data_8YO8
# 
_entry.id   8YO8 
# 
_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   8YO8         pdb_00008yo8 10.2210/pdb8yo8/pdb 
WWPDB D_1300045937 ?            ?                   
# 
_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                        8YO8 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-12 
_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 'SULFATE ION'                           96.063    1   ?       ? ? ? 
3 non-polymer syn '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE' 801.549   1   ?       ? ? ? 
4 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE       663.425   1   ?       ? ? ? 
5 water       nat water                                   18.015    205 ?       ? ? ? 
# 
_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 'SULFATE ION'                           SO4 
3 '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE' 6FA 
4 NICOTINAMIDE-ADENINE-DINUCLEOTIDE       NAD 
5 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 
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE       ? 'C21 H27 N7 O14 P2' 663.425 
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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 6FA ? ? 6FA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAD ? ? NAD ? ? 'SUBJECT OF INVESTIGATION' ? 
3 SO4 ? ? SO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4 1   401 1   SO4 SO4 A . 
C 3 6FA 1   402 401 6FA 6FA A . 
D 4 NAD 1   403 402 NAD NAD A . 
E 5 HOH 1   501 160 HOH HOH A . 
E 5 HOH 2   502 195 HOH HOH A . 
E 5 HOH 3   503 82  HOH HOH A . 
E 5 HOH 4   504 170 HOH HOH A . 
E 5 HOH 5   505 89  HOH HOH A . 
E 5 HOH 6   506 115 HOH HOH A . 
E 5 HOH 7   507 197 HOH HOH A . 
E 5 HOH 8   508 14  HOH HOH A . 
E 5 HOH 9   509 112 HOH HOH A . 
E 5 HOH 10  510 26  HOH HOH A . 
E 5 HOH 11  511 41  HOH HOH A . 
E 5 HOH 12  512 58  HOH HOH A . 
E 5 HOH 13  513 62  HOH HOH A . 
E 5 HOH 14  514 64  HOH HOH A . 
E 5 HOH 15  515 39  HOH HOH A . 
E 5 HOH 16  516 71  HOH HOH A . 
E 5 HOH 17  517 65  HOH HOH A . 
E 5 HOH 18  518 86  HOH HOH A . 
E 5 HOH 19  519 12  HOH HOH A . 
E 5 HOH 20  520 84  HOH HOH A . 
E 5 HOH 21  521 44  HOH HOH A . 
E 5 HOH 22  522 99  HOH HOH A . 
E 5 HOH 23  523 20  HOH HOH A . 
E 5 HOH 24  524 11  HOH HOH A . 
E 5 HOH 25  525 98  HOH HOH A . 
E 5 HOH 26  526 130 HOH HOH A . 
E 5 HOH 27  527 21  HOH HOH A . 
E 5 HOH 28  528 22  HOH HOH A . 
E 5 HOH 29  529 114 HOH HOH A . 
E 5 HOH 30  530 28  HOH HOH A . 
E 5 HOH 31  531 25  HOH HOH A . 
E 5 HOH 32  532 30  HOH HOH A . 
E 5 HOH 33  533 2   HOH HOH A . 
E 5 HOH 34  534 143 HOH HOH A . 
E 5 HOH 35  535 36  HOH HOH A . 
E 5 HOH 36  536 17  HOH HOH A . 
E 5 HOH 37  537 38  HOH HOH A . 
E 5 HOH 38  538 93  HOH HOH A . 
E 5 HOH 39  539 4   HOH HOH A . 
E 5 HOH 40  540 125 HOH HOH A . 
E 5 HOH 41  541 187 HOH HOH A . 
E 5 HOH 42  542 102 HOH HOH A . 
E 5 HOH 43  543 135 HOH HOH A . 
E 5 HOH 44  544 146 HOH HOH A . 
E 5 HOH 45  545 9   HOH HOH A . 
E 5 HOH 46  546 27  HOH HOH A . 
E 5 HOH 47  547 81  HOH HOH A . 
E 5 HOH 48  548 52  HOH HOH A . 
E 5 HOH 49  549 161 HOH HOH A . 
E 5 HOH 50  550 63  HOH HOH A . 
E 5 HOH 51  551 59  HOH HOH A . 
E 5 HOH 52  552 48  HOH HOH A . 
E 5 HOH 53  553 110 HOH HOH A . 
E 5 HOH 54  554 7   HOH HOH A . 
E 5 HOH 55  555 186 HOH HOH A . 
E 5 HOH 56  556 69  HOH HOH A . 
E 5 HOH 57  557 32  HOH HOH A . 
E 5 HOH 58  558 111 HOH HOH A . 
E 5 HOH 59  559 80  HOH HOH A . 
E 5 HOH 60  560 182 HOH HOH A . 
E 5 HOH 61  561 5   HOH HOH A . 
E 5 HOH 62  562 67  HOH HOH A . 
E 5 HOH 63  563 45  HOH HOH A . 
E 5 HOH 64  564 129 HOH HOH A . 
E 5 HOH 65  565 24  HOH HOH A . 
E 5 HOH 66  566 23  HOH HOH A . 
E 5 HOH 67  567 43  HOH HOH A . 
E 5 HOH 68  568 179 HOH HOH A . 
E 5 HOH 69  569 105 HOH HOH A . 
E 5 HOH 70  570 70  HOH HOH A . 
E 5 HOH 71  571 40  HOH HOH A . 
E 5 HOH 72  572 100 HOH HOH A . 
E 5 HOH 73  573 57  HOH HOH A . 
E 5 HOH 74  574 47  HOH HOH A . 
E 5 HOH 75  575 168 HOH HOH A . 
E 5 HOH 76  576 94  HOH HOH A . 
E 5 HOH 77  577 150 HOH HOH A . 
E 5 HOH 78  578 72  HOH HOH A . 
E 5 HOH 79  579 78  HOH HOH A . 
E 5 HOH 80  580 92  HOH HOH A . 
E 5 HOH 81  581 165 HOH HOH A . 
E 5 HOH 82  582 201 HOH HOH A . 
E 5 HOH 83  583 37  HOH HOH A . 
E 5 HOH 84  584 19  HOH HOH A . 
E 5 HOH 85  585 121 HOH HOH A . 
E 5 HOH 86  586 50  HOH HOH A . 
E 5 HOH 87  587 142 HOH HOH A . 
E 5 HOH 88  588 120 HOH HOH A . 
E 5 HOH 89  589 76  HOH HOH A . 
E 5 HOH 90  590 8   HOH HOH A . 
E 5 HOH 91  591 46  HOH HOH A . 
E 5 HOH 92  592 123 HOH HOH A . 
E 5 HOH 93  593 34  HOH HOH A . 
E 5 HOH 94  594 151 HOH HOH A . 
E 5 HOH 95  595 16  HOH HOH A . 
E 5 HOH 96  596 3   HOH HOH A . 
E 5 HOH 97  597 141 HOH HOH A . 
E 5 HOH 98  598 137 HOH HOH A . 
E 5 HOH 99  599 60  HOH HOH A . 
E 5 HOH 100 600 1   HOH HOH A . 
E 5 HOH 101 601 13  HOH HOH A . 
E 5 HOH 102 602 126 HOH HOH A . 
E 5 HOH 103 603 173 HOH HOH A . 
E 5 HOH 104 604 192 HOH HOH A . 
E 5 HOH 105 605 6   HOH HOH A . 
E 5 HOH 106 606 33  HOH HOH A . 
E 5 HOH 107 607 138 HOH HOH A . 
E 5 HOH 108 608 10  HOH HOH A . 
E 5 HOH 109 609 122 HOH HOH A . 
E 5 HOH 110 610 85  HOH HOH A . 
E 5 HOH 111 611 75  HOH HOH A . 
E 5 HOH 112 612 56  HOH HOH A . 
E 5 HOH 113 613 183 HOH HOH A . 
E 5 HOH 114 614 74  HOH HOH A . 
E 5 HOH 115 615 188 HOH HOH A . 
E 5 HOH 116 616 95  HOH HOH A . 
E 5 HOH 117 617 132 HOH HOH A . 
E 5 HOH 118 618 31  HOH HOH A . 
E 5 HOH 119 619 181 HOH HOH A . 
E 5 HOH 120 620 104 HOH HOH A . 
E 5 HOH 121 621 66  HOH HOH A . 
E 5 HOH 122 622 106 HOH HOH A . 
E 5 HOH 123 623 113 HOH HOH A . 
E 5 HOH 124 624 54  HOH HOH A . 
E 5 HOH 125 625 15  HOH HOH A . 
E 5 HOH 126 626 148 HOH HOH A . 
E 5 HOH 127 627 109 HOH HOH A . 
E 5 HOH 128 628 108 HOH HOH A . 
E 5 HOH 129 629 18  HOH HOH A . 
E 5 HOH 130 630 184 HOH HOH A . 
E 5 HOH 131 631 77  HOH HOH A . 
E 5 HOH 132 632 101 HOH HOH A . 
E 5 HOH 133 633 145 HOH HOH A . 
E 5 HOH 134 634 55  HOH HOH A . 
E 5 HOH 135 635 29  HOH HOH A . 
E 5 HOH 136 636 79  HOH HOH A . 
E 5 HOH 137 637 35  HOH HOH A . 
E 5 HOH 138 638 87  HOH HOH A . 
E 5 HOH 139 639 96  HOH HOH A . 
E 5 HOH 140 640 180 HOH HOH A . 
E 5 HOH 141 641 190 HOH HOH A . 
E 5 HOH 142 642 149 HOH HOH A . 
E 5 HOH 143 643 189 HOH HOH A . 
E 5 HOH 144 644 144 HOH HOH A . 
E 5 HOH 145 645 103 HOH HOH A . 
E 5 HOH 146 646 166 HOH HOH A . 
E 5 HOH 147 647 88  HOH HOH A . 
E 5 HOH 148 648 196 HOH HOH A . 
E 5 HOH 149 649 153 HOH HOH A . 
E 5 HOH 150 650 116 HOH HOH A . 
E 5 HOH 151 651 164 HOH HOH A . 
E 5 HOH 152 652 118 HOH HOH A . 
E 5 HOH 153 653 158 HOH HOH A . 
E 5 HOH 154 654 73  HOH HOH A . 
E 5 HOH 155 655 127 HOH HOH A . 
E 5 HOH 156 656 140 HOH HOH A . 
E 5 HOH 157 657 42  HOH HOH A . 
E 5 HOH 158 658 53  HOH HOH A . 
E 5 HOH 159 659 97  HOH HOH A . 
E 5 HOH 160 660 157 HOH HOH A . 
E 5 HOH 161 661 155 HOH HOH A . 
E 5 HOH 162 662 200 HOH HOH A . 
E 5 HOH 163 663 134 HOH HOH A . 
E 5 HOH 164 664 175 HOH HOH A . 
E 5 HOH 165 665 194 HOH HOH A . 
E 5 HOH 166 666 51  HOH HOH A . 
E 5 HOH 167 667 156 HOH HOH A . 
E 5 HOH 168 668 169 HOH HOH A . 
E 5 HOH 169 669 177 HOH HOH A . 
E 5 HOH 170 670 203 HOH HOH A . 
E 5 HOH 171 671 191 HOH HOH A . 
E 5 HOH 172 672 139 HOH HOH A . 
E 5 HOH 173 673 159 HOH HOH A . 
E 5 HOH 174 674 162 HOH HOH A . 
E 5 HOH 175 675 68  HOH HOH A . 
E 5 HOH 176 676 124 HOH HOH A . 
E 5 HOH 177 677 147 HOH HOH A . 
E 5 HOH 178 678 61  HOH HOH A . 
E 5 HOH 179 679 90  HOH HOH A . 
E 5 HOH 180 680 198 HOH HOH A . 
E 5 HOH 181 681 133 HOH HOH A . 
E 5 HOH 182 682 163 HOH HOH A . 
E 5 HOH 183 683 152 HOH HOH A . 
E 5 HOH 184 684 199 HOH HOH A . 
E 5 HOH 185 685 117 HOH HOH A . 
E 5 HOH 186 686 131 HOH HOH A . 
E 5 HOH 187 687 193 HOH HOH A . 
E 5 HOH 188 688 91  HOH HOH A . 
E 5 HOH 189 689 171 HOH HOH A . 
E 5 HOH 190 690 128 HOH HOH A . 
E 5 HOH 191 691 49  HOH HOH A . 
E 5 HOH 192 692 185 HOH HOH A . 
E 5 HOH 193 693 202 HOH HOH A . 
E 5 HOH 194 694 176 HOH HOH A . 
E 5 HOH 195 695 172 HOH HOH A . 
E 5 HOH 196 696 178 HOH HOH A . 
E 5 HOH 197 697 205 HOH HOH A . 
E 5 HOH 198 698 107 HOH HOH A . 
E 5 HOH 199 699 83  HOH HOH A . 
E 5 HOH 200 700 119 HOH HOH A . 
E 5 HOH 201 701 204 HOH HOH A . 
E 5 HOH 202 702 167 HOH HOH A . 
E 5 HOH 203 703 174 HOH HOH A . 
E 5 HOH 204 704 154 HOH HOH A . 
E 5 HOH 205 705 136 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 ARG 78  ? NE  ? A ARG 72  NE  
2  1 Y 1 A ARG 78  ? CZ  ? A ARG 72  CZ  
3  1 Y 1 A ARG 78  ? NH1 ? A ARG 72  NH1 
4  1 Y 1 A ARG 78  ? NH2 ? A ARG 72  NH2 
5  1 Y 1 A LYS 88  ? CD  ? A LYS 82  CD  
6  1 Y 1 A LYS 88  ? CE  ? A LYS 82  CE  
7  1 Y 1 A LYS 88  ? NZ  ? A LYS 82  NZ  
8  1 Y 1 A GLU 98  ? CG  ? A GLU 92  CG  
9  1 Y 1 A GLU 98  ? CD  ? A GLU 92  CD  
10 1 Y 1 A GLU 98  ? OE1 ? A GLU 92  OE1 
11 1 Y 1 A GLU 98  ? OE2 ? A GLU 92  OE2 
12 1 Y 1 A ARG 137 ? NE  ? A ARG 131 NE  
13 1 Y 1 A ARG 137 ? CZ  ? A ARG 131 CZ  
14 1 Y 1 A ARG 137 ? NH1 ? A ARG 131 NH1 
15 1 Y 1 A ARG 137 ? NH2 ? A ARG 131 NH2 
16 1 Y 1 A LYS 182 ? CG  ? A LYS 176 CG  
17 1 Y 1 A LYS 182 ? CD  ? A LYS 176 CD  
18 1 Y 1 A LYS 182 ? CE  ? A LYS 176 CE  
19 1 Y 1 A LYS 182 ? NZ  ? A LYS 176 NZ  
20 1 Y 1 A GLU 183 ? CD  ? A GLU 177 CD  
21 1 Y 1 A GLU 183 ? OE1 ? A GLU 177 OE1 
22 1 Y 1 A GLU 183 ? OE2 ? A GLU 177 OE2 
23 1 Y 1 A GLU 194 ? CD  ? A GLU 188 CD  
24 1 Y 1 A GLU 194 ? OE1 ? A GLU 188 OE1 
25 1 Y 1 A GLU 194 ? OE2 ? A GLU 188 OE2 
26 1 Y 1 A GLU 214 ? CG  ? A GLU 208 CG  
27 1 Y 1 A GLU 214 ? CD  ? A GLU 208 CD  
28 1 Y 1 A GLU 214 ? OE1 ? A GLU 208 OE1 
29 1 Y 1 A GLU 214 ? OE2 ? A GLU 208 OE2 
30 1 Y 1 A GLU 219 ? CG  ? A GLU 213 CG  
31 1 Y 1 A GLU 219 ? CD  ? A GLU 213 CD  
32 1 Y 1 A GLU 219 ? OE1 ? A GLU 213 OE1 
33 1 Y 1 A GLU 219 ? OE2 ? A GLU 213 OE2 
34 1 Y 1 A GLU 222 ? CD  ? A GLU 216 CD  
35 1 Y 1 A GLU 222 ? OE1 ? A GLU 216 OE1 
36 1 Y 1 A GLU 222 ? OE2 ? A GLU 216 OE2 
37 1 Y 1 A ARG 253 ? CD  ? A ARG 247 CD  
38 1 Y 1 A ARG 253 ? NE  ? A ARG 247 NE  
39 1 Y 1 A ARG 253 ? CZ  ? A ARG 247 CZ  
40 1 Y 1 A ARG 253 ? NH1 ? A ARG 247 NH1 
41 1 Y 1 A ARG 253 ? NH2 ? A ARG 247 NH2 
42 1 Y 1 A GLU 257 ? CD  ? A GLU 251 CD  
43 1 Y 1 A GLU 257 ? OE1 ? A GLU 251 OE1 
44 1 Y 1 A GLU 257 ? OE2 ? A GLU 251 OE2 
45 1 Y 1 A ARG 259 ? CG  ? A ARG 253 CG  
46 1 Y 1 A ARG 259 ? CD  ? A ARG 253 CD  
47 1 Y 1 A ARG 259 ? NE  ? A ARG 253 NE  
48 1 Y 1 A ARG 259 ? CZ  ? A ARG 253 CZ  
49 1 Y 1 A ARG 259 ? NH1 ? A ARG 253 NH1 
50 1 Y 1 A ARG 259 ? NH2 ? A ARG 253 NH2 
51 1 Y 1 A SER 263 ? OG  ? A SER 257 OG  
52 1 Y 1 A ARG 290 ? CG  ? A ARG 284 CG  
53 1 Y 1 A ARG 290 ? CD  ? A ARG 284 CD  
54 1 Y 1 A ARG 290 ? NE  ? A ARG 284 NE  
55 1 Y 1 A ARG 290 ? CZ  ? A ARG 284 CZ  
56 1 Y 1 A ARG 290 ? NH1 ? A ARG 284 NH1 
57 1 Y 1 A ARG 290 ? NH2 ? A ARG 284 NH2 
58 1 Y 1 A ARG 316 ? NE  ? A ARG 310 NE  
59 1 Y 1 A ARG 316 ? CZ  ? A ARG 310 CZ  
60 1 Y 1 A ARG 316 ? NH1 ? A ARG 310 NH1 
61 1 Y 1 A ARG 316 ? NH2 ? A ARG 310 NH2 
# 
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 scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.2_4158          3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    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                     8YO8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.162 
_cell.length_a_esd                 ? 
_cell.length_b                     60.162 
_cell.length_b_esd                 ? 
_cell.length_c                     195.256 
_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                         8YO8 
_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                   8YO8 
_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             2.52 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.12 
_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              7.7 
_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, 16.5% 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         2021-10-04 
_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   0.987 
_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        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          24.41 
_reflns.entry_id                                       8YO8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               32.54 
_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                                     28766 
_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                           84.01 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.07 
_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                             2813 
_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                               0.425 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                                 8YO8 
_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                            2.00 
_refine.ls_d_res_low                             32.54 
_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                     24080 
_refine.ls_number_reflns_R_free                  1233 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.01 
_refine.ls_percent_reflns_R_free                 5.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1877 
_refine.ls_R_factor_R_free                       0.2225 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1858 
_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                          1.36 
_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                 23.13 
_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                            0.17 
_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                       2.00 
_refine_hist.d_res_low                        32.54 
_refine_hist.number_atoms_solvent             205 
_refine_hist.number_atoms_total               3060 
_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        2752 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         103 
_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' ? 0.007  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.878  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.621 ? 1092 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 465  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 496  ? 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' 2.00 2.08 . . 73  1035 36.00  . . . . 0.2191 . . . . . . . . . . . 0.2213 
'X-RAY DIFFRACTION' 2.08 2.17 . . 77  1479 50.00  . . . . 0.2103 . . . . . . . . . . . 0.2669 
'X-RAY DIFFRACTION' 2.17 2.29 . . 93  2082 70.00  . . . . 0.2193 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 2.29 2.43 . . 174 2892 98.00  . . . . 0.2152 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 2.43 2.62 . . 147 3030 100.00 . . . . 0.2167 . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 2.62 2.88 . . 134 3036 100.00 . . . . 0.2063 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 2.88 3.30 . . 164 3008 100.00 . . . . 0.1947 . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 3.30 4.16 . . 199 3045 100.00 . . . . 0.1640 . . . . . . . . . . . 0.1960 
# 
_struct.entry_id                     8YO8 
_struct.title                        'Crystal structure of hFSP1 with both 6-OH-FAD and NAD (hFSP1-6-OH-FAD-NAD)' 
_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        8YO8 
_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 ? 
E N N 5 ? 
# 
_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              8YO8 
_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 8YO8 PRO A 1 ? UNP Q9BRQ8 ? ? 'expression tag'        7 1 
1 8YO8 HIS A 2 ? UNP Q9BRQ8 ? ? 'expression tag'        8 2 
1 8YO8 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)' 6810  ? 
2 MORE         -54   ? 
2 'SSA (A^2)'  28910 ? 
# 
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,E 
2 1,2 A,B,C,D,E 
# 
_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 ASN A 43  ? ALA A 46  ? ASN A 49  ALA A 52  5 ? 4  
HELX_P HELX_P3  AA3 LEU A 47  ? VAL A 51  ? LEU A 53  VAL A 57  5 ? 5  
HELX_P HELX_P4  AA4 PHE A 55  ? LYS A 58  ? PHE A 61  LYS A 64  5 ? 4  
HELX_P HELX_P5  AA5 TYR A 63  ? LYS A 68  ? TYR A 69  LYS A 74  1 ? 6  
HELX_P HELX_P6  AA6 SER A 118 ? SER A 136 ? SER A 124 SER A 142 1 ? 19 
HELX_P HELX_P7  AA7 GLY A 145 ? TYR A 159 ? GLY A 151 TYR A 165 1 ? 15 
HELX_P HELX_P8  AA8 LEU A 179 ? GLY A 194 ? LEU A 185 GLY A 200 1 ? 16 
HELX_P HELX_P9  AA9 ASN A 205 ? LEU A 209 ? ASN A 211 LEU A 215 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 250 ? LEU A 254 ? PHE A 256 LEU A 260 5 ? 5  
HELX_P HELX_P11 AB2 GLY A 278 ? ALA A 281 ? GLY A 284 ALA A 287 5 ? 4  
HELX_P HELX_P12 AB3 MET A 288 ? LYS A 308 ? MET A 294 LYS A 314 1 ? 21 
HELX_P HELX_P13 AB4 GLY A 341 ? LYS A 349 ? GLY A 347 LYS A 355 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 354 ? MET A 362 ? PHE A 360 MET A 368 1 ? 9  
# 
_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       2.45 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 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 
AA3 2 3 ? 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 ? anti-parallel 
AA7 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  
AA3 3 ALA A 93  ? PRO A 95  ? ALA A 99  PRO A 101 
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 198 ? GLN A 202 LEU A 204 
AA5 2 GLU A 163 ? ILE A 167 ? GLU A 169 ILE A 173 
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 PHE A 322 ? SER A 325 ? PHE A 328 SER A 331 
AA7 2 GLY A 331 ? ILE A 335 ? GLY A 337 ILE A 341 
AA7 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  
AA3 2 3 N VAL A 86  ? N VAL A 92  O LEU A 94  ? O LEU A 100 
AA4 1 2 N THR A 106 ? N THR A 112 O LYS A 240 ? O LYS A 246 
AA5 1 2 O GLN A 196 ? O GLN A 202 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 PHE A 322 ? N PHE A 328 O GLN A 334 ? O GLN A 340 
AA7 2 3 N GLY A 333 ? N GLY A 339 O VAL A 340 ? O VAL A 346 
# 
_pdbx_entry_details.entry_id                   8YO8 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 685 ? ? O A HOH 704 ? ? 1.83 
2  1 O   A HOH 594 ? ? O A HOH 630 ? ? 1.85 
3  1 O   A HOH 638 ? ? O A HOH 676 ? ? 1.87 
4  1 OD1 A ASN 303 ? ? O A HOH 501 ? ? 1.89 
5  1 O   A HOH 679 ? ? O A HOH 698 ? ? 1.99 
6  1 O   A GLU 275 ? ? O A HOH 502 ? ? 2.00 
7  1 O   A HOH 621 ? ? O A HOH 702 ? ? 2.08 
8  1 O   A HOH 658 ? ? O A HOH 686 ? ? 2.12 
9  1 O   A HOH 526 ? ? O A HOH 589 ? ? 2.12 
10 1 O   A HOH 609 ? ? O A HOH 646 ? ? 2.14 
11 1 O   A HOH 652 ? ? O A HOH 689 ? ? 2.16 
12 1 OG  A SER 342 ? ? O A HOH 503 ? ? 2.16 
13 1 O   A HOH 588 ? ? O A HOH 695 ? ? 2.16 
14 1 OXT A PRO 373 ? ? O A HOH 504 ? ? 2.17 
15 1 ND1 A HIS 277 ? ? O A HOH 502 ? ? 2.17 
16 1 OE1 A GLN 29  ? ? O A HOH 501 ? ? 2.18 
# 
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  ? ? 54.14   -129.13 
2 1 ALA A 108 ? ? -140.43 49.63   
3 1 ALA A 180 ? ? 62.13   -174.90 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 548 ? E HOH . 
2 1 A HOH 688 ? E HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 32.6826 21.2612 24.1694 0.1672 ? 0.0029  ? -0.0366 ? 0.2659 ? -0.0664 ? 0.2170 ? 1.1499 ? 0.7126 ? 
0.5820 ? 1.9779 ? 1.1627 ? 1.8031 ? 0.0742  ? 0.0290  ? -0.1256 ? 0.4179  ? 0.2020  ? -0.4190 ? 0.1893  ? 0.5747  ? -0.1839 ? 
2 'X-RAY DIFFRACTION' ? refined 29.1692 10.9300 6.2588  0.1268 ? 0.0759  ? 0.0487  ? 0.2645 ? -0.0197 ? 0.2555 ? 1.7566 ? 1.0968 ? 
0.2379 ? 2.7153 ? 0.8545 ? 1.7666 ? -0.0289 ? 0.1648  ? -0.2487 ? 0.0112  ? 0.1279  ? -0.3532 ? 0.1663  ? 0.6339  ? -0.2367 ? 
3 'X-RAY DIFFRACTION' ? refined 11.8955 -0.2815 9.4819  0.2800 ? -0.0037 ? 0.0486  ? 0.1184 ? -0.0171 ? 0.2484 ? 1.2083 ? 0.2693 ? 
0.0334 ? 2.0853 ? 0.5875 ? 2.0514 ? 0.0806  ? -0.1713 ? -0.2762 ? 0.3584  ? -0.0597 ? 0.2350  ? 0.5920  ? -0.1438 ? 0.0566  ? 
4 'X-RAY DIFFRACTION' ? refined 25.4396 -2.9973 12.1703 0.4928 ? 0.0964  ? -0.0576 ? 0.1419 ? -0.0282 ? 0.3142 ? 0.9238 ? 0.1476 ? 
0.1987 ? 1.6559 ? 0.8446 ? 2.0793 ? 0.0952  ? -0.1021 ? -0.3386 ? 0.7657  ? -0.0516 ? -0.3732 ? 0.4356  ? 0.0984  ? -0.2530 ? 
