  364 SER A N     1 
ATOM   2668 C CA    . SER A 1 358 ? 21.327 24.896  16.552  1.00 47.18  ?  364 SER A CA    1 
ATOM   2669 C C     . SER A 1 358 ? 22.102 26.046  15.933  1.00 45.80  ?  364 SER A C     1 
ATOM   2670 O O     . SER A 1 358 ? 23.033 26.575  16.551  1.00 47.18  ?  364 SER A O     1 
ATOM   2671 C CB    . SER A 1 358 ? 21.915 23.566  16.098  1.00 45.68  ?  364 SER A CB    1 
ATOM   2672 O OG    . SER A 1 358 ? 21.224 22.497  16.703  1.00 49.18  ?  364 SER A OG    1 
ATOM   2673 N N     . TRP A 1 359 ? 21.746 26.431  14.707  1.00 44.29  ?  365 TRP A N     1 
ATOM   2674 C CA    . TRP A 1 359 ? 22.381 27.584  14.076  1.00 45.11  ?  365 TRP A CA    1 
ATOM   2675 C C     . TRP A 1 359 ? 22.078 28.864  14.846  1.00 44.16  ?  365 TRP A C     1 
ATOM   2676 O O     . TRP A 1 359 ? 22.947 29.730  14.981  1.00 43.70  ?  365 TRP A O     1 
ATOM   2677 C CB    . TRP A 1 359 ? 21.939 27.692  12.602  1.00 44.45  ?  365 TRP A CB    1 
ATOM   2678 C CG    . TRP A 1 359 ? 22.561 26.626  11.779  1.00 45.01  ?  365 TRP A CG    1 
ATOM   2679 C CD1   . TRP A 1 359 ? 22.029 25.410  11.463  1.00 46.30  ?  365 TRP A CD1   1 
ATOM   2680 C CD2   . TRP A 1 359 ? 23.873 26.651  11.198  1.00 46.71  ?  365 TRP A CD2   1 
ATOM   2681 N NE1   . TRP A 1 359 ? 22.929 24.680  10.700  1.00 42.82  ?  365 TRP A NE1   1 
ATOM   2682 C CE2   . TRP A 1 359 ? 24.068 25.420  10.544  1.00 40.34  ?  365 TRP A CE2   1 
ATOM   2683 C CE3   . TRP A 1 359 ? 24.897 27.601  11.162  1.00 47.39  ?  365 TRP A CE3   1 
ATOM   2684 C CZ2   . TRP A 1 359 ? 25.231 25.120  9.881   1.00 43.35  ?  365 TRP A CZ2   1 
ATOM   2685 C CZ3   . TRP A 1 359 ? 26.055 27.294  10.495  1.00 44.30  ?  365 TRP A CZ3   1 
ATOM   2686 C CH2   . TRP A 1 359 ? 26.212 26.068  9.863   1.00 46.53  ?  365 TRP A CH2   1 
ATOM   2687 N N     . LYS A 1 360 ? 20.857 29.004  15.363  1.00 44.59  ?  366 LYS A N     1 
ATOM   2688 C CA    . LYS A 1 360 ? 20.564 30.148  16.220  1.00 47.99  ?  366 LYS A CA    1 
ATOM   2689 C C     . LYS A 1 360 ? 21.425 30.114  17.484  1.00 45.89  ?  366 LYS A C     1 
ATOM   2690 O O     . LYS A 1 360 ? 22.057 31.113  17.841  1.00 46.44  ?  366 LYS A O     1 
ATOM   2691 C CB    . LYS A 1 360 ? 19.068 30.207  16.558  1.00 45.48  ?  366 LYS A CB    1 
ATOM   2692 C CG    . LYS A 1 360 ? 18.669 31.551  17.167  1.00 54.63  ?  366 LYS A CG    1 
ATOM   2693 C CD    . LYS A 1 360 ? 17.164 31.702  17.412  1.00 60.90  ?  366 LYS A CD    1 
ATOM   2694 C CE    . LYS A 1 360 ? 16.789 31.627  18.893  1.00 68.09  ?  366 LYS A CE    1 
ATOM   2695 N NZ    . LYS A 1 360 ? 17.351 32.713  19.781  1.00 75.90  ?  366 LYS A NZ    1 
ATOM   2696 N N     . THR A 1 361 ? 21.493 28.965  18.157  1.00 43.53  ?  367 THR A N     1 
ATOM   2697 C CA    . THR A 1 361 ? 22.307 28.895  19.368  1.00 47.25  ?  367 THR A CA    1 
ATOM   2698 C C     . THR A 1 361 ? 23.753 29.270  19.073  1.00 48.45  ?  367 THR A C     1 
ATOM   2699 O O     . THR A 1 361 ? 24.375 30.028  19.827  1.00 54.11  ?  367 THR A O     1 
ATOM   2700 C CB    . THR A 1 361 ? 22.230 27.491  19.987  1.00 50.41  ?  367 THR A CB    1 
ATOM   2701 O OG1   . THR A 1 361 ? 20.922 27.245  20.517  1.00 47.42  ?  367 THR A OG1   1 
ATOM   2702 C CG2   . THR A 1 361 ? 23.246 27.315  21.092  1.00 41.96  ?  367 THR A CG2   1 
ATOM   2703 N N     . MET A 1 362 ? 24.299 28.760  17.972  1.00 48.95  ?  368 MET A N     1 
ATOM   2704 C CA    . MET A 1 362 ? 25.683 29.015  17.591  1.00 48.46  ?  368 MET A CA    1 
ATOM   2705 C C     . MET A 1 362 ? 25.881 30.385  16.953  1.00 50.79  ?  368 MET A C     1 
ATOM   2706 O O     . MET A 1 362 ? 27.026 30.762  16.685  1.00 50.22  ?  368 MET A O     1 
ATOM   2707 C CB    . MET A 1 362 ? 26.178 27.928  16.633  1.00 43.58  ?  368 MET A CB    1 
ATOM   2708 C CG    . MET A 1 362 ? 26.253 26.543  17.243  1.00 50.24  ?  368 MET A CG    1 
ATOM   2709 S SD    . MET A 1 362 ? 27.553 26.359  18.484  1.00 48.74  ?  368 MET A SD    1 
ATOM   2710 C CE    . MET A 1 362 ? 28.992 26.101  17.462  1.00 43.09  ?  368 MET A CE    1 
ATOM   2711 N N     . ARG A 1 363 ? 24.802 31.134  16.721  1.00 50.34  ?  369 ARG A N     1 
ATOM   2712 C CA    . ARG A 1 363 ? 24.883 32.486  16.178  1.00 46.42  ?  369 ARG A CA    1 
ATOM   2713 C C     . ARG A 1 363 ? 25.581 32.490  14.823  1.00 54.30  ?  369 ARG A C     1 
ATOM   2714 O O     . ARG A 1 363 ? 26.415 33.345  14.528  1.00 57.27  ?  369 ARG A O     1 
ATOM   2715 C CB    . ARG A 1 363 ? 25.568 33.436  17.161  1.00 52.83  ?  369 ARG A CB    1 
ATOM   2716 C CG    . ARG A 1 363 ? 24.665 33.822  18.331  1.00 56.90  ?  369 ARG A CG    1 
ATOM   2717 C CD    . ARG A 1 363 ? 25.383 34.656  19.370  1.00 59.49  ?  369 ARG A CD    1 
ATOM   2718 N NE    . ARG A 1 363 ? 25.993 33.803  20.386  1.00 71.17  ?  369 ARG A NE    1 
ATOM   2719 C CZ    . ARG A 1 363 ? 27.296 33.567  20.512  1.00 72.74  ?  369 ARG A CZ    1 
ATOM   2720 N NH1   . ARG A 1 363 ? 28.189 34.148  19.717  1.00 67.52  ?  369 ARG A NH1   1 
ATOM   2721 N NH2   . ARG A 1 363 ? 27.716 32.734  21.468  1.00 69.45  ?  369 ARG A NH2   1 
ATOM   2722 N N     . GLN A 1 364 ? 25.236 31.521  13.990  1.00 51.68  ?  370 GLN A N     1 
ATOM   2723 C CA    . GLN A 1 364 ? 25.839 31.392  12.681  1.00 48.35  ?  370 GLN A CA    1 
ATOM   2724 C C     . GLN A 1 364 ? 24.736 31.181  11.654  1.00 51.28  ?  370 GLN A C     1 
ATOM   2725 O O     . GLN A 1 364 ? 23.597 30.837  11.982  1.00 51.53  ?  370 GLN A O     1 
ATOM   2726 C CB    . GLN A 1 364 ? 26.836 30.235  12.627  1.00 46.69  ?  370 GLN A CB    1 
ATOM   2727 C CG    . GLN A 1 364 ? 28.171 30.483  13.233  1.00 43.34  ?  370 GLN A CG    1 
ATOM   2728 C CD    . GLN A 1 364 ? 29.062 29.279  13.047  1.00 46.45  ?  370 GLN A CD    1 
ATOM   2729 O OE1   . GLN A 1 364 ? 29.163 28.730  11.940  1.00 45.62  ?  370 GLN A OE1   1 
ATOM   2730 N NE2   . GLN A 1 364 ? 29.710 28.844  14.129  1.00 44.39  ?  370 GLN A NE2   1 
ATOM   2731 N N     . SER A 1 365 ? 25.080 31.401  10.415  1.00 51.17  ?  371 SER A N     1 
ATOM   2732 C CA    . SER A 1 365 ? 24.073 31.130  9.426   1.00 52.85  ?  371 SER A CA    1 
ATOM   2733 C C     . SER A 1 365 ? 24.475 29.909  8.607   1.00 51.21  ?  371 SER A C     1 
ATOM   2734 O O     . SER A 1 365 ? 25.658 29.747  8.275   1.00 47.41  ?  371 SER A O     1 
ATOM   2735 C CB    . SER A 1 365 ? 23.867 32.342  8.507   1.00 54.14  ?  371 SER A CB    1 
ATOM   2736 O OG    . SER A 1 365 ? 23.162 33.383  9.184   1.00 61.46  ?  371 SER A OG    1 
ATOM   2737 N N     . PRO A 1 366 ? 23.528 29.025  8.296   1.00 49.78  ?  372 PRO A N     1 
ATOM   2738 C CA    . PRO A 1 366 ? 23.875 27.820  7.552   1.00 51.87  ?  372 PRO A CA    1 
ATOM   2739 C C     . PRO A 1 366 ? 24.376 28.176  6.165   1.00 52.44  ?  372 PRO A C     1 
ATOM   2740 O O     . PRO A 1 366 ? 24.039 29.243  5.622   1.00 52.95  ?  372 PRO A O     1 
ATOM   2741 C CB    . PRO A 1 366 ? 22.554 27.039  7.501   1.00 50.19  ?  372 PRO A CB    1 
ATOM   2742 C CG    . PRO A 1 366 ? 21.485 28.050  7.750   1.00 46.09  ?  372 PRO A CG    1 
ATOM   2743 C CD    . PRO A 1 366 ? 22.086 29.111  8.598   1.00 50.47  ?  372 PRO A CD    1 
ATOM   2744 N N     . PRO A 1 367 ? 25.211 27.315  5.560   1.00 54.62  ?  373 PRO A N     1 
ATOM   2745 C CA    . PRO A 1 367 ? 25.775 27.495  4.223   1.00 59.33  ?  373 PRO A CA    1 
ATOM   2746 C C     . PRO A 1 367 ? 24.783 27.049  3.163   1.00 67.21  ?  373 PRO A C     1 
ATOM   2747 O O     . PRO A 1 367 ? 24.848 27.460  1.998   1.00 74.52  ?  373 PRO A O     1 
ATOM   2748 C CB    . PRO A 1 367 ? 27.013 26.578  4.221   1.00 59.15  ?  373 PRO A CB    1 
ATOM   2749 C CG    . PRO A 1 367 ? 27.069 25.938  5.593   1.00 57.44  ?  373 PRO A CG    1 
ATOM   2750 C CD    . PRO A 1 367 ? 25.690 26.062  6.163   1.00 56.98  ?  373 PRO A CD    1 
ATOM   2751 O OXT   . PRO A 1 367 ? 23.886 26.249  3.469   1.00 67.94  -1 373 PRO A OXT   1 
HETATM 2752 N N1    . 6FA B 2 .   ? 16.339 14.680  20.968  1.00 52.23  ?  401 6FA A N1    1 
HETATM 2753 C C2    . 6FA B 2 .   ? 15.418 15.671  20.953  1.00 52.20  ?  401 6FA A C2    1 
HETATM 2754 O O2    . 6FA B 2 .   ? 15.401 16.535  21.840  1.00 53.07  ?  401 6FA A O2    1 
HETATM 2755 N N3    . 6FA B 2 .   ? 14.471 15.752  19.980  1.00 48.85  ?  401 6FA A N3    1 
HETATM 2756 C C4    . 6FA B 2 .   ? 14.413 14.856  18.946  1.00 48.91  ?  401 6FA A C4    1 
HETATM 2757 O O4    . 6FA B 2 .   ? 13.542 14.963  18.097  1.00 47.65  ?  401 6FA A O4    1 
HETATM 2758 C C4A   . 6FA B 2 .   ? 15.349 13.816  18.928  1.00 50.64  ?  401 6FA A C4A   1 
HETATM 2759 N N5    . 6FA B 2 .   ? 15.297 12.950  17.954  1.00 51.71  ?  401 6FA A N5    1 
HETATM 2760 C C5A   . 6FA B 2 .   ? 16.187 11.943  17.953  1.00 51.11  ?  401 6FA A C5A   1 
HETATM 2761 C C6    . 6FA B 2 .   ? 16.120 10.989  16.894  1.00 53.78  ?  401 6FA A C6    1 
HETATM 2762 O O6    . 6FA B 2 .   ? 15.162 11.161  15.948  1.00 58.85  ?  401 6FA A O6    1 
HETATM 2763 C C7    . 6FA B 2 .   ? 17.007 9.932   16.867  1.00 50.37  ?  401 6FA A C7    1 
HETATM 2764 C C7M   . 6FA B 2 .   ? 16.948 8.916   15.758  1.00 52.84  ?  401 6FA A C7M   1 
HETATM 2765 C C8    . 6FA B 2 .   ? 17.972 9.795   17.878  1.00 53.30  ?  401 6FA A C8    1 
HETATM 2766 C C8M   . 6FA B 2 .   ? 18.941 8.644   17.847  1.00 50.33  ?  401 6FA A C8M   1 
HETATM 2767 C C9    . 6FA B 2 .   ? 18.060 10.727  18.890  1.00 54.51  ?  401 6FA A C9    1 
HETATM 2768 C C9A   . 6FA B 2 .   ? 17.169 11.808  18.951  1.00 52.27  ?  401 6FA A C9A   1 
HETATM 2769 N N10   . 6FA B 2 .   ? 17.226 12.752  19.967  1.00 52.88  ?  401 6FA A N10   1 
HETATM 2770 C C10   . 6FA B 2 .   ? 16.309 13.791  19.999  1.00 52.60  ?  401 6FA A C10   1 
HETATM 2771 C "C1'" . 6FA B 2 .   ? 18.233 12.601  21.032  1.00 48.77  ?  401 6FA A "C1'" 1 
HETATM 2772 C "C2'" . 6FA B 2 .   ? 19.445 13.469  20.826  1.00 49.26  ?  401 6FA A "C2'" 1 
HETATM 2773 O "O2'" . 6FA B 2 .   ? 20.035 13.146  19.583  1.00 52.01  ?  401 6FA A "O2'" 1 
HETATM 2774 C "C3'" . 6FA B 2 .   ? 20.455 13.237  21.950  1.00 51.84  ?  401 6FA A "C3'" 1 
HETATM 2775 O "O3'" . 6FA B 2 .   ? 19.779 13.009  23.184  1.00 51.86  ?  401 6FA A "O3'" 1 
HETATM 2776 C "C4'" . 6FA B 2 .   ? 21.372 14.441  22.138  1.00 51.29  ?  401 6FA A "C4'" 1 
HETATM 2777 O "O4'" . 6FA B 2 .   ? 22.246 14.537  21.012  1.00 49.53  ?  401 6FA A "O4'" 1 
HETATM 2778 C "C5'" . 6FA B 2 .   ? 22.160 14.362  23.426  1.00 47.59  ?  401 6FA A "C5'" 1 
HETATM 2779 O "O5'" . 6FA B 2 .   ? 22.843 15.626  23.652  1.00 43.71  ?  401 6FA A "O5'" 1 
HETATM 2780 P P     . 6FA B 2 .   ? 24.203 15.616  24.485  1.00 42.64  ?  401 6FA A P     1 
HETATM 2781 O O1P   . 6FA B 2 .   ? 24.825 16.975  24.448  1.00 46.47  -1 401 6FA A O1P   1 
HETATM 2782 O O2P   . 6FA B 2 .   ? 23.937 14.962  25.807  1.00 54.90  ?  401 6FA A O2P   1 
HETATM 2783 O O3P   . 6FA B 2 .   ? 25.111 14.629  23.620  1.00 49.57  ?  401 6FA A O3P   1 
HETATM 2784 P PA    . 6FA B 2 .   ? 25.711 14.712  22.135  1.00 42.22  ?  401 6FA A PA    1 
HETATM 2785 O O1A   . 6FA B 2 .   ? 26.057 13.319  21.722  1.00 53.89  -1 401 6FA A O1A   1 
HETATM 2786 O O2A   . 6FA B 2 .   ? 24.784 15.547  21.325  1.00 43.57  ?  401 6FA A O2A   1 
HETATM 2787 O O5B   . 6FA B 2 .   ? 27.082 15.495  22.341  1.00 43.22  ?  401 6FA A O5B   1 
HETATM 2788 C C5B   . 6FA B 2 .   ? 28.153 14.793  22.991  1.00 42.38  ?  401 6FA A C5B   1 
HETATM 2789 C C4B   . 6FA B 2 .   ? 29.452 15.348  22.475  1.00 43.93  ?  401 6FA A C4B   1 
HETATM 2790 O O4B   . 6FA B 2 .   ? 30.517 14.927  23.359  1.00 44.29  ?  401 6FA A O4B   1 
HETATM 2791 C C3B   . 6FA B 2 .   ? 29.882 14.885  21.072  1.00 44.06  ?  401 6FA A C3B   1 
HETATM 2792 O O3B   . 6FA B 2 .   ? 30.315 15.993  20.301  1.00 43.51  ?  401 6FA A O3B   1 
HETATM 2793 C C2B   . 6FA B 2 .   ? 31.123 14.030  21.352  1.00 52.35  ?  401 6FA A C2B   1 
HETATM 2794 O O2B   . 6FA B 2 .   ? 32.020 13.939  20.263  1.00 52.36  ?  401 6FA A O2B   1 
HETATM 2795 C C1B   . 6FA B 2 .   ? 31.675 14.721  22.596  1.00 47.58  ?  401 6FA A C1B   1 
HETATM 2796 N N9A   . 6FA B 2 .   ? 32.549 13.866  23.386  1.00 51.48  ?  401 6FA A N9A   1 
HETATM 2797 C C8A   . 6FA B 2 .   ? 32.138 12.760  24.083  1.00 49.18  ?  401 6FA A C8A   1 
HETATM 2798 N N7A   . 6FA B 2 .   ? 33.115 12.145  24.694  1.00 54.20  ?  401 6FA A N7A   1 
HETATM 2799 C C5X   . 6FA B 2 .   ? 34.238 12.905  24.404  1.00 52.04  ?  401 6FA A C5X   1 
HETATM 2800 C C6A   . 6FA B 2 .   ? 35.585 12.771  24.785  1.00 55.46  ?  401 6FA A C6A   1 
HETATM 2801 N N6A   . 6FA B 2 .   ? 36.032 11.788  25.560  1.00 57.36  ?  401 6FA A N6A   1 
HETATM 2802 N N1A   . 6FA B 2 .   ? 36.458 13.700  24.329  1.00 57.59  ?  401 6FA A N1A   1 
HETATM 2803 C C2A   . 6FA B 2 .   ? 35.988 14.682  23.548  1.00 55.71  ?  401 6FA A C2A   1 
HETATM 2804 N N3A   . 6FA B 2 .   ? 34.746 14.908  23.123  1.00 53.12  ?  401 6FA A N3A   1 
HETATM 2805 C C4X   . 6FA B 2 .   ? 33.904 13.975  23.598  1.00 50.43  ?  401 6FA A C4X   1 
HETATM 2806 S S     . SO4 C 3 .   ? 13.397 3.398   -11.788 1.00 76.12  ?  402 SO4 A S     1 
HETATM 2807 O O1    . SO4 C 3 .   ? 14.215 2.691   -12.776 1.00 80.55  ?  402 SO4 A O1    1 
HETATM 2808 O O2    . SO4 C 3 .   ? 12.174 3.851   -12.456 1.00 62.72  ?  402 SO4 A O2    1 
HETATM 2809 O O3    . SO4 C 3 .   ? 13.035 2.478   -10.712 1.00 69.01  -1 402 SO4 A O3    1 
HETATM 2810 O O4    . SO4 C 3 .   ? 14.170 4.529   -11.239 1.00 62.77  ?  402 SO4 A O4    1 
HETATM 2811 O O     . HOH D 4 .   ? 26.516 -2.376  3.377   1.00 51.13  ?  501 HOH A O     1 
HETATM 2812 O O     . HOH D 4 .   ? 33.788 18.156  12.811  1.00 48.68  ?  502 HOH A O     1 
HETATM 2813 O O     . HOH D 4 .   ? 29.470 6.973   14.909  1.00 47.67  ?  503 HOH A O     1 
HETATM 2814 O O     . HOH D 4 .   ? 16.746 13.079  -1.301  1.00 50.83  ?  504 HOH A O     1 
HETATM 2815 O O     . HOH D 4 .   ? 28.932 33.487  15.387  1.00 56.59  ?  505 HOH A O     1 
HETATM 2816 O O     . HOH D 4 .   ? 10.377 -1.708  0.015   1.00 48.73  ?  506 HOH A O     1 
HETATM 2817 O O     . HOH D 4 .   ? 28.078 28.724  7.767   1.00 43.86  ?  507 HOH A O     1 
HETATM 2818 O O     . HOH D 4 .   ? 17.378 3.001   -7.208  1.00 49.93  ?  508 HOH A O     1 
HETATM 2819 O O     . HOH D 4 .   ? 7.906  18.340  4.530   1.00 46.63  ?  509 HOH A O     1 
HETATM 2820 O O     . HOH D 4 .   ? 41.428 35.679  44.122  1.00 42.63  ?  510 HOH A O     1 
HETATM 2821 O O     . HOH D 4 .   ? 15.075 3.693   20.035  1.00 61.09  ?  511 HOH A O     1 
HETATM 2822 O O     . HOH D 4 .   ? 37.045 28.317  42.645  1.00 56.35  ?  512 HOH A O     1 
HETATM 2823 O O     . HOH D 4 .   ? 28.485 23.520  7.488   1.00 45.70  ?  513 HOH A O     1 
HETATM 2824 O O     . HOH D 4 .   ? 11.353 -8.637  2.499   1.00 59.74  ?  514 HOH A O     1 
HETATM 2825 O O     . HOH D 4 .   ? 6.428  -5.834  -2.102  1.00 69.09  ?  515 HOH A O     1 
HETATM 2826 O O     . HOH D 4 .   ? -2.151 4.289   23.625  1.00 61.02  ?  516 HOH A O     1 
HETATM 2827 O O     . HOH D 4 .   ? 29.276 11.168  22.244  1.00 45.89  ?  517 HOH A O     1 
HETATM 2828 O O     . HOH D 4 .   ? 30.219 26.440  10.586  1.00 43.10  ?  518 HOH A O     1 
HETATM 2829 O O     . HOH D 4 .   ? 9.826  20.946  11.049  1.00 50.66  ?  519 HOH A O     1 
HETATM 2830 O O     . HOH D 4 .   ? 5.991  8.570   1.344   1.00 46.42  ?  520 HOH A O     1 
HETATM 2831 O O     . HOH D 4 .   ? 23.266 5.496   15.661  1.00 51.37  ?  521 HOH A O     1 
HETATM 2832 O O     . HOH D 4 .   ? 21.240 7.198   25.256  1.00 57.50  ?  522 HOH A O     1 
HETATM 2833 O O     . HOH D 4 .   ? 20.366 32.745  9.924   1.00 56.98  ?  523 HOH A O     1 
HETATM 2834 O O     . HOH D 4 .   ? 27.840 32.295  9.713   1.00 46.26  ?  524 HOH A O     1 
HETATM 2835 O O     . HOH D 4 .   ? 36.617 33.244  28.934  1.00 53.79  ?  525 HOH A O     1 
HETATM 2836 O O     . HOH D 4 .   ? 15.219 18.883  4.543   1.00 60.24  ?  526 HOH A O     1 
HETATM 2837 O O     . HOH D 4 .   ? 34.258 33.952  28.594  1.00 58.40  ?  527 HOH A O     1 
HETATM 2838 O O     . HOH D 4 .   ? 24.978 12.805  -3.817  1.00 50.52  ?  528 HOH A O     1 
HETATM 2839 O O     . HOH D 4 .   ? -0.659 -5.186  14.170  1.00 61.59  ?  529 HOH A O     1 
HETATM 2840 O O     . HOH D 4 .   ? 30.300 23.956  4.944   1.00 46.58  ?  530 HOH A O     1 
HETATM 2841 O O     . HOH D 4 .   ? 29.610 26.250  8.133   1.00 50.78  ?  531 HOH A O     1 
HETATM 2842 O O     . HOH D 4 .   ? 17.711 4.548   37.218  1.00 61.15  ?  532 HOH A O     1 
HETATM 2843 O O     . HOH D 4 .   ? 19.001 2.051   37.652  1.00 57.41  ?  533 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 1   ? 1.0280 0.7145 0.7342 0.0079  -0.1038 -0.0264 7   PRO A N   
2    C CA  . PRO A 1   ? 0.9647 0.6404 0.6559 0.0067  -0.1090 -0.0265 7   PRO A CA  
3    C C   . PRO A 1   ? 0.9296 0.6008 0.6202 0.0011  -0.1102 -0.0299 7   PRO A C   
4    O O   . PRO A 1   ? 0.9640 0.6431 0.6581 -0.0046 -0.1168 -0.0303 7   PRO A O   
5    C CB  . PRO A 1   ? 0.8613 0.5464 0.5505 0.0046  -0.1185 -0.0236 7   PRO A CB  
6    C CG  . PRO A 1   ? 0.9558 0.6550 0.6579 0.0066  -0.1172 -0.0213 7   PRO A CG  
7    C CD  . PRO A 1   ? 0.9450 0.6470 0.6594 0.0061  -0.1095 -0.0240 7   PRO A CD  
8    N N   . HIS A 2   ? 0.8890 0.5480 0.5757 0.0027  -0.1037 -0.0323 8   HIS A N   
9    C CA  . HIS A 2   ? 0.8945 0.5506 0.5832 -0.0024 -0.1039 -0.0353 8   HIS A CA  
10   C C   . HIS A 2   ? 0.9222 0.5661 0.5975 -0.0046 -0.1079 -0.0364 8   HIS A C   
11   O O   . HIS A 2   ? 0.8998 0.5423 0.5768 -0.0094 -0.1096 -0.0384 8   HIS A O   
12   C CB  . HIS A 2   ? 0.9152 0.5673 0.6102 -0.0005 -0.0945 -0.0375 8   HIS A CB  
13   C CG  . HIS A 2   ? 0.9774 0.6436 0.6881 -0.0022 -0.0920 -0.0377 8   HIS A CG  
14   N ND1 . HIS A 2   ? 0.9983 0.6710 0.7156 0.0019  -0.0875 -0.0362 8   HIS A ND1 
15   C CD2 . HIS A 2   ? 0.9415 0.6173 0.6626 -0.0080 -0.0937 -0.0390 8   HIS A CD2 
16   C CE1 . HIS A 2   ? 1.0175 0.7028 0.7485 -0.0014 -0.0862 -0.0370 8   HIS A CE1 
17   N NE2 . HIS A 2   ? 0.9990 0.6867 0.7325 -0.0074 -0.0900 -0.0386 8   HIS A NE2 
18   N N   . MET A 3   ? 0.8739 0.5092 0.5363 -0.0013 -0.1094 -0.0351 9   MET A N   
19   C CA  . MET A 3   ? 0.8594 0.4843 0.5084 -0.0038 -0.1142 -0.0360 9   MET A CA  
20   C C   . MET A 3   ? 0.8363 0.4502 0.4834 -0.0059 -0.1104 -0.0393 9   MET A C   
21   O O   . MET A 3   ? 0.8299 0.4416 0.4741 -0.0110 -0.1151 -0.0407 9   MET A O   
22   C CB  . MET A 3   ? 0.8198 0.4541 0.4688 -0.0094 -0.1240 -0.0351 9   MET A CB  
23   C CG  . MET A 3   ? 0.8489 0.4953 0.5010 -0.0076 -0.1279 -0.0316 9   MET A CG  
24   S SD  . MET A 3   ? 1.0156 0.6696 0.6623 -0.0132 -0.1398 -0.0302 9   MET A SD  
25   C CE  . MET A 3   ? 0.9312 0.6013 0.5866 -0.0099 -0.1417 -0.0261 9   MET A CE  
26   N N   . GLY A 4   ? 0.8183 0.4251 0.4670 -0.0018 -0.1018 -0.0405 10  GLY A N   
27   C CA  . GLY A 4   ? 0.8230 0.4188 0.4700 -0.0027 -0.0971 -0.0433 10  GLY A CA  
28   C C   . GLY A 4   ? 0.9321 0.5352 0.5928 -0.0058 -0.0944 -0.0446 10  GLY A C   
29   O O   . GLY A 4   ? 0.9814 0.5769 0.6434 -0.0047 -0.0879 -0.0465 10  GLY A O   
30   N N   . ALA A 5   ? 0.9210 0.5390 0.5923 -0.0099 -0.0992 -0.0437 11  ALA A N   
31   C CA  . ALA A 5   ? 0.9299 0.5555 0.6138 -0.0138 -0.0975 -0.0448 11  ALA A CA  
32   C C   . ALA A 5   ? 0.9980 0.6271 0.6911 -0.0103 -0.0890 -0.0452 11  ALA A C   
33   O O   . ALA A 5   ? 1.0305 0.6585 0.7218 -0.0051 -0.0850 -0.0443 11  ALA A O   
34   C CB  . ALA A 5   ? 0.8884 0.5295 0.5809 -0.0191 -0.1050 -0.0437 11  ALA A CB  
35   N N   . LEU A 6   ? 0.9747 0.6079 0.6775 -0.0134 -0.0861 -0.0465 12  LEU A N   
36   C CA  . LEU A 6   ? 0.9487 0.5860 0.6609 -0.0113 -0.0780 -0.0473 12  LEU A CA  
37   C C   . LEU A 6   ? 0.9616 0.6165 0.6872 -0.0146 -0.0800 -0.0465 12  LEU A C   
38   O O   . LEU A 6   ? 0.9413 0.6047 0.6715 -0.0201 -0.0866 -0.0460 12  LEU A O   
39   C CB  . LEU A 6   ? 0.9374 0.5685 0.6521 -0.0126 -0.0729 -0.0491 12  LEU A CB  
40   C CG  . LEU A 6   ? 0.9554 0.5689 0.6589 -0.0092 -0.0688 -0.0504 12  LEU A CG  
41   C CD1 . LEU A 6   ? 0.8962 0.5072 0.6056 -0.0106 -0.0631 -0.0520 12  LEU A CD1 
42   C CD2 . LEU A 6   ? 1.0003 0.6063 0.6966 -0.0025 -0.0636 -0.0502 12  LEU A CD2 
43   N N   . HIS A 7   ? 0.9531 0.6133 0.6850 -0.0113 -0.0742 -0.0463 13  HIS A N   
44   C CA  . HIS A 7   ? 0.9437 0.6199 0.6899 -0.0146 -0.0735 -0.0464 13  HIS A CA  
45   C C   . HIS A 7   ? 0.9494 0.6245 0.7005 -0.0109 -0.0634 -0.0476 13  HIS A C   
46   O O   . HIS A 7   ? 0.9499 0.6213 0.6975 -0.0053 -0.0596 -0.0469 13  HIS A O   
47   C CB  . HIS A 7   ? 0.9129 0.6001 0.6620 -0.0152 -0.0793 -0.0444 13  HIS A CB  
48   C CG  . HIS A 7   ? 1.0403 0.7441 0.8036 -0.0200 -0.0802 -0.0446 13  HIS A CG  
49   N ND1 . HIS A 7   ? 1.0692 0.7779 0.8421 -0.0228 -0.0748 -0.0464 13  HIS A ND1 
50   C CD2 . HIS A 7   ? 1.1039 0.8209 0.8736 -0.0228 -0.0858 -0.0434 13  HIS A CD2 
51   C CE1 . HIS A 7   ? 0.9813 0.7054 0.7657 -0.0273 -0.0769 -0.0463 13  HIS A CE1 
52   N NE2 . HIS A 7   ? 1.1549 0.8842 0.9377 -0.0273 -0.0835 -0.0445 13  HIS A NE2 
53   N N   . VAL A 8   ? 0.8978 0.5753 0.6562 -0.0138 -0.0589 -0.0493 14  VAL A N   
54   C CA  . VAL A 8   ? 0.8906 0.5669 0.6537 -0.0109 -0.0491 -0.0508 14  VAL A CA  
55   C C   . VAL A 8   ? 0.8681 0.5606 0.6449 -0.0139 -0.0471 -0.0511 14  VAL A C   
56   O O   . VAL A 8   ? 0.8679 0.5718 0.6527 -0.0199 -0.0517 -0.0510 14  VAL A O   
57   C CB  . VAL A 8   ? 0.8387 0.5076 0.6012 -0.0121 -0.0446 -0.0525 14  VAL A CB  
58   C CG1 . VAL A 8   ? 0.7981 0.4664 0.5655 -0.0093 -0.0343 -0.0541 14  VAL A CG1 
59   C CG2 . VAL A 8   ? 0.8464 0.4990 0.5952 -0.0091 -0.0462 -0.0523 14  VAL A CG2 
60   N N   . VAL A 9   ? 0.8256 0.5191 0.6053 -0.0097 -0.0403 -0.0515 15  VAL A N   
61   C CA  . VAL A 9   ? 0.8409 0.5486 0.6335 -0.0121 -0.0368 -0.0522 15  VAL A CA  
62   C C   . VAL A 9   ? 0.8353 0.5407 0.6321 -0.0110 -0.0265 -0.0545 15  VAL A C   
63   O O   . VAL A 9   ? 0.8031 0.4968 0.5930 -0.0053 -0.0205 -0.0549 15  VAL A O   
64   C CB  . VAL A 9   ? 0.8406 0.5528 0.6344 -0.0084 -0.0372 -0.0506 15  VAL A CB  
65   C CG1 . VAL A 9   ? 0.7924 0.5176 0.5996 -0.0104 -0.0316 -0.0519 15  VAL A CG1 
66   C CG2 . VAL A 9   ? 0.8448 0.5617 0.6360 -0.0105 -0.0477 -0.0484 15  VAL A CG2 
67   N N   . ILE A 10  ? 0.7735 0.4898 0.5811 -0.0168 -0.0247 -0.0560 16  ILE A N   
68   C CA  . ILE A 10  ? 0.7605 0.4773 0.5736 -0.0170 -0.0151 -0.0584 16  ILE A CA  
69   C C   . ILE A 10  ? 0.7696 0.4988 0.5934 -0.0180 -0.0106 -0.0593 16  ILE A C   
70   O O   . ILE A 10  ? 0.8081 0.5511 0.6409 -0.0236 -0.0145 -0.0592 16  ILE A O   
71   C CB  . ILE A 10  ? 0.7599 0.4808 0.5777 -0.0231 -0.0158 -0.0593 16  ILE A CB  
72   C CG1 . ILE A 10  ? 0.7570 0.4658 0.5645 -0.0222 -0.0211 -0.0581 16  ILE A CG1 
73   C CG2 . ILE A 10  ? 0.6855 0.4064 0.5081 -0.0232 -0.0059 -0.0616 16  ILE A CG2 
74   C CD1 . ILE A 10  ? 0.7588 0.4706 0.5703 -0.0276 -0.0225 -0.0583 16  ILE A CD1 
75   N N   . VAL A 11  ? 0.7887 0.5127 0.6116 -0.0127 -0.0025 -0.0602 17  VAL A N   
76   C CA  . VAL A 11  ? 0.8075 0.5423 0.6409 -0.0135 0.0032  -0.0614 17  VAL A CA  
77   C C   . VAL A 11  ? 0.7103 0.4478 0.5501 -0.0163 0.0122  -0.0644 17  VAL A C   
78   O O   . VAL A 11  ? 0.7186 0.4454 0.5532 -0.0122 0.0192  -0.0655 17  VAL A O   
79   C CB  . VAL A 11  ? 0.8475 0.5764 0.6772 -0.0062 0.0069  -0.0603 17  VAL A CB  
80   C CG1 . VAL A 11  ? 0.8254 0.5642 0.6664 -0.0072 0.0145  -0.0621 17  VAL A CG1 
81   C CG2 . VAL A 11  ? 0.8396 0.5693 0.6650 -0.0045 -0.0024 -0.0571 17  VAL A CG2 
82   N N   . GLY A 12  ? 0.7560 0.5082 0.6069 -0.0235 0.0117  -0.0657 18  GLY A N   
83   C CA  . GLY A 12  ? 0.7498 0.5076 0.6081 -0.0277 0.0193  -0.0685 18  GLY A CA  
84   C C   . GLY A 12  ? 0.7419 0.5031 0.6015 -0.0337 0.0151  -0.0683 18  GLY A C   
85   O O   . GLY A 12  ? 0.7496 0.5001 0.6006 -0.0317 0.0119  -0.0671 18  GLY A O   
86   N N   . GLY A 13  ? 0.6917 0.4681 0.5623 -0.0412 0.0151  -0.0695 19  GLY A N   
87   C CA  . GLY A 13  ? 0.6300 0.4112 0.5029 -0.0474 0.0107  -0.0689 19  GLY A CA  
88   C C   . GLY A 13  ? 0.6591 0.4443 0.5376 -0.0509 0.0186  -0.0711 19  GLY A C   
89   O O   . GLY A 13  ? 0.7599 0.5584 0.6473 -0.0583 0.0175  -0.0715 19  GLY A O   
90   N N   . GLY A 14  ? 0.6130 0.3872 0.4864 -0.0458 0.0266  -0.0725 20  GLY A N   
91   C CA  . GLY A 14  ? 0.5923 0.3683 0.4694 -0.0485 0.0343  -0.0745 20  GLY A CA  
92   C C   . GLY A 14  ? 0.6008 0.3691 0.4726 -0.0485 0.0317  -0.0730 20  GLY A C   
93   O O   . GLY A 14  ? 0.6123 0.3781 0.4804 -0.0490 0.0230  -0.0705 20  GLY A O   
94   N N   . PHE A 15  ? 0.6002 0.3646 0.4718 -0.0479 0.0396  -0.0747 21  PHE A N   
95   C CA  . PHE A 15  ? 0.6404 0.3970 0.5074 -0.0475 0.0383  -0.0733 21  PHE A CA  
96   C C   . PHE A 15  ? 0.6595 0.3996 0.5143 -0.0409 0.0333  -0.0714 21  PHE A C   
97   O O   . PHE A 15  ? 0.6705 0.4075 0.5225 -0.0421 0.0268  -0.0692 21  PHE A O   
98   C CB  . PHE A 15  ? 0.6499 0.4035 0.5176 -0.0468 0.0485  -0.0756 21  PHE A CB  
99   C CG  . PHE A 15  ? 0.6360 0.4057 0.5151 -0.0544 0.0525  -0.0771 21  PHE A CG  
100  C CD1 . PHE A 15  ? 0.6748 0.4533 0.5603 -0.0563 0.0589  -0.0799 21  PHE A CD1 
101  C CD2 . PHE A 15  ? 0.7011 0.4779 0.5849 -0.0600 0.0499  -0.0756 21  PHE A CD2 
102  C CE1 . PHE A 15  ? 0.6778 0.4719 0.5738 -0.0641 0.0628  -0.0815 21  PHE A CE1 
103  C CE2 . PHE A 15  ? 0.6778 0.4706 0.5721 -0.0677 0.0534  -0.0768 21  PHE A CE2 
104  C CZ  . PHE A 15  ? 0.6065 0.4078 0.5067 -0.0698 0.0600  -0.0800 21  PHE A CZ  
105  N N   . GLY A 16  ? 0.6377 0.3673 0.4852 -0.0340 0.0362  -0.0721 22  GLY A N   
106  C CA  . GLY A 16  ? 0.6529 0.3675 0.4886 -0.0281 0.0314  -0.0704 22  GLY A CA  
107  C C   . GLY A 16  ? 0.6468 0.3650 0.4815 -0.0298 0.0208  -0.0680 22  GLY A C   
108  O O   . GLY A 16  ? 0.7117 0.4239 0.5411 -0.0300 0.0143  -0.0661 22  GLY A O   
109  N N   . GLY A 17  ? 0.6486 0.3765 0.4885 -0.0312 0.0191  -0.0681 23  GLY A N   
110  C CA  . GLY A 17  ? 0.6580 0.3901 0.4974 -0.0328 0.0092  -0.0660 23  GLY A CA  
111  C C   . GLY A 17  ? 0.6907 0.4295 0.5336 -0.0391 0.0019  -0.0644 23  GLY A C   
112  O O   . GLY A 17  ? 0.7715 0.5056 0.6087 -0.0386 -0.0062 -0.0624 23  GLY A O   
113  N N   . ILE A 18  ? 0.6280 0.3780 0.4805 -0.0452 0.0044  -0.0651 24  ILE A N   
114  C CA  . ILE A 18  ? 0.6451 0.4018 0.5015 -0.0512 -0.0027 -0.0632 24  ILE A CA  
115  C C   . ILE A 18  ? 0.6214 0.3653 0.4704 -0.0489 -0.0035 -0.0620 24  ILE A C   
116  O O   . ILE A 18  ? 0.6569 0.4002 0.5047 -0.0514 -0.0109 -0.0599 24  ILE A O   
117  C CB  . ILE A 18  ? 0.6355 0.4093 0.5046 -0.0591 -0.0006 -0.0639 24  ILE A CB  
118  C CG1 . ILE A 18  ? 0.6351 0.4079 0.5067 -0.0589 0.0092  -0.0658 24  ILE A CG1 
119  C CG2 . ILE A 18  ? 0.6215 0.4090 0.4984 -0.0624 -0.0010 -0.0649 24  ILE A CG2 
120  C CD1 . ILE A 18  ? 0.6570 0.4408 0.5371 -0.0658 0.0094  -0.0652 24  ILE A CD1 
121  N N   . ALA A 19  ? 0.6384 0.3718 0.4827 -0.0444 0.0041  -0.0634 25  ALA A N   
122  C CA  . ALA A 19  ? 0.6538 0.3730 0.4899 -0.0412 0.0035  -0.0624 25  ALA A CA  
123  C C   . ALA A 19  ? 0.7262 0.4333 0.5513 -0.0367 -0.0028 -0.0612 25  ALA A C   
124  O O   . ALA A 19  ? 0.7749 0.4758 0.5957 -0.0373 -0.0082 -0.0596 25  ALA A O   
125  C CB  . ALA A 19  ? 0.6484 0.3587 0.4813 -0.0369 0.0133  -0.0644 25  ALA A CB  
126  N N   . ALA A 20  ? 0.7053 0.4091 0.5257 -0.0324 -0.0022 -0.0619 26  ALA A N   
127  C CA  . ALA A 20  ? 0.7418 0.4347 0.5514 -0.0283 -0.0082 -0.0607 26  ALA A CA  
128  C C   . ALA A 20  ? 0.7601 0.4611 0.5721 -0.0329 -0.0182 -0.0588 26  ALA A C   
129  O O   . ALA A 20  ? 0.7463 0.4394 0.5509 -0.0323 -0.0244 -0.0574 26  ALA A O   
130  C CB  . ALA A 20  ? 0.7340 0.4219 0.5385 -0.0224 -0.0046 -0.0615 26  ALA A CB  
131  N N   . ALA A 21  ? 0.7645 0.4815 0.5868 -0.0377 -0.0198 -0.0588 27  ALA A N   
132  C CA  . ALA A 21  ? 0.7431 0.4687 0.5683 -0.0424 -0.0292 -0.0571 27  ALA A CA  
133  C C   . ALA A 21  ? 0.7684 0.4935 0.5946 -0.0467 -0.0336 -0.0556 27  ALA A C   
134  O O   . ALA A 21  ? 0.8047 0.5275 0.6269 -0.0480 -0.0415 -0.0540 27  ALA A O   
135  C CB  . ALA A 21  ? 0.7204 0.4636 0.5572 -0.0471 -0.0290 -0.0576 27  ALA A CB  
136  N N   . SER A 22  ? 0.7592 0.4859 0.5905 -0.0487 -0.0285 -0.0560 28  SER A N   
137  C CA  . SER A 22  ? 0.7701 0.4971 0.6036 -0.0527 -0.0322 -0.0542 28  SER A CA  
138  C C   . SER A 22  ? 0.7621 0.4716 0.5843 -0.0484 -0.0339 -0.0536 28  SER A C   
139  O O   . SER A 22  ? 0.7898 0.4976 0.6109 -0.0510 -0.0401 -0.0518 28  SER A O   
140  C CB  . SER A 22  ? 0.7965 0.5306 0.6388 -0.0560 -0.0261 -0.0545 28  SER A CB  
141  O OG  . SER A 22  ? 0.9071 0.6583 0.7606 -0.0634 -0.0296 -0.0535 28  SER A OG  
142  N N   . GLN A 23  ? 0.8206 0.5171 0.6344 -0.0420 -0.0281 -0.0551 29  GLN A N   
143  C CA  . GLN A 23  ? 0.8075 0.4869 0.6097 -0.0377 -0.0294 -0.0548 29  GLN A CA  
144  C C   . GLN A 23  ? 0.8295 0.5051 0.6243 -0.0373 -0.0376 -0.0538 29  GLN A C   
145  O O   . GLN A 23  ? 0.8144 0.4842 0.6052 -0.0387 -0.0430 -0.0526 29  GLN A O   
146  C CB  . GLN A 23  ? 0.8237 0.4909 0.6186 -0.0311 -0.0214 -0.0567 29  GLN A CB  
147  C CG  . GLN A 23  ? 0.9723 0.6224 0.7569 -0.0274 -0.0209 -0.0566 29  GLN A CG  
148  C CD  . GLN A 23  ? 1.0649 0.7131 0.8538 -0.0285 -0.0158 -0.0566 29  GLN A CD  
149  O OE1 . GLN A 23  ? 1.0518 0.7043 0.8460 -0.0281 -0.0085 -0.0578 29  GLN A OE1 
150  N NE2 . GLN A 23  ? 1.0243 0.6663 0.8111 -0.0299 -0.0193 -0.0553 29  GLN A NE2 
151  N N   . LEU A 24  ? 0.8157 0.4949 0.6090 -0.0353 -0.0386 -0.0544 30  LEU A N   
152  C CA  . LEU A 24  ? 0.7862 0.4640 0.5733 -0.0352 -0.0466 -0.0534 30  LEU A CA  
153  C C   . LEU A 24  ? 0.7766 0.4644 0.5697 -0.0418 -0.0545 -0.0518 30  LEU A C   
154  O O   . LEU A 24  ? 0.8311 0.5141 0.6178 -0.0425 -0.0614 -0.0508 30  LEU A O   
155  C CB  . LEU A 24  ? 0.7590 0.4425 0.5465 -0.0327 -0.0458 -0.0538 30  LEU A CB  
156  C CG  . LEU A 24  ? 0.8094 0.4819 0.5895 -0.0256 -0.0387 -0.0551 30  LEU A CG  
157  C CD1 . LEU A 24  ? 0.8150 0.4960 0.5997 -0.0239 -0.0359 -0.0555 30  LEU A CD1 
158  C CD2 . LEU A 24  ? 0.8027 0.4600 0.5685 -0.0213 -0.0422 -0.0546 30  LEU A CD2 
159  N N   . GLN A 25  ? 0.7788 0.4811 0.5842 -0.0470 -0.0538 -0.0515 31  GLN A N   
160  C CA  . GLN A 25  ? 0.7873 0.4992 0.5986 -0.0534 -0.0612 -0.0498 31  GLN A CA  
161  C C   . GLN A 25  ? 0.8004 0.5037 0.6089 -0.0548 -0.0633 -0.0486 31  GLN A C   
162  O O   . GLN A 25  ? 0.8885 0.5926 0.6959 -0.0581 -0.0707 -0.0472 31  GLN A O   
163  C CB  . GLN A 25  ? 0.7718 0.5015 0.5969 -0.0589 -0.0597 -0.0497 31  GLN A CB  
164  C CG  . GLN A 25  ? 0.8080 0.5494 0.6393 -0.0656 -0.0679 -0.0480 31  GLN A CG  
165  C CD  . GLN A 25  ? 0.8877 0.6475 0.7314 -0.0707 -0.0670 -0.0483 31  GLN A CD  
166  O OE1 . GLN A 25  ? 0.8169 0.5839 0.6688 -0.0739 -0.0628 -0.0483 31  GLN A OE1 
167  N NE2 . GLN A 25  ? 0.8688 0.6367 0.7141 -0.0718 -0.0711 -0.0485 31  GLN A NE2 
168  N N   . ALA A 26  ? 0.7880 0.4825 0.5949 -0.0521 -0.0568 -0.0491 32  ALA A N   
169  C CA  . ALA A 26  ? 0.7531 0.4387 0.5576 -0.0530 -0.0581 -0.0479 32  ALA A CA  
170  C C   . ALA A 26  ? 0.7977 0.4675 0.5891 -0.0495 -0.0615 -0.0481 32  ALA A C   
171  O O   . ALA A 26  ? 0.8201 0.4847 0.6095 -0.0516 -0.0656 -0.0469 32  ALA A O   
172  C CB  . ALA A 26  ? 0.6844 0.3655 0.4913 -0.0510 -0.0499 -0.0483 32  ALA A CB  
173  N N   . LEU A 27  ? 0.8461 0.5078 0.6283 -0.0442 -0.0597 -0.0497 33  LEU A N   
174  C CA  . LEU A 27  ? 0.8691 0.5163 0.6380 -0.0410 -0.0629 -0.0501 33  LEU A CA  
175  C C   . LEU A 27  ? 0.8868 0.5390 0.6530 -0.0433 -0.0714 -0.0494 33  LEU A C   
176  O O   . LEU A 27  ? 0.9533 0.5947 0.7085 -0.0414 -0.0747 -0.0497 33  LEU A O   
177  C CB  . LEU A 27  ? 0.8758 0.5118 0.6356 -0.0342 -0.0568 -0.0519 33  LEU A CB  
178  C CG  . LEU A 27  ? 0.8472 0.4793 0.6097 -0.0314 -0.0476 -0.0529 33  LEU A CG  
179  C CD1 . LEU A 27  ? 0.8510 0.4792 0.6084 -0.0257 -0.0423 -0.0544 33  LEU A CD1 
180  C CD2 . LEU A 27  ? 0.7684 0.3863 0.5253 -0.0299 -0.0455 -0.0531 33  LEU A CD2 
181  N N   . ASN A 28  ? 0.9017 0.5701 0.6774 -0.0475 -0.0747 -0.0486 34  ASN A N   
182  C CA  . ASN A 28  ? 0.9352 0.6101 0.7096 -0.0500 -0.0827 -0.0479 34  ASN A CA  
183  C C   . ASN A 28  ? 0.9302 0.5998 0.6952 -0.0449 -0.0829 -0.0487 34  ASN A C   
184  O O   . ASN A 28  ? 0.9452 0.6134 0.7039 -0.0456 -0.0894 -0.0482 34  ASN A O   
185  C CB  . ASN A 28  ? 0.9497 0.6201 0.7204 -0.0536 -0.0896 -0.0469 34  ASN A CB  
186  C CG  . ASN A 28  ? 1.0787 0.7601 0.8521 -0.0581 -0.0979 -0.0459 34  ASN A CG  
187  O OD1 . ASN A 28  ? 1.0552 0.7499 0.8356 -0.0594 -0.0985 -0.0458 34  ASN A OD1 
188  N ND2 . ASN A 28  ? 1.1673 0.8433 0.9350 -0.0607 -0.1042 -0.0453 34  ASN A ND2 
189  N N   . VAL A 29  ? 0.8571 0.5239 0.6214 -0.0401 -0.0756 -0.0497 35  VAL A N   
190  C CA  . VAL A 29  ? 0.8416 0.5048 0.5986 -0.0350 -0.0750 -0.0501 35  VAL A CA  
191  C C   . VAL A 29  ? 0.9086 0.5878 0.6742 -0.0369 -0.0771 -0.0495 35  VAL A C   
192  O O   . VAL A 29  ? 0.8818 0.5720 0.6587 -0.0393 -0.0736 -0.0498 35  VAL A O   
193  C CB  . VAL A 29  ? 0.8562 0.5098 0.6093 -0.0291 -0.0660 -0.0514 35  VAL A CB  
194  C CG1 . VAL A 29  ? 0.8432 0.4950 0.5905 -0.0241 -0.0650 -0.0513 35  VAL A CG1 
195  C CG2 . VAL A 29  ? 0.8253 0.4626 0.5693 -0.0270 -0.0639 -0.0521 35  VAL A CG2 
196  N N   . PRO A 30  ? 0.9285 0.6096 0.6894 -0.0360 -0.0825 -0.0486 36  PRO A N   
197  C CA  . PRO A 30  ? 0.9110 0.6071 0.6805 -0.0374 -0.0841 -0.0480 36  PRO A CA  
198  C C   . PRO A 30  ? 0.8687 0.5668 0.6427 -0.0333 -0.0755 -0.0489 36  PRO A C   
199  O O   . PRO A 30  ? 0.8646 0.5517 0.6310 -0.0275 -0.0705 -0.0494 36  PRO A O   
200  C CB  . PRO A 30  ? 0.9177 0.6121 0.6788 -0.0358 -0.0907 -0.0468 36  PRO A CB  
201  C CG  . PRO A 30  ? 0.9840 0.6656 0.7341 -0.0362 -0.0945 -0.0468 36  PRO A CG  
202  C CD  . PRO A 30  ? 0.9105 0.5808 0.6584 -0.0341 -0.0876 -0.0481 36  PRO A CD  
203  N N   . PHE A 31  ? 0.8570 0.5694 0.6434 -0.0366 -0.0737 -0.0492 37  PHE A N   
204  C CA  . PHE A 31  ? 0.8466 0.5615 0.6380 -0.0333 -0.0651 -0.0503 37  PHE A CA  
205  C C   . PHE A 31  ? 0.8145 0.5469 0.6187 -0.0373 -0.0656 -0.0504 37  PHE A C   
206  O O   . PHE A 31  ? 0.8397 0.5822 0.6502 -0.0434 -0.0712 -0.0499 37  PHE A O   
207  C CB  . PHE A 31  ? 0.8487 0.5575 0.6415 -0.0326 -0.0573 -0.0519 37  PHE A CB  
208  C CG  . PHE A 31  ? 0.8063 0.5260 0.6101 -0.0391 -0.0571 -0.0522 37  PHE A CG  
209  C CD1 . PHE A 31  ? 0.7750 0.4942 0.5785 -0.0436 -0.0628 -0.0513 37  PHE A CD1 
210  C CD2 . PHE A 31  ? 0.8115 0.5420 0.6261 -0.0409 -0.0511 -0.0535 37  PHE A CD2 
211  C CE1 . PHE A 31  ? 0.7929 0.5225 0.6067 -0.0496 -0.0627 -0.0512 37  PHE A CE1 
212  C CE2 . PHE A 31  ? 0.7665 0.5079 0.5914 -0.0473 -0.0510 -0.0537 37  PHE A CE2 
213  C CZ  . PHE A 31  ? 0.8020 0.5431 0.6265 -0.0516 -0.0569 -0.0524 37  PHE A CZ  
214  N N   . MET A 32  ? 0.8311 0.5665 0.6389 -0.0339 -0.0594 -0.0511 38  MET A N   
215  C CA  . MET A 32  ? 0.8388 0.5899 0.6591 -0.0372 -0.0577 -0.0517 38  MET A CA  
216  C C   . MET A 32  ? 0.8356 0.5863 0.6609 -0.0352 -0.0470 -0.0537 38  MET A C   
217  O O   . MET A 32  ? 0.8280 0.5683 0.6470 -0.0289 -0.0414 -0.0540 38  MET A O   
218  C CB  . MET A 32  ? 0.8459 0.6019 0.6660 -0.0348 -0.0611 -0.0504 38  MET A CB  
219  C CG  . MET A 32  ? 0.9310 0.7043 0.7641 -0.0393 -0.0616 -0.0508 38  MET A CG  
220  S SD  . MET A 32  ? 1.0274 0.8121 0.8673 -0.0488 -0.0691 -0.0507 38  MET A SD  
221  C CE  . MET A 32  ? 1.0465 0.8467 0.8938 -0.0518 -0.0753 -0.0497 38  MET A CE  
222  N N   . LEU A 33  ? 0.7835 0.5455 0.6196 -0.0408 -0.0442 -0.0551 39  LEU A N   
223  C CA  . LEU A 33  ? 0.7778 0.5416 0.6199 -0.0401 -0.0341 -0.0572 39  LEU A CA  
224  C C   . LEU A 33  ? 0.7488 0.5261 0.6011 -0.0418 -0.0316 -0.0581 39  LEU A C   
225  O O   . LEU A 33  ? 0.7555 0.5457 0.6152 -0.0474 -0.0369 -0.0577 39  LEU A O   
226  C CB  . LEU A 33  ? 0.7549 0.5222 0.6021 -0.0454 -0.0321 -0.0582 39  LEU A CB  
227  C CG  . LEU A 33  ? 0.6970 0.4717 0.5534 -0.0477 -0.0229 -0.0606 39  LEU A CG  
228  C CD1 . LEU A 33  ? 0.6904 0.4523 0.5409 -0.0415 -0.0140 -0.0619 39  LEU A CD1 
229  C CD2 . LEU A 33  ? 0.6813 0.4646 0.5449 -0.0549 -0.0240 -0.0607 39  LEU A CD2 
230  N N   . VAL A 34  ? 0.7702 0.5444 0.6230 -0.0370 -0.0234 -0.0593 40  VAL A N   
231  C CA  . VAL A 34  ? 0.7581 0.5439 0.6207 -0.0379 -0.0198 -0.0602 40  VAL A CA  
232  C C   . VAL A 34  ? 0.7572 0.5463 0.6269 -0.0392 -0.0093 -0.0632 40  VAL A C   
233  O O   . VAL A 34  ? 0.7704 0.5488 0.6350 -0.0351 -0.0026 -0.0641 40  VAL A O   
234  C CB  . VAL A 34  ? 0.7764 0.5570 0.6345 -0.0309 -0.0194 -0.0588 40  VAL A CB  
235  C CG1 . VAL A 34  ? 0.7700 0.5646 0.6379 -0.0334 -0.0208 -0.0587 40  VAL A CG1 
236  C CG2 . VAL A 34  ? 0.8389 0.6084 0.6846 -0.0270 -0.0271 -0.0561 40  VAL A CG2 
237  N N   . ASP A 35  ? 0.7148 0.5191 0.5963 -0.0452 -0.0077 -0.0647 41  ASP A N   
238  C CA  . ASP A 35  ? 0.7320 0.5421 0.6216 -0.0474 0.0023  -0.0677 41  ASP A CA  
239  C C   . ASP A 35  ? 0.7633 0.5878 0.6638 -0.0508 0.0032  -0.0687 41  ASP A C   
240  O O   . ASP A 35  ? 0.7625 0.5954 0.6659 -0.0542 -0.0048 -0.0673 41  ASP A O   
241  C CB  . ASP A 35  ? 0.7071 0.5216 0.6001 -0.0538 0.0032  -0.0689 41  ASP A CB  
242  C CG  . ASP A 35  ? 0.7309 0.5468 0.6289 -0.0547 0.0144  -0.0720 41  ASP A CG  
243  O OD1 . ASP A 35  ? 0.7543 0.5834 0.6627 -0.0600 0.0184  -0.0741 41  ASP A OD1 
244  O OD2 . ASP A 35  ? 0.7305 0.5342 0.6216 -0.0502 0.0195  -0.0724 41  ASP A OD2 
245  N N   . MET A 36  ? 0.7351 0.5705 0.7085 -0.0226 -0.0251 -0.1070 42  MET A N   
246  C CA  . MET A 36  ? 0.7228 0.5869 0.7161 -0.0196 -0.0267 -0.1157 42  MET A CA  
247  C C   . MET A 36  ? 0.6911 0.5831 0.6976 -0.0256 -0.0137 -0.1109 42  MET A C   
248  O O   . MET A 36  ? 0.7197 0.6386 0.7465 -0.0263 -0.0124 -0.1166 42  MET A O   
249  C CB  . MET A 36  ? 0.7664 0.6230 0.7504 -0.0103 -0.0335 -0.1228 42  MET A CB  
250  C CG  . MET A 36  ? 0.7637 0.6141 0.7338 -0.0098 -0.0257 -0.1166 42  MET A CG  
251  S SD  . MET A 36  ? 0.9020 0.7397 0.8595 0.0007  -0.0346 -0.1244 42  MET A SD  
252  C CE  . MET A 36  ? 0.7831 0.5771 0.7124 0.0024  -0.0398 -0.1203 42  MET A CE  
253  N N   . LYS A 37  ? 0.6685 0.5543 0.6637 -0.0299 -0.0041 -0.1009 43  LYS A N   
254  C CA  . LYS A 37  ? 0.6472 0.5558 0.6519 -0.0358 0.0076  -0.0957 43  LYS A CA  
255  C C   . LYS A 37  ? 0.6578 0.5705 0.6700 -0.0449 0.0126  -0.0894 43  LYS A C   
256  O O   . LYS A 37  ? 0.6728 0.5683 0.6805 -0.0467 0.0075  -0.0878 43  LYS A O   
257  C CB  . LYS A 37  ? 0.5982 0.4983 0.5882 -0.0355 0.0145  -0.0886 43  LYS A CB  
258  C CG  . LYS A 37  ? 0.6334 0.5206 0.6122 -0.0271 0.0084  -0.0934 43  LYS A CG  
259  C CD  . LYS A 37  ? 0.6852 0.5680 0.6537 -0.0271 0.0152  -0.0873 43  LYS A CD  
260  C CE  . LYS A 37  ? 0.6917 0.5579 0.6500 -0.0330 0.0212  -0.0768 43  LYS A CE  
261  N NZ  . LYS A 37  ? 0.6414 0.4800 0.5872 -0.0324 0.0161  -0.0757 43  LYS A NZ  
262  N N   . ASP A 38  ? 0.6184 0.5528 0.6408 -0.0508 0.0225  -0.0856 44  ASP A N   
263  C CA  . ASP A 38  ? 0.5927 0.5296 0.6200 -0.0602 0.0282  -0.0784 44  ASP A CA  
264  C C   . ASP A 38  ? 0.6019 0.5259 0.6140 -0.0645 0.0357  -0.0671 44  ASP A C   
265  O O   . ASP A 38  ? 0.6280 0.5521 0.6419 -0.0723 0.0406  -0.0602 44  ASP A O   
266  C CB  . ASP A 38  ? 0.6068 0.5734 0.6540 -0.0653 0.0351  -0.0804 44  ASP A CB  
267  C CG  . ASP A 38  ? 0.7334 0.7141 0.7773 -0.0658 0.0453  -0.0771 44  ASP A CG  
268  O OD1 . ASP A 38  ? 0.7387 0.7156 0.7736 -0.0584 0.0432  -0.0798 44  ASP A OD1 
269  O OD2 . ASP A 38  ? 0.7811 0.7751 0.8303 -0.0733 0.0549  -0.0717 44  ASP A OD2 
270  N N   . SER A 39  ? 0.5841 0.4966 0.5821 -0.0596 0.0364  -0.0653 45  SER A N   
271  C CA  . SER A 39  ? 0.6143 0.5148 0.5998 -0.0633 0.0428  -0.0554 45  SER A CA  
272  C C   . SER A 39  ? 0.6106 0.4886 0.5804 -0.0575 0.0396  -0.0548 45  SER A C   
273  O O   . SER A 39  ? 0.6454 0.5213 0.6131 -0.0506 0.0344  -0.0614 45  SER A O   
274  C CB  . SER A 39  ? 0.6124 0.5307 0.6005 -0.0662 0.0519  -0.0516 45  SER A CB  
275  O OG  . SER A 39  ? 0.6081 0.5460 0.6048 -0.0618 0.0519  -0.0590 45  SER A OG  
276  N N   . PHE A 40  ? 0.5933 0.4539 0.5524 -0.0607 0.0429  -0.0468 46  PHE A N   
277  C CA  . PHE A 40  ? 0.5725 0.4117 0.5176 -0.0564 0.0420  -0.0452 46  PHE A CA  
278  C C   . PHE A 40  ? 0.6350 0.4824 0.5792 -0.0536 0.0460  -0.0448 46  PHE A C   
279  O O   . PHE A 40  ? 0.6038 0.4672 0.5535 -0.0566 0.0514  -0.0419 46  PHE A O   
280  C CB  . PHE A 40  ? 0.6281 0.4482 0.5639 -0.0607 0.0451  -0.0372 46  PHE A CB  
281  C CG  . PHE A 40  ? 0.6052 0.4075 0.5293 -0.0579 0.0476  -0.0340 46  PHE A CG  
282  C CD1 . PHE A 40  ? 0.6111 0.3920 0.5242 -0.0533 0.0436  -0.0367 46  PHE A CD1 
283  C CD2 . PHE A 40  ? 0.6042 0.4105 0.5283 -0.0597 0.0540  -0.0286 46  PHE A CD2 
284  C CE1 . PHE A 40  ? 0.6040 0.3692 0.5077 -0.0513 0.0471  -0.0340 46  PHE A CE1 
285  C CE2 . PHE A 40  ? 0.6467 0.4381 0.5630 -0.0572 0.0564  -0.0264 46  PHE A CE2 
286  C CZ  . PHE A 40  ? 0.6660 0.4373 0.5727 -0.0533 0.0535  -0.0290 46  PHE A CZ  
287  N N   . HIS A 41  ? 0.6378 0.4730 0.5744 -0.0477 0.0429  -0.0479 47  HIS A N   
288  C CA  . HIS A 41  ? 0.5700 0.4119 0.5064 -0.0440 0.0447  -0.0490 47  HIS A CA  
289  C C   . HIS A 41  ? 0.6139 0.4363 0.5407 -0.0437 0.0475  -0.0440 47  HIS A C   
290  O O   . HIS A 41  ? 0.6614 0.4643 0.5795 -0.0409 0.0448  -0.0454 47  HIS A O   
291  C CB  . HIS A 41  ? 0.5375 0.3839 0.4755 -0.0371 0.0381  -0.0581 47  HIS A CB  
292  C CG  . HIS A 41  ? 0.6328 0.4845 0.5701 -0.0328 0.0388  -0.0596 47  HIS A CG  
293  N ND1 . HIS A 41  ? 0.5887 0.4494 0.5280 -0.0351 0.0447  -0.0548 47  HIS A ND1 
294  C CD2 . HIS A 41  ? 0.5923 0.4406 0.5268 -0.0263 0.0337  -0.0657 47  HIS A CD2 
295  C CE1 . HIS A 41  ? 0.5632 0.4261 0.5015 -0.0300 0.0429  -0.0580 47  HIS A CE1 
296  N NE2 . HIS A 41  ? 0.6435 0.4992 0.5791 -0.0249 0.0365  -0.0645 47  HIS A NE2 
297  N N   . HIS A 42  ? 0.5975 0.4241 0.5256 -0.0464 0.0532  -0.0383 48  HIS A N   
298  C CA  . HIS A 42  ? 0.5818 0.3919 0.5039 -0.0462 0.0562  -0.0340 48  HIS A CA  
299  C C   . HIS A 42  ? 0.6163 0.4259 0.5380 -0.0406 0.0539  -0.0384 48  HIS A C   
300  O O   . HIS A 42  ? 0.6881 0.5055 0.6134 -0.0396 0.0556  -0.0374 48  HIS A O   
301  C CB  . HIS A 42  ? 0.5800 0.3943 0.5045 -0.0506 0.0616  -0.0272 48  HIS A CB  
302  C CG  . HIS A 42  ? 0.6064 0.4044 0.5272 -0.0507 0.0648  -0.0229 48  HIS A CG  
303  N ND1 . HIS A 42  ? 0.6475 0.4310 0.5639 -0.0542 0.0678  -0.0180 48  HIS A ND1 
304  C CD2 . HIS A 42  ? 0.6701 0.4646 0.5922 -0.0479 0.0657  -0.0233 48  HIS A CD2 
305  C CE1 . HIS A 42  ? 0.6678 0.4401 0.5835 -0.0534 0.0710  -0.0156 48  HIS A CE1 
306  N NE2 . HIS A 42  ? 0.6404 0.4194 0.5603 -0.0498 0.0697  -0.0187 48  HIS A NE2 
307  N N   . ASN A 43  ? 0.6132 0.4121 0.5296 -0.0365 0.0492  -0.0436 49  ASN A N   
308  C CA  . ASN A 43  ? 0.5783 0.3792 0.4949 -0.0310 0.0456  -0.0489 49  ASN A CA  
309  C C   . ASN A 43  ? 0.6295 0.4211 0.5453 -0.0306 0.0490  -0.0459 49  ASN A C   
310  O O   . ASN A 43  ? 0.6303 0.4262 0.5483 -0.0266 0.0463  -0.0495 49  ASN A O   
311  C CB  . ASN A 43  ? 0.5982 0.3871 0.5077 -0.0268 0.0392  -0.0550 49  ASN A CB  
312  C CG  . ASN A 43  ? 0.6826 0.4449 0.5803 -0.0281 0.0406  -0.0522 49  ASN A CG  
313  O OD1 . ASN A 43  ? 0.7003 0.4522 0.5958 -0.0315 0.0469  -0.0460 49  ASN A OD1 
314  N ND2 . ASN A 43  ? 0.6240 0.3742 0.5134 -0.0249 0.0344  -0.0570 49  ASN A ND2 
315  N N   . VAL A 44  ? 0.6533 0.4331 0.5673 -0.0345 0.0546  -0.0396 50  VAL A N   
316  C CA  . VAL A 44  ? 0.6908 0.4638 0.6074 -0.0343 0.0580  -0.0372 50  VAL A CA  
317  C C   . VAL A 44  ? 0.6785 0.4696 0.6040 -0.0337 0.0576  -0.0368 50  VAL A C   
318  O O   . VAL A 44  ? 0.7303 0.5197 0.6599 -0.0317 0.0575  -0.0373 50  VAL A O   
319  C CB  . VAL A 44  ? 0.6712 0.4282 0.5849 -0.0383 0.0643  -0.0312 50  VAL A CB  
320  C CG1 . VAL A 44  ? 0.7210 0.4726 0.6406 -0.0384 0.0682  -0.0290 50  VAL A CG1 
321  C CG2 . VAL A 44  ? 0.7263 0.4628 0.6284 -0.0381 0.0644  -0.0321 50  VAL A CG2 
322  N N   . ALA A 45  ? 0.5842 0.3917 0.5123 -0.0352 0.0573  -0.0360 51  ALA A N   
323  C CA  . ALA A 45  ? 0.6509 0.4738 0.5841 -0.0340 0.0567  -0.0360 51  ALA A CA  
324  C C   . ALA A 45  ? 0.6170 0.4549 0.5512 -0.0295 0.0521  -0.0425 51  ALA A C   
325  O O   . ALA A 45  ? 0.5585 0.4100 0.4950 -0.0284 0.0518  -0.0428 51  ALA A O   
326  C CB  . ALA A 45  ? 0.6185 0.4491 0.5525 -0.0388 0.0603  -0.0305 51  ALA A CB  
327  N N   . ALA A 46  ? 0.5960 0.4306 0.5278 -0.0265 0.0482  -0.0479 52  ALA A N   
328  C CA  . ALA A 46  ? 0.5763 0.4257 0.5099 -0.0218 0.0436  -0.0548 52  ALA A CA  
329  C C   . ALA A 46  ? 0.6246 0.4794 0.5600 -0.0171 0.0408  -0.0575 52  ALA A C   
330  O O   . ALA A 46  ? 0.6192 0.4900 0.5562 -0.0140 0.0389  -0.0614 52  ALA A O   
331  C CB  . ALA A 46  ? 0.5280 0.3698 0.4581 -0.0187 0.0386  -0.0606 52  ALA A CB  
332  N N   . LEU A 47  ? 0.6405 0.4820 0.5758 -0.0164 0.0405  -0.0559 53  LEU A N   
333  C CA  . LEU A 47  ? 0.6317 0.4776 0.5693 -0.0115 0.0364  -0.0593 53  LEU A CA  
334  C C   . LEU A 47  ? 0.6371 0.4934 0.5771 -0.0123 0.0382  -0.0559 53  LEU A C   
335  O O   . LEU A 47  ? 0.6503 0.5178 0.5901 -0.0080 0.0349  -0.0595 53  LEU A O   
336  C CB  . LEU A 47  ? 0.6356 0.4642 0.5741 -0.0106 0.0351  -0.0592 53  LEU A CB  
337  C CG  . LEU A 47  ? 0.6789 0.4921 0.6118 -0.0104 0.0341  -0.0614 53  LEU A CG  
338  C CD1 . LEU A 47  ? 0.6426 0.4388 0.5764 -0.0102 0.0342  -0.0610 53  LEU A CD1 
339  C CD2 . LEU A 47  ? 0.6717 0.4919 0.6008 -0.0053 0.0277  -0.0688 53  LEU A CD2 
340  N N   . ARG A 48  ? 0.6405 0.4921 0.5816 -0.0174 0.0432  -0.0492 54  ARG A N   
341  C CA  . ARG A 48  ? 0.6384 0.4986 0.5794 -0.0183 0.0444  -0.0460 54  ARG A CA  
342  C C   . ARG A 48  ? 0.6431 0.5200 0.5805 -0.0184 0.0457  -0.0473 54  ARG A C   
343  O O   . ARG A 48  ? 0.6784 0.5645 0.6131 -0.0160 0.0447  -0.0481 54  ARG A O   
344  C CB  . ARG A 48  ? 0.6276 0.4791 0.5699 -0.0238 0.0490  -0.0388 54  ARG A CB  
345  C CG  . ARG A 48  ? 0.6661 0.5247 0.6061 -0.0246 0.0495  -0.0353 54  ARG A CG  
346  C CD  . ARG A 48  ? 0.7360 0.5841 0.6797 -0.0264 0.0500  -0.0307 54  ARG A CD  
347  N NE  . ARG A 48  ? 0.7086 0.5466 0.6599 -0.0238 0.0475  -0.0331 54  ARG A NE  
348  C CZ  . ARG A 48  ? 0.6631 0.4897 0.6207 -0.0261 0.0496  -0.0299 54  ARG A CZ  
349  N NH1 . ARG A 48  ? 0.6320 0.4553 0.5885 -0.0303 0.0532  -0.0245 54  ARG A NH1 
350  N NH2 . ARG A 48  ? 0.6759 0.4940 0.6413 -0.0243 0.0485  -0.0324 54  ARG A NH2 
351  N N   . ALA A 49  ? 0.6492 0.5295 0.5862 -0.0211 0.0480  -0.0479 55  ALA A N   
352  C CA  . ALA A 49  ? 0.5959 0.4932 0.5321 -0.0215 0.0499  -0.0500 55  ALA A CA  
353  C C   . ALA A 49  ? 0.6192 0.5274 0.5555 -0.0145 0.0455  -0.0579 55  ALA A C   
354  O O   . ALA A 49  ? 0.6236 0.5474 0.5593 -0.0138 0.0475  -0.0601 55  ALA A O   
355  C CB  . ALA A 49  ? 0.4923 0.3907 0.4306 -0.0257 0.0523  -0.0497 55  ALA A CB  
356  N N   . SER A 50  ? 0.6698 0.5698 0.6069 -0.0095 0.0398  -0.0622 56  SER A N   
357  C CA  . SER A 50  ? 0.6764 0.5849 0.6129 -0.0023 0.0345  -0.0698 56  SER A CA  
358  C C   . SER A 50  ? 0.6580 0.5699 0.5915 0.0014  0.0327  -0.0698 56  SER A C   
359  O O   . SER A 50  ? 0.6679 0.5874 0.5999 0.0077  0.0284  -0.0761 56  SER A O   
360  C CB  . SER A 50  ? 0.6077 0.5041 0.5449 0.0016  0.0284  -0.0744 56  SER A CB  
361  O OG  . SER A 50  ? 0.6494 0.5438 0.5874 0.0003  0.0281  -0.0766 56  SER A OG  
362  N N   . VAL A 51  ? 0.6508 0.5563 0.5830 -0.0019 0.0350  -0.0634 57  VAL A N   
363  C CA  . VAL A 51  ? 0.6750 0.5800 0.6041 0.0023  0.0313  -0.0637 57  VAL A CA  
364  C C   . VAL A 51  ? 0.7073 0.6145 0.6310 -0.0012 0.0355  -0.0577 57  VAL A C   
365  O O   . VAL A 51  ? 0.7085 0.6172 0.6266 0.0027  0.0327  -0.0583 57  VAL A O   
366  C CB  . VAL A 51  ? 0.6458 0.5358 0.5800 0.0038  0.0263  -0.0636 57  VAL A CB  
367  C CG1 . VAL A 51  ? 0.6488 0.5349 0.5858 0.0077  0.0216  -0.0698 57  VAL A CG1 
368  C CG2 . VAL A 51  ? 0.6433 0.5219 0.5816 -0.0027 0.0307  -0.0569 57  VAL A CG2 
369  N N   . GLU A 52  ? 0.6657 0.5716 0.5897 -0.0082 0.0417  -0.0517 58  GLU A N   
370  C CA  . GLU A 52  ? 0.6708 0.5765 0.5886 -0.0120 0.0454  -0.0455 58  GLU A CA  
371  C C   . GLU A 52  ? 0.6605 0.5796 0.5733 -0.0155 0.0520  -0.0445 58  GLU A C   
372  O O   . GLU A 52  ? 0.6430 0.5657 0.5605 -0.0200 0.0560  -0.0438 58  GLU A O   
373  C CB  . GLU A 52  ? 0.6875 0.5802 0.6089 -0.0176 0.0472  -0.0389 58  GLU A CB  
374  C CG  . GLU A 52  ? 0.7572 0.6474 0.6711 -0.0208 0.0496  -0.0326 58  GLU A CG  
375  C CD  . GLU A 52  ? 0.7555 0.6348 0.6726 -0.0269 0.0523  -0.0261 58  GLU A CD  
376  O OE1 . GLU A 52  ? 0.8156 0.6846 0.7407 -0.0265 0.0502  -0.0263 58  GLU A OE1 
377  O OE2 . GLU A 52  ? 0.8054 0.6857 0.7166 -0.0321 0.0568  -0.0209 58  GLU A OE2 
378  N N   . THR A 53  ? 0.6736 0.5992 0.5768 -0.0135 0.0533  -0.0445 59  THR A N   
379  C CA  . THR A 53  ? 0.6618 0.6004 0.5601 -0.0172 0.0609  -0.0435 59  THR A CA  
380  C C   . THR A 53  ? 0.6839 0.6187 0.5828 -0.0262 0.0668  -0.0359 59  THR A C   
381  O O   . THR A 53  ? 0.6770 0.5991 0.5724 -0.0289 0.0658  -0.0300 59  THR A O   
382  C CB  . THR A 53  ? 0.6887 0.6302 0.5732 -0.0138 0.0618  -0.0434 59  THR A CB  
383  O OG1 . THR A 53  ? 0.7460 0.6916 0.6295 -0.0050 0.0561  -0.0509 59  THR A OG1 
384  C CG2 . THR A 53  ? 0.5624 0.5169 0.4413 -0.0184 0.0714  -0.0419 59  THR A CG2 
385  N N   . GLY A 54  ? 0.5976 0.5433 0.5017 -0.0307 0.0725  -0.0366 60  GLY A N   
386  C CA  . GLY A 54  ? 0.6184 0.5611 0.5232 -0.0394 0.0779  -0.0297 60  GLY A CA  
387  C C   . GLY A 54  ? 0.6890 0.6186 0.6005 -0.0424 0.0752  -0.0267 60  GLY A C   
388  O O   . GLY A 54  ? 0.7373 0.6623 0.6486 -0.0493 0.0789  -0.0207 60  GLY A O   
389  N N   . PHE A 55  ? 0.5970 0.5192 0.5136 -0.0374 0.0692  -0.0304 61  PHE A N   
390  C CA  . PHE A 55  ? 0.6180 0.5270 0.5398 -0.0403 0.0679  -0.0276 61  PHE A CA  
391  C C   . PHE A 55  ? 0.6239 0.5372 0.5523 -0.0429 0.0692  -0.0301 61  PHE A C   
392  O O   . PHE A 55  ? 0.6288 0.5336 0.5587 -0.0479 0.0708  -0.0259 61  PHE A O   
393  C CB  . PHE A 55  ? 0.5966 0.4948 0.5212 -0.0349 0.0621  -0.0303 61  PHE A CB  
394  C CG  . PHE A 55  ? 0.6574 0.5403 0.5856 -0.0378 0.0620  -0.0268 61  PHE A CG  
395  C CD1 . PHE A 55  ? 0.7237 0.5975 0.6498 -0.0419 0.0640  -0.0201 61  PHE A CD1 
396  C CD2 . PHE A 55  ? 0.6268 0.5033 0.5595 -0.0361 0.0600  -0.0303 61  PHE A CD2 
397  C CE1 . PHE A 55  ? 0.6984 0.5583 0.6279 -0.0442 0.0646  -0.0172 61  PHE A CE1 
398  C CE2 . PHE A 55  ? 0.6466 0.5081 0.5810 -0.0387 0.0611  -0.0270 61  PHE A CE2 
399  C CZ  . PHE A 55  ? 0.6386 0.4923 0.5719 -0.0427 0.0636  -0.0206 61  PHE A CZ  
400  N N   . ALA A 56  ? 0.6179 0.5440 0.5501 -0.0394 0.0683  -0.0370 62  ALA A N   
401  C CA  . ALA A 56  ? 0.5625 0.4904 0.5018 -0.0402 0.0671  -0.0408 62  ALA A CA  
402  C C   . ALA A 56  ? 0.5747 0.5047 0.5165 -0.0481 0.0718  -0.0363 62  ALA A C   
403  O O   . ALA A 56  ? 0.6043 0.5280 0.5502 -0.0498 0.0699  -0.0370 62  ALA A O   
404  C CB  . ALA A 56  ? 0.5776 0.5208 0.5214 -0.0348 0.0650  -0.0495 62  ALA A CB  
405  N N   . LYS A 57  ? 0.6247 0.5620 0.5634 -0.0529 0.0775  -0.0316 63  LYS A N   
406  C CA  . LYS A 57  ? 0.5907 0.5289 0.5322 -0.0609 0.0817  -0.0270 63  LYS A CA  
407  C C   . LYS A 57  ? 0.6399 0.5592 0.5779 -0.0647 0.0806  -0.0204 63  LYS A C   
408  O O   . LYS A 57  ? 0.6580 0.5753 0.5985 -0.0708 0.0827  -0.0169 63  LYS A O   
409  C CB  . LYS A 57  ? 0.5528 0.5023 0.4907 -0.0658 0.0888  -0.0234 63  LYS A CB  
410  C CG  . LYS A 57  ? 0.6418 0.5818 0.5675 -0.0664 0.0901  -0.0169 63  LYS A CG  
411  C CD  . LYS A 57  ? 0.7182 0.6706 0.6375 -0.0673 0.0960  -0.0165 63  LYS A CD  
412  C CE  . LYS A 57  ? 0.8120 0.7574 0.7216 -0.0745 0.1007  -0.0078 63  LYS A CE  
413  N NZ  . LYS A 57  ? 0.9094 0.8367 0.8108 -0.0722 0.0957  -0.0033 63  LYS A NZ  
414  N N   . LYS A 58  ? 0.6466 0.5524 0.5800 -0.0610 0.0776  -0.0188 64  LYS A N   
415  C CA  . LYS A 58  ? 0.6439 0.5316 0.5754 -0.0632 0.0765  -0.0141 64  LYS A CA  
416  C C   . LYS A 58  ? 0.6086 0.4874 0.5436 -0.0609 0.0729  -0.0179 64  LYS A C   
417  O O   . LYS A 58  ? 0.6094 0.4727 0.5422 -0.0628 0.0727  -0.0144 64  LYS A O   
418  C CB  . LYS A 58  ? 0.6230 0.5003 0.5500 -0.0603 0.0750  -0.0114 64  LYS A CB  
419  C CG  . LYS A 58  ? 0.7216 0.6043 0.6426 -0.0609 0.0768  -0.0082 64  LYS A CG  
420  C CD  . LYS A 58  ? 0.8083 0.6904 0.7248 -0.0684 0.0811  -0.0014 64  LYS A CD  
421  C CE  . LYS A 58  ? 0.8767 0.7581 0.7839 -0.0687 0.0820  0.0026  64  LYS A CE  
422  N NZ  . LYS A 58  ? 0.9392 0.8341 0.8433 -0.0647 0.0827  -0.0018 64  LYS A NZ  
423  N N   . THR A 59  ? 0.5535 0.4404 0.4925 -0.0568 0.0700  -0.0251 65  THR A N   
424  C CA  . THR A 59  ? 0.5950 0.4707 0.5344 -0.0533 0.0656  -0.0292 65  THR A CA  
425  C C   . THR A 59  ? 0.5734 0.4537 0.5174 -0.0545 0.0634  -0.0333 65  THR A C   
426  O O   . THR A 59  ? 0.6049 0.4756 0.5477 -0.0509 0.0588  -0.0376 65  THR A O   
427  C CB  . THR A 59  ? 0.5873 0.4638 0.5265 -0.0461 0.0618  -0.0350 65  THR A CB  
428  O OG1 . THR A 59  ? 0.5899 0.4852 0.5333 -0.0434 0.0609  -0.0408 65  THR A OG1 
429  C CG2 . THR A 59  ? 0.5506 0.4217 0.4869 -0.0446 0.0628  -0.0317 65  THR A CG2 
430  N N   . PHE A 60  ? 0.5958 0.4900 0.5453 -0.0592 0.0662  -0.0325 66  PHE A N   
431  C CA  . PHE A 60  ? 0.5885 0.4873 0.5449 -0.0609 0.0637  -0.0364 66  PHE A CA  
432  C C   . PHE A 60  ? 0.5938 0.4911 0.5516 -0.0690 0.0672  -0.0301 66  PHE A C   
433  O O   . PHE A 60  ? 0.5863 0.4918 0.5439 -0.0736 0.0728  -0.0252 66  PHE A O   
434  C CB  . PHE A 60  ? 0.5070 0.4279 0.4730 -0.0584 0.0633  -0.0438 66  PHE A CB  
435  C CG  . PHE A 60  ? 0.5180 0.4391 0.4835 -0.0500 0.0577  -0.0516 66  PHE A CG  
436  C CD1 . PHE A 60  ? 0.5729 0.4855 0.5394 -0.0462 0.0506  -0.0575 66  PHE A CD1 
437  C CD2 . PHE A 60  ? 0.5586 0.4867 0.5215 -0.0457 0.0589  -0.0531 66  PHE A CD2 
438  C CE1 . PHE A 60  ? 0.5672 0.4784 0.5320 -0.0385 0.0449  -0.0645 66  PHE A CE1 
439  C CE2 . PHE A 60  ? 0.5477 0.4752 0.5099 -0.0379 0.0532  -0.0603 66  PHE A CE2 
440  C CZ  . PHE A 60  ? 0.5975 0.5165 0.5606 -0.0345 0.0463  -0.0659 66  PHE A CZ  
441  N N   . ILE A 61  ? 0.5793 0.4645 0.5371 -0.0706 0.0635  -0.0301 67  ILE A N   
442  C CA  . ILE A 61  ? 0.5973 0.4788 0.5560 -0.0781 0.0657  -0.0242 67  ILE A CA  
443  C C   . ILE A 61  ? 0.5967 0.4833 0.5651 -0.0798 0.0614  -0.0291 67  ILE A C   
444  O O   . ILE A 61  ? 0.6116 0.4873 0.5783 -0.0753 0.0547  -0.0340 67  ILE A O   
445  C CB  . ILE A 61  ? 0.6071 0.4652 0.5550 -0.0791 0.0655  -0.0180 67  ILE A CB  
446  C CG1 . ILE A 61  ? 0.6088 0.4608 0.5496 -0.0753 0.0678  -0.0158 67  ILE A CG1 
447  C CG2 . ILE A 61  ? 0.5886 0.4450 0.5365 -0.0869 0.0687  -0.0110 67  ILE A CG2 
448  C CD1 . ILE A 61  ? 0.6038 0.4346 0.5358 -0.0758 0.0686  -0.0104 67  ILE A CD1 
449  N N   . SER A 62  ? 0.5726 0.4747 0.5506 -0.0862 0.0652  -0.0277 68  SER A N   
450  C CA  . SER A 62  ? 0.5904 0.5003 0.5813 -0.0888 0.0615  -0.0324 68  SER A CA  
451  C C   . SER A 62  ? 0.6122 0.5004 0.5980 -0.0890 0.0546  -0.0315 68  SER A C   
452  O O   . SER A 62  ? 0.6064 0.4797 0.5836 -0.0930 0.0563  -0.0241 68  SER A O   
453  C CB  . SER A 62  ? 0.5481 0.4742 0.5482 -0.0977 0.0685  -0.0284 68  SER A CB  
454  O OG  . SER A 62  ? 0.6437 0.5757 0.6576 -0.1016 0.0650  -0.0318 68  SER A OG  
455  N N   . TYR A 63  ? 0.6128 0.4985 0.6035 -0.0843 0.0464  -0.0394 69  TYR A N   
456  C CA  . TYR A 63  ? 0.6081 0.4726 0.5930 -0.0843 0.0393  -0.0391 69  TYR A CA  
457  C C   . TYR A 63  ? 0.6308 0.5000 0.6255 -0.0927 0.0398  -0.0359 69  TYR A C   
458  O O   . TYR A 63  ? 0.6371 0.4884 0.6231 -0.0959 0.0388  -0.0301 69  TYR A O   
459  C CB  . TYR A 63  ? 0.5987 0.4579 0.5853 -0.0770 0.0292  -0.0488 69  TYR A CB  
460  C CG  . TYR A 63  ? 0.5963 0.4434 0.5699 -0.0687 0.0270  -0.0517 69  TYR A CG  
461  C CD1 . TYR A 63  ? 0.6069 0.4295 0.5622 -0.0669 0.0281  -0.0465 69  TYR A CD1 
462  C CD2 . TYR A 63  ? 0.6199 0.4795 0.5999 -0.0626 0.0236  -0.0601 69  TYR A CD2 
463  C CE1 . TYR A 63  ? 0.6305 0.4419 0.5748 -0.0601 0.0267  -0.0490 69  TYR A CE1 
464  C CE2 . TYR A 63  ? 0.5870 0.4349 0.5551 -0.0554 0.0212  -0.0628 69  TYR A CE2 
465  C CZ  . TYR A 63  ? 0.6153 0.4391 0.5658 -0.0545 0.0230  -0.0570 69  TYR A CZ  
466  O OH  . TYR A 63  ? 0.6229 0.4346 0.5623 -0.0481 0.0210  -0.0596 69  TYR A OH  
467  N N   . SER A 64  ? 0.6137 0.5070 0.6271 -0.0964 0.0415  -0.0399 70  SER A N   
468  C CA  . SER A 64  ? 0.6105 0.5088 0.6363 -0.1042 0.0406  -0.0385 70  SER A CA  
469  C C   . SER A 64  ? 0.6568 0.5501 0.6761 -0.1126 0.0479  -0.0277 70  SER A C   
470  O O   . SER A 64  ? 0.6593 0.5453 0.6816 -0.1184 0.0454  -0.0246 70  SER A O   
471  C CB  . SER A 64  ? 0.6238 0.5509 0.6723 -0.1067 0.0430  -0.0450 70  SER A CB  
472  O OG  . SER A 64  ? 0.6953 0.6381 0.7425 -0.1072 0.0530  -0.0427 70  SER A OG  
473  N N   . VAL A 65  ? 0.6422 0.5386 0.6524 -0.1131 0.0562  -0.0222 71  VAL A N   
474  C CA  . VAL A 65  ? 0.5997 0.4889 0.6017 -0.1202 0.0621  -0.0120 71  VAL A CA  
475  C C   . VAL A 65  ? 0.6428 0.5042 0.6302 -0.1187 0.0570  -0.0077 71  VAL A C   
476  O O   . VAL A 65  ? 0.6817 0.5340 0.6666 -0.1250 0.0572  -0.0016 71  VAL A O   
477  C CB  . VAL A 65  ? 0.6293 0.5260 0.6236 -0.1196 0.0706  -0.0080 71  VAL A CB  
478  C CG1 . VAL A 65  ? 0.5624 0.4456 0.5439 -0.1247 0.0746  0.0022  71  VAL A CG1 
479  C CG2 . VAL A 65  ? 0.5196 0.4431 0.5272 -0.1228 0.0772  -0.0110 71  VAL A CG2 
480  N N   . THR A 66  ? 0.6276 0.4746 0.6050 -0.1104 0.0523  -0.0111 72  THR A N   
481  C CA  . THR A 66  ? 0.6961 0.5164 0.6586 -0.1087 0.0489  -0.0072 72  THR A CA  
482  C C   . THR A 66  ? 0.6672 0.4752 0.6314 -0.1081 0.0397  -0.0110 72  THR A C   
483  O O   . THR A 66  ? 0.6788 0.4701 0.6360 -0.1111 0.0376  -0.0063 72  THR A O   
484  C CB  . THR A 66  ? 0.7321 0.5398 0.6817 -0.1005 0.0490  -0.0085 72  THR A CB  
485  O OG1 . THR A 66  ? 0.7612 0.5780 0.7087 -0.1008 0.0564  -0.0047 72  THR A OG1 
486  C CG2 . THR A 66  ? 0.6702 0.4500 0.6045 -0.0985 0.0463  -0.0051 72  THR A CG2 
487  N N   . PHE A 67  ? 0.6549 0.4702 0.6280 -0.1039 0.0336  -0.0198 73  PHE A N   
488  C CA  . PHE A 67  ? 0.6827 0.4825 0.6543 -0.1010 0.0232  -0.0246 73  PHE A CA  
489  C C   . PHE A 67  ? 0.7040 0.5186 0.6957 -0.1060 0.0183  -0.0289 73  PHE A C   
490  O O   . PHE A 67  ? 0.7460 0.5465 0.7371 -0.1047 0.0087  -0.0321 73  PHE A O   
491  C CB  . PHE A 67  ? 0.6757 0.4667 0.6396 -0.0912 0.0175  -0.0320 73  PHE A CB  
492  C CG  . PHE A 67  ? 0.6472 0.4204 0.5916 -0.0865 0.0217  -0.0282 73  PHE A CG  
493  C CD1 . PHE A 67  ? 0.6810 0.4285 0.6088 -0.0865 0.0217  -0.0227 73  PHE A CD1 
494  C CD2 . PHE A 67  ? 0.6675 0.4496 0.6109 -0.0821 0.0258  -0.0303 73  PHE A CD2 
495  C CE1 . PHE A 67  ? 0.6757 0.4079 0.5878 -0.0825 0.0265  -0.0195 73  PHE A CE1 
496  C CE2 . PHE A 67  ? 0.6666 0.4329 0.5943 -0.0783 0.0298  -0.0270 73  PHE A CE2 
497  C CZ  . PHE A 67  ? 0.6903 0.4321 0.6031 -0.0786 0.0305  -0.0217 73  PHE A CZ  
498  N N   . LYS A 68  ? 0.6861 0.5278 0.6953 -0.1117 0.0248  -0.0290 74  LYS A N   
499  C CA  . LYS A 68  ? 0.6831 0.5423 0.7147 -0.1179 0.0224  -0.0327 74  LYS A CA  
500  C C   . LYS A 68  ? 0.7401 0.5954 0.7789 -0.1112 0.0099  -0.0433 74  LYS A C   
501  O O   . LYS A 68  ? 0.7820 0.6376 0.8170 -0.1030 0.0071  -0.0496 74  LYS A O   
502  C CB  . LYS A 68  ? 0.7419 0.5932 0.7733 -0.1269 0.0236  -0.0248 74  LYS A CB  
503  C CG  . LYS A 68  ? 0.6950 0.5544 0.7229 -0.1346 0.0357  -0.0152 74  LYS A CG  
504  C CD  . LYS A 68  ? 0.7374 0.5733 0.7416 -0.1324 0.0377  -0.0073 74  LYS A CD  
505  N N   . ASP A 69  ? 0.7757 0.6256 0.8240 -0.1142 0.0014  -0.0458 75  ASP A N   
506  C CA  . ASP A 69  ? 0.8074 0.6558 0.8659 -0.1084 -0.0115 -0.0567 75  ASP A CA  
507  C C   . ASP A 69  ? 0.8057 0.6240 0.8411 -0.0982 -0.0212 -0.0596 75  ASP A C   
508  O O   . ASP A 69  ? 0.8276 0.6414 0.8683 -0.0923 -0.0332 -0.0690 75  ASP A O   
509  C CB  . ASP A 69  ? 0.9389 0.7889 1.0144 -0.1152 -0.0182 -0.0578 75  ASP A CB  
510  C CG  . ASP A 69  ? 1.0298 0.8748 1.1007 -0.1251 -0.0109 -0.0465 75  ASP A CG  
511  O OD1 . ASP A 69  ? 1.0287 0.8501 1.0754 -0.1235 -0.0094 -0.0392 75  ASP A OD1 
512  O OD2 . ASP A 69  ? 1.1382 1.0026 1.2297 -0.1345 -0.0064 -0.0451 75  ASP A OD2 
513  N N   . ASN A 70  ? 0.7797 0.5771 0.7901 -0.0960 -0.0165 -0.0523 76  ASN A N   
514  C CA  . ASN A 70  ? 0.7838 0.5533 0.7707 -0.0865 -0.0228 -0.0546 76  ASN A CA  
515  C C   . ASN A 70  ? 0.7778 0.5549 0.7616 -0.0795 -0.0206 -0.0594 76  ASN A C   
516  O O   . ASN A 70  ? 0.7615 0.5159 0.7252 -0.0720 -0.0244 -0.0609 76  ASN A O   
517  C CB  . ASN A 70  ? 0.7934 0.5382 0.7565 -0.0872 -0.0176 -0.0451 76  ASN A CB  
518  C CG  . ASN A 70  ? 0.8413 0.5708 0.8017 -0.0918 -0.0224 -0.0412 76  ASN A CG  
519  O OD1 . ASN A 70  ? 0.8014 0.5282 0.7573 -0.0977 -0.0153 -0.0325 76  ASN A OD1 
520  N ND2 . ASN A 70  ? 0.8324 0.5512 0.7957 -0.0889 -0.0355 -0.0479 76  ASN A ND2 
521  N N   . PHE A 71  ? 0.7618 0.5689 0.7639 -0.0818 -0.0142 -0.0615 77  PHE A N   
522  C CA  . PHE A 71  ? 0.7204 0.5364 0.7212 -0.0752 -0.0126 -0.0666 77  PHE A CA  
523  C C   . PHE A 71  ? 0.7331 0.5704 0.7563 -0.0727 -0.0194 -0.0776 77  PHE A C   
524  O O   . PHE A 71  ? 0.7823 0.6375 0.8271 -0.0786 -0.0200 -0.0796 77  PHE A O   
525  C CB  . PHE A 71  ? 0.7019 0.5342 0.7030 -0.0788 0.0010  -0.0601 77  PHE A CB  
526  C CG  . PHE A 71  ? 0.7093 0.5566 0.7144 -0.0730 0.0025  -0.0661 77  PHE A CG  
527  C CD1 . PHE A 71  ? 0.6660 0.4960 0.6535 -0.0650 -0.0002 -0.0679 77  PHE A CD1 
528  C CD2 . PHE A 71  ? 0.6830 0.5613 0.7093 -0.0755 0.0068  -0.0701 77  PHE A CD2 
529  C CE1 . PHE A 71  ? 0.6603 0.5033 0.6514 -0.0595 0.0002  -0.0736 77  PHE A CE1 
530  C CE2 . PHE A 71  ? 0.6500 0.5416 0.6794 -0.0695 0.0077  -0.0761 77  PHE A CE2 
531  C CZ  . PHE A 71  ? 0.6544 0.5281 0.6662 -0.0615 0.0039  -0.0778 77  PHE A CZ  
532  N N   . ARG A 72  ? 0.7341 0.5693 0.7529 -0.0641 -0.0247 -0.0850 78  ARG A N   
533  C CA  . ARG A 72  ? 0.7510 0.6068 0.7913 -0.0606 -0.0316 -0.0964 78  ARG A CA  
534  C C   . ARG A 72  ? 0.7591 0.6202 0.7937 -0.0532 -0.0302 -0.1007 78  ARG A C   
535  O O   . ARG A 72  ? 0.7573 0.5940 0.7706 -0.0462 -0.0355 -0.1016 78  ARG A O   
536  C CB  . ARG A 72  ? 0.7970 0.6361 0.8383 -0.0559 -0.0477 -0.1044 78  ARG A CB  
537  C CG  . ARG A 72  ? 0.8502 0.7139 0.9205 -0.0545 -0.0549 -0.1160 78  ARG A CG  
538  C CD  . ARG A 72  ? 0.8543 0.7072 0.9188 -0.0430 -0.0682 -0.1270 78  ARG A CD  
539  N NE  . ARG A 72  ? 0.9465 0.8203 1.0396 -0.0409 -0.0775 -0.1392 78  ARG A NE  
540  C CZ  . ARG A 72  ? 1.0125 0.8816 1.1182 -0.0418 -0.0890 -0.1443 78  ARG A CZ  
541  N NH1 . ARG A 72  ? 0.9780 0.8223 1.0696 -0.0450 -0.0926 -0.1380 78  ARG A NH1 
542  N NH2 . ARG A 72  ? 0.9793 0.8691 1.1130 -0.0390 -0.0975 -0.1565 78  ARG A NH2 
543  N N   . GLN A 73  ? 0.7360 0.6276 0.7883 -0.0549 -0.0225 -0.1031 79  GLN A N   