5 'X-RAY DIFFRACTION' ? refined 24.0669 12.6012 36.8137 1.2001 ? -0.3139 ? -0.1178 ? 0.2278 ? -0.1529 ? 0.0786 ? 0.7205 ? 0.7286 ? 
0.1913 ? 1.4617 ? 0.9870 ? 1.5501 ? 0.2059  ? -0.3633 ? -0.1821 ? 0.9028  ? -0.1350 ? -0.0121 ? 0.7813  ? -0.1765 ? -0.0949 ? 
6 'X-RAY DIFFRACTION' ? refined 21.5396 24.2189 34.1111 0.3235 ? -0.1384 ? 0.0823  ? 0.3168 ? -0.0901 ? 0.1921 ? 1.0964 ? 0.7846 ? 
1.2185 ? 2.6488 ? 2.2983 ? 3.1520 ? 0.2359  ? -0.4159 ? 0.2636  ? 0.6845  ? -0.3308 ? 0.2287  ? 0.1953  ? -0.1502 ? 0.1211  ? 
7 'X-RAY DIFFRACTION' ? refined 8.1527  16.5996 22.7012 0.3222 ? -0.0376 ? 0.1019  ? 0.2967 ? -0.0977 ? 0.2282 ? 0.7749 ? 0.6278 ? 
0.2425 ? 1.6121 ? 1.1142 ? 1.4076 ? 0.3419  ? -0.3934 ? 0.1856  ? 0.6128  ? -0.2679 ? 0.1950  ? 0.2697  ? -0.1400 ? 0.2321  ? 
8 'X-RAY DIFFRACTION' ? refined 19.3249 25.3544 13.1118 0.1541 ? 0.0233  ? 0.0539  ? 0.1186 ? -0.0087 ? 0.1566 ? 4.1231 ? 2.8154 ? 
0.2968 ? 4.3109 ? 0.8683 ? 1.8795 ? 0.0095  ? -0.0387 ? 0.5236  ? -0.1152 ? -0.1054 ? 0.1778  ? -0.3952 ? 0.0899  ? 0.0996  ? 
# 
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 113 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 114 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 256 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 257 through 294 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 295 through 313 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 314 through 354 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 355 through 373 )
;
# 
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 
NAD PA     P N S 337 
NAD O1A    O N N 338 
NAD O2A    O N N 339 
NAD O5B    O N N 340 
NAD C5B    C N N 341 
NAD C4B    C N R 342 
NAD O4B    O N N 343 
NAD C3B    C N S 344 
NAD O3B    O N N 345 
NAD C2B    C N R 346 
NAD O2B    O N N 347 
NAD C1B    C N R 348 
NAD N9A    N Y N 349 
NAD C8A    C Y N 350 
NAD N7A    N Y N 351 
NAD C5A    C Y N 352 
NAD C6A    C Y N 353 
NAD N6A    N N N 354 
NAD N1A    N Y N 355 
NAD C2A    C Y N 356 
NAD N3A    N Y N 357 
NAD C4A    C Y N 358 
NAD O3     O N N 359 
NAD PN     P N N 360 
NAD O1N    O N N 361 
NAD O2N    O N N 362 
NAD O5D    O N N 363 
NAD C5D    C N N 364 
NAD C4D    C N R 365 
NAD O4D    O N N 366 
NAD C3D    C N S 367 
NAD O3D    O N N 368 
NAD C2D    C N R 369 
NAD O2D    O N N 370 
NAD C1D    C N R 371 
NAD N1N    N Y N 372 
NAD C2N    C Y N 373 
NAD C3N    C Y N 374 
NAD C7N    C N N 375 
NAD O7N    O N N 376 
NAD N7N    N N N 377 
NAD C4N    C Y N 378 
NAD C5N    C Y N 379 
NAD C6N    C Y N 380 
NAD HOA2   H N N 381 
NAD H51A   H N N 382 
NAD H52A   H N N 383 
NAD H4B    H N N 384 
NAD H3B    H N N 385 
NAD HO3A   H N N 386 
NAD H2B    H N N 387 
NAD HO2A   H N N 388 
NAD H1B    H N N 389 
NAD H8A    H N N 390 
NAD H61A   H N N 391 
NAD H62A   H N N 392 
NAD H2A    H N N 393 
NAD H51N   H N N 394 
NAD H52N   H N N 395 
NAD H4D    H N N 396 
NAD H3D    H N N 397 
NAD HO3N   H N N 398 
NAD H2D    H N N 399 
NAD HO2N   H N N 400 
NAD H1D    H N N 401 
NAD H2N    H N N 402 
NAD H71N   H N N 403 
NAD H72N   H N N 404 
NAD H4N    H N N 405 
NAD H5N    H N N 406 
NAD H6N    H N N 407 
PHE N      N N N 408 
PHE CA     C N S 409 
PHE C      C N N 410 
PHE O      O N N 411 
PHE CB     C N N 412 
PHE CG     C Y N 413 
PHE CD1    C Y N 414 
PHE CD2    C Y N 415 
PHE CE1    C Y N 416 
PHE CE2    C Y N 417 
PHE CZ     C Y N 418 
PHE OXT    O N N 419 
PHE H      H N N 420 
PHE H2     H N N 421 
PHE HA     H N N 422 
PHE HB2    H N N 423 
PHE HB3    H N N 424 
PHE HD1    H N N 425 
PHE HD2    H N N 426 
PHE HE1    H N N 427 
PHE HE2    H N N 428 
PHE HZ     H N N 429 
PHE HXT    H N N 430 
PRO N      N N N 431 
PRO CA     C N S 432 
PRO C      C N N 433 
PRO O      O N N 434 
PRO CB     C N N 435 
PRO CG     C N N 436 
PRO CD     C N N 437 
PRO OXT    O N N 438 
PRO H      H N N 439 
PRO HA     H N N 440 
PRO HB2    H N N 441 
PRO HB3    H N N 442 
PRO HG2    H N N 443 
PRO HG3    H N N 444 
PRO HD2    H N N 445 
PRO HD3    H N N 446 
PRO HXT    H N N 447 
SER N      N N N 448 
SER CA     C N S 449 
SER C      C N N 450 
SER O      O N N 451 
SER CB     C N N 452 
SER OG     O N N 453 
SER OXT    O N N 454 
SER H      H N N 455 
SER H2     H N N 456 
SER HA     H N N 457 
SER HB2    H N N 458 
SER HB3    H N N 459 
SER HG     H N N 460 
SER HXT    H N N 461 
SO4 S      S N N 462 
SO4 O1     O N N 463 
SO4 O2     O N N 464 
SO4 O3     O N N 465 
SO4 O4     O N N 466 
THR N      N N N 467 
THR CA     C N S 468 
THR C      C N N 469 
THR O      O N N 470 
THR CB     C N R 471 
THR OG1    O N N 472 
THR CG2    C N N 473 
THR OXT    O N N 474 
THR H      H N N 475 
THR H2     H N N 476 
THR HA     H N N 477 
THR HB     H N N 478 
THR HG1    H N N 479 
THR HG21   H N N 480 
THR HG22   H N N 481 
THR HG23   H N N 482 
THR HXT    H N N 483 
TRP N      N N N 484 
TRP CA     C N S 485 
TRP C      C N N 486 
TRP O      O N N 487 
TRP CB     C N N 488 
TRP CG     C Y N 489 
TRP CD1    C Y N 490 
TRP CD2    C Y N 491 
TRP NE1    N Y N 492 
TRP CE2    C Y N 493 
TRP CE3    C Y N 494 
TRP CZ2    C Y N 495 
TRP CZ3    C Y N 496 
TRP CH2    C Y N 497 
TRP OXT    O N N 498 
TRP H      H N N 499 
TRP H2     H N N 500 
TRP HA     H N N 501 
TRP HB2    H N N 502 
TRP HB3    H N N 503 
TRP HD1    H N N 504 
TRP HE1    H N N 505 
TRP HE3    H N N 506 
TRP HZ2    H N N 507 
TRP HZ3    H N N 508 
TRP HH2    H N N 509 
TRP HXT    H N N 510 
TYR N      N N N 511 
TYR CA     C N S 512 
TYR C      C N N 513 
TYR O      O N N 514 
TYR CB     C N N 515 
TYR CG     C Y N 516 
TYR CD1    C Y N 517 
TYR CD2    C Y N 518 
TYR CE1    C Y N 519 
TYR CE2    C Y N 520 
TYR CZ     C Y N 521 
TYR OH     O N N 522 
TYR OXT    O N N 523 
TYR H      H N N 524 
TYR H2     H N N 525 
TYR HA     H N N 526 
TYR HB2    H N N 527 
TYR HB3    H N N 528 
TYR HD1    H N N 529 
TYR HD2    H N N 530 
TYR HE1    H N N 531 
TYR HE2    H N N 532 
TYR HH     H N N 533 
TYR HXT    H N N 534 
VAL N      N N N 535 
VAL CA     C N S 536 
VAL C      C N N 537 
VAL O      O N N 538 
VAL CB     C N N 539 
VAL CG1    C N N 540 
VAL CG2    C N N 541 
VAL OXT    O N N 542 
VAL H      H N N 543 
VAL H2     H N N 544 
VAL HA     H N N 545 
VAL HB     H N N 546 
VAL HG11   H N N 547 
VAL HG12   H N N 548 
VAL HG13   H N N 549 
VAL HG21   H N N 550 
VAL HG22   H N N 551 
VAL HG23   H N N 552 
VAL HXT    H N N 553 
# 
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 
NAD PA    O1A    doub N N 329 
NAD PA    O2A    sing N N 330 
NAD PA    O5B    sing N N 331 
NAD PA    O3     sing N N 332 
NAD O2A   HOA2   sing N N 333 
NAD O5B   C5B    sing N N 334 
NAD C5B   C4B    sing N N 335 
NAD C5B   H51A   sing N N 336 
NAD C5B   H52A   sing N N 337 
NAD C4B   O4B    sing N N 338 
NAD C4B   C3B    sing N N 339 
NAD C4B   H4B    sing N N 340 
NAD O4B   C1B    sing N N 341 
NAD C3B   O3B    sing N N 342 
NAD C3B   C2B    sing N N 343 
NAD C3B   H3B    sing N N 344 
NAD O3B   HO3A   sing N N 345 
NAD C2B   O2B    sing N N 346 
NAD C2B   C1B    sing N N 347 
NAD C2B   H2B    sing N N 348 
NAD O2B   HO2A   sing N N 349 
NAD C1B   N9A    sing N N 350 
NAD C1B   H1B    sing N N 351 
NAD N9A   C8A    sing Y N 352 
NAD N9A   C4A    sing Y N 353 
NAD C8A   N7A    doub Y N 354 
NAD C8A   H8A    sing N N 355 
NAD N7A   C5A    sing Y N 356 
NAD C5A   C6A    sing Y N 357 
NAD C5A   C4A    doub Y N 358 
NAD C6A   N6A    sing N N 359 
NAD C6A   N1A    doub Y N 360 
NAD N6A   H61A   sing N N 361 
NAD N6A   H62A   sing N N 362 
NAD N1A   C2A    sing Y N 363 
NAD C2A   N3A    doub Y N 364 
NAD C2A   H2A    sing N N 365 
NAD N3A   C4A    sing Y N 366 
NAD O3    PN     sing N N 367 
NAD PN    O1N    doub N N 368 
NAD PN    O2N    sing N N 369 
NAD PN    O5D    sing N N 370 
NAD O5D   C5D    sing N N 371 
NAD C5D   C4D    sing N N 372 
NAD C5D   H51N   sing N N 373 
NAD C5D   H52N   sing N N 374 
NAD C4D   O4D    sing N N 375 
NAD C4D   C3D    sing N N 376 
NAD C4D   H4D    sing N N 377 
NAD O4D   C1D    sing N N 378 
NAD C3D   O3D    sing N N 379 
NAD C3D   C2D    sing N N 380 
NAD C3D   H3D    sing N N 381 
NAD O3D   HO3N   sing N N 382 
NAD C2D   O2D    sing N N 383 
NAD C2D   C1D    sing N N 384 
NAD C2D   H2D    sing N N 385 
NAD O2D   HO2N   sing N N 386 
NAD C1D   N1N    sing N N 387 
NAD C1D   H1D    sing N N 388 
NAD N1N   C2N    sing Y N 389 
NAD N1N   C6N    doub Y N 390 
NAD C2N   C3N    doub Y N 391 
NAD C2N   H2N    sing N N 392 
NAD C3N   C7N    sing N N 393 
NAD C3N   C4N    sing Y N 394 
NAD C7N   O7N    doub N N 395 
NAD C7N   N7N    sing N N 396 
NAD N7N   H71N   sing N N 397 
NAD N7N   H72N   sing N N 398 
NAD C4N   C5N    doub Y N 399 
NAD C4N   H4N    sing N N 400 
NAD C5N   C6N    sing Y N 401 
NAD C5N   H5N    sing N N 402 
NAD C6N   H6N    sing N N 403 
PHE N     CA     sing N N 404 
PHE N     H      sing N N 405 
PHE N     H2     sing N N 406 
PHE CA    C      sing N N 407 
PHE CA    CB     sing N N 408 
PHE CA    HA     sing N N 409 
PHE C     O      doub N N 410 
PHE C     OXT    sing N N 411 
PHE CB    CG     sing N N 412 
PHE CB    HB2    sing N N 413 
PHE CB    HB3    sing N N 414 
PHE CG    CD1    doub Y N 415 
PHE CG    CD2    sing Y N 416 
PHE CD1   CE1    sing Y N 417 
PHE CD1   HD1    sing N N 418 
PHE CD2   CE2    doub Y N 419 
PHE CD2   HD2    sing N N 420 
PHE CE1   CZ     doub Y N 421 
PHE CE1   HE1    sing N N 422 
PHE CE2   CZ     sing Y N 423 
PHE CE2   HE2    sing N N 424 
PHE CZ    HZ     sing N N 425 
PHE OXT   HXT    sing N N 426 
PRO N     CA     sing N N 427 
PRO N     CD     sing N N 428 
PRO N     H      sing N N 429 
PRO CA    C      sing N N 430 
PRO CA    CB     sing N N 431 
PRO CA    HA     sing N N 432 
PRO C     O      doub N N 433 
PRO C     OXT    sing N N 434 
PRO CB    CG     sing N N 435 
PRO CB    HB2    sing N N 436 
PRO CB    HB3    sing N N 437 
PRO CG    CD     sing N N 438 
PRO CG    HG2    sing N N 439 
PRO CG    HG3    sing N N 440 
PRO CD    HD2    sing N N 441 
PRO CD    HD3    sing N N 442 
PRO OXT   HXT    sing N N 443 
SER N     CA     sing N N 444 
SER N     H      sing N N 445 
SER N     H2     sing N N 446 
SER CA    C      sing N N 447 
SER CA    CB     sing N N 448 
SER CA    HA     sing N N 449 
SER C     O      doub N N 450 
SER C     OXT    sing N N 451 
SER CB    OG     sing N N 452 
SER CB    HB2    sing N N 453 
SER CB    HB3    sing N N 454 
SER OG    HG     sing N N 455 
SER OXT   HXT    sing N N 456 
SO4 S     O1     doub N N 457 
SO4 S     O2     doub N N 458 
SO4 S     O3     sing N N 459 
SO4 S     O4     sing N N 460 
THR N     CA     sing N N 461 
THR N     H      sing N N 462 
THR N     H2     sing N N 463 
THR CA    C      sing N N 464 
THR CA    CB     sing N N 465 
THR CA    HA     sing N N 466 
THR C     O      doub N N 467 
THR C     OXT    sing N N 468 
THR CB    OG1    sing N N 469 
THR CB    CG2    sing N N 470 
THR CB    HB     sing N N 471 
THR OG1   HG1    sing N N 472 
THR CG2   HG21   sing N N 473 
THR CG2   HG22   sing N N 474 
THR CG2   HG23   sing N N 475 
THR OXT   HXT    sing N N 476 
TRP N     CA     sing N N 477 
TRP N     H      sing N N 478 
TRP N     H2     sing N N 479 
TRP CA    C      sing N N 480 
TRP CA    CB     sing N N 481 
TRP CA    HA     sing N N 482 
TRP C     O      doub N N 483 
TRP C     OXT    sing N N 484 
TRP CB    CG     sing N N 485 
TRP CB    HB2    sing N N 486 
TRP CB    HB3    sing N N 487 
TRP CG    CD1    doub Y N 488 
TRP CG    CD2    sing Y N 489 
TRP CD1   NE1    sing Y N 490 
TRP CD1   HD1    sing N N 491 
TRP CD2   CE2    doub Y N 492 
TRP CD2   CE3    sing Y N 493 
TRP NE1   CE2    sing Y N 494 
TRP NE1   HE1    sing N N 495 
TRP CE2   CZ2    sing Y N 496 
TRP CE3   CZ3    doub Y N 497 
TRP CE3   HE3    sing N N 498 
TRP CZ2   CH2    doub Y N 499 
TRP CZ2   HZ2    sing N N 500 
TRP CZ3   CH2    sing Y N 501 
TRP CZ3   HZ3    sing N N 502 
TRP CH2   HH2    sing N N 503 
TRP OXT   HXT    sing N N 504 
TYR N     CA     sing N N 505 
TYR N     H      sing N N 506 
TYR N     H2     sing N N 507 
TYR CA    C      sing N N 508 
TYR CA    CB     sing N N 509 
TYR CA    HA     sing N N 510 
TYR C     O      doub N N 511 
TYR C     OXT    sing N N 512 
TYR CB    CG     sing N N 513 
TYR CB    HB2    sing N N 514 
TYR CB    HB3    sing N N 515 
TYR CG    CD1    doub Y N 516 
TYR CG    CD2    sing Y N 517 
TYR CD1   CE1    sing Y N 518 
TYR CD1   HD1    sing N N 519 
TYR CD2   CE2    doub Y N 520 
TYR CD2   HD2    sing N N 521 
TYR CE1   CZ     doub Y N 522 
TYR CE1   HE1    sing N N 523 
TYR CE2   CZ     sing Y N 524 
TYR CE2   HE2    sing N N 525 
TYR CZ    OH     sing N N 526 
TYR OH    HH     sing N N 527 
TYR OXT   HXT    sing N N 528 
VAL N     CA     sing N N 529 
VAL N     H      sing N N 530 
VAL N     H2     sing N N 531 
VAL CA    C      sing N N 532 
VAL CA    CB     sing N N 533 
VAL CA    HA     sing N N 534 
VAL C     O      doub N N 535 
VAL C     OXT    sing N N 536 
VAL CB    CG1    sing N N 537 
VAL CB    CG2    sing N N 538 
VAL CB    HB     sing N N 539 
VAL CG1   HG11   sing N N 540 
VAL CG1   HG12   sing N N 541 
VAL CG1   HG13   sing N N 542 
VAL CG2   HG21   sing N N 543 
VAL CG2   HG22   sing N N 544 
VAL CG2   HG23   sing N N 545 
VAL OXT   HXT    sing N N 546 
# 
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          ? 