544  C CA  . GLN A 73  ? 0.6878 0.5872 0.7375 -0.0475 -0.0223 -0.1086 79  GLN A CA  
545  C C   . GLN A 73  ? 0.7187 0.6148 0.7743 -0.0388 -0.0369 -0.1213 79  GLN A C   
546  O O   . GLN A 73  ? 0.7697 0.6789 0.8466 -0.0397 -0.0433 -0.1285 79  GLN A O   
547  C CB  . GLN A 73  ? 0.6525 0.5851 0.7196 -0.0513 -0.0108 -0.1086 79  GLN A CB  
548  C CG  . GLN A 73  ? 0.6575 0.5979 0.7203 -0.0439 -0.0095 -0.1131 79  GLN A CG  
549  C CD  . GLN A 73  ? 0.7326 0.7003 0.8057 -0.0484 0.0039  -0.1101 79  GLN A CD  
550  O OE1 . GLN A 73  ? 0.6897 0.6685 0.7711 -0.0573 0.0126  -0.1039 79  GLN A OE1 
551  N NE2 . GLN A 73  ? 0.7150 0.6924 0.7862 -0.0421 0.0053  -0.1146 79  GLN A NE2 
552  N N   . GLY A 74  ? 0.6864 0.5646 0.7237 -0.0303 -0.0425 -0.1242 80  GLY A N   
553  C CA  . GLY A 74  ? 0.7162 0.5883 0.7557 -0.0211 -0.0572 -0.1362 80  GLY A CA  
554  C C   . GLY A 74  ? 0.8042 0.6522 0.8179 -0.0134 -0.0607 -0.1363 80  GLY A C   
555  O O   . GLY A 74  ? 0.8070 0.6366 0.7999 -0.0155 -0.0537 -0.1269 80  GLY A O   
556  N N   . LEU A 75  ? 0.7779 0.6266 0.7942 -0.0045 -0.0715 -0.1473 81  LEU A N   
557  C CA  . LEU A 75  ? 0.8081 0.6321 0.8004 0.0034  -0.0771 -0.1490 81  LEU A CA  
558  C C   . LEU A 75  ? 0.8572 0.6487 0.8335 0.0088  -0.0922 -0.1535 81  LEU A C   
559  O O   . LEU A 75  ? 0.9241 0.7209 0.9150 0.0121  -0.1041 -0.1630 81  LEU A O   
560  C CB  . LEU A 75  ? 0.8370 0.6798 0.8395 0.0105  -0.0803 -0.1585 81  LEU A CB  
561  C CG  . LEU A 75  ? 0.8297 0.6475 0.8071 0.0180  -0.0852 -0.1595 81  LEU A CG  
562  C CD1 . LEU A 75  ? 0.8544 0.6745 0.8222 0.0138  -0.0708 -0.1494 81  LEU A CD1 
563  C CD2 . LEU A 75  ? 0.8578 0.6854 0.8437 0.0274  -0.0960 -0.1724 81  LEU A CD2 
564  N N   . VAL A 76  ? 0.8377 0.5955 0.7846 0.0098  -0.0917 -0.1469 82  VAL A N   
565  C CA  . VAL A 76  ? 0.9469 0.6697 0.8739 0.0148  -0.1052 -0.1501 82  VAL A CA  
566  C C   . VAL A 76  ? 0.9791 0.6871 0.8934 0.0250  -0.1168 -0.1591 82  VAL A C   
567  O O   . VAL A 76  ? 0.9939 0.6933 0.8928 0.0269  -0.1114 -0.1559 82  VAL A O   
568  C CB  . VAL A 76  ? 0.9343 0.6261 0.8343 0.0109  -0.0984 -0.1389 82  VAL A CB  
569  C CG1 . VAL A 76  ? 0.9921 0.6465 0.8699 0.0164  -0.1124 -0.1424 82  VAL A CG1 
570  C CG2 . VAL A 76  ? 0.9018 0.6092 0.8145 0.0010  -0.0869 -0.1300 82  VAL A CG2 
571  N N   . VAL A 77  ? 1.0035 0.7075 0.9243 0.0316  -0.1333 -0.1704 83  VAL A N   
572  C CA  . VAL A 77  ? 1.0292 0.7183 0.9382 0.0420  -0.1464 -0.1800 83  VAL A CA  
573  C C   . VAL A 77  ? 1.0516 0.6927 0.9252 0.0471  -0.1571 -0.1796 83  VAL A C   
574  O O   . VAL A 77  ? 1.1281 0.7464 0.9784 0.0529  -0.1607 -0.1808 83  VAL A O   
575  C CB  . VAL A 77  ? 1.0100 0.7246 0.9482 0.0474  -0.1590 -0.1941 83  VAL A CB  
576  C CG1 . VAL A 77  ? 0.9671 0.7272 0.9365 0.0431  -0.1470 -0.1948 83  VAL A CG1 
577  C CG2 . VAL A 77  ? 1.0346 0.7456 0.9838 0.0464  -0.1692 -0.1982 83  VAL A CG2 
578  N N   . GLY A 78  ? 1.0811 0.7044 0.9481 0.0453  -0.1621 -0.1777 84  GLY A N   
579  C CA  . GLY A 78  ? 1.1342 0.7099 0.9649 0.0505  -0.1719 -0.1773 84  GLY A CA  
580  C C   . GLY A 78  ? 1.1384 0.6956 0.9592 0.0457  -0.1707 -0.1707 84  GLY A C   
581  O O   . GLY A 78  ? 1.0927 0.6736 0.9381 0.0395  -0.1673 -0.1692 84  GLY A O   
582  N N   . ILE A 79  ? 1.1567 0.6801 0.9442 0.0478  -0.1699 -0.1630 85  ILE A N   
583  C CA  . ILE A 79  ? 1.1809 0.6866 0.9557 0.0449  -0.1689 -0.1554 85  ILE A CA  
584  C C   . ILE A 79  ? 1.2220 0.7174 0.9896 0.0526  -0.1843 -0.1581 85  ILE A C   
585  O O   . ILE A 79  ? 1.2574 0.7439 1.0097 0.0589  -0.1887 -0.1575 85  ILE A O   
586  C CB  . ILE A 79  ? 1.1846 0.6704 0.9316 0.0409  -0.1528 -0.1414 85  ILE A CB  
587  C CG1 . ILE A 79  ? 1.1789 0.6740 0.9312 0.0347  -0.1380 -0.1385 85  ILE A CG1 
588  C CG2 . ILE A 79  ? 1.2188 0.6907 0.9567 0.0374  -0.1506 -0.1344 85  ILE A CG2 
589  C CD1 . ILE A 79  ? 1.1178 0.6431 0.8993 0.0270  -0.1318 -0.1372 85  ILE A CD1 
590  N N   . ASP A 80  ? 1.1831 0.6789 0.9616 0.0519  -0.1933 -0.1612 86  ASP A N   
591  C CA  . ASP A 80  ? 1.2481 0.7307 1.0174 0.0587  -0.2080 -0.1624 86  ASP A CA  
592  C C   . ASP A 80  ? 1.2704 0.7282 1.0120 0.0566  -0.2016 -0.1506 86  ASP A C   
593  O O   . ASP A 80  ? 1.2533 0.7101 1.0012 0.0521  -0.2011 -0.1489 86  ASP A O   
594  C CB  . ASP A 80  ? 1.2630 0.7630 1.0640 0.0597  -0.2228 -0.1740 86  ASP A CB  
595  C CG  . ASP A 80  ? 1.4195 0.9079 1.2142 0.0679  -0.2400 -0.1768 86  ASP A CG  
596  O OD1 . ASP A 80  ? 1.4851 0.9481 1.2481 0.0710  -0.2397 -0.1679 86  ASP A OD1 
597  O OD2 . ASP A 80  ? 1.5297 1.0352 1.3523 0.0713  -0.2541 -0.1884 86  ASP A OD2 
598  N N   . LEU A 81  ? 1.3221 0.7604 1.0336 0.0599  -0.1971 -0.1428 87  LEU A N   
599  C CA  . LEU A 81  ? 1.3157 0.7318 1.0002 0.0578  -0.1889 -0.1317 87  LEU A CA  
600  C C   . LEU A 81  ? 1.3755 0.7795 1.0543 0.0617  -0.2026 -0.1327 87  LEU A C   
601  O O   . LEU A 81  ? 1.3459 0.7408 1.0168 0.0581  -0.1977 -0.1268 87  LEU A O   
602  C CB  . LEU A 81  ? 1.3328 0.7321 0.9880 0.0602  -0.1814 -0.1243 87  LEU A CB  
603  C CG  . LEU A 81  ? 1.3295 0.7353 0.9845 0.0545  -0.1636 -0.1193 87  LEU A CG  
604  C CD1 . LEU A 81  ? 1.3546 0.7434 0.9818 0.0566  -0.1572 -0.1124 87  LEU A CD1 
605  C CD2 . LEU A 81  ? 1.3199 0.7269 0.9778 0.0467  -0.1500 -0.1129 87  LEU A CD2 
606  N N   . LYS A 82  ? 1.4646 0.8684 1.1474 0.0695  -0.2203 -0.1402 88  LYS A N   
607  C CA  . LYS A 82  ? 1.5333 0.9233 1.2082 0.0743  -0.2347 -0.1410 88  LYS A CA  
608  C C   . LYS A 82  ? 1.5083 0.9095 1.2074 0.0695  -0.2380 -0.1446 88  LYS A C   
609  O O   . LYS A 82  ? 1.4781 0.8654 1.1651 0.0687  -0.2392 -0.1397 88  LYS A O   
610  C CB  . LYS A 82  ? 1.4772 0.8666 1.1550 0.0838  -0.2539 -0.1490 88  LYS A CB  
611  N N   . ASN A 83  ? 1.4285 0.8550 1.1620 0.0661  -0.2394 -0.1532 89  ASN A N   
612  C CA  . ASN A 83  ? 1.4045 0.8435 1.1646 0.0609  -0.2435 -0.1577 89  ASN A CA  
613  C C   . ASN A 83  ? 1.3113 0.7579 1.0781 0.0504  -0.2262 -0.1523 89  ASN A C   
614  O O   . ASN A 83  ? 1.3127 0.7736 1.1059 0.0445  -0.2283 -0.1568 89  ASN A O   
615  C CB  . ASN A 83  ? 1.4358 0.8992 1.2328 0.0634  -0.2578 -0.1719 89  ASN A CB  
616  C CG  . ASN A 83  ? 1.5635 1.0199 1.3550 0.0743  -0.2755 -0.1773 89  ASN A CG  
617  O OD1 . ASN A 83  ? 1.6075 1.0619 1.3879 0.0796  -0.2757 -0.1778 89  ASN A OD1 
618  N ND2 . ASN A 83  ? 1.6188 1.0704 1.4173 0.0779  -0.2910 -0.1810 89  ASN A ND2 
619  N N   . GLN A 84  ? 1.2637 0.7010 1.0081 0.0479  -0.2097 -0.1430 90  GLN A N   
620  C CA  . GLN A 84  ? 1.2623 0.7043 1.0096 0.0387  -0.1928 -0.1366 90  GLN A CA  
621  C C   . GLN A 84  ? 1.1779 0.6454 0.9607 0.0325  -0.1934 -0.1449 90  GLN A C   
622  O O   . GLN A 84  ? 1.1773 0.6507 0.9755 0.0254  -0.1924 -0.1446 90  GLN A O   
623  C CB  . GLN A 84  ? 1.2314 0.6583 0.9655 0.0353  -0.1889 -0.1282 90  GLN A CB  
624  C CG  . GLN A 84  ? 1.3021 0.7046 1.0021 0.0414  -0.1896 -0.1212 90  GLN A CG  
625  C CD  . GLN A 84  ? 1.2450 0.6372 0.9208 0.0394  -0.1716 -0.1110 90  GLN A CD  
626  O OE1 . GLN A 84  ? 1.2278 0.6151 0.8964 0.0343  -0.1596 -0.1032 90  GLN A OE1 
627  N NE2 . GLN A 84  ? 1.1803 0.5696 0.8442 0.0436  -0.1698 -0.1111 90  GLN A NE2 
628  N N   . MET A 85  ? 1.1753 0.6586 0.9715 0.0350  -0.1956 -0.1527 91  MET A N   
629  C CA  . MET A 85  ? 1.1734 0.6835 1.0043 0.0298  -0.1966 -0.1622 91  MET A CA  
630  C C   . MET A 85  ? 1.1262 0.6530 0.9568 0.0275  -0.1803 -0.1573 91  MET A C   
631  O O   . MET A 85  ? 1.1714 0.6744 0.9723 0.0314  -0.1760 -0.1533 91  MET A O   
632  C CB  . MET A 85  ? 1.1927 0.7207 1.0506 0.0356  -0.2142 -0.1765 91  MET A CB  
633  C CG  . MET A 85  ? 1.1816 0.7089 1.0535 0.0357  -0.2277 -0.1803 91  MET A CG  
634  S SD  . MET A 85  ? 1.2761 0.8289 1.1763 0.0219  -0.2160 -0.1737 91  MET A SD  
635  C CE  . MET A 85  ? 1.2007 0.7927 1.1521 0.0211  -0.2288 -0.1873 91  MET A CE  
636  N N   . VAL A 86  ? 1.1013 0.6720 0.9662 0.0209  -0.1701 -0.1564 92  VAL A N   
637  C CA  . VAL A 86  ? 1.0497 0.6413 0.9191 0.0191  -0.1562 -0.1530 92  VAL A CA  
638  C C   . VAL A 86  ? 1.0542 0.6862 0.9606 0.0197  -0.1597 -0.1625 92  VAL A C   
639  O O   . VAL A 86  ? 1.0215 0.6825 0.9582 0.0134  -0.1573 -0.1632 92  VAL A O   
640  C CB  . VAL A 86  ? 0.9954 0.5978 0.8643 0.0095  -0.1358 -0.1395 92  VAL A CB  
641  C CG1 . VAL A 86  ? 1.0020 0.6404 0.8912 0.0061  -0.1232 -0.1381 92  VAL A CG1 
642  C CG2 . VAL A 86  ? 0.9449 0.5089 0.7752 0.0110  -0.1299 -0.1313 92  VAL A CG2 
643  N N   . LEU A 87  ? 1.0776 0.7105 0.9812 0.0273  -0.1654 -0.1700 93  LEU A N   
644  C CA  . LEU A 87  ? 1.0641 0.7295 0.9996 0.0306  -0.1726 -0.1818 93  LEU A CA  
645  C C   . LEU A 87  ? 0.9977 0.7009 0.9533 0.0251  -0.1556 -0.1778 93  LEU A C   
646  O O   . LEU A 87  ? 0.9882 0.6855 0.9267 0.0257  -0.1464 -0.1724 93  LEU A O   
647  C CB  . LEU A 87  ? 1.0960 0.7407 1.0170 0.0426  -0.1893 -0.1929 93  LEU A CB  
648  C CG  . LEU A 87  ? 1.1125 0.7257 1.0213 0.0504  -0.2112 -0.2017 93  LEU A CG  
649  C CD1 . LEU A 87  ? 1.1282 0.6984 1.0009 0.0494  -0.2114 -0.1930 93  LEU A CD1 
650  C CD2 . LEU A 87  ? 1.1333 0.7315 1.0314 0.0624  -0.2273 -0.2134 93  LEU A CD2 
651  N N   . LEU A 88  ? 0.9823 0.7232 0.9734 0.0195  -0.1514 -0.1805 94  LEU A N   
652  C CA  . LEU A 88  ? 0.9778 0.7551 0.9884 0.0139  -0.1352 -0.1768 94  LEU A CA  
653  C C   . LEU A 88  ? 1.0599 0.8644 1.0950 0.0199  -0.1414 -0.1897 94  LEU A C   
654  O O   . LEU A 88  ? 1.1026 0.9130 1.1560 0.0239  -0.1552 -0.2008 94  LEU A O   
655  C CB  . LEU A 88  ? 0.9719 0.7725 1.0038 0.0025  -0.1237 -0.1698 94  LEU A CB  
656  C CG  . LEU A 88  ? 0.9283 0.7066 0.9394 -0.0043 -0.1158 -0.1567 94  LEU A CG  
657  C CD1 . LEU A 88  ? 0.8324 0.6369 0.8657 -0.0156 -0.1037 -0.1499 94  LEU A CD1 
658  C CD2 . LEU A 88  ? 0.8797 0.6406 0.8626 -0.0031 -0.1062 -0.1482 94  LEU A CD2 
659  N N   . GLN A 89  ? 1.0144 0.8352 1.0500 0.0209  -0.1317 -0.1885 95  GLN A N   
660  C CA  . GLN A 89  ? 1.0350 0.8845 1.0943 0.0264  -0.1354 -0.2003 95  GLN A CA  
661  C C   . GLN A 89  ? 1.0401 0.9253 1.1377 0.0207  -0.1326 -0.2051 95  GLN A C   
662  O O   . GLN A 89  ? 0.9651 0.8687 1.0736 0.0106  -0.1177 -0.1963 95  GLN A O   
663  C CB  . GLN A 89  ? 0.9914 0.8550 1.0461 0.0267  -0.1229 -0.1965 95  GLN A CB  
664  C CG  . GLN A 89  ? 1.0396 0.9270 1.1132 0.0345  -0.1285 -0.2095 95  GLN A CG  
665  C CD  . GLN A 89  ? 1.1053 1.0155 1.1822 0.0329  -0.1140 -0.2058 95  GLN A CD  
666  O OE1 . GLN A 89  ? 1.0424 0.9373 1.0960 0.0317  -0.1065 -0.1966 95  GLN A OE1 
667  N NE2 . GLN A 89  ? 1.1306 1.0777 1.2370 0.0329  -0.1097 -0.2131 95  GLN A NE2 
668  N N   . GLY A 90  ? 1.0580 0.9520 1.1761 0.0271  -0.1472 -0.2190 96  GLY A N   
669  C CA  . GLY A 90  ? 1.0545 0.9791 1.2104 0.0221  -0.1469 -0.2250 96  GLY A CA  
670  C C   . GLY A 90  ? 1.0576 0.9646 1.2180 0.0228  -0.1627 -0.2297 96  GLY A C   
671  O O   . GLY A 90  ? 1.0987 1.0299 1.2934 0.0205  -0.1665 -0.2378 96  GLY A O   
672  N N   . GLY A 91  ? 1.0328 0.8982 1.1602 0.0259  -0.1718 -0.2251 97  GLY A N   
673  C CA  . GLY A 91  ? 1.0858 0.9309 1.2144 0.0283  -0.1891 -0.2307 97  GLY A CA  
674  C C   . GLY A 91  ? 1.0894 0.9088 1.1979 0.0213  -0.1857 -0.2186 97  GLY A C   
675  O O   . GLY A 91  ? 1.1108 0.8942 1.1973 0.0264  -0.2004 -0.2202 97  GLY A O   
676  N N   . GLU A 92  ? 1.0684 0.9044 1.1824 0.0099  -0.1670 -0.2067 98  GLU A N   
677  C CA  . GLU A 92  ? 1.0527 0.8694 1.1536 0.0024  -0.1636 -0.1959 98  GLU A CA  
678  C C   . GLU A 92  ? 1.0807 0.8514 1.1372 0.0075  -0.1682 -0.1896 98  GLU A C   
679  O O   . GLU A 92  ? 1.0654 0.8246 1.0995 0.0123  -0.1642 -0.1874 98  GLU A O   
680  C CB  . GLU A 92  ? 0.9670 0.8076 1.0773 -0.0097 -0.1420 -0.1837 98  GLU A CB  
681  N N   . ALA A 93  ? 1.1548 0.8987 1.1988 0.0065  -0.1767 -0.1872 99  ALA A N   
682  C CA  . ALA A 93  ? 1.1378 0.8372 1.1396 0.0100  -0.1792 -0.1801 99  ALA A CA  
683  C C   . ALA A 93  ? 1.0964 0.7885 1.0914 0.0004  -0.1691 -0.1678 99  ALA A C   
684  O O   . ALA A 93  ? 1.0858 0.7939 1.1050 -0.0061 -0.1701 -0.1681 99  ALA A O   
685  C CB  . ALA A 93  ? 1.1158 0.7812 1.1015 0.0203  -0.2018 -0.1899 99  ALA A CB  
686  N N   . LEU A 94  ? 1.0835 0.7521 1.0467 -0.0004 -0.1591 -0.1571 100 LEU A N   
687  C CA  . LEU A 94  ? 1.0447 0.7041 0.9981 -0.0086 -0.1489 -0.1451 100 LEU A CA  
688  C C   . LEU A 94  ? 1.0454 0.6574 0.9618 -0.0033 -0.1577 -0.1428 100 LEU A C   
689  O O   . LEU A 94  ? 0.9764 0.5628 0.8626 0.0025  -0.1563 -0.1409 100 LEU A O   
690  C CB  . LEU A 94  ? 0.9895 0.6631 0.9388 -0.0147 -0.1284 -0.1342 100 LEU A CB  
691  C CG  . LEU A 94  ? 1.0077 0.7270 0.9916 -0.0212 -0.1179 -0.1348 100 LEU A CG  
692  C CD1 . LEU A 94  ? 1.0014 0.7305 0.9773 -0.0250 -0.1001 -0.1254 100 LEU A CD1 
693  C CD2 . LEU A 94  ? 1.0242 0.7626 1.0337 -0.0303 -0.1164 -0.1329 100 LEU A CD2 
694  N N   . PRO A 95  ? 1.0709 0.6688 0.9877 -0.0048 -0.1670 -0.1431 101 PRO A N   
695  C CA  . PRO A 95  ? 1.0504 0.6011 0.9297 0.0009  -0.1756 -0.1413 101 PRO A CA  
696  C C   . PRO A 95  ? 1.0262 0.5609 0.8811 -0.0040 -0.1596 -0.1278 101 PRO A C   
697  O O   . PRO A 95  ? 1.0155 0.5715 0.8857 -0.0133 -0.1469 -0.1198 101 PRO A O   
698  C CB  . PRO A 95  ? 1.0336 0.5800 0.9270 0.0001  -0.1908 -0.1465 101 PRO A CB  
699  C CG  . PRO A 95  ? 1.0407 0.6314 0.9751 -0.0103 -0.1820 -0.1449 101 PRO A CG  
700  C CD  . PRO A 95  ? 1.0104 0.6339 0.9624 -0.0109 -0.1721 -0.1470 101 PRO A CD  
701  N N   . PHE A 96  ? 1.0415 0.5377 0.8581 0.0023  -0.1603 -0.1254 102 PHE A N   
702  C CA  . PHE A 96  ? 1.0550 0.5339 0.8479 -0.0015 -0.1454 -0.1135 102 PHE A CA  
703  C C   . PHE A 96  ? 1.0761 0.5192 0.8369 0.0043  -0.1505 -0.1100 102 PHE A C   
704  O O   . PHE A 96  ? 1.1663 0.6015 0.9162 0.0128  -0.1601 -0.1135 102 PHE A O   
705  C CB  . PHE A 96  ? 1.0287 0.5112 0.8108 -0.0009 -0.1313 -0.1091 102 PHE A CB  
706  C CG  . PHE A 96  ? 1.0834 0.5423 0.8431 0.0086  -0.1396 -0.1155 102 PHE A CG  
707  C CD1 . PHE A 96  ? 1.1115 0.5515 0.8425 0.0134  -0.1345 -0.1075 102 PHE A CD1 
708  C CD2 . PHE A 96  ? 1.0962 0.5748 0.8733 0.0124  -0.1467 -0.1246 102 PHE A CD2 
709  C CE1 . PHE A 96  ? 1.1186 0.5521 0.8351 0.0211  -0.1382 -0.1092 102 PHE A CE1 
710  C CE2 . PHE A 96  ? 1.0917 0.5586 0.8519 0.0210  -0.1520 -0.1276 102 PHE A CE2 
711  C CZ  . PHE A 96  ? 1.0949 0.5410 0.8254 0.0248  -0.1470 -0.1189 102 PHE A CZ  
712  N N   . SER A 97  ? 0.9777 0.4116 0.7278 -0.0004 -0.1408 -0.1004 103 SER A N   
713  C CA  . SER A 97  ? 0.9917 0.4061 0.7131 0.0048  -0.1371 -0.0929 103 SER A CA  
714  C C   . SER A 97  ? 1.0727 0.4821 0.7747 0.0061  -0.1216 -0.0861 103 SER A C   
715  O O   . SER A 97  ? 1.0654 0.4613 0.7447 0.0125  -0.1215 -0.0837 103 SER A O   
716  C CB  . SER A 97  ? 1.0652 0.4734 0.7848 0.0000  -0.1341 -0.0864 103 SER A CB  
717  O OG  . SER A 97  ? 1.0563 0.4646 0.7693 -0.0056 -0.1165 -0.0771 103 SER A OG  
718  N N   . HIS A 98  ? 1.0550 0.4751 0.7658 -0.0003 -0.1088 -0.0831 104 HIS A N   
719  C CA  . HIS A 98  ? 1.0705 0.4892 0.7682 0.0000  -0.0940 -0.0774 104 HIS A CA  
720  C C   . HIS A 98  ? 1.0627 0.4966 0.7761 -0.0029 -0.0911 -0.0820 104 HIS A C   
721  O O   . HIS A 98  ? 0.9801 0.4365 0.7193 -0.0084 -0.0929 -0.0848 104 HIS A O   
722  C CB  . HIS A 98  ? 1.0555 0.4708 0.7457 -0.0050 -0.0786 -0.0671 104 HIS A CB  
723  C CG  . HIS A 98  ? 1.1043 0.5051 0.7777 -0.0021 -0.0799 -0.0625 104 HIS A CG  
724  N ND1 . HIS A 98  ? 1.0934 0.4905 0.7719 -0.0021 -0.0917 -0.0650 104 HIS A ND1 
725  C CD2 . HIS A 98  ? 1.0869 0.4757 0.7385 0.0008  -0.0712 -0.0561 104 HIS A CD2 
726  C CE1 . HIS A 98  ? 1.0703 0.4533 0.7295 0.0011  -0.0902 -0.0601 104 HIS A CE1 
727  N NE2 . HIS A 98  ? 1.1003 0.4780 0.7427 0.0028  -0.0777 -0.0548 104 HIS A NE2 
728  N N   . LEU A 99  ? 1.0463 0.4789 0.7491 0.0005  -0.0842 -0.0807 105 LEU A N   
729  C CA  . LEU A 99  ? 1.0175 0.4631 0.7319 -0.0005 -0.0825 -0.0857 105 LEU A CA  
730  C C   . LEU A 99  ? 1.0270 0.4729 0.7335 -0.0035 -0.0650 -0.0780 105 LEU A C   
731  O O   . LEU A 99  ? 1.0546 0.4903 0.7434 -0.0002 -0.0586 -0.0726 105 LEU A O   
732  C CB  . LEU A 99  ? 0.9881 0.4339 0.7007 0.0075  -0.0946 -0.0939 105 LEU A CB  
733  C CG  . LEU A 99  ? 1.0223 0.4844 0.7477 0.0077  -0.0935 -0.0996 105 LEU A CG  
734  C CD1 . LEU A 99  ? 0.9318 0.4376 0.6965 0.0034  -0.0958 -0.1032 105 LEU A CD1 
735  C CD2 . LEU A 99  ? 1.0125 0.4689 0.7285 0.0161  -0.1027 -0.1050 105 LEU A CD2 
736  N N   . ILE A 100 ? 0.9540 0.4326 0.6850 -0.0096 -0.0553 -0.0749 106 ILE A N   
737  C CA  . ILE A 100 ? 0.9194 0.4041 0.6489 -0.0124 -0.0399 -0.0686 106 ILE A CA  
738  C C   . ILE A 100 ? 0.8986 0.4071 0.6436 -0.0107 -0.0409 -0.0735 106 ILE A C   
739  O O   . ILE A 100 ? 0.9409 0.4819 0.7126 -0.0129 -0.0438 -0.0768 106 ILE A O   
740  C CB  . ILE A 100 ? 0.9415 0.4460 0.6863 -0.0203 -0.0277 -0.0603 106 ILE A CB  
741  C CG1 . ILE A 100 ? 0.8684 0.3481 0.5969 -0.0215 -0.0267 -0.0554 106 ILE A CG1 
742  C CG2 . ILE A 100 ? 0.8972 0.4112 0.6444 -0.0227 -0.0134 -0.0549 106 ILE A CG2 
743  C CD1 . ILE A 100 ? 0.8670 0.3625 0.6077 -0.0287 -0.0148 -0.0471 106 ILE A CD1 
744  N N   . LEU A 101 ? 0.9486 0.4407 0.6768 -0.0068 -0.0383 -0.0742 107 LEU A N   
745  C CA  . LEU A 101 ? 0.8821 0.3931 0.6220 -0.0044 -0.0399 -0.0791 107 LEU A CA  
746  C C   . LEU A 101 ? 0.9391 0.4645 0.6862 -0.0089 -0.0247 -0.0724 107 LEU A C   
747  O O   . LEU A 101 ? 0.9337 0.4376 0.6631 -0.0098 -0.0153 -0.0667 107 LEU A O   
748  C CB  . LEU A 101 ? 0.9227 0.4052 0.6394 0.0033  -0.0495 -0.0854 107 LEU A CB  
749  C CG  . LEU A 101 ? 0.9582 0.4333 0.6741 0.0086  -0.0673 -0.0942 107 LEU A CG  
750  C CD1 . LEU A 101 ? 1.0699 0.5299 0.7688 0.0162  -0.0754 -0.0971 107 LEU A CD1 
751  C CD2 . LEU A 101 ? 0.9396 0.4543 0.6891 0.0078  -0.0732 -0.1003 107 LEU A CD2 
752  N N   . ALA A 102 ? 0.8775 0.4389 0.6509 -0.0117 -0.0222 -0.0732 108 ALA A N   
753  C CA  . ALA A 102 ? 0.8429 0.4217 0.6269 -0.0165 -0.0088 -0.0668 108 ALA A CA  
754  C C   . ALA A 102 ? 0.7906 0.3989 0.5939 -0.0152 -0.0104 -0.0714 108 ALA A C   
755  O O   . ALA A 102 ? 0.8017 0.4392 0.6257 -0.0194 -0.0055 -0.0694 108 ALA A O   
756  C CB  . ALA A 102 ? 0.7473 0.3391 0.5429 -0.0232 -0.0017 -0.0600 108 ALA A CB  
757  N N   . THR A 103 ? 0.8426 0.4421 0.6379 -0.0092 -0.0176 -0.0779 109 THR A N   
758  C CA  . THR A 103 ? 0.8235 0.4488 0.6360 -0.0062 -0.0233 -0.0849 109 THR A CA  
759  C C   . THR A 103 ? 0.7852 0.4222 0.6027 -0.0065 -0.0158 -0.0830 109 THR A C   
760  O O   . THR A 103 ? 0.7652 0.4227 0.5954 -0.0036 -0.0199 -0.0888 109 THR A O   
761  C CB  . THR A 103 ? 0.8383 0.4481 0.6403 0.0014  -0.0376 -0.0942 109 THR A CB  
762  O OG1 . THR A 103 ? 0.9170 0.4940 0.6932 0.0044  -0.0369 -0.0929 109 THR A OG1 
763  C CG2 . THR A 103 ? 0.8550 0.4561 0.6554 0.0022  -0.0470 -0.0974 109 THR A CG2 
764  N N   . GLY A 104 ? 0.8380 0.4619 0.6460 -0.0096 -0.0053 -0.0757 110 GLY A N   
765  C CA  . GLY A 104 ? 0.8106 0.4471 0.6263 -0.0110 0.0026  -0.0729 110 GLY A CA  
766  C C   . GLY A 104 ? 0.8619 0.4966 0.6742 -0.0055 -0.0031 -0.0790 110 GLY A C   
767  O O   . GLY A 104 ? 0.8864 0.5015 0.6843 -0.0004 -0.0120 -0.0844 110 GLY A O   
768  N N   . SER A 105 ? 0.8409 0.4955 0.6662 -0.0063 0.0016  -0.0782 111 SER A N   
769  C CA  . SER A 105 ? 0.8656 0.5185 0.6882 -0.0016 -0.0027 -0.0831 111 SER A CA  
770  C C   . SER A 105 ? 0.8938 0.5779 0.7349 0.0014  -0.0080 -0.0892 111 SER A C   
771  O O   . SER A 105 ? 0.9106 0.6199 0.7681 -0.0018 -0.0044 -0.0876 111 SER A O   
772  C CB  . SER A 105 ? 0.9036 0.5501 0.7243 -0.0041 0.0067  -0.0776 111 SER A CB  
773  O OG  . SER A 105 ? 0.9380 0.5543 0.7409 -0.0064 0.0124  -0.0726 111 SER A OG  
774  N N   . THR A 106 ? 0.9242 0.6051 0.7614 0.0075  -0.0162 -0.0963 112 THR A N   
775  C CA  . THR A 106 ? 0.8075 0.5148 0.6597 0.0118  -0.0222 -0.1036 112 THR A CA  
776  C C   . THR A 106 ? 0.8600 0.5702 0.7129 0.0137  -0.0204 -0.1038 112 THR A C   
777  O O   . THR A 106 ? 0.8479 0.5346 0.6869 0.0138  -0.0190 -0.1014 112 THR A O   
778  C CB  . THR A 106 ? 0.8495 0.5499 0.6968 0.0183  -0.0355 -0.1130 112 THR A CB  
779  O OG1 . THR A 106 ? 0.9371 0.6663 0.8036 0.0191  -0.0386 -0.1181 112 THR A OG1 
780  C CG2 . THR A 106 ? 0.8576 0.5483 0.6965 0.0250  -0.0433 -0.1193 112 THR A CG2 
781  N N   . GLY A 107 ? 0.8547 0.5933 0.7238 0.0149  -0.0198 -0.1064 113 GLY A N   
782  C CA  . GLY A 107 ? 0.7882 0.5315 0.6595 0.0168  -0.0186 -0.1066 113 GLY A CA  
783  C C   . GLY A 107 ? 0.7882 0.5622 0.6752 0.0200  -0.0205 -0.1117 113 GLY A C   
784  O O   . GLY A 107 ? 0.8103 0.6032 0.7075 0.0203  -0.0217 -0.1150 113 GLY A O   
785  N N   . PRO A 108 ? 0.7729 0.5518 0.6618 0.0225  -0.0206 -0.1126 114 PRO A N   
786  C CA  . PRO A 108 ? 0.7503 0.5574 0.6522 0.0258  -0.0214 -0.1171 114 PRO A CA  
787  C C   . PRO A 108 ? 0.7100 0.5359 0.6222 0.0201  -0.0116 -0.1106 114 PRO A C   
788  O O   . PRO A 108 ? 0.7097 0.5267 0.6198 0.0144  -0.0043 -0.1024 114 PRO A O   
789  C CB  . PRO A 108 ? 0.7159 0.5169 0.6138 0.0301  -0.0252 -0.1194 114 PRO A CB  
790  C CG  . PRO A 108 ? 0.8319 0.6015 0.7152 0.0289  -0.0265 -0.1166 114 PRO A CG  
791  C CD  . PRO A 108 ? 0.8181 0.5760 0.6971 0.0225  -0.0201 -0.1100 114 PRO A CD  
792  N N   . PHE A 109 ? 0.7172 0.5685 0.6403 0.0218  -0.0113 -0.1146 115 PHE A N   
793  C CA  . PHE A 109 ? 0.7086 0.5786 0.6398 0.0177  -0.0029 -0.1095 115 PHE A CA  
794  C C   . PHE A 109 ? 0.6481 0.5166 0.5772 0.0194  -0.0019 -0.1075 115 PHE A C   
795  O O   . PHE A 109 ? 0.6608 0.5261 0.5870 0.0256  -0.0087 -0.1132 115 PHE A O   
796  C CB  . PHE A 109 ? 0.6716 0.5682 0.6136 0.0201  -0.0029 -0.1155 115 PHE A CB  
797  C CG  . PHE A 109 ? 0.6289 0.5428 0.5773 0.0149  0.0064  -0.1099 115 PHE A CG  
798  C CD1 . PHE A 109 ? 0.6680 0.5832 0.6195 0.0076  0.0125  -0.1040 115 PHE A CD1 
799  C CD2 . PHE A 109 ? 0.6642 0.5918 0.6141 0.0175  0.0087  -0.1106 115 PHE A CD2 
800  C CE1 . PHE A 109 ? 0.6592 0.5888 0.6150 0.0026  0.0210  -0.0986 115 PHE A CE1 
801  C CE2 . PHE A 109 ? 0.6175 0.5590 0.5706 0.0128  0.0172  -0.1053 115 PHE A CE2 
802  C CZ  . PHE A 109 ? 0.5767 0.5192 0.5328 0.0052  0.0234  -0.0992 115 PHE A CZ  
803  N N   . PRO A 110 ? 0.6749 0.5449 0.6056 0.0143  0.0055  -0.0997 116 PRO A N   
804  C CA  . PRO A 110 ? 0.6463 0.5194 0.5797 0.0069  0.0137  -0.0920 116 PRO A CA  
805  C C   . PRO A 110 ? 0.6732 0.5252 0.6012 0.0016  0.0168  -0.0856 116 PRO A C   
806  O O   . PRO A 110 ? 0.7054 0.5597 0.6355 -0.0042 0.0228  -0.0798 116 PRO A O   
807  C CB  . PRO A 110 ? 0.6632 0.5454 0.5990 0.0058  0.0181  -0.0879 116 PRO A CB  
808  C CG  . PRO A 110 ? 0.6461 0.5175 0.5787 0.0102  0.0132  -0.0899 116 PRO A CG  
809  C CD  . PRO A 110 ? 0.6545 0.5247 0.5849 0.0166  0.0051  -0.0988 116 PRO A CD  
810  N N   . GLY A 111 ? 0.6889 0.5199 0.6096 0.0031  0.0137  -0.0861 117 GLY A N   
811  C CA  . GLY A 111 ? 0.6721 0.4825 0.5869 -0.0019 0.0182  -0.0797 117 GLY A CA  
812  C C   . GLY A 111 ? 0.7436 0.5502 0.6558 -0.0050 0.0191  -0.0786 117 GLY A C   
813  O O   . GLY A 111 ? 0.6654 0.4648 0.5763 -0.0105 0.0251  -0.0719 117 GLY A O   
814  N N   . LYS A 112 ? 0.7150 0.5259 0.6268 -0.0012 0.0123  -0.0855 118 LYS A N   
815  C CA  . LYS A 112 ? 0.6885 0.4988 0.6003 -0.0035 0.0115  -0.0857 118 LYS A CA  
816  C C   . LYS A 112 ? 0.7183 0.5542 0.6418 -0.0015 0.0088  -0.0917 118 LYS A C   
817  O O   . LYS A 112 ? 0.7392 0.5890 0.6674 0.0034  0.0057  -0.0973 118 LYS A O   
818  C CB  . LYS A 112 ? 0.7298 0.5165 0.6295 -0.0007 0.0049  -0.0892 118 LYS A CB  
819  C CG  . LYS A 112 ? 0.7374 0.4959 0.6234 -0.0022 0.0077  -0.0845 118 LYS A CG  
820  C CD  . LYS A 112 ? 0.7575 0.5070 0.6412 -0.0089 0.0163  -0.0758 118 LYS A CD  
821  C CE  . LYS A 112 ? 0.8226 0.5418 0.6913 -0.0096 0.0189  -0.0725 118 LYS A CE  
822  N NZ  . LYS A 112 ? 0.7947 0.5056 0.6626 -0.0155 0.0288  -0.0640 118 LYS A NZ  
823  N N   . PHE A 113 ? 0.7376 0.5788 0.6658 -0.0052 0.0100  -0.0907 119 PHE A N   
824  C CA  . PHE A 113 ? 0.6650 0.5308 0.6063 -0.0047 0.0089  -0.0959 119 PHE A CA  
825  C C   . PHE A 113 ? 0.7124 0.5717 0.6549 -0.0062 0.0046  -0.0979 119 PHE A C   
826  O O   . PHE A 113 ? 0.7020 0.5578 0.6449 -0.0125 0.0093  -0.0916 119 PHE A O   
827  C CB  . PHE A 113 ? 0.6091 0.4938 0.5584 -0.0101 0.0180  -0.0902 119 PHE A CB  
828  C CG  . PHE A 113 ? 0.6159 0.5252 0.5788 -0.0113 0.0194  -0.0942 119 PHE A CG  
829  C CD1 . PHE A 113 ? 0.6718 0.5837 0.6406 -0.0171 0.0214  -0.0918 119 PHE A CD1 
830  C CD2 . PHE A 113 ? 0.6528 0.5827 0.6230 -0.0069 0.0193  -0.1003 119 PHE A CD2 
831  C CE1 . PHE A 113 ? 0.6794 0.6147 0.6628 -0.0190 0.0235  -0.0956 119 PHE A CE1 
832  C CE2 . PHE A 113 ? 0.6640 0.6173 0.6476 -0.0084 0.0220  -0.1042 119 PHE A CE2 
833  C CZ  . PHE A 113 ? 0.6755 0.6320 0.6665 -0.0147 0.0244  -0.1018 119 PHE A CZ  
834  N N   . ASN A 114 ? 0.7292 0.5855 0.6717 -0.0002 -0.0051 -0.1069 120 ASN A N   
835  C CA  . ASN A 114 ? 0.8206 0.6701 0.7646 -0.0004 -0.0114 -0.1103 120 ASN A CA  
836  C C   . ASN A 114 ? 0.8201 0.6939 0.7810 0.0034  -0.0167 -0.1203 120 ASN A C   
837  O O   . ASN A 114 ? 0.8525 0.7217 0.8127 0.0104  -0.0271 -0.1293 120 ASN A O   
838  C CB  . ASN A 114 ? 0.8683 0.6858 0.7943 0.0038  -0.0197 -0.1121 120 ASN A CB  
839  C CG  . ASN A 114 ? 0.8559 0.6506 0.7659 0.0008  -0.0133 -0.1032 120 ASN A CG  
840  O OD1 . ASN A 114 ? 0.8831 0.6702 0.7858 0.0038  -0.0132 -0.1033 120 ASN A OD1 
841  N ND2 . ASN A 114 ? 0.7998 0.5838 0.7055 -0.0053 -0.0079 -0.0957 120 ASN A ND2 
842  N N   . GLU A 115 ? 0.7883 0.6879 0.7644 -0.0011 -0.0091 -0.1187 121 GLU A N   
843  C CA  . GLU A 115 ? 0.7581 0.6843 0.7527 0.0014  -0.0111 -0.1275 121 GLU A CA  
844  C C   . GLU A 115 ? 0.7749 0.7123 0.7829 -0.0059 -0.0073 -0.1253 121 GLU A C   
845  O O   . GLU A 115 ? 0.7609 0.6978 0.7670 -0.0136 0.0016  -0.1157 121 GLU A O   
846  C CB  . GLU A 115 ? 0.7484 0.6973 0.7493 0.0025  -0.0039 -0.1281 121 GLU A CB  
847  C CG  . GLU A 115 ? 0.8462 0.7924 0.8402 0.0110  -0.0093 -0.1339 121 GLU A CG  
848  C CD  . GLU A 115 ? 1.0148 0.9866 1.0170 0.0124  -0.0026 -0.1359 121 GLU A CD  
849  O OE1 . GLU A 115 ? 1.0406 1.0337 1.0558 0.0076  0.0052  -0.1350 121 GLU A OE1 
850  O OE2 . GLU A 115 ? 1.0634 1.0333 1.0586 0.0183  -0.0048 -0.1383 121 GLU A OE2 
851  N N   . VAL A 116 ? 0.7781 0.7252 0.8003 -0.0034 -0.0146 -0.1343 122 VAL A N   
852  C CA  . VAL A 116 ? 0.7562 0.7209 0.7962 -0.0104 -0.0100 -0.1335 122 VAL A CA  
853  C C   . VAL A 116 ? 0.7673 0.7607 0.8191 -0.0139 0.0020  -0.1320 122 VAL A C   
854  O O   . VAL A 116 ? 0.7432 0.7517 0.7998 -0.0080 0.0019  -0.1387 122 VAL A O   
855  C CB  . VAL A 116 ? 0.7588 0.7285 0.8137 -0.0063 -0.0213 -0.1447 122 VAL A CB  
856  C CG1 . VAL A 116 ? 0.7426 0.7305 0.8182 -0.0142 -0.0168 -0.1441 122 VAL A CG1 
857  C CG2 . VAL A 116 ? 0.7853 0.7220 0.8231 -0.0020 -0.0337 -0.1458 122 VAL A CG2 
858  N N   . SER A 117 ? 0.7389 0.7383 0.7934 -0.0233 0.0123  -0.1230 123 SER A N   
859  C CA  . SER A 117 ? 0.7323 0.7524 0.7911 -0.0272 0.0247  -0.1190 123 SER A CA  
860  C C   . SER A 117 ? 0.7213 0.7429 0.7824 -0.0382 0.0337  -0.1092 123 SER A C   
861  O O   . SER A 117 ? 0.7270 0.7304 0.7826 -0.0420 0.0305  -0.1042 123 SER A O   
862  C CB  . SER A 117 ? 0.7264 0.7375 0.7678 -0.0237 0.0275  -0.1146 123 SER A CB  
863  O OG  . SER A 117 ? 0.7617 0.7469 0.7867 -0.0266 0.0269  -0.1057 123 SER A OG  
864  N N   . SER A 118 ? 0.6281 0.6697 0.6953 -0.0429 0.0451  -0.1063 124 SER A N   
865  C CA  . SER A 118 ? 0.6093 0.6497 0.6736 -0.0531 0.0545  -0.0954 124 SER A CA  
866  C C   . SER A 118 ? 0.5663 0.5895 0.6094 -0.0534 0.0580  -0.0860 124 SER A C   
867  O O   . SER A 118 ? 0.5510 0.5682 0.5842 -0.0462 0.0550  -0.0881 124 SER A O   
868  C CB  . SER A 118 ? 0.5902 0.6575 0.6685 -0.0587 0.0658  -0.0959 124 SER A CB  
869  O OG  . SER A 118 ? 0.6261 0.7056 0.7003 -0.0535 0.0706  -0.0988 124 SER A OG  
870  N N   . GLN A 119 ? 0.5141 0.5290 0.5515 -0.0616 0.0636  -0.0759 125 GLN A N   
871  C CA  . GLN A 119 ? 0.5405 0.5418 0.5605 -0.0626 0.0676  -0.0670 125 GLN A CA  
872  C C   . GLN A 119 ? 0.5916 0.6063 0.6077 -0.0598 0.0739  -0.0676 125 GLN A C   
873  O O   . GLN A 119 ? 0.6002 0.6053 0.6043 -0.0545 0.0719  -0.0667 125 GLN A O   
874  C CB  . GLN A 119 ? 0.5784 0.5719 0.5948 -0.0721 0.0730  -0.0569 125 GLN A CB  
875  C CG  . GLN A 119 ? 0.6434 0.6220 0.6428 -0.0731 0.0763  -0.0479 125 GLN A CG  
876  C CD  . GLN A 119 ? 0.6593 0.6251 0.6539 -0.0814 0.0790  -0.0385 125 GLN A CD  
877  O OE1 . GLN A 119 ? 0.6391 0.5869 0.6297 -0.0814 0.0737  -0.0366 125 GLN A OE1 
878  N NE2 . GLN A 119 ? 0.7155 0.6893 0.7091 -0.0882 0.0872  -0.0325 125 GLN A NE2 
879  N N   . GLN A 120 ? 0.5287 0.5653 0.5547 -0.0633 0.0816  -0.0695 126 GLN A N   
880  C CA  . GLN A 120 ? 0.5335 0.5812 0.5534 -0.0606 0.0881  -0.0697 126 GLN A CA  
881  C C   . GLN A 120 ? 0.5779 0.6311 0.5988 -0.0499 0.0820  -0.0794 126 GLN A C   
882  O O   . GLN A 120 ? 0.6084 0.6598 0.6180 -0.0452 0.0829  -0.0789 126 GLN A O   
883  C CB  . GLN A 120 ? 0.5291 0.5980 0.5582 -0.0672 0.0991  -0.0692 126 GLN A CB  
884  C CG  . GLN A 120 ? 0.5873 0.6494 0.6091 -0.0775 0.1069  -0.0580 126 GLN A CG  
885  C CD  . GLN A 120 ? 0.7227 0.7624 0.7245 -0.0771 0.1049  -0.0492 126 GLN A CD  
886  O OE1 . GLN A 120 ? 0.7163 0.7396 0.7143 -0.0815 0.1021  -0.0429 126 GLN A OE1 
887  N NE2 . GLN A 120 ? 0.6511 0.6901 0.6406 -0.0716 0.1061  -0.0492 126 GLN A NE2 
888  N N   . ALA A 121 ? 0.5836 0.6424 0.6173 -0.0457 0.0748  -0.0886 127 ALA A N   
889  C CA  . ALA A 121 ? 0.5720 0.6332 0.6053 -0.0351 0.0677  -0.0978 127 ALA A CA  
890  C C   . ALA A 121 ? 0.5779 0.6151 0.5955 -0.0304 0.0602  -0.0950 127 ALA A C   
891  O O   . ALA A 121 ? 0.6152 0.6513 0.6255 -0.0234 0.0576  -0.0980 127 ALA A O   
892  C CB  . ALA A 121 ? 0.5307 0.6012 0.5808 -0.0314 0.0604  -0.1086 127 ALA A CB  
893  N N   . ALA A 122 ? 0.5889 0.6065 0.6017 -0.0341 0.0567  -0.0894 128 ALA A N   
894  C CA  . ALA A 122 ? 0.6068 0.6012 0.6056 -0.0305 0.0511  -0.0863 128 ALA A CA  
895  C C   . ALA A 122 ? 0.5920 0.5826 0.5793 -0.0311 0.0564  -0.0795 128 ALA A C   
896  O O   . ALA A 122 ? 0.6100 0.5933 0.5898 -0.0250 0.0525  -0.0813 128 ALA A O   
897  C CB  . ALA A 122 ? 0.5376 0.5125 0.5330 -0.0351 0.0483  -0.0811 128 ALA A CB  
898  N N   . ILE A 123 ? 0.5756 0.5698 0.5614 -0.0386 0.0646  -0.0718 129 ILE A N   
899  C CA  . ILE A 123 ? 0.5905 0.5815 0.5654 -0.0392 0.0692  -0.0655 129 ILE A CA  
900  C C   . ILE A 123 ? 0.6178 0.6214 0.5910 -0.0322 0.0693  -0.0716 129 ILE A C   
901  O O   . ILE A 123 ? 0.6281 0.6234 0.5923 -0.0274 0.0664  -0.0709 129 ILE A O   
902  C CB  . ILE A 123 ? 0.5772 0.5726 0.5511 -0.0481 0.0780  -0.0576 129 ILE A CB  
903  C CG1 . ILE A 123 ? 0.5960 0.5762 0.5695 -0.0546 0.0772  -0.0511 129 ILE A CG1 
904  C CG2 . ILE A 123 ? 0.5299 0.5225 0.4916 -0.0479 0.0820  -0.0523 129 ILE A CG2 
905  C CD1 . ILE A 123 ? 0.5738 0.5568 0.5460 -0.0637 0.0851  -0.0431 129 ILE A CD1 
906  N N   . GLN A 124 ? 0.5791 0.6031 0.5618 -0.0313 0.0724  -0.0779 130 GLN A N   
907  C CA  . GLN A 124 ? 0.6206 0.6577 0.6015 -0.0245 0.0732  -0.0841 130 GLN A CA  
908  C C   . GLN A 124 ? 0.6708 0.7001 0.6493 -0.0150 0.0631  -0.0908 130 GLN A C   
909  O O   . GLN A 124 ? 0.6588 0.6891 0.6298 -0.0091 0.0618  -0.0929 130 GLN A O   
910  C CB  . GLN A 124 ? 0.5787 0.6397 0.5729 -0.0253 0.0786  -0.0906 130 GLN A CB  
911  C CG  . GLN A 124 ? 0.6970 0.7723 0.6871 -0.0196 0.0826  -0.0953 130 GLN A CG  