# 
_atom_sites.entry_id                    8YO8 
_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]   0.016622 
_atom_sites.fract_transf_matrix[1][2]   0.009597 
_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]   0.019193 
_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]   0.005121 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . PRO A 1 1   ? 45.233 25.596  41.970  1.00 44.79 ?  7   PRO A N     1 
ATOM   2    C CA    . PRO A 1 1   ? 44.662 26.545  42.929  1.00 42.39 ?  7   PRO A CA    1 
ATOM   3    C C     . PRO A 1 1   ? 44.040 27.748  42.234  1.00 40.21 ?  7   PRO A C     1 
ATOM   4    O O     . PRO A 1 1   ? 44.746 28.618  41.730  1.00 40.30 ?  7   PRO A O     1 
ATOM   5    C CB    . PRO A 1 1   ? 45.868 26.961  43.780  1.00 44.84 ?  7   PRO A CB    1 
ATOM   6    C CG    . PRO A 1 1   ? 47.096 26.609  42.969  1.00 45.99 ?  7   PRO A CG    1 
ATOM   7    C CD    . PRO A 1 1   ? 46.671 25.842  41.751  1.00 48.00 ?  7   PRO A CD    1 
ATOM   8    N N     . HIS A 1 2   ? 42.714 27.795  42.203  1.00 38.41 ?  8   HIS A N     1 
ATOM   9    C CA    . HIS A 1 2   ? 42.031 28.915  41.581  1.00 36.47 ?  8   HIS A CA    1 
ATOM   10   C C     . HIS A 1 2   ? 41.792 30.081  42.530  1.00 36.75 ?  8   HIS A C     1 
ATOM   11   O O     . HIS A 1 2   ? 41.426 31.165  42.064  1.00 35.54 ?  8   HIS A O     1 
ATOM   12   C CB    . HIS A 1 2   ? 40.723 28.432  40.982  1.00 34.48 ?  8   HIS A CB    1 
ATOM   13   C CG    . HIS A 1 2   ? 40.928 27.483  39.845  1.00 37.21 ?  8   HIS A CG    1 
ATOM   14   N ND1   . HIS A 1 2   ? 41.032 27.907  38.536  1.00 34.57 ?  8   HIS A ND1   1 
ATOM   15   C CD2   . HIS A 1 2   ? 41.114 26.142  39.827  1.00 37.44 ?  8   HIS A CD2   1 
ATOM   16   C CE1   . HIS A 1 2   ? 41.239 26.861  37.756  1.00 38.38 ?  8   HIS A CE1   1 
ATOM   17   N NE2   . HIS A 1 2   ? 41.291 25.779  38.514  1.00 42.93 ?  8   HIS A NE2   1 
ATOM   18   N N     . MET A 1 3   ? 42.020 29.889  43.835  1.00 38.47 ?  9   MET A N     1 
ATOM   19   C CA    . MET A 1 3   ? 41.920 30.957  44.829  1.00 39.10 ?  9   MET A CA    1 
ATOM   20   C C     . MET A 1 3   ? 40.597 31.708  44.723  1.00 37.27 ?  9   MET A C     1 
ATOM   21   O O     . MET A 1 3   ? 40.547 32.934  44.787  1.00 36.99 ?  9   MET A O     1 
ATOM   22   C CB    . MET A 1 3   ? 43.104 31.912  44.718  1.00 40.11 ?  9   MET A CB    1 
ATOM   23   C CG    . MET A 1 3   ? 44.440 31.204  44.848  1.00 42.17 ?  9   MET A CG    1 
ATOM   24   S SD    . MET A 1 3   ? 45.831 32.341  44.953  1.00 43.81 ?  9   MET A SD    1 
ATOM   25   C CE    . MET A 1 3   ? 47.202 31.191  45.007  1.00 46.23 ?  9   MET A CE    1 
ATOM   26   N N     . GLY A 1 4   ? 39.511 30.960  44.545  1.00 36.13 ?  10  GLY A N     1 
ATOM   27   C CA    . GLY A 1 4   ? 38.180 31.510  44.511  1.00 34.64 ?  10  GLY A CA    1 
ATOM   28   C C     . GLY A 1 4   ? 37.639 31.800  43.125  1.00 32.55 ?  10  GLY A C     1 
ATOM   29   O O     . GLY A 1 4   ? 36.418 31.860  42.960  1.00 35.10 ?  10  GLY A O     1 
ATOM   30   N N     . ALA A 1 5   ? 38.505 31.969  42.128  1.00 32.30 ?  11  ALA A N     1 
ATOM   31   C CA    . ALA A 1 5   ? 38.056 32.311  40.783  1.00 31.26 ?  11  ALA A CA    1 
ATOM   32   C C     . ALA A 1 5   ? 37.364 31.130  40.110  1.00 29.89 ?  11  ALA A C     1 
ATOM   33   O O     . ALA A 1 5   ? 37.645 29.965  40.400  1.00 30.19 ?  11  ALA A O     1 
ATOM   34   C CB    . ALA A 1 5   ? 39.237 32.765  39.929  1.00 30.86 ?  11  ALA A CB    1 
ATOM   35   N N     . LEU A 1 6   ? 36.459 31.442  39.183  1.00 30.26 ?  12  LEU A N     1 
ATOM   36   C CA    . LEU A 1 6   ? 35.794 30.416  38.386  1.00 31.49 ?  12  LEU A CA    1 
ATOM   37   C C     . LEU A 1 6   ? 36.599 30.094  37.138  1.00 30.11 ?  12  LEU A C     1 
ATOM   38   O O     . LEU A 1 6   ? 37.049 30.998  36.425  1.00 31.85 ?  12  LEU A O     1 
ATOM   39   C CB    . LEU A 1 6   ? 34.395 30.855  37.952  1.00 30.30 ?  12  LEU A CB    1 
ATOM   40   C CG    . LEU A 1 6   ? 33.329 31.170  38.995  1.00 30.73 ?  12  LEU A CG    1 
ATOM   41   C CD1   . LEU A 1 6   ? 31.994 31.256  38.295  1.00 29.12 ?  12  LEU A CD1   1 
ATOM   42   C CD2   . LEU A 1 6   ? 33.304 30.098  40.055  1.00 32.85 ?  12  LEU A CD2   1 
ATOM   43   N N     . HIS A 1 7   ? 36.750 28.806  36.860  1.00 29.67 ?  13  HIS A N     1 
ATOM   44   C CA    . HIS A 1 7   ? 37.116 28.345  35.531  1.00 27.81 ?  13  HIS A CA    1 
ATOM   45   C C     . HIS A 1 7   ? 36.372 27.038  35.311  1.00 31.51 ?  13  HIS A C     1 
ATOM   46   O O     . HIS A 1 7   ? 36.713 26.017  35.918  1.00 26.40 ?  13  HIS A O     1 
ATOM   47   C CB    . HIS A 1 7   ? 38.624 28.160  35.338  1.00 29.70 ?  13  HIS A CB    1 
ATOM   48   C CG    . HIS A 1 7   ? 38.983 27.831  33.913  1.00 35.37 ?  13  HIS A CG    1 
ATOM   49   N ND1   . HIS A 1 7   ? 39.686 26.699  33.549  1.00 36.76 ?  13  HIS A ND1   1 
ATOM   50   C CD2   . HIS A 1 7   ? 38.664 28.457  32.753  1.00 32.87 ?  13  HIS A CD2   1 
ATOM   51   C CE1   . HIS A 1 7   ? 39.809 26.658  32.234  1.00 35.59 ?  13  HIS A CE1   1 
ATOM   52   N NE2   . HIS A 1 7   ? 39.195 27.712  31.725  1.00 35.38 ?  13  HIS A NE2   1 
ATOM   53   N N     . VAL A 1 8   ? 35.351 27.080  34.458  1.00 26.35 ?  14  VAL A N     1 
ATOM   54   C CA    . VAL A 1 8   ? 34.505 25.930  34.181  1.00 26.38 ?  14  VAL A CA    1 
ATOM   55   C C     . VAL A 1 8   ? 35.067 25.179  32.985  1.00 27.79 ?  14  VAL A C     1 
ATOM   56   O O     . VAL A 1 8   ? 35.449 25.782  31.982  1.00 24.55 ?  14  VAL A O     1 
ATOM   57   C CB    . VAL A 1 8   ? 33.053 26.367  33.912  1.00 24.30 ?  14  VAL A CB    1 
ATOM   58   C CG1   . VAL A 1 8   ? 32.135 25.138  33.814  1.00 22.08 ?  14  VAL A CG1   1 
ATOM   59   C CG2   . VAL A 1 8   ? 32.583 27.325  34.991  1.00 22.01 ?  14  VAL A CG2   1 
ATOM   60   N N     . VAL A 1 9   ? 35.104 23.857  33.078  1.00 24.74 ?  15  VAL A N     1 
ATOM   61   C CA    . VAL A 1 9   ? 35.457 23.018  31.948  1.00 23.50 ?  15  VAL A CA    1 
ATOM   62   C C     . VAL A 1 9   ? 34.226 22.208  31.587  1.00 22.16 ?  15  VAL A C     1 
ATOM   63   O O     . VAL A 1 9   ? 33.605 21.599  32.466  1.00 22.45 ?  15  VAL A O     1 
ATOM   64   C CB    . VAL A 1 9   ? 36.664 22.119  32.268  1.00 26.70 ?  15  VAL A CB    1 
ATOM   65   C CG1   . VAL A 1 9   ? 36.995 21.227  31.077  1.00 26.03 ?  15  VAL A CG1   1 
ATOM   66   C CG2   . VAL A 1 9   ? 37.870 22.986  32.652  1.00 27.52 ?  15  VAL A CG2   1 
ATOM   67   N N     . ILE A 1 10  ? 33.851 22.250  30.305  1.00 22.79 ?  16  ILE A N     1 
ATOM   68   C CA    . ILE A 1 10  ? 32.768 21.450  29.735  1.00 22.07 ?  16  ILE A CA    1 
ATOM   69   C C     . ILE A 1 10  ? 33.397 20.356  28.889  1.00 23.55 ?  16  ILE A C     1 
ATOM   70   O O     . ILE A 1 10  ? 34.119 20.656  27.934  1.00 24.37 ?  16  ILE A O     1 
ATOM   71   C CB    . ILE A 1 10  ? 31.834 22.293  28.856  1.00 22.38 ?  16  ILE A CB    1 
ATOM   72   C CG1   . ILE A 1 10  ? 31.360 23.537  29.611  1.00 20.06 ?  16  ILE A CG1   1 
ATOM   73   C CG2   . ILE A 1 10  ? 30.672 21.426  28.366  1.00 20.00 ?  16  ILE A CG2   1 
ATOM   74   C CD1   . ILE A 1 10  ? 30.634 24.504  28.729  1.00 19.43 ?  16  ILE A CD1   1 
ATOM   75   N N     . VAL A 1 11  ? 33.108 19.097  29.207  1.00 23.86 ?  17  VAL A N     1 
ATOM   76   C CA    . VAL A 1 11  ? 33.604 17.972  28.419  1.00 24.57 ?  17  VAL A CA    1 
ATOM   77   C C     . VAL A 1 11  ? 32.447 17.481  27.561  1.00 20.07 ?  17  VAL A C     1 
ATOM   78   O O     . VAL A 1 11  ? 31.500 16.876  28.058  1.00 23.36 ?  17  VAL A O     1 
ATOM   79   C CB    . VAL A 1 11  ? 34.195 16.877  29.305  1.00 28.60 ?  17  VAL A CB    1 
ATOM   80   C CG1   . VAL A 1 11  ? 34.470 15.605  28.492  1.00 25.99 ?  17  VAL A CG1   1 
ATOM   81   C CG2   . VAL A 1 11  ? 35.485 17.389  29.905  1.00 24.65 ?  17  VAL A CG2   1 
ATOM   82   N N     . GLY A 1 12  ? 32.508 17.788  26.267  1.00 21.12 ?  18  GLY A N     1 
ATOM   83   C CA    . GLY A 1 12  ? 31.486 17.405  25.303  1.00 21.27 ?  18  GLY A CA    1 
ATOM   84   C C     . GLY A 1 12  ? 30.804 18.615  24.686  1.00 21.25 ?  18  GLY A C     1 
ATOM   85   O O     . GLY A 1 12  ? 30.231 19.439  25.414  1.00 17.00 ?  18  GLY A O     1 
ATOM   86   N N     . GLY A 1 13  ? 30.864 18.742  23.356  1.00 18.97 ?  19  GLY A N     1 
ATOM   87   C CA    . GLY A 1 13  ? 30.268 19.870  22.658  1.00 17.15 ?  19  GLY A CA    1 
ATOM   88   C C     . GLY A 1 13  ? 29.014 19.509  21.884  1.00 17.45 ?  19  GLY A C     1 
ATOM   89   O O     . GLY A 1 13  ? 28.863 19.836  20.696  1.00 16.03 ?  19  GLY A O     1 
ATOM   90   N N     . GLY A 1 14  ? 28.118 18.796  22.551  1.00 18.17 ?  20  GLY A N     1 
ATOM   91   C CA    . GLY A 1 14  ? 26.845 18.413  21.991  1.00 16.81 ?  20  GLY A CA    1 
ATOM   92   C C     . GLY A 1 14  ? 25.794 19.448  22.298  1.00 15.81 ?  20  GLY A C     1 
ATOM   93   O O     . GLY A 1 14  ? 26.092 20.614  22.559  1.00 15.34 ?  20  GLY A O     1 
ATOM   94   N N     . PHE A 1 15  ? 24.531 19.014  22.239  1.00 14.27 ?  21  PHE A N     1 
ATOM   95   C CA    . PHE A 1 15  ? 23.424 19.907  22.572  1.00 15.08 ?  21  PHE A CA    1 
ATOM   96   C C     . PHE A 1 15  ? 23.576 20.478  23.978  1.00 17.90 ?  21  PHE A C     1 
ATOM   97   O O     . PHE A 1 15  ? 23.376 21.682  24.197  1.00 14.95 ?  21  PHE A O     1 
ATOM   98   C CB    . PHE A 1 15  ? 22.096 19.165  22.423  1.00 16.76 ?  21  PHE A CB    1 
ATOM   99   C CG    . PHE A 1 15  ? 21.685 18.940  20.995  1.00 16.50 ?  21  PHE A CG    1 
ATOM   100  C CD1   . PHE A 1 15  ? 21.022 19.940  20.281  1.00 16.27 ?  21  PHE A CD1   1 
ATOM   101  C CD2   . PHE A 1 15  ? 21.969 17.741  20.353  1.00 18.36 ?  21  PHE A CD2   1 
ATOM   102  C CE1   . PHE A 1 15  ? 20.631 19.729  18.958  1.00 16.62 ?  21  PHE A CE1   1 
ATOM   103  C CE2   . PHE A 1 15  ? 21.589 17.538  19.013  1.00 15.23 ?  21  PHE A CE2   1 
ATOM   104  C CZ    . PHE A 1 15  ? 20.927 18.527  18.333  1.00 16.76 ?  21  PHE A CZ    1 
ATOM   105  N N     . GLY A 1 16  ? 23.950 19.644  24.941  1.00 15.05 ?  22  GLY A N     1 
ATOM   106  C CA    . GLY A 1 16  ? 24.158 20.161  26.286  1.00 16.64 ?  22  GLY A CA    1 
ATOM   107  C C     . GLY A 1 16  ? 25.347 21.104  26.355  1.00 18.05 ?  22  GLY A C     1 
ATOM   108  O O     . GLY A 1 16  ? 25.259 22.201  26.919  1.00 17.07 ?  22  GLY A O     1 
ATOM   109  N N     . GLY A 1 17  ? 26.469 20.707  25.751  1.00 18.09 ?  23  GLY A N     1 
ATOM   110  C CA    . GLY A 1 17  ? 27.690 21.484  25.910  1.00 17.55 ?  23  GLY A CA    1 
ATOM   111  C C     . GLY A 1 17  ? 27.651 22.844  25.226  1.00 20.08 ?  23  GLY A C     1 
ATOM   112  O O     . GLY A 1 17  ? 28.202 23.817  25.748  1.00 18.30 ?  23  GLY A O     1 
ATOM   113  N N     . ILE A 1 18  ? 27.021 22.939  24.045  1.00 15.33 ?  24  ILE A N     1 
ATOM   114  C CA    . ILE A 1 18  ? 27.012 24.252  23.404  1.00 15.80 ?  24  ILE A CA    1 
ATOM   115  C C     . ILE A 1 18  ? 26.038 25.181  24.108  1.00 17.42 ?  24  ILE A C     1 
ATOM   116  O O     . ILE A 1 18  ? 26.239 26.401  24.112  1.00 16.12 ?  24  ILE A O     1 
ATOM   117  C CB    . ILE A 1 18  ? 26.718 24.192  21.882  1.00 15.09 ?  24  ILE A CB    1 
ATOM   118  C CG1   . ILE A 1 18  ? 25.314 23.663  21.581  1.00 16.07 ?  24  ILE A CG1   1 
ATOM   119  C CG2   . ILE A 1 18  ? 27.793 23.418  21.137  1.00 13.78 ?  24  ILE A CG2   1 
ATOM   120  C CD1   . ILE A 1 18  ? 24.840 23.979  20.123  1.00 14.96 ?  24  ILE A CD1   1 
ATOM   121  N N     . ALA A 1 19  ? 24.975 24.646  24.712  1.00 15.01 ?  25  ALA A N     1 
ATOM   122  C CA    . ALA A 1 19  ? 24.101 25.499  25.512  1.00 18.81 ?  25  ALA A CA    1 
ATOM   123  C C     . ALA A 1 19  ? 24.822 26.003  26.750  1.00 18.51 ?  25  ALA A C     1 
ATOM   124  O O     . ALA A 1 19  ? 24.741 27.194  27.082  1.00 18.56 ?  25  ALA A O     1 
ATOM   125  C CB    . ALA A 1 19  ? 22.836 24.751  25.915  1.00 17.67 ?  25  ALA A CB    1 
ATOM   126  N N     . ALA A 1 20  ? 25.537 25.115  27.445  1.00 18.06 ?  26  ALA A N     1 
ATOM   127  C CA    . ALA A 1 20  ? 26.310 25.545  28.612  1.00 20.70 ?  26  ALA A CA    1 
ATOM   128  C C     . ALA A 1 20  ? 27.358 26.576  28.220  1.00 18.67 ?  26  ALA A C     1 
ATOM   129  O O     . ALA A 1 20  ? 27.503 27.617  28.879  1.00 19.88 ?  26  ALA A O     1 
ATOM   130  C CB    . ALA A 1 20  ? 26.973 24.345  29.288  1.00 16.19 ?  26  ALA A CB    1 
ATOM   131  N N     . ALA A 1 21  ? 28.084 26.313  27.128  1.00 18.86 ?  27  ALA A N     1 
ATOM   132  C CA    . ALA A 1 21  ? 29.160 27.208  26.710  1.00 17.59 ?  27  ALA A CA    1 
ATOM   133  C C     . ALA A 1 21  ? 28.613 28.563  26.306  1.00 19.96 ?  27  ALA A C     1 
ATOM   134  O O     . ALA A 1 21  ? 29.226 29.603  26.586  1.00 17.59 ?  27  ALA A O     1 
ATOM   135  C CB    . ALA A 1 21  ? 29.933 26.582  25.548  1.00 16.98 ?  27  ALA A CB    1 
ATOM   136  N N     . SER A 1 22  ? 27.473 28.563  25.611  1.00 17.36 ?  28  SER A N     1 
ATOM   137  C CA    . SER A 1 22  ? 26.862 29.808  25.178  1.00 20.87 ?  28  SER A CA    1 
ATOM   138  C C     . SER A 1 22  ? 26.421 30.643  26.371  1.00 23.59 ?  28  SER A C     1 
ATOM   139  O O     . SER A 1 22  ? 26.573 31.871  26.366  1.00 21.22 ?  28  SER A O     1 
ATOM   140  C CB    . SER A 1 22  ? 25.675 29.520  24.257  1.00 21.83 ?  28  SER A CB    1 
ATOM   141  O OG    . SER A 1 22  ? 25.015 30.735  23.932  1.00 30.45 ?  28  SER A OG    1 
ATOM   142  N N     . GLN A 1 23  ? 25.864 30.002  27.404  1.00 18.98 ?  29  GLN A N     1 
ATOM   143  C CA    . GLN A 1 23  ? 25.459 30.775  28.572  1.00 25.14 ?  29  GLN A CA    1 
ATOM   144  C C     . GLN A 1 23  ? 26.670 31.288  29.346  1.00 23.07 ?  29  GLN A C     1 
ATOM   145  O O     . GLN A 1 23  ? 26.681 32.443  29.798  1.00 21.36 ?  29  GLN A O     1 
ATOM   146  C CB    . GLN A 1 23  ? 24.556 29.952  29.478  1.00 24.22 ?  29  GLN A CB    1 
ATOM   147  C CG    . GLN A 1 23  ? 24.243 30.695  30.772  1.00 31.79 ?  29  GLN A CG    1 
ATOM   148  C CD    . GLN A 1 23  ? 22.766 30.786  31.070  1.00 37.55 ?  29  GLN A CD    1 
ATOM   149  O OE1   . GLN A 1 23  ? 21.985 29.902  30.686  1.00 45.98 ?  29  GLN A OE1   1 
ATOM   150  N NE2   . GLN A 1 23  ? 22.367 31.861  31.758  1.00 40.88 ?  29  GLN A NE2   1 
ATOM   151  N N     . LEU A 1 24  ? 27.699 30.449  29.514  1.00 21.31 ?  30  LEU A N     1 
ATOM   152  C CA    . LEU A 1 24  ? 28.903 30.903  30.207  1.00 19.75 ?  30  LEU A CA    1 
ATOM   153  C C     . LEU A 1 24  ? 29.550 32.064  29.467  1.00 21.98 ?  30  LEU A C     1 
ATOM   154  O O     . LEU A 1 24  ? 29.994 33.039  30.088  1.00 19.38 ?  30  LEU A O     1 
ATOM   155  C CB    . LEU A 1 24  ? 29.879 29.741  30.372  1.00 20.79 ?  30  LEU A CB    1 
ATOM   156  C CG    . LEU A 1 24  ? 29.508 28.706  31.448  1.00 19.34 ?  30  LEU A CG    1 
ATOM   157  C CD1   . LEU A 1 24  ? 30.225 27.394  31.198  1.00 20.30 ?  30  LEU A CD1   1 
ATOM   158  C CD2   . LEU A 1 24  ? 29.836 29.214  32.842  1.00 18.14 ?  30  LEU A CD2   1 
ATOM   159  N N     . GLN A 1 25  ? 29.585 31.988  28.132  1.00 20.91 ?  31  GLN A N     1 
ATOM   160  C CA    . GLN A 1 25  ? 30.122 33.079  27.322  1.00 21.50 ?  31  GLN A CA    1 
ATOM   161  C C     . GLN A 1 25  ? 29.336 34.368  27.530  1.00 22.39 ?  31  GLN A C     1 
ATOM   162  O O     . GLN A 1 25  ? 29.924 35.447  27.617  1.00 25.09 ?  31  GLN A O     1 
ATOM   163  C CB    . GLN A 1 25  ? 30.110 32.686  25.842  1.00 21.50 ?  31  GLN A CB    1 
ATOM   164  C CG    . GLN A 1 25  ? 30.918 33.598  24.943  1.00 23.72 ?  31  GLN A CG    1 
ATOM   165  C CD    . GLN A 1 25  ? 30.951 33.092  23.525  1.00 27.94 ?  31  GLN A CD    1 
ATOM   166  O OE1   . GLN A 1 25  ? 29.964 33.185  22.814  1.00 31.65 ?  31  GLN A OE1   1 
ATOM   167  N NE2   . GLN A 1 25  ? 32.066 32.503  23.126  1.00 24.29 ?  31  GLN A NE2   1 
ATOM   168  N N     . ALA A 1 26  ? 28.004 34.285  27.600  1.00 23.93 ?  32  ALA A N     1 
ATOM   169  C CA    . ALA A 1 26  ? 27.201 35.497  27.783  1.00 25.36 ?  32  ALA A CA    1 
ATOM   170  C C     . ALA A 1 26  ? 27.334 36.077  29.189  1.00 23.88 ?  32  ALA A C     1 
ATOM   171  O O     . ALA A 1 26  ? 27.163 37.289  29.383  1.00 25.11 ?  32  ALA A O     1 
ATOM   172  C CB    . ALA A 1 26  ? 25.730 35.207  27.474  1.00 25.00 ?  32  ALA A CB    1 
ATOM   173  N N     . LEU A 1 27  ? 27.613 35.242  30.183  1.00 23.28 ?  33  LEU A N     1 
ATOM   174  C CA    . LEU A 1 27  ? 27.864 35.735  31.535  1.00 23.36 ?  33  LEU A CA    1 
ATOM   175  C C     . LEU A 1 27  ? 29.294 36.228  31.739  1.00 23.61 ?  33  LEU A C     1 
ATOM   176  O O     . LEU A 1 27  ? 29.596 36.747  32.823  1.00 26.62 ?  33  LEU A O     1 
ATOM   177  C CB    . LEU A 1 27  ? 27.565 34.633  32.561  1.00 21.52 ?  33  LEU A CB    1 
ATOM   178  C CG    . LEU A 1 27  ? 26.112 34.180  32.624  1.00 24.37 ?  33  LEU A CG    1 
ATOM   179  C CD1   . LEU A 1 27  ? 25.979 32.888  33.455  1.00 22.89 ?  33  LEU A CD1   1 
ATOM   180  C CD2   . LEU A 1 27  ? 25.232 35.313  33.167  1.00 20.29 ?  33  LEU A CD2   1 
ATOM   181  N N     . ASN A 1 28  ? 30.168 36.064  30.741  1.00 22.33 ?  34  ASN A N     1 
ATOM   182  C CA    . ASN A 1 28  ? 31.600 36.383  30.818  1.00 24.24 ?  34  ASN A CA    1 
ATOM   183  C C     . ASN A 1 28  ? 32.311 35.558  31.900  1.00 27.03 ?  34  ASN A C     1 
ATOM   184  O O     . ASN A 1 28  ? 33.229 36.039  32.573  1.00 26.25 ?  34  ASN A O     1 
ATOM   185  C CB    . ASN A 1 28  ? 31.830 37.890  31.023  1.00 26.13 ?  34  ASN A CB    1 
ATOM   186  C CG    . ASN A 1 28  ? 33.217 38.353  30.542  1.00 31.16 ?  34  ASN A CG    1 
ATOM   187  O OD1   . ASN A 1 28  ? 33.892 37.660  29.771  1.00 33.67 ?  34  ASN A OD1   1 
ATOM   188  N ND2   . ASN A 1 28  ? 33.637 39.530  30.986  1.00 31.56 ?  34  ASN A ND2   1 
ATOM   189  N N     . VAL A 1 29  ? 31.902 34.306  32.082  1.00 24.13 ?  35  VAL A N     1 
ATOM   190  C CA    . VAL A 1 29  ? 32.525 33.438  33.080  1.00 24.59 ?  35  VAL A CA    1 
ATOM   191  C C     . VAL A 1 29  ? 33.634 32.669  32.365  1.00 25.66 ?  35  VAL A C     1 
ATOM   192  O O     . VAL A 1 29  ? 33.392 32.110  31.285  1.00 22.67 ?  35  VAL A O     1 
ATOM   193  C CB    . VAL A 1 29  ? 31.493 32.502  33.734  1.00 23.53 ?  35  VAL A CB    1 
ATOM   194  C CG1   . VAL A 1 29  ? 32.177 31.402  34.550  1.00 20.72 ?  35  VAL A CG1   1 
ATOM   195  C CG2   . VAL A 1 29  ? 30.544 33.296  34.620  1.00 23.23 ?  35  VAL A CG2   1 
ATOM   196  N N     . PRO A 1 30  ? 34.859 32.646  32.898  1.00 24.58 ?  36  PRO A N     1 