912  C CD  . GLN A 124 ? 0.7692 0.8381 0.7431 -0.0224 0.0891  -0.0867 130 GLN A CD  
913  O OE1 . GLN A 124 ? 0.8103 0.8738 0.7728 -0.0160 0.0861  -0.0877 130 GLN A OE1 
914  N NE2 . GLN A 124 ? 0.7361 0.8041 0.7084 -0.0319 0.0971  -0.0785 130 GLN A NE2 
915  N N   . ALA A 125 ? 0.5329 0.5529 0.5164 -0.0135 0.0556  -0.0942 131 ALA A N   
916  C CA  . ALA A 125 ? 0.5583 0.5678 0.5379 -0.0052 0.0460  -0.0999 131 ALA A CA  
917  C C   . ALA A 125 ? 0.5856 0.5785 0.5526 -0.0040 0.0446  -0.0942 131 ALA A C   
918  O O   . ALA A 125 ? 0.5885 0.5792 0.5511 0.0031  0.0394  -0.0986 131 ALA A O   
919  C CB  . ALA A 125 ? 0.5548 0.5522 0.5382 -0.0050 0.0387  -0.1027 131 ALA A CB  
920  N N   . TYR A 126 ? 0.5303 0.5116 0.4925 -0.0107 0.0486  -0.0847 132 TYR A N   
921  C CA  . TYR A 126 ? 0.5554 0.5217 0.5084 -0.0096 0.0471  -0.0798 132 TYR A CA  
922  C C   . TYR A 126 ? 0.6663 0.6409 0.6136 -0.0082 0.0509  -0.0780 132 TYR A C   
923  O O   . TYR A 126 ? 0.6656 0.6336 0.6073 -0.0032 0.0468  -0.0789 132 TYR A O   
924  C CB  . TYR A 126 ? 0.5401 0.4898 0.4905 -0.0163 0.0492  -0.0712 132 TYR A CB  
925  C CG  . TYR A 126 ? 0.5392 0.4732 0.4901 -0.0154 0.0438  -0.0729 132 TYR A CG  
926  C CD1 . TYR A 126 ? 0.5405 0.4756 0.4964 -0.0175 0.0427  -0.0752 132 TYR A CD1 
927  C CD2 . TYR A 126 ? 0.5606 0.4780 0.5064 -0.0121 0.0394  -0.0728 132 TYR A CD2 
928  C CE1 . TYR A 126 ? 0.5922 0.5105 0.5456 -0.0160 0.0373  -0.0770 132 TYR A CE1 
929  C CE2 . TYR A 126 ? 0.5770 0.4785 0.5209 -0.0112 0.0351  -0.0743 132 TYR A CE2 
930  C CZ  . TYR A 126 ? 0.6095 0.5105 0.5558 -0.0129 0.0339  -0.0763 132 TYR A CZ  
931  O OH  . TYR A 126 ? 0.6545 0.5369 0.5960 -0.0117 0.0293  -0.0778 132 TYR A OH  
932  N N   . GLU A 127 ? 0.6291 0.6171 0.5770 -0.0127 0.0587  -0.0755 133 GLU A N   
933  C CA  . GLU A 127 ? 0.6771 0.6721 0.6169 -0.0109 0.0624  -0.0744 133 GLU A CA  
934  C C   . GLU A 127 ? 0.6959 0.7005 0.6353 -0.0017 0.0582  -0.0835 133 GLU A C   
935  O O   . GLU A 127 ? 0.6957 0.6975 0.6261 0.0030  0.0563  -0.0837 133 GLU A O   
936  C CB  . GLU A 127 ? 0.7168 0.7244 0.6569 -0.0177 0.0724  -0.0705 133 GLU A CB  
937  C CG  . GLU A 127 ? 0.7245 0.7213 0.6621 -0.0265 0.0763  -0.0607 133 GLU A CG  
938  C CD  . GLU A 127 ? 0.8184 0.7999 0.7441 -0.0262 0.0747  -0.0542 133 GLU A CD  
939  O OE1 . GLU A 127 ? 0.8207 0.8021 0.7389 -0.0200 0.0720  -0.0566 133 GLU A OE1 
940  O OE2 . GLU A 127 ? 0.7674 0.7367 0.6919 -0.0320 0.0756  -0.0470 133 GLU A OE2 
941  N N   . ASP A 128 ? 0.6796 0.6950 0.6286 0.0014  0.0559  -0.0916 134 ASP A N   
942  C CA  . ASP A 128 ? 0.6490 0.6724 0.5982 0.0109  0.0507  -0.1011 134 ASP A CA  
943  C C   . ASP A 128 ? 0.6765 0.6831 0.6197 0.0167  0.0412  -0.1022 134 ASP A C   
944  O O   . ASP A 128 ? 0.6757 0.6833 0.6123 0.0233  0.0380  -0.1055 134 ASP A O   
945  C CB  . ASP A 128 ? 0.6435 0.6784 0.6052 0.0131  0.0483  -0.1097 134 ASP A CB  
946  C CG  . ASP A 128 ? 0.7791 0.8351 0.7493 0.0090  0.0577  -0.1111 134 ASP A CG  
947  O OD1 . ASP A 128 ? 0.8206 0.8807 0.7851 0.0038  0.0667  -0.1047 134 ASP A OD1 
948  O OD2 . ASP A 128 ? 0.8386 0.9066 0.8215 0.0109  0.0560  -0.1189 134 ASP A OD2 
949  N N   . MET A 129 ? 0.6547 0.6453 0.6000 0.0143  0.0368  -0.0995 135 MET A N   
950  C CA  . MET A 129 ? 0.6342 0.6077 0.5749 0.0182  0.0291  -0.0996 135 MET A CA  
951  C C   . MET A 129 ? 0.6479 0.6157 0.5808 0.0185  0.0300  -0.0945 135 MET A C   
952  O O   . MET A 129 ? 0.6930 0.6563 0.6221 0.0249  0.0237  -0.0980 135 MET A O   
953  C CB  . MET A 129 ? 0.6358 0.5922 0.5785 0.0136  0.0275  -0.0954 135 MET A CB  
954  C CG  . MET A 129 ? 0.6938 0.6319 0.6331 0.0168  0.0206  -0.0957 135 MET A CG  
955  S SD  . MET A 129 ? 0.7731 0.7083 0.7129 0.0251  0.0107  -0.1062 135 MET A SD  
956  C CE  . MET A 129 ? 0.6264 0.5594 0.5615 0.0322  0.0048  -0.1092 135 MET A CE  
957  N N   . VAL A 130 ? 0.6496 0.6167 0.5799 0.0119  0.0368  -0.0865 136 VAL A N   
958  C CA  . VAL A 130 ? 0.6222 0.5827 0.5447 0.0122  0.0369  -0.0817 136 VAL A CA  
959  C C   . VAL A 130 ? 0.6588 0.6293 0.5744 0.0193  0.0354  -0.0869 136 VAL A C   
960  O O   . VAL A 130 ? 0.6770 0.6397 0.5869 0.0240  0.0299  -0.0873 136 VAL A O   
961  C CB  . VAL A 130 ? 0.6663 0.6254 0.5861 0.0039  0.0446  -0.0728 136 VAL A CB  
962  C CG1 . VAL A 130 ? 0.5990 0.5516 0.5092 0.0049  0.0441  -0.0684 136 VAL A CG1 
963  C CG2 . VAL A 130 ? 0.6435 0.5908 0.5691 -0.0024 0.0455  -0.0677 136 VAL A CG2 
964  N N   . ARG A 131 ? 0.6632 0.6507 0.5793 0.0203  0.0403  -0.0912 137 ARG A N   
965  C CA  . ARG A 131 ? 0.6636 0.6606 0.5720 0.0276  0.0397  -0.0967 137 ARG A CA  
966  C C   . ARG A 131 ? 0.6618 0.6563 0.5719 0.0367  0.0296  -0.1051 137 ARG A C   
967  O O   . ARG A 131 ? 0.6867 0.6797 0.5885 0.0435  0.0252  -0.1081 137 ARG A O   
968  C CB  . ARG A 131 ? 0.6531 0.6699 0.5631 0.0262  0.0487  -0.0995 137 ARG A CB  
969  C CG  . ARG A 131 ? 0.7673 0.7862 0.6729 0.0176  0.0589  -0.0912 137 ARG A CG  
970  C CD  . ARG A 131 ? 0.8850 0.9220 0.8000 0.0131  0.0677  -0.0935 137 ARG A CD  
971  N NE  . ARG A 131 ? 0.9664 1.0011 0.8832 0.0026  0.0750  -0.0848 137 ARG A NE  
972  C CZ  . ARG A 131 ? 0.9763 1.0243 0.9033 -0.0034 0.0824  -0.0851 137 ARG A CZ  
973  N NH1 . ARG A 131 ? 1.0399 1.1052 0.9777 0.0002  0.0835  -0.0940 137 ARG A NH1 
974  N NH2 . ARG A 131 ? 0.8743 0.9183 0.8015 -0.0130 0.0885  -0.0768 137 ARG A NH2 
975  N N   . GLN A 132 ? 0.6443 0.6366 0.5637 0.0371  0.0252  -0.1090 138 GLN A N   
976  C CA  . GLN A 132 ? 0.6399 0.6265 0.5598 0.0452  0.0148  -0.1163 138 GLN A CA  
977  C C   . GLN A 132 ? 0.6651 0.6341 0.5804 0.0464  0.0086  -0.1127 138 GLN A C   
978  O O   . GLN A 132 ? 0.6438 0.6095 0.5553 0.0539  0.0009  -0.1177 138 GLN A O   
979  C CB  . GLN A 132 ? 0.6234 0.6064 0.5519 0.0446  0.0110  -0.1199 138 GLN A CB  
980  C CG  . GLN A 132 ? 0.6032 0.6030 0.5394 0.0435  0.0156  -0.1244 138 GLN A CG  
981  C CD  . GLN A 132 ? 0.6832 0.7018 0.6186 0.0503  0.0170  -0.1322 138 GLN A CD  
982  O OE1 . GLN A 132 ? 0.6664 0.6845 0.5985 0.0589  0.0096  -0.1392 138 GLN A OE1 
983  N NE2 . GLN A 132 ? 0.7620 0.7968 0.7002 0.0463  0.0270  -0.1310 138 GLN A NE2 
984  N N   . VAL A 133 ? 0.6802 0.6381 0.5970 0.0392  0.0115  -0.1043 139 VAL A N   
985  C CA  . VAL A 133 ? 0.6333 0.5751 0.5491 0.0397  0.0059  -0.1011 139 VAL A CA  
986  C C   . VAL A 133 ? 0.6273 0.5702 0.5345 0.0427  0.0054  -0.0995 139 VAL A C   
987  O O   . VAL A 133 ? 0.6840 0.6193 0.5889 0.0483  -0.0026 -0.1022 139 VAL A O   
988  C CB  . VAL A 133 ? 0.6392 0.5691 0.5605 0.0314  0.0096  -0.0933 139 VAL A CB  
989  C CG1 . VAL A 133 ? 0.6627 0.5793 0.5841 0.0308  0.0064  -0.0889 139 VAL A CG1 
990  C CG2 . VAL A 133 ? 0.5945 0.5172 0.5215 0.0308  0.0069  -0.0959 139 VAL A CG2 
991  N N   . GLN A 134 ? 0.6554 0.6067 0.5566 0.0392  0.0134  -0.0955 140 GLN A N   
992  C CA  . GLN A 134 ? 0.6297 0.5812 0.5190 0.0425  0.0131  -0.0944 140 GLN A CA  
993  C C   . GLN A 134 ? 0.5912 0.5487 0.4742 0.0525  0.0073  -0.1030 140 GLN A C   
994  O O   . GLN A 134 ? 0.5959 0.5452 0.4723 0.0581  0.0000  -0.1043 140 GLN A O   
995  C CB  . GLN A 134 ? 0.6207 0.5806 0.5034 0.0367  0.0238  -0.0890 140 GLN A CB  
996  C CG  . GLN A 134 ? 0.6542 0.6023 0.5362 0.0296  0.0261  -0.0798 140 GLN A CG  
997  C CD  . GLN A 134 ? 0.6725 0.6267 0.5558 0.0207  0.0364  -0.0739 140 GLN A CD  
998  O OE1 . GLN A 134 ? 0.7179 0.6865 0.6018 0.0195  0.0430  -0.0764 140 GLN A OE1 
999  N NE2 . GLN A 134 ? 0.6521 0.5952 0.5366 0.0145  0.0377  -0.0663 140 GLN A NE2 
1000 N N   . ARG A 135 ? 0.6029 0.5740 0.4888 0.0553  0.0094  -0.1095 141 ARG A N   
1001 C CA  . ARG A 135 ? 0.6626 0.6405 0.5429 0.0652  0.0043  -0.1184 141 ARG A CA  
1002 C C   . ARG A 135 ? 0.6428 0.6082 0.5253 0.0714  -0.0084 -0.1227 141 ARG A C   
1003 O O   . ARG A 135 ? 0.6567 0.6221 0.5315 0.0800  -0.0148 -0.1285 141 ARG A O   
1004 C CB  . ARG A 135 ? 0.6656 0.6602 0.5523 0.0668  0.0081  -0.1253 141 ARG A CB  
1005 C CG  . ARG A 135 ? 0.6953 0.7061 0.5810 0.0621  0.0207  -0.1234 141 ARG A CG  
1006 C CD  . ARG A 135 ? 0.7238 0.7526 0.6133 0.0681  0.0224  -0.1333 141 ARG A CD  
1007 N NE  . ARG A 135 ? 0.8903 0.9208 0.7678 0.0779  0.0185  -0.1393 141 ARG A NE  
1008 C CZ  . ARG A 135 ? 0.8622 0.9065 0.7405 0.0856  0.0181  -0.1490 141 ARG A CZ  
1009 N NH1 . ARG A 135 ? 0.8408 0.8995 0.7325 0.0848  0.0212  -0.1543 141 ARG A NH1 
1010 N NH2 . ARG A 135 ? 0.8209 0.8640 0.6864 0.0949  0.0139  -0.1540 141 ARG A NH2 
1011 N N   . SER A 136 ? 0.6353 0.5635 0.6050 -0.0353 0.0113  -0.0469 142 SER A N   
1012 C CA  . SER A 136 ? 0.6119 0.5303 0.5783 -0.0364 0.0120  -0.0518 142 SER A CA  
1013 C C   . SER A 136 ? 0.6191 0.5386 0.5889 -0.0386 0.0133  -0.0555 142 SER A C   
1014 O O   . SER A 136 ? 0.7243 0.6461 0.6978 -0.0409 0.0146  -0.0540 142 SER A O   
1015 C CB  . SER A 136 ? 0.6103 0.5151 0.5720 -0.0395 0.0130  -0.0506 142 SER A CB  
1016 O OG  . SER A 136 ? 0.6012 0.5055 0.5603 -0.0376 0.0112  -0.0472 142 SER A OG  
1017 N N   . ARG A 137 ? 0.5731 0.4906 0.5419 -0.0378 0.0128  -0.0606 143 ARG A N   
1018 C CA  . ARG A 137 ? 0.6357 0.5530 0.6082 -0.0407 0.0138  -0.0644 143 ARG A CA  
1019 C C   . ARG A 137 ? 0.6284 0.5323 0.5988 -0.0451 0.0160  -0.0662 143 ARG A C   
1020 O O   . ARG A 137 ? 0.6171 0.5201 0.5913 -0.0488 0.0180  -0.0671 143 ARG A O   
1021 C CB  . ARG A 137 ? 0.6275 0.5508 0.6007 -0.0380 0.0116  -0.0693 143 ARG A CB  
1022 C CG  . ARG A 137 ? 0.6659 0.5872 0.6428 -0.0415 0.0120  -0.0741 143 ARG A CG  
1023 C CD  . ARG A 137 ? 0.7315 0.6623 0.7153 -0.0429 0.0126  -0.0729 143 ARG A CD  
1024 N NE  . ARG A 137 ? 0.8005 0.7442 0.7853 -0.0385 0.0104  -0.0715 143 ARG A NE  
1025 C CZ  . ARG A 137 ? 0.7950 0.7490 0.7850 -0.0382 0.0097  -0.0711 143 ARG A CZ  
1026 N NH1 . ARG A 137 ? 0.7552 0.7090 0.7508 -0.0418 0.0109  -0.0724 143 ARG A NH1 
1027 N NH2 . ARG A 137 ? 0.8142 0.7793 0.8039 -0.0339 0.0079  -0.0693 143 ARG A NH2 
1028 N N   . PHE A 138 ? 0.6262 0.5201 0.5906 -0.0446 0.0156  -0.0666 144 PHE A N   
1029 C CA  . PHE A 138 ? 0.6234 0.5037 0.5845 -0.0486 0.0178  -0.0674 144 PHE A CA  
1030 C C   . PHE A 138 ? 0.6482 0.5211 0.6040 -0.0490 0.0186  -0.0629 144 PHE A C   
1031 O O   . PHE A 138 ? 0.6475 0.5216 0.6002 -0.0455 0.0165  -0.0607 144 PHE A O   
1032 C CB  . PHE A 138 ? 0.6121 0.4851 0.5699 -0.0477 0.0163  -0.0716 144 PHE A CB  
1033 C CG  . PHE A 138 ? 0.6167 0.4961 0.5792 -0.0475 0.0149  -0.0767 144 PHE A CG  
1034 C CD1 . PHE A 138 ? 0.6472 0.5374 0.6108 -0.0427 0.0121  -0.0783 144 PHE A CD1 
1035 C CD2 . PHE A 138 ? 0.6260 0.5009 0.5919 -0.0523 0.0164  -0.0798 144 PHE A CD2 
1036 C CE1 . PHE A 138 ? 0.6119 0.5077 0.5788 -0.0424 0.0104  -0.0832 144 PHE A CE1 
1037 C CE2 . PHE A 138 ? 0.6904 0.5712 0.6608 -0.0524 0.0144  -0.0847 144 PHE A CE2 
1038 C CZ  . PHE A 138 ? 0.5832 0.4741 0.5536 -0.0473 0.0112  -0.0866 144 PHE A CZ  
1039 N N   . ILE A 139 ? 0.6141 0.4802 0.5691 -0.0531 0.0216  -0.0615 145 ILE A N   
1040 C CA  . ILE A 139 ? 0.6104 0.4687 0.5596 -0.0540 0.0224  -0.0576 145 ILE A CA  
1041 C C   . ILE A 139 ? 0.6136 0.4585 0.5580 -0.0579 0.0255  -0.0582 145 ILE A C   
1042 O O   . ILE A 139 ? 0.6082 0.4525 0.5563 -0.0612 0.0283  -0.0603 145 ILE A O   
1043 C CB  . ILE A 139 ? 0.6035 0.4679 0.5558 -0.0546 0.0233  -0.0546 145 ILE A CB  
1044 C CG1 . ILE A 139 ? 0.6168 0.4949 0.5743 -0.0511 0.0206  -0.0537 145 ILE A CG1 
1045 C CG2 . ILE A 139 ? 0.5751 0.4312 0.5208 -0.0554 0.0235  -0.0511 145 ILE A CG2 
1046 C CD1 . ILE A 139 ? 0.5876 0.4718 0.5485 -0.0513 0.0208  -0.0503 145 ILE A CD1 
1047 N N   . VAL A 140 ? 0.6352 0.4698 0.5716 -0.0574 0.0248  -0.0562 146 VAL A N   
1048 C CA  . VAL A 140 ? 0.6341 0.4552 0.5643 -0.0609 0.0278  -0.0557 146 VAL A CA  
1049 C C   . VAL A 140 ? 0.6321 0.4486 0.5566 -0.0617 0.0286  -0.0519 146 VAL A C   
1050 O O   . VAL A 140 ? 0.6489 0.4660 0.5701 -0.0589 0.0254  -0.0495 146 VAL A O   
1051 C CB  . VAL A 140 ? 0.6772 0.4883 0.6015 -0.0598 0.0261  -0.0564 146 VAL A CB  
1052 C CG1 . VAL A 140 ? 0.6709 0.4673 0.5869 -0.0631 0.0289  -0.0544 146 VAL A CG1 
1053 C CG2 . VAL A 140 ? 0.6645 0.4776 0.5937 -0.0599 0.0256  -0.0607 146 VAL A CG2 
1054 N N   . VAL A 141 ? 0.6513 0.4637 0.5749 -0.0652 0.0329  -0.0516 147 VAL A N   
1055 C CA  . VAL A 141 ? 0.6469 0.4519 0.5629 -0.0662 0.0342  -0.0487 147 VAL A CA  
1056 C C   . VAL A 141 ? 0.6744 0.4652 0.5813 -0.0683 0.0364  -0.0480 147 VAL A C   
1057 O O   . VAL A 141 ? 0.6892 0.4765 0.5975 -0.0714 0.0401  -0.0494 147 VAL A O   
1058 C CB  . VAL A 141 ? 0.6538 0.4631 0.5736 -0.0681 0.0378  -0.0488 147 VAL A CB  
1059 C CG1 . VAL A 141 ? 0.6627 0.4627 0.5731 -0.0689 0.0393  -0.0464 147 VAL A CG1 
1060 C CG2 . VAL A 141 ? 0.5996 0.4224 0.5283 -0.0659 0.0355  -0.0491 147 VAL A CG2 
1061 N N   . VAL A 142 ? 0.6427 0.4255 0.5404 -0.0668 0.0338  -0.0454 148 VAL A N   
1062 C CA  . VAL A 142 ? 0.7051 0.4737 0.5929 -0.0682 0.0352  -0.0440 148 VAL A CA  
1063 C C   . VAL A 142 ? 0.7717 0.5332 0.6513 -0.0703 0.0384  -0.0420 148 VAL A C   
1064 O O   . VAL A 142 ? 0.7498 0.5102 0.6243 -0.0687 0.0357  -0.0402 148 VAL A O   
1065 C CB  . VAL A 142 ? 0.7640 0.5278 0.6461 -0.0648 0.0301  -0.0425 148 VAL A CB  
1066 C CG1 . VAL A 142 ? 0.6839 0.4324 0.5549 -0.0662 0.0315  -0.0405 148 VAL A CG1 
1067 C CG2 . VAL A 142 ? 0.7377 0.5083 0.6271 -0.0621 0.0272  -0.0448 148 VAL A CG2 
1068 N N   . GLY A 143 ? 0.7470 0.5036 0.6254 -0.0739 0.0442  -0.0424 149 GLY A N   
1069 C CA  . GLY A 143 ? 0.7172 0.4667 0.5870 -0.0756 0.0479  -0.0407 149 GLY A CA  
1070 C C   . GLY A 143 ? 0.7739 0.5304 0.6504 -0.0774 0.0530  -0.0423 149 GLY A C   
1071 O O   . GLY A 143 ? 0.7700 0.5367 0.6540 -0.0759 0.0513  -0.0435 149 GLY A O   
1072 N N   . GLY A 144 ? 0.7986 0.5500 0.6728 -0.0807 0.0592  -0.0421 150 GLY A N   
1073 C CA  . GLY A 144 ? 0.7950 0.5525 0.6750 -0.0824 0.0648  -0.0434 150 GLY A CA  
1074 C C   . GLY A 144 ? 0.8403 0.5911 0.7098 -0.0822 0.0682  -0.0420 150 GLY A C   
1075 O O   . GLY A 144 ? 0.8399 0.5903 0.7096 -0.0843 0.0749  -0.0422 150 GLY A O   
1076 N N   . GLY A 145 ? 0.8637 0.6092 0.7239 -0.0796 0.0637  -0.0408 151 GLY A N   
1077 C CA  . GLY A 145 ? 0.8399 0.5807 0.6914 -0.0787 0.0657  -0.0405 151 GLY A CA  
1078 C C   . GLY A 145 ? 0.8621 0.6136 0.7235 -0.0773 0.0657  -0.0427 151 GLY A C   
1079 O O   . GLY A 145 ? 0.8546 0.6172 0.7289 -0.0770 0.0642  -0.0441 151 GLY A O   
1080 N N   . SER A 146 ? 0.8684 0.6161 0.7230 -0.0761 0.0674  -0.0431 152 SER A N   
1081 C CA  . SER A 146 ? 0.8566 0.6130 0.7198 -0.0744 0.0674  -0.0450 152 SER A CA  
1082 C C   . SER A 146 ? 0.7948 0.5596 0.6668 -0.0728 0.0604  -0.0450 152 SER A C   
1083 O O   . SER A 146 ? 0.7668 0.5421 0.6504 -0.0720 0.0605  -0.0463 152 SER A O   
1084 C CB  . SER A 146 ? 0.8938 0.6426 0.7464 -0.0729 0.0686  -0.0456 152 SER A CB  
1085 O OG  . SER A 146 ? 0.9529 0.6958 0.7983 -0.0740 0.0762  -0.0458 152 SER A OG  
1086 N N   . ALA A 147 ? 0.7733 0.5341 0.6399 -0.0721 0.0544  -0.0434 153 ALA A N   
1087 C CA  . ALA A 147 ? 0.7204 0.4891 0.5945 -0.0705 0.0479  -0.0428 153 ALA A CA  
1088 C C   . ALA A 147 ? 0.7633 0.5423 0.6493 -0.0707 0.0474  -0.0434 153 ALA A C   
1089 O O   . ALA A 147 ? 0.7187 0.5083 0.6150 -0.0695 0.0455  -0.0440 153 ALA A O   
1090 C CB  . ALA A 147 ? 0.7166 0.4785 0.5817 -0.0696 0.0419  -0.0408 153 ALA A CB  
1091 N N   . GLY A 148 ? 0.7202 0.4955 0.6042 -0.0721 0.0490  -0.0433 154 GLY A N   
1092 C CA  . GLY A 148 ? 0.7362 0.5201 0.6306 -0.0722 0.0482  -0.0445 154 GLY A CA  
1093 C C   . GLY A 148 ? 0.7703 0.5634 0.6755 -0.0732 0.0524  -0.0466 154 GLY A C   
1094 O O   . GLY A 148 ? 0.7085 0.5126 0.6241 -0.0722 0.0502  -0.0477 154 GLY A O   
1095 N N   . VAL A 149 ? 0.7263 0.5157 0.6293 -0.0751 0.0584  -0.0471 155 VAL A N   
1096 C CA  . VAL A 149 ? 0.7219 0.5204 0.6357 -0.0760 0.0627  -0.0490 155 VAL A CA  
1097 C C   . VAL A 149 ? 0.7138 0.5221 0.6353 -0.0734 0.0600  -0.0495 155 VAL A C   
1098 O O   . VAL A 149 ? 0.6958 0.5152 0.6288 -0.0730 0.0595  -0.0508 155 VAL A O   
1099 C CB  . VAL A 149 ? 0.7742 0.5668 0.6831 -0.0778 0.0698  -0.0490 155 VAL A CB  
1100 C CG1 . VAL A 149 ? 0.8405 0.6428 0.7597 -0.0775 0.0735  -0.0507 155 VAL A CG1 
1101 C CG2 . VAL A 149 ? 0.7796 0.5664 0.6858 -0.0813 0.0734  -0.0485 155 VAL A CG2 
1102 N N   . GLU A 150 ? 0.6793 0.4832 0.5944 -0.0715 0.0579  -0.0484 156 GLU A N   
1103 C CA  . GLU A 150 ? 0.6860 0.4979 0.6080 -0.0692 0.0553  -0.0484 156 GLU A CA  
1104 C C   . GLU A 150 ? 0.7131 0.5329 0.6410 -0.0678 0.0492  -0.0474 156 GLU A C   
1105 O O   . GLU A 150 ? 0.6528 0.4827 0.5899 -0.0663 0.0477  -0.0476 156 GLU A O   
1106 C CB  . GLU A 150 ? 0.7205 0.5245 0.6340 -0.0679 0.0544  -0.0476 156 GLU A CB  
1107 C CG  . GLU A 150 ? 0.8368 0.6347 0.7452 -0.0682 0.0606  -0.0489 156 GLU A CG  
1108 C CD  . GLU A 150 ? 0.9024 0.6906 0.8002 -0.0669 0.0589  -0.0485 156 GLU A CD  
1109 O OE1 . GLU A 150 ? 0.9648 0.7468 0.8548 -0.0672 0.0542  -0.0470 156 GLU A OE1 
1110 O OE2 . GLU A 150 ? 0.8647 0.6516 0.7620 -0.0655 0.0619  -0.0498 156 GLU A OE2 
1111 N N   . MET A 151 ? 0.6869 0.5021 0.6090 -0.0679 0.0457  -0.0463 157 MET A N   
1112 C CA  . MET A 151 ? 0.6486 0.4713 0.5755 -0.0663 0.0405  -0.0453 157 MET A CA  
1113 C C   . MET A 151 ? 0.6939 0.5266 0.6307 -0.0663 0.0412  -0.0473 157 MET A C   
1114 O O   . MET A 151 ? 0.6814 0.5246 0.6260 -0.0645 0.0385  -0.0471 157 MET A O   
1115 C CB  . MET A 151 ? 0.6705 0.4858 0.5891 -0.0661 0.0372  -0.0439 157 MET A CB  
1116 C CG  . MET A 151 ? 0.6164 0.4392 0.5394 -0.0641 0.0322  -0.0430 157 MET A CG  
1117 S SD  . MET A 151 ? 0.8338 0.6614 0.7582 -0.0623 0.0272  -0.0400 157 MET A SD  
1118 C CE  . MET A 151 ? 0.6873 0.5279 0.6236 -0.0614 0.0282  -0.0406 157 MET A CE  
1119 N N   . ALA A 152 ? 0.6441 0.4736 0.5808 -0.0685 0.0448  -0.0491 158 ALA A N   
1120 C CA  . ALA A 152 ? 0.6282 0.4663 0.5740 -0.0690 0.0452  -0.0514 158 ALA A CA  
1121 C C   . ALA A 152 ? 0.6203 0.4685 0.5758 -0.0686 0.0470  -0.0524 158 ALA A C   
1122 O O   . ALA A 152 ? 0.7193 0.5780 0.6831 -0.0674 0.0449  -0.0535 158 ALA A O   
1123 C CB  . ALA A 152 ? 0.6195 0.4507 0.5631 -0.0722 0.0488  -0.0529 158 ALA A CB  
1124 N N   . ALA A 153 ? 0.6657 0.5108 0.6200 -0.0692 0.0510  -0.0521 159 ALA A N   
1125 C CA  . ALA A 153 ? 0.6852 0.5396 0.6488 -0.0683 0.0527  -0.0529 159 ALA A CA  
1126 C C   . ALA A 153 ? 0.6332 0.4942 0.5999 -0.0652 0.0483  -0.0512 159 ALA A C   
1127 O O   . ALA A 153 ? 0.6188 0.4903 0.5947 -0.0638 0.0476  -0.0517 159 ALA A O   
1128 C CB  . ALA A 153 ? 0.6649 0.5136 0.6254 -0.0690 0.0582  -0.0531 159 ALA A CB  
1129 N N   . GLU A 154 ? 0.6299 0.4847 0.5891 -0.0642 0.0453  -0.0490 160 GLU A N   
1130 C CA  . GLU A 154 ? 0.6185 0.4785 0.5802 -0.0618 0.0411  -0.0467 160 GLU A CA  
1131 C C   . GLU A 154 ? 0.6390 0.5096 0.6069 -0.0605 0.0374  -0.0465 160 GLU A C   
1132 O O   . GLU A 154 ? 0.6428 0.5228 0.6177 -0.0586 0.0358  -0.0455 160 GLU A O   
1133 C CB  . GLU A 154 ? 0.6399 0.4904 0.5922 -0.0619 0.0386  -0.0445 160 GLU A CB  
1134 C CG  . GLU A 154 ? 0.7105 0.5616 0.6635 -0.0605 0.0359  -0.0421 160 GLU A CG  
1135 C CD  . GLU A 154 ? 0.7524 0.6026 0.7078 -0.0598 0.0390  -0.0429 160 GLU A CD  
1136 O OE1 . GLU A 154 ? 0.7299 0.5701 0.6781 -0.0604 0.0419  -0.0440 160 GLU A OE1 
1137 O OE2 . GLU A 154 ? 0.7894 0.6492 0.7537 -0.0581 0.0384  -0.0424 160 GLU A OE2 
1138 N N   . ILE A 155 ? 0.6197 0.4887 0.5848 -0.0611 0.0362  -0.0474 161 ILE A N   
1139 C CA  . ILE A 155 ? 0.5984 0.4769 0.5682 -0.0594 0.0329  -0.0477 161 ILE A CA  
1140 C C   . ILE A 155 ? 0.6451 0.5331 0.6239 -0.0594 0.0342  -0.0503 161 ILE A C   
1141 O O   . ILE A 155 ? 0.6441 0.5426 0.6285 -0.0572 0.0317  -0.0498 161 ILE A O   
1142 C CB  . ILE A 155 ? 0.6320 0.5052 0.5963 -0.0597 0.0316  -0.0487 161 ILE A CB  
1143 C CG1 . ILE A 155 ? 0.6181 0.4843 0.5748 -0.0592 0.0294  -0.0458 161 ILE A CG1 
1144 C CG2 . ILE A 155 ? 0.5721 0.4548 0.5409 -0.0576 0.0288  -0.0500 161 ILE A CG2 
1145 C CD1 . ILE A 155 ? 0.6484 0.5060 0.5982 -0.0598 0.0290  -0.0466 161 ILE A CD1 
1146 N N   . LYS A 156 ? 0.5999 0.4846 0.5799 -0.0619 0.0381  -0.0529 162 LYS A N   
1147 C CA  . LYS A 156 ? 0.6102 0.5043 0.5994 -0.0622 0.0388  -0.0556 162 LYS A CA  
1148 C C   . LYS A 156 ? 0.6031 0.5053 0.5992 -0.0605 0.0392  -0.0545 162 LYS A C   
1149 O O   . LYS A 156 ? 0.6065 0.5194 0.6104 -0.0593 0.0377  -0.0557 162 LYS A O   
1150 C CB  . LYS A 156 ? 0.5852 0.4745 0.5753 -0.0658 0.0430  -0.0582 162 LYS A CB  
1151 C CG  . LYS A 156 ? 0.6455 0.5344 0.6359 -0.0672 0.0415  -0.0609 162 LYS A CG  
1152 C CD  . LYS A 156 ? 0.6040 0.5053 0.6034 -0.0662 0.0389  -0.0633 162 LYS A CD  
1153 C CE  . LYS A 156 ? 0.6360 0.5355 0.6351 -0.0677 0.0372  -0.0667 162 LYS A CE  
1154 N NZ  . LYS A 156 ? 0.6788 0.5892 0.6868 -0.0677 0.0350  -0.0700 162 LYS A NZ  
1155 N N   . THR A 157 ? 0.6172 0.5141 0.6105 -0.0601 0.0411  -0.0524 163 THR A N   
1156 C CA  . THR A 157 ? 0.6164 0.5202 0.6164 -0.0580 0.0413  -0.0514 163 THR A CA  
1157 C C   . THR A 157 ? 0.5951 0.5064 0.5972 -0.0551 0.0366  -0.0487 163 THR A C   
1158 O O   . THR A 157 ? 0.5776 0.4987 0.5872 -0.0532 0.0355  -0.0485 163 THR A O   
1159 C CB  . THR A 157 ? 0.6072 0.5024 0.6030 -0.0580 0.0445  -0.0503 163 THR A CB  
1160 O OG1 . THR A 157 ? 0.6571 0.5458 0.6503 -0.0606 0.0494  -0.0524 163 THR A OG1 
1161 C CG2 . THR A 157 ? 0.5491 0.4511 0.5524 -0.0555 0.0450  -0.0496 163 THR A CG2 
1162 N N   . GLU A 158 ? 0.5912 0.4982 0.5868 -0.0548 0.0339  -0.0464 164 GLU A N   
1163 C CA  . GLU A 158 ? 0.5668 0.4810 0.5641 -0.0523 0.0298  -0.0431 164 GLU A CA  
1164 C C   . GLU A 158 ? 0.6150 0.5389 0.6153 -0.0511 0.0273  -0.0444 164 GLU A C   
1165 O O   . GLU A 158 ? 0.5771 0.5103 0.5810 -0.0486 0.0246  -0.0423 164 GLU A O   
1166 C CB  . GLU A 158 ? 0.5511 0.4582 0.5413 -0.0526 0.0278  -0.0401 164 GLU A CB  
1167 C CG  . GLU A 158 ? 0.6605 0.5574 0.6466 -0.0536 0.0294  -0.0389 164 GLU A CG  
1168 C CD  . GLU A 158 ? 0.6820 0.5825 0.6736 -0.0519 0.0294  -0.0371 164 GLU A CD  
1169 O OE1 . GLU A 158 ? 0.7447 0.6511 0.7391 -0.0504 0.0262  -0.0337 164 GLU A OE1 
1170 O OE2 . GLU A 158 ? 0.6612 0.5586 0.6542 -0.0519 0.0328  -0.0390 164 GLU A OE2 
1171 N N   . TYR A 159 ? 0.6162 0.5376 0.6146 -0.0526 0.0281  -0.0479 165 TYR A N   
1172 C CA  . TYR A 159 ? 0.5747 0.5033 0.5743 -0.0513 0.0255  -0.0498 165 TYR A CA  
1173 C C   . TYR A 159 ? 0.5888 0.5172 0.5915 -0.0534 0.0273  -0.0546 165 TYR A C   
1174 O O   . TYR A 159 ? 0.6020 0.5243 0.6007 -0.0549 0.0276  -0.0569 165 TYR A O   
1175 C CB  . TYR A 159 ? 0.5587 0.4831 0.5516 -0.0506 0.0237  -0.0488 165 TYR A CB  
1176 C CG  . TYR A 159 ? 0.5541 0.4788 0.5447 -0.0492 0.0219  -0.0439 165 TYR A CG  
1177 C CD1 . TYR A 159 ? 0.5932 0.5285 0.5870 -0.0464 0.0193  -0.0411 165 TYR A CD1 
1178 C CD2 . TYR A 159 ? 0.5731 0.4877 0.5585 -0.0508 0.0226  -0.0419 165 TYR A CD2 
1179 C CE1 . TYR A 159 ? 0.6040 0.5398 0.5967 -0.0457 0.0177  -0.0362 165 TYR A CE1 
1180 C CE2 . TYR A 159 ? 0.5958 0.5107 0.5799 -0.0500 0.0205  -0.0375 165 TYR A CE2 
1181 C CZ  . TYR A 159 ? 0.6260 0.5514 0.6141 -0.0477 0.0182  -0.0345 165 TYR A CZ  
1182 O OH  . TYR A 159 ? 0.6458 0.5714 0.6333 -0.0476 0.0162  -0.0298 165 TYR A OH  
1183 N N   . PRO A 160 ? 0.5926 0.5276 0.6027 -0.0537 0.0283  -0.0559 166 PRO A N   
1184 C CA  . PRO A 160 ? 0.6405 0.5767 0.6552 -0.0562 0.0297  -0.0603 166 PRO A CA  
1185 C C   . PRO A 160 ? 0.6470 0.5848 0.6601 -0.0561 0.0268  -0.0636 166 PRO A C   
1186 O O   . PRO A 160 ? 0.6400 0.5731 0.6535 -0.0592 0.0281  -0.0670 166 PRO A O   
1187 C CB  . PRO A 160 ? 0.6583 0.6054 0.6824 -0.0551 0.0294  -0.0606 166 PRO A CB  
1188 C CG  . PRO A 160 ? 0.5980 0.5452 0.6215 -0.0527 0.0297  -0.0562 166 PRO A CG  
1189 C CD  . PRO A 160 ? 0.5707 0.5126 0.5860 -0.0516 0.0280  -0.0532 166 PRO A CD  
1190 N N   . GLU A 161 ? 0.6235 0.5674 0.6346 -0.0527 0.0232  -0.0626 167 GLU A N   
1191 C CA  . GLU A 161 ? 0.6347 0.5812 0.6441 -0.0515 0.0202  -0.0661 167 GLU A CA  
1192 C C   . GLU A 161 ? 0.6241 0.5604 0.6255 -0.0518 0.0202  -0.0665 167 GLU A C   
1193 O O   . GLU A 161 ? 0.6398 0.5766 0.6389 -0.0505 0.0179  -0.0697 167 GLU A O   
1194 C CB  . GLU A 161 ? 0.6504 0.6083 0.6603 -0.0471 0.0167  -0.0646 167 GLU A CB  
1195 C CG  . GLU A 161 ? 0.7013 0.6581 0.7056 -0.0446 0.0161  -0.0599 167 GLU A CG  
1196 C CD  . GLU A 161 ? 0.6545 0.6106 0.6603 -0.0448 0.0176  -0.0548 167 GLU A CD  
1197 O OE1 . GLU A 161 ? 0.6256 0.5804 0.6358 -0.0467 0.0197  -0.0550 167 GLU A OE1 
1198 O OE2 . GLU A 161 ? 0.6834 0.6405 0.6861 -0.0429 0.0166  -0.0506 167 GLU A OE2 
1199 N N   . LYS A 162 ? 0.5981 0.5251 0.5949 -0.0531 0.0225  -0.0636 168 LYS A N   
1200 C CA  . LYS A 162 ? 0.5889 0.5060 0.5784 -0.0533 0.0223  -0.0641 168 LYS A CA  
1201 C C   . LYS A 162 ? 0.5834 0.4913 0.5725 -0.0574 0.0247  -0.0674 168 LYS A C   
1202 O O   . LYS A 162 ? 0.6232 0.5323 0.6178 -0.0603 0.0270  -0.0686 168 LYS A O   
1203 C CB  . LYS A 162 ? 0.5526 0.4641 0.5368 -0.0527 0.0229  -0.0595 168 LYS A CB  
1204 C CG  . LYS A 162 ? 0.5590 0.4797 0.5440 -0.0490 0.0204  -0.0561 168 LYS A CG  
1205 C CD  . LYS A 162 ? 0.6029 0.5186 0.5831 -0.0486 0.0201  -0.0517 168 LYS A CD  
1206 C CE  . LYS A 162 ? 0.6257 0.5522 0.6084 -0.0454 0.0177  -0.0480 168 LYS A CE  
1207 N NZ  . LYS A 162 ? 0.6286 0.5625 0.6107 -0.0419 0.0154  -0.0494 168 LYS A NZ  
1208 N N   . GLU A 163 ? 0.5903 0.4896 0.5735 -0.0574 0.0240  -0.0687 169 GLU A N   
1209 C CA  . GLU A 163 ? 0.6574 0.5461 0.6390 -0.0613 0.0261  -0.0711 169 GLU A CA  
1210 C C   . GLU A 163 ? 0.6351 0.5121 0.6091 -0.0623 0.0282  -0.0677 169 GLU A C   
1211 O O   . GLU A 163 ? 0.6303 0.5032 0.5980 -0.0596 0.0261  -0.0664 169 GLU A O   
1212 C CB  . GLU A 163 ? 0.6762 0.5625 0.6562 -0.0605 0.0233  -0.0754 169 GLU A CB  
1213 C CG  . GLU A 163 ? 0.7703 0.6667 0.7570 -0.0600 0.0208  -0.0796 169 GLU A CG  
1214 C CD  . GLU A 163 ? 0.8982 0.7948 0.8922 -0.0652 0.0229  -0.0821 169 GLU A CD  
1215 O OE1 . GLU A 163 ? 0.8361 0.7250 0.8298 -0.0691 0.0269  -0.0802 169 GLU A OE1 
1216 O OE2 . GLU A 163 ? 0.9617 0.8666 0.9617 -0.0654 0.0205  -0.0858 169 GLU A OE2 
1217 N N   . VAL A 164 ? 0.6717 0.5435 0.6459 -0.0658 0.0322  -0.0664 170 VAL A N   
1218 C CA  . VAL A 164 ? 0.6570 0.5178 0.6232 -0.0668 0.0344  -0.0632 170 VAL A CA  
1219 C C   . VAL A 164 ? 0.6339 0.4834 0.5970 -0.0709 0.0375  -0.0643 170 VAL A C   
1220 O O   . VAL A 164 ? 0.6659 0.5168 0.6346 -0.0744 0.0408  -0.0657 170 VAL A O   
1221 C CB  . VAL A 164 ? 0.6412 0.5045 0.6086 -0.0670 0.0368  -0.0604 170 VAL A CB  
1222 C CG1 . VAL A 164 ? 0.6269 0.4787 0.5848 -0.0676 0.0382  -0.0574 170 VAL A CG1 
1223 C CG2 . VAL A 164 ? 0.6407 0.5155 0.6124 -0.0635 0.0338  -0.0591 170 VAL A CG2 
1224 N N   . THR A 165 ? 0.6183 0.4569 0.5729 -0.0704 0.0366  -0.0633 171 THR A N   
1225 C CA  . THR A 165 ? 0.7069 0.5330 0.6568 -0.0742 0.0396  -0.0632 171 THR A CA  
1226 C C   . THR A 165 ? 0.6719 0.4882 0.6123 -0.0744 0.0415  -0.0593 171 THR A C   
1227 O O   . THR A 165 ? 0.6907 0.5053 0.6254 -0.0710 0.0385  -0.0573 171 THR A O   
1228 C CB  . THR A 165 ? 0.6752 0.4949 0.6224 -0.0735 0.0367  -0.0654 171 THR A CB  
1229 O OG1 . THR A 165 ? 0.7074 0.5350 0.6631 -0.0741 0.0352  -0.0696 171 THR A OG1 
1230 C CG2 . THR A 165 ? 0.6806 0.4857 0.6217 -0.0773 0.0396  -0.0644 171 THR A CG2 
1231 N N   . LEU A 166 ? 0.6909 0.5011 0.6294 -0.0782 0.0466  -0.0583 172 LEU A N   
1232 C CA  . LEU A 166 ? 0.7006 0.5004 0.6288 -0.0787 0.0488  -0.0549 172 LEU A CA  
1233 C C   . LEU A 166 ? 0.6940 0.4804 0.6153 -0.0816 0.0509  -0.0541 172 LEU A C   
1234 O O   . LEU A 166 ? 0.7075 0.4928 0.6333 -0.0855 0.0542  -0.0554 172 LEU A O   
1235 C CB  . LEU A 166 ? 0.6993 0.5021 0.6293 -0.0803 0.0535  -0.0541 172 LEU A CB  
1236 C CG  . LEU A 166 ? 0.6687 0.4604 0.5875 -0.0811 0.0567  -0.0511 172 LEU A CG  
1237 C CD1 . LEU A 166 ? 0.7101 0.4990 0.6213 -0.0776 0.0523  -0.0492 172 LEU A CD1 
1238 C CD2 . LEU A 166 ? 0.7173 0.5127 0.6391 -0.0826 0.0621  -0.0512 172 LEU A CD2 
1239 N N   . ILE A 167 ? 0.7029 0.4793 0.6136 -0.0797 0.0487  -0.0516 173 ILE A N   
1240 C CA  . ILE A 167 ? 0.7836 0.5462 0.6866 -0.0818 0.0499  -0.0503 173 ILE A CA  
1241 C C   . ILE A 167 ? 0.7703 0.5229 0.6618 -0.0826 0.0528  -0.0466 173 ILE A C   
1242 O O   . ILE A 167 ? 0.7664 0.5187 0.6521 -0.0795 0.0500  -0.0450 173 ILE A O   
1243 C CB  . ILE A 167 ? 0.7989 0.5572 0.6987 -0.0783 0.0443  -0.0507 173 ILE A CB  
1244 C CG1 . ILE A 167 ? 0.7596 0.5272 0.6697 -0.0774 0.0417  -0.0549 173 ILE A CG1 
1245 C CG2 . ILE A 167 ? 0.7733 0.5158 0.6638 -0.0801 0.0454  -0.0486 173 ILE A CG2 
1246 C CD1 . ILE A 167 ? 0.7311 0.4980 0.6392 -0.0726 0.0361  -0.0559 173 ILE A CD1 
1247 N N   . HIS A 168 ? 0.8174 0.5618 0.7053 -0.0868 0.0581  -0.0452 174 HIS A N   
1248 C CA  . HIS A 168 ? 0.8499 0.5861 0.7271 -0.0878 0.0620  -0.0420 174 HIS A CA  
1249 C C   . HIS A 168 ? 0.8640 0.5865 0.7332 -0.0911 0.0654  -0.0394 174 HIS A C   
1250 O O   . HIS A 168 ? 0.8670 0.5890 0.7426 -0.0949 0.0681  -0.0404 174 HIS A O   
1251 C CB  . HIS A 168 ? 0.7760 0.5199 0.6582 -0.0895 0.0674  -0.0428 174 HIS A CB  
1252 C CG  . HIS A 168 ? 0.8741 0.6100 0.7445 -0.0898 0.0713  -0.0400 174 HIS A CG  
1253 N ND1 . HIS A 168 ? 0.8720 0.5996 0.7298 -0.0869 0.0677  -0.0379 174 HIS A ND1 
1254 C CD2 . HIS A 168 ? 0.8798 0.6144 0.7484 -0.0926 0.0785  -0.0391 174 HIS A CD2 
1255 C CE1 . HIS A 168 ? 0.8429 0.5640 0.6910 -0.0878 0.0723  -0.0360 174 HIS A CE1 
1256 N NE2 . HIS A 168 ? 0.8938 0.6189 0.7479 -0.0911 0.0792  -0.0367 174 HIS A NE2 
1257 N N   . SER A 169 ? 0.8950 0.6062 0.7501 -0.0900 0.0652  -0.0360 175 SER A N   
1258 C CA  . SER A 169 ? 0.8896 0.5863 0.7353 -0.0924 0.0673  -0.0328 175 SER A CA  
1259 C C   . SER A 169 ? 0.9236 0.6173 0.7686 -0.0976 0.0758  -0.0311 175 SER A C   
1260 O O   . SER A 169 ? 0.9595 0.6444 0.8028 -0.1012 0.0783  -0.0292 175 SER A O   
1261 C CB  . SER A 169 ? 0.8817 0.5676 0.7121 -0.0890 0.0639  -0.0295 175 SER A CB  
1262 O OG  . SER A 169 ? 0.9430 0.6302 0.7669 -0.0881 0.0658  -0.0287 175 SER A OG  
1263 N N   . GLN A 170 ? 0.9479 0.6486 0.7945 -0.0982 0.0804  -0.0316 176 GLN A N   
1264 C CA  . GLN A 170 ? 0.9599 0.6596 0.8071 -0.1028 0.0890  -0.0301 176 GLN A CA  
1265 C C   . GLN A 170 ? 0.9596 0.6723 0.8244 -0.1060 0.0917  -0.0333 176 GLN A C   
1266 O O   . GLN A 170 ? 0.9452 0.6662 0.8206 -0.1047 0.0867  -0.0366 176 GLN A O   
1267 C CB  . GLN A 170 ? 1.0243 0.7236 0.8626 -0.1014 0.0933  -0.0289 176 GLN A CB  
1268 C CG  . GLN A 170 ? 1.0776 0.7621 0.8976 -0.1011 0.0947  -0.0246 176 GLN A CG  
1269 C CD  . GLN A 170 ? 1.1230 0.8004 0.9342 -0.0969 0.0863  -0.0239 176 GLN A CD  
1270 O OE1 . GLN A 170 ? 1.1711 0.8553 0.9854 -0.0932 0.0807  -0.0264 176 GLN A OE1 
1271 N NE2 . GLN A 170 ? 1.1524 0.8165 0.9531 -0.0976 0.0853  -0.0203 176 GLN A NE2 
1272 N N   . VAL A 171 ? 0.9893 0.7041 0.8571 -0.1100 0.0996  -0.0321 177 VAL A N   
1273 C CA  . VAL A 171 ? 0.9816 0.7089 0.8663 -0.1135 0.1028  -0.0347 177 VAL A CA  
1274 C C   . VAL A 171 ? 0.9781 0.7183 0.8694 -0.1115 0.1057  -0.0369 177 VAL A C   
1275 O O   . VAL A 171 ? 0.9499 0.7033 0.8563 -0.1121 0.1052  -0.0401 177 VAL A O   
1276 C CB  . VAL A 171 ? 1.0112 0.7334 0.8978 -0.1202 0.1097  -0.0318 177 VAL A CB  
1277 C CG1 . VAL A 171 ? 0.9374 0.6488 0.8086 -0.1208 0.1161  -0.0271 177 VAL A CG1 
1278 C CG2 . VAL A 171 ? 0.9546 0.6911 0.8589 -0.1241 0.1141  -0.0341 177 VAL A CG2 
1279 N N   . ALA A 172 ? 0.9829 0.7196 0.8630 -0.1085 0.1081  -0.0355 178 ALA A N   
1280 C CA  . ALA A 172 ? 0.9414 0.6883 0.8258 -0.1054 0.1098  -0.0377 178 ALA A CA  
1281 C C   . ALA A 172 ? 0.9594 0.7062 0.8388 -0.1000 0.1024  -0.0392 178 ALA A C   
1282 O O   . ALA A 172 ? 0.9482 0.6846 0.8156 -0.0982 0.0979  -0.0375 178 ALA A O   
1283 C CB  . ALA A 172 ? 0.8626 0.6058 0.7381 -0.1058 0.1181  -0.0356 178 ALA A CB  
1284 N N   . LEU A 173 ? 0.9056 0.6641 0.7942 -0.0974 0.1011  -0.0420 179 LEU A N   
1285 C CA  . LEU A 173 ? 0.9051 0.6649 0.7913 -0.0928 0.0940  -0.0432 179 LEU A CA  
1286 C C   . LEU A 173 ? 0.9219 0.6786 0.7987 -0.0897 0.0957  -0.0431 179 LEU A C   
1287 O O   . LEU A 173 ? 0.9402 0.6969 0.8152 -0.0903 0.1027  -0.0429 179 LEU A O   
1288 C CB  . LEU A 173 ? 0.8502 0.6242 0.7521 -0.0917 0.0902  -0.0462 179 LEU A CB  
1289 C CG  . LEU A 173 ? 0.8862 0.6626 0.7964 -0.0945 0.0879  -0.0470 179 LEU A CG  
1290 C CD1 . LEU A 173 ? 0.8334 0.6246 0.7596 -0.0941 0.0860  -0.0500 179 LEU A CD1 
1291 C CD2 . LEU A 173 ? 0.8665 0.6349 0.7692 -0.0929 0.0813  -0.0461 179 LEU A CD2 
1292 N N   . ALA A 174 ? 0.8637 0.6176 0.7345 -0.0862 0.0891  -0.0432 180 ALA A N   
1293 C CA  . ALA A 174 ? 0.9123 0.6618 0.7735 -0.0831 0.0887  -0.0435 180 ALA A CA  
1294 C C   . ALA A 174 ? 0.9206 0.6569 0.7650 -0.0837 0.0928  -0.0414 180 ALA A C   
1295 O O   . ALA A 174 ? 0.9310 0.6611 0.7708 -0.0866 0.0958  -0.0392 180 ALA A O   
1296 C CB  . ALA A 174 ? 0.8815 0.6407 0.7517 -0.0816 0.0921  -0.0458 180 ALA A CB  
1297 N N   . ASP A 175 ? 0.9290 0.6607 0.7639 -0.0811 0.0931  -0.0421 181 ASP A N   
1298 C CA  . ASP A 175 ? 1.0030 0.7212 0.8193 -0.0808 0.0951  -0.0403 181 ASP A CA  
1299 C C   . ASP A 175 ? 1.0234 0.7388 0.8360 -0.0834 0.1047  -0.0389 181 ASP A C   
1300 O O   . ASP A 175 ? 1.0067 0.7302 0.8281 -0.0838 0.1112  -0.0403 181 ASP A O   
1301 C CB  . ASP A 175 ? 1.0547 0.7692 0.8626 -0.0773 0.0932  -0.0422 181 ASP A CB  
1302 C CG  . ASP A 175 ? 1.1267 0.8397 0.9330 -0.0754 0.0833  -0.0424 181 ASP A CG  
1303 O OD1 . ASP A 175 ? 1.1652 0.8726 0.9659 -0.0761 0.0786  -0.0402 181 ASP A OD1 
1304 O OD2 . ASP A 175 ? 1.1326 0.8504 0.9441 -0.0732 0.0802  -0.0446 181 ASP A OD2 
1305 N N   . LYS A 176 ? 1.0485 0.7524 0.8479 -0.0849 0.1056  -0.0357 182 LYS A N   
1306 C CA  . LYS A 176 ? 1.0768 0.7773 0.8719 -0.0879 0.1148  -0.0333 182 LYS A CA  
1307 C C   . LYS A 176 ? 1.0813 0.7817 0.8700 -0.0860 0.1222  -0.0346 182 LYS A C   
1308 O O   . LYS A 176 ? 1.0751 0.7797 0.8682 -0.0882 0.1311  -0.0339 182 LYS A O   
1309 C CB  . LYS A 176 ? 1.0906 0.7772 0.8704 -0.0893 0.1137  -0.0292 182 LYS A CB  
1310 C CG  . LYS A 176 ? 1.1077 0.7852 0.8742 -0.0860 0.1051  -0.0290 182 LYS A CG  
1311 N N   . GLU A 177 ? 1.0561 0.7521 0.8350 -0.0820 0.1188  -0.0368 183 GLU A N   
1312 C CA  . GLU A 177 ? 1.0664 0.7610 0.8376 -0.0795 0.1254  -0.0386 183 GLU A CA  
1313 C C   . GLU A 177 ? 0.9946 0.7025 0.7819 -0.0782 0.1292  -0.0419 183 GLU A C   
1314 O O   . GLU A 177 ? 1.0634 0.7710 0.8457 -0.0754 0.1346  -0.0440 183 GLU A O   
1315 C CB  . GLU A 177 ? 1.1309 0.8152 0.8857 -0.0757 0.1198  -0.0403 183 GLU A CB  
1316 C CG  . GLU A 177 ? 1.1696 0.8410 0.9085 -0.0762 0.1141  -0.0373 183 GLU A CG  
1317 C CD  . GLU A 177 ? 1.2757 0.9493 1.0224 -0.0766 0.1038  -0.0369 183 GLU A CD  
1318 O OE1 . GLU A 177 ? 1.1611 0.8465 0.9259 -0.0772 0.1022  -0.0384 183 GLU A OE1 
1319 O OE2 . GLU A 177 ? 1.3309 0.9951 1.0656 -0.0761 0.0975  -0.0351 183 GLU A OE2 
1320 N N   . LEU A 178 ? 0.9535 0.6729 0.7594 -0.0797 0.1264  -0.0426 184 LEU A N   
1321 C CA  . LEU A 178 ? 0.9021 0.6346 0.7235 -0.0782 0.1297  -0.0455 184 LEU A CA  
1322 C C   . LEU A 178 ? 0.9265 0.6659 0.7555 -0.0810 0.1399  -0.0443 184 LEU A C   
1323 O O   . LEU A 178 ? 0.9019 0.6380 0.7286 -0.0851 0.1432  -0.0410 184 LEU A O   
1324 C CB  . LEU A 178 ? 0.9339 0.6764 0.7718 -0.0784 0.1224  -0.0467 184 LEU A CB  
1325 C CG  . LEU A 178 ? 0.9784 0.7181 0.8135 -0.0753 0.1129  -0.0482 184 LEU A CG  
1326 C CD1 . LEU A 178 ? 0.9221 0.6723 0.7732 -0.0762 0.1068  -0.0486 184 LEU A CD1 
1327 C CD2 . LEU A 178 ? 0.9195 0.6589 0.7518 -0.0710 0.1135  -0.0512 184 LEU A CD2 
1328 N N   . LEU A 179 ? 0.8519 0.6010 0.6903 -0.0787 0.1450  -0.0468 185 LEU A N   
1329 C CA  . LEU A 179 ? 0.8798 0.6394 0.7302 -0.0813 0.1541  -0.0460 185 LEU A CA  
1330 C C   . LEU A 179 ? 0.8966 0.6636 0.7619 -0.0865 0.1517  -0.0443 185 LEU A C   
1331 O O   . LEU A 179 ? 0.9218 0.6946 0.7975 -0.0861 0.1441  -0.0459 185 LEU A O   
1332 C CB  . LEU A 179 ? 0.8491 0.6204 0.7115 -0.0773 0.1573  -0.0493 185 LEU A CB  
1333 C CG  . LEU A 179 ? 0.8700 0.6353 0.7194 -0.0721 0.1620  -0.0514 185 LEU A CG  
1334 C CD1 . LEU A 179 ? 0.8595 0.6355 0.7218 -0.0676 0.1624  -0.0550 185 LEU A CD1 
1335 C CD2 . LEU A 179 ? 0.8499 0.6134 0.6920 -0.0737 0.1732  -0.0491 185 LEU A CD2 
1336 N N   . PRO A 180 ? 0.8903 0.6572 0.7570 -0.0914 0.1579  -0.0412 186 PRO A N   
1337 C CA  . PRO A 180 ? 0.8769 0.6515 0.7594 -0.0965 0.1559  -0.0403 186 PRO A CA  
1338 C C   . PRO A 180 ? 0.9349 0.7263 0.8383 -0.0956 0.1543  -0.0435 186 PRO A C   
1339 O O   . PRO A 180 ? 0.9300 0.7269 0.8449 -0.0979 0.1485  -0.0441 186 PRO A O   
1340 C CB  . PRO A 180 ? 0.8886 0.6621 0.7703 -0.1015 0.1653  -0.0366 186 PRO A CB  
1341 C CG  . PRO A 180 ? 0.9405 0.7002 0.7999 -0.0994 0.1693  -0.0346 186 PRO A CG  
1342 C CD  . PRO A 180 ? 0.8825 0.6416 0.7357 -0.0926 0.1668  -0.0383 186 PRO A CD  
1343 N N   . SER A 181 ? 0.9339 0.7333 0.8422 -0.0919 0.1592  -0.0455 187 SER A N   
1344 C CA  . SER A 181 ? 0.8779 0.6928 0.8052 -0.0902 0.1571  -0.0484 187 SER A CA  
1345 C C   . SER A 181 ? 0.8982 0.7121 0.8256 -0.0869 0.1467  -0.0505 187 SER A C   
1346 O O   . SER A 181 ? 0.8935 0.7179 0.8357 -0.0874 0.1418  -0.0519 187 SER A O   
1347 C CB  . SER A 181 ? 0.8846 0.7073 0.8159 -0.0860 0.1645  -0.0501 187 SER A CB  
1348 O OG  . SER A 181 ? 0.8969 0.7085 0.8110 -0.0810 0.1650  -0.0510 187 SER A OG  
1349 N N   . VAL A 182 ? 0.9053 0.7069 0.8164 -0.0836 0.1431  -0.0506 188 VAL A N   
1350 C CA  . VAL A 182 ? 0.8710 0.6709 0.7815 -0.0810 0.1332  -0.0519 188 VAL A CA  
1351 C C   . VAL A 182 ? 0.8533 0.6517 0.7662 -0.0847 0.1270  -0.0506 188 VAL A C   
1352 O O   . VAL A 182 ? 0.8039 0.6102 0.7276 -0.0843 0.1208  -0.0518 188 VAL A O   
1353 C CB  . VAL A 182 ? 0.8613 0.6481 0.7537 -0.0771 0.1309  -0.0523 188 VAL A CB  
1354 C CG1 . VAL A 182 ? 0.8374 0.6210 0.7279 -0.0756 0.1205  -0.0527 188 VAL A CG1 
1355 C CG2 . VAL A 182 ? 0.8695 0.6589 0.7619 -0.0724 0.1354  -0.0547 188 VAL A CG2 
1356 N N   . ARG A 183 ? 0.8848 0.6732 0.7875 -0.0882 0.1286  -0.0480 189 ARG A N   
1357 C CA  . ARG A 183 ? 0.8643 0.6494 0.7676 -0.0910 0.1224  -0.0469 189 ARG A CA  
1358 C C   . ARG A 183 ? 0.8576 0.6551 0.7792 -0.0943 0.1219  -0.0479 189 ARG A C   
1359 O O   . ARG A 183 ? 0.8450 0.6456 0.7724 -0.0943 0.1148  -0.0489 189 ARG A O   
1360 C CB  . ARG A 183 ? 0.8836 0.6550 0.7724 -0.0939 0.1248  -0.0436 189 ARG A CB  
1361 C CG  . ARG A 183 ? 0.9154 0.6742 0.7851 -0.0906 0.1246  -0.0427 189 ARG A CG  
1362 C CD  . ARG A 183 ? 0.9470 0.6918 0.8016 -0.0931 0.1256  -0.0392 189 ARG A CD  
1363 N NE  . ARG A 183 ? 0.9418 0.6813 0.7940 -0.0934 0.1171  -0.0384 189 ARG A NE  
1364 C CZ  . ARG A 183 ? 0.9737 0.7015 0.8147 -0.0953 0.1162  -0.0353 189 ARG A CZ  
1365 N NH1 . ARG A 183 ? 1.0153 0.7349 0.8459 -0.0975 0.1231  -0.0323 189 ARG A NH1 
1366 N NH2 . ARG A 183 ? 0.9886 0.7127 0.8287 -0.0948 0.1083  -0.0349 189 ARG A NH2 
1367 N N   . GLN A 184 ? 0.8676 0.6733 0.7990 -0.0968 0.1293  -0.0479 190 GLN A N   
1368 C CA  . GLN A 184 ? 0.8770 0.6949 0.8263 -0.1002 0.1287  -0.0491 190 GLN A CA  
1369 C C   . GLN A 184 ? 0.8719 0.7021 0.8335 -0.0967 0.1232  -0.0521 190 GLN A C   
1370 O O   . GLN A 184 ? 0.8793 0.7153 0.8501 -0.0981 0.1176  -0.0534 190 GLN A O   
1371 C CB  . GLN A 184 ? 0.8208 0.6455 0.7783 -0.1037 0.1381  -0.0481 190 GLN A CB  
1372 C CG  . GLN A 184 ? 0.8977 0.7199 0.8589 -0.1105 0.1400  -0.0461 190 GLN A CG  
1373 C CD  . GLN A 184 ? 0.9261 0.7533 0.8983 -0.1126 0.1322  -0.0482 190 GLN A CD  
1374 O OE1 . GLN A 184 ? 0.8869 0.7281 0.8756 -0.1134 0.1312  -0.0505 190 GLN A OE1 
1375 N NE2 . GLN A 184 ? 0.9661 0.7819 0.9287 -0.1132 0.1264  -0.0474 190 GLN A NE2 
1376 N N   . GLU A 185 ? 0.8065 0.6407 0.7681 -0.0919 0.1246  -0.0533 191 GLU A N   
1377 C CA  . GLU A 185 ? 0.8414 0.6873 0.8149 -0.0885 0.1197  -0.0556 191 GLU A CA  
1378 C C   . GLU A 185 ? 0.8738 0.7158 0.8428 -0.0866 0.1104  -0.0560 191 GLU A C   
1379 O O   . GLU A 185 ? 0.8341 0.6858 0.8137 -0.0855 0.1052  -0.0574 191 GLU A O   
1380 C CB  . GLU A 185 ? 0.8102 0.6596 0.7840 -0.0836 0.1232  -0.0567 191 GLU A CB  
1381 C CG  . GLU A 185 ? 0.8706 0.7343 0.8596 -0.0806 0.1201  -0.0587 191 GLU A CG  
1382 C CD  . GLU A 185 ? 0.9082 0.7857 0.9145 -0.0841 0.1221  -0.0594 191 GLU A CD  
1383 N N   . VAL A 186 ? 0.8297 0.6582 0.7831 -0.0861 0.1083  -0.0544 192 VAL A N   
1384 C CA  . VAL A 186 ? 0.7939 0.6190 0.7434 -0.0848 0.0999  -0.0543 192 VAL A CA  
1385 C C   . VAL A 186 ? 0.8360 0.6650 0.7931 -0.0881 0.0966  -0.0548 192 VAL A C   
1386 O O   . VAL A 186 ? 0.8581 0.6924 0.8203 -0.0866 0.0901  -0.0559 192 VAL A O   
1387 C CB  . VAL A 186 ? 0.7929 0.6029 0.7246 -0.0839 0.0985  -0.0525 192 VAL A CB  
1388 C CG1 . VAL A 186 ? 0.8051 0.6115 0.7337 -0.0839 0.0910  -0.0519 192 VAL A CG1 
1389 C CG2 . VAL A 186 ? 0.7781 0.5854 0.7036 -0.0797 0.0981  -0.0529 192 VAL A CG2 
1390 N N   . LYS A 187 ? 0.8274 0.6536 0.7854 -0.0928 0.1010  -0.0541 193 LYS A N   
1391 C CA  . LYS A 187 ? 0.8277 0.6567 0.7931 -0.0961 0.0977  -0.0550 193 LYS A CA  
1392 C C   . LYS A 187 ? 0.8049 0.6497 0.7874 -0.0962 0.0963  -0.0577 193 LYS A C   
1393 O O   . LYS A 187 ? 0.7749 0.6247 0.7628 -0.0955 0.0900  -0.0594 193 LYS A O   
1394 C CB  . LYS A 187 ? 0.8552 0.6765 0.8176 -0.1015 0.1026  -0.0533 193 LYS A CB  
1395 C CG  . LYS A 187 ? 0.8589 0.6763 0.8225 -0.1044 0.0978  -0.0539 193 LYS A CG  
1396 C CD  . LYS A 187 ? 0.8525 0.6691 0.8223 -0.1107 0.1024  -0.0533 193 LYS A CD  
1397 C CE  . LYS A 187 ? 0.9435 0.7457 0.9002 -0.1133 0.1076  -0.0495 193 LYS A CE  
1398 N NZ  . LYS A 187 ? 1.0269 0.8259 0.9887 -0.1199 0.1104  -0.0485 193 LYS A NZ  
1399 N N   . GLU A 188 ? 0.8531 0.7064 0.8443 -0.0967 0.1021  -0.0580 194 GLU A N   
1400 C CA  . GLU A 188 ? 0.8549 0.7241 0.8627 -0.0963 0.1008  -0.0604 194 GLU A CA  
1401 C C   . GLU A 188 ? 0.7865 0.6611 0.7960 -0.0915 0.0934  -0.0616 194 GLU A C   
1402 O O   . GLU A 188 ? 0.7704 0.6532 0.7887 -0.0918 0.0884  -0.0636 194 GLU A O   
1403 C CB  . GLU A 188 ? 0.9455 0.8225 0.9602 -0.0953 0.1078  -0.0603 194 GLU A CB  
1404 C CG  . GLU A 188 ? 1.0235 0.9032 1.0445 -0.1004 0.1157  -0.0594 194 GLU A CG  
1405 C CD  . GLU A 188 ? 1.1522 1.0414 1.1805 -0.0977 0.1223  -0.0596 194 GLU A CD  
1406 O OE1 . GLU A 188 ? 1.1940 1.0952 1.2331 -0.0943 0.1196  -0.0614 194 GLU A OE1 
1407 O OE2 . GLU A 188 ? 1.2063 1.0907 1.2289 -0.0987 0.1301  -0.0578 194 GLU A OE2 
1408 N N   . ILE A 189 ? 0.7931 0.6629 0.7938 -0.0871 0.0928  -0.0605 195 ILE A N   
1409 C CA  . ILE A 189 ? 0.7737 0.6488 0.7762 -0.0826 0.0866  -0.0610 195 ILE A CA  
1410 C C   . ILE A 189 ? 0.7598 0.6322 0.7587 -0.0827 0.0796  -0.0612 195 ILE A C   
1411 O O   . ILE A 189 ? 0.7573 0.6387 0.7634 -0.0809 0.0745  -0.0624 195 ILE A O   
1412 C CB  . ILE A 189 ? 0.7799 0.6485 0.7731 -0.0786 0.0877  -0.0596 195 ILE A CB  
1413 C CG1 . ILE A 189 ? 0.7819 0.6550 0.7802 -0.0775 0.0944  -0.0600 195 ILE A CG1 
1414 C CG2 . ILE A 189 ? 0.7343 0.6060 0.7277 -0.0745 0.0810  -0.0593 195 ILE A CG2 
1415 C CD1 . ILE A 189 ? 0.8088 0.6730 0.7960 -0.0740 0.0964  -0.0592 195 ILE A CD1 
1416 N N   . LEU A 190 ? 0.7295 0.5895 0.7169 -0.0843 0.0793  -0.0599 196 LEU A N   
1417 C CA  . LEU A 190 ? 0.6821 0.5394 0.6660 -0.0839 0.0730  -0.0602 196 LEU A CA  
1418 C C   . LEU A 190 ? 0.7276 0.5927 0.7218 -0.0863 0.0709  -0.0627 196 LEU A C   
1419 O O   . LEU A 190 ? 0.7280 0.5983 0.7248 -0.0843 0.0651  -0.0640 196 LEU A O   
1420 C CB  . LEU A 190 ? 0.7094 0.5519 0.6798 -0.0853 0.0735  -0.0584 196 LEU A CB  
1421 C CG  . LEU A 190 ? 0.7345 0.5687 0.6930 -0.0823 0.0726  -0.0562 196 LEU A CG  
1422 C CD1 . LEU A 190 ? 0.7446 0.5646 0.6901 -0.0838 0.0729  -0.0544 196 LEU A CD1 
1423 C CD2 . LEU A 190 ? 0.6931 0.5326 0.6528 -0.0783 0.0660  -0.0560 196 LEU A CD2 
1424 N N   . LEU A 191 ? 0.7306 0.5971 0.7311 -0.0906 0.0754  -0.0636 197 LEU A N   
1425 C CA  . LEU A 191 ? 0.6846 0.5578 0.6950 -0.0936 0.0730  -0.0664 197 LEU A CA  
1426 C C   . LEU A 191 ? 0.7217 0.6105 0.7446 -0.0913 0.0702  -0.0684 197 LEU A C   
1427 O O   . LEU A 191 ? 0.6939 0.5884 0.7212 -0.0908 0.0648  -0.0707 197 LEU A O   
1428 C CB  . LEU A 191 ? 0.6917 0.5620 0.7059 -0.0994 0.0786  -0.0663 197 LEU A CB  
1429 C CG  . LEU A 191 ? 0.7221 0.5762 0.7237 -0.1019 0.0801  -0.0643 197 LEU A CG  
1430 C CD1 . LEU A 191 ? 0.6541 0.5045 0.6571 -0.1071 0.0876  -0.0626 197 LEU A CD1 
1431 C CD2 . LEU A 191 ? 0.6156 0.4651 0.6156 -0.1028 0.0742  -0.0662 197 LEU A CD2 
1432 N N   . ARG A 192 ? 0.7000 0.5955 0.7280 -0.0896 0.0737  -0.0676 198 ARG A N   
1433 C CA  . ARG A 192 ? 0.6793 0.5893 0.7185 -0.0868 0.0708  -0.0690 198 ARG A CA  
1434 C C   . ARG A 192 ? 0.6933 0.6053 0.7285 -0.0819 0.0645  -0.0686 198 ARG A C   
1435 O O   . ARG A 192 ? 0.6688 0.5919 0.7120 -0.0801 0.0603  -0.0701 198 ARG A O   
1436 C CB  . ARG A 192 ? 0.6651 0.5811 0.7103 -0.0854 0.0761  -0.0681 198 ARG A CB  
1437 C CG  . ARG A 192 ? 0.7596 0.6793 0.8136 -0.0902 0.0817  -0.0689 198 ARG A CG  
1438 C CD  . ARG A 192 ? 0.8663 0.7814 0.9165 -0.0899 0.0895  -0.0669 198 ARG A CD  
1439 N NE  . ARG A 192 ? 0.9040 0.8296 0.9626 -0.0859 0.0913  -0.0670 198 ARG A NE  
1440 C CZ  . ARG A 192 ? 0.9584 0.8819 1.0145 -0.0841 0.0977  -0.0658 198 ARG A CZ  
1441 N NH1 . ARG A 192 ? 0.8540 0.7651 0.8984 -0.0858 0.1028  -0.0642 198 ARG A NH1 
1442 N NH2 . ARG A 192 ? 0.9895 0.9234 1.0548 -0.0802 0.0990  -0.0662 198 ARG A NH2 
1443 N N   . LYS A 193 ? 0.7091 0.6108 0.7321 -0.0799 0.0635  -0.0665 199 LYS A N   
1444 C CA  . LYS A 193 ? 0.6683 0.5721 0.6878 -0.0759 0.0576  -0.0657 199 LYS A CA  
1445 C C   . LYS A 193 ? 0.6790 0.5817 0.6963 -0.0765 0.0528  -0.0675 199 LYS A C   
1446 O O   . LYS A 193 ? 0.6853 0.5905 0.6998 -0.0732 0.0481  -0.0668 199 LYS A O   
1447 C CB  . LYS A 193 ? 0.6566 0.5509 0.6650 -0.0736 0.0579  -0.0627 199 LYS A CB  
1448 C CG  . LYS A 193 ? 0.6206 0.5173 0.6309 -0.0710 0.0604  -0.0612 199 LYS A CG  
1449 C CD  . LYS A 193 ? 0.6217 0.5081 0.6207 -0.0692 0.0601  -0.0587 199 LYS A CD  
1450 C CE  . LYS A 193 ? 0.5889 0.4755 0.5890 -0.0669 0.0633  -0.0578 199 LYS A CE  
1451 N NZ  . LYS A 193 ? 0.5769 0.4717 0.5825 -0.0631 0.0594  -0.0567 199 LYS A NZ  
1452 N N   . GLY A 194 ? 0.7013 0.6006 0.7201 -0.0807 0.0539  -0.0696 200 GLY A N   
1453 C CA  . GLY A 194 ? 0.6328 0.5303 0.6496 -0.0811 0.0494  -0.0719 200 GLY A CA  
1454 C C   . GLY A 194 ? 0.6780 0.5623 0.6826 -0.0807 0.0486  -0.0704 200 GLY A C   
1455 O O   . GLY A 194 ? 0.6983 0.5811 0.7003 -0.0797 0.0445  -0.0722 200 GLY A O   
1456 N N   . VAL A 195 ? 0.6485 0.5234 0.6453 -0.0811 0.0523  -0.0675 201 VAL A N   
1457 C CA  . VAL A 195 ? 0.6460 0.5082 0.6313 -0.0809 0.0515  -0.0660 201 VAL A CA  
1458 C C   . VAL A 195 ? 0.6846 0.5387 0.6690 -0.0853 0.0531  -0.0674 201 VAL A C   
1459 O O   . VAL A 195 ? 0.7140 0.5678 0.7030 -0.0894 0.0577  -0.0677 201 VAL A O   
1460 C CB  . VAL A 195 ? 0.6458 0.5003 0.6226 -0.0802 0.0545  -0.0625 201 VAL A CB  
1461 C CG1 . VAL A 195 ? 0.6435 0.4858 0.6084 -0.0794 0.0527  -0.0607 201 VAL A CG1 
1462 C CG2 . VAL A 195 ? 0.6080 0.4700 0.5869 -0.0765 0.0532  -0.0611 201 VAL A CG2 
1463 N N   . GLN A 196 ? 0.7166 0.5641 0.6953 -0.0844 0.0496  -0.0682 202 GLN A N   
1464 C CA  . GLN A 196 ? 0.7314 0.5692 0.7081 -0.0883 0.0505  -0.0694 202 GLN A CA  
1465 C C   . GLN A 196 ? 0.7577 0.5813 0.7228 -0.0891 0.0534  -0.0658 202 GLN A C   
1466 O O   . GLN A 196 ? 0.7893 0.6080 0.7459 -0.0855 0.0506  -0.0640 202 GLN A O   
1467 C CB  . GLN A 196 ? 0.7101 0.5477 0.6866 -0.0864 0.0449  -0.0725 202 GLN A CB  
1468 C CG  . GLN A 196 ? 0.7700 0.6223 0.7559 -0.0843 0.0414  -0.0757 202 GLN A CG  
1469 C CD  . GLN A 196 ? 0.9782 0.8303 0.9672 -0.0852 0.0376  -0.0803 202 GLN A CD  
1470 O OE1 . GLN A 196 ? 1.0113 0.8517 0.9956 -0.0873 0.0374  -0.0811 202 GLN A OE1 
1471 N NE2 . GLN A 196 ? 0.9152 0.7800 0.9119 -0.0836 0.0343  -0.0835 202 GLN A NE2 
1472 N N   . LEU A 197 ? 0.7848 0.6023 0.7496 -0.0938 0.0588  -0.0645 203 LEU A N   
1473 C CA  . LEU A 197 ? 0.7440 0.5481 0.6972 -0.0948 0.0621  -0.0609 203 LEU A CA  
1474 C C   . LEU A 197 ? 0.7777 0.5691 0.7257 -0.0974 0.0614  -0.0607 203 LEU A C   
1475 O O   . LEU A 197 ? 0.7909 0.5824 0.7458 -0.1016 0.0624  -0.0627 203 LEU A O   
1476 C CB  . LEU A 197 ? 0.7396 0.5443 0.6942 -0.0980 0.0692  -0.0590 203 LEU A CB  
1477 C CG  . LEU A 197 ? 0.7762 0.5925 0.7364 -0.0955 0.0704  -0.0593 203 LEU A CG  
1478 C CD1 . LEU A 197 ? 0.7634 0.5782 0.7229 -0.0980 0.0778  -0.0573 203 LEU A CD1 
1479 C CD2 . LEU A 197 ? 0.7883 0.6039 0.7412 -0.0902 0.0662  -0.0581 203 LEU A CD2 
1480 N N   . LEU A 198 ? 0.8044 0.5849 0.7407 -0.0950 0.0596  -0.0584 204 LEU A N   
1481 C CA  . LEU A 198 ? 0.8369 0.6032 0.7660 -0.0967 0.0590  -0.0573 204 LEU A CA  
1482 C C   . LEU A 198 ? 0.8863 0.6416 0.8044 -0.0982 0.0636  -0.0527 204 LEU A C   
1483 O O   . LEU A 198 ? 0.8461 0.5950 0.7537 -0.0947 0.0615  -0.0504 204 LEU A O   
1484 C CB  . LEU A 198 ? 0.8200 0.5831 0.7444 -0.0919 0.0526  -0.0583 204 LEU A CB  
1485 C CG  . LEU A 198 ? 0.8750 0.6404 0.8064 -0.0921 0.0489  -0.0626 204 LEU A CG  
1486 C CD1 . LEU A 198 ? 0.9261 0.6872 0.8511 -0.0866 0.0433  -0.0631 204 LEU A CD1 
1487 C CD2 . LEU A 198 ? 0.9250 0.6804 0.8572 -0.0981 0.0520  -0.0626 204 LEU A CD2 
1488 N N   . LEU A 199 ? 0.9139 0.6674 0.8344 -0.1035 0.0699  -0.0515 205 LEU A N   
1489 C CA  . LEU A 199 ? 0.8465 0.5904 0.7563 -0.1050 0.0752  -0.0471 205 LEU A CA  
1490 C C   . LEU A 199 ? 0.9110 0.6386 0.8114 -0.1072 0.0754  -0.0443 205 LEU A C   
1491 O O   . LEU A 199 ? 0.9256 0.6496 0.8305 -0.1095 0.0735  -0.0459 205 LEU A O   
1492 C CB  . LEU A 199 ? 0.8937 0.6442 0.8105 -0.1092 0.0826  -0.0467 205 LEU A CB  
1493 C CG  . LEU A 199 ? 0.8315 0.5975 0.7577 -0.1071 0.0831  -0.0491 205 LEU A CG  
1494 C CD1 . LEU A 199 ? 0.8366 0.6077 0.7685 -0.1110 0.0911  -0.0482 205 LEU A CD1 
1495 C CD2 . LEU A 199 ? 0.7965 0.5624 0.7143 -0.1016 0.0803  -0.0482 205 LEU A CD2 
1496 N N   . SER A 200 ? 0.9128 0.6300 0.7994 -0.1062 0.0774  -0.0402 206 SER A N   
1497 C CA  . SER A 200 ? 0.9350 0.6356 0.8106 -0.1080 0.0781  -0.0365 206 SER A CA  
1498 C C   . SER A 200 ? 0.9641 0.6582 0.8370 -0.1046 0.0708  -0.0376 206 SER A C   
1499 O O   . SER A 200 ? 0.9641 0.6469 0.8344 -0.1070 0.0705  -0.0364 206 SER A O   
1500 C CB  . SER A 200 ? 0.9711 0.6680 0.8515 -0.1150 0.0843  -0.0351 206 SER A CB  
1501 O OG  . SER A 200 ? 1.0212 0.7252 0.9047 -0.1177 0.0916  -0.0341 206 SER A OG  
1502 N N   . GLU A 201 ? 0.9710 0.6718 0.8444 -0.0989 0.0650  -0.0398 207 GLU A N   
1503 C CA  . GLU A 201 ? 0.9815 0.6778 0.8523 -0.0946 0.0582  -0.0408 207 GLU A CA  
1504 C C   . GLU A 201 ? 0.9241 0.6202 0.7861 -0.0890 0.0543  -0.0390 207 GLU A C   
1505 O O   . GLU A 201 ? 0.8683 0.5723 0.7305 -0.0880 0.0554  -0.0388 207 GLU A O   
1506 C CB  . GLU A 201 ? 0.9663 0.6738 0.8497 -0.0932 0.0543  -0.0461 207 GLU A CB  
1507 C CG  . GLU A 201 ? 1.0061 0.7182 0.9008 -0.0990 0.0579  -0.0486 207 GLU A CG  
1508 C CD  . GLU A 201 ? 1.0817 0.7907 0.9818 -0.0995 0.0540  -0.0523 207 GLU A CD  
1509 O OE1 . GLU A 201 ? 1.0818 0.7872 0.9779 -0.0944 0.0484  -0.0535 207 GLU A OE1 
1510 O OE2 . GLU A 201 ? 1.1185 0.8288 1.0270 -0.1049 0.0564  -0.0541 207 GLU A OE2 
1511 N N   . ARG A 202 ? 0.9757 0.6630 0.8306 -0.0854 0.0495  -0.0378 208 ARG A N   
1512 C CA  . ARG A 202 ? 1.0006 0.6871 0.8474 -0.0802 0.0451  -0.0358 208 ARG A CA  
1513 C C   . ARG A 202 ? 0.9424 0.6339 0.7937 -0.0749 0.0385  -0.0384 208 ARG A C   
1514 O O   . ARG A 202 ? 0.9734 0.6588 0.8259 -0.0743 0.0366  -0.0397 208 ARG A O   
1515 C CB  . ARG A 202 ? 1.0794 0.7499 0.9115 -0.0804 0.0457  -0.0310 208 ARG A CB  
1516 C CG  . ARG A 202 ? 1.1347 0.8035 0.9579 -0.0753 0.0407  -0.0287 208 ARG A CG  
1517 C CD  . ARG A 202 ? 1.2256 0.8796 1.0334 -0.0762 0.0423  -0.0238 208 ARG A CD  
1518 N NE  . ARG A 202 ? 1.3340 0.9887 1.1374 -0.0796 0.0480  -0.0224 208 ARG A NE  
1519 C CZ  . ARG A 202 ? 1.3114 0.9726 1.1127 -0.0779 0.0470  -0.0227 208 ARG A CZ  
1520 N NH1 . ARG A 202 ? 1.2456 0.9142 1.0497 -0.0735 0.0407  -0.0240 208 ARG A NH1 
1521 N NH2 . ARG A 202 ? 1.3063 0.9667 1.1027 -0.0807 0.0526  -0.0218 208 ARG A NH2 
1522 N N   . VAL A 203 ? 0.9181 0.6207 0.7723 -0.0710 0.0350  -0.0392 209 VAL A N   
1523 C CA  . VAL A 203 ? 0.9685 0.6776 0.8275 -0.0657 0.0294  -0.0414 209 VAL A CA  
1524 C C   . VAL A 203 ? 0.9942 0.6921 0.8438 -0.0618 0.0253  -0.0388 209 VAL A C   
1525 O O   . VAL A 203 ? 0.9168 0.6101 0.7577 -0.0605 0.0240  -0.0352 209 VAL A O   
1526 C CB  . VAL A 203 ? 0.8912 0.6154 0.7561 -0.0630 0.0271  -0.0423 209 VAL A CB  
1527 C CG1 . VAL A 203 ? 0.9128 0.6420 0.7798 -0.0569 0.0213  -0.0430 209 VAL A CG1 
1528 C CG2 . VAL A 203 ? 0.8649 0.6011 0.7409 -0.0655 0.0298  -0.0456 209 VAL A CG2 
1529 N N   . SER A 204 ? 0.9797 0.6734 0.8311 -0.0594 0.0228  -0.0408 210 SER A N   
1530 C CA  . SER A 204 ? 0.9918 0.6728 0.8346 -0.0558 0.0193  -0.0385 210 SER A CA  
1531 C C   . SER A 204 ? 1.0234 0.7114 0.8679 -0.0485 0.0133  -0.0391 210 SER A C   
1532 O O   . SER A 204 ? 1.0969 0.7764 0.9336 -0.0448 0.0100  -0.0361 210 SER A O   
1533 C CB  . SER A 204 ? 0.9473 0.6169 0.7902 -0.0576 0.0204  -0.0402 210 SER A CB  
1534 O OG  . SER A 204 ? 1.0039 0.6825 0.8570 -0.0562 0.0190  -0.0455 210 SER A OG  
1535 N N   . ASN A 205 ? 0.9657 0.6689 0.8201 -0.0461 0.0119  -0.0425 211 ASN A N   
1536 C CA  . ASN A 205 ? 0.9922 0.7035 0.8492 -0.0391 0.0068  -0.0429 211 ASN A CA  
1537 C C   . ASN A 205 ? 0.9888 0.7143 0.8495 -0.0382 0.0055  -0.0413 211 ASN A C   
1538 O O   . ASN A 205 ? 1.0127 0.7515 0.8806 -0.0342 0.0032  -0.0429 211 ASN A O   
1539 C CB  . ASN A 205 ? 0.9878 0.7049 0.8523 -0.0360 0.0056  -0.0480 211 ASN A CB  
1540 C CG  . ASN A 205 ? 0.9447 0.6761 0.8189 -0.0384 0.0079  -0.0514 211 ASN A CG  
1541 O OD1 . ASN A 205 ? 0.9161 0.6488 0.7918 -0.0441 0.0116  -0.0510 211 ASN A OD1 
1542 N ND2 . ASN A 205 ? 0.9621 0.7045 0.8428 -0.0338 0.0056  -0.0548 211 ASN A ND2 
1543 N N   . LEU A 206 ? 0.9720 0.6941 0.8270 -0.0415 0.0070  -0.0380 212 LEU A N   
1544 C CA  . LEU A 206 ? 0.9955 0.7297 0.8544 -0.0422 0.0065  -0.0369 212 LEU A CA  
1545 C C   . LEU A 206 ? 1.0238 0.7653 0.8837 -0.0370 0.0010  -0.0349 212 LEU A C   
1546 O O   . LEU A 206 ? 1.0189 0.7747 0.8866 -0.0358 -0.0002 -0.0353 212 LEU A O   
1547 C CB  . LEU A 206 ? 0.9351 0.6621 0.7867 -0.0471 0.0096  -0.0345 212 LEU A CB  
1548 C CG  . LEU A 206 ? 0.9327 0.6703 0.7881 -0.0487 0.0100  -0.0340 212 LEU A CG  
1549 C CD1 . LEU A 206 ? 0.9280 0.6781 0.7947 -0.0499 0.0123  -0.0373 212 LEU A CD1 
1550 C CD2 . LEU A 206 ? 1.0119 0.7403 0.8586 -0.0531 0.0134  -0.0321 212 LEU A CD2 
1551 N N   . GLU A 207 ? 1.0666 0.7988 0.9189 -0.0339 -0.0023 -0.0324 213 GLU A N   
1552 C CA  . GLU A 207 ? 1.0805 0.8203 0.9346 -0.0288 -0.0078 -0.0303 213 GLU A CA  
1553 C C   . GLU A 207 ? 1.0425 0.7960 0.9071 -0.0240 -0.0093 -0.0328 213 GLU A C   
1554 O O   . GLU A 207 ? 1.0857 0.8504 0.9550 -0.0206 -0.0129 -0.0312 213 GLU A O   
1555 C CB  . GLU A 207 ? 1.1753 0.9023 1.0199 -0.0256 -0.0112 -0.0274 213 GLU A CB  
1556 C CG  . GLU A 207 ? 1.2063 0.9155 1.0390 -0.0298 -0.0084 -0.0257 213 GLU A CG  
1557 C CD  . GLU A 207 ? 1.2911 0.9969 1.1159 -0.0327 -0.0091 -0.0224 213 GLU A CD  
1558 O OE1 . GLU A 207 ? 1.3410 1.0569 1.1704 -0.0351 -0.0086 -0.0228 213 GLU A OE1 
1559 O OE2 . GLU A 207 ? 1.3244 1.0168 1.1378 -0.0325 -0.0103 -0.0194 213 GLU A OE2 
1560 N N   . GLU A 208 ? 1.0214 0.7746 0.8896 -0.0238 -0.0067 -0.0368 214 GLU A N   
1561 C CA  . GLU A 208 ? 0.9538 0.7187 0.8303 -0.0189 -0.0079 -0.0398 214 GLU A CA  
1562 C C   . GLU A 208 ? 0.9697 0.7489 0.8551 -0.0211 -0.0054 -0.0420 214 GLU A C   
1563 O O   . GLU A 208 ? 1.0179 0.8079 0.9099 -0.0172 -0.0060 -0.0445 214 GLU A O   
1564 C CB  . GLU A 208 ? 0.9391 0.6938 0.8133 -0.0167 -0.0073 -0.0433 214 GLU A CB  
1565 N N   . LEU A 209 ? 1.0516 0.6345 0.8815 -0.0414 -0.0691 -0.1108 215 LEU A N   
1566 C CA  . LEU A 209 ? 0.9978 0.6281 0.8526 -0.0417 -0.0568 -0.1126 215 LEU A CA  
1567 C C   . LEU A 209 ? 0.9614 0.6108 0.8271 -0.0334 -0.0626 -0.1088 215 LEU A C   
1568 O O   . LEU A 209 ? 0.9568 0.5792 0.8022 -0.0305 -0.0698 -0.1021 215 LEU A O   
1569 C CB  . LEU A 209 ? 0.9377 0.5677 0.7786 -0.0513 -0.0389 -0.1085 215 LEU A CB  
1570 C CG  . LEU A 209 ? 0.9518 0.5641 0.7797 -0.0613 -0.0299 -0.1111 215 LEU A CG  
1571 C CD1 . LEU A 209 ? 0.9633 0.5716 0.7742 -0.0697 -0.0136 -0.1056 215 LEU A CD1 
1572 C CD2 . LEU A 209 ? 0.9464 0.5920 0.8031 -0.0623 -0.0260 -0.1205 215 LEU A CD2 
1573 N N   . PRO A 210 ? 0.9059 0.6017 0.8033 -0.0300 -0.0595 -0.1132 216 PRO A N   
1574 C CA  . PRO A 210 ? 0.8604 0.5789 0.7695 -0.0235 -0.0622 -0.1091 216 PRO A CA  
1575 C C   . PRO A 210 ? 0.8830 0.6065 0.7817 -0.0284 -0.0483 -0.1021 216 PRO A C   
1576 O O   . PRO A 210 ? 0.8378 0.5802 0.7430 -0.0350 -0.0339 -0.1038 216 PRO A O   
1577 C CB  . PRO A 210 ? 0.8480 0.6148 0.7942 -0.0200 -0.0621 -0.1167 216 PRO A CB  
1578 C CG  . PRO A 210 ? 0.8334 0.5986 0.7861 -0.0234 -0.0618 -0.1252 216 PRO A CG  
1579 C CD  . PRO A 210 ? 0.8072 0.5362 0.7315 -0.0318 -0.0545 -0.1223 216 PRO A CD  
1580 N N   . LEU A 211 ? 0.8597 0.5664 0.7430 -0.0250 -0.0527 -0.0946 217 LEU A N   
1581 C CA  . LEU A 211 ? 0.8150 0.5232 0.6872 -0.0290 -0.0406 -0.0880 217 LEU A CA  
1582 C C   . LEU A 211 ? 0.8003 0.5471 0.6960 -0.0237 -0.0396 -0.0861 217 LEU A C   
1583 O O   . LEU A 211 ? 0.8174 0.5734 0.7255 -0.0158 -0.0519 -0.0864 217 LEU A O   
1584 C CB  . LEU A 211 ? 0.8842 0.5467 0.7216 -0.0298 -0.0450 -0.0809 217 LEU A CB  
1585 C CG  . LEU A 211 ? 0.8961 0.5178 0.7072 -0.0360 -0.0455 -0.0816 217 LEU A CG  
1586 C CD1 . LEU A 211 ? 0.9129 0.4919 0.6894 -0.0371 -0.0492 -0.0739 217 LEU A CD1 
1587 C CD2 . LEU A 211 ? 0.8737 0.5053 0.6856 -0.0456 -0.0289 -0.0845 217 LEU A CD2 
1588 N N   . ASN A 212 ? 0.7669 0.5366 0.6692 -0.0282 -0.0251 -0.0843 218 ASN A N   
1589 C CA  . ASN A 212 ? 0.7543 0.5577 0.6755 -0.0243 -0.0226 -0.0811 218 ASN A CA  
1590 C C   . ASN A 212 ? 0.7232 0.5658 0.6773 -0.0187 -0.0293 -0.0860 218 ASN A C   
1591 O O   . ASN A 212 ? 0.7270 0.5884 0.6940 -0.0128 -0.0349 -0.0830 218 ASN A O   
1592 C CB  . ASN A 212 ? 0.7764 0.5573 0.6802 -0.0198 -0.0294 -0.0736 218 ASN A CB  
1593 C CG  . ASN A 212 ? 0.7957 0.5392 0.6671 -0.0255 -0.0226 -0.0689 218 ASN A CG  
1594 O OD1 . ASN A 212 ? 0.8029 0.5496 0.6697 -0.0329 -0.0083 -0.0693 218 ASN A OD1 
1595 N ND2 . ASN A 212 ? 0.7984 0.5059 0.6464 -0.0225 -0.0328 -0.0647 218 ASN A ND2 
1596 N N   . GLU A 213 ? 0.7233 0.5796 0.6914 -0.0208 -0.0285 -0.0936 219 GLU A N   
1597 C CA  . GLU A 213 ? 0.7127 0.6041 0.7106 -0.0157 -0.0356 -0.0992 219 GLU A CA  
1598 C C   . GLU A 213 ? 0.6430 0.5609 0.6590 -0.0209 -0.0269 -0.1069 219 GLU A C   
1599 O O   . GLU A 213 ? 0.7246 0.6220 0.7299 -0.0253 -0.0251 -0.1111 219 GLU A O   
1600 C CB  . GLU A 213 ? 0.7578 0.6272 0.7514 -0.0091 -0.0526 -0.1017 219 GLU A CB  
1601 C CG  . GLU A 213 ? 0.7810 0.6694 0.7966 -0.0067 -0.0593 -0.1112 219 GLU A CG  
1602 C CD  . GLU A 213 ? 0.8984 0.7515 0.9013 -0.0024 -0.0741 -0.1139 219 GLU A CD  
1603 O OE1 . GLU A 213 ? 0.9268 0.7427 0.9045 -0.0007 -0.0802 -0.1076 219 GLU A OE1 
1604 O OE2 . GLU A 213 ? 0.8291 0.6914 0.8472 -0.0008 -0.0797 -0.1224 219 GLU A OE2 
1605 N N   . TYR A 214 ? 0.5984 0.5610 0.6409 -0.0209 -0.0214 -0.1084 220 TYR A N   
1606 C CA  . TYR A 214 ? 0.5966 0.5883 0.6584 -0.0256 -0.0135 -0.1158 220 TYR A CA  
1607 C C   . TYR A 214 ? 0.6229 0.6126 0.6936 -0.0233 -0.0230 -0.1248 220 TYR A C   
1608 O O   . TYR A 214 ? 0.6382 0.6305 0.7173 -0.0164 -0.0357 -0.1266 220 TYR A O   
1609 C CB  . TYR A 214 ? 0.5604 0.6012 0.6499 -0.0251 -0.0084 -0.1154 220 TYR A CB  
1610 C CG  . TYR A 214 ? 0.5461 0.6209 0.6590 -0.0286 -0.0034 -0.1241 220 TYR A CG  
1611 C CD1 . TYR A 214 ? 0.5386 0.6243 0.6532 -0.0363 0.0106  -0.1257 220 TYR A CD1 
1612 C CD2 . TYR A 214 ? 0.5608 0.6571 0.6943 -0.0245 -0.0124 -0.1311 220 TYR A CD2 
1613 C CE1 . TYR A 214 ? 0.5043 0.6207 0.6398 -0.0398 0.0151  -0.1336 220 TYR A CE1 
1614 C CE2 . TYR A 214 ? 0.4862 0.6135 0.6407 -0.0281 -0.0076 -0.1395 220 TYR A CE2 
1615 C CZ  . TYR A 214 ? 0.4760 0.6129 0.6310 -0.0356 0.0059  -0.1405 220 TYR A CZ  
1616 O OH  . TYR A 214 ? 0.5279 0.6952 0.7032 -0.0394 0.0107  -0.1489 220 TYR A OH  
1617 N N   . ARG A 215 ? 0.5733 0.5588 0.6427 -0.0292 -0.0167 -0.1309 221 ARG A N   
1618 C CA  . ARG A 215 ? 0.5966 0.5863 0.6784 -0.0281 -0.0232 -0.1407 221 ARG A CA  
1619 C C   . ARG A 215 ? 0.6200 0.6402 0.7188 -0.0348 -0.0113 -0.1470 221 ARG A C   
1620 O O   . ARG A 215 ? 0.6102 0.6326 0.7024 -0.0414 0.0018  -0.1439 221 ARG A O   
1621 C CB  . ARG A 215 ? 0.6494 0.5917 0.7075 -0.0286 -0.0302 -0.1423 221 ARG A CB  
1622 C CG  . ARG A 215 ? 0.6894 0.5984 0.7296 -0.0221 -0.0433 -0.1367 221 ARG A CG  
1623 C CD  . ARG A 215 ? 0.7273 0.6534 0.7878 -0.0137 -0.0570 -0.1414 221 ARG A CD  
1624 N NE  . ARG A 215 ? 0.8213 0.7135 0.8650 -0.0074 -0.0709 -0.1372 221 ARG A NE  
1625 C CZ  . ARG A 215 ? 0.8816 0.7364 0.9097 -0.0061 -0.0803 -0.1395 221 ARG A CZ  
1626 N NH1 . ARG A 215 ? 0.8344 0.6790 0.8606 -0.0108 -0.0775 -0.1458 221 ARG A NH1 
1627 N NH2 . ARG A 215 ? 0.9107 0.7371 0.9246 -0.0002 -0.0931 -0.1351 221 ARG A NH2 
1628 N N   . GLU A 216 ? 0.5814 0.6258 0.7026 -0.0331 -0.0157 -0.1564 222 GLU A N   
1629 C CA  . GLU A 216 ? 0.5649 0.6381 0.7024 -0.0395 -0.0050 -0.1631 222 GLU A CA  
1630 C C   . GLU A 216 ? 0.5682 0.6108 0.6869 -0.0465 0.0017  -0.1650 222 GLU A C   
1631 O O   . GLU A 216 ? 0.5070 0.5633 0.6283 -0.0538 0.0148  -0.1658 222 GLU A O   
1632 C CB  . GLU A 216 ? 0.4788 0.5826 0.6433 -0.0362 -0.0117 -0.1733 222 GLU A CB  
1633 N N   . TYR A 217 ? 0.5742 0.5745 0.6730 -0.0447 -0.0072 -0.1652 223 TYR A N   
1634 C CA  . TYR A 217 ? 0.5698 0.5376 0.6491 -0.0514 -0.0023 -0.1668 223 TYR A CA  
1635 C C   . TYR A 217 ? 0.6358 0.5525 0.6842 -0.0498 -0.0101 -0.1604 223 TYR A C   
1636 O O   . TYR A 217 ? 0.6463 0.5462 0.6927 -0.0429 -0.0244 -0.1616 223 TYR A O   
1637 C CB  . TYR A 217 ? 0.5651 0.5389 0.6585 -0.0525 -0.0056 -0.1782 223 TYR A CB  
1638 C CG  . TYR A 217 ? 0.6181 0.5606 0.6921 -0.0603 0.0005  -0.1793 223 TYR A CG  
1639 C CD1 . TYR A 217 ? 0.5811 0.5400 0.6587 -0.0689 0.0155  -0.1809 223 TYR A CD1 
1640 C CD2 . TYR A 217 ? 0.6445 0.5399 0.6952 -0.0594 -0.0086 -0.1781 223 TYR A CD2 
1641 C CE1 . TYR A 217 ? 0.6458 0.5761 0.7052 -0.0766 0.0215  -0.1816 223 TYR A CE1 
1642 C CE2 . TYR A 217 ? 0.6660 0.5322 0.6980 -0.0672 -0.0030 -0.1784 223 TYR A CE2 
1643 C CZ  . TYR A 217 ? 0.6958 0.5798 0.7324 -0.0759 0.0123  -0.1803 223 TYR A CZ  
1644 O OH  . TYR A 217 ? 0.8484 0.7036 0.8664 -0.0841 0.0182  -0.1807 223 TYR A OH  
1645 N N   . ILE A 218 ? 0.6370 0.5289 0.6615 -0.0564 -0.0007 -0.1541 224 ILE A N   
1646 C CA  . ILE A 218 ? 0.6208 0.4618 0.6128 -0.0569 -0.0063 -0.1482 224 ILE A CA  
1647 C C   . ILE A 218 ? 0.6737 0.4932 0.6481 -0.0670 0.0046  -0.1486 224 ILE A C   