ATOM   197  C CA    . PRO A 1 30  ? 35.934 31.896  32.232  1.00 26.87 ?  36  PRO A CA    1 
ATOM   198  C C     . PRO A 1 30  ? 35.584 30.419  32.098  1.00 23.95 ?  36  PRO A C     1 
ATOM   199  O O     . PRO A 1 30  ? 35.149 29.769  33.055  1.00 23.33 ?  36  PRO A O     1 
ATOM   200  C CB    . PRO A 1 30  ? 37.144 32.112  33.154  1.00 26.24 ?  36  PRO A CB    1 
ATOM   201  C CG    . PRO A 1 30  ? 36.864 33.399  33.841  1.00 29.57 ?  36  PRO A CG    1 
ATOM   202  C CD    . PRO A 1 30  ? 35.357 33.408  34.052  1.00 27.51 ?  36  PRO A CD    1 
ATOM   203  N N     . PHE A 1 31  ? 35.784 29.886  30.901  1.00 23.26 ?  37  PHE A N     1 
ATOM   204  C CA    . PHE A 1 31  ? 35.481 28.484  30.674  1.00 23.36 ?  37  PHE A CA    1 
ATOM   205  C C     . PHE A 1 31  ? 36.273 28.005  29.476  1.00 24.55 ?  37  PHE A C     1 
ATOM   206  O O     . PHE A 1 31  ? 36.766 28.802  28.673  1.00 23.08 ?  37  PHE A O     1 
ATOM   207  C CB    . PHE A 1 31  ? 33.979 28.232  30.433  1.00 21.58 ?  37  PHE A CB    1 
ATOM   208  C CG    . PHE A 1 31  ? 33.491 28.685  29.081  1.00 21.27 ?  37  PHE A CG    1 
ATOM   209  C CD1   . PHE A 1 31  ? 33.263 30.035  28.825  1.00 23.41 ?  37  PHE A CD1   1 
ATOM   210  C CD2   . PHE A 1 31  ? 33.260 27.762  28.061  1.00 20.79 ?  37  PHE A CD2   1 
ATOM   211  C CE1   . PHE A 1 31  ? 32.809 30.458  27.574  1.00 20.73 ?  37  PHE A CE1   1 
ATOM   212  C CE2   . PHE A 1 31  ? 32.819 28.167  26.802  1.00 19.64 ?  37  PHE A CE2   1 
ATOM   213  C CZ    . PHE A 1 31  ? 32.582 29.508  26.556  1.00 21.82 ?  37  PHE A CZ    1 
ATOM   214  N N     . MET A 1 32  ? 36.349 26.682  29.358  1.00 24.69 ?  38  MET A N     1 
ATOM   215  C CA    . MET A 1 32  ? 36.903 25.992  28.201  1.00 26.25 ?  38  MET A CA    1 
ATOM   216  C C     . MET A 1 32  ? 35.938 24.878  27.808  1.00 24.69 ?  38  MET A C     1 
ATOM   217  O O     . MET A 1 32  ? 35.574 24.042  28.647  1.00 23.02 ?  38  MET A O     1 
ATOM   218  C CB    . MET A 1 32  ? 38.282 25.416  28.534  1.00 28.11 ?  38  MET A CB    1 
ATOM   219  C CG    . MET A 1 32  ? 39.032 24.865  27.328  1.00 33.66 ?  38  MET A CG    1 
ATOM   220  S SD    . MET A 1 32  ? 39.455 26.192  26.187  1.00 38.10 ?  38  MET A SD    1 
ATOM   221  C CE    . MET A 1 32  ? 40.395 27.255  27.298  1.00 36.17 ?  38  MET A CE    1 
ATOM   222  N N     . LEU A 1 33  ? 35.504 24.873  26.556  1.00 23.28 ?  39  LEU A N     1 
ATOM   223  C CA    . LEU A 1 33  ? 34.704 23.774  26.028  1.00 23.97 ?  39  LEU A CA    1 
ATOM   224  C C     . LEU A 1 33  ? 35.609 22.831  25.253  1.00 24.60 ?  39  LEU A C     1 
ATOM   225  O O     . LEU A 1 33  ? 36.376 23.272  24.392  1.00 25.38 ?  39  LEU A O     1 
ATOM   226  C CB    . LEU A 1 33  ? 33.579 24.289  25.131  1.00 22.65 ?  39  LEU A CB    1 
ATOM   227  C CG    . LEU A 1 33  ? 32.848 23.266  24.246  1.00 23.40 ?  39  LEU A CG    1 
ATOM   228  C CD1   . LEU A 1 33  ? 32.006 22.303  25.082  1.00 19.73 ?  39  LEU A CD1   1 
ATOM   229  C CD2   . LEU A 1 33  ? 31.998 23.985  23.215  1.00 18.51 ?  39  LEU A CD2   1 
ATOM   230  N N     . VAL A 1 34  ? 35.513 21.539  25.554  1.00 25.54 ?  40  VAL A N     1 
ATOM   231  C CA    . VAL A 1 34  ? 36.353 20.518  24.936  1.00 24.40 ?  40  VAL A CA    1 
ATOM   232  C C     . VAL A 1 34  ? 35.467 19.555  24.155  1.00 24.55 ?  40  VAL A C     1 
ATOM   233  O O     . VAL A 1 34  ? 34.464 19.056  24.681  1.00 23.84 ?  40  VAL A O     1 
ATOM   234  C CB    . VAL A 1 34  ? 37.182 19.758  25.985  1.00 24.40 ?  40  VAL A CB    1 
ATOM   235  C CG1   . VAL A 1 34  ? 38.222 18.871  25.308  1.00 27.03 ?  40  VAL A CG1   1 
ATOM   236  C CG2   . VAL A 1 34  ? 37.833 20.722  26.919  1.00 27.42 ?  40  VAL A CG2   1 
ATOM   237  N N     . ASP A 1 35  ? 35.840 19.290  22.905  1.00 22.39 ?  41  ASP A N     1 
ATOM   238  C CA    . ASP A 1 35  ? 35.171 18.285  22.098  1.00 22.10 ?  41  ASP A CA    1 
ATOM   239  C C     . ASP A 1 35  ? 36.193 17.652  21.169  1.00 23.96 ?  41  ASP A C     1 
ATOM   240  O O     . ASP A 1 35  ? 37.130 18.310  20.725  1.00 26.64 ?  41  ASP A O     1 
ATOM   241  C CB    . ASP A 1 35  ? 34.028 18.877  21.264  1.00 20.46 ?  41  ASP A CB    1 
ATOM   242  C CG    . ASP A 1 35  ? 33.116 17.810  20.711  1.00 22.34 ?  41  ASP A CG    1 
ATOM   243  O OD1   . ASP A 1 35  ? 32.209 17.372  21.452  1.00 22.27 ?  41  ASP A OD1   1 
ATOM   244  O OD2   . ASP A 1 35  ? 33.324 17.405  19.544  1.00 20.64 -1 41  ASP A OD2   1 
ATOM   245  N N     . MET A 1 36  ? 35.993 16.377  20.854  1.00 23.90 ?  42  MET A N     1 
ATOM   246  C CA    . MET A 1 36  ? 36.934 15.695  19.969  1.00 27.10 ?  42  MET A CA    1 
ATOM   247  C C     . MET A 1 36  ? 36.818 16.163  18.515  1.00 24.67 ?  42  MET A C     1 
ATOM   248  O O     . MET A 1 36  ? 37.802 16.082  17.771  1.00 25.82 ?  42  MET A O     1 
ATOM   249  C CB    . MET A 1 36  ? 36.718 14.187  20.052  1.00 27.10 ?  42  MET A CB    1 
ATOM   250  C CG    . MET A 1 36  ? 35.383 13.773  19.454  1.00 27.48 ?  42  MET A CG    1 
ATOM   251  S SD    . MET A 1 36  ? 35.226 11.985  19.363  1.00 31.95 ?  42  MET A SD    1 
ATOM   252  C CE    . MET A 1 36  ? 35.120 11.562  21.094  1.00 27.21 ?  42  MET A CE    1 
ATOM   253  N N     . LYS A 1 37  ? 35.640 16.619  18.081  1.00 23.68 ?  43  LYS A N     1 
ATOM   254  C CA    . LYS A 1 37  ? 35.451 17.139  16.726  1.00 23.63 ?  43  LYS A CA    1 
ATOM   255  C C     . LYS A 1 37  ? 35.790 18.629  16.665  1.00 25.16 ?  43  LYS A C     1 
ATOM   256  O O     . LYS A 1 37  ? 35.968 19.294  17.692  1.00 21.82 ?  43  LYS A O     1 
ATOM   257  C CB    . LYS A 1 37  ? 34.012 16.958  16.251  1.00 21.67 ?  43  LYS A CB    1 
ATOM   258  C CG    . LYS A 1 37  ? 33.407 15.584  16.427  1.00 24.88 ?  43  LYS A CG    1 
ATOM   259  C CD    . LYS A 1 37  ? 31.975 15.571  15.886  1.00 21.33 ?  43  LYS A CD    1 
ATOM   260  C CE    . LYS A 1 37  ? 30.929 15.716  16.986  1.00 17.79 ?  43  LYS A CE    1 
ATOM   261  N NZ    . LYS A 1 37  ? 30.970 17.013  17.721  1.00 16.43 ?  43  LYS A NZ    1 
ATOM   262  N N     . ASP A 1 38  ? 35.853 19.169  15.444  1.00 21.58 ?  44  ASP A N     1 
ATOM   263  C CA    . ASP A 1 38  ? 36.007 20.609  15.291  1.00 23.25 ?  44  ASP A CA    1 
ATOM   264  C C     . ASP A 1 38  ? 34.678 21.325  15.106  1.00 21.58 ?  44  ASP A C     1 
ATOM   265  O O     . ASP A 1 38  ? 34.665 22.556  15.019  1.00 20.51 ?  44  ASP A O     1 
ATOM   266  C CB    . ASP A 1 38  ? 36.993 20.954  14.147  1.00 27.35 ?  44  ASP A CB    1 
ATOM   267  C CG    . ASP A 1 38  ? 36.388 20.839  12.724  1.00 29.65 ?  44  ASP A CG    1 
ATOM   268  O OD1   . ASP A 1 38  ? 35.230 20.376  12.536  1.00 29.59 ?  44  ASP A OD1   1 
ATOM   269  O OD2   . ASP A 1 38  ? 37.103 21.225  11.760  1.00 31.67 -1 44  ASP A OD2   1 
ATOM   270  N N     . SER A 1 39  ? 33.556 20.600  15.092  1.00 18.19 ?  45  SER A N     1 
ATOM   271  C CA    . SER A 1 39  ? 32.256 21.232  14.910  1.00 17.59 ?  45  SER A CA    1 
ATOM   272  C C     . SER A 1 39  ? 31.181 20.490  15.684  1.00 19.33 ?  45  SER A C     1 
ATOM   273  O O     . SER A 1 39  ? 31.241 19.269  15.864  1.00 17.31 ?  45  SER A O     1 
ATOM   274  C CB    . SER A 1 39  ? 31.816 21.286  13.440  1.00 19.83 ?  45  SER A CB    1 
ATOM   275  O OG    . SER A 1 39  ? 32.815 20.803  12.599  1.00 26.50 ?  45  SER A OG    1 
ATOM   276  N N     . PHE A 1 40  ? 30.189 21.257  16.126  1.00 16.83 ?  46  PHE A N     1 
ATOM   277  C CA    . PHE A 1 40  ? 28.970 20.694  16.669  1.00 15.28 ?  46  PHE A CA    1 
ATOM   278  C C     . PHE A 1 40  ? 28.233 19.906  15.592  1.00 15.50 ?  46  PHE A C     1 
ATOM   279  O O     . PHE A 1 40  ? 28.193 20.310  14.429  1.00 15.29 ?  46  PHE A O     1 
ATOM   280  C CB    . PHE A 1 40  ? 28.088 21.829  17.207  1.00 14.66 ?  46  PHE A CB    1 
ATOM   281  C CG    . PHE A 1 40  ? 26.684 21.400  17.543  1.00 14.67 ?  46  PHE A CG    1 
ATOM   282  C CD1   . PHE A 1 40  ? 26.403 20.807  18.767  1.00 14.62 ?  46  PHE A CD1   1 
ATOM   283  C CD2   . PHE A 1 40  ? 25.652 21.584  16.629  1.00 14.46 ?  46  PHE A CD2   1 
ATOM   284  C CE1   . PHE A 1 40  ? 25.116 20.405  19.080  1.00 16.30 ?  46  PHE A CE1   1 
ATOM   285  C CE2   . PHE A 1 40  ? 24.365 21.177  16.928  1.00 13.96 ?  46  PHE A CE2   1 
ATOM   286  C CZ    . PHE A 1 40  ? 24.101 20.585  18.165  1.00 14.38 ?  46  PHE A CZ    1 
ATOM   287  N N     . HIS A 1 41  ? 27.651 18.774  15.979  1.00 13.80 ?  47  HIS A N     1 
ATOM   288  C CA    . HIS A 1 41  ? 26.880 17.923  15.078  1.00 15.78 ?  47  HIS A CA    1 
ATOM   289  C C     . HIS A 1 41  ? 25.413 17.927  15.491  1.00 14.51 ?  47  HIS A C     1 
ATOM   290  O O     . HIS A 1 41  ? 25.070 17.434  16.574  1.00 15.08 ?  47  HIS A O     1 
ATOM   291  C CB    . HIS A 1 41  ? 27.396 16.486  15.087  1.00 13.64 ?  47  HIS A CB    1 
ATOM   292  C CG    . HIS A 1 41  ? 26.698 15.601  14.098  1.00 14.41 ?  47  HIS A CG    1 
ATOM   293  N ND1   . HIS A 1 41  ? 26.547 14.243  14.283  1.00 15.89 ?  47  HIS A ND1   1 
ATOM   294  C CD2   . HIS A 1 41  ? 26.102 15.888  12.916  1.00 14.34 ?  47  HIS A CD2   1 
ATOM   295  C CE1   . HIS A 1 41  ? 25.910 13.727  13.246  1.00 16.61 ?  47  HIS A CE1   1 
ATOM   296  N NE2   . HIS A 1 41  ? 25.625 14.705  12.405  1.00 16.42 ?  47  HIS A NE2   1 
ATOM   297  N N     . HIS A 1 42  ? 24.546 18.467  14.629  1.00 13.20 ?  48  HIS A N     1 
ATOM   298  C CA    . HIS A 1 42  ? 23.101 18.466  14.900  1.00 13.65 ?  48  HIS A CA    1 
ATOM   299  C C     . HIS A 1 42  ? 22.592 17.074  14.525  1.00 15.63 ?  48  HIS A C     1 
ATOM   300  O O     . HIS A 1 42  ? 22.061 16.840  13.433  1.00 13.33 ?  48  HIS A O     1 
ATOM   301  C CB    . HIS A 1 42  ? 22.405 19.580  14.115  1.00 13.23 ?  48  HIS A CB    1 
ATOM   302  C CG    . HIS A 1 42  ? 20.974 19.784  14.492  1.00 16.47 ?  48  HIS A CG    1 
ATOM   303  N ND1   . HIS A 1 42  ? 20.576 20.707  15.439  1.00 15.77 ?  48  HIS A ND1   1 
ATOM   304  C CD2   . HIS A 1 42  ? 19.845 19.159  14.076  1.00 15.08 ?  48  HIS A CD2   1 
ATOM   305  C CE1   . HIS A 1 42  ? 19.261 20.647  15.581  1.00 16.36 ?  48  HIS A CE1   1 
ATOM   306  N NE2   . HIS A 1 42  ? 18.794 19.720  14.762  1.00 15.56 ?  48  HIS A NE2   1 
ATOM   307  N N     . ASN A 1 43  ? 22.804 16.107  15.432  1.00 13.38 ?  49  ASN A N     1 
ATOM   308  C CA    . ASN A 1 43  ? 22.682 14.710  15.015  1.00 15.67 ?  49  ASN A CA    1 
ATOM   309  C C     . ASN A 1 43  ? 21.233 14.257  14.898  1.00 16.75 ?  49  ASN A C     1 
ATOM   310  O O     . ASN A 1 43  ? 20.977 13.160  14.375  1.00 14.76 ?  49  ASN A O     1 
ATOM   311  C CB    . ASN A 1 43  ? 23.459 13.793  15.979  1.00 16.05 ?  49  ASN A CB    1 
ATOM   312  C CG    . ASN A 1 43  ? 23.035 13.957  17.426  1.00 20.31 ?  49  ASN A CG    1 
ATOM   313  O OD1   . ASN A 1 43  ? 21.949 14.475  17.718  1.00 20.18 ?  49  ASN A OD1   1 
ATOM   314  N ND2   . ASN A 1 43  ? 23.886 13.494  18.356  1.00 20.95 ?  49  ASN A ND2   1 
ATOM   315  N N     . VAL A 1 44  ? 20.289 15.072  15.382  1.00 14.05 ?  50  VAL A N     1 
ATOM   316  C CA    . VAL A 1 44  ? 18.874 14.834  15.120  1.00 18.37 ?  50  VAL A CA    1 
ATOM   317  C C     . VAL A 1 44  ? 18.608 14.825  13.618  1.00 16.45 ?  50  VAL A C     1 
ATOM   318  O O     . VAL A 1 44  ? 17.676 14.162  13.143  1.00 17.85 ?  50  VAL A O     1 
ATOM   319  C CB    . VAL A 1 44  ? 18.015 15.898  15.846  1.00 18.24 ?  50  VAL A CB    1 
ATOM   320  C CG1   . VAL A 1 44  ? 16.564 15.774  15.444  1.00 19.71 ?  50  VAL A CG1   1 
ATOM   321  C CG2   . VAL A 1 44  ? 18.129 15.755  17.358  1.00 19.53 ?  50  VAL A CG2   1 
ATOM   322  N N     . ALA A 1 45  ? 19.424 15.530  12.837  1.00 13.22 ?  51  ALA A N     1 
ATOM   323  C CA    . ALA A 1 45  ? 19.217 15.565  11.396  1.00 12.77 ?  51  ALA A CA    1 
ATOM   324  C C     . ALA A 1 45  ? 20.142 14.633  10.639  1.00 14.52 ?  51  ALA A C     1 
ATOM   325  O O     . ALA A 1 45  ? 20.227 14.736  9.415   1.00 13.01 ?  51  ALA A O     1 
ATOM   326  C CB    . ALA A 1 45  ? 19.380 16.986  10.880  1.00 12.28 ?  51  ALA A CB    1 
ATOM   327  N N     . ALA A 1 46  ? 20.822 13.714  11.328  1.00 12.92 ?  52  ALA A N     1 
ATOM   328  C CA    . ALA A 1 46  ? 21.843 12.911  10.665  1.00 15.00 ?  52  ALA A CA    1 
ATOM   329  C C     . ALA A 1 46  ? 21.244 11.933  9.657   1.00 14.64 ?  52  ALA A C     1 
ATOM   330  O O     . ALA A 1 46  ? 21.906 11.580  8.677   1.00 13.63 ?  52  ALA A O     1 
ATOM   331  C CB    . ALA A 1 46  ? 22.675 12.168  11.717  1.00 13.40 ?  52  ALA A CB    1 
ATOM   332  N N     . LEU A 1 47  ? 20.002 11.480  9.875   1.00 13.73 ?  53  LEU A N     1 
ATOM   333  C CA    . LEU A 1 47  ? 19.390 10.545  8.938   1.00 14.37 ?  53  LEU A CA    1 
ATOM   334  C C     . LEU A 1 47  ? 18.921 11.266  7.668   1.00 16.09 ?  53  LEU A C     1 
ATOM   335  O O     . LEU A 1 47  ? 19.144 10.779  6.555   1.00 16.67 ?  53  LEU A O     1 
ATOM   336  C CB    . LEU A 1 47  ? 18.250 9.790   9.635   1.00 12.49 ?  53  LEU A CB    1 
ATOM   337  C CG    . LEU A 1 47  ? 18.671 9.057   10.929  1.00 16.78 ?  53  LEU A CG    1 
ATOM   338  C CD1   . LEU A 1 47  ? 17.547 8.211   11.534  1.00 14.17 ?  53  LEU A CD1   1 
ATOM   339  C CD2   . LEU A 1 47  ? 19.905 8.168   10.689  1.00 14.70 ?  53  LEU A CD2   1 
ATOM   340  N N     . ARG A 1 48  ? 18.311 12.444  7.806   1.00 14.24 ?  54  ARG A N     1 
ATOM   341  C CA    . ARG A 1 48  ? 18.045 13.288  6.644   1.00 14.08 ?  54  ARG A CA    1 
ATOM   342  C C     . ARG A 1 48  ? 19.340 13.619  5.900   1.00 16.60 ?  54  ARG A C     1 
ATOM   343  O O     . ARG A 1 48  ? 19.373 13.624  4.661   1.00 17.06 ?  54  ARG A O     1 
ATOM   344  C CB    . ARG A 1 48  ? 17.332 14.560  7.107   1.00 14.39 ?  54  ARG A CB    1 
ATOM   345  C CG    . ARG A 1 48  ? 16.920 15.584  6.031   1.00 15.82 ?  54  ARG A CG    1 
ATOM   346  C CD    . ARG A 1 48  ? 15.724 15.146  5.202   1.00 18.00 ?  54  ARG A CD    1 
ATOM   347  N NE    . ARG A 1 48  ? 14.623 14.635  6.011   1.00 16.83 ?  54  ARG A NE    1 
ATOM   348  C CZ    . ARG A 1 48  ? 13.734 15.389  6.647   1.00 17.80 ?  54  ARG A CZ    1 
ATOM   349  N NH1   . ARG A 1 48  ? 13.759 16.717  6.563   1.00 13.98 ?  54  ARG A NH1   1 
ATOM   350  N NH2   . ARG A 1 48  ? 12.804 14.797  7.398   1.00 15.04 ?  54  ARG A NH2   1 
ATOM   351  N N     . ALA A 1 49  ? 20.431 13.873  6.631   1.00 13.08 ?  55  ALA A N     1 
ATOM   352  C CA    . ALA A 1 49  ? 21.702 14.096  5.943   1.00 14.18 ?  55  ALA A CA    1 
ATOM   353  C C     . ALA A 1 49  ? 22.250 12.841  5.268   1.00 14.23 ?  55  ALA A C     1 
ATOM   354  O O     . ALA A 1 49  ? 23.190 12.952  4.476   1.00 14.61 ?  55  ALA A O     1 
ATOM   355  C CB    . ALA A 1 49  ? 22.742 14.650  6.910   1.00 14.46 ?  55  ALA A CB    1 
ATOM   356  N N     . SER A 1 50  ? 21.682 11.661  5.527   1.00 15.02 ?  56  SER A N     1 
ATOM   357  C CA    . SER A 1 50  ? 22.121 10.452  4.831   1.00 16.91 ?  56  SER A CA    1 
ATOM   358  C C     . SER A 1 50  ? 21.356 10.166  3.550   1.00 18.64 ?  56  SER A C     1 
ATOM   359  O O     . SER A 1 50  ? 21.712 9.214   2.847   1.00 16.99 ?  56  SER A O     1 
ATOM   360  C CB    . SER A 1 50  ? 22.005 9.227   5.739   1.00 16.04 ?  56  SER A CB    1 
ATOM   361  O OG    . SER A 1 50  ? 22.852 9.384   6.853   1.00 17.49 ?  56  SER A OG    1 
ATOM   362  N N     . VAL A 1 51  ? 20.318 10.944  3.232   1.00 16.69 ?  57  VAL A N     1 
ATOM   363  C CA    . VAL A 1 51  ? 19.506 10.672  2.050   1.00 19.09 ?  57  VAL A CA    1 
ATOM   364  C C     . VAL A 1 51  ? 19.316 11.896  1.151   1.00 20.05 ?  57  VAL A C     1 
ATOM   365  O O     . VAL A 1 51  ? 18.857 11.759  0.016   1.00 18.92 ?  57  VAL A O     1 
ATOM   366  C CB    . VAL A 1 51  ? 18.133 10.111  2.454   1.00 17.38 ?  57  VAL A CB    1 
ATOM   367  C CG1   . VAL A 1 51  ? 18.299 8.809   3.217   1.00 16.48 ?  57  VAL A CG1   1 
ATOM   368  C CG2   . VAL A 1 51  ? 17.379 11.135  3.271   1.00 16.34 ?  57  VAL A CG2   1 
ATOM   369  N N     . GLU A 1 52  ? 19.655 13.096  1.621   1.00 16.50 ?  58  GLU A N     1 
ATOM   370  C CA    . GLU A 1 52  ? 19.397 14.314  0.844   1.00 19.13 ?  58  GLU A CA    1 
ATOM   371  C C     . GLU A 1 52  ? 20.720 14.965  0.449   1.00 16.40 ?  58  GLU A C     1 
ATOM   372  O O     . GLU A 1 52  ? 21.457 15.440  1.308   1.00 14.76 ?  58  GLU A O     1 
ATOM   373  C CB    . GLU A 1 52  ? 18.520 15.297  1.633   1.00 17.01 ?  58  GLU A CB    1 
ATOM   374  C CG    . GLU A 1 52  ? 18.388 16.641  0.915   1.00 21.51 ?  58  GLU A CG    1 
ATOM   375  C CD    . GLU A 1 52  ? 17.526 17.664  1.661   1.00 22.87 ?  58  GLU A CD    1 
ATOM   376  O OE1   . GLU A 1 52  ? 16.783 17.270  2.583   1.00 21.93 ?  58  GLU A OE1   1 
ATOM   377  O OE2   . GLU A 1 52  ? 17.588 18.866  1.314   1.00 22.89 -1 58  GLU A OE2   1 
ATOM   378  N N     . THR A 1 53  ? 21.010 14.995  -0.855  1.00 18.79 ?  59  THR A N     1 
ATOM   379  C CA    . THR A 1 53  ? 22.210 15.652  -1.346  1.00 19.88 ?  59  THR A CA    1 
ATOM   380  C C     . THR A 1 53  ? 22.261 17.103  -0.880  1.00 20.80 ?  59  THR A C     1 
ATOM   381  O O     . THR A 1 53  ? 21.260 17.823  -0.933  1.00 18.74 ?  59  THR A O     1 
ATOM   382  C CB    . THR A 1 53  ? 22.256 15.618  -2.879  1.00 20.95 ?  59  THR A CB    1 
ATOM   383  O OG1   . THR A 1 53  ? 22.263 14.257  -3.345  1.00 24.70 ?  59  THR A OG1   1 
ATOM   384  C CG2   . THR A 1 53  ? 23.507 16.336  -3.381  1.00 20.35 ?  59  THR A CG2   1 
ATOM   385  N N     . GLY A 1 54  ? 23.453 17.540  -0.461  1.00 19.20 ?  60  GLY A N     1 
ATOM   386  C CA    . GLY A 1 54  ? 23.664 18.913  -0.064  1.00 18.11 ?  60  GLY A CA    1 
ATOM   387  C C     . GLY A 1 54  ? 23.185 19.261  1.330   1.00 20.00 ?  60  GLY A C     1 
ATOM   388  O O     . GLY A 1 54  ? 23.430 20.384  1.776   1.00 20.19 ?  60  GLY A O     1 
ATOM   389  N N     . PHE A 1 55  ? 22.528 18.336  2.048   1.00 16.94 ?  61  PHE A N     1 
ATOM   390  C CA    . PHE A 1 55  ? 21.965 18.682  3.347   1.00 15.53 ?  61  PHE A CA    1 
ATOM   391  C C     . PHE A 1 55  ? 22.994 18.644  4.478   1.00 16.46 ?  61  PHE A C     1 
ATOM   392  O O     . PHE A 1 55  ? 22.812 19.321  5.492   1.00 13.29 ?  61  PHE A O     1 
ATOM   393  C CB    . PHE A 1 55  ? 20.804 17.743  3.687   1.00 14.92 ?  61  PHE A CB    1 
ATOM   394  C CG    . PHE A 1 55  ? 20.054 18.140  4.912   1.00 14.97 ?  61  PHE A CG    1 
ATOM   395  C CD1   . PHE A 1 55  ? 19.211 19.245  4.896   1.00 17.42 ?  61  PHE A CD1   1 