1648 O O   . ILE A 218 ? 0.6418 0.4812 0.6206 -0.0735 0.0192  -0.1481 224 ILE A O   
1649 C CB  . ILE A 218 ? 0.6653 0.4957 0.6418 -0.0543 -0.0062 -0.1379 224 ILE A CB  
1650 C CG1 . ILE A 218 ? 0.6484 0.4927 0.6383 -0.0443 -0.0187 -0.1368 224 ILE A CG1 
1651 C CG2 . ILE A 218 ? 0.7442 0.5221 0.6843 -0.0574 -0.0085 -0.1315 224 ILE A CG2 
1652 C CD1 . ILE A 218 ? 0.6115 0.4567 0.5928 -0.0423 -0.0159 -0.1274 224 ILE A CD1 
1653 N N   . LYS A 219 ? 0.7138 0.4930 0.6686 -0.0686 -0.0024 -0.1496 225 LYS A N   
1654 C CA  . LYS A 219 ? 0.8141 0.5689 0.7497 -0.0788 0.0071  -0.1495 225 LYS A CA  
1655 C C   . LYS A 219 ? 0.8704 0.5784 0.7699 -0.0812 0.0053  -0.1404 225 LYS A C   
1656 O O   . LYS A 219 ? 0.8801 0.5556 0.7653 -0.0768 -0.0086 -0.1387 225 LYS A O   
1657 C CB  . LYS A 219 ? 0.8631 0.6085 0.8044 -0.0807 0.0021  -0.1582 225 LYS A CB  
1658 C CG  . LYS A 219 ? 0.8914 0.6225 0.8190 -0.0922 0.0147  -0.1590 225 LYS A CG  
1659 C CD  . LYS A 219 ? 1.0234 0.7469 0.9582 -0.0944 0.0102  -0.1681 225 LYS A CD  
1660 C CE  . LYS A 219 ? 1.1341 0.8057 1.0430 -0.0937 -0.0026 -0.1655 225 LYS A CE  
1661 N NZ  . LYS A 219 ? 1.1338 0.7898 1.0420 -0.0993 -0.0034 -0.1724 225 LYS A NZ  
1662 N N   . VAL A 220 ? 0.8964 0.6016 0.7818 -0.0884 0.0192  -0.1351 226 VAL A N   
1663 C CA  . VAL A 220 ? 0.8708 0.5331 0.7207 -0.0927 0.0204  -0.1269 226 VAL A CA  
1664 C C   . VAL A 220 ? 0.9370 0.5713 0.7690 -0.1026 0.0258  -0.1288 226 VAL A C   
1665 O O   . VAL A 220 ? 0.8998 0.5547 0.7443 -0.1090 0.0371  -0.1341 226 VAL A O   
1666 C CB  . VAL A 220 ? 0.8423 0.5179 0.6874 -0.0951 0.0329  -0.1206 226 VAL A CB  
1667 C CG1 . VAL A 220 ? 0.8897 0.5218 0.6978 -0.1001 0.0350  -0.1127 226 VAL A CG1 
1668 C CG2 . VAL A 220 ? 0.7982 0.5011 0.6618 -0.0853 0.0268  -0.1187 226 VAL A CG2 
1669 N N   . GLN A 221 ? 0.9883 0.5754 0.7910 -0.1041 0.0172  -0.1246 227 GLN A N   
1670 C CA  . GLN A 221 ? 1.0355 0.5903 0.8180 -0.1135 0.0202  -0.1255 227 GLN A CA  
1671 C C   . GLN A 221 ? 1.0559 0.5732 0.8016 -0.1209 0.0260  -0.1168 227 GLN A C   
1672 O O   . GLN A 221 ? 1.0829 0.5840 0.8134 -0.1165 0.0200  -0.1100 227 GLN A O   
1673 C CB  . GLN A 221 ? 1.0416 0.5708 0.8220 -0.1094 0.0033  -0.1290 227 GLN A CB  
1674 C CG  . GLN A 221 ? 1.0438 0.5999 0.8539 -0.1077 0.0015  -0.1394 227 GLN A CG  
1675 C CD  . GLN A 221 ? 1.1538 0.6834 0.9620 -0.1026 -0.0162 -0.1427 227 GLN A CD  
1676 O OE1 . GLN A 221 ? 1.1631 0.6649 0.9559 -0.0969 -0.0294 -0.1376 227 GLN A OE1 
1677 N NE2 . GLN A 221 ? 1.1731 0.7102 0.9968 -0.1045 -0.0170 -0.1515 227 GLN A NE2 
1678 N N   . THR A 222 ? 1.0712 0.5750 0.8025 -0.1323 0.0378  -0.1171 228 THR A N   
1679 C CA  . THR A 222 ? 1.1496 0.6171 0.8449 -0.1410 0.0443  -0.1096 228 THR A CA  
1680 C C   . THR A 222 ? 1.2456 0.6699 0.9169 -0.1482 0.0390  -0.1093 228 THR A C   
1681 O O   . THR A 222 ? 1.2381 0.6661 0.9226 -0.1493 0.0359  -0.1158 228 THR A O   
1682 C CB  . THR A 222 ? 1.1794 0.6672 0.8751 -0.1499 0.0652  -0.1093 228 THR A CB  
1683 O OG1 . THR A 222 ? 1.1767 0.6678 0.8769 -0.1590 0.0740  -0.1149 228 THR A OG1 
1684 C CG2 . THR A 222 ? 1.0942 0.6309 0.8199 -0.1433 0.0712  -0.1112 228 THR A CG2 
1685 N N   . ASP A 223 ? 1.2192 0.6024 0.8544 -0.1535 0.0384  -0.1014 229 ASP A N   
1686 C CA  . ASP A 223 ? 1.2993 0.6369 0.9064 -0.1614 0.0335  -0.0992 229 ASP A CA  
1687 C C   . ASP A 223 ? 1.2870 0.6291 0.8957 -0.1731 0.0472  -0.1038 229 ASP A C   
1688 O O   . ASP A 223 ? 1.2954 0.6071 0.8901 -0.1787 0.0418  -0.1043 229 ASP A O   
1689 C CB  . ASP A 223 ? 1.3569 0.6541 0.9246 -0.1662 0.0331  -0.0896 229 ASP A CB  
1690 C CG  . ASP A 223 ? 1.3914 0.7035 0.9518 -0.1724 0.0517  -0.0866 229 ASP A CG  
1691 O OD1 . ASP A 223 ? 1.3790 0.7319 0.9647 -0.1734 0.0650  -0.0917 229 ASP A OD1 
1692 O OD2 . ASP A 223 ? 1.4735 0.7566 1.0031 -0.1763 0.0529  -0.0793 229 ASP A OD2 
1693 N N   . LYS A 224 ? 1.2612 0.6401 0.8867 -0.1770 0.0643  -0.1069 230 LYS A N   
1694 C CA  . LYS A 224 ? 1.2138 0.6028 0.8450 -0.1875 0.0778  -0.1120 230 LYS A CA  
1695 C C   . LYS A 224 ? 1.2469 0.6701 0.9144 -0.1826 0.0749  -0.1216 230 LYS A C   
1696 O O   . LYS A 224 ? 1.2770 0.7145 0.9543 -0.1904 0.0859  -0.1269 230 LYS A O   
1697 C CB  . LYS A 224 ? 1.2235 0.6347 0.8544 -0.1946 0.0980  -0.1108 230 LYS A CB  
1698 N N   . GLY A 225 ? 1.2426 0.6797 0.9303 -0.1701 0.0605  -0.1242 231 GLY A N   
1699 C CA  . GLY A 225 ? 1.1707 0.6396 0.8924 -0.1650 0.0567  -0.1337 231 GLY A CA  
1700 C C   . GLY A 225 ? 1.0942 0.6176 0.8486 -0.1618 0.0672  -0.1384 231 GLY A C   
1701 O O   . GLY A 225 ? 1.0575 0.6100 0.8402 -0.1592 0.0662  -0.1468 231 GLY A O   
1702 N N   . THR A 226 ? 1.1091 0.6472 0.8604 -0.1621 0.0772  -0.1335 232 THR A N   
1703 C CA  . THR A 226 ? 1.0098 0.5990 0.7915 -0.1588 0.0864  -0.1370 232 THR A CA  
1704 C C   . THR A 226 ? 1.0350 0.6456 0.8384 -0.1454 0.0731  -0.1383 232 THR A C   
1705 O O   . THR A 226 ? 1.0239 0.6154 0.8140 -0.1391 0.0632  -0.1323 232 THR A O   
1706 C CB  . THR A 226 ? 1.0029 0.5987 0.7739 -0.1632 0.1007  -0.1311 232 THR A CB  
1707 O OG1 . THR A 226 ? 1.0624 0.6349 0.8104 -0.1760 0.1127  -0.1296 232 THR A OG1 
1708 C CG2 . THR A 226 ? 0.9765 0.6248 0.7793 -0.1608 0.1108  -0.1349 232 THR A CG2 
1709 N N   . GLU A 227 ? 1.0011 0.6515 0.8376 -0.1415 0.0730  -0.1461 233 GLU A N   
1710 C CA  . GLU A 227 ? 0.9416 0.6169 0.8014 -0.1295 0.0615  -0.1482 233 GLU A CA  
1711 C C   . GLU A 227 ? 0.8836 0.6066 0.7674 -0.1275 0.0716  -0.1486 233 GLU A C   
1712 O O   . GLU A 227 ? 0.9103 0.6611 0.8094 -0.1333 0.0839  -0.1532 233 GLU A O   
1713 C CB  . GLU A 227 ? 1.0157 0.6978 0.8946 -0.1258 0.0511  -0.1573 233 GLU A CB  
1714 C CG  . GLU A 227 ? 1.0682 0.7023 0.9249 -0.1249 0.0370  -0.1561 233 GLU A CG  
1715 C CD  . GLU A 227 ? 1.1836 0.8172 1.0540 -0.1254 0.0308  -0.1655 233 GLU A CD  
1716 O OE1 . GLU A 227 ? 1.1569 0.8238 1.0572 -0.1185 0.0257  -0.1730 233 GLU A OE1 
1717 O OE2 . GLU A 227 ? 1.2385 0.8383 1.0897 -0.1328 0.0310  -0.1655 233 GLU A OE2 
1718 N N   . VAL A 228 ? 0.8855 0.6164 0.7715 -0.1196 0.0663  -0.1435 234 VAL A N   
1719 C CA  . VAL A 228 ? 0.7914 0.5637 0.6977 -0.1169 0.0742  -0.1423 234 VAL A CA  
1720 C C   . VAL A 228 ? 0.7519 0.5482 0.6813 -0.1057 0.0614  -0.1445 234 VAL A C   
1721 O O   . VAL A 228 ? 0.7426 0.5190 0.6618 -0.0987 0.0491  -0.1403 234 VAL A O   
1722 C CB  . VAL A 228 ? 0.7939 0.5532 0.6801 -0.1187 0.0813  -0.1333 234 VAL A CB  
1723 C CG1 . VAL A 228 ? 0.7141 0.5168 0.6221 -0.1174 0.0913  -0.1325 234 VAL A CG1 
1724 C CG2 . VAL A 228 ? 0.8124 0.5382 0.6699 -0.1298 0.0915  -0.1309 234 VAL A CG2 
1725 N N   . ALA A 229 ? 0.7014 0.5398 0.6614 -0.1044 0.0641  -0.1514 235 ALA A N   
1726 C CA  . ALA A 229 ? 0.6769 0.5455 0.6617 -0.0949 0.0543  -0.1538 235 ALA A CA  
1727 C C   . ALA A 229 ? 0.6227 0.5163 0.6150 -0.0916 0.0592  -0.1474 235 ALA A C   
1728 O O   . ALA A 229 ? 0.6141 0.5233 0.6079 -0.0973 0.0729  -0.1453 235 ALA A O   
1729 C CB  . ALA A 229 ? 0.6043 0.5084 0.6180 -0.0957 0.0559  -0.1639 235 ALA A CB  
1730 N N   . THR A 230 ? 0.5546 0.4518 0.5519 -0.0825 0.0477  -0.1445 236 THR A N   
1731 C CA  . THR A 230 ? 0.5573 0.4706 0.5575 -0.0792 0.0506  -0.1373 236 THR A CA  
1732 C C   . THR A 230 ? 0.5145 0.4504 0.5344 -0.0694 0.0385  -0.1379 236 THR A C   
1733 O O   . THR A 230 ? 0.5275 0.4586 0.5536 -0.0648 0.0267  -0.1429 236 THR A O   
1734 C CB  . THR A 230 ? 0.5950 0.4678 0.5631 -0.0804 0.0511  -0.1288 236 THR A CB  
1735 O OG1 . THR A 230 ? 0.6187 0.5087 0.5898 -0.0793 0.0579  -0.1225 236 THR A OG1 
1736 C CG2 . THR A 230 ? 0.6243 0.4677 0.5797 -0.0731 0.0348  -0.1265 236 THR A CG2 
1737 N N   . ASN A 231 ? 0.5569 0.5173 0.5868 -0.0663 0.0412  -0.1327 237 ASN A N   
1738 C CA  . ASN A 231 ? 0.5490 0.5268 0.5937 -0.0572 0.0297  -0.1314 237 ASN A CA  
1739 C C   . ASN A 231 ? 0.5672 0.5158 0.5916 -0.0522 0.0220  -0.1232 237 ASN A C   
1740 O O   . ASN A 231 ? 0.5762 0.5280 0.6078 -0.0445 0.0096  -0.1227 237 ASN A O   
1741 C CB  . ASN A 231 ? 0.5263 0.5525 0.5975 -0.0564 0.0358  -0.1307 237 ASN A CB  
1742 C CG  . ASN A 231 ? 0.5544 0.6137 0.6477 -0.0609 0.0427  -0.1386 237 ASN A CG  
1743 O OD1 . ASN A 231 ? 0.5464 0.6298 0.6488 -0.0660 0.0550  -0.1379 237 ASN A OD1 
1744 N ND2 . ASN A 231 ? 0.5705 0.6317 0.6732 -0.0591 0.0349  -0.1466 237 ASN A ND2 
1745 N N   . LEU A 232 ? 0.6335 0.5550 0.6335 -0.0564 0.0292  -0.1170 238 LEU A N   
1746 C CA  . LEU A 232 ? 0.6183 0.5149 0.5993 -0.0521 0.0234  -0.1089 238 LEU A CA  
1747 C C   . LEU A 232 ? 0.6284 0.4802 0.5760 -0.0580 0.0277  -0.1055 238 LEU A C   
1748 O O   . LEU A 232 ? 0.6515 0.5028 0.5932 -0.0660 0.0410  -0.1063 238 LEU A O   
1749 C CB  . LEU A 232 ? 0.5825 0.5064 0.5745 -0.0505 0.0299  -0.1033 238 LEU A CB  
1750 C CG  . LEU A 232 ? 0.6072 0.5128 0.5851 -0.0451 0.0233  -0.0954 238 LEU A CG  
1751 C CD1 . LEU A 232 ? 0.6278 0.5338 0.6138 -0.0366 0.0069  -0.0963 238 LEU A CD1 
1752 C CD2 . LEU A 232 ? 0.5615 0.4946 0.5510 -0.0447 0.0315  -0.0905 238 LEU A CD2 
1753 N N   . VAL A 233 ? 0.6728 0.4876 0.5986 -0.0542 0.0166  -0.1018 239 VAL A N   
1754 C CA  . VAL A 233 ? 0.6579 0.4280 0.5494 -0.0595 0.0194  -0.0975 239 VAL A CA  
1755 C C   . VAL A 233 ? 0.7118 0.4667 0.5878 -0.0558 0.0167  -0.0893 239 VAL A C   
1756 O O   . VAL A 233 ? 0.7173 0.4657 0.5937 -0.0480 0.0032  -0.0872 239 VAL A O   
1757 C CB  . VAL A 233 ? 0.7408 0.4747 0.6162 -0.0595 0.0083  -0.1001 239 VAL A CB  
1758 C CG1 . VAL A 233 ? 0.7644 0.4515 0.6029 -0.0649 0.0101  -0.0945 239 VAL A CG1 
1759 C CG2 . VAL A 233 ? 0.7540 0.5003 0.6429 -0.0640 0.0120  -0.1083 239 VAL A CG2 
1760 N N   . ILE A 234 ? 0.7093 0.4580 0.5714 -0.0615 0.0294  -0.0852 240 ILE A N   
1761 C CA  . ILE A 234 ? 0.7060 0.4381 0.5510 -0.0593 0.0287  -0.0779 240 ILE A CA  
1762 C C   . ILE A 234 ? 0.7747 0.4593 0.5827 -0.0655 0.0309  -0.0747 240 ILE A C   
1763 O O   . ILE A 234 ? 0.7468 0.4233 0.5442 -0.0744 0.0429  -0.0763 240 ILE A O   
1764 C CB  . ILE A 234 ? 0.6607 0.4234 0.5192 -0.0605 0.0415  -0.0755 240 ILE A CB  
1765 C CG1 . ILE A 234 ? 0.6137 0.4248 0.5090 -0.0555 0.0401  -0.0786 240 ILE A CG1 
1766 C CG2 . ILE A 234 ? 0.6289 0.3735 0.4702 -0.0574 0.0396  -0.0684 240 ILE A CG2 
1767 C CD1 . ILE A 234 ? 0.5560 0.3998 0.4673 -0.0569 0.0523  -0.0766 240 ILE A CD1 
1768 N N   . LEU A 235 ? 0.7728 0.4267 0.5608 -0.0612 0.0194  -0.0700 241 LEU A N   
1769 C CA  . LEU A 235 ? 0.7928 0.3999 0.5444 -0.0667 0.0192  -0.0666 241 LEU A CA  
1770 C C   . LEU A 235 ? 0.8714 0.4699 0.6065 -0.0690 0.0279  -0.0609 241 LEU A C   
1771 O O   . LEU A 235 ? 0.8815 0.4914 0.6241 -0.0623 0.0236  -0.0575 241 LEU A O   
1772 C CB  . LEU A 235 ? 0.8289 0.4058 0.5677 -0.0609 0.0007  -0.0651 241 LEU A CB  
1773 C CG  . LEU A 235 ? 0.9664 0.4927 0.6669 -0.0666 -0.0019 -0.0615 241 LEU A CG  
1774 C CD1 . LEU A 235 ? 0.9576 0.4746 0.6495 -0.0768 0.0086  -0.0649 241 LEU A CD1 
1775 C CD2 . LEU A 235 ? 0.9981 0.4992 0.6909 -0.0599 -0.0215 -0.0607 241 LEU A CD2 
1776 N N   . CYS A 236 ? 0.9353 0.5146 0.6488 -0.0786 0.0404  -0.0602 242 CYS A N   
1777 C CA  . CYS A 236 ? 0.8829 0.4541 0.5804 -0.0818 0.0505  -0.0559 242 CYS A CA  
1778 C C   . CYS A 236 ? 1.0127 0.5375 0.6712 -0.0901 0.0530  -0.0532 242 CYS A C   
1779 O O   . CYS A 236 ? 1.1004 0.6201 0.7465 -0.0990 0.0678  -0.0535 242 CYS A O   
1780 C CB  . CYS A 236 ? 0.8363 0.4428 0.5531 -0.0860 0.0677  -0.0585 242 CYS A CB  
1781 S SG  . CYS A 236 ? 0.8720 0.5296 0.6294 -0.0765 0.0651  -0.0593 242 CYS A SG  
1782 N N   . THR A 237 ? 1.0794 0.5699 0.7180 -0.0876 0.0384  -0.0507 243 THR A N   
1783 C CA  . THR A 237 ? 1.1647 0.6095 0.7642 -0.0952 0.0394  -0.0471 243 THR A CA  
1784 C C   . THR A 237 ? 1.2026 0.6165 0.7842 -0.0889 0.0216  -0.0425 243 THR A C   
1785 O O   . THR A 237 ? 1.2074 0.6272 0.8042 -0.0808 0.0070  -0.0437 243 THR A O   
1786 C CB  . THR A 237 ? 1.1880 0.6173 0.7778 -0.1041 0.0433  -0.0504 243 THR A CB  
1787 O OG1 . THR A 237 ? 1.3810 0.7663 0.9316 -0.1125 0.0455  -0.0464 243 THR A OG1 
1788 C CG2 . THR A 237 ? 1.0973 0.5250 0.6994 -0.0986 0.0281  -0.0532 243 THR A CG2 
1789 N N   . GLY A 238 ? 1.2196 0.6015 0.7696 -0.0926 0.0229  -0.0375 244 GLY A N   
1790 C CA  . GLY A 238 ? 1.2064 0.5547 0.7354 -0.0879 0.0062  -0.0329 244 GLY A CA  
1791 C C   . GLY A 238 ? 1.2296 0.5765 0.7526 -0.0827 0.0038  -0.0285 244 GLY A C   
1792 O O   . GLY A 238 ? 1.2435 0.5792 0.7644 -0.0748 -0.0120 -0.0258 244 GLY A O   
1793 N N   . ILE A 239 ? 1.1948 0.5524 0.7149 -0.0870 0.0192  -0.0280 245 ILE A N   
1794 C CA  . ILE A 239 ? 1.1448 0.4969 0.6556 -0.0831 0.0178  -0.0240 245 ILE A CA  
1795 C C   . ILE A 239 ? 1.2159 0.5186 0.6850 -0.0877 0.0116  -0.0193 245 ILE A C   
1796 O O   . ILE A 239 ? 1.2651 0.5427 0.7087 -0.0980 0.0194  -0.0191 245 ILE A O   
1797 C CB  . ILE A 239 ? 1.1224 0.4994 0.6424 -0.0866 0.0362  -0.0253 245 ILE A CB  
1798 C CG1 . ILE A 239 ? 1.1248 0.5491 0.6843 -0.0839 0.0431  -0.0300 245 ILE A CG1 
1799 C CG2 . ILE A 239 ? 1.0968 0.4755 0.6154 -0.0805 0.0333  -0.0219 245 ILE A CG2 
1800 C CD1 . ILE A 239 ? 1.0957 0.5440 0.6834 -0.0726 0.0292  -0.0302 245 ILE A CD1 
1801 N N   . LYS A 240 ? 1.2007 0.4889 0.6622 -0.0803 -0.0028 -0.0154 246 LYS A N   
1802 C CA  . LYS A 240 ? 1.1756 0.4174 0.5975 -0.0840 -0.0099 -0.0106 246 LYS A CA  
1803 C C   . LYS A 240 ? 1.2173 0.4564 0.6367 -0.0763 -0.0183 -0.0070 246 LYS A C   
1804 O O   . LYS A 240 ? 1.1708 0.4412 0.6198 -0.0670 -0.0226 -0.0080 246 LYS A O   
1805 C CB  . LYS A 240 ? 1.2582 0.4704 0.6666 -0.0842 -0.0250 -0.0094 246 LYS A CB  
1806 C CG  . LYS A 240 ? 1.2749 0.4997 0.7069 -0.0723 -0.0433 -0.0100 246 LYS A CG  
1807 C CD  . LYS A 240 ? 1.3232 0.5331 0.7455 -0.0699 -0.0593 -0.0069 246 LYS A CD  
1808 C CE  . LYS A 240 ? 1.4286 0.6253 0.8397 -0.0788 -0.0541 -0.0083 246 LYS A CE  
1809 N NZ  . LYS A 240 ? 1.5920 0.8051 1.0291 -0.0778 -0.0532 -0.0146 246 LYS A NZ  
1810 N N   . ILE A 241 ? 1.2181 0.4231 0.6030 -0.0803 -0.0203 -0.0027 247 ILE A N   
1811 C CA  . ILE A 241 ? 1.2036 0.4086 0.5847 -0.0738 -0.0268 0.0007  247 ILE A CA  
1812 C C   . ILE A 241 ? 1.2031 0.4174 0.6015 -0.0621 -0.0472 0.0023  247 ILE A C   
1813 O O   . ILE A 241 ? 1.2404 0.4501 0.6402 -0.0603 -0.0587 0.0027  247 ILE A O   
1814 C CB  . ILE A 241 ? 1.3008 0.4811 0.6469 -0.0801 -0.0245 0.0043  247 ILE A CB  
1815 C CG1 . ILE A 241 ? 1.3357 0.5059 0.6638 -0.0928 -0.0045 0.0022  247 ILE A CG1 
1816 C CG2 . ILE A 241 ? 1.2708 0.4516 0.6127 -0.0747 -0.0283 0.0067  247 ILE A CG2 
1817 C CD1 . ILE A 241 ? 1.2562 0.4383 0.5926 -0.0949 0.0117  -0.0007 247 ILE A CD1 
1818 N N   . ASN A 242 ? 1.1602 0.3880 0.5725 -0.0542 -0.0517 0.0032  248 ASN A N   
1819 C CA  . ASN A 242 ? 1.1759 0.4150 0.6062 -0.0432 -0.0701 0.0045  248 ASN A CA  
1820 C C   . ASN A 242 ? 1.2359 0.4612 0.6468 -0.0408 -0.0802 0.0088  248 ASN A C   
1821 O O   . ASN A 242 ? 1.2383 0.4693 0.6514 -0.0364 -0.0817 0.0104  248 ASN A O   
1822 C CB  . ASN A 242 ? 1.1277 0.3914 0.5867 -0.0359 -0.0697 0.0026  248 ASN A CB  
1823 C CG  . ASN A 242 ? 1.1402 0.4183 0.6211 -0.0252 -0.0877 0.0029  248 ASN A CG  
1824 O OD1 . ASN A 242 ? 1.1045 0.3739 0.5776 -0.0225 -0.1008 0.0051  248 ASN A OD1 
1825 N ND2 . ASN A 242 ? 1.1971 0.5100 0.7116 -0.0188 -0.0875 0.0005  248 ASN A ND2 
1826 N N   . SER A 243 ? 1.1651 0.3725 0.5577 -0.0437 -0.0877 0.0106  249 SER A N   
1827 C CA  . SER A 243 ? 1.2701 0.4617 0.6415 -0.0427 -0.0978 0.0141  249 SER A CA  
1828 C C   . SER A 243 ? 1.3063 0.5075 0.6938 -0.0328 -0.1169 0.0148  249 SER A C   
1829 O O   . SER A 243 ? 1.3262 0.5138 0.6970 -0.0321 -0.1271 0.0172  249 SER A O   
1830 C CB  . SER A 243 ? 1.3465 0.5126 0.6885 -0.0513 -0.0966 0.0156  249 SER A CB  
1831 O OG  . SER A 243 ? 1.4326 0.5938 0.7668 -0.0604 -0.0798 0.0138  249 SER A OG  
1832 N N   . SER A 244 ? 1.2490 0.4729 0.6679 -0.0255 -0.1219 0.0125  250 SER A N   
1833 C CA  . SER A 244 ? 1.2592 0.4937 0.6947 -0.0164 -0.1395 0.0126  250 SER A CA  
1834 C C   . SER A 244 ? 1.3438 0.5736 0.7680 -0.0134 -0.1468 0.0153  250 SER A C   
1835 O O   . SER A 244 ? 1.3614 0.5815 0.7763 -0.0116 -0.1596 0.0166  250 SER A O   
1836 C CB  . SER A 244 ? 1.1983 0.4601 0.6686 -0.0091 -0.1411 0.0096  250 SER A CB  
1837 O OG  . SER A 244 ? 1.2685 0.5397 0.7436 -0.0097 -0.1294 0.0096  250 SER A OG  
1838 N N   . ALA A 245 ? 1.3359 0.5714 0.7598 -0.0133 -0.1384 0.0160  251 ALA A N   
1839 C CA  . ALA A 245 ? 1.3302 0.5663 0.7498 -0.0092 -0.1454 0.0179  251 ALA A CA  
1840 C C   . ALA A 245 ? 1.4286 0.6388 0.8142 -0.0146 -0.1476 0.0200  251 ALA A C   
1841 O O   . ALA A 245 ? 1.4648 0.6730 0.8462 -0.0109 -0.1585 0.0210  251 ALA A O   
1842 C CB  . ALA A 245 ? 1.3008 0.5489 0.7287 -0.0082 -0.1348 0.0179  251 ALA A CB  
1843 N N   . TYR A 246 ? 1.3583 0.5482 0.7189 -0.0237 -0.1375 0.0206  252 TYR A N   
1844 C CA  . TYR A 246 ? 1.4180 0.5837 0.7450 -0.0294 -0.1369 0.0225  252 TYR A CA  
1845 C C   . TYR A 246 ? 1.4953 0.6373 0.7972 -0.0364 -0.1392 0.0235  252 TYR A C   
1846 O O   . TYR A 246 ? 1.5163 0.6367 0.7883 -0.0417 -0.1392 0.0250  252 TYR A O   
1847 C CB  . TYR A 246 ? 1.4236 0.5844 0.7374 -0.0350 -0.1201 0.0223  252 TYR A CB  
1848 C CG  . TYR A 246 ? 1.3743 0.5329 0.6856 -0.0424 -0.1037 0.0209  252 TYR A CG  
1849 C CD1 . TYR A 246 ? 1.4193 0.5558 0.7039 -0.0518 -0.0979 0.0214  252 TYR A CD1 
1850 C CD2 . TYR A 246 ? 1.3073 0.4859 0.6424 -0.0404 -0.0938 0.0190  252 TYR A CD2 
1851 C CE1 . TYR A 246 ? 1.3969 0.5321 0.6794 -0.0592 -0.0824 0.0197  252 TYR A CE1 
1852 C CE2 . TYR A 246 ? 1.2768 0.4537 0.6097 -0.0477 -0.0782 0.0171  252 TYR A CE2 
1853 C CZ  . TYR A 246 ? 1.3784 0.5340 0.6853 -0.0571 -0.0725 0.0174  252 TYR A CZ  
1854 O OH  . TYR A 246 ? 1.3620 0.5165 0.6669 -0.0650 -0.0566 0.0151  252 TYR A OH  
1855 N N   . ARG A 247 ? 1.5645 0.7094 0.8772 -0.0365 -0.1415 0.0227  253 ARG A N   
1856 C CA  . ARG A 247 ? 1.5519 0.6741 0.8406 -0.0444 -0.1407 0.0238  253 ARG A CA  
1857 C C   . ARG A 247 ? 1.5954 0.7005 0.8660 -0.0436 -0.1562 0.0257  253 ARG A C   
1858 O O   . ARG A 247 ? 1.6431 0.7237 0.8817 -0.0512 -0.1543 0.0274  253 ARG A O   
1859 C CB  . ARG A 247 ? 1.5146 0.6453 0.8219 -0.0442 -0.1400 0.0220  253 ARG A CB  
1860 C CG  . ARG A 247 ? 1.6315 0.7404 0.9152 -0.0538 -0.1346 0.0229  253 ARG A CG  
1861 C CD  . ARG A 247 ? 1.6355 0.7483 0.9350 -0.0518 -0.1420 0.0217  253 ARG A CD  
1862 N NE  . ARG A 247 ? 1.7758 0.8636 1.0489 -0.0594 -0.1437 0.0236  253 ARG A NE  
1863 C CZ  . ARG A 247 ? 1.8141 0.8872 1.0743 -0.0580 -0.1583 0.0257  253 ARG A CZ  
1864 N NH1 . ARG A 247 ? 1.8018 0.8834 1.0738 -0.0493 -0.1727 0.0258  253 ARG A NH1 
1865 N NH2 . ARG A 247 ? 1.8537 0.9032 1.0886 -0.0659 -0.1585 0.0276  253 ARG A NH2 
1866 N N   . LYS A 248 ? 1.6222 0.7396 0.9126 -0.0348 -0.1717 0.0252  254 LYS A N   
1867 C CA  . LYS A 248 ? 1.6364 0.7391 0.9122 -0.0335 -0.1873 0.0266  254 LYS A CA  
1868 C C   . LYS A 248 ? 1.6726 0.7577 0.9193 -0.0375 -0.1866 0.0281  254 LYS A C   
1869 O O   . LYS A 248 ? 1.8239 0.8863 1.0446 -0.0417 -0.1936 0.0297  254 LYS A O   
1870 C CB  . LYS A 248 ? 1.6174 0.7400 0.9220 -0.0231 -0.2023 0.0250  254 LYS A CB  
1871 C CG  . LYS A 248 ? 1.7004 0.8101 0.9932 -0.0212 -0.2192 0.0258  254 LYS A CG  
1872 N N   . ALA A 249 ? 1.6546 0.7490 0.9046 -0.0364 -0.1781 0.0276  255 ALA A N   
1873 C CA  . ALA A 249 ? 1.6007 0.6806 0.8262 -0.0391 -0.1781 0.0284  255 ALA A CA  
1874 C C   . ALA A 249 ? 1.6498 0.7083 0.8435 -0.0496 -0.1634 0.0291  255 ALA A C   
1875 O O   . ALA A 249 ? 1.7279 0.7662 0.8929 -0.0540 -0.1650 0.0299  255 ALA A O   
1876 C CB  . ALA A 249 ? 1.6148 0.7150 0.8599 -0.0323 -0.1773 0.0273  255 ALA A CB  
1877 N N   . PHE A 250 ? 1.6054 0.6678 0.8032 -0.0541 -0.1487 0.0286  256 PHE A N   
1878 C CA  . PHE A 250 ? 1.5882 0.6320 0.7573 -0.0647 -0.1332 0.0287  256 PHE A CA  
1879 C C   . PHE A 250 ? 1.6571 0.6865 0.8128 -0.0725 -0.1291 0.0293  256 PHE A C   
1880 O O   . PHE A 250 ? 1.6495 0.6707 0.7907 -0.0810 -0.1134 0.0287  256 PHE A O   
1881 C CB  . PHE A 250 ? 1.6012 0.6598 0.7829 -0.0653 -0.1164 0.0270  256 PHE A CB  
1882 C CG  . PHE A 250 ? 1.6091 0.6789 0.7998 -0.0594 -0.1173 0.0264  256 PHE A CG  
1883 C CD1 . PHE A 250 ? 1.5527 0.6468 0.7758 -0.0488 -0.1269 0.0260  256 PHE A CD1 
1884 C CD2 . PHE A 250 ? 1.6642 0.7209 0.8316 -0.0647 -0.1073 0.0259  256 PHE A CD2 
1885 C CE1 . PHE A 250 ? 1.5083 0.6131 0.7403 -0.0436 -0.1274 0.0256  256 PHE A CE1 
1886 C CE2 . PHE A 250 ? 1.6302 0.6972 0.8067 -0.0592 -0.1078 0.0253  256 PHE A CE2 
1887 C CZ  . PHE A 250 ? 1.5226 0.6139 0.7317 -0.0486 -0.1181 0.0253  256 PHE A CZ  
1888 N N   . GLU A 251 ? 1.6771 0.7042 0.8385 -0.0697 -0.1427 0.0303  257 GLU A N   
1889 C CA  . GLU A 251 ? 1.7058 0.7190 0.8552 -0.0769 -0.1398 0.0311  257 GLU A CA  
1890 C C   . GLU A 251 ? 1.8100 0.7961 0.9199 -0.0889 -0.1297 0.0319  257 GLU A C   
1891 O O   . GLU A 251 ? 1.7422 0.7223 0.8436 -0.0971 -0.1164 0.0314  257 GLU A O   
1892 C CB  . GLU A 251 ? 1.6469 0.6554 0.8007 -0.0728 -0.1581 0.0324  257 GLU A CB  
1893 N N   . SER A 252 ? 1.8189 0.7887 0.9045 -0.0904 -0.1353 0.0328  258 SER A N   
1894 C CA  . SER A 252 ? 1.8332 0.7767 0.8798 -0.1019 -0.1259 0.0331  258 SER A CA  
1895 C C   . SER A 252 ? 1.8335 0.7821 0.8780 -0.1078 -0.1047 0.0310  258 SER A C   
1896 O O   . SER A 252 ? 1.8144 0.7450 0.8324 -0.1189 -0.0927 0.0306  258 SER A O   
1897 C CB  . SER A 252 ? 1.7853 0.7142 0.8104 -0.1013 -0.1352 0.0336  258 SER A CB  
1898 O OG  . SER A 252 ? 1.8491 0.7711 0.8559 -0.1068 -0.1213 0.0320  258 SER A OG  
1899 N N   . ARG A 253 ? 1.8497 0.8226 0.9221 -0.1007 -0.0997 0.0294  259 ARG A N   
1900 C CA  . ARG A 253 ? 1.8264 0.8049 0.8979 -0.1052 -0.0804 0.0271  259 ARG A CA  
1901 C C   . ARG A 253 ? 1.7908 0.7862 0.8849 -0.1065 -0.0684 0.0256  259 ARG A C   
1902 O O   . ARG A 253 ? 1.7627 0.7561 0.8485 -0.1141 -0.0504 0.0235  259 ARG A O   
1903 C CB  . ARG A 253 ? 1.8023 0.7954 0.8881 -0.0974 -0.0816 0.0263  259 ARG A CB  
1904 C CG  . ARG A 253 ? 1.7956 0.7705 0.8554 -0.0982 -0.0892 0.0269  259 ARG A CG  
1905 C CD  . ARG A 253 ? 1.8604 0.8076 0.8806 -0.1112 -0.0781 0.0263  259 ARG A CD  
1906 N NE  . ARG A 253 ? 1.9148 0.8406 0.9063 -0.1131 -0.0869 0.0268  259 ARG A NE  
1907 C CZ  . ARG A 253 ? 1.9258 0.8258 0.8801 -0.1241 -0.0790 0.0259  259 ARG A CZ  
1908 N NH1 . ARG A 253 ? 1.8714 0.7640 0.8126 -0.1342 -0.0620 0.0243  259 ARG A NH1 
1909 N NH2 . ARG A 253 ? 1.9750 0.8563 0.9047 -0.1253 -0.0883 0.0261  259 ARG A NH2 
1910 N N   . LEU A 254 ? 1.8230 0.8347 0.9453 -0.0995 -0.0774 0.0260  260 LEU A N   
1911 C CA  . LEU A 254 ? 1.6881 0.7167 0.8334 -0.1003 -0.0665 0.0240  260 LEU A CA  
1912 C C   . LEU A 254 ? 1.7253 0.7369 0.8484 -0.1126 -0.0547 0.0236  260 LEU A C   
1913 O O   . LEU A 254 ? 1.7722 0.7654 0.8766 -0.1165 -0.0626 0.0256  260 LEU A O   
1914 C CB  . LEU A 254 ? 1.5954 0.6420 0.7724 -0.0909 -0.0798 0.0242  260 LEU A CB  
1915 N N   . ALA A 255 ? 1.6927 0.7099 0.8171 -0.1190 -0.0355 0.0209  261 ALA A N   
1916 C CA  . ALA A 255 ? 1.7012 0.7081 0.8120 -0.1302 -0.0231 0.0197  261 ALA A CA  
1917 C C   . ALA A 255 ? 1.7421 0.7594 0.8756 -0.1268 -0.0304 0.0199  261 ALA A C   
1918 O O   . ALA A 255 ? 1.6999 0.7339 0.8605 -0.1160 -0.0429 0.0202  261 ALA A O   
1919 C CB  . ALA A 255 ? 1.6163 0.6314 0.7293 -0.1370 -0.0010 0.0160  261 ALA A CB  
1920 N N   . SER A 256 ? 1.7520 0.7593 0.8741 -0.1363 -0.0224 0.0193  262 SER A N   
1921 C CA  . SER A 256 ? 1.7434 0.7567 0.8834 -0.1336 -0.0306 0.0195  262 SER A CA  
1922 C C   . SER A 256 ? 1.7848 0.8269 0.9636 -0.1264 -0.0277 0.0164  262 SER A C   
1923 O O   . SER A 256 ? 1.7509 0.8043 0.9528 -0.1179 -0.0410 0.0165  262 SER A O   
1924 C CB  . SER A 256 ? 1.7723 0.7697 0.8928 -0.1458 -0.0212 0.0192  262 SER A CB  
1925 N N   . SER A 257 ? 1.7690 0.8236 0.9556 -0.1296 -0.0107 0.0132  263 SER A N   
1926 C CA  . SER A 257 ? 1.6492 0.7306 0.8707 -0.1243 -0.0057 0.0096  263 SER A CA  
1927 C C   . SER A 257 ? 1.5493 0.6483 0.7953 -0.1110 -0.0184 0.0102  263 SER A C   
1928 O O   . SER A 257 ? 1.6013 0.7225 0.8760 -0.1063 -0.0151 0.0072  263 SER A O   
1929 C CB  . SER A 257 ? 1.6076 0.6962 0.8287 -0.1320 0.0164  0.0060  263 SER A CB  
1930 O OG  . SER A 257 ? 1.5344 0.6303 0.7590 -0.1271 0.0186  0.0060  263 SER A OG  
1931 N N   . GLY A 258 ? 1.5831 0.6735 0.8191 -0.1051 -0.0328 0.0136  264 GLY A N   
1932 C CA  . GLY A 258 ? 1.5014 0.6086 0.7594 -0.0932 -0.0440 0.0141  264 GLY A CA  
1933 C C   . GLY A 258 ? 1.4964 0.6059 0.7488 -0.0921 -0.0375 0.0142  264 GLY A C   
1934 O O   . GLY A 258 ? 1.4555 0.5725 0.7173 -0.0831 -0.0489 0.0156  264 GLY A O   
1935 N N   . ALA A 259 ? 1.4810 0.5845 0.7186 -0.1011 -0.0193 0.0125  265 ALA A N   
1936 C CA  . ALA A 259 ? 1.4902 0.5957 0.7232 -0.1002 -0.0121 0.0121  265 ALA A CA  
1937 C C   . ALA A 259 ? 1.5298 0.6136 0.7326 -0.1015 -0.0195 0.0150  265 ALA A C   
1938 O O   . ALA A 259 ? 1.5471 0.6106 0.7261 -0.1066 -0.0249 0.0169  265 ALA A O   
1939 C CB  . ALA A 259 ? 1.4855 0.5919 0.7133 -0.1098 0.0105  0.0086  265 ALA A CB  
1940 N N   . LEU A 260 ? 1.4890 0.5774 0.6936 -0.0967 -0.0201 0.0152  266 LEU A N   
1941 C CA  . LEU A 260 ? 1.4841 0.5526 0.6599 -0.0985 -0.0247 0.0170  266 LEU A CA  
1942 C C   . LEU A 260 ? 1.5094 0.5621 0.6582 -0.1101 -0.0059 0.0149  266 LEU A C   
1943 O O   . LEU A 260 ? 1.5331 0.5968 0.6924 -0.1122 0.0095  0.0120  266 LEU A O   
1944 C CB  . LEU A 260 ? 1.3986 0.4793 0.5889 -0.0884 -0.0332 0.0176  266 LEU A CB  
1945 C CG  . LEU A 260 ? 1.4100 0.5102 0.6308 -0.0767 -0.0502 0.0189  266 LEU A CG  
1946 C CD1 . LEU A 260 ? 1.3435 0.4699 0.5966 -0.0691 -0.0468 0.0175  266 LEU A CD1 
1947 C CD2 . LEU A 260 ? 1.4754 0.5664 0.6856 -0.0717 -0.0676 0.0214  266 LEU A CD2 
1948 N N   . ARG A 261 ? 1.6112 0.6382 0.7257 -0.1181 -0.0068 0.0160  267 ARG A N   
1949 C CA  . ARG A 261 ? 1.6931 0.7033 0.7789 -0.1292 0.0100  0.0137  267 ARG A CA  
1950 C C   . ARG A 261 ? 1.6462 0.6572 0.7290 -0.1255 0.0119  0.0129  267 ARG A C   
1951 O O   . ARG A 261 ? 1.5955 0.6078 0.6820 -0.1170 -0.0034 0.0151  267 ARG A O   
1952 C CB  . ARG A 261 ? 1.7288 0.7103 0.7773 -0.1384 0.0068  0.0151  267 ARG A CB  
1953 C CG  . ARG A 261 ? 1.7690 0.7465 0.8198 -0.1370 -0.0071 0.0179  267 ARG A CG  
1954 C CD  . ARG A 261 ? 1.9049 0.8522 0.9170 -0.1450 -0.0130 0.0196  267 ARG A CD  
1955 N NE  . ARG A 261 ? 1.8599 0.8023 0.8733 -0.1379 -0.0349 0.0231  267 ARG A NE  
1956 C CZ  . ARG A 261 ? 1.9572 0.8905 0.9656 -0.1400 -0.0436 0.0251  267 ARG A CZ  
1957 N NH1 . ARG A 261 ? 2.0610 0.9878 1.0613 -0.1493 -0.0329 0.0243  267 ARG A NH1 
1958 N NH2 . ARG A 261 ? 2.0148 0.9455 1.0272 -0.1327 -0.0635 0.0278  267 ARG A NH2 
1959 N N   . VAL A 262 ? 1.6265 0.6372 0.7033 -0.1321 0.0311  0.0093  268 VAL A N   
1960 C CA  . VAL A 262 ? 1.6637 0.6762 0.7398 -0.1290 0.0353  0.0079  268 VAL A CA  
1961 C C   . VAL A 262 ? 1.6616 0.6575 0.7099 -0.1413 0.0551  0.0041  268 VAL A C   
1962 O O   . VAL A 262 ? 1.6403 0.6319 0.6804 -0.1514 0.0689  0.0018  268 VAL A O   
1963 C CB  . VAL A 262 ? 1.6072 0.6484 0.7224 -0.1197 0.0378  0.0067  268 VAL A CB  
1964 C CG1 . VAL A 262 ? 1.5238 0.5805 0.6642 -0.1069 0.0172  0.0101  268 VAL A CG1 
1965 C CG2 . VAL A 262 ? 1.5426 0.5972 0.6745 -0.1249 0.0533  0.0036  268 VAL A CG2 
1966 N N   . ASN A 263 ? 1.7096 0.6968 0.7444 -0.1408 0.0569  0.0030  269 ASN A N   
1967 C CA  . ASN A 263 ? 1.7148 0.6881 0.7259 -0.1520 0.0767  -0.0015 269 ASN A CA  
1968 C C   . ASN A 263 ? 1.7401 0.7340 0.7774 -0.1516 0.0939  -0.0057 269 ASN A C   
1969 O O   . ASN A 263 ? 1.6166 0.6337 0.6875 -0.1446 0.0915  -0.0052 269 ASN A O   
1970 C CB  . ASN A 263 ? 1.7582 0.7132 0.7440 -0.1520 0.0727  -0.0016 269 ASN A CB  
1971 C CG  . ASN A 263 ? 1.7530 0.7210 0.7598 -0.1382 0.0567  0.0011  269 ASN A CG  
1972 O OD1 . ASN A 263 ? 1.7399 0.7267 0.7728 -0.1317 0.0616  -0.0005 269 ASN A OD1 
1973 N ND2 . ASN A 263 ? 1.7884 0.7468 0.7848 -0.1336 0.0373  0.0049  269 ASN A ND2 
1974 N N   . GLU A 264 ? 1.7523 0.7381 0.7753 -0.1592 0.1115  -0.0105 270 GLU A N   
1975 C CA  . GLU A 264 ? 1.6948 0.7000 0.7436 -0.1589 0.1282  -0.0157 270 GLU A CA  
1976 C C   . GLU A 264 ? 1.6916 0.7154 0.7675 -0.1457 0.1206  -0.0159 270 GLU A C   
1977 O O   . GLU A 264 ? 1.6152 0.6745 0.7249 -0.1409 0.1309  -0.0207 270 GLU A O   
1978 C CB  . GLU A 264 ? 1.7804 0.7784 0.8092 -0.1711 0.1502  -0.0222 270 GLU A CB  
1979 C CG  . GLU A 264 ? 1.8769 0.8402 0.8628 -0.1776 0.1485  -0.0216 270 GLU A CG  
1980 C CD  . GLU A 264 ? 1.9313 0.8897 0.8993 -0.1896 0.1710  -0.0289 270 GLU A CD  
1981 O OE1 . GLU A 264 ? 1.9688 0.9497 0.9534 -0.1945 0.1873  -0.0339 270 GLU A OE1 
1982 O OE2 . GLU A 264 ? 2.0015 0.9369 0.9404 -0.1937 0.1722  -0.0302 270 GLU A OE2 
1983 N N   . HIS A 265 ? 1.7070 0.7228 0.7767 -0.1377 0.1017  -0.0111 271 HIS A N   
1984 C CA  . HIS A 265 ? 1.6699 0.7021 0.7654 -0.1248 0.0917  -0.0102 271 HIS A CA  
1985 C C   . HIS A 265 ? 1.5474 0.5986 0.6711 -0.1137 0.0736  -0.0051 271 HIS A C   
1986 O O   . HIS A 265 ? 1.4471 0.5107 0.5900 -0.1027 0.0613  -0.0031 271 HIS A O   
1987 C CB  . HIS A 265 ? 1.6569 0.6713 0.7289 -0.1232 0.0836  -0.0089 271 HIS A CB  
1988 C CG  . HIS A 265 ? 1.7164 0.7070 0.7532 -0.1356 0.0993  -0.0132 271 HIS A CG  
1989 N ND1 . HIS A 265 ? 1.7383 0.7341 0.7798 -0.1415 0.1206  -0.0209 271 HIS A ND1 
1990 C CD2 . HIS A 265 ? 1.7116 0.6746 0.7088 -0.1435 0.0971  -0.0119 271 HIS A CD2 
1991 C CE1 . HIS A 265 ? 1.7258 0.6966 0.7311 -0.1529 0.1313  -0.0240 271 HIS A CE1 
1992 N NE2 . HIS A 265 ? 1.7428 0.6932 0.7202 -0.1544 0.1173  -0.0180 271 HIS A NE2 
1993 N N   . LEU A 266 ? 1.5675 0.6210 0.6938 -0.1169 0.0718  -0.0034 272 LEU A N   
1994 C CA  . LEU A 266 ? 1.5076 0.5783 0.6598 -0.1078 0.0561  0.0004  272 LEU A CA  
1995 C C   . LEU A 266 ? 1.5020 0.5667 0.6480 -0.1002 0.0340  0.0051  272 LEU A C   
1996 O O   . LEU A 266 ? 1.4563 0.5385 0.6281 -0.0900 0.0198  0.0076  272 LEU A O   
1997 C CB  . LEU A 266 ? 1.3986 0.4974 0.5902 -0.0995 0.0587  -0.0012 272 LEU A CB  
1998 C CG  . LEU A 266 ? 1.4433 0.5634 0.6516 -0.1053 0.0787  -0.0064 272 LEU A CG  
1999 C CD1 . LEU A 266 ? 1.3645 0.5283 0.6179 -0.0953 0.0812  -0.0087 272 LEU A CD1 
2000 C CD2 . LEU A 266 ? 1.5025 0.6212 0.7107 -0.1104 0.0787  -0.0054 272 LEU A CD2 
2001 N N   . GLN A 267 ? 1.5639 0.6040 0.6756 -0.1055 0.0311  0.0058  273 GLN A N   
2002 C CA  . GLN A 267 ? 1.5639 0.5965 0.6674 -0.0996 0.0106  0.0096  273 GLN A CA  
2003 C C   . GLN A 267 ? 1.5589 0.5828 0.6526 -0.1027 0.0016  0.0119  273 GLN A C   
2004 O O   . GLN A 267 ? 1.5896 0.5988 0.6623 -0.1132 0.0117  0.0108  273 GLN A O   
2005 C CB  . GLN A 267 ? 1.5648 0.5744 0.6357 -0.1037 0.0108  0.0090  273 GLN A CB  
2006 C CG  . GLN A 267 ? 1.5759 0.5915 0.6541 -0.1012 0.0202  0.0062  273 GLN A CG  
2007 C CD  . GLN A 267 ? 1.6580 0.6512 0.7051 -0.1042 0.0181  0.0058  273 GLN A CD  
2008 O OE1 . GLN A 267 ? 1.6536 0.6449 0.6993 -0.0976 0.0015  0.0083  273 GLN A OE1 
2009 N NE2 . GLN A 267 ? 1.7411 0.7171 0.7626 -0.1148 0.0354  0.0022  273 GLN A NE2 
2010 N N   . VAL A 268 ? 1.5394 0.5725 0.6488 -0.0937 -0.0174 0.0150  274 VAL A N   
2011 C CA  . VAL A 268 ? 1.6067 0.6327 0.7100 -0.0955 -0.0274 0.0171  274 VAL A CA  
2012 C C   . VAL A 268 ? 1.6742 0.6707 0.7382 -0.1023 -0.0326 0.0179  274 VAL A C   
2013 O O   . VAL A 268 ? 1.6908 0.6805 0.7456 -0.0985 -0.0431 0.0187  274 VAL A O   
2014 C CB  . VAL A 268 ? 1.5826 0.6284 0.7165 -0.0839 -0.0454 0.0193  274 VAL A CB  
2015 C CG1 . VAL A 268 ? 1.5815 0.6179 0.7078 -0.0857 -0.0565 0.0213  274 VAL A CG1 
2016 C CG2 . VAL A 268 ? 1.4539 0.5275 0.6249 -0.0783 -0.0394 0.0182  274 VAL A CG2 
2017 N N   . GLU A 269 ? 1.7144 0.6934 0.7549 -0.1130 -0.0249 0.0175  275 GLU A N   
2018 C CA  . GLU A 269 ? 1.8046 0.7544 0.8065 -0.1209 -0.0293 0.0181  275 GLU A CA  
2019 C C   . GLU A 269 ? 1.8438 0.7894 0.8443 -0.1135 -0.0512 0.0207  275 GLU A C   
2020 O O   . GLU A 269 ? 1.7220 0.6824 0.7470 -0.1053 -0.0645 0.0227  275 GLU A O   
2021 C CB  . GLU A 269 ? 1.8214 0.7600 0.8103 -0.1299 -0.0248 0.0184  275 GLU A CB  
2022 C CG  . GLU A 269 ? 1.8548 0.7860 0.8285 -0.1417 -0.0025 0.0151  275 GLU A CG  
2023 C CD  . GLU A 269 ? 1.9213 0.8366 0.8757 -0.1516 -0.0002 0.0155  275 GLU A CD  
2024 O OE1 . GLU A 269 ? 1.8812 0.7913 0.8350 -0.1487 -0.0164 0.0186  275 GLU A OE1 
2025 O OE2 . GLU A 269 ? 1.9452 0.8532 0.8854 -0.1626 0.0177  0.0126  275 GLU A OE2 
2026 N N   . GLY A 270 ? 1.7599 0.6850 0.7316 -0.1167 -0.0544 0.0203  276 GLY A N   
2027 C CA  . GLY A 270 ? 1.7831 0.7031 0.7515 -0.1105 -0.0742 0.0221  276 GLY A CA  
2028 C C   . GLY A 270 ? 1.8236 0.7619 0.8151 -0.0997 -0.0810 0.0220  276 GLY A C   
2029 O O   . GLY A 270 ? 1.8448 0.7798 0.8344 -0.0945 -0.0972 0.0230  276 GLY A O   
2030 N N   . HIS A 271 ? 1.7889 0.7465 0.8026 -0.0964 -0.0693 0.0207  277 HIS A N   
2031 C CA  . HIS A 271 ? 1.7328 0.7084 0.7694 -0.0865 -0.0745 0.0205  277 HIS A CA  
2032 C C   . HIS A 271 ? 1.7059 0.6826 0.7397 -0.0895 -0.0569 0.0180  277 HIS A C   
2033 O O   . HIS A 271 ? 1.7279 0.7030 0.7576 -0.0965 -0.0401 0.0163  277 HIS A O   
2034 C CB  . HIS A 271 ? 1.6501 0.6558 0.7290 -0.0760 -0.0825 0.0218  277 HIS A CB  
2035 C CG  . HIS A 271 ? 1.6635 0.6693 0.7475 -0.0731 -0.0988 0.0237  277 HIS A CG  
2036 N ND1 . HIS A 271 ? 1.7208 0.7176 0.7959 -0.0790 -0.0969 0.0244  277 HIS A ND1 
2037 C CD2 . HIS A 271 ? 1.6744 0.6872 0.7707 -0.0652 -0.1171 0.0248  277 HIS A CD2 
2038 C CE1 . HIS A 271 ? 1.7417 0.7400 0.8242 -0.0745 -0.1136 0.0261  277 HIS A CE1 
2039 N NE2 . HIS A 271 ? 1.7528 0.7610 0.8482 -0.0662 -0.1258 0.0262  277 HIS A NE2 
2040 N N   . SER A 272 ? 1.6248 0.6036 0.6601 -0.0844 -0.0608 0.0175  278 SER A N   
2041 C CA  . SER A 272 ? 1.6425 0.6254 0.6807 -0.0852 -0.0459 0.0151  278 SER A CA  
2042 C C   . SER A 272 ? 1.5419 0.5556 0.6219 -0.0744 -0.0475 0.0154  278 SER A C   
2043 O O   . SER A 272 ? 1.5198 0.5415 0.6096 -0.0750 -0.0332 0.0132  278 SER A O   
2044 C CB  . SER A 272 ? 1.6711 0.6338 0.6811 -0.0877 -0.0473 0.0141  278 SER A CB  
2045 O OG  . SER A 272 ? 1.6952 0.6653 0.7167 -0.0785 -0.0657 0.0158  278 SER A OG  
2046 N N   . ASN A 273 ? 1.4656 0.4965 0.5703 -0.0650 -0.0643 0.0176  279 ASN A N   
2047 C CA  . ASN A 273 ? 1.4019 0.4618 0.5455 -0.0546 -0.0681 0.0179  279 ASN A CA  
2048 C C   . ASN A 273 ? 1.4041 0.4859 0.5782 -0.0507 -0.0697 0.0189  279 ASN A C   
2049 O O   . ASN A 273 ? 1.3501 0.4563 0.5569 -0.0417 -0.0764 0.0196  279 ASN A O   
2050 C CB  . ASN A 273 ? 1.3817 0.4464 0.5321 -0.0467 -0.0860 0.0192  279 ASN A CB  
2051 C CG  . ASN A 273 ? 1.4024 0.4666 0.5541 -0.0446 -0.1023 0.0209  279 ASN A CG  
2052 O OD1 . ASN A 273 ? 1.4434 0.4926 0.5765 -0.0511 -0.1012 0.0213  279 ASN A OD1 
2053 N ND2 . ASN A 273 ? 1.4089 0.4900 0.5834 -0.0357 -0.1172 0.0217  279 ASN A ND2 
2054 N N   . VAL A 274 ? 1.4714 0.5447 0.6351 -0.0574 -0.0642 0.0189  280 VAL A N   
2055 C CA  . VAL A 274 ? 1.3728 0.4642 0.5626 -0.0544 -0.0657 0.0196  280 VAL A CA  
2056 C C   . VAL A 274 ? 1.3812 0.4718 0.5691 -0.0619 -0.0464 0.0176  280 VAL A C   
2057 O O   . VAL A 274 ? 1.4300 0.4993 0.5886 -0.0719 -0.0370 0.0167  280 VAL A O   
2058 C CB  . VAL A 274 ? 1.4295 0.5130 0.6119 -0.0550 -0.0792 0.0214  280 VAL A CB  
2059 C CG1 . VAL A 274 ? 1.4359 0.5338 0.6398 -0.0543 -0.0771 0.0215  280 VAL A CG1 
2060 C CG2 . VAL A 274 ? 1.3944 0.4852 0.5875 -0.0463 -0.0984 0.0227  280 VAL A CG2 
2061 N N   . TYR A 275 ? 1.3681 0.4820 0.5871 -0.0573 -0.0405 0.0167  281 TYR A N   
2062 C CA  . TYR A 275 ? 1.3740 0.4906 0.5961 -0.0637 -0.0218 0.0141  281 TYR A CA  
2063 C C   . TYR A 275 ? 1.3052 0.4373 0.5499 -0.0621 -0.0235 0.0144  281 TYR A C   
2064 O O   . TYR A 275 ? 1.2652 0.4116 0.5309 -0.0540 -0.0381 0.0163  281 TYR A O   
2065 C CB  . TYR A 275 ? 1.2885 0.4180 0.5267 -0.0608 -0.0111 0.0119  281 TYR A CB  
2066 C CG  . TYR A 275 ? 1.3384 0.4513 0.5532 -0.0637 -0.0063 0.0106  281 TYR A CG  
2067 C CD1 . TYR A 275 ? 1.3806 0.4906 0.5915 -0.0576 -0.0206 0.0126  281 TYR A CD1 
2068 C CD2 . TYR A 275 ? 1.3651 0.4655 0.5621 -0.0728 0.0128  0.0069  281 TYR A CD2 
2069 C CE1 . TYR A 275 ? 1.2998 0.3940 0.4889 -0.0602 -0.0165 0.0112  281 TYR A CE1 
2070 C CE2 . TYR A 275 ? 1.4149 0.4995 0.5902 -0.0755 0.0175  0.0052  281 TYR A CE2 
2071 C CZ  . TYR A 275 ? 1.3745 0.4557 0.5457 -0.0691 0.0026  0.0075  281 TYR A CZ  
2072 O OH  . TYR A 275 ? 1.4389 0.5040 0.5883 -0.0720 0.0073  0.0057  281 TYR A OH  
2073 N N   . ALA A 276 ? 1.3271 0.4554 0.5663 -0.0705 -0.0081 0.0121  282 ALA A N   
2074 C CA  . ALA A 276 ? 1.2742 0.4170 0.5348 -0.0701 -0.0065 0.0116  282 ALA A CA  
2075 C C   . ALA A 276 ? 1.3147 0.4662 0.5851 -0.0751 0.0136  0.0077  282 ALA A C   
2076 O O   . ALA A 276 ? 1.2721 0.4098 0.5216 -0.0837 0.0285  0.0052  282 ALA A O   
2077 C CB  . ALA A 276 ? 1.2630 0.3904 0.5052 -0.0766 -0.0098 0.0126  282 ALA A CB  
2078 N N   . ILE A 277 ? 1.1999 0.3744 0.5022 -0.0700 0.0143  0.0067  283 ILE A N   
2079 C CA  . ILE A 277 ? 1.1593 0.3655 0.4860 -0.0713 0.0317  0.0023  283 ILE A CA  
2080 C C   . ILE A 277 ? 1.2069 0.4405 0.5615 -0.0705 0.0337  0.0007  283 ILE A C   
2081 O O   . ILE A 277 ? 1.2269 0.4600 0.5893 -0.0661 0.0200  0.0029  283 ILE A O   
2082 C CB  . ILE A 277 ? 1.1426 0.3748 0.4948 -0.0624 0.0311  0.0019  283 ILE A CB  
2083 C CG1 . ILE A 277 ? 1.0724 0.3242 0.4530 -0.0511 0.0146  0.0048  283 ILE A CG1 
2084 C CG2 . ILE A 277 ? 1.1372 0.3431 0.4626 -0.0632 0.0297  0.0028  283 ILE A CG2 
2085 C CD1 . ILE A 277 ? 1.0473 0.3287 0.4570 -0.0426 0.0144  0.0046  283 ILE A CD1 
2086 N N   . GLY A 278 ? 1.1533 0.4114 0.5234 -0.0749 0.0512  -0.0036 284 GLY A N   
2087 C CA  . GLY A 278 ? 1.1759 0.4627 0.5736 -0.0746 0.0549  -0.0057 284 GLY A CA  
2088 C C   . GLY A 278 ? 1.2150 0.4790 0.5937 -0.0813 0.0517  -0.0051 284 GLY A C   
2089 O O   . GLY A 278 ? 1.2713 0.5053 0.6171 -0.0910 0.0582  -0.0053 284 GLY A O   
2090 N N   . ASP A 279 ? 1.1969 0.4752 0.5964 -0.0761 0.0415  -0.0044 285 ASP A N   
2091 C CA  . ASP A 279 ? 1.2295 0.4936 0.6183 -0.0823 0.0405  -0.0049 285 ASP A CA  
2092 C C   . ASP A 279 ? 1.2541 0.4727 0.6062 -0.0851 0.0276  -0.0009 285 ASP A C   
2093 O O   . ASP A 279 ? 1.2840 0.4804 0.6149 -0.0938 0.0305  -0.0010 285 ASP A O   
2094 C CB  . ASP A 279 ? 1.1767 0.4708 0.6000 -0.0758 0.0334  -0.0061 285 ASP A CB  
2095 C CG  . ASP A 279 ? 1.1843 0.5200 0.6394 -0.0767 0.0486  -0.0105 285 ASP A CG  
2096 O OD1 . ASP A 279 ? 1.2093 0.5513 0.6614 -0.0813 0.0637  -0.0126 285 ASP A OD1 
2097 O OD2 . ASP A 279 ? 1.1310 0.4928 0.6138 -0.0730 0.0453  -0.0122 285 ASP A OD2 
2098 N N   . CYS A 280 ? 1.2600 0.4639 0.6040 -0.0783 0.0132  0.0028  286 CYS A N   
2099 C CA  . CYS A 280 ? 1.3259 0.5025 0.6445 -0.0788 -0.0009 0.0065  286 CYS A CA  
2100 C C   . CYS A 280 ? 1.3846 0.5367 0.6673 -0.0871 0.0059  0.0075  286 CYS A C   
2101 O O   . CYS A 280 ? 1.4016 0.5368 0.6641 -0.0875 -0.0052 0.0104  286 CYS A O   
2102 C CB  . CYS A 280 ? 1.2731 0.4587 0.6058 -0.0669 -0.0202 0.0094  286 CYS A CB  
2103 S SG  . CYS A 280 ? 1.2073 0.3967 0.5401 -0.0618 -0.0192 0.0104  286 CYS A SG  
2104 N N   . ALA A 281 ? 1.3435 0.4934 0.6182 -0.0939 0.0240  0.0048  287 ALA A N   
2105 C CA  . ALA A 281 ? 1.4209 0.5481 0.6619 -0.1024 0.0323  0.0048  287 ALA A CA  
2106 C C   . ALA A 281 ? 1.5402 0.6548 0.7630 -0.1149 0.0453  0.0029  287 ALA A C   
2107 O O   . ALA A 281 ? 1.5506 0.6775 0.7886 -0.1190 0.0582  -0.0005 287 ALA A O   
2108 C CB  . ALA A 281 ? 1.4163 0.5485 0.6596 -0.1026 0.0450  0.0023  287 ALA A CB  
2109 N N   . ASP A 282 ? 1.5443 0.6344 0.7345 -0.1213 0.0420  0.0050  288 ASP A N   
2110 C CA  . ASP A 282 ? 1.5777 0.6534 0.7472 -0.1337 0.0530  0.0037  288 ASP A CA  
2111 C C   . ASP A 282 ? 1.6691 0.7402 0.8251 -0.1435 0.0748  -0.0003 288 ASP A C   
2112 O O   . ASP A 282 ? 1.7723 0.8241 0.8992 -0.1491 0.0785  -0.0002 288 ASP A O   
2113 C CB  . ASP A 282 ? 1.6249 0.6760 0.7645 -0.1368 0.0410  0.0072  288 ASP A CB  
2114 N N   . VAL A 283 ? 1.6992 0.7883 0.8767 -0.1461 0.0898  -0.0043 289 VAL A N   
2115 C CA  . VAL A 283 ? 1.7761 0.8709 0.9509 -0.1532 0.1107  -0.0091 289 VAL A CA  
2116 C C   . VAL A 283 ? 1.9149 1.0183 1.0905 -0.1641 0.1281  -0.0132 289 VAL A C   
2117 O O   . VAL A 283 ? 2.0051 1.1203 1.1811 -0.1699 0.1460  -0.0180 289 VAL A O   
2118 C CB  . VAL A 283 ? 1.7480 0.8831 0.9619 -0.1421 0.1130  -0.0120 289 VAL A CB  
2119 C CG1 . VAL A 283 ? 1.6997 0.8236 0.9079 -0.1333 0.0991  -0.0086 289 VAL A CG1 
2120 C CG2 . VAL A 283 ? 1.7079 0.8767 0.9613 -0.1344 0.1082  -0.0126 289 VAL A CG2 
2121 N N   . ARG A 284 ? 1.9065 1.0049 1.0830 -0.1671 0.1234  -0.0117 290 ARG A N   
2122 C CA  . ARG A 284 ? 1.9181 1.0254 1.0968 -0.1774 0.1391  -0.0155 290 ARG A CA  
2123 C C   . ARG A 284 ? 1.9301 1.0838 1.1477 -0.1741 0.1539  -0.0216 290 ARG A C   
2124 O O   . ARG A 284 ? 1.9787 1.1423 1.1968 -0.1833 0.1716  -0.0261 290 ARG A O   
2125 C CB  . ARG A 284 ? 1.8963 0.9708 1.0331 -0.1924 0.1509  -0.0158 290 ARG A CB  
2126 N N   . THR A 285 ? 1.8334 1.0159 1.0837 -0.1612 0.1467  -0.0217 291 THR A N   
2127 C CA  . THR A 285 ? 1.7478 0.9760 1.0388 -0.1561 0.1569  -0.0265 291 THR A CA  
2128 C C   . THR A 285 ? 1.7032 0.9540 1.0230 -0.1517 0.1505  -0.0266 291 THR A C   
2129 O O   . THR A 285 ? 1.7101 0.9409 1.0188 -0.1518 0.1378  -0.0232 291 THR A O   
2130 C CB  . THR A 285 ? 1.6928 0.9382 1.0019 -0.1448 0.1518  -0.0261 291 THR A CB  
2131 N N   . PRO A 286 ? 1.7211 1.0138 1.0782 -0.1480 0.1592  -0.0306 292 PRO A N   
2132 C CA  . PRO A 286 ? 1.6278 0.9446 1.0142 -0.1429 0.1525  -0.0310 292 PRO A CA  
2133 C C   . PRO A 286 ? 1.4546 0.7876 0.8652 -0.1292 0.1355  -0.0280 292 PRO A C   
2134 O O   . PRO A 286 ? 1.4312 0.7861 0.8673 -0.1246 0.1297  -0.0287 292 PRO A O   
2135 C CB  . PRO A 286 ? 1.5773 0.9323 0.9920 -0.1456 0.1701  -0.0367 292 PRO A CB  
2136 C CG  . PRO A 286 ? 1.5448 0.9081 0.9618 -0.1430 0.1776  -0.0379 292 PRO A CG  
2137 C CD  . PRO A 286 ? 1.6761 0.9957 1.0494 -0.1497 0.1769  -0.0357 292 PRO A CD  
2138 N N   . LYS A 287 ? 1.3758 0.6996 0.7794 -0.1228 0.1278  -0.0252 293 LYS A N   
2139 C CA  . LYS A 287 ? 1.3092 0.6453 0.7328 -0.1102 0.1111  -0.0221 293 LYS A CA  
2140 C C   . LYS A 287 ? 1.1420 0.5257 0.6088 -0.1028 0.1155  -0.0246 293 LYS A C   
2141 O O   . LYS A 287 ? 1.1015 0.5094 0.5931 -0.1007 0.1141  -0.0260 293 LYS A O   
2142 C CB  . LYS A 287 ? 1.2868 0.6084 0.7069 -0.1075 0.0946  -0.0192 293 LYS A CB  
2143 C CG  . LYS A 287 ? 1.3805 0.6539 0.7585 -0.1136 0.0873  -0.0158 293 LYS A CG  
2144 C CD  . LYS A 287 ? 1.4649 0.7152 0.8170 -0.1146 0.0881  -0.0137 293 LYS A CD  
2145 C CE  . LYS A 287 ? 1.4677 0.6699 0.7748 -0.1232 0.0843  -0.0106 293 LYS A CE  
2146 N NZ  . LYS A 287 ? 1.4332 0.6140 0.7323 -0.1180 0.0635  -0.0061 293 LYS A NZ  
2147 N N   . MET A 288 ? 1.1605 0.5573 0.6361 -0.0989 0.1205  -0.0250 294 MET A N   
2148 C CA  . MET A 288 ? 1.0414 0.4817 0.5559 -0.0925 0.1254  -0.0270 294 MET A CA  
2149 C C   . MET A 288 ? 1.0329 0.4797 0.5587 -0.0816 0.1132  -0.0235 294 MET A C   
2150 O O   . MET A 288 ? 1.0620 0.4810 0.5636 -0.0808 0.1073  -0.0210 294 MET A O   
2151 C CB  . MET A 288 ? 1.0746 0.5287 0.5930 -0.0984 0.1452  -0.0316 294 MET A CB  
2152 C CG  . MET A 288 ? 1.1052 0.5536 0.6119 -0.1099 0.1594  -0.0354 294 MET A CG  
2153 S SD  . MET A 288 ? 1.1950 0.6760 0.7336 -0.1093 0.1595  -0.0374 294 MET A SD  
2154 C CE  . MET A 288 ? 1.0223 0.5528 0.6024 -0.1045 0.1707  -0.0408 294 MET A CE  
2155 N N   . ALA A 289 ? 0.8030 0.5580 0.5829 -0.0906 0.1135  -0.0689 295 ALA A N   
2156 C CA  . ALA A 289 ? 0.7380 0.4909 0.5131 -0.0891 0.1099  -0.0639 295 ALA A CA  
2157 C C   . ALA A 289 ? 0.7760 0.5177 0.5500 -0.0893 0.1164  -0.0645 295 ALA A C   
2158 O O   . ALA A 289 ? 0.8206 0.5501 0.5827 -0.0913 0.1155  -0.0616 295 ALA A O   
2159 C CB  . ALA A 289 ? 0.7835 0.5551 0.5710 -0.0834 0.1029  -0.0606 295 ALA A CB  
2160 N N   . TYR A 290 ? 0.7865 0.5322 0.5729 -0.0869 0.1225  -0.0684 296 TYR A N   
2161 C CA  . TYR A 290 ? 0.7485 0.4846 0.5344 -0.0860 0.1280  -0.0697 296 TYR A CA  
2162 C C   . TYR A 290 ? 0.8037 0.5207 0.5728 -0.0914 0.1340  -0.0718 296 TYR A C   
2163 O O   . TYR A 290 ? 0.8321 0.5363 0.5921 -0.0917 0.1347  -0.0707 296 TYR A O   
2164 C CB  . TYR A 290 ? 0.7605 0.5062 0.5641 -0.0819 0.1332  -0.0741 296 TYR A CB  
2165 C CG  . TYR A 290 ? 0.8460 0.5904 0.6518 -0.0848 0.1420  -0.0797 296 TYR A CG  
2166 C CD1 . TYR A 290 ? 0.8155 0.5485 0.6158 -0.0866 0.1508  -0.0836 296 TYR A CD1 
2167 C CD2 . TYR A 290 ? 0.8217 0.5770 0.6356 -0.0857 0.1412  -0.0812 296 TYR A CD2 
2168 C CE1 . TYR A 290 ? 0.8091 0.5427 0.6117 -0.0897 0.1590  -0.0882 296 TYR A CE1 
2169 C CE2 . TYR A 290 ? 0.8426 0.5973 0.6590 -0.0892 0.1487  -0.0856 296 TYR A CE2 
2170 C CZ  . TYR A 290 ? 0.8448 0.5892 0.6557 -0.0914 0.1579  -0.0888 296 TYR A CZ  
2171 O OH  . TYR A 290 ? 0.8871 0.6326 0.7007 -0.0954 0.1656  -0.0926 296 TYR A OH  
2172 N N   . LEU A 291 ? 0.8511 0.5654 0.6150 -0.0959 0.1374  -0.0745 297 LEU A N   
2173 C CA  . LEU A 291 ? 0.8278 0.5240 0.5741 -0.1016 0.1423  -0.0760 297 LEU A CA  
2174 C C   . LEU A 291 ? 0.8811 0.5657 0.6113 -0.1039 0.1361  -0.0715 297 LEU A C   
2175 O O   . LEU A 291 ? 0.8717 0.5398 0.5883 -0.1064 0.1390  -0.0717 297 LEU A O   
2176 C CB  . LEU A 291 ? 0.8748 0.5712 0.6188 -0.1065 0.1451  -0.0787 297 LEU A CB  
2177 C CG  . LEU A 291 ? 0.9288 0.6336 0.6863 -0.1060 0.1531  -0.0833 297 LEU A CG  
2178 C CD1 . LEU A 291 ? 0.9550 0.6597 0.7100 -0.1117 0.1545  -0.0849 297 LEU A CD1 
2179 C CD2 . LEU A 291 ? 0.8999 0.5956 0.6541 -0.1058 0.1624  -0.0865 297 LEU A CD2 
2180 N N   . ALA A 292 ? 0.8498 0.5432 0.5812 -0.1029 0.1273  -0.0675 298 ALA A N   
2181 C CA  . ALA A 292 ? 0.8209 0.5054 0.5381 -0.1051 0.1210  -0.0630 298 ALA A CA  
2182 C C   . ALA A 292 ? 0.8730 0.5496 0.5875 -0.1033 0.1204  -0.0601 298 ALA A C   
2183 O O   . ALA A 292 ? 0.8433 0.5039 0.5426 -0.1066 0.1195  -0.0583 298 ALA A O   
2184 C CB  . ALA A 292 ? 0.7546 0.4540 0.4765 -0.1032 0.1118  -0.0595 298 ALA A CB  
2185 N N   . GLY A 293 ? 0.8092 0.4957 0.5380 -0.0982 0.1206  -0.0599 299 GLY A N   
2186 C CA  . GLY A 293 ? 0.8203 0.4983 0.5472 -0.0963 0.1193  -0.0575 299 GLY A CA  
2187 C C   . GLY A 293 ? 0.8660 0.5264 0.5840 -0.0976 0.1272  -0.0622 299 GLY A C   
2188 O O   . GLY A 293 ? 0.9571 0.6020 0.6627 -0.0991 0.1254  -0.0602 299 GLY A O   
2189 N N   . LEU A 294 ? 0.8739 0.5369 0.5983 -0.0970 0.1358  -0.0684 300 LEU A N   
2190 C CA  . LEU A 294 ? 0.8835 0.5319 0.5994 -0.0981 0.1442  -0.0734 300 LEU A CA  
2191 C C   . LEU A 294 ? 0.9283 0.5586 0.6229 -0.1040 0.1445  -0.0726 300 LEU A C   
2192 O O   . LEU A 294 ? 0.9685 0.5826 0.6512 -0.1044 0.1456  -0.0731 300 LEU A O   
2193 C CB  . LEU A 294 ? 0.9173 0.5742 0.6431 -0.0977 0.1534  -0.0796 300 LEU A CB  
2194 C CG  . LEU A 294 ? 0.9614 0.6349 0.7087 -0.0916 0.1548  -0.0819 300 LEU A CG  
2195 C CD1 . LEU A 294 ? 0.9711 0.6511 0.7262 -0.0924 0.1648  -0.0881 300 LEU A CD1 
2196 C CD2 . LEU A 294 ? 0.9568 0.6262 0.7081 -0.0860 0.1527  -0.0820 300 LEU A CD2 
2197 N N   . HIS A 295 ? 0.9484 0.5808 0.6378 -0.1086 0.1429  -0.0715 301 HIS A N   
2198 C CA  . HIS A 295 ? 0.9559 0.5719 0.6255 -0.1143 0.1414  -0.0700 301 HIS A CA  
2199 C C   . HIS A 295 ? 0.9421 0.5479 0.6024 -0.1140 0.1339  -0.0649 301 HIS A C   
2200 O O   . HIS A 295 ? 0.9887 0.5762 0.6320 -0.1174 0.1342  -0.0647 301 HIS A O   
2201 C CB  . HIS A 295 ? 0.9235 0.5460 0.5918 -0.1179 0.1374  -0.0687 301 HIS A CB  
2202 C CG  . HIS A 295 ? 1.0131 0.6431 0.6883 -0.1196 0.1436  -0.0731 301 HIS A CG  
2203 N ND1 . HIS A 295 ? 1.0134 0.6502 0.6899 -0.1221 0.1397  -0.0728 301 HIS A ND1 
2204 C CD2 . HIS A 295 ? 1.0548 0.6865 0.7360 -0.1193 0.1529  -0.0779 301 HIS A CD2 
2205 C CE1 . HIS A 295 ? 1.0472 0.6889 0.7301 -0.1238 0.1460  -0.0766 301 HIS A CE1 
2206 N NE2 . HIS A 295 ? 1.1126 0.7523 0.7990 -0.1223 0.1545  -0.0796 301 HIS A NE2 
2207 N N   . ALA A 296 ? 0.9549 0.5723 0.6260 -0.1102 0.1269  -0.0604 302 ALA A N   
2208 C CA  . ALA A 296 ? 0.9446 0.5542 0.6075 -0.1108 0.1188  -0.0543 302 ALA A CA  
2209 C C   . ALA A 296 ? 0.9675 0.5620 0.6252 -0.1090 0.1203  -0.0553 302 ALA A C   
2210 O O   . ALA A 296 ? 0.9884 0.5663 0.6314 -0.1117 0.1170  -0.0528 302 ALA A O   
2211 C CB  . ALA A 296 ? 0.8546 0.4826 0.5304 -0.1079 0.1106  -0.0486 302 ALA A CB  
2212 N N   . ASN A 297 ? 0.9813 0.5810 0.6509 -0.1041 0.1248  -0.0591 303 ASN A N   
2213 C CA  . ASN A 297 ? 0.9873 0.5721 0.6517 -0.1016 0.1266  -0.0615 303 ASN A CA  
2214 C C   . ASN A 297 ? 1.0110 0.5775 0.6583 -0.1049 0.1337  -0.0664 303 ASN A C   
2215 O O   . ASN A 297 ? 1.0192 0.5678 0.6539 -0.1050 0.1319  -0.0663 303 ASN A O   
2216 C CB  . ASN A 297 ? 0.9899 0.5849 0.6710 -0.0954 0.1306  -0.0658 303 ASN A CB  
2217 C CG  . ASN A 297 ? 1.1300 0.7376 0.8251 -0.0918 0.1222  -0.0605 303 ASN A CG  
2218 O OD1 . ASN A 297 ? 1.1061 0.7158 0.7984 -0.0941 0.1136  -0.0531 303 ASN A OD1 
2219 N ND2 . ASN A 297 ? 1.2029 0.8198 0.9135 -0.0862 0.1244  -0.0639 303 ASN A ND2 
2220 N N   . ILE A 298 ? 0.9890 0.5598 0.6356 -0.1077 0.1414  -0.0707 304 ILE A N   
2221 C CA  . ILE A 298 ? 0.9959 0.5507 0.6255 -0.1119 0.1482  -0.0747 304 ILE A CA  
2222 C C   . ILE A 298 ? 1.0457 0.5843 0.6570 -0.1167 0.1417  -0.0701 304 ILE A C   
2223 O O   . ILE A 298 ? 1.0405 0.5599 0.6362 -0.1179 0.1429  -0.0717 304 ILE A O   
2224 C CB  . ILE A 298 ? 1.0483 0.6126 0.6814 -0.1152 0.1556  -0.0783 304 ILE A CB  
2225 C CG1 . ILE A 298 ? 1.0775 0.6575 0.7288 -0.1106 0.1626  -0.0831 304 ILE A CG1 
2226 C CG2 . ILE A 298 ? 1.0202 0.5679 0.6341 -0.1208 0.1615  -0.0812 304 ILE A CG2 
2227 C CD1 . ILE A 298 ? 1.1339 0.7065 0.7817 -0.1084 0.1720  -0.0897 304 ILE A CD1 
2228 N N   . ALA A 299 ? 1.0049 0.5511 0.6177 -0.1193 0.1344  -0.0648 305 ALA A N   
2229 C CA  . ALA A 299 ? 0.9957 0.5277 0.5916 -0.1243 0.1286  -0.0609 305 ALA A CA  
2230 C C   . ALA A 299 ? 1.0363 0.5563 0.6259 -0.1230 0.1215  -0.0566 305 ALA A C   
2231 O O   . ALA A 299 ? 1.0660 0.5665 0.6383 -0.1262 0.1201  -0.0561 305 ALA A O   
2232 C CB  . ALA A 299 ? 0.9412 0.4861 0.5413 -0.1267 0.1224  -0.0568 305 ALA A CB  
2233 N N   . VAL A 300 ? 1.0123 0.5430 0.6154 -0.1186 0.1164  -0.0531 306 VAL A N   
2234 C CA  . VAL A 300 ? 0.9739 0.4933 0.5719 -0.1178 0.1085  -0.0482 306 VAL A CA  
2235 C C   . VAL A 300 ? 1.0446 0.5450 0.6334 -0.1155 0.1130  -0.0534 306 VAL A C   
2236 O O   . VAL A 300 ? 1.0532 0.5345 0.6274 -0.1173 0.1087  -0.0516 306 VAL A O   
2237 C CB  . VAL A 300 ? 0.9576 0.4935 0.5726 -0.1140 0.1018  -0.0430 306 VAL A CB  
2238 C CG1 . VAL A 300 ? 0.9339 0.4575 0.5436 -0.1140 0.0927  -0.0372 306 VAL A CG1 
2239 C CG2 . VAL A 300 ? 0.8897 0.4447 0.5126 -0.1159 0.0974  -0.0382 306 VAL A CG2 
2240 N N   . ALA A 301 ? 1.0226 0.5284 0.6197 -0.1113 0.1214  -0.0602 307 ALA A N   
2241 C CA  . ALA A 301 ? 1.0276 0.5173 0.6163 -0.1083 0.1265  -0.0664 307 ALA A CA  
2242 C C   . ALA A 301 ? 1.1510 0.6214 0.7181 -0.1132 0.1301  -0.0688 307 ALA A C   
2243 O O   . ALA A 301 ? 1.1156 0.5663 0.6691 -0.1126 0.1279  -0.0697 307 ALA A O   
2244 C CB  . ALA A 301 ? 1.0196 0.5216 0.6214 -0.1036 0.1362  -0.0738 307 ALA A CB  
2245 N N   . ASN A 302 ? 1.1293 0.6045 0.6927 -0.1182 0.1350  -0.0697 308 ASN A N   
2246 C CA  . ASN A 302 ? 1.1387 0.5963 0.6817 -0.1233 0.1387  -0.0720 308 ASN A CA  
2247 C C   . ASN A 302 ? 1.1540 0.5967 0.6829 -0.1274 0.1291  -0.0659 308 ASN A C   
2248 O O   . ASN A 302 ? 1.2021 0.6256 0.7122 -0.1308 0.1305  -0.0676 308 ASN A O   
2249 C CB  . ASN A 302 ? 1.1246 0.5915 0.6684 -0.1278 0.1455  -0.0742 308 ASN A CB  
2250 C CG  . ASN A 302 ? 1.1808 0.6586 0.7344 -0.1250 0.1565  -0.0809 308 ASN A CG  
2251 O OD1 . ASN A 302 ? 1.2146 0.6911 0.7722 -0.1195 0.1601  -0.0850 308 ASN A OD1 
2252 N ND2 . ASN A 302 ? 1.1911 0.6798 0.7489 -0.1288 0.1616  -0.0822 308 ASN A ND2 
2253 N N   . ILE A 303 ? 1.1046 0.5562 0.6420 -0.1274 0.1194  -0.0588 309 ILE A N   
2254 C CA  . ILE A 303 ? 1.1207 0.5585 0.6460 -0.1308 0.1098  -0.0527 309 ILE A CA  
2255 C C   . ILE A 303 ? 1.2107 0.6319 0.7300 -0.1275 0.1058  -0.0525 309 ILE A C   
2256 O O   . ILE A 303 ? 1.2963 0.6963 0.7983 -0.1300 0.1030  -0.0522 309 ILE A O   
2257 C CB  . ILE A 303 ? 1.0786 0.5328 0.6147 -0.1322 0.1008  -0.0449 309 ILE A CB  
2258 C CG1 . ILE A 303 ? 1.0954 0.5632 0.6349 -0.1352 0.1034  -0.0456 309 ILE A CG1 
2259 C CG2 . ILE A 303 ? 1.0735 0.5144 0.5982 -0.1356 0.0909  -0.0384 309 ILE A CG2 
2260 C CD1 . ILE A 303 ? 0.9388 0.4236 0.4875 -0.1363 0.0944  -0.0386 309 ILE A CD1 
2261 N N   . VAL A 304 ? 1.1774 0.6070 0.7107 -0.1217 0.1051  -0.0531 310 VAL A N   
2262 C CA  . VAL A 304 ? 1.2052 0.6184 0.7333 -0.1179 0.1007  -0.0536 310 VAL A CA  
2263 C C   . VAL A 304 ? 1.2221 0.6184 0.7364 -0.1160 0.1091  -0.0624 310 VAL A C   
2264 O O   . VAL A 304 ? 1.2355 0.6102 0.7349 -0.1158 0.1052  -0.0629 310 VAL A O   
2265 C CB  . VAL A 304 ? 1.1627 0.5892 0.7095 -0.1120 0.0975  -0.0525 310 VAL A CB  
2266 C CG1 . VAL A 304 ? 1.1937 0.6014 0.7346 -0.1080 0.0914  -0.0531 310 VAL A CG1 
2267 C CG2 . VAL A 304 ? 1.1383 0.5822 0.6976 -0.1143 0.0894  -0.0436 310 VAL A CG2 
2268 N N   . ASN A 305 ? 1.1982 0.6047 0.7175 -0.1144 0.1207  -0.0694 311 ASN A N   
2269 C CA  . ASN A 305 ? 1.2653 0.6584 0.7716 -0.1128 0.1297  -0.0779 311 ASN A CA  
2270 C C   . ASN A 305 ? 1.3408 0.7150 0.8248 -0.1191 0.1299  -0.0773 311 ASN A C   
2271 O O   . ASN A 305 ? 1.4156 0.7706 0.8838 -0.1177 0.1318  -0.0817 311 ASN A O   
2272 C CB  . ASN A 305 ? 1.2801 0.6903 0.7968 -0.1113 0.1421  -0.0844 311 ASN A CB  
2273 C CG  . ASN A 305 ? 1.2578 0.6797 0.7919 -0.1033 0.1440  -0.0884 311 ASN A CG  
2274 O OD1 . ASN A 305 ? 1.2254 0.6379 0.7595 -0.0983 0.1375  -0.0884 311 ASN A OD1 
2275 N ND2 . ASN A 305 ? 1.2632 0.7050 0.8121 -0.1021 0.1523  -0.0919 311 ASN A ND2 
2276 N N   . SER A 306 ? 1.3024 0.6812 0.7844 -0.1255 0.1274  -0.0723 312 SER A N   
2277 C CA  . SER A 306 ? 1.3299 0.6916 0.7918 -0.1313 0.1262  -0.0712 312 SER A CA  
2278 C C   . SER A 306 ? 1.3609 0.7114 0.8158 -0.1298 0.1148  -0.0651 312 SER A C   
2279 O O   . SER A 306 ? 1.4645 0.8073 0.9070 -0.1304 0.1137  -0.0641 312 SER A O   
2280 C CB  . SER A 306 ? 1.3299 0.7035 0.7946 -0.1373 0.1245  -0.0666 312 SER A CB  
2281 O OG  . SER A 306 ? 1.4690 0.8428 0.9325 -0.1392 0.1127  -0.0582 312 SER A OG  
2282 N N   . VAL A 307 ? 1.3711 0.7202 0.8336 -0.1281 0.1060  -0.0609 313 VAL A N   
2283 C CA  . VAL A 307 ? 1.4082 0.7466 0.8647 -0.1267 0.0948  -0.0553 313 VAL A CA  
2284 C C   . VAL A 307 ? 1.4019 0.7263 0.8533 -0.1203 0.0962  -0.0612 313 VAL A C   
2285 O O   . VAL A 307 ? 1.4316 0.7454 0.8720 -0.1188 0.0925  -0.0606 313 VAL A O   
2286 C CB  . VAL A 307 ? 1.3112 0.6542 0.7775 -0.1285 0.0837  -0.0470 313 VAL A CB  
2287 N N   . LYS A 308 ? 1.4150 0.7393 0.8745 -0.1159 0.1012  -0.0675 314 LYS A N   
2288 C CA  . LYS A 308 ? 1.3206 0.6332 0.7770 -0.1086 0.1031  -0.0748 314 LYS A CA  
2289 C C   . LYS A 308 ? 1.4588 0.7696 0.9055 -0.1065 0.1153  -0.0836 314 LYS A C   
2290 O O   . LYS A 308 ? 1.4380 0.7428 0.8838 -0.0998 0.1196  -0.0918 314 LYS A O   
2291 C CB  . LYS A 308 ? 1.2861 0.6160 0.7637 -0.1024 0.1035  -0.0763 314 LYS A CB  
2292 C CG  . LYS A 308 ? 1.2231 0.5564 0.7121 -0.1020 0.0901  -0.0675 314 LYS A CG  
2293 C CD  . LYS A 308 ? 1.2257 0.5742 0.7343 -0.0949 0.0911  -0.0704 314 LYS A CD  
2294 C CE  . LYS A 308 ? 1.2441 0.5993 0.7655 -0.0954 0.0784  -0.0609 314 LYS A CE  
2295 N NZ  . LYS A 308 ? 1.2521 0.6243 0.7935 -0.0893 0.0794  -0.0632 314 LYS A NZ  
2296 N N   . GLN A 309 ? 1.5070 0.8234 0.9470 -0.1121 0.1207  -0.0822 315 GLN A N   
2297 C CA  . GLN A 309 ? 1.5321 0.8483 0.9628 -0.1120 0.1326  -0.0891 315 GLN A CA  
2298 C C   . GLN A 309 ? 1.4928 0.8133 0.9299 -0.1064 0.1437  -0.0997 315 GLN A C   
2299 O O   . GLN A 309 ? 1.5638 0.8760 0.9967 -0.0997 0.1452  -0.1060 315 GLN A O   
2300 C CB  . GLN A 309 ? 1.5258 0.8276 0.9409 -0.1102 0.1288  -0.0884 315 GLN A CB  
2301 C CG  . GLN A 309 ? 1.5283 0.8300 0.9328 -0.1170 0.1274  -0.0822 315 GLN A CG  
2302 C CD  . GLN A 309 ? 1.6203 0.9299 1.0312 -0.1222 0.1183  -0.0729 315 GLN A CD  
2303 O OE1 . GLN A 309 ? 1.6491 0.9601 1.0693 -0.1208 0.1097  -0.0691 315 GLN A OE1 
2304 N NE2 . GLN A 309 ? 1.6704 0.9855 1.0763 -0.1281 0.1198  -0.0693 315 GLN A NE2 
2305 N N   . ARG A 310 ? 1.4478 0.7851 0.8973 -0.1086 0.1507  -0.1012 316 ARG A N   
2306 C CA  . ARG A 310 ? 1.4367 0.7917 0.9017 -0.1026 0.1598  -0.1079 316 ARG A CA  
2307 C C   . ARG A 310 ? 1.4759 0.8478 0.9460 -0.1081 0.1702  -0.1086 316 ARG A C   
2308 O O   . ARG A 310 ? 1.4197 0.7924 0.8863 -0.1155 0.1675  -0.1028 316 ARG A O   
2309 C CB  . ARG A 310 ? 1.4063 0.7749 0.8932 -0.0972 0.1526  -0.1048 316 ARG A CB  
2310 C CG  . ARG A 310 ? 1.3638 0.7290 0.8558 -0.0874 0.1521  -0.1114 316 ARG A CG  
2311 C CD  . ARG A 310 ? 1.3107 0.6843 0.8211 -0.0834 0.1416  -0.1065 316 ARG A CD  
2312 N N   . PRO A 311 ? 1.4847 0.8702 0.9630 -0.1048 0.1815  -0.1158 317 PRO A N   
2313 C CA  . PRO A 311 ? 1.4673 0.8695 0.9518 -0.1104 0.1907  -0.1160 317 PRO A CA  
2314 C C   . PRO A 311 ? 1.3679 0.7886 0.8725 -0.1117 0.1854  -0.1098 317 PRO A C   
2315 O O   . PRO A 311 ? 1.3625 0.7946 0.8848 -0.1056 0.1819  -0.1097 317 PRO A O   
2316 C CB  . PRO A 311 ? 1.4593 0.8732 0.9508 -0.1051 0.2029  -0.1250 317 PRO A CB  
2317 C CG  . PRO A 311 ? 1.3491 0.7486 0.8328 -0.0971 0.2008  -0.1305 317 PRO A CG  
2318 C CD  . PRO A 311 ? 1.3983 0.7852 0.8813 -0.0956 0.1862  -0.1241 317 PRO A CD  
2319 N N   . LEU A 312 ? 1.3392 0.7624 0.8406 -0.1196 0.1841  -0.1048 318 LEU A N   
2320 C CA  . LEU A 312 ? 1.3085 0.7508 0.8284 -0.1208 0.1801  -0.0998 318 LEU A CA  
2321 C C   . LEU A 312 ? 1.3024 0.7665 0.8413 -0.1175 0.1889  -0.1044 318 LEU A C   
2322 O O   . LEU A 312 ? 1.3552 0.8209 0.8910 -0.1171 0.1996  -0.1107 318 LEU A O   
2323 C CB  . LEU A 312 ? 1.2712 0.7120 0.7834 -0.1293 0.1777  -0.0950 318 LEU A CB  
2324 C CG  . LEU A 312 ? 1.2915 0.7103 0.7827 -0.1341 0.1705  -0.0911 318 LEU A CG  
2325 C CD1 . LEU A 312 ? 1.2599 0.6823 0.7494 -0.1410 0.1663  -0.0863 318 LEU A CD1 
2326 C CD2 . LEU A 312 ? 1.3215 0.7310 0.8120 -0.1301 0.1600  -0.0873 318 LEU A CD2 
2327 N N   . GLN A 313 ? 1.3178 0.7993 0.8766 -0.1151 0.1845  -0.1012 319 GLN A N   
2328 C CA  . GLN A 313 ? 1.3157 0.8187 0.8939 -0.1125 0.1917  -0.1047 319 GLN A CA  
2329 C C   . GLN A 313 ? 1.2856 0.8006 0.8690 -0.1190 0.1926  -0.1015 319 GLN A C   
2330 O O   . GLN A 313 ? 1.2410 0.7511 0.8179 -0.1236 0.1852  -0.0959 319 GLN A O   
2331 C CB  . GLN A 313 ? 1.2769 0.7919 0.8748 -0.1048 0.1866  -0.1042 319 GLN A CB  
2332 C CG  . GLN A 313 ? 1.2642 0.7805 0.8669 -0.1051 0.1742  -0.0963 319 GLN A CG  
2333 C CD  . GLN A 313 ? 1.3101 0.8311 0.9264 -0.0974 0.1683  -0.0959 319 GLN A CD  
2334 O OE1 . GLN A 313 ? 1.2341 0.7706 0.8669 -0.0956 0.1635  -0.0923 319 GLN A OE1 
2335 N NE2 . GLN A 313 ? 1.3613 0.8685 0.9704 -0.0928 0.1681  -0.0997 319 GLN A NE2 
2336 N N   . ALA A 314 ? 1.2812 0.8119 0.8766 -0.1191 0.2013  -0.1054 320 ALA A N   
2337 C CA  . ALA A 314 ? 1.3032 0.8435 0.9018 -0.1256 0.2033  -0.1034 320 ALA A CA  
2338 C C   . ALA A 314 ? 1.2393 0.8017 0.8619 -0.1223 0.2010  -0.1022 320 ALA A C   
2339 O O   . ALA A 314 ? 1.2262 0.7976 0.8634 -0.1151 0.2004  -0.1039 320 ALA A O   
2340 C CB  . ALA A 314 ? 1.3296 0.8697 0.9210 -0.1303 0.2151  -0.1080 320 ALA A CB  
2341 N N   . TYR A 315 ? 1.2496 0.8198 0.8758 -0.1276 0.1993  -0.0994 321 TYR A N   
2342 C CA  . TYR A 315 ? 1.2459 0.8366 0.8934 -0.1254 0.1969  -0.0982 321 TYR A CA  
2343 C C   . TYR A 315 ? 1.2782 0.8804 0.9335 -0.1287 0.2064  -0.1018 321 TYR A C   
2344 O O   . TYR A 315 ? 1.3129 0.9096 0.9574 -0.1363 0.2088  -0.1011 321 TYR A O   
2345 C CB  . TYR A 315 ? 1.2478 0.8394 0.8941 -0.1283 0.1865  -0.0925 321 TYR A CB  
2346 C CG  . TYR A 315 ? 1.3085 0.9191 0.9724 -0.1283 0.1847  -0.0918 321 TYR A CG  
2347 C CD1 . TYR A 315 ? 1.2962 0.9241 0.9811 -0.1218 0.1847  -0.0928 321 TYR A CD1 
2348 C CD2 . TYR A 315 ? 1.3133 0.9239 0.9725 -0.1346 0.1822  -0.0901 321 TYR A CD2 
2349 C CE1 . TYR A 315 ? 1.2871 0.9319 0.9879 -0.1215 0.1826  -0.0923 321 TYR A CE1 
2350 C CE2 . TYR A 315 ? 1.3250 0.9522 1.0002 -0.1342 0.1796  -0.0896 321 TYR A CE2 
2351 C CZ  . TYR A 315 ? 1.3188 0.9632 1.0147 -0.1276 0.1800  -0.0907 321 TYR A CZ  
2352 O OH  . TYR A 315 ? 1.3397 1.0001 1.0512 -0.1270 0.1770  -0.0904 321 TYR A OH  
2353 N N   . LYS A 316 ? 1.2617 0.8796 0.9357 -0.1233 0.2113  -0.1053 322 LYS A N   
2354 C CA  . LYS A 316 ? 1.2588 0.8895 0.9424 -0.1258 0.2210  -0.1089 322 LYS A CA  
2355 C C   . LYS A 316 ? 1.2810 0.9307 0.9854 -0.1250 0.2176  -0.1073 322 LYS A C   
2356 O O   . LYS A 316 ? 1.2656 0.9292 0.9887 -0.1183 0.2180  -0.1094 322 LYS A O   
2357 C CB  . LYS A 316 ? 1.2075 0.8423 0.8967 -0.1202 0.2303  -0.1152 322 LYS A CB  
2358 N N   . PRO A 317 ? 1.3030 0.9538 1.0052 -0.1315 0.2138  -0.1040 323 PRO A N   
2359 C CA  . PRO A 317 ? 1.2464 0.9146 0.9679 -0.1302 0.2095  -0.1026 323 PRO A CA  
2360 C C   . PRO A 317 ? 1.2508 0.9357 0.9906 -0.1285 0.2182  -0.1067 323 PRO A C   
2361 O O   . PRO A 317 ? 1.2459 0.9302 0.9815 -0.1322 0.2282  -0.1097 323 PRO A O   
2362 C CB  . PRO A 317 ? 1.2457 0.9085 0.9576 -0.1386 0.2053  -0.0994 323 PRO A CB  
2363 C CG  . PRO A 317 ? 1.3266 0.9685 1.0142 -0.1430 0.2047  -0.0982 323 PRO A CG  
2364 C CD  . PRO A 317 ? 1.3217 0.9576 1.0036 -0.1402 0.2135  -0.1019 323 PRO A CD  
2365 N N   . GLY A 318 ? 1.2414 0.9422 1.0019 -0.1228 0.2141  -0.1066 324 GLY A N   
2366 C CA  . GLY A 318 ? 1.1171 0.8354 0.8975 -0.1210 0.2205  -0.1099 324 GLY A CA  
2367 C C   . GLY A 318 ? 1.0977 0.8280 0.8908 -0.1239 0.2156  -0.1076 324 GLY A C   
2368 O O   . GLY A 318 ? 1.0498 0.7738 0.8339 -0.1289 0.2087  -0.1040 324 GLY A O   
2369 N N   . ALA A 319 ? 1.0557 0.8034 0.8701 -0.1205 0.2187  -0.1101 325 ALA A N   
2370 C CA  . ALA A 319 ? 1.0231 0.7827 0.8512 -0.1227 0.2140  -0.1083 325 ALA A CA  
2371 C C   . ALA A 319 ? 1.0336 0.7950 0.8657 -0.1177 0.2013  -0.1051 325 ALA A C   
2372 O O   . ALA A 319 ? 0.9947 0.7513 0.8230 -0.1120 0.1971  -0.1044 325 ALA A O   
2373 C CB  . ALA A 319 ? 1.0181 0.7961 0.8688 -0.1199 0.2204  -0.1117 325 ALA A CB  
2374 N N   . LEU A 320 ? 1.0108 0.7797 0.8511 -0.1200 0.1951  -0.1033 326 LEU A N   
2375 C CA  . LEU A 320 ? 0.9947 0.7646 0.8355 -0.1166 0.1828  -0.1004 326 LEU A CA  
2376 C C   . LEU A 320 ? 0.9138 0.6964 0.7716 -0.1071 0.1789  -0.1010 326 LEU A C   
2377 O O   . LEU A 320 ? 0.9010 0.6975 0.7778 -0.1044 0.1812  -0.1031 326 LEU A O   
2378 C CB  . LEU A 320 ? 0.9953 0.7690 0.8396 -0.1215 0.1772  -0.0990 326 LEU A CB  
2379 C CG  . LEU A 320 ? 1.0021 0.7739 0.8415 -0.1196 0.1644  -0.0963 326 LEU A CG  
2380 C CD1 . LEU A 320 ? 0.9754 0.7625 0.8326 -0.1112 0.1576  -0.0965 326 LEU A CD1 
2381 C CD2 . LEU A 320 ? 1.0356 0.7939 0.8565 -0.1190 0.1623  -0.0946 326 LEU A CD2 
2382 N N   . THR A 321 ? 0.9015 0.6797 0.7528 -0.1025 0.1724  -0.0988 327 THR A N   
2383 C CA  . THR A 321 ? 0.8964 0.6862 0.7619 -0.0943 0.1662  -0.0981 327 THR A CA  