ATOM   396  C CD2   . PHE A 1 55  ? 20.192 17.429  6.100   1.00 16.23 ?  61  PHE A CD2   1 
ATOM   397  C CE1   . PHE A 1 55  ? 18.511 19.645  6.033   1.00 18.40 ?  61  PHE A CE1   1 
ATOM   398  C CE2   . PHE A 1 55  ? 19.498 17.824  7.248   1.00 16.55 ?  61  PHE A CE2   1 
ATOM   399  C CZ    . PHE A 1 55  ? 18.649 18.931  7.215   1.00 18.07 ?  61  PHE A CZ    1 
ATOM   400  N N     . ALA A 1 56  ? 24.060 17.853  4.352   1.00 17.88 ?  62  ALA A N     1 
ATOM   401  C CA    . ALA A 1 56  ? 24.938 17.620  5.503   1.00 15.70 ?  62  ALA A CA    1 
ATOM   402  C C     . ALA A 1 56  ? 25.607 18.894  5.995   1.00 13.99 ?  62  ALA A C     1 
ATOM   403  O O     . ALA A 1 56  ? 25.816 19.048  7.197   1.00 13.70 ?  62  ALA A O     1 
ATOM   404  C CB    . ALA A 1 56  ? 26.001 16.586  5.151   1.00 17.24 ?  62  ALA A CB    1 
ATOM   405  N N     . LYS A 1 57  ? 25.907 19.832  5.098   1.00 14.40 ?  63  LYS A N     1 
ATOM   406  C CA    . LYS A 1 57  ? 26.580 21.068  5.498   1.00 18.59 ?  63  LYS A CA    1 
ATOM   407  C C     . LYS A 1 57  ? 25.732 21.914  6.447   1.00 18.88 ?  63  LYS A C     1 
ATOM   408  O O     . LYS A 1 57  ? 26.264 22.804  7.123   1.00 16.87 ?  63  LYS A O     1 
ATOM   409  C CB    . LYS A 1 57  ? 26.978 21.872  4.249   1.00 17.27 ?  63  LYS A CB    1 
ATOM   410  C CG    . LYS A 1 57  ? 25.829 22.461  3.457   1.00 20.80 ?  63  LYS A CG    1 
ATOM   411  C CD    . LYS A 1 57  ? 26.374 23.347  2.332   1.00 26.98 ?  63  LYS A CD    1 
ATOM   412  C CE    . LYS A 1 57  ? 25.350 23.608  1.252   1.00 31.28 ?  63  LYS A CE    1 
ATOM   413  N NZ    . LYS A 1 57  ? 25.083 22.358  0.468   1.00 36.11 ?  63  LYS A NZ    1 
ATOM   414  N N     . LYS A 1 58  ? 24.438 21.626  6.551   1.00 17.49 ?  64  LYS A N     1 
ATOM   415  C CA    . LYS A 1 58  ? 23.564 22.280  7.509   1.00 17.87 ?  64  LYS A CA    1 
ATOM   416  C C     . LYS A 1 58  ? 23.588 21.619  8.878   1.00 14.42 ?  64  LYS A C     1 
ATOM   417  O O     . LYS A 1 58  ? 22.961 22.129  9.800   1.00 12.99 ?  64  LYS A O     1 
ATOM   418  C CB    . LYS A 1 58  ? 22.129 22.302  6.952   1.00 17.91 ?  64  LYS A CB    1 
ATOM   419  C CG    . LYS A 1 58  ? 22.078 23.038  5.615   1.00 21.57 ?  64  LYS A CG    1 
ATOM   420  C CD    . LYS A 1 58  ? 20.698 22.973  4.984   1.00 30.75 ?  64  LYS A CD    1 
ATOM   421  C CE    . LYS A 1 58  ? 20.550 24.060  3.934   1.00 38.56 ?  64  LYS A CE    1 
ATOM   422  N NZ    . LYS A 1 58  ? 20.408 25.405  4.593   1.00 46.69 ?  64  LYS A NZ    1 
ATOM   423  N N     . THR A 1 59  ? 24.294 20.505  9.039   1.00 14.29 ?  65  THR A N     1 
ATOM   424  C CA    . THR A 1 59  ? 24.257 19.762  10.289  1.00 15.11 ?  65  THR A CA    1 
ATOM   425  C C     . THR A 1 59  ? 25.569 19.811  11.059  1.00 15.87 ?  65  THR A C     1 
ATOM   426  O O     . THR A 1 59  ? 25.657 19.189  12.123  1.00 13.78 ?  65  THR A O     1 
ATOM   427  C CB    . THR A 1 59  ? 23.874 18.292  10.043  1.00 14.16 ?  65  THR A CB    1 
ATOM   428  O OG1   . THR A 1 59  ? 24.916 17.619  9.316   1.00 14.05 ?  65  THR A OG1   1 
ATOM   429  C CG2   . THR A 1 59  ? 22.591 18.208  9.251   1.00 13.55 ?  65  THR A CG2   1 
ATOM   430  N N     . PHE A 1 60  ? 26.580 20.538  10.571  1.00 13.47 ?  66  PHE A N     1 
ATOM   431  C CA    . PHE A 1 60  ? 27.843 20.725  11.290  1.00 15.68 ?  66  PHE A CA    1 
ATOM   432  C C     . PHE A 1 60  ? 28.138 22.216  11.444  1.00 18.59 ?  66  PHE A C     1 
ATOM   433  O O     . PHE A 1 60  ? 28.091 22.957  10.457  1.00 15.86 ?  66  PHE A O     1 
ATOM   434  C CB    . PHE A 1 60  ? 28.999 20.033  10.563  1.00 16.93 ?  66  PHE A CB    1 
ATOM   435  C CG    . PHE A 1 60  ? 28.960 18.528  10.669  1.00 13.58 ?  66  PHE A CG    1 
ATOM   436  C CD1   . PHE A 1 60  ? 29.382 17.896  11.830  1.00 16.76 ?  66  PHE A CD1   1 
ATOM   437  C CD2   . PHE A 1 60  ? 28.484 17.757  9.628   1.00 13.67 ?  66  PHE A CD2   1 
ATOM   438  C CE1   . PHE A 1 60  ? 29.340 16.521  11.949  1.00 15.88 ?  66  PHE A CE1   1 
ATOM   439  C CE2   . PHE A 1 60  ? 28.428 16.367  9.732   1.00 15.61 ?  66  PHE A CE2   1 
ATOM   440  C CZ    . PHE A 1 60  ? 28.857 15.751  10.891  1.00 17.32 ?  66  PHE A CZ    1 
ATOM   441  N N     . ILE A 1 61  ? 28.467 22.652  12.671  1.00 17.36 ?  67  ILE A N     1 
ATOM   442  C CA    . ILE A 1 61  ? 28.662 24.073  12.982  1.00 17.82 ?  67  ILE A CA    1 
ATOM   443  C C     . ILE A 1 61  ? 30.010 24.258  13.684  1.00 19.61 ?  67  ILE A C     1 
ATOM   444  O O     . ILE A 1 61  ? 30.231 23.706  14.765  1.00 17.26 ?  67  ILE A O     1 
ATOM   445  C CB    . ILE A 1 61  ? 27.527 24.625  13.859  1.00 17.11 ?  67  ILE A CB    1 
ATOM   446  C CG1   . ILE A 1 61  ? 26.157 24.280  13.251  1.00 16.72 ?  67  ILE A CG1   1 
ATOM   447  C CG2   . ILE A 1 61  ? 27.723 26.117  14.058  1.00 18.30 ?  67  ILE A CG2   1 
ATOM   448  C CD1   . ILE A 1 61  ? 24.958 24.596  14.133  1.00 14.28 ?  67  ILE A CD1   1 
ATOM   449  N N     . SER A 1 62  ? 30.901 25.041  13.082  1.00 21.28 ?  68  SER A N     1 
ATOM   450  C CA    . SER A 1 62  ? 32.230 25.255  13.654  1.00 21.88 ?  68  SER A CA    1 
ATOM   451  C C     . SER A 1 62  ? 32.168 25.767  15.092  1.00 21.19 ?  68  SER A C     1 
ATOM   452  O O     . SER A 1 62  ? 31.497 26.765  15.378  1.00 19.32 ?  68  SER A O     1 
ATOM   453  C CB    . SER A 1 62  ? 33.002 26.253  12.799  1.00 22.25 ?  68  SER A CB    1 
ATOM   454  O OG    . SER A 1 62  ? 34.145 26.741  13.496  1.00 26.68 ?  68  SER A OG    1 
ATOM   455  N N     . TYR A 1 63  ? 32.908 25.094  15.992  1.00 20.82 ?  69  TYR A N     1 
ATOM   456  C CA    . TYR A 1 63  ? 33.024 25.573  17.372  1.00 21.67 ?  69  TYR A CA    1 
ATOM   457  C C     . TYR A 1 63  ? 33.795 26.881  17.436  1.00 24.17 ?  69  TYR A C     1 
ATOM   458  O O     . TYR A 1 63  ? 33.389 27.823  18.127  1.00 22.32 ?  69  TYR A O     1 
ATOM   459  C CB    . TYR A 1 63  ? 33.738 24.550  18.270  1.00 21.31 ?  69  TYR A CB    1 
ATOM   460  C CG    . TYR A 1 63  ? 32.981 23.283  18.560  1.00 20.25 ?  69  TYR A CG    1 
ATOM   461  C CD1   . TYR A 1 63  ? 31.763 23.308  19.248  1.00 15.94 ?  69  TYR A CD1   1 
ATOM   462  C CD2   . TYR A 1 63  ? 33.497 22.057  18.169  1.00 17.85 ?  69  TYR A CD2   1 
ATOM   463  C CE1   . TYR A 1 63  ? 31.075 22.133  19.512  1.00 14.92 ?  69  TYR A CE1   1 
ATOM   464  C CE2   . TYR A 1 63  ? 32.837 20.891  18.432  1.00 17.60 ?  69  TYR A CE2   1 
ATOM   465  C CZ    . TYR A 1 63  ? 31.625 20.929  19.094  1.00 17.26 ?  69  TYR A CZ    1 
ATOM   466  O OH    . TYR A 1 63  ? 30.980 19.750  19.330  1.00 14.75 ?  69  TYR A OH    1 
ATOM   467  N N     . SER A 1 64  ? 34.949 26.935  16.764  1.00 22.37 ?  70  SER A N     1 
ATOM   468  C CA    . SER A 1 64  ? 35.865 28.050  16.979  1.00 25.33 ?  70  SER A CA    1 
ATOM   469  C C     . SER A 1 64  ? 35.273 29.355  16.473  1.00 24.95 ?  70  SER A C     1 
ATOM   470  O O     . SER A 1 64  ? 35.553 30.412  17.039  1.00 26.13 ?  70  SER A O     1 
ATOM   471  C CB    . SER A 1 64  ? 37.220 27.772  16.315  1.00 24.12 ?  70  SER A CB    1 
ATOM   472  O OG    . SER A 1 64  ? 37.067 27.614  14.911  1.00 31.20 ?  70  SER A OG    1 
ATOM   473  N N     . VAL A 1 65  ? 34.432 29.300  15.440  1.00 23.39 ?  71  VAL A N     1 
ATOM   474  C CA    . VAL A 1 65  ? 33.781 30.516  14.959  1.00 23.71 ?  71  VAL A CA    1 
ATOM   475  C C     . VAL A 1 65  ? 32.905 31.122  16.047  1.00 25.01 ?  71  VAL A C     1 
ATOM   476  O O     . VAL A 1 65  ? 32.827 32.350  16.198  1.00 23.89 ?  71  VAL A O     1 
ATOM   477  C CB    . VAL A 1 65  ? 32.978 30.218  13.684  1.00 22.94 ?  71  VAL A CB    1 
ATOM   478  C CG1   . VAL A 1 65  ? 32.021 31.373  13.361  1.00 20.55 ?  71  VAL A CG1   1 
ATOM   479  C CG2   . VAL A 1 65  ? 33.940 30.002  12.513  1.00 21.33 ?  71  VAL A CG2   1 
ATOM   480  N N     . THR A 1 66  ? 32.227 30.277  16.819  1.00 21.98 ?  72  THR A N     1 
ATOM   481  C CA    . THR A 1 66  ? 31.352 30.795  17.861  1.00 22.85 ?  72  THR A CA    1 
ATOM   482  C C     . THR A 1 66  ? 32.107 31.066  19.150  1.00 23.70 ?  72  THR A C     1 
ATOM   483  O O     . THR A 1 66  ? 31.857 32.078  19.817  1.00 24.77 ?  72  THR A O     1 
ATOM   484  C CB    . THR A 1 66  ? 30.209 29.820  18.131  1.00 22.84 ?  72  THR A CB    1 
ATOM   485  O OG1   . THR A 1 66  ? 29.305 29.844  17.019  1.00 23.42 ?  72  THR A OG1   1 
ATOM   486  C CG2   . THR A 1 66  ? 29.473 30.218  19.389  1.00 21.85 ?  72  THR A CG2   1 
ATOM   487  N N     . PHE A 1 67  ? 33.033 30.182  19.524  1.00 22.01 ?  73  PHE A N     1 
ATOM   488  C CA    . PHE A 1 67  ? 33.633 30.274  20.848  1.00 25.79 ?  73  PHE A CA    1 
ATOM   489  C C     . PHE A 1 67  ? 35.102 30.687  20.866  1.00 25.86 ?  73  PHE A C     1 
ATOM   490  O O     . PHE A 1 67  ? 35.593 31.075  21.930  1.00 26.37 ?  73  PHE A O     1 
ATOM   491  C CB    . PHE A 1 67  ? 33.479 28.937  21.582  1.00 22.58 ?  73  PHE A CB    1 
ATOM   492  C CG    . PHE A 1 67  ? 32.051 28.536  21.794  1.00 19.98 ?  73  PHE A CG    1 
ATOM   493  C CD1   . PHE A 1 67  ? 31.249 29.239  22.676  1.00 19.39 ?  73  PHE A CD1   1 
ATOM   494  C CD2   . PHE A 1 67  ? 31.512 27.453  21.125  1.00 21.18 ?  73  PHE A CD2   1 
ATOM   495  C CE1   . PHE A 1 67  ? 29.931 28.877  22.881  1.00 21.75 ?  73  PHE A CE1   1 
ATOM   496  C CE2   . PHE A 1 67  ? 30.186 27.083  21.335  1.00 20.59 ?  73  PHE A CE2   1 
ATOM   497  C CZ    . PHE A 1 67  ? 29.405 27.788  22.213  1.00 19.90 ?  73  PHE A CZ    1 
ATOM   498  N N     . LYS A 1 68  ? 35.812 30.600  19.748  1.00 23.35 ?  74  LYS A N     1 
ATOM   499  C CA    . LYS A 1 68  ? 37.186 31.123  19.652  1.00 28.40 ?  74  LYS A CA    1 
ATOM   500  C C     . LYS A 1 68  ? 38.023 30.514  20.773  1.00 30.10 ?  74  LYS A C     1 
ATOM   501  O O     . LYS A 1 68  ? 37.994 29.279  20.948  1.00 26.12 ?  74  LYS A O     1 
ATOM   502  C CB    . LYS A 1 68  ? 37.099 32.650  19.625  1.00 29.76 ?  74  LYS A CB    1 
ATOM   503  C CG    . LYS A 1 68  ? 36.239 33.171  18.458  1.00 32.01 ?  74  LYS A CG    1 
ATOM   504  C CD    . LYS A 1 68  ? 35.876 34.637  18.624  1.00 40.28 ?  74  LYS A CD    1 
ATOM   505  C CE    . LYS A 1 68  ? 35.328 35.216  17.316  1.00 46.20 ?  74  LYS A CE    1 
ATOM   506  N NZ    . LYS A 1 68  ? 35.248 36.717  17.337  1.00 51.19 ?  74  LYS A NZ    1 
ATOM   507  N N     . ASP A 1 69  ? 38.753 31.307  21.572  1.00 27.46 ?  75  ASP A N     1 
ATOM   508  C CA    . ASP A 1 69  ? 39.716 30.745  22.518  1.00 28.90 ?  75  ASP A CA    1 
ATOM   509  C C     . ASP A 1 69  ? 39.071 30.073  23.714  1.00 29.23 ?  75  ASP A C     1 
ATOM   510  O O     . ASP A 1 69  ? 39.798 29.554  24.574  1.00 27.79 ?  75  ASP A O     1 
ATOM   511  C CB    . ASP A 1 69  ? 40.673 31.826  23.016  1.00 35.57 ?  75  ASP A CB    1 
ATOM   512  C CG    . ASP A 1 69  ? 41.800 32.105  22.036  1.00 39.74 ?  75  ASP A CG    1 
ATOM   513  O OD1   . ASP A 1 69  ? 41.871 31.420  20.987  1.00 38.35 ?  75  ASP A OD1   1 
ATOM   514  O OD2   . ASP A 1 69  ? 42.611 33.020  22.315  1.00 42.32 -1 75  ASP A OD2   1 
ATOM   515  N N     . ASN A 1 70  ? 37.747 30.098  23.812  1.00 27.61 ?  76  ASN A N     1 
ATOM   516  C CA    . ASN A 1 70  ? 37.033 29.319  24.808  1.00 27.67 ?  76  ASN A CA    1 
ATOM   517  C C     . ASN A 1 70  ? 36.784 27.888  24.355  1.00 27.38 ?  76  ASN A C     1 
ATOM   518  O O     . ASN A 1 70  ? 36.149 27.127  25.087  1.00 25.23 ?  76  ASN A O     1 
ATOM   519  C CB    . ASN A 1 70  ? 35.697 29.992  25.148  1.00 26.43 ?  76  ASN A CB    1 
ATOM   520  C CG    . ASN A 1 70  ? 35.878 31.267  25.972  1.00 29.65 ?  76  ASN A CG    1 
ATOM   521  O OD1   . ASN A 1 70  ? 35.500 32.359  25.544  1.00 27.68 ?  76  ASN A OD1   1 
ATOM   522  N ND2   . ASN A 1 70  ? 36.460 31.124  27.163  1.00 27.90 ?  76  ASN A ND2   1 
ATOM   523  N N     . PHE A 1 71  ? 37.244 27.515  23.162  1.00 27.02 ?  77  PHE A N     1 
ATOM   524  C CA    . PHE A 1 71  ? 37.125 26.155  22.660  1.00 24.33 ?  77  PHE A CA    1 
ATOM   525  C C     . PHE A 1 71  ? 38.507 25.537  22.461  1.00 26.62 ?  77  PHE A C     1 
ATOM   526  O O     . PHE A 1 71  ? 39.437 26.194  21.972  1.00 24.84 ?  77  PHE A O     1 
ATOM   527  C CB    . PHE A 1 71  ? 36.345 26.113  21.350  1.00 23.94 ?  77  PHE A CB    1 
ATOM   528  C CG    . PHE A 1 71  ? 36.371 24.772  20.695  1.00 24.00 ?  77  PHE A CG    1 
ATOM   529  C CD1   . PHE A 1 71  ? 35.686 23.705  21.252  1.00 20.91 ?  77  PHE A CD1   1 
ATOM   530  C CD2   . PHE A 1 71  ? 37.112 24.567  19.543  1.00 23.89 ?  77  PHE A CD2   1 
ATOM   531  C CE1   . PHE A 1 71  ? 35.736 22.461  20.675  1.00 23.65 ?  77  PHE A CE1   1 
ATOM   532  C CE2   . PHE A 1 71  ? 37.161 23.318  18.954  1.00 23.41 ?  77  PHE A CE2   1 
ATOM   533  C CZ    . PHE A 1 71  ? 36.471 22.265  19.523  1.00 20.18 ?  77  PHE A CZ    1 
ATOM   534  N N     . ARG A 1 72  ? 38.639 24.267  22.839  1.00 25.91 ?  78  ARG A N     1 
ATOM   535  C CA    . ARG A 1 72  ? 39.831 23.488  22.514  1.00 27.90 ?  78  ARG A CA    1 
ATOM   536  C C     . ARG A 1 72  ? 39.391 22.112  22.058  1.00 27.15 ?  78  ARG A C     1 
ATOM   537  O O     . ARG A 1 72  ? 38.728 21.397  22.812  1.00 27.92 ?  78  ARG A O     1 
ATOM   538  C CB    . ARG A 1 72  ? 40.793 23.358  23.699  1.00 32.33 ?  78  ARG A CB    1 
ATOM   539  C CG    . ARG A 1 72  ? 41.926 22.360  23.424  1.00 33.91 ?  78  ARG A CG    1 
ATOM   540  C CD    . ARG A 1 72  ? 43.307 22.870  23.837  1.00 37.89 ?  78  ARG A CD    1 
ATOM   541  N N     . GLN A 1 73  ? 39.744 21.754  20.823  1.00 30.51 ?  79  GLN A N     1 
ATOM   542  C CA    . GLN A 1 73  ? 39.544 20.394  20.334  1.00 28.28 ?  79  GLN A CA    1 
ATOM   543  C C     . GLN A 1 73  ? 40.496 19.433  21.047  1.00 31.37 ?  79  GLN A C     1 
ATOM   544  O O     . GLN A 1 73  ? 41.681 19.729  21.227  1.00 30.81 ?  79  GLN A O     1 
ATOM   545  C CB    . GLN A 1 73  ? 39.772 20.337  18.820  1.00 29.09 ?  79  GLN A CB    1 
ATOM   546  C CG    . GLN A 1 73  ? 39.551 18.975  18.189  1.00 29.14 ?  79  GLN A CG    1 
ATOM   547  C CD    . GLN A 1 73  ? 39.532 19.038  16.655  1.00 33.56 ?  79  GLN A CD    1 
ATOM   548  O OE1   . GLN A 1 73  ? 39.919 20.052  16.052  1.00 40.03 ?  79  GLN A OE1   1 
ATOM   549  N NE2   . GLN A 1 73  ? 39.077 17.954  16.018  1.00 31.72 ?  79  GLN A NE2   1 
ATOM   550  N N     . GLY A 1 74  ? 39.971 18.285  21.460  1.00 29.35 ?  80  GLY A N     1 
ATOM   551  C CA    . GLY A 1 74  ? 40.807 17.267  22.076  1.00 30.71 ?  80  GLY A CA    1 
ATOM   552  C C     . GLY A 1 74  ? 39.964 16.110  22.564  1.00 31.97 ?  80  GLY A C     1 
ATOM   553  O O     . GLY A 1 74  ? 38.738 16.190  22.658  1.00 29.68 ?  80  GLY A O     1 
ATOM   554  N N     . LEU A 1 75  ? 40.651 15.028  22.897  1.00 33.83 ?  81  LEU A N     1 
ATOM   555  C CA    . LEU A 1 75  ? 40.021 13.800  23.371  1.00 31.94 ?  81  LEU A CA    1 
ATOM   556  C C     . LEU A 1 75  ? 40.314 13.644  24.860  1.00 36.84 ?  81  LEU A C     1 
ATOM   557  O O     . LEU A 1 75  ? 41.474 13.475  25.259  1.00 39.07 ?  81  LEU A O     1 
ATOM   558  C CB    . LEU A 1 75  ? 40.538 12.601  22.580  1.00 36.44 ?  81  LEU A CB    1 
ATOM   559  C CG    . LEU A 1 75  ? 39.873 11.264  22.899  1.00 36.92 ?  81  LEU A CG    1 
ATOM   560  C CD1   . LEU A 1 75  ? 38.396 11.353  22.589  1.00 34.12 ?  81  LEU A CD1   1 
ATOM   561  C CD2   . LEU A 1 75  ? 40.524 10.149  22.099  1.00 36.88 ?  81  LEU A CD2   1 
ATOM   562  N N     . VAL A 1 76  ? 39.275 13.717  25.684  1.00 34.71 ?  82  VAL A N     1 
ATOM   563  C CA    . VAL A 1 76  ? 39.465 13.607  27.127  1.00 35.96 ?  82  VAL A CA    1 
ATOM   564  C C     . VAL A 1 76  ? 39.578 12.134  27.496  1.00 39.06 ?  82  VAL A C     1 
ATOM   565  O O     . VAL A 1 76  ? 38.678 11.343  27.197  1.00 36.84 ?  82  VAL A O     1 
ATOM   566  C CB    . VAL A 1 76  ? 38.321 14.280  27.889  1.00 35.42 ?  82  VAL A CB    1 
ATOM   567  C CG1   . VAL A 1 76  ? 38.505 14.071  29.389  1.00 34.18 ?  82  VAL A CG1   1 
ATOM   568  C CG2   . VAL A 1 76  ? 38.267 15.773  27.542  1.00 31.73 ?  82  VAL A CG2   1 
ATOM   569  N N     . VAL A 1 77  ? 40.683 11.761  28.148  1.00 37.99 ?  83  VAL A N     1 
ATOM   570  C CA    . VAL A 1 77  ? 40.951 10.368  28.501  1.00 41.33 ?  83  VAL A CA    1 
ATOM   571  C C     . VAL A 1 77  ? 40.764 10.088  29.989  1.00 41.27 ?  83  VAL A C     1 
ATOM   572  O O     . VAL A 1 77  ? 40.910 8.934   30.412  1.00 43.25 ?  83  VAL A O     1 
ATOM   573  C CB    . VAL A 1 77  ? 42.363 9.932   28.055  1.00 38.60 ?  83  VAL A CB    1 
ATOM   574  C CG1   . VAL A 1 77  ? 42.458 9.869   26.541  1.00 37.85 ?  83  VAL A CG1   1 
ATOM   575  C CG2   . VAL A 1 77  ? 43.421 10.877  28.630  1.00 39.75 ?  83  VAL A CG2   1 
ATOM   576  N N     . GLY A 1 78  ? 40.447 11.088  30.795  1.00 42.70 ?  84  GLY A N     1 
ATOM   577  C CA    . GLY A 1 78  ? 40.312 10.843  32.219  1.00 41.93 ?  84  GLY A CA    1 
ATOM   578  C C     . GLY A 1 78  ? 40.197 12.140  32.982  1.00 42.53 ?  84  GLY A C     1 
ATOM   579  O O     . GLY A 1 78  ? 40.471 13.230  32.468  1.00 38.13 ?  84  GLY A O     1 
ATOM   580  N N     . ILE A 1 79  ? 39.806 11.999  34.244  1.00 44.04 ?  85  ILE A N     1 
ATOM   581  C CA    . ILE A 1 79  ? 39.572 13.130  35.128  1.00 45.48 ?  85  ILE A CA    1 
ATOM   582  C C     . ILE A 1 79  ? 40.379 12.894  36.399  1.00 46.71 ?  85  ILE A C     1 
ATOM   583  O O     . ILE A 1 79  ? 40.184 11.879  37.075  1.00 50.64 ?  85  ILE A O     1 
ATOM   584  C CB    . ILE A 1 79  ? 38.073 13.300  35.449  1.00 46.25 ?  85  ILE A CB    1 
ATOM   585  C CG1   . ILE A 1 79  ? 37.234 13.386  34.165  1.00 43.51 ?  85  ILE A CG1   1 
ATOM   586  C CG2   . ILE A 1 79  ? 37.836 14.511  36.347  1.00 44.60 ?  85  ILE A CG2   1 
ATOM   587  C CD1   . ILE A 1 79  ? 37.367 14.695  33.410  1.00 39.69 ?  85  ILE A CD1   1 
ATOM   588  N N     . ASP A 1 80  ? 41.301 13.815  36.705  1.00 45.38 ?  86  ASP A N     1 
ATOM   589  C CA    . ASP A 1 80  ? 42.118 13.777  37.921  1.00 46.00 ?  86  ASP A CA    1 
ATOM   590  C C     . ASP A 1 80  ? 41.378 14.554  39.004  1.00 48.57 ?  86  ASP A C     1 
ATOM   591  O O     . ASP A 1 80  ? 41.493 15.780  39.096  1.00 46.78 ?  86  ASP A O     1 
ATOM   592  C CB    . ASP A 1 80  ? 43.500 14.362  37.643  1.00 46.67 ?  86  ASP A CB    1 
ATOM   593  C CG    . ASP A 1 80  ? 44.409 14.395  38.873  1.00 53.54 ?  86  ASP A CG    1 
ATOM   594  O OD1   . ASP A 1 80  ? 43.976 14.067  40.008  1.00 54.83 ?  86  ASP A OD1   1 
ATOM   595  O OD2   . ASP A 1 80  ? 45.590 14.769  38.688  1.00 52.77 -1 86  ASP A OD2   1 
ATOM   596  N N     . LEU A 1 81  ? 40.623 13.833  39.838  1.00 51.04 ?  87  LEU A N     1 
ATOM   597  C CA    . LEU A 1 81  ? 39.725 14.491  40.785  1.00 48.81 ?  87  LEU A CA    1 
ATOM   598  C C     . LEU A 1 81  ? 40.486 15.170  41.912  1.00 48.63 ?  87  LEU A C     1 
ATOM   599  O O     . LEU A 1 81  ? 40.116 16.272  42.334  1.00 52.67 ?  87  LEU A O     1 
ATOM   600  C CB    . LEU A 1 81  ? 38.727 13.483  41.349  1.00 46.32 ?  87  LEU A CB    1 
ATOM   601  C CG    . LEU A 1 81  ? 37.554 13.206  40.419  1.00 47.58 ?  87  LEU A CG    1 
ATOM   602  C CD1   . LEU A 1 81  ? 36.830 11.947  40.837  1.00 51.23 ?  87  LEU A CD1   1 
ATOM   603  C CD2   . LEU A 1 81  ? 36.622 14.409  40.423  1.00 46.88 ?  87  LEU A CD2   1 
ATOM   604  N N     . LYS A 1 82  ? 41.549 14.533  42.412  1.00 50.78 ?  88  LYS A N     1 
ATOM   605  C CA    . LYS A 1 82  ? 42.278 15.089  43.547  1.00 54.22 ?  88  LYS A CA    1 
ATOM   606  C C     . LYS A 1 82  ? 42.892 16.442  43.198  1.00 53.58 ?  88  LYS A C     1 
ATOM   607  O O     . LYS A 1 82  ? 42.893 17.364  44.026  1.00 55.02 ?  88  LYS A O     1 
ATOM   608  C CB    . LYS A 1 82  ? 43.351 14.099  44.014  1.00 52.10 ?  88  LYS A CB    1 
ATOM   609  C CG    . LYS A 1 82  ? 43.844 14.316  45.441  1.00 54.78 ?  88  LYS A CG    1 
ATOM   610  N N     . ASN A 1 83  ? 43.400 16.591  41.975  1.00 50.58 ?  89  ASN A N     1 
ATOM   611  C CA    . ASN A 1 83  ? 44.018 17.838  41.545  1.00 50.09 ?  89  ASN A CA    1 
ATOM   612  C C     . ASN A 1 83  ? 43.152 18.616  40.570  1.00 48.78 ?  89  ASN A C     1 
ATOM   613  O O     . ASN A 1 83  ? 43.643 19.556  39.938  1.00 48.84 ?  89  ASN A O     1 
ATOM   614  C CB    . ASN A 1 83  ? 45.383 17.562  40.927  1.00 49.52 ?  89  ASN A CB    1 
ATOM   615  C CG    . ASN A 1 83  ? 46.292 16.814  41.866  1.00 54.45 ?  89  ASN A CG    1 
ATOM   616  O OD1   . ASN A 1 83  ? 46.556 15.625  41.668  1.00 56.40 ?  89  ASN A OD1   1 
ATOM   617  N ND2   . ASN A 1 83  ? 46.775 17.495  42.900  1.00 53.05 ?  89  ASN A ND2   1 
ATOM   618  N N     . GLN A 1 84  ? 41.888 18.226  40.415  1.00 48.62 ?  90  GLN A N     1 
ATOM   619  C CA    . GLN A 1 84  ? 40.891 18.980  39.659  1.00 44.02 ?  90  GLN A CA    1 
ATOM   620  C C     . GLN A 1 84  ? 41.402 19.355  38.267  1.00 42.85 ?  90  GLN A C     1 
ATOM   621  O O     . GLN A 1 84  ? 41.506 20.527  37.898  1.00 41.66 ?  90  GLN A O     1 
ATOM   622  C CB    . GLN A 1 84  ? 40.461 20.212  40.453  1.00 42.38 ?  90  GLN A CB    1 
ATOM   623  C CG    . GLN A 1 84  ? 39.955 19.860  41.839  1.00 46.14 ?  90  GLN A CG    1 
ATOM   624  C CD    . GLN A 1 84  ? 38.451 19.689  41.884  1.00 44.36 ?  90  GLN A CD    1 
ATOM   625  O OE1   . GLN A 1 84  ? 37.708 20.672  41.878  1.00 46.77 ?  90  GLN A OE1   1 
ATOM   626  N NE2   . GLN A 1 84  ? 37.992 18.441  41.945  1.00 44.43 ?  90  GLN A NE2   1 
ATOM   627  N N     . MET A 1 85  ? 41.715 18.325  37.486  1.00 42.67 ?  91  MET A N     1 
ATOM   628  C CA    . MET A 1 85  ? 42.250 18.510  36.148  1.00 40.93 ?  91  MET A CA    1 
ATOM   629  C C     . MET A 1 85  ? 41.494 17.619  35.176  1.00 41.29 ?  91  MET A C     1 
ATOM   630  O O     . MET A 1 85  ? 41.069 16.517  35.535  1.00 43.11 ?  91  MET A O     1 
ATOM   631  C CB    . MET A 1 85  ? 43.756 18.192  36.107  1.00 42.86 ?  91  MET A CB    1 
ATOM   632  C CG    . MET A 1 85  ? 44.614 19.155  36.898  1.00 48.47 ?  91  MET A CG    1 
ATOM   633  S SD    . MET A 1 85  ? 45.301 20.503  35.897  1.00 56.43 ?  91  MET A SD    1 
ATOM   634  C CE    . MET A 1 85  ? 47.033 20.015  35.882  1.00 49.78 ?  91  MET A CE    1 
ATOM   635  N N     . VAL A 1 86  ? 41.305 18.108  33.957  1.00 37.10 ?  92  VAL A N     1 
ATOM   636  C CA    . VAL A 1 86  ? 40.761 17.309  32.868  1.00 38.69 ?  92  VAL A CA    1 
ATOM   637  C C     . VAL A 1 86  ? 41.926 16.884  31.987  1.00 39.52 ?  92  VAL A C     1 
ATOM   638  O O     . VAL A 1 86  ? 42.668 17.735  31.475  1.00 38.75 ?  92  VAL A O     1 
ATOM   639  C CB    . VAL A 1 86  ? 39.700 18.083  32.069  1.00 35.98 ?  92  VAL A CB    1 
ATOM   640  C CG1   . VAL A 1 86  ? 39.414 17.374  30.748  1.00 39.08 ?  92  VAL A CG1   1 
ATOM   641  C CG2   . VAL A 1 86  ? 38.425 18.211  32.884  1.00 34.50 ?  92  VAL A CG2   1 
ATOM   642  N N     . LEU A 1 87  ? 42.077 15.568  31.807  1.00 39.21 ?  93  LEU A N     1 
ATOM   643  C CA    . LEU A 1 87  ? 43.240 14.968  31.162  1.00 39.70 ?  93  LEU A CA    1 
ATOM   644  C C     . LEU A 1 87  ? 42.940 14.708  29.687  1.00 40.99 ?  93  LEU A C     1 
ATOM   645  O O     . LEU A 1 87  ? 42.024 13.944  29.357  1.00 39.81 ?  93  LEU A O     1 
ATOM   646  C CB    . LEU A 1 87  ? 43.638 13.668  31.871  1.00 39.81 ?  93  LEU A CB    1 
ATOM   647  C CG    . LEU A 1 87  ? 43.728 13.680  33.408  1.00 44.41 ?  93  LEU A CG    1 
ATOM   648  C CD1   . LEU A 1 87  ? 44.246 12.341  33.948  1.00 43.83 ?  93  LEU A CD1   1 
ATOM   649  C CD2   . LEU A 1 87  ? 44.571 14.830  33.960  1.00 41.95 ?  93  LEU A CD2   1 
ATOM   650  N N     . LEU A 1 88  ? 43.713 15.340  28.806  1.00 40.89 ?  94  LEU A N     1 
ATOM   651  C CA    . LEU A 1 88  ? 43.552 15.204  27.365  1.00 39.87 ?  94  LEU A CA    1 
ATOM   652  C C     . LEU A 1 88  ? 44.530 14.171  26.822  1.00 42.45 ?  94  LEU A C     1 
ATOM   653  O O     . LEU A 1 88  ? 45.624 13.983  27.361  1.00 43.77 ?  94  LEU A O     1 
ATOM   654  C CB    . LEU A 1 88  ? 43.796 16.541  26.652  1.00 41.36 ?  94  LEU A CB    1 
ATOM   655  C CG    . LEU A 1 88  ? 42.645 17.519  26.421  1.00 39.34 ?  94  LEU A CG    1 
ATOM   656  C CD1   . LEU A 1 88  ? 41.687 17.511  27.589  1.00 39.15 ?  94  LEU A CD1   1 
ATOM   657  C CD2   . LEU A 1 88  ? 43.192 18.927  26.174  1.00 39.47 ?  94  LEU A CD2   1 
ATOM   658  N N     . GLN A 1 89  ? 44.133 13.505  25.740  1.00 42.32 ?  95  GLN A N     1 
ATOM   659  C CA    . GLN A 1 89  ? 45.091 12.697  24.996  1.00 44.84 ?  95  GLN A CA    1 
ATOM   660  C C     . GLN A 1 89  ? 46.214 13.592  24.488  1.00 44.20 ?  95  GLN A C     1 
ATOM   661  O O     . GLN A 1 89  ? 45.981 14.723  24.056  1.00 44.73 ?  95  GLN A O     1 
ATOM   662  C CB    . GLN A 1 89  ? 44.405 11.980  23.829  1.00 42.48 ?  95  GLN A CB    1 
ATOM   663  C CG    . GLN A 1 89  ? 45.346 11.144  22.965  1.00 44.96 ?  95  GLN A CG    1 
ATOM   664  C CD    . GLN A 1 89  ? 44.721 10.753  21.648  1.00 51.69 ?  95  GLN A CD    1 
ATOM   665  O OE1   . GLN A 1 89  ? 44.036 9.730   21.554  1.00 48.66 ?  95  GLN A OE1   1 
ATOM   666  N NE2   . GLN A 1 89  ? 44.937 11.576  20.615  1.00 52.89 ?  95  GLN A NE2   1 
ATOM   667  N N     . GLY A 1 90  ? 47.440 13.090  24.558  1.00 45.54 ?  96  GLY A N     1 
ATOM   668  C CA    . GLY A 1 90  ? 48.613 13.873  24.275  1.00 44.16 ?  96  GLY A CA    1 
ATOM   669  C C     . GLY A 1 90  ? 49.323 14.381  25.508  1.00 47.84 ?  96  GLY A C     1 
ATOM   670  O O     . GLY A 1 90  ? 50.499 14.756  25.422  1.00 51.95 ?  96  GLY A O     1 
ATOM   671  N N     . GLY A 1 91  ? 48.638 14.406  26.650  1.00 46.79 ?  97  GLY A N     1 
ATOM   672  C CA    . GLY A 1 91  ? 49.241 14.771  27.912  1.00 46.28 ?  97  GLY A CA    1 
ATOM   673  C C     . GLY A 1 91  ? 48.837 16.125  28.445  1.00 47.43 ?  97  GLY A C     1 
ATOM   674  O O     . GLY A 1 91  ? 49.246 16.467  29.562  1.00 49.68 ?  97  GLY A O     1 
ATOM   675  N N     . GLU A 1 92  ? 48.064 16.913  27.698  1.00 45.63 ?  98  GLU A N     1 
ATOM   676  C CA    . GLU A 1 92  ? 47.681 18.229  28.190  1.00 44.08 ?  98  GLU A CA    1 
ATOM   677  C C     . GLU A 1 92  ? 46.637 18.095  29.297  1.00 46.05 ?  98  GLU A C     1 
ATOM   678  O O     . GLU A 1 92  ? 45.873 17.124  29.352  1.00 44.27 ?  98  GLU A O     1 
ATOM   679  C CB    . GLU A 1 92  ? 47.155 19.105  27.049  1.00 41.15 ?  98  GLU A CB    1 
ATOM   680  N N     . ALA A 1 93  ? 46.622 19.078  30.199  1.00 43.70 ?  99  ALA A N     1 
ATOM   681  C CA    . ALA A 1 93  ? 45.718 19.071  31.341  1.00 44.68 ?  99  ALA A CA    1 
ATOM   682  C C     . ALA A 1 93  ? 45.009 20.413  31.467  1.00 44.86 ?  99  ALA A C     1 
ATOM   683  O O     . ALA A 1 93  ? 45.625 21.476  31.314  1.00 43.94 ?  99  ALA A O     1 
ATOM   684  C CB    . ALA A 1 93  ? 46.463 18.758  32.640  1.00 41.65 ?  99  ALA A CB    1 
ATOM   685  N N     . LEU A 1 94  ? 43.717 20.351  31.766  1.00 40.25 ?  100 LEU A N     1 
ATOM   686  C CA    . LEU A 1 94  ? 42.885 21.542  31.933  1.00 39.19 ?  100 LEU A CA    1 
ATOM   687  C C     . LEU A 1 94  ? 42.391 21.657  33.371  1.00 38.87 ?  100 LEU A C     1 
ATOM   688  O O     . LEU A 1 94  ? 41.588 20.814  33.817  1.00 35.86 ?  100 LEU A O     1 
ATOM   689  C CB    . LEU A 1 94  ? 41.708 21.492  30.963  1.00 35.21 ?  100 LEU A CB    1 
ATOM   690  C CG    . LEU A 1 94  ? 42.143 21.457  29.502  1.00 36.47 ?  100 LEU A CG    1 
ATOM   691  C CD1   . LEU A 1 94  ? 40.928 21.355  28.597  1.00 38.16 ?  100 LEU A CD1   1 
ATOM   692  C CD2   . LEU A 1 94  ? 42.939 22.701  29.186  1.00 35.53 ?  100 LEU A CD2   1 
ATOM   693  N N     . PRO A 1 95  ? 42.829 22.658  34.133  1.00 40.41 ?  101 PRO A N     1 
ATOM   694  C CA    . PRO A 1 95  ? 42.333 22.815  35.509  1.00 38.38 ?  101 PRO A CA    1 
ATOM   695  C C     . PRO A 1 95  ? 40.943 23.444  35.539  1.00 36.34 ?  101 PRO A C     1 
ATOM   696  O O     . PRO A 1 95  ? 40.561 24.206  34.650  1.00 35.93 ?  101 PRO A O     1 
ATOM   697  C CB    . PRO A 1 95  ? 43.381 23.733  36.158  1.00 40.94 ?  101 PRO A CB    1 
ATOM   698  C CG    . PRO A 1 95  ? 43.916 24.547  35.004  1.00 41.02 ?  101 PRO A CG    1 
ATOM   699  C CD    . PRO A 1 95  ? 43.800 23.702  33.755  1.00 40.02 ?  101 PRO A CD    1 
ATOM   700  N N     . PHE A 1 96  ? 40.167 23.086  36.566  1.00 36.71 ?  102 PHE A N     1 
ATOM   701  C CA    . PHE A 1 96  ? 38.798 23.576  36.677  1.00 33.38 ?  102 PHE A CA    1 
ATOM   702  C C     . PHE A 1 96  ? 38.435 23.836  38.129  1.00 34.22 ?  102 PHE A C     1 
ATOM   703  O O     . PHE A 1 96  ? 38.971 23.207  39.046  1.00 37.29 ?  102 PHE A O     1 
ATOM   704  C CB    . PHE A 1 96  ? 37.777 22.599  36.087  1.00 32.21 ?  102 PHE A CB    1 
ATOM   705  C CG    . PHE A 1 96  ? 37.804 21.221  36.706  1.00 33.13 ?  102 PHE A CG    1 
ATOM   706  C CD1   . PHE A 1 96  ? 37.071 20.938  37.847  1.00 32.77 ?  102 PHE A CD1   1 
ATOM   707  C CD2   . PHE A 1 96  ? 38.512 20.191  36.099  1.00 37.27 ?  102 PHE A CD2   1 
ATOM   708  C CE1   . PHE A 1 96  ? 37.076 19.658  38.400  1.00 34.62 ?  102 PHE A CE1   1 
ATOM   709  C CE2   . PHE A 1 96  ? 38.526 18.910  36.646  1.00 34.94 ?  102 PHE A CE2   1 
ATOM   710  C CZ    . PHE A 1 96  ? 37.809 18.645  37.792  1.00 36.03 ?  102 PHE A CZ    1 
ATOM   711  N N     . SER A 1 97  ? 37.527 24.787  38.328  1.00 30.26 ?  103 SER A N     1 
ATOM   712  C CA    . SER A 1 97  ? 36.849 24.915  39.610  1.00 33.34 ?  103 SER A CA    1 
ATOM   713  C C     . SER A 1 97  ? 35.523 24.176  39.595  1.00 32.35 ?  103 SER A C     1 
ATOM   714  O O     . SER A 1 97  ? 35.064 23.695  40.640  1.00 30.40 ?  103 SER A O     1 
ATOM   715  C CB    . SER A 1 97  ? 36.605 26.389  39.946  1.00 31.95 ?  103 SER A CB    1 
ATOM   716  O OG    . SER A 1 97  ? 35.729 26.971  38.995  1.00 29.94 ?  103 SER A OG    1 
ATOM   717  N N     . HIS A 1 98  ? 34.905 24.093  38.420  1.00 27.73 ?  104 HIS A N     1 
ATOM   718  C CA    . HIS A 1 98  ? 33.665 23.369  38.211  1.00 30.74 ?  104 HIS A CA    1 
ATOM   719  C C     . HIS A 1 98  ? 33.773 22.583  36.915  1.00 28.00 ?  104 HIS A C     1 
ATOM   720  O O     . HIS A 1 98  ? 34.392 23.044  35.953  1.00 27.42 ?  104 HIS A O     1 
ATOM   721  C CB    . HIS A 1 98  ? 32.478 24.325  38.173  1.00 30.05 ?  104 HIS A CB    1 
ATOM   722  C CG    . HIS A 1 98  ? 32.329 25.127  39.427  1.00 28.61 ?  104 HIS A CG    1 
ATOM   723  N ND1   . HIS A 1 98  ? 33.237 26.092  39.802  1.00 29.38 ?  104 HIS A ND1   1 
ATOM   724  C CD2   . HIS A 1 98  ? 31.401 25.081  40.409  1.00 31.29 ?  104 HIS A CD2   1 
ATOM   725  C CE1   . HIS A 1 98  ? 32.869 26.618  40.955  1.00 31.57 ?  104 HIS A CE1   1 
ATOM   726  N NE2   . HIS A 1 98  ? 31.754 26.025  41.344  1.00 33.44 ?  104 HIS A NE2   1 
ATOM   727  N N     . LEU A 1 99  ? 33.191 21.386  36.908  1.00 28.05 ?  105 LEU A N     1 
ATOM   728  C CA    . LEU A 1 99  ? 33.232 20.493  35.759  1.00 26.68 ?  105 LEU A CA    1 
ATOM   729  C C     . LEU A 1 99  ? 31.817 20.157  35.307  1.00 29.33 ?  105 LEU A C     1 
ATOM   730  O O     . LEU A 1 99  ? 30.975 19.750  36.117  1.00 29.68 ?  105 LEU A O     1 
ATOM   731  C CB    . LEU A 1 99  ? 33.994 19.220  36.104  1.00 29.53 ?  105 LEU A CB    1 
ATOM   732  C CG    . LEU A 1 99  ? 33.987 18.110  35.061  1.00 30.97 ?  105 LEU A CG    1 
ATOM   733  C CD1   . LEU A 1 99  ? 34.833 18.491  33.860  1.00 26.39 ?  105 LEU A CD1   1 
ATOM   734  C CD2   . LEU A 1 99  ? 34.501 16.855  35.749  1.00 31.18 ?  105 LEU A CD2   1 
ATOM   735  N N     . ILE A 1 100 ? 31.562 20.305  34.011  1.00 26.49 ?  106 ILE A N     1 
ATOM   736  C CA    . ILE A 1 100 ? 30.296 19.925  33.405  1.00 24.13 ?  106 ILE A CA    1 
ATOM   737  C C     . ILE A 1 100 ? 30.583 18.779  32.451  1.00 26.98 ?  106 ILE A C     1 
ATOM   738  O O     . ILE A 1 100 ? 31.316 18.956  31.471  1.00 23.70 ?  106 ILE A O     1 
ATOM   739  C CB    . ILE A 1 100 ? 29.645 21.099  32.658  1.00 24.65 ?  106 ILE A CB    1 
ATOM   740  C CG1   . ILE A 1 100 ? 29.302 22.247  33.613  1.00 22.72 ?  106 ILE A CG1   1 
ATOM   741  C CG2   . ILE A 1 100 ? 28.400 20.636  31.925  1.00 24.37 ?  106 ILE A CG2   1 
ATOM   742  C CD1   . ILE A 1 100 ? 28.630 23.436  32.877  1.00 21.00 ?  106 ILE A CD1   1 
ATOM   743  N N     . LEU A 1 101 ? 30.007 17.610  32.725  1.00 24.89 ?  107 LEU A N     1 
ATOM   744  C CA    . LEU A 1 101 ? 30.183 16.453  31.860  1.00 26.81 ?  107 LEU A CA    1 
ATOM   745  C C     . LEU A 1 101 ? 28.980 16.341  30.927  1.00 22.76 ?  107 LEU A C     1 
ATOM   746  O O     . LEU A 1 101 ? 27.833 16.245  31.375  1.00 22.86 ?  107 LEU A O     1 
ATOM   747  C CB    . LEU A 1 101 ? 30.398 15.181  32.683  1.00 27.07 ?  107 LEU A CB    1 
ATOM   748  C CG    . LEU A 1 101 ? 31.704 15.160  33.498  1.00 29.94 ?  107 LEU A CG    1 
ATOM   749  C CD1   . LEU A 1 101 ? 31.688 14.116  34.608  1.00 36.41 ?  107 LEU A CD1   1 
ATOM   750  C CD2   . LEU A 1 101 ? 32.916 14.951  32.614  1.00 29.73 ?  107 LEU A CD2   1 
ATOM   751  N N     . ALA A 1 102 ? 29.246 16.389  29.630  1.00 24.27 ?  108 ALA A N     1 
ATOM   752  C CA    . ALA A 1 102 ? 28.207 16.448  28.617  1.00 22.26 ?  108 ALA A CA    1 
ATOM   753  C C     . ALA A 1 102 ? 28.613 15.570  27.440  1.00 24.06 ?  108 ALA A C     1 
ATOM   754  O O     . ALA A 1 102 ? 28.577 15.986  26.282  1.00 21.04 ?  108 ALA A O     1 
ATOM   755  C CB    . ALA A 1 102 ? 27.971 17.892  28.183  1.00 20.71 ?  108 ALA A CB    1 
ATOM   756  N N     . THR A 1 103 ? 29.010 14.330  27.740  1.00 25.25 ?  109 THR A N     1 
ATOM   757  C CA    . THR A 1 103 ? 29.687 13.459  26.784  1.00 24.65 ?  109 THR A CA    1 
ATOM   758  C C     . THR A 1 103 ? 28.750 12.708  25.848  1.00 25.12 ?  109 THR A C     1 
ATOM   759  O O     . THR A 1 103 ? 29.239 12.026  24.941  1.00 25.79 ?  109 THR A O     1 
ATOM   760  C CB    . THR A 1 103 ? 30.539 12.449  27.531  1.00 27.39 ?  109 THR A CB    1 
ATOM   761  O OG1   . THR A 1 103 ? 29.703 11.752  28.465  1.00 29.90 ?  109 THR A OG1   1 
ATOM   762  C CG2   . THR A 1 103 ? 31.646 13.172  28.282  1.00 29.31 ?  109 THR A CG2   1 
ATOM   763  N N     . GLY A 1 104 ? 27.437 12.798  26.043  1.00 25.41 ?  110 GLY A N     1 
ATOM   764  C CA    . GLY A 1 104 ? 26.488 12.212  25.100  1.00 26.00 ?  110 GLY A CA    1 
ATOM   765  C C     . GLY A 1 104 ? 26.557 10.696  24.988  1.00 27.04 ?  110 GLY A C     1 
ATOM   766  O O     . GLY A 1 104 ? 26.910 9.979   25.932  1.00 26.38 ?  110 GLY A O     1 
ATOM   767  N N     . SER A 1 105 ? 26.206 10.206  23.795  1.00 26.67 ?  111 SER A N     1 
ATOM   768  C CA    . SER A 1 105 ? 26.138 8.786   23.466  1.00 27.82 ?  111 SER A CA    1 
ATOM   769  C C     . SER A 1 105 ? 26.966 8.471   22.224  1.00 28.92 ?  111 SER A C     1 
ATOM   770  O O     . SER A 1 105 ? 27.204 9.332   21.373  1.00 28.50 ?  111 SER A O     1 
ATOM   771  C CB    . SER A 1 105 ? 24.696 8.337   23.195  1.00 28.38 ?  111 SER A CB    1 
ATOM   772  O OG    . SER A 1 105 ? 23.902 8.375   24.357  1.00 34.78 ?  111 SER A OG    1 
ATOM   773  N N     . THR A 1 106 ? 27.358 7.205   22.114  1.00 27.37 ?  112 THR A N     1 
ATOM   774  C CA    . THR A 1 106 ? 28.088 6.667   20.976  1.00 28.09 ?  112 THR A CA    1 
ATOM   775  C C     . THR A 1 106 ? 27.271 5.565   20.301  1.00 26.98 ?  112 THR A C     1 
ATOM   776  O O     . THR A 1 106 ? 26.483 4.871   20.942  1.00 25.40 ?  112 THR A O     1 
ATOM   777  C CB    . THR A 1 106 ? 29.449 6.118   21.430  1.00 32.82 ?  112 THR A CB    1 
ATOM   778  O OG1   . THR A 1 106 ? 30.232 5.760   20.293  1.00 43.57 ?  112 THR A OG1   1 
ATOM   779  C CG2   . THR A 1 106 ? 29.268 4.885   22.284  1.00 30.84 ?  112 THR A CG2   1 
ATOM   780  N N     . GLY A 1 107 ? 27.457 5.397   18.997  1.00 23.93 ?  113 GLY A N     1 
ATOM   781  C CA    . GLY A 1 107 ? 26.747 4.368   18.280  1.00 23.80 ?  113 GLY A CA    1 
ATOM   782  C C     . GLY A 1 107 ? 27.157 4.340   16.827  1.00 25.76 ?  113 GLY A C     1 
ATOM   783  O O     . GLY A 1 107 ? 28.049 5.085   16.404  1.00 24.39 ?  113 GLY A O     1 
ATOM   784  N N     . PRO A 1 108 ? 26.510 3.485   16.032  1.00 22.65 ?  114 PRO A N     1 
ATOM   785  C CA    . PRO A 1 108 ? 26.893 3.362   14.614  1.00 23.77 ?  114 PRO A CA    1 
ATOM   786  C C     . PRO A 1 108 ? 26.577 4.608   13.799  1.00 20.78 ?  114 PRO A C     1 
ATOM   787  O O     . PRO A 1 108 ? 25.554 5.273   13.994  1.00 18.81 ?  114 PRO A O     1 
ATOM   788  C CB    . PRO A 1 108 ? 26.078 2.156   14.121  1.00 21.75 ?  114 PRO A CB    1 
ATOM   789  C CG    . PRO A 1 108 ? 24.944 2.025   15.100  1.00 24.99 ?  114 PRO A CG    1 
ATOM   790  C CD    . PRO A 1 108 ? 25.495 2.490   16.422  1.00 22.45 ?  114 PRO A CD    1 
ATOM   791  N N     . PHE A 1 109 ? 27.499 4.923   12.892  1.00 20.18 ?  115 PHE A N     1 
ATOM   792  C CA    . PHE A 1 109 ? 27.218 5.778   11.750  1.00 22.06 ?  115 PHE A CA    1 
ATOM   793  C C     . PHE A 1 109 ? 26.096 5.148   10.924  1.00 20.32 ?  115 PHE A C     1 
ATOM   794  O O     . PHE A 1 109 ? 26.024 3.925   10.820  1.00 21.81 ?  115 PHE A O     1 