2384 C C   . THR A 321 ? 0.8405 0.6324 0.7026 -0.0930 0.1546  -0.0946 327 THR A C   
2385 O O   . THR A 321 ? 0.7972 0.5786 0.6429 -0.0950 0.1506  -0.0921 327 THR A O   
2386 C CB  . THR A 321 ? 0.8332 0.6182 0.6960 -0.0893 0.1679  -0.0981 327 THR A CB  
2387 O OG1 . THR A 321 ? 0.9325 0.7185 0.8016 -0.0888 0.1781  -0.1024 327 THR A OG1 
2388 C CG2 . THR A 321 ? 0.8067 0.6029 0.6826 -0.0817 0.1603  -0.0964 327 THR A CG2 
2389 N N   . PHE A 322 ? 0.8517 0.6577 0.7294 -0.0895 0.1492  -0.0949 328 PHE A N   
2390 C CA  . PHE A 322 ? 0.8315 0.6428 0.7084 -0.0864 0.1380  -0.0924 328 PHE A CA  
2391 C C   . PHE A 322 ? 0.7681 0.5962 0.6655 -0.0803 0.1340  -0.0934 328 PHE A C   
2392 O O   . PHE A 322 ? 0.7466 0.5810 0.6561 -0.0818 0.1369  -0.0959 328 PHE A O   
2393 C CB  . PHE A 322 ? 0.8551 0.6601 0.7209 -0.0919 0.1333  -0.0919 328 PHE A CB  
2394 C CG  . PHE A 322 ? 0.8869 0.6985 0.7520 -0.0879 0.1216  -0.0901 328 PHE A CG  
2395 C CD1 . PHE A 322 ? 0.9135 0.7279 0.7751 -0.0828 0.1168  -0.0873 328 PHE A CD1 
2396 C CD2 . PHE A 322 ? 0.9259 0.7415 0.7940 -0.0889 0.1151  -0.0912 328 PHE A CD2 
2397 C CE1 . PHE A 322 ? 0.8347 0.6575 0.6958 -0.0787 0.1064  -0.0858 328 PHE A CE1 
2398 C CE2 . PHE A 322 ? 0.8890 0.7117 0.7565 -0.0842 0.1041  -0.0904 328 PHE A CE2 
2399 C CZ  . PHE A 322 ? 0.8808 0.7079 0.7448 -0.0790 0.1002  -0.0878 328 PHE A CZ  
2400 N N   . LEU A 323 ? 0.7487 0.5842 0.6499 -0.0739 0.1274  -0.0912 329 LEU A N   
2401 C CA  . LEU A 323 ? 0.7011 0.5522 0.6204 -0.0674 0.1225  -0.0918 329 LEU A CA  
2402 C C   . LEU A 323 ? 0.6864 0.5443 0.6034 -0.0648 0.1116  -0.0900 329 LEU A C   
2403 O O   . LEU A 323 ? 0.6989 0.5533 0.6030 -0.0644 0.1069  -0.0871 329 LEU A O   
2404 C CB  . LEU A 323 ? 0.6811 0.5359 0.6066 -0.0618 0.1231  -0.0904 329 LEU A CB  
2405 C CG  . LEU A 323 ? 0.6618 0.5083 0.5867 -0.0636 0.1330  -0.0925 329 LEU A CG  
2406 C CD1 . LEU A 323 ? 0.6723 0.5173 0.5966 -0.0590 0.1314  -0.0902 329 LEU A CD1 
2407 C CD2 . LEU A 323 ? 0.6899 0.5444 0.6324 -0.0628 0.1387  -0.0967 329 LEU A CD2 
2408 N N   . LEU A 324 ? 0.6740 0.5419 0.6033 -0.0628 0.1073  -0.0921 330 LEU A N   
2409 C CA  . LEU A 324 ? 0.6847 0.5608 0.6136 -0.0589 0.0964  -0.0914 330 LEU A CA  
2410 C C   . LEU A 324 ? 0.7037 0.5944 0.6458 -0.0510 0.0916  -0.0904 330 LEU A C   
2411 O O   . LEU A 324 ? 0.7026 0.6002 0.6608 -0.0486 0.0940  -0.0923 330 LEU A O   
2412 C CB  . LEU A 324 ? 0.6746 0.5519 0.6078 -0.0613 0.0928  -0.0942 330 LEU A CB  
2413 C CG  . LEU A 324 ? 0.7715 0.6346 0.6886 -0.0689 0.0940  -0.0943 330 LEU A CG  
2414 C CD1 . LEU A 324 ? 0.8126 0.6743 0.7364 -0.0735 0.0944  -0.0967 330 LEU A CD1 
2415 C CD2 . LEU A 324 ? 0.7854 0.6473 0.6892 -0.0671 0.0846  -0.0931 330 LEU A CD2 
2416 N N   . SER A 325 ? 0.7359 0.6314 0.6708 -0.0472 0.0847  -0.0874 331 SER A N   
2417 C CA  . SER A 325 ? 0.7041 0.6142 0.6488 -0.0398 0.0784  -0.0859 331 SER A CA  
2418 C C   . SER A 325 ? 0.7254 0.6463 0.6775 -0.0358 0.0701  -0.0885 331 SER A C   
2419 O O   . SER A 325 ? 0.7917 0.7118 0.7341 -0.0363 0.0643  -0.0891 331 SER A O   
2420 C CB  . SER A 325 ? 0.6933 0.6047 0.6259 -0.0384 0.0745  -0.0811 331 SER A CB  
2421 O OG  . SER A 325 ? 0.7513 0.6761 0.6922 -0.0322 0.0695  -0.0786 331 SER A OG  
2422 N N   . MET A 326 ? 0.6893 0.6198 0.6584 -0.0315 0.0687  -0.0903 332 MET A N   
2423 C CA  . MET A 326 ? 0.6521 0.5933 0.6289 -0.0267 0.0598  -0.0928 332 MET A CA  
2424 C C   . MET A 326 ? 0.6777 0.6335 0.6594 -0.0189 0.0529  -0.0906 332 MET A C   
2425 O O   . MET A 326 ? 0.6462 0.6110 0.6428 -0.0143 0.0509  -0.0917 332 MET A O   
2426 C CB  . MET A 326 ? 0.7097 0.6514 0.7024 -0.0279 0.0623  -0.0964 332 MET A CB  
2427 C CG  . MET A 326 ? 0.7465 0.6757 0.7352 -0.0361 0.0683  -0.0984 332 MET A CG  
2428 S SD  . MET A 326 ? 0.8557 0.7786 0.8297 -0.0389 0.0603  -0.0997 332 MET A SD  
2429 C CE  . MET A 326 ? 0.7421 0.6513 0.6956 -0.0447 0.0669  -0.0966 332 MET A CE  
2430 N N   . GLY A 327 ? 0.7040 0.6625 0.6729 -0.0176 0.0491  -0.0873 333 GLY A N   
2431 C CA  . GLY A 327 ? 0.6307 0.6025 0.6025 -0.0115 0.0441  -0.0840 333 GLY A CA  
2432 C C   . GLY A 327 ? 0.6578 0.6258 0.6328 -0.0131 0.0504  -0.0803 333 GLY A C   
2433 O O   . GLY A 327 ? 0.6486 0.6037 0.6210 -0.0184 0.0584  -0.0804 333 GLY A O   
2434 N N   . ARG A 328 ? 0.6094 0.5886 0.5899 -0.0081 0.0461  -0.0771 334 ARG A N   
2435 C CA  . ARG A 328 ? 0.5898 0.5649 0.5729 -0.0092 0.0504  -0.0733 334 ARG A CA  
2436 C C   . ARG A 328 ? 0.6254 0.5990 0.6256 -0.0078 0.0544  -0.0765 334 ARG A C   
2437 O O   . ARG A 328 ? 0.5955 0.5621 0.5982 -0.0094 0.0594  -0.0751 334 ARG A O   
2438 C CB  . ARG A 328 ? 0.5798 0.5665 0.5598 -0.0056 0.0438  -0.0674 334 ARG A CB  
2439 C CG  . ARG A 328 ? 0.5584 0.5597 0.5513 0.0012  0.0374  -0.0680 334 ARG A CG  
2440 C CD  . ARG A 328 ? 0.5251 0.5382 0.5140 0.0040  0.0312  -0.0615 334 ARG A CD  
2441 N NE  . ARG A 328 ? 0.5886 0.6098 0.5638 0.0042  0.0266  -0.0592 334 ARG A NE  
2442 C CZ  . ARG A 328 ? 0.6248 0.6431 0.5869 0.0001  0.0275  -0.0539 334 ARG A CZ  
2443 N NH1 . ARG A 328 ? 0.6269 0.6330 0.5866 -0.0046 0.0324  -0.0503 334 ARG A NH1 
2444 N NH2 . ARG A 328 ? 0.6048 0.6329 0.5561 0.0011  0.0229  -0.0524 334 ARG A NH2 
2445 N N   . ASN A 329 ? 0.6006 0.5805 0.6130 -0.0048 0.0521  -0.0809 335 ASN A N   
2446 C CA  . ASN A 329 ? 0.5381 0.5189 0.5682 -0.0029 0.0551  -0.0839 335 ASN A CA  
2447 C C   . ASN A 329 ? 0.5663 0.5390 0.6022 -0.0072 0.0622  -0.0889 335 ASN A C   
2448 O O   . ASN A 329 ? 0.6105 0.5857 0.6624 -0.0057 0.0645  -0.0919 335 ASN A O   
2449 C CB  . ASN A 329 ? 0.5437 0.5386 0.5858 0.0040  0.0468  -0.0848 335 ASN A CB  
2450 C CG  . ASN A 329 ? 0.5557 0.5560 0.5966 0.0057  0.0410  -0.0880 335 ASN A CG  
2451 O OD1 . ASN A 329 ? 0.5567 0.5509 0.5861 0.0018  0.0420  -0.0889 335 ASN A OD1 
2452 N ND2 . ASN A 329 ? 0.5242 0.5354 0.5770 0.0116  0.0342  -0.0900 335 ASN A ND2 
2453 N N   . ASP A 330 ? 0.6076 0.5711 0.6311 -0.0129 0.0657  -0.0895 336 ASP A N   
2454 C CA  . ASP A 330 ? 0.6187 0.5759 0.6473 -0.0175 0.0715  -0.0937 336 ASP A CA  
2455 C C   . ASP A 330 ? 0.6571 0.6008 0.6695 -0.0246 0.0777  -0.0931 336 ASP A C   
2456 O O   . ASP A 330 ? 0.6488 0.5884 0.6458 -0.0257 0.0759  -0.0899 336 ASP A O   
2457 C CB  . ASP A 330 ? 0.6563 0.6203 0.6909 -0.0156 0.0645  -0.0966 336 ASP A CB  
2458 C CG  . ASP A 330 ? 0.7526 0.7175 0.8042 -0.0172 0.0683  -0.1005 336 ASP A CG  
2459 O OD1 . ASP A 330 ? 0.6622 0.6202 0.7164 -0.0220 0.0779  -0.1016 336 ASP A OD1 
2460 O OD2 . ASP A 330 ? 0.7519 0.7251 0.8140 -0.0135 0.0612  -0.1026 336 ASP A OD2 
2461 N N   . GLY A 331 ? 0.6594 0.5963 0.6753 -0.0298 0.0848  -0.0961 337 GLY A N   
2462 C CA  . GLY A 331 ? 0.6776 0.6015 0.6783 -0.0370 0.0903  -0.0959 337 GLY A CA  
2463 C C   . GLY A 331 ? 0.6579 0.5773 0.6660 -0.0422 0.0991  -0.0991 337 GLY A C   
2464 O O   . GLY A 331 ? 0.6743 0.6014 0.6999 -0.0402 0.1005  -0.1015 337 GLY A O   
2465 N N   . VAL A 332 ? 0.6581 0.5653 0.6525 -0.0492 0.1048  -0.0989 338 VAL A N   
2466 C CA  . VAL A 332 ? 0.6533 0.5555 0.6514 -0.0552 0.1145  -0.1013 338 VAL A CA  
2467 C C   . VAL A 332 ? 0.6618 0.5493 0.6401 -0.0619 0.1197  -0.1001 338 VAL A C   
2468 O O   . VAL A 332 ? 0.6961 0.5779 0.6593 -0.0620 0.1145  -0.0977 338 VAL A O   
2469 C CB  . VAL A 332 ? 0.6697 0.5771 0.6784 -0.0577 0.1117  -0.1033 338 VAL A CB  
2470 C CG1 . VAL A 332 ? 0.6939 0.5955 0.6893 -0.0608 0.1041  -0.1022 338 VAL A CG1 
2471 C CG2 . VAL A 332 ? 0.7322 0.6380 0.7480 -0.0638 0.1221  -0.1054 338 VAL A CG2 
2472 N N   . GLY A 333 ? 0.7192 0.6009 0.6972 -0.0672 0.1300  -0.1018 339 GLY A N   
2473 C CA  . GLY A 333 ? 0.7292 0.5964 0.6881 -0.0738 0.1352  -0.1009 339 GLY A CA  
2474 C C   . GLY A 333 ? 0.7322 0.5961 0.6935 -0.0775 0.1474  -0.1033 339 GLY A C   
2475 O O   . GLY A 333 ? 0.7360 0.6095 0.7143 -0.0762 0.1519  -0.1058 339 GLY A O   
2476 N N   . GLN A 334 ? 0.7595 0.6101 0.7033 -0.0820 0.1527  -0.1025 340 GLN A N   
2477 C CA  . GLN A 334 ? 0.8269 0.6735 0.7698 -0.0857 0.1645  -0.1050 340 GLN A CA  
2478 C C   . GLN A 334 ? 0.8362 0.6717 0.7653 -0.0842 0.1679  -0.1046 340 GLN A C   
2479 O O   . GLN A 334 ? 0.8451 0.6708 0.7582 -0.0851 0.1628  -0.1017 340 GLN A O   
2480 C CB  . GLN A 334 ? 0.8141 0.6544 0.7485 -0.0952 0.1688  -0.1049 340 GLN A CB  
2481 C CG  . GLN A 334 ? 0.8041 0.6312 0.7181 -0.0994 0.1632  -0.1020 340 GLN A CG  
2482 C CD  . GLN A 334 ? 0.8712 0.6915 0.7769 -0.1090 0.1659  -0.1015 340 GLN A CD  
2483 O OE1 . GLN A 334 ? 0.9036 0.7257 0.8113 -0.1116 0.1586  -0.1004 340 GLN A OE1 
2484 N NE2 . GLN A 334 ? 0.8741 0.6862 0.7699 -0.1144 0.1761  -0.1024 340 GLN A NE2 
2485 N N   . ILE A 335 ? 0.8741 0.7115 0.8101 -0.0815 0.1759  -0.1078 341 ILE A N   
2486 C CA  . ILE A 335 ? 0.8836 0.7100 0.8076 -0.0798 0.1797  -0.1082 341 ILE A CA  
2487 C C   . ILE A 335 ? 0.8745 0.6956 0.7926 -0.0850 0.1914  -0.1115 341 ILE A C   
2488 O O   . ILE A 335 ? 0.9657 0.7968 0.8982 -0.0841 0.1985  -0.1154 341 ILE A O   
2489 C CB  . ILE A 335 ? 0.8642 0.6969 0.8009 -0.0712 0.1781  -0.1097 341 ILE A CB  
2490 C CG1 . ILE A 335 ? 0.8056 0.6412 0.7434 -0.0666 0.1664  -0.1054 341 ILE A CG1 
2491 C CG2 . ILE A 335 ? 0.9131 0.7344 0.8396 -0.0698 0.1836  -0.1116 341 ILE A CG2 
2492 C CD1 . ILE A 335 ? 0.8194 0.6640 0.7733 -0.0586 0.1635  -0.1065 341 ILE A CD1 
2493 N N   . SER A 336 ? 0.8875 0.6937 0.7847 -0.0904 0.1934  -0.1101 342 SER A N   
2494 C CA  . SER A 336 ? 0.9508 0.7510 0.8394 -0.0961 0.2044  -0.1128 342 SER A CA  
2495 C C   . SER A 336 ? 0.8829 0.6944 0.7831 -0.1013 0.2093  -0.1140 342 SER A C   
2496 O O   . SER A 336 ? 0.9269 0.7470 0.8375 -0.1010 0.2185  -0.1179 342 SER A O   
2497 C CB  . SER A 336 ? 0.9314 0.7303 0.8218 -0.0910 0.2118  -0.1172 342 SER A CB  
2498 O OG  . SER A 336 ? 0.9769 0.7645 0.8565 -0.0866 0.2063  -0.1156 342 SER A OG  
2499 N N   . GLY A 337 ? 0.8769 0.6890 0.7761 -0.1059 0.2025  -0.1107 343 GLY A N   
2500 C CA  . GLY A 337 ? 0.8576 0.6756 0.7621 -0.1133 0.2059  -0.1105 343 GLY A CA  
2501 C C   . GLY A 337 ? 0.8212 0.6577 0.7505 -0.1107 0.2076  -0.1126 343 GLY A C   
2502 O O   . GLY A 337 ? 0.8229 0.6651 0.7577 -0.1174 0.2106  -0.1122 343 GLY A O   
2503 N N   . PHE A 338 ? 0.8408 0.6865 0.7851 -0.1017 0.2054  -0.1147 344 PHE A N   
2504 C CA  . PHE A 338 ? 0.8811 0.7440 0.8494 -0.0987 0.2048  -0.1163 344 PHE A CA  
2505 C C   . PHE A 338 ? 0.8563 0.7243 0.8338 -0.0917 0.1927  -0.1146 344 PHE A C   
2506 O O   . PHE A 338 ? 0.8046 0.6654 0.7728 -0.0873 0.1865  -0.1129 344 PHE A O   
2507 C CB  . PHE A 338 ? 0.8564 0.7291 0.8384 -0.0941 0.2144  -0.1214 344 PHE A CB  
2508 C CG  . PHE A 338 ? 0.8817 0.7487 0.8597 -0.0859 0.2140  -0.1234 344 PHE A CG  
2509 C CD1 . PHE A 338 ? 0.9042 0.7758 0.8927 -0.0776 0.2055  -0.1230 344 PHE A CD1 
2510 C CD2 . PHE A 338 ? 0.9094 0.7665 0.8734 -0.0866 0.2218  -0.1257 344 PHE A CD2 
2511 C CE1 . PHE A 338 ? 0.9476 0.8134 0.9326 -0.0707 0.2043  -0.1243 344 PHE A CE1 
2512 C CE2 . PHE A 338 ? 0.9336 0.7846 0.8941 -0.0792 0.2205  -0.1274 344 PHE A CE2 
2513 C CZ  . PHE A 338 ? 0.8939 0.7490 0.8651 -0.0715 0.2115  -0.1266 344 PHE A CZ  
2514 N N   . TYR A 339 ? 0.8103 0.6916 0.8067 -0.0908 0.1897  -0.1151 345 TYR A N   
2515 C CA  . TYR A 339 ? 0.7683 0.6557 0.7740 -0.0851 0.1780  -0.1135 345 TYR A CA  
2516 C C   . TYR A 339 ? 0.7920 0.6845 0.8070 -0.0753 0.1762  -0.1152 345 TYR A C   
2517 O O   . TYR A 339 ? 0.7703 0.6699 0.7980 -0.0721 0.1831  -0.1188 345 TYR A O   
2518 C CB  . TYR A 339 ? 0.7265 0.6261 0.7500 -0.0873 0.1758  -0.1138 345 TYR A CB  
2519 C CG  . TYR A 339 ? 0.7919 0.6993 0.8269 -0.0814 0.1638  -0.1128 345 TYR A CG  
2520 C CD1 . TYR A 339 ? 0.7429 0.6615 0.7959 -0.0731 0.1620  -0.1149 345 TYR A CD1 
2521 C CD2 . TYR A 339 ? 0.8187 0.7223 0.8469 -0.0840 0.1541  -0.1102 345 TYR A CD2 
2522 C CE1 . TYR A 339 ? 0.7295 0.6553 0.7924 -0.0677 0.1511  -0.1140 345 TYR A CE1 
2523 C CE2 . TYR A 339 ? 0.8339 0.7451 0.8722 -0.0782 0.1431  -0.1098 345 TYR A CE2 
2524 C CZ  . TYR A 339 ? 0.7514 0.6739 0.8069 -0.0701 0.1419  -0.1116 345 TYR A CZ  
2525 O OH  . TYR A 339 ? 0.8000 0.7300 0.8649 -0.0643 0.1308  -0.1112 345 TYR A OH  
2526 N N   . VAL A 340 ? 0.7623 0.6517 0.7714 -0.0707 0.1666  -0.1125 346 VAL A N   
2527 C CA  . VAL A 340 ? 0.7557 0.6510 0.7747 -0.0618 0.1622  -0.1130 346 VAL A CA  
2528 C C   . VAL A 340 ? 0.7209 0.6247 0.7486 -0.0580 0.1509  -0.1110 346 VAL A C   
2529 O O   . VAL A 340 ? 0.7452 0.6460 0.7640 -0.0611 0.1447  -0.1086 346 VAL A O   
2530 C CB  . VAL A 340 ? 0.7473 0.6312 0.7505 -0.0594 0.1614  -0.1112 346 VAL A CB  
2531 C CG1 . VAL A 340 ? 0.7937 0.6681 0.7871 -0.0632 0.1723  -0.1136 346 VAL A CG1 
2532 C CG2 . VAL A 340 ? 0.7562 0.6324 0.7426 -0.0616 0.1537  -0.1068 346 VAL A CG2 
2533 N N   . GLY A 341 ? 0.7000 0.6147 0.7455 -0.0511 0.1480  -0.1125 347 GLY A N   
2534 C CA  . GLY A 341 ? 0.6929 0.6179 0.7502 -0.0475 0.1386  -0.1116 347 GLY A CA  
2535 C C   . GLY A 341 ? 0.6640 0.5893 0.7155 -0.0417 0.1285  -0.1084 347 GLY A C   
2536 O O   . GLY A 341 ? 0.6858 0.6029 0.7225 -0.0414 0.1279  -0.1059 347 GLY A O   
2537 N N   . ARG A 342 ? 0.6707 0.6068 0.7349 -0.0369 0.1203  -0.1083 348 ARG A N   
2538 C CA  . ARG A 342 ? 0.6393 0.5781 0.6979 -0.0319 0.1099  -0.1050 348 ARG A CA  
2539 C C   . ARG A 342 ? 0.6265 0.5652 0.6852 -0.0267 0.1092  -0.1034 348 ARG A C   
2540 O O   . ARG A 342 ? 0.6403 0.5751 0.6854 -0.0259 0.1048  -0.0996 348 ARG A O   
2541 C CB  . ARG A 342 ? 0.6470 0.5974 0.7193 -0.0280 0.1015  -0.1059 348 ARG A CB  
2542 C CG  . ARG A 342 ? 0.6437 0.5940 0.7188 -0.0335 0.1020  -0.1078 348 ARG A CG  
2543 C CD  . ARG A 342 ? 0.6876 0.6492 0.7803 -0.0295 0.0949  -0.1095 348 ARG A CD  
2544 N NE  . ARG A 342 ? 0.6711 0.6360 0.7577 -0.0253 0.0832  -0.1079 348 ARG A NE  
2545 C CZ  . ARG A 342 ? 0.6526 0.6268 0.7513 -0.0208 0.0747  -0.1092 348 ARG A CZ  
2546 N NH1 . ARG A 342 ? 0.7499 0.7307 0.8680 -0.0200 0.0760  -0.1116 348 ARG A NH1 
2547 N NH2 . ARG A 342 ? 0.6684 0.6455 0.7593 -0.0167 0.0643  -0.1082 348 ARG A NH2 
2548 N N   . LEU A 343 ? 0.6187 0.5618 0.6930 -0.0233 0.1129  -0.1061 349 LEU A N   
2549 C CA  . LEU A 343 ? 0.5905 0.5321 0.6651 -0.0186 0.1113  -0.1046 349 LEU A CA  
2550 C C   . LEU A 343 ? 0.6543 0.5826 0.7105 -0.0221 0.1158  -0.1027 349 LEU A C   
2551 O O   . LEU A 343 ? 0.6389 0.5637 0.6852 -0.0204 0.1105  -0.0984 349 LEU A O   
2552 C CB  . LEU A 343 ? 0.5613 0.5083 0.6553 -0.0147 0.1153  -0.1089 349 LEU A CB  
2553 C CG  . LEU A 343 ? 0.6112 0.5593 0.7113 -0.0083 0.1109  -0.1079 349 LEU A CG  
2554 C CD1 . LEU A 343 ? 0.5339 0.4895 0.6558 -0.0042 0.1138  -0.1131 349 LEU A CD1 
2555 C CD2 . LEU A 343 ? 0.6912 0.6271 0.7777 -0.0094 0.1140  -0.1065 349 LEU A CD2 
2556 N N   . MET A 344 ? 0.6617 0.5828 0.7131 -0.0274 0.1252  -0.1055 350 MET A N   
2557 C CA  . MET A 344 ? 0.6329 0.5403 0.6668 -0.0308 0.1299  -0.1043 350 MET A CA  
2558 C C   . MET A 344 ? 0.6312 0.5327 0.6464 -0.0335 0.1241  -0.0992 350 MET A C   
2559 O O   . MET A 344 ? 0.6346 0.5285 0.6380 -0.0332 0.1220  -0.0958 350 MET A O   
2560 C CB  . MET A 344 ? 0.7782 0.6805 0.8100 -0.0363 0.1409  -0.1083 350 MET A CB  
2561 C CG  . MET A 344 ? 0.8615 0.7568 0.8923 -0.0352 0.1484  -0.1113 350 MET A CG  
2562 S SD  . MET A 344 ? 1.0474 0.9280 1.0573 -0.0352 0.1447  -0.1068 350 MET A SD  
2563 C CE  . MET A 344 ? 0.9238 0.7971 0.9141 -0.0432 0.1446  -0.1036 350 MET A CE  
2564 N N   . VAL A 345 ? 0.6277 0.5321 0.6395 -0.0365 0.1213  -0.0986 351 VAL A N   
2565 C CA  . VAL A 345 ? 0.6196 0.5186 0.6134 -0.0391 0.1161  -0.0945 351 VAL A CA  
2566 C C   . VAL A 345 ? 0.6609 0.5670 0.6545 -0.0338 0.1065  -0.0903 351 VAL A C   
2567 O O   . VAL A 345 ? 0.6390 0.5399 0.6179 -0.0349 0.1031  -0.0861 351 VAL A O   
2568 C CB  . VAL A 345 ? 0.6654 0.5656 0.6564 -0.0431 0.1145  -0.0956 351 VAL A CB  
2569 C CG1 . VAL A 345 ? 0.6380 0.5352 0.6125 -0.0441 0.1074  -0.0919 351 VAL A CG1 
2570 C CG2 . VAL A 345 ? 0.6817 0.5734 0.6691 -0.0498 0.1241  -0.0986 351 VAL A CG2 
2571 N N   . ARG A 346 ? 0.6457 0.5639 0.6555 -0.0282 0.1018  -0.0910 352 ARG A N   
2572 C CA  . ARG A 346 ? 0.5975 0.5236 0.6074 -0.0233 0.0927  -0.0867 352 ARG A CA  
2573 C C   . ARG A 346 ? 0.6105 0.5300 0.6146 -0.0226 0.0930  -0.0832 352 ARG A C   
2574 O O   . ARG A 346 ? 0.6611 0.5810 0.6545 -0.0224 0.0872  -0.0780 352 ARG A O   
2575 C CB  . ARG A 346 ? 0.6394 0.5788 0.6682 -0.0175 0.0881  -0.0886 352 ARG A CB  
2576 C CG  . ARG A 346 ? 0.5854 0.5340 0.6156 -0.0122 0.0789  -0.0842 352 ARG A CG  
2577 C CD  . ARG A 346 ? 0.5107 0.4719 0.5584 -0.0067 0.0740  -0.0865 352 ARG A CD  
2578 N NE  . ARG A 346 ? 0.6029 0.5633 0.6665 -0.0051 0.0791  -0.0902 352 ARG A NE  
2579 C CZ  . ARG A 346 ? 0.6101 0.5746 0.6883 -0.0047 0.0821  -0.0952 352 ARG A CZ  
2580 N NH1 . ARG A 346 ? 0.5813 0.5505 0.6610 -0.0056 0.0796  -0.0968 352 ARG A NH1 
2581 N NH2 . ARG A 346 ? 0.5899 0.5537 0.6817 -0.0033 0.0873  -0.0986 352 ARG A NH2 
2582 N N   . LEU A 347 ? 0.6215 0.5351 0.6324 -0.0222 0.0994  -0.0862 353 LEU A N   
2583 C CA  . LEU A 347 ? 0.6090 0.5146 0.6147 -0.0214 0.0989  -0.0833 353 LEU A CA  
2584 C C   . LEU A 347 ? 0.6620 0.5538 0.6482 -0.0267 0.1021  -0.0811 353 LEU A C   
2585 O O   . LEU A 347 ? 0.6967 0.5833 0.6737 -0.0269 0.0980  -0.0762 353 LEU A O   
2586 C CB  . LEU A 347 ? 0.6379 0.5413 0.6570 -0.0184 0.1040  -0.0880 353 LEU A CB  
2587 C CG  . LEU A 347 ? 0.7193 0.6345 0.7585 -0.0123 0.0999  -0.0899 353 LEU A CG  
2588 C CD1 . LEU A 347 ? 0.7266 0.6378 0.7770 -0.0095 0.1052  -0.0949 353 LEU A CD1 
2589 C CD2 . LEU A 347 ? 0.6285 0.5501 0.6675 -0.0088 0.0892  -0.0838 353 LEU A CD2 
2590 N N   . THR A 348 ? 0.6323 0.5180 0.6117 -0.0315 0.1089  -0.0842 354 THR A N   
2591 C CA  . THR A 348 ? 0.6250 0.4964 0.5858 -0.0365 0.1121  -0.0825 354 THR A CA  
2592 C C   . THR A 348 ? 0.6624 0.5346 0.6093 -0.0390 0.1058  -0.0775 354 THR A C   
2593 O O   . THR A 348 ? 0.7670 0.6331 0.7022 -0.0402 0.1024  -0.0727 354 THR A O   
2594 C CB  . THR A 348 ? 0.6861 0.5501 0.6445 -0.0409 0.1220  -0.0877 354 THR A CB  
2595 O OG1 . THR A 348 ? 0.6524 0.5184 0.6252 -0.0379 0.1278  -0.0927 354 THR A OG1 
2596 C CG2 . THR A 348 ? 0.6943 0.5423 0.6338 -0.0455 0.1256  -0.0864 354 THR A CG2 
2597 N N   . LYS A 349 ? 0.6510 0.5308 0.5991 -0.0397 0.1036  -0.0785 355 LYS A N   
2598 C CA  . LYS A 349 ? 0.6545 0.5354 0.5894 -0.0417 0.0978  -0.0749 355 LYS A CA  
2599 C C   . LYS A 349 ? 0.6627 0.5594 0.6035 -0.0368 0.0885  -0.0722 355 LYS A C   
2600 O O   . LYS A 349 ? 0.6387 0.5381 0.5700 -0.0367 0.0827  -0.0672 355 LYS A O   
2601 C CB  . LYS A 349 ? 0.6158 0.4917 0.5443 -0.0463 0.1012  -0.0783 355 LYS A CB  
2602 C CG  . LYS A 349 ? 0.6334 0.5065 0.5458 -0.0490 0.0963  -0.0754 355 LYS A CG  
2603 C CD  . LYS A 349 ? 0.6437 0.5107 0.5501 -0.0536 0.0986  -0.0788 355 LYS A CD  
2604 C CE  . LYS A 349 ? 0.6833 0.5515 0.5773 -0.0544 0.0915  -0.0767 355 LYS A CE  
2605 N NZ  . LYS A 349 ? 0.7796 0.6352 0.6617 -0.0606 0.0945  -0.0788 355 LYS A NZ  
2606 N N   . SER A 350 ? 0.6152 0.5232 0.5714 -0.0328 0.0866  -0.0751 356 SER A N   
2607 C CA  . SER A 350 ? 0.6645 0.5870 0.6240 -0.0287 0.0779  -0.0739 356 SER A CA  
2608 C C   . SER A 350 ? 0.6468 0.5788 0.6079 -0.0244 0.0712  -0.0685 356 SER A C   
2609 O O   . SER A 350 ? 0.6122 0.5546 0.5688 -0.0222 0.0641  -0.0658 356 SER A O   
2610 C CB  . SER A 350 ? 0.6753 0.6059 0.6506 -0.0258 0.0776  -0.0788 356 SER A CB  
2611 O OG  . SER A 350 ? 0.6301 0.5535 0.6027 -0.0303 0.0821  -0.0828 356 SER A OG  
2612 N N   . ARG A 351 ? 0.6774 0.6063 0.6445 -0.0233 0.0729  -0.0669 357 ARG A N   
2613 C CA  . ARG A 351 ? 0.6657 0.6029 0.6337 -0.0202 0.0659  -0.0610 357 ARG A CA  
2614 C C   . ARG A 351 ? 0.6971 0.6311 0.6483 -0.0236 0.0630  -0.0548 357 ARG A C   
2615 O O   . ARG A 351 ? 0.6882 0.6342 0.6352 -0.0219 0.0562  -0.0506 357 ARG A O   
2616 C CB  . ARG A 351 ? 0.7272 0.6605 0.7059 -0.0181 0.0675  -0.0611 357 ARG A CB  
2617 C CG  . ARG A 351 ? 0.7569 0.6991 0.7544 -0.0131 0.0670  -0.0656 357 ARG A CG  
2618 C CD  . ARG A 351 ? 0.7933 0.7363 0.8013 -0.0096 0.0644  -0.0640 357 ARG A CD  
2619 N NE  . ARG A 351 ? 0.9229 0.8711 0.9247 -0.0088 0.0564  -0.0563 357 ARG A NE  
2620 C CZ  . ARG A 351 ? 0.9621 0.9016 0.9531 -0.0121 0.0553  -0.0509 357 ARG A CZ  
2621 N NH1 . ARG A 351 ? 0.9049 0.8292 0.8884 -0.0159 0.0616  -0.0526 357 ARG A NH1 
2622 N NH2 . ARG A 351 ? 1.0059 0.9522 0.9931 -0.0116 0.0474  -0.0434 357 ARG A NH2 
2623 N N   . ASP A 352 ? 0.7011 0.6196 0.6423 -0.0284 0.0681  -0.0541 358 ASP A N   
2624 C CA  . ASP A 352 ? 0.6531 0.5674 0.5795 -0.0319 0.0652  -0.0476 358 ASP A CA  
2625 C C   . ASP A 352 ? 0.6290 0.5345 0.5406 -0.0367 0.0682  -0.0486 358 ASP A C   
2626 O O   . ASP A 352 ? 0.6323 0.5347 0.5315 -0.0398 0.0655  -0.0433 358 ASP A O   
2627 C CB  . ASP A 352 ? 0.6658 0.5683 0.5913 -0.0333 0.0663  -0.0445 358 ASP A CB  
2628 N N   . LEU A 353 ? 0.6253 0.5265 0.5380 -0.0377 0.0732  -0.0549 359 LEU A N   
2629 C CA  . LEU A 353 ? 0.6255 0.5173 0.5242 -0.0425 0.0757  -0.0564 359 LEU A CA  
2630 C C   . LEU A 353 ? 0.6144 0.4907 0.4994 -0.0474 0.0784  -0.0529 359 LEU A C   
2631 O O   . LEU A 353 ? 0.6694 0.5412 0.5407 -0.0508 0.0769  -0.0509 359 LEU A O   
2632 C CB  . LEU A 353 ? 0.6254 0.5293 0.5187 -0.0412 0.0689  -0.0551 359 LEU A CB  
2633 C CG  . LEU A 353 ? 0.6348 0.5511 0.5399 -0.0367 0.0662  -0.0598 359 LEU A CG  
2634 C CD1 . LEU A 353 ? 0.5922 0.5251 0.4958 -0.0327 0.0577  -0.0576 359 LEU A CD1 
2635 C CD2 . LEU A 353 ? 0.6237 0.5313 0.5270 -0.0396 0.0704  -0.0658 359 LEU A CD2 
2636 N N   . PHE A 354 ? 0.6180 0.4860 0.5069 -0.0473 0.0817  -0.0525 360 PHE A N   
2637 C CA  . PHE A 354 ? 0.6374 0.4890 0.5145 -0.0512 0.0842  -0.0500 360 PHE A CA  
2638 C C   . PHE A 354 ? 0.6485 0.5020 0.5153 -0.0530 0.0771  -0.0421 360 PHE A C   
2639 O O   . PHE A 354 ? 0.6841 0.5240 0.5384 -0.0571 0.0781  -0.0397 360 PHE A O   
2640 C CB  . PHE A 354 ? 0.6407 0.4772 0.5068 -0.0560 0.0913  -0.0543 360 PHE A CB  
2641 C CG  . PHE A 354 ? 0.5858 0.4214 0.4608 -0.0556 0.0984  -0.0615 360 PHE A CG  
2642 C CD1 . PHE A 354 ? 0.6079 0.4410 0.4937 -0.0532 0.1034  -0.0650 360 PHE A CD1 
2643 C CD2 . PHE A 354 ? 0.6339 0.4710 0.5063 -0.0577 0.0999  -0.0649 360 PHE A CD2 
2644 C CE1 . PHE A 354 ? 0.6258 0.4598 0.5204 -0.0531 0.1103  -0.0713 360 PHE A CE1 
2645 C CE2 . PHE A 354 ? 0.6529 0.4896 0.5335 -0.0582 0.1063  -0.0708 360 PHE A CE2 
2646 C CZ  . PHE A 354 ? 0.6594 0.4952 0.5514 -0.0560 0.1118  -0.0739 360 PHE A CZ  
2647 N N   . VAL A 355 ? 0.6674 0.5380 0.5392 -0.0501 0.0700  -0.0378 361 VAL A N   
2648 C CA  . VAL A 355 ? 0.6471 0.5225 0.5091 -0.0523 0.0634  -0.0300 361 VAL A CA  
2649 C C   . VAL A 355 ? 0.6489 0.5132 0.5067 -0.0548 0.0617  -0.0244 361 VAL A C   
2650 O O   . VAL A 355 ? 0.6787 0.5351 0.5238 -0.0592 0.0600  -0.0198 361 VAL A O   
2651 C CB  . VAL A 355 ? 0.6539 0.5519 0.5230 -0.0482 0.0563  -0.0268 361 VAL A CB  
2652 C CG1 . VAL A 355 ? 0.5660 0.4708 0.4272 -0.0505 0.0496  -0.0177 361 VAL A CG1 
2653 C CG2 . VAL A 355 ? 0.6535 0.5607 0.5222 -0.0464 0.0563  -0.0317 361 VAL A CG2 
2654 N N   . SER A 356 ? 0.6549 0.5174 0.5232 -0.0520 0.0617  -0.0246 362 SER A N   
2655 C CA  . SER A 356 ? 0.6297 0.4816 0.4947 -0.0539 0.0583  -0.0191 362 SER A CA  
2656 C C   . SER A 356 ? 0.6884 0.5188 0.5411 -0.0580 0.0629  -0.0207 362 SER A C   
2657 O O   . SER A 356 ? 0.6899 0.5107 0.5349 -0.0610 0.0587  -0.0149 362 SER A O   
2658 C CB  . SER A 356 ? 0.6393 0.4916 0.5185 -0.0494 0.0579  -0.0211 362 SER A CB  
2659 O OG  . SER A 356 ? 0.7416 0.5857 0.6264 -0.0474 0.0663  -0.0303 362 SER A OG  
2660 N N   . THR A 357 ? 0.7137 0.5362 0.5641 -0.0584 0.0709  -0.0284 363 THR A N   
2661 C CA  . THR A 357 ? 0.6623 0.4645 0.5006 -0.0621 0.0760  -0.0309 363 THR A CA  
2662 C C   . THR A 357 ? 0.7012 0.4981 0.5238 -0.0672 0.0721  -0.0249 363 THR A C   
2663 O O   . THR A 357 ? 0.7354 0.5166 0.5484 -0.0701 0.0712  -0.0224 363 THR A O   
2664 C CB  . THR A 357 ? 0.7066 0.5054 0.5456 -0.0621 0.0849  -0.0395 363 THR A CB  
2665 O OG1 . THR A 357 ? 0.7101 0.5134 0.5643 -0.0575 0.0887  -0.0450 363 THR A OG1 
2666 C CG2 . THR A 357 ? 0.8906 0.6694 0.7161 -0.0660 0.0903  -0.0421 363 THR A CG2 
2667 N N   . SER A 358 ? 0.7488 0.5586 0.5686 -0.0681 0.0693  -0.0229 364 SER A N   
2668 C CA  . SER A 358 ? 0.7268 0.5333 0.5324 -0.0728 0.0656  -0.0176 364 SER A CA  
2669 C C   . SER A 358 ? 0.7087 0.5187 0.5128 -0.0744 0.0575  -0.0080 364 SER A C   
2670 O O   . SER A 358 ? 0.7338 0.5327 0.5262 -0.0789 0.0550  -0.0034 364 SER A O   
2671 C CB  . SER A 358 ? 0.7036 0.5245 0.5077 -0.0725 0.0642  -0.0187 364 SER A CB  
2672 O OG  . SER A 358 ? 0.7491 0.5655 0.5541 -0.0719 0.0708  -0.0270 364 SER A OG  
2673 N N   . TRP A 359 ? 0.6807 0.5060 0.4962 -0.0712 0.0528  -0.0044 365 TRP A N   
2674 C CA  . TRP A 359 ? 0.6901 0.5189 0.5050 -0.0732 0.0447  0.0054  365 TRP A CA  
2675 C C   . TRP A 359 ? 0.6861 0.4938 0.4979 -0.0748 0.0442  0.0065  365 TRP A C   
2676 O O   . TRP A 359 ? 0.6851 0.4863 0.4892 -0.0790 0.0383  0.0142  365 TRP A O   
2677 C CB  . TRP A 359 ? 0.6705 0.5197 0.4985 -0.0693 0.0400  0.0085  365 TRP A CB  
2678 C CG  . TRP A 359 ? 0.6704 0.5409 0.4987 -0.0681 0.0381  0.0094  365 TRP A CG  
2679 C CD1 . TRP A 359 ? 0.6812 0.5622 0.5157 -0.0639 0.0417  0.0022  365 TRP A CD1 
2680 C CD2 . TRP A 359 ? 0.6895 0.5737 0.5115 -0.0711 0.0319  0.0177  365 TRP A CD2 
2681 N NE1 . TRP A 359 ? 0.6317 0.5318 0.4637 -0.0634 0.0377  0.0051  365 TRP A NE1 
2682 C CE2 . TRP A 359 ? 0.6017 0.5047 0.4262 -0.0678 0.0321  0.0144  365 TRP A CE2 
2683 C CE3 . TRP A 359 ? 0.7009 0.5839 0.5157 -0.0764 0.0258  0.0277  365 TRP A CE3 
2684 C CZ2 . TRP A 359 ? 0.6354 0.5565 0.4554 -0.0689 0.0271  0.0200  365 TRP A CZ2 
2685 C CZ3 . TRP A 359 ? 0.6570 0.5586 0.4677 -0.0782 0.0210  0.0340  365 TRP A CZ3 
2686 C CH2 . TRP A 359 ? 0.6779 0.5987 0.4912 -0.0743 0.0219  0.0299  365 TRP A CH2 
2687 N N   . LYS A 360 ? 0.6930 0.4903 0.5110 -0.0714 0.0500  -0.0012 366 LYS A N   
2688 C CA  . LYS A 360 ? 0.7443 0.5206 0.5583 -0.0721 0.0499  -0.0018 366 LYS A CA  
2689 C C   . LYS A 360 ? 0.7290 0.4879 0.5266 -0.0769 0.0520  -0.0018 366 LYS A C   
2690 O O   . LYS A 360 ? 0.7427 0.4892 0.5325 -0.0801 0.0465  0.0039  366 LYS A O   
2691 C CB  . LYS A 360 ? 0.7112 0.4816 0.5353 -0.0669 0.0566  -0.0111 366 LYS A CB  
2692 C CG  . LYS A 360 ? 0.8337 0.5854 0.6564 -0.0660 0.0545  -0.0116 366 LYS A CG  
2693 C CD  . LYS A 360 ? 0.9105 0.6587 0.7446 -0.0601 0.0605  -0.0209 366 LYS A CD  
2694 C CE  . LYS A 360 ? 1.0102 0.7406 0.8363 -0.0601 0.0691  -0.0291 366 LYS A CE  
2695 N NZ  . LYS A 360 ? 1.1203 0.8296 0.9339 -0.0622 0.0653  -0.0268 366 LYS A NZ  
2696 N N   . THR A 361 ? 0.7014 0.4590 0.4935 -0.0777 0.0591  -0.0077 367 THR A N   
2697 C CA  . THR A 361 ? 0.7596 0.5002 0.5356 -0.0824 0.0608  -0.0079 367 THR A CA  
2698 C C   . THR A 361 ? 0.7767 0.5199 0.5442 -0.0872 0.0524  0.0021  367 THR A C   
2699 O O   . THR A 361 ? 0.8575 0.5841 0.6143 -0.0907 0.0496  0.0055  367 THR A O   
2700 C CB  . THR A 361 ? 0.8010 0.5419 0.5726 -0.0830 0.0685  -0.0150 367 THR A CB  
2701 O OG1 . THR A 361 ? 0.7629 0.4983 0.5405 -0.0798 0.0769  -0.0239 367 THR A OG1 
2702 C CG2 . THR A 361 ? 0.7047 0.4303 0.4591 -0.0882 0.0690  -0.0141 367 THR A CG2 
2703 N N   . MET A 362 ? 0.7744 0.5389 0.5466 -0.0872 0.0482  0.0069  368 MET A N   
2704 C CA  . MET A 362 ? 0.7682 0.5396 0.5336 -0.0918 0.0406  0.0165  368 MET A CA  
2705 C C   . MET A 362 ? 0.7963 0.5684 0.5650 -0.0933 0.0321  0.0258  368 MET A C   
2706 O O   . MET A 362 ? 0.7894 0.5662 0.5525 -0.0979 0.0253  0.0349  368 MET A O   
2707 C CB  . MET A 362 ? 0.6970 0.4927 0.4662 -0.0906 0.0394  0.0175  368 MET A CB  
2708 C CG  . MET A 362 ? 0.7834 0.5781 0.5474 -0.0901 0.0455  0.0097  368 MET A CG  
2709 S SD  . MET A 362 ? 0.7758 0.5543 0.5216 -0.0963 0.0450  0.0112  368 MET A SD  
2710 C CE  . MET A 362 ? 0.6969 0.4988 0.4416 -0.0982 0.0369  0.0198  368 MET A CE  
2711 N N   . ARG A 363 ? 0.7891 0.5566 0.5670 -0.0897 0.0319  0.0239  369 ARG A N   
2712 C CA  . ARG A 363 ? 0.7391 0.5044 0.5201 -0.0911 0.0231  0.0323  369 ARG A CA  
2713 C C   . ARG A 363 ? 0.8295 0.6185 0.6152 -0.0930 0.0159  0.0420  369 ARG A C   
2714 O O   . ARG A 363 ? 0.8683 0.6577 0.6502 -0.0978 0.0076  0.0524  369 ARG A O   
2715 C CB  . ARG A 363 ? 0.8318 0.5748 0.6006 -0.0958 0.0189  0.0365  369 ARG A CB  
2716 C CG  . ARG A 363 ? 0.8922 0.6116 0.6583 -0.0929 0.0243  0.0275  369 ARG A CG  
2717 C CD  . ARG A 363 ? 0.9371 0.6336 0.6897 -0.0971 0.0202  0.0307  369 ARG A CD  
2718 N NE  . ARG A 363 ? 1.0917 0.7805 0.8321 -0.0997 0.0261  0.0268  369 ARG A NE  
2719 C CZ  . ARG A 363 ? 1.1141 0.8047 0.8449 -0.1053 0.0225  0.0332  369 ARG A CZ  
2720 N NH1 . ARG A 363 ? 1.0444 0.7450 0.7761 -0.1095 0.0130  0.0446  369 ARG A NH1 
2721 N NH2 . ARG A 363 ? 1.0787 0.7613 0.7989 -0.1070 0.0282  0.0283  369 ARG A NH2 
2722 N N   . GLN A 364 ? 0.7868 0.5962 0.5807 -0.0892 0.0190  0.0388  370 GLN A N   
2723 C CA  . GLN A 364 ? 0.7349 0.5691 0.5332 -0.0901 0.0132  0.0467  370 GLN A CA  
2724 C C   . GLN A 364 ? 0.7626 0.6108 0.5750 -0.0841 0.0140  0.0434  370 GLN A C   
2725 O O   . GLN A 364 ? 0.7660 0.6072 0.5847 -0.0793 0.0202  0.0339  370 GLN A O   
2726 C CB  . GLN A 364 ? 0.7111 0.5596 0.5033 -0.0914 0.0150  0.0465  370 GLN A CB  
2727 C CG  . GLN A 364 ? 0.6748 0.5173 0.4546 -0.0978 0.0116  0.0529  370 GLN A CG  
2728 C CD  . GLN A 364 ? 0.7101 0.5692 0.4857 -0.0979 0.0131  0.0517  370 GLN A CD  
2729 O OE1 . GLN A 364 ? 0.6892 0.5726 0.4713 -0.0951 0.0115  0.0530  370 GLN A OE1 
2730 N NE2 . GLN A 364 ? 0.6918 0.5381 0.4565 -0.1006 0.0158  0.0488  370 GLN A NE2 
2731 N N   . SER A 365 ? 0.7529 0.6210 0.5702 -0.0846 0.0076  0.0513  371 SER A N   
2732 C CA  . SER A 365 ? 0.7654 0.6470 0.5955 -0.0788 0.0082  0.0479  371 SER A CA  
2733 C C   . SER A 365 ? 0.7358 0.6422 0.5677 -0.0763 0.0094  0.0467  371 SER A C   
2734 O O   . SER A 365 ? 0.6855 0.6050 0.5108 -0.0798 0.0058  0.0534  371 SER A O   
2735 C CB  . SER A 365 ? 0.7786 0.6639 0.6147 -0.0800 -0.0005 0.0568  371 SER A CB  
2736 O OG  . SER A 365 ? 0.8786 0.7408 0.7159 -0.0800 -0.0016 0.0553  371 SER A OG  
2737 N N   . PRO A 366 ? 0.7126 0.6256 0.5532 -0.0701 0.0142  0.0378  372 PRO A N   
2738 C CA  . PRO A 366 ? 0.7312 0.6664 0.5732 -0.0669 0.0148  0.0356  372 PRO A CA  
2739 C C   . PRO A 366 ? 0.7297 0.6880 0.5748 -0.0672 0.0074  0.0448  372 PRO A C   
2740 O O   . PRO A 366 ? 0.7348 0.6924 0.5847 -0.0684 0.0023  0.0512  372 PRO A O   
2741 C CB  . PRO A 366 ? 0.7067 0.6411 0.5591 -0.0604 0.0204  0.0248  372 PRO A CB  
2742 C CG  . PRO A 366 ? 0.6577 0.5765 0.5170 -0.0597 0.0209  0.0239  372 PRO A CG  
2743 C CD  . PRO A 366 ? 0.7223 0.6232 0.5723 -0.0656 0.0189  0.0295  372 PRO A CD  
2744 N N   . PRO A 367 ? 0.7512 0.7308 0.5933 -0.0661 0.0061  0.0459  373 PRO A N   
2745 C CA  . PRO A 367 ? 0.8018 0.8069 0.6457 -0.0661 -0.0003 0.0542  373 PRO A CA  
2746 C C   . PRO A 367 ? 0.8932 0.9119 0.7485 -0.0590 -0.0007 0.0498  373 PRO A C   
2747 O O   . PRO A 367 ? 0.9787 1.0149 0.8379 -0.0585 -0.0062 0.0566  373 PRO A O   
2748 C CB  . PRO A 367 ? 0.7971 0.8176 0.6328 -0.0666 -0.0003 0.0543  373 PRO A CB  
2749 C CG  . PRO A 367 ? 0.7841 0.7849 0.6135 -0.0673 0.0058  0.0461  373 PRO A CG  
2750 C CD  . PRO A 367 ? 0.7828 0.7634 0.6189 -0.0647 0.0106  0.0386  373 PRO A CD  
2751 O OXT . PRO A 367 ? 0.9028 0.9151 0.7635 -0.0539 0.0044  0.0394  373 PRO A OXT 
# 