ATOM   795  C CB    . PHE A 1 109 ? 28.490 5.921   10.900  1.00 19.59 ?  115 PHE A CB    1 
ATOM   796  C CG    . PHE A 1 109 ? 28.380 6.937   9.816   1.00 20.77 ?  115 PHE A CG    1 
ATOM   797  C CD1   . PHE A 1 109 ? 28.569 8.276   10.092  1.00 19.48 ?  115 PHE A CD1   1 
ATOM   798  C CD2   . PHE A 1 109 ? 28.086 6.552   8.512   1.00 23.27 ?  115 PHE A CD2   1 
ATOM   799  C CE1   . PHE A 1 109 ? 28.457 9.222   9.091   1.00 20.03 ?  115 PHE A CE1   1 
ATOM   800  C CE2   . PHE A 1 109 ? 27.972 7.488   7.503   1.00 22.23 ?  115 PHE A CE2   1 
ATOM   801  C CZ    . PHE A 1 109 ? 28.171 8.825   7.787   1.00 20.36 ?  115 PHE A CZ    1 
ATOM   802  N N     . PRO A 1 110 ? 25.206 5.950   10.316  1.00 21.36 ?  116 PRO A N     1 
ATOM   803  C CA    . PRO A 1 110 ? 25.145 7.428   10.266  1.00 19.78 ?  116 PRO A CA    1 
ATOM   804  C C     . PRO A 1 110 ? 24.498 8.103   11.471  1.00 19.34 ?  116 PRO A C     1 
ATOM   805  O O     . PRO A 1 110 ? 24.637 9.311   11.609  1.00 16.64 ?  116 PRO A O     1 
ATOM   806  C CB    . PRO A 1 110 ? 24.304 7.686   9.005   1.00 18.36 ?  116 PRO A CB    1 
ATOM   807  C CG    . PRO A 1 110 ? 23.315 6.533   9.024   1.00 19.86 ?  116 PRO A CG    1 
ATOM   808  C CD    . PRO A 1 110 ? 24.155 5.341   9.469   1.00 19.19 ?  116 PRO A CD    1 
ATOM   809  N N     . GLY A 1 111 ? 23.787 7.378   12.342  1.00 22.07 ?  117 GLY A N     1 
ATOM   810  C CA    . GLY A 1 111 ? 23.016 8.013   13.403  1.00 19.77 ?  117 GLY A CA    1 
ATOM   811  C C     . GLY A 1 111 ? 23.848 8.773   14.417  1.00 22.85 ?  117 GLY A C     1 
ATOM   812  O O     . GLY A 1 111 ? 23.321 9.681   15.073  1.00 20.26 ?  117 GLY A O     1 
ATOM   813  N N     . LYS A 1 112 ? 25.126 8.404   14.577  1.00 18.12 ?  118 LYS A N     1 
ATOM   814  C CA    . LYS A 1 112 ? 26.077 9.095   15.439  1.00 22.73 ?  118 LYS A CA    1 
ATOM   815  C C     . LYS A 1 112 ? 27.378 9.277   14.665  1.00 23.16 ?  118 LYS A C     1 
ATOM   816  O O     . LYS A 1 112 ? 27.755 8.422   13.858  1.00 22.79 ?  118 LYS A O     1 
ATOM   817  C CB    . LYS A 1 112 ? 26.374 8.309   16.750  1.00 22.65 ?  118 LYS A CB    1 
ATOM   818  C CG    . LYS A 1 112 ? 25.174 8.072   17.652  1.00 23.96 ?  118 LYS A CG    1 
ATOM   819  C CD    . LYS A 1 112 ? 24.529 9.399   18.089  1.00 29.23 ?  118 LYS A CD    1 
ATOM   820  C CE    . LYS A 1 112 ? 23.458 9.189   19.169  1.00 28.99 ?  118 LYS A CE    1 
ATOM   821  N NZ    . LYS A 1 112 ? 22.600 10.429  19.427  1.00 27.34 ?  118 LYS A NZ    1 
ATOM   822  N N     . PHE A 1 113 ? 28.067 10.388  14.917  1.00 20.47 ?  119 PHE A N     1 
ATOM   823  C CA    . PHE A 1 113 ? 29.348 10.668  14.270  1.00 22.67 ?  119 PHE A CA    1 
ATOM   824  C C     . PHE A 1 113 ? 30.352 11.125  15.323  1.00 25.42 ?  119 PHE A C     1 
ATOM   825  O O     . PHE A 1 113 ? 30.413 12.307  15.676  1.00 28.25 ?  119 PHE A O     1 
ATOM   826  C CB    . PHE A 1 113 ? 29.203 11.717  13.177  1.00 19.93 ?  119 PHE A CB    1 
ATOM   827  C CG    . PHE A 1 113 ? 30.469 11.978  12.446  1.00 22.50 ?  119 PHE A CG    1 
ATOM   828  C CD1   . PHE A 1 113 ? 30.855 11.159  11.396  1.00 24.25 ?  119 PHE A CD1   1 
ATOM   829  C CD2   . PHE A 1 113 ? 31.289 13.027  12.812  1.00 22.00 ?  119 PHE A CD2   1 
ATOM   830  C CE1   . PHE A 1 113 ? 32.043 11.378  10.726  1.00 23.82 ?  119 PHE A CE1   1 
ATOM   831  C CE2   . PHE A 1 113 ? 32.466 13.250  12.150  1.00 24.78 ?  119 PHE A CE2   1 
ATOM   832  C CZ    . PHE A 1 113 ? 32.848 12.422  11.102  1.00 24.85 ?  119 PHE A CZ    1 
ATOM   833  N N     . ASN A 1 114 ? 31.164 10.214  15.807  1.00 25.70 ?  120 ASN A N     1 
ATOM   834  C CA    . ASN A 1 114 ? 32.106 10.533  16.872  1.00 30.12 ?  120 ASN A CA    1 
ATOM   835  C C     . ASN A 1 114 ? 33.510 10.185  16.398  1.00 29.17 ?  120 ASN A C     1 
ATOM   836  O O     . ASN A 1 114 ? 34.147 9.247   16.872  1.00 32.75 ?  120 ASN A O     1 
ATOM   837  C CB    . ASN A 1 114 ? 31.726 9.812   18.163  1.00 32.63 ?  120 ASN A CB    1 
ATOM   838  C CG    . ASN A 1 114 ? 30.449 10.375  18.763  1.00 32.96 ?  120 ASN A CG    1 
ATOM   839  O OD1   . ASN A 1 114 ? 30.346 11.588  19.003  1.00 32.73 ?  120 ASN A OD1   1 
ATOM   840  N ND2   . ASN A 1 114 ? 29.454 9.516   18.956  1.00 31.41 ?  120 ASN A ND2   1 
ATOM   841  N N     . GLU A 1 115 ? 33.985 10.956  15.441  1.00 31.39 ?  121 GLU A N     1 
ATOM   842  C CA    . GLU A 1 115 ? 35.312 10.783  14.886  1.00 33.19 ?  121 GLU A CA    1 
ATOM   843  C C     . GLU A 1 115 ? 36.070 12.083  15.067  1.00 33.11 ?  121 GLU A C     1 
ATOM   844  O O     . GLU A 1 115 ? 35.480 13.166  15.039  1.00 32.16 ?  121 GLU A O     1 
ATOM   845  C CB    . GLU A 1 115 ? 35.252 10.397  13.407  1.00 32.16 ?  121 GLU A CB    1 
ATOM   846  C CG    . GLU A 1 115 ? 34.713 8.990   13.155  1.00 37.65 ?  121 GLU A CG    1 
ATOM   847  C CD    . GLU A 1 115 ? 34.509 8.688   11.663  1.00 49.64 ?  121 GLU A CD    1 
ATOM   848  O OE1   . GLU A 1 115 ? 35.442 8.960   10.870  1.00 53.07 ?  121 GLU A OE1   1 
ATOM   849  O OE2   . GLU A 1 115 ? 33.416 8.185   11.276  1.00 50.67 -1 121 GLU A OE2   1 
ATOM   850  N N     . VAL A 1 116 ? 37.371 11.975  15.290  1.00 31.98 ?  122 VAL A N     1 
ATOM   851  C CA    . VAL A 1 116 ? 38.203 13.159  15.177  1.00 34.92 ?  122 VAL A CA    1 
ATOM   852  C C     . VAL A 1 116 ? 38.375 13.443  13.696  1.00 39.94 ?  122 VAL A C     1 
ATOM   853  O O     . VAL A 1 116 ? 38.840 12.580  12.939  1.00 38.61 ?  122 VAL A O     1 
ATOM   854  C CB    . VAL A 1 116 ? 39.558 12.962  15.865  1.00 32.99 ?  122 VAL A CB    1 
ATOM   855  C CG1   . VAL A 1 116 ? 40.392 14.234  15.743  1.00 31.17 ?  122 VAL A CG1   1 
ATOM   856  C CG2   . VAL A 1 116 ? 39.360 12.578  17.335  1.00 32.96 ?  122 VAL A CG2   1 
ATOM   857  N N     . SER A 1 117 ? 37.973 14.634  13.270  1.00 39.18 ?  123 SER A N     1 
ATOM   858  C CA    . SER A 1 117 ? 38.180 15.019  11.878  1.00 40.20 ?  123 SER A CA    1 
ATOM   859  C C     . SER A 1 117 ? 37.714 16.453  11.703  1.00 39.82 ?  123 SER A C     1 
ATOM   860  O O     . SER A 1 117 ? 37.131 17.069  12.609  1.00 40.86 ?  123 SER A O     1 
ATOM   861  C CB    . SER A 1 117 ? 37.434 14.107  10.895  1.00 39.49 ?  123 SER A CB    1 
ATOM   862  O OG    . SER A 1 117 ? 36.100 14.561  10.708  1.00 39.19 ?  123 SER A OG    1 
ATOM   863  N N     . SER A 1 118 ? 37.942 16.955  10.502  1.00 33.59 ?  124 SER A N     1 
ATOM   864  C CA    . SER A 1 118 ? 37.595 18.318  10.175  1.00 30.44 ?  124 SER A CA    1 
ATOM   865  C C     . SER A 1 118 ? 36.135 18.407  9.740   1.00 25.57 ?  124 SER A C     1 
ATOM   866  O O     . SER A 1 118 ? 35.484 17.408  9.405   1.00 24.76 ?  124 SER A O     1 
ATOM   867  C CB    . SER A 1 118 ? 38.514 18.835  9.072   1.00 27.76 ?  124 SER A CB    1 
ATOM   868  O OG    . SER A 1 118 ? 38.341 18.055  7.904   1.00 25.58 ?  124 SER A OG    1 
ATOM   869  N N     . GLN A 1 119 ? 35.638 19.640  9.721   1.00 22.47 ?  125 GLN A N     1 
ATOM   870  C CA    . GLN A 1 119 ? 34.268 19.886  9.300   1.00 22.18 ?  125 GLN A CA    1 
ATOM   871  C C     . GLN A 1 119 ? 34.007 19.389  7.883   1.00 21.69 ?  125 GLN A C     1 
ATOM   872  O O     . GLN A 1 119 ? 32.922 18.872  7.596   1.00 18.87 ?  125 GLN A O     1 
ATOM   873  C CB    . GLN A 1 119 ? 33.958 21.376  9.396   1.00 25.21 ?  125 GLN A CB    1 
ATOM   874  C CG    . GLN A 1 119 ? 32.485 21.682  9.158   1.00 23.38 ?  125 GLN A CG    1 
ATOM   875  C CD    . GLN A 1 119 ? 32.175 23.148  9.300   1.00 27.48 ?  125 GLN A CD    1 
ATOM   876  O OE1   . GLN A 1 119 ? 32.380 23.938  8.371   1.00 38.90 ?  125 GLN A OE1   1 
ATOM   877  N NE2   . GLN A 1 119 ? 31.706 23.528  10.465  1.00 26.57 ?  125 GLN A NE2   1 
ATOM   878  N N     . GLN A 1 120 ? 34.975 19.546  6.976   1.00 21.66 ?  126 GLN A N     1 
ATOM   879  C CA    . GLN A 1 120 ? 34.718 19.129  5.599   1.00 23.09 ?  126 GLN A CA    1 
ATOM   880  C C     . GLN A 1 120 ? 34.758 17.606  5.453   1.00 21.99 ?  126 GLN A C     1 
ATOM   881  O O     . GLN A 1 120 ? 33.984 17.042  4.673   1.00 20.91 ?  126 GLN A O     1 
ATOM   882  C CB    . GLN A 1 120 ? 35.702 19.805  4.634   1.00 22.86 ?  126 GLN A CB    1 
ATOM   883  C CG    . GLN A 1 120 ? 35.402 21.296  4.377   1.00 27.12 ?  126 GLN A CG    1 
ATOM   884  C CD    . GLN A 1 120 ? 33.877 21.630  4.400   1.00 32.59 ?  126 GLN A CD    1 
ATOM   885  O OE1   . GLN A 1 120 ? 33.104 21.135  3.562   1.00 26.52 ?  126 GLN A OE1   1 
ATOM   886  N NE2   . GLN A 1 120 ? 33.455 22.458  5.375   1.00 26.29 ?  126 GLN A NE2   1 
ATOM   887  N N     . ALA A 1 121 ? 35.644 16.920  6.182   1.00 22.47 ?  127 ALA A N     1 
ATOM   888  C CA    . ALA A 1 121 ? 35.631 15.460  6.156   1.00 22.74 ?  127 ALA A CA    1 
ATOM   889  C C     . ALA A 1 121 ? 34.328 14.904  6.733   1.00 21.13 ?  127 ALA A C     1 
ATOM   890  O O     . ALA A 1 121 ? 33.774 13.937  6.199   1.00 20.84 ?  127 ALA A O     1 
ATOM   891  C CB    . ALA A 1 121 ? 36.839 14.898  6.908   1.00 24.36 ?  127 ALA A CB    1 
ATOM   892  N N     . ALA A 1 122 ? 33.805 15.514  7.805   1.00 20.89 ?  128 ALA A N     1 
ATOM   893  C CA    . ALA A 1 122 ? 32.541 15.044  8.386   1.00 19.74 ?  128 ALA A CA    1 
ATOM   894  C C     . ALA A 1 122 ? 31.381 15.210  7.414   1.00 17.73 ?  128 ALA A C     1 
ATOM   895  O O     . ALA A 1 122 ? 30.562 14.297  7.242   1.00 17.16 ?  128 ALA A O     1 
ATOM   896  C CB    . ALA A 1 122 ? 32.242 15.792  9.688   1.00 18.37 ?  128 ALA A CB    1 
ATOM   897  N N     . ILE A 1 123 ? 31.263 16.400  6.817   1.00 17.52 ?  129 ILE A N     1 
ATOM   898  C CA    . ILE A 1 123 ? 30.240 16.659  5.807   1.00 17.59 ?  129 ILE A CA    1 
ATOM   899  C C     . ILE A 1 123 ? 30.353 15.654  4.661   1.00 18.81 ?  129 ILE A C     1 
ATOM   900  O O     . ILE A 1 123 ? 29.348 15.098  4.200   1.00 16.64 ?  129 ILE A O     1 
ATOM   901  C CB    . ILE A 1 123 ? 30.359 18.112  5.297   1.00 18.51 ?  129 ILE A CB    1 
ATOM   902  C CG1   . ILE A 1 123 ? 29.887 19.114  6.351   1.00 18.28 ?  129 ILE A CG1   1 
ATOM   903  C CG2   . ILE A 1 123 ? 29.550 18.318  4.025   1.00 19.01 ?  129 ILE A CG2   1 
ATOM   904  C CD1   . ILE A 1 123 ? 30.308 20.543  6.026   1.00 18.18 ?  129 ILE A CD1   1 
ATOM   905  N N     . GLN A 1 124 ? 31.580 15.396  4.199   1.00 18.68 ?  130 GLN A N     1 
ATOM   906  C CA    . GLN A 1 124 ? 31.793 14.450  3.109   1.00 19.85 ?  130 GLN A CA    1 
ATOM   907  C C     . GLN A 1 124 ? 31.416 13.018  3.487   1.00 20.79 ?  130 GLN A C     1 
ATOM   908  O O     . GLN A 1 124 ? 31.049 12.224  2.609   1.00 20.00 ?  130 GLN A O     1 
ATOM   909  C CB    . GLN A 1 124 ? 33.245 14.491  2.654   1.00 22.12 ?  130 GLN A CB    1 
ATOM   910  C CG    . GLN A 1 124 ? 33.467 13.706  1.377   1.00 28.15 ?  130 GLN A CG    1 
ATOM   911  C CD    . GLN A 1 124 ? 32.755 14.329  0.189   1.00 30.08 ?  130 GLN A CD    1 
ATOM   912  O OE1   . GLN A 1 124 ? 32.897 15.527  -0.078  1.00 33.87 ?  130 GLN A OE1   1 
ATOM   913  N NE2   . GLN A 1 124 ? 31.974 13.525  -0.523  1.00 28.19 ?  130 GLN A NE2   1 
ATOM   914  N N     . ALA A 1 125 ? 31.539 12.648  4.760   1.00 19.39 ?  131 ALA A N     1 
ATOM   915  C CA    . ALA A 1 125 ? 31.123 11.305  5.153   1.00 22.18 ?  131 ALA A CA    1 
ATOM   916  C C     . ALA A 1 125 ? 29.620 11.118  4.963   1.00 20.05 ?  131 ALA A C     1 
ATOM   917  O O     . ALA A 1 125 ? 29.172 10.026  4.588   1.00 18.65 ?  131 ALA A O     1 
ATOM   918  C CB    . ALA A 1 125 ? 31.516 11.031  6.611   1.00 21.22 ?  131 ALA A CB    1 
ATOM   919  N N     . TYR A 1 126 ? 28.831 12.168  5.204   1.00 16.50 ?  132 TYR A N     1 
ATOM   920  C CA    . TYR A 1 126 ? 27.391 12.078  4.985   1.00 15.69 ?  132 TYR A CA    1 
ATOM   921  C C     . TYR A 1 126 ? 27.049 12.198  3.499   1.00 19.78 ?  132 TYR A C     1 
ATOM   922  O O     . TYR A 1 126 ? 26.160 11.489  3.009   1.00 18.16 ?  132 TYR A O     1 
ATOM   923  C CB    . TYR A 1 126 ? 26.668 13.130  5.842   1.00 15.32 ?  132 TYR A CB    1 
ATOM   924  C CG    . TYR A 1 126 ? 26.543 12.680  7.286   1.00 14.27 ?  132 TYR A CG    1 
ATOM   925  C CD1   . TYR A 1 126 ? 25.480 11.888  7.682   1.00 15.45 ?  132 TYR A CD1   1 
ATOM   926  C CD2   . TYR A 1 126 ? 27.515 12.987  8.227   1.00 14.83 ?  132 TYR A CD2   1 
ATOM   927  C CE1   . TYR A 1 126 ? 25.381 11.422  8.986   1.00 14.95 ?  132 TYR A CE1   1 
ATOM   928  C CE2   . TYR A 1 126 ? 27.419 12.534  9.553   1.00 14.93 ?  132 TYR A CE2   1 
ATOM   929  C CZ    . TYR A 1 126 ? 26.354 11.750  9.913   1.00 16.01 ?  132 TYR A CZ    1 
ATOM   930  O OH    . TYR A 1 126 ? 26.228 11.272  11.198  1.00 19.49 ?  132 TYR A OH    1 
ATOM   931  N N     . GLU A 1 127 ? 27.759 13.050  2.748   1.00 19.97 ?  133 GLU A N     1 
ATOM   932  C CA    . GLU A 1 127 ? 27.565 13.064  1.293   1.00 19.63 ?  133 GLU A CA    1 
ATOM   933  C C     . GLU A 1 127 ? 27.935 11.720  0.670   1.00 22.41 ?  133 GLU A C     1 
ATOM   934  O O     . GLU A 1 127 ? 27.277 11.267  -0.274  1.00 22.48 ?  133 GLU A O     1 
ATOM   935  C CB    . GLU A 1 127 ? 28.370 14.193  0.641   1.00 18.17 ?  133 GLU A CB    1 
ATOM   936  C CG    . GLU A 1 127 ? 27.862 15.599  0.983   1.00 22.56 ?  133 GLU A CG    1 
ATOM   937  C CD    . GLU A 1 127 ? 26.427 15.869  0.472   1.00 27.72 ?  133 GLU A CD    1 
ATOM   938  O OE1   . GLU A 1 127 ? 25.925 15.131  -0.427  1.00 26.17 ?  133 GLU A OE1   1 
ATOM   939  O OE2   . GLU A 1 127 ? 25.800 16.830  0.973   1.00 27.00 -1 133 GLU A OE2   1 
ATOM   940  N N     . ASP A 1 128 ? 28.993 11.068  1.171   1.00 21.32 ?  134 ASP A N     1 
ATOM   941  C CA    . ASP A 1 128 ? 29.318 9.729   0.689   1.00 23.92 ?  134 ASP A CA    1 
ATOM   942  C C     . ASP A 1 128 ? 28.206 8.743   1.014   1.00 24.51 ?  134 ASP A C     1 
ATOM   943  O O     . ASP A 1 128 ? 27.878 7.879   0.194   1.00 23.36 ?  134 ASP A O     1 
ATOM   944  C CB    . ASP A 1 128 ? 30.636 9.243   1.285   1.00 24.34 ?  134 ASP A CB    1 
ATOM   945  C CG    . ASP A 1 128 ? 31.856 9.904   0.642   1.00 32.26 ?  134 ASP A CG    1 
ATOM   946  O OD1   . ASP A 1 128 ? 31.711 10.619  -0.390  1.00 31.84 ?  134 ASP A OD1   1 
ATOM   947  O OD2   . ASP A 1 128 ? 32.974 9.706   1.178   1.00 36.87 -1 134 ASP A OD2   1 
ATOM   948  N N     . MET A 1 129 ? 27.638 8.841   2.218   1.00 21.43 ?  135 MET A N     1 
ATOM   949  C CA    . MET A 1 129 ? 26.505 8.003   2.596   1.00 22.75 ?  135 MET A CA    1 
ATOM   950  C C     . MET A 1 129 ? 25.338 8.196   1.635   1.00 20.19 ?  135 MET A C     1 
ATOM   951  O O     . MET A 1 129 ? 24.734 7.226   1.173   1.00 18.82 ?  135 MET A O     1 
ATOM   952  C CB    . MET A 1 129 ? 26.079 8.325   4.032   1.00 20.13 ?  135 MET A CB    1 
ATOM   953  C CG    . MET A 1 129 ? 25.002 7.405   4.596   1.00 19.77 ?  135 MET A CG    1 
ATOM   954  S SD    . MET A 1 129 ? 25.613 5.696   4.816   1.00 26.19 ?  135 MET A SD    1 
ATOM   955  C CE    . MET A 1 129 ? 24.088 4.817   4.657   1.00 27.12 ?  135 MET A CE    1 
ATOM   956  N N     . VAL A 1 130 ? 24.995 9.451   1.336   1.00 19.99 ?  136 VAL A N     1 
ATOM   957  C CA    . VAL A 1 130 ? 23.952 9.728   0.349   1.00 18.29 ?  136 VAL A CA    1 
ATOM   958  C C     . VAL A 1 130 ? 24.259 9.025   -0.975  1.00 19.90 ?  136 VAL A C     1 
ATOM   959  O O     . VAL A 1 130 ? 23.363 8.468   -1.615  1.00 17.87 ?  136 VAL A O     1 
ATOM   960  C CB    . VAL A 1 130 ? 23.798 11.250  0.145   1.00 20.02 ?  136 VAL A CB    1 
ATOM   961  C CG1   . VAL A 1 130 ? 22.782 11.543  -0.953  1.00 20.37 ?  136 VAL A CG1   1 
ATOM   962  C CG2   . VAL A 1 130 ? 23.420 11.945  1.446   1.00 18.89 ?  136 VAL A CG2   1 
ATOM   963  N N     . ARG A 1 131 ? 25.522 9.053   -1.423  1.00 19.94 ?  137 ARG A N     1 
ATOM   964  C CA    . ARG A 1 131 ? 25.848 8.387   -2.686  1.00 22.66 ?  137 ARG A CA    1 
ATOM   965  C C     . ARG A 1 131 ? 25.689 6.868   -2.592  1.00 21.80 ?  137 ARG A C     1 
ATOM   966  O O     . ARG A 1 131 ? 25.331 6.230   -3.585  1.00 20.49 ?  137 ARG A O     1 
ATOM   967  C CB    . ARG A 1 131 ? 27.265 8.750   -3.143  1.00 23.41 ?  137 ARG A CB    1 
ATOM   968  C CG    . ARG A 1 131 ? 27.434 10.228  -3.542  1.00 28.52 ?  137 ARG A CG    1 
ATOM   969  C CD    . ARG A 1 131 ? 28.900 10.560  -3.873  1.00 35.75 ?  137 ARG A CD    1 
ATOM   970  N N     . GLN A 1 132 ? 25.946 6.259   -1.428  1.00 21.26 ?  138 GLN A N     1 
ATOM   971  C CA    . GLN A 1 132 ? 25.727 4.812   -1.345  1.00 22.88 ?  138 GLN A CA    1 
ATOM   972  C C     . GLN A 1 132 ? 24.237 4.490   -1.417  1.00 20.81 ?  138 GLN A C     1 
ATOM   973  O O     . GLN A 1 132 ? 23.828 3.531   -2.085  1.00 19.54 ?  138 GLN A O     1 
ATOM   974  C CB    . GLN A 1 132 ? 26.324 4.231   -0.058  1.00 22.24 ?  138 GLN A CB    1 
ATOM   975  C CG    . GLN A 1 132 ? 27.769 4.617   0.251   1.00 24.53 ?  138 GLN A CG    1 
ATOM   976  C CD    . GLN A 1 132 ? 28.790 4.067   -0.720  1.00 29.78 ?  138 GLN A CD    1 
ATOM   977  O OE1   . GLN A 1 132 ? 28.547 3.090   -1.450  1.00 27.20 ?  138 GLN A OE1   1 
ATOM   978  N NE2   . GLN A 1 132 ? 29.963 4.693   -0.732  1.00 35.43 ?  138 GLN A NE2   1 
ATOM   979  N N     . VAL A 1 133 ? 23.414 5.277   -0.720  1.00 20.51 ?  139 VAL A N     1 
ATOM   980  C CA    . VAL A 1 133 ? 21.971 5.091   -0.800  1.00 17.01 ?  139 VAL A CA    1 
ATOM   981  C C     . VAL A 1 133 ? 21.510 5.268   -2.244  1.00 19.26 ?  139 VAL A C     1 
ATOM   982  O O     . VAL A 1 133 ? 20.708 4.474   -2.753  1.00 17.70 ?  139 VAL A O     1 
ATOM   983  C CB    . VAL A 1 133 ? 21.257 6.048   0.174   1.00 19.25 ?  139 VAL A CB    1 
ATOM   984  C CG1   . VAL A 1 133 ? 19.777 6.192   -0.163  1.00 16.61 ?  139 VAL A CG1   1 
ATOM   985  C CG2   . VAL A 1 133 ? 21.414 5.544   1.617   1.00 17.65 ?  139 VAL A CG2   1 
ATOM   986  N N     . GLN A 1 134 ? 22.054 6.266   -2.950  1.00 17.70 ?  140 GLN A N     1 
ATOM   987  C CA    . GLN A 1 134 ? 21.601 6.518   -4.319  1.00 20.15 ?  140 GLN A CA    1 
ATOM   988  C C     . GLN A 1 134 ? 21.957 5.370   -5.249  1.00 20.84 ?  140 GLN A C     1 
ATOM   989  O O     . GLN A 1 134 ? 21.164 5.012   -6.127  1.00 21.92 ?  140 GLN A O     1 
ATOM   990  C CB    . GLN A 1 134 ? 22.164 7.846   -4.829  1.00 19.41 ?  140 GLN A CB    1 
ATOM   991  C CG    . GLN A 1 134 ? 21.363 8.983   -4.236  1.00 21.54 ?  140 GLN A CG    1 
ATOM   992  C CD    . GLN A 1 134 ? 21.935 10.360  -4.465  1.00 24.65 ?  140 GLN A CD    1 
ATOM   993  O OE1   . GLN A 1 134 ? 23.108 10.523  -4.831  1.00 22.55 ?  140 GLN A OE1   1 
ATOM   994  N NE2   . GLN A 1 134 ? 21.111 11.380  -4.195  1.00 26.69 ?  140 GLN A NE2   1 
ATOM   995  N N     . ARG A 1 135 ? 23.118 4.745   -5.046  1.00 20.59 ?  141 ARG A N     1 
ATOM   996  C CA    . ARG A 1 135 ? 23.520 3.646   -5.919  1.00 24.94 ?  141 ARG A CA    1 
ATOM   997  C C     . ARG A 1 135 ? 22.732 2.365   -5.666  1.00 22.13 ?  141 ARG A C     1 
ATOM   998  O O     . ARG A 1 135 ? 22.730 1.477   -6.529  1.00 23.43 ?  141 ARG A O     1 
ATOM   999  C CB    . ARG A 1 135 ? 25.017 3.368   -5.754  1.00 23.26 ?  141 ARG A CB    1 
ATOM   1000 C CG    . ARG A 1 135 ? 25.882 3.872   -6.891  1.00 36.09 ?  141 ARG A CG    1 
ATOM   1001 C CD    . ARG A 1 135 ? 27.376 3.579   -6.637  1.00 39.76 ?  141 ARG A CD    1 
ATOM   1002 N NE    . ARG A 1 135 ? 27.902 4.441   -5.579  1.00 39.27 ?  141 ARG A NE    1 
ATOM   1003 C CZ    . ARG A 1 135 ? 28.992 4.192   -4.858  1.00 43.75 ?  141 ARG A CZ    1 
ATOM   1004 N NH1   . ARG A 1 135 ? 29.694 3.077   -5.024  1.00 45.09 ?  141 ARG A NH1   1 
ATOM   1005 N NH2   . ARG A 1 135 ? 29.386 5.085   -3.946  1.00 39.67 ?  141 ARG A NH2   1 
ATOM   1006 N N     . SER A 1 136 ? 22.050 2.264   -4.528  1.00 17.87 ?  142 SER A N     1 
ATOM   1007 C CA    . SER A 1 136 ? 21.566 0.994   -3.994  1.00 20.35 ?  142 SER A CA    1 
ATOM   1008 C C     . SER A 1 136 ? 20.077 0.860   -4.257  1.00 21.43 ?  142 SER A C     1 
ATOM   1009 O O     . SER A 1 136 ? 19.279 1.602   -3.676  1.00 18.54 ?  142 SER A O     1 
ATOM   1010 C CB    . SER A 1 136 ? 21.828 0.913   -2.491  1.00 18.81 ?  142 SER A CB    1 
ATOM   1011 O OG    . SER A 1 136 ? 23.210 1.025   -2.193  1.00 18.01 ?  142 SER A OG    1 
ATOM   1012 N N     . ARG A 1 137 ? 19.694 -0.115  -5.085  1.00 17.61 ?  143 ARG A N     1 
ATOM   1013 C CA    . ARG A 1 137 ? 18.269 -0.357  -5.307  1.00 21.37 ?  143 ARG A CA    1 
ATOM   1014 C C     . ARG A 1 137 ? 17.610 -1.023  -4.096  1.00 20.51 ?  143 ARG A C     1 
ATOM   1015 O O     . ARG A 1 137 ? 16.444 -0.749  -3.785  1.00 19.66 ?  143 ARG A O     1 
ATOM   1016 C CB    . ARG A 1 137 ? 18.065 -1.218  -6.553  1.00 21.56 ?  143 ARG A CB    1 
ATOM   1017 C CG    . ARG A 1 137 ? 16.612 -1.688  -6.747  1.00 21.94 ?  143 ARG A CG    1 
ATOM   1018 C CD    . ARG A 1 137 ? 15.715 -0.533  -7.145  1.00 22.46 ?  143 ARG A CD    1 
ATOM   1019 N NE    . ARG A 1 137 ? 15.934 -0.180  -8.549  1.00 27.87 ?  143 ARG A NE    1 
ATOM   1020 C CZ    . ARG A 1 137 ? 15.189 0.674   -9.241  1.00 26.23 ?  143 ARG A CZ    1 
ATOM   1021 N NH1   . ARG A 1 137 ? 14.161 1.306   -8.687  1.00 24.85 ?  143 ARG A NH1   1 
ATOM   1022 N NH2   . ARG A 1 137 ? 15.482 0.900   -10.519 1.00 24.59 ?  143 ARG A NH2   1 
ATOM   1023 N N     . PHE A 1 138 ? 18.322 -1.938  -3.444  1.00 18.19 ?  144 PHE A N     1 
ATOM   1024 C CA    . PHE A 1 138 ? 17.828 -2.719  -2.316  1.00 18.80 ?  144 PHE A CA    1 
ATOM   1025 C C     . PHE A 1 138 ? 18.640 -2.336  -1.082  1.00 18.71 ?  144 PHE A C     1 
ATOM   1026 O O     . PHE A 1 138 ? 19.875 -2.341  -1.136  1.00 18.45 ?  144 PHE A O     1 
ATOM   1027 C CB    . PHE A 1 138 ? 17.974 -4.226  -2.577  1.00 19.00 ?  144 PHE A CB    1 
ATOM   1028 C CG    . PHE A 1 138 ? 17.204 -4.721  -3.761  1.00 21.96 ?  144 PHE A CG    1 
ATOM   1029 C CD1   . PHE A 1 138 ? 17.719 -4.597  -5.042  1.00 21.43 ?  144 PHE A CD1   1 
ATOM   1030 C CD2   . PHE A 1 138 ? 15.969 -5.333  -3.593  1.00 21.11 ?  144 PHE A CD2   1 
ATOM   1031 C CE1   . PHE A 1 138 ? 17.010 -5.051  -6.145  1.00 21.47 ?  144 PHE A CE1   1 
ATOM   1032 C CE2   . PHE A 1 138 ? 15.255 -5.774  -4.682  1.00 25.86 ?  144 PHE A CE2   1 
ATOM   1033 C CZ    . PHE A 1 138 ? 15.783 -5.646  -5.964  1.00 25.93 ?  144 PHE A CZ    1 
ATOM   1034 N N     . ILE A 1 139 ? 17.956 -1.999  0.013   1.00 16.92 ?  145 ILE A N     1 
ATOM   1035 C CA    . ILE A 1 139 ? 18.595 -1.506  1.235   1.00 16.31 ?  145 ILE A CA    1 
ATOM   1036 C C     . ILE A 1 139 ? 17.988 -2.203  2.447   1.00 18.78 ?  145 ILE A C     1 
ATOM   1037 O O     . ILE A 1 139 ? 16.764 -2.354  2.546   1.00 19.04 ?  145 ILE A O     1 
ATOM   1038 C CB    . ILE A 1 139 ? 18.439 0.022   1.374   1.00 15.59 ?  145 ILE A CB    1 
ATOM   1039 C CG1   . ILE A 1 139 ? 18.989 0.722   0.127   1.00 16.14 ?  145 ILE A CG1   1 
ATOM   1040 C CG2   . ILE A 1 139 ? 19.120 0.532   2.655   1.00 13.73 ?  145 ILE A CG2   1 
ATOM   1041 C CD1   . ILE A 1 139 ? 18.829 2.219   0.134   1.00 17.21 ?  145 ILE A CD1   1 
ATOM   1042 N N     . VAL A 1 140 ? 18.834 -2.593  3.396   1.00 17.20 ?  146 VAL A N     1 
ATOM   1043 C CA    . VAL A 1 140 ? 18.389 -3.185  4.650   1.00 16.93 ?  146 VAL A CA    1 
ATOM   1044 C C     . VAL A 1 140 ? 18.775 -2.248  5.785   1.00 16.48 ?  146 VAL A C     1 
ATOM   1045 O O     . VAL A 1 140 ? 19.937 -1.838  5.884   1.00 16.28 ?  146 VAL A O     1 
ATOM   1046 C CB    . VAL A 1 140 ? 18.994 -4.586  4.862   1.00 18.42 ?  146 VAL A CB    1 
ATOM   1047 C CG1   . VAL A 1 140 ? 18.860 -5.024  6.326   1.00 19.32 ?  146 VAL A CG1   1 
ATOM   1048 C CG2   . VAL A 1 140 ? 18.319 -5.592  3.941   1.00 19.13 ?  146 VAL A CG2   1 
ATOM   1049 N N     . VAL A 1 141 ? 17.801 -1.903  6.624   1.00 16.32 ?  147 VAL A N     1 
ATOM   1050 C CA    . VAL A 1 141 ? 18.047 -1.230  7.892   1.00 16.23 ?  147 VAL A CA    1 
ATOM   1051 C C     . VAL A 1 141 ? 17.910 -2.264  8.998   1.00 17.63 ?  147 VAL A C     1 
ATOM   1052 O O     . VAL A 1 141 ? 16.900 -2.975  9.068   1.00 20.93 ?  147 VAL A O     1 
ATOM   1053 C CB    . VAL A 1 141 ? 17.077 -0.052  8.105   1.00 15.71 ?  147 VAL A CB    1 
ATOM   1054 C CG1   . VAL A 1 141 ? 17.302 0.599   9.484   1.00 17.50 ?  147 VAL A CG1   1 
ATOM   1055 C CG2   . VAL A 1 141 ? 17.192 0.987   6.949   1.00 14.09 ?  147 VAL A CG2   1 
ATOM   1056 N N     . VAL A 1 142 ? 18.926 -2.372  9.846   1.00 18.25 ?  148 VAL A N     1 
ATOM   1057 C CA    . VAL A 1 142 ? 18.931 -3.322  10.958  1.00 19.79 ?  148 VAL A CA    1 
ATOM   1058 C C     . VAL A 1 142 ? 18.651 -2.556  12.241  1.00 20.68 ?  148 VAL A C     1 
ATOM   1059 O O     . VAL A 1 142 ? 19.404 -1.646  12.607  1.00 19.47 ?  148 VAL A O     1 
ATOM   1060 C CB    . VAL A 1 142 ? 20.264 -4.076  11.073  1.00 20.86 ?  148 VAL A CB    1 
ATOM   1061 C CG1   . VAL A 1 142 ? 20.128 -5.197  12.097  1.00 22.94 ?  148 VAL A CG1   1 
ATOM   1062 C CG2   . VAL A 1 142 ? 20.701 -4.640  9.726   1.00 20.80 ?  148 VAL A CG2   1 
ATOM   1063 N N     . GLY A 1 143 ? 17.582 -2.941  12.931  1.00 21.01 ?  149 GLY A N     1 
ATOM   1064 C CA    . GLY A 1 143 ? 17.211 -2.330  14.185  1.00 21.32 ?  149 GLY A CA    1 
ATOM   1065 C C     . GLY A 1 143 ? 16.016 -1.432  13.981  1.00 21.75 ?  149 GLY A C     1 
ATOM   1066 O O     . GLY A 1 143 ? 16.097 -0.467  13.226  1.00 21.39 ?  149 GLY A O     1 
ATOM   1067 N N     . GLY A 1 144 ? 14.895 -1.762  14.621  1.00 23.94 ?  150 GLY A N     1 
ATOM   1068 C CA    . GLY A 1 144 ? 13.666 -1.009  14.483  1.00 22.00 ?  150 GLY A CA    1 
ATOM   1069 C C     . GLY A 1 144 ? 13.333 -0.236  15.745  1.00 23.34 ?  150 GLY A C     1 
ATOM   1070 O O     . GLY A 1 144 ? 12.166 -0.141  16.140  1.00 25.52 ?  150 GLY A O     1 
ATOM   1071 N N     . GLY A 1 145 ? 14.360 0.294   16.403  1.00 21.67 ?  151 GLY A N     1 
ATOM   1072 C CA    . GLY A 1 145 ? 14.166 1.320   17.404  1.00 22.70 ?  151 GLY A CA    1 
ATOM   1073 C C     . GLY A 1 145 ? 13.725 2.600   16.723  1.00 22.40 ?  151 GLY A C     1 
ATOM   1074 O O     . GLY A 1 145 ? 13.447 2.641   15.527  1.00 18.27 ?  151 GLY A O     1 
ATOM   1075 N N     . SER A 1 146 ? 13.679 3.678   17.501  1.00 23.40 ?  152 SER A N     1 
ATOM   1076 C CA    . SER A 1 146 ? 13.213 4.927   16.913  1.00 21.34 ?  152 SER A CA    1 
ATOM   1077 C C     . SER A 1 146 ? 14.131 5.401   15.791  1.00 21.48 ?  152 SER A C     1 
ATOM   1078 O O     . SER A 1 146 ? 13.651 5.975   14.814  1.00 20.82 ?  152 SER A O     1 
ATOM   1079 C CB    . SER A 1 146 ? 13.044 6.001   17.997  1.00 27.45 ?  152 SER A CB    1 
ATOM   1080 O OG    . SER A 1 146 ? 14.255 6.242   18.680  1.00 31.68 ?  152 SER A OG    1 
ATOM   1081 N N     . ALA A 1 147 ? 15.439 5.131   15.874  1.00 22.23 ?  153 ALA A N     1 
ATOM   1082 C CA    . ALA A 1 147 ? 16.337 5.543   14.790  1.00 21.05 ?  153 ALA A CA    1 
ATOM   1083 C C     . ALA A 1 147 ? 16.101 4.727   13.520  1.00 18.69 ?  153 ALA A C     1 
ATOM   1084 O O     . ALA A 1 147 ? 16.067 5.270   12.407  1.00 15.84 ?  153 ALA A O     1 
ATOM   1085 C CB    . ALA A 1 147 ? 17.790 5.401   15.231  1.00 18.79 ?  153 ALA A CB    1 
ATOM   1086 N N     . GLY A 1 148 ? 15.949 3.417   13.660  1.00 17.97 ?  154 GLY A N     1 
ATOM   1087 C CA    . GLY A 1 148 ? 15.747 2.590   12.491  1.00 16.36 ?  154 GLY A CA    1 
ATOM   1088 C C     . GLY A 1 148 ? 14.458 2.890   11.756  1.00 16.08 ?  154 GLY A C     1 
ATOM   1089 O O     . GLY A 1 148 ? 14.420 2.873   10.522  1.00 14.57 ?  154 GLY A O     1 
ATOM   1090 N N     . VAL A 1 149 ? 13.375 3.135   12.492  1.00 17.57 ?  155 VAL A N     1 
ATOM   1091 C CA    . VAL A 1 149 ? 12.114 3.435   11.812  1.00 16.05 ?  155 VAL A CA    1 
ATOM   1092 C C     . VAL A 1 149 ? 12.207 4.776   11.100  1.00 17.37 ?  155 VAL A C     1 
ATOM   1093 O O     . VAL A 1 149 ? 11.665 4.936   9.998   1.00 15.54 ?  155 VAL A O     1 
ATOM   1094 C CB    . VAL A 1 149 ? 10.935 3.377   12.804  1.00 19.33 ?  155 VAL A CB    1 
ATOM   1095 C CG1   . VAL A 1 149 ? 10.931 2.026   13.497  1.00 17.99 ?  155 VAL A CG1   1 
ATOM   1096 C CG2   . VAL A 1 149 ? 11.012 4.487   13.840  1.00 19.09 ?  155 VAL A CG2   1 
ATOM   1097 N N     . GLU A 1 150 ? 12.968 5.728   11.661  1.00 15.10 ?  156 GLU A N     1 
ATOM   1098 C CA    . GLU A 1 150 ? 13.201 6.981   10.946  1.00 16.92 ?  156 GLU A CA    1 
ATOM   1099 C C     . GLU A 1 150 ? 14.079 6.765   9.716   1.00 16.94 ?  156 GLU A C     1 
ATOM   1100 O O     . GLU A 1 150 ? 13.779 7.297   8.640   1.00 15.13 ?  156 GLU A O     1 
ATOM   1101 C CB    . GLU A 1 150 ? 13.809 8.032   11.887  1.00 15.55 ?  156 GLU A CB    1 
ATOM   1102 C CG    . GLU A 1 150 ? 12.788 8.614   12.872  1.00 19.08 ?  156 GLU A CG    1 
ATOM   1103 C CD    . GLU A 1 150 ? 13.329 9.768   13.734  1.00 24.78 ?  156 GLU A CD    1 
ATOM   1104 O OE1   . GLU A 1 150 ? 14.570 9.887   13.868  1.00 26.76 ?  156 GLU A OE1   1 
ATOM   1105 O OE2   . GLU A 1 150 ? 12.513 10.561  14.268  1.00 22.37 -1 156 GLU A OE2   1 
ATOM   1106 N N     . MET A 1 151 ? 15.150 5.971   9.839   1.00 14.42 ?  157 MET A N     1 
ATOM   1107 C CA    . MET A 1 151 ? 16.031 5.735   8.697   1.00 13.63 ?  157 MET A CA    1 
ATOM   1108 C C     . MET A 1 151 ? 15.266 5.133   7.529   1.00 15.98 ?  157 MET A C     1 
ATOM   1109 O O     . MET A 1 151 ? 15.383 5.593   6.385   1.00 16.60 ?  157 MET A O     1 
ATOM   1110 C CB    . MET A 1 151 ? 17.186 4.817   9.106   1.00 16.60 ?  157 MET A CB    1 
ATOM   1111 C CG    . MET A 1 151 ? 18.249 4.560   8.032   1.00 15.91 ?  157 MET A CG    1 
ATOM   1112 S SD    . MET A 1 151 ? 19.323 5.993   7.749   1.00 26.82 ?  157 MET A SD    1 
ATOM   1113 C CE    . MET A 1 151 ? 18.583 6.726   6.311   1.00 16.69 ?  157 MET A CE    1 
ATOM   1114 N N     . ALA A 1 152 ? 14.481 4.092   7.799   1.00 15.39 ?  158 ALA A N     1 
ATOM   1115 C CA    . ALA A 1 152 ? 13.732 3.415   6.749   1.00 17.33 ?  158 ALA A CA    1 
ATOM   1116 C C     . ALA A 1 152 ? 12.704 4.348   6.123   1.00 17.29 ?  158 ALA A C     1 
ATOM   1117 O O     . ALA A 1 152 ? 12.539 4.386   4.893   1.00 14.80 ?  158 ALA A O     1 
ATOM   1118 C CB    . ALA A 1 152 ? 13.051 2.165   7.320   1.00 14.90 ?  158 ALA A CB    1 
ATOM   1119 N N     . ALA A 1 153 ? 12.017 5.119   6.951   1.00 13.46 ?  159 ALA A N     1 
ATOM   1120 C CA    . ALA A 1 153 ? 11.016 6.043   6.444   1.00 17.55 ?  159 ALA A CA    1 
ATOM   1121 C C     . ALA A 1 153 ? 11.654 7.127   5.583   1.00 15.75 ?  159 ALA A C     1 
ATOM   1122 O O     . ALA A 1 153 ? 11.112 7.491   4.530   1.00 13.91 ?  159 ALA A O     1 
ATOM   1123 C CB    . ALA A 1 153 ? 10.248 6.648   7.620   1.00 16.28 ?  159 ALA A CB    1 
ATOM   1124 N N     . GLU A 1 154 ? 12.826 7.621   5.993   1.00 12.77 ?  160 GLU A N     1 
ATOM   1125 C CA    . GLU A 1 154 ? 13.510 8.650   5.216   1.00 15.48 ?  160 GLU A CA    1 
ATOM   1126 C C     . GLU A 1 154 ? 13.869 8.143   3.831   1.00 15.22 ?  160 GLU A C     1 
ATOM   1127 O O     . GLU A 1 154 ? 13.669 8.853   2.831   1.00 13.58 ?  160 GLU A O     1 
ATOM   1128 C CB    . GLU A 1 154 ? 14.779 9.122   5.924   1.00 13.13 ?  160 GLU A CB    1 
ATOM   1129 C CG    . GLU A 1 154 ? 14.576 10.034  7.113   1.00 17.20 ?  160 GLU A CG    1 
ATOM   1130 C CD    . GLU A 1 154 ? 14.144 11.477  6.747   1.00 18.32 ?  160 GLU A CD    1 
ATOM   1131 O OE1   . GLU A 1 154 ? 14.421 11.962  5.620   1.00 16.65 ?  160 GLU A OE1   1 
ATOM   1132 O OE2   . GLU A 1 154 ? 13.508 12.122  7.607   1.00 19.00 -1 160 GLU A OE2   1 
ATOM   1133 N N     . ILE A 1 155 ? 14.434 6.925   3.754   1.00 13.12 ?  161 ILE A N     1 
ATOM   1134 C CA    . ILE A 1 155 ? 14.822 6.358   2.458   1.00 13.15 ?  161 ILE A CA    1 
ATOM   1135 C C     . ILE A 1 155 ? 13.612 6.206   1.545   1.00 13.10 ?  161 ILE A C     1 
ATOM   1136 O O     . ILE A 1 155 ? 13.668 6.556   0.357   1.00 13.77 ?  161 ILE A O     1 
ATOM   1137 C CB    . ILE A 1 155 ? 15.553 5.014   2.646   1.00 15.75 ?  161 ILE A CB    1 
ATOM   1138 C CG1   . ILE A 1 155 ? 16.848 5.215   3.468   1.00 13.96 ?  161 ILE A CG1   1 
ATOM   1139 C CG2   . ILE A 1 155 ? 15.834 4.366   1.287   1.00 13.16 ?  161 ILE A CG2   1 
ATOM   1140 C CD1   . ILE A 1 155 ? 17.517 3.884   3.898   1.00 13.65 ?  161 ILE A CD1   1 
ATOM   1141 N N     . LYS A 1 156 ? 12.504 5.649   2.062   1.00 11.30 ?  162 LYS A N     1 
ATOM   1142 C CA    . LYS A 1 156 ? 11.350 5.424   1.186   1.00 14.48 ?  162 LYS A CA    1 
ATOM   1143 C C     . LYS A 1 156 ? 10.647 6.727   0.829   1.00 16.02 ?  162 LYS A C     1 
ATOM   1144 O O     . LYS A 1 156 ? 9.971  6.797   -0.203  1.00 15.35 ?  162 LYS A O     1 
ATOM   1145 C CB    . LYS A 1 156 ? 10.339 4.459   1.819   1.00 17.09 ?  162 LYS A CB    1 
ATOM   1146 C CG    . LYS A 1 156 ? 10.477 3.025   1.397   1.00 20.32 ?  162 LYS A CG    1 
ATOM   1147 C CD    . LYS A 1 156 ? 10.375 2.847   -0.111  1.00 19.21 ?  162 LYS A CD    1 
ATOM   1148 C CE    . LYS A 1 156 ? 9.360  1.767   -0.439  1.00 20.95 ?  162 LYS A CE    1 
ATOM   1149 N NZ    . LYS A 1 156 ? 9.499  1.237   -1.815  1.00 16.86 ?  162 LYS A NZ    1 
ATOM   1150 N N     . THR A 1 157 ? 10.775 7.763   1.659   1.00 13.41 ?  163 THR A N     1 
ATOM   1151 C CA    . THR A 1 157 ? 10.164 9.047   1.311   1.00 14.73 ?  163 THR A CA    1 
ATOM   1152 C C     . THR A 1 157 ? 10.963 9.769   0.238   1.00 16.28 ?  163 THR A C     1 
ATOM   1153 O O     . THR A 1 157 ? 10.378 10.344  -0.691  1.00 15.26 ?  163 THR A O     1 
ATOM   1154 C CB    . THR A 1 157 ? 10.048 9.936   2.547   1.00 14.99 ?  163 THR A CB    1 
ATOM   1155 O OG1   . THR A 1 157 ? 9.378  9.209   3.586   1.00 16.02 ?  163 THR A OG1   1 
ATOM   1156 C CG2   . THR A 1 157 ? 9.270  11.243  2.228   1.00 14.39 ?  163 THR A CG2   1 
ATOM   1157 N N     . GLU A 1 158 ? 12.295 9.784   0.361   1.00 12.93 ?  164 GLU A N     1 
ATOM   1158 C CA    . GLU A 1 158 ? 13.115 10.428  -0.668  1.00 15.66 ?  164 GLU A CA    1 
ATOM   1159 C C     . GLU A 1 158 ? 13.217 9.589   -1.945  1.00 15.44 ?  164 GLU A C     1 
ATOM   1160 O O     . GLU A 1 158 ? 13.305 10.144  -3.050  1.00 15.70 ?  164 GLU A O     1 
ATOM   1161 C CB    . GLU A 1 158 ? 14.511 10.714  -0.111  1.00 14.36 ?  164 GLU A CB    1 
ATOM   1162 C CG    . GLU A 1 158 ? 14.480 11.679  1.062   1.00 16.44 ?  164 GLU A CG    1 
ATOM   1163 C CD    . GLU A 1 158 ? 13.787 13.002  0.696   1.00 20.04 ?  164 GLU A CD    1 
ATOM   1164 O OE1   . GLU A 1 158 ? 14.334 13.707  -0.173  1.00 23.81 ?  164 GLU A OE1   1 
ATOM   1165 O OE2   . GLU A 1 158 ? 12.691 13.326  1.247   1.00 19.69 -1 164 GLU A OE2   1 
ATOM   1166 N N     . TYR A 1 159 ? 13.181 8.263   -1.827  1.00 14.96 ?  165 TYR A N     1 
ATOM   1167 C CA    . TYR A 1 159 ? 13.393 7.352   -2.954  1.00 15.61 ?  165 TYR A CA    1 
ATOM   1168 C C     . TYR A 1 159 ? 12.308 6.285   -3.000  1.00 15.89 ?  165 TYR A C     1 
ATOM   1169 O O     . TYR A 1 159 ? 12.574 5.100   -2.751  1.00 14.68 ?  165 TYR A O     1 
ATOM   1170 C CB    . TYR A 1 159 ? 14.767 6.691   -2.858  1.00 14.66 ?  165 TYR A CB    1 
ATOM   1171 C CG    . TYR A 1 159 ? 15.891 7.680   -2.696  1.00 17.08 ?  165 TYR A CG    1 
ATOM   1172 C CD1   . TYR A 1 159 ? 16.503 8.261   -3.804  1.00 18.72 ?  165 TYR A CD1   1 
ATOM   1173 C CD2   . TYR A 1 159 ? 16.348 8.023   -1.436  1.00 15.47 ?  165 TYR A CD2   1 
ATOM   1174 C CE1   . TYR A 1 159 ? 17.527 9.171   -3.650  1.00 17.93 ?  165 TYR A CE1   1 
ATOM   1175 C CE2   . TYR A 1 159 ? 17.377 8.933   -1.270  1.00 18.06 ?  165 TYR A CE2   1 
ATOM   1176 C CZ    . TYR A 1 159 ? 17.963 9.492   -2.385  1.00 19.27 ?  165 TYR A CZ    1 
ATOM   1177 O OH    . TYR A 1 159 ? 18.972 10.394  -2.213  1.00 17.46 ?  165 TYR A OH    1 
ATOM   1178 N N     . PRO A 1 160 ? 11.077 6.660   -3.346  1.00 16.02 ?  166 PRO A N     1 
ATOM   1179 C CA    . PRO A 1 160 ? 9.980  5.669   -3.338  1.00 17.64 ?  166 PRO A CA    1 
ATOM   1180 C C     . PRO A 1 160 ? 10.281 4.424   -4.151  1.00 19.01 ?  166 PRO A C     1 
ATOM   1181 O O     . PRO A 1 160 ? 9.735  3.346   -3.866  1.00 16.65 ?  166 PRO A O     1 
ATOM   1182 C CB    . PRO A 1 160 ? 8.801  6.436   -3.948  1.00 18.15 ?  166 PRO A CB    1 
ATOM   1183 C CG    . PRO A 1 160 ? 9.168  7.866   -3.865  1.00 19.23 ?  166 PRO A CG    1 
ATOM   1184 C CD    . PRO A 1 160 ? 10.638 8.002   -3.756  1.00 14.07 ?  166 PRO A CD    1 
ATOM   1185 N N     . GLU A 1 161 ? 11.126 4.546   -5.180  1.00 17.18 ?  167 GLU A N     1 
ATOM   1186 C CA    . GLU A 1 161 ? 11.423 3.424   -6.050  1.00 19.61 ?  167 GLU A CA    1 
ATOM   1187 C C     . GLU A 1 161 ? 12.413 2.426   -5.447  1.00 17.79 ?  167 GLU A C     1 
ATOM   1188 O O     . GLU A 1 161 ? 12.638 1.378   -6.050  1.00 16.90 ?  167 GLU A O     1 
ATOM   1189 C CB    . GLU A 1 161 ? 11.957 3.947   -7.396  1.00 20.15 ?  167 GLU A CB    1 
ATOM   1190 C CG    . GLU A 1 161 ? 13.425 4.468   -7.358  1.00 18.06 ?  167 GLU A CG    1 
ATOM   1191 C CD    . GLU A 1 161 ? 13.629 5.868   -6.724  1.00 20.97 ?  167 GLU A CD    1 
ATOM   1192 O OE1   . GLU A 1 161 ? 12.671 6.485   -6.183  1.00 16.70 ?  167 GLU A OE1   1 
ATOM   1193 O OE2   . GLU A 1 161 ? 14.789 6.361   -6.774  1.00 20.24 -1 167 GLU A OE2   1 
ATOM   1194 N N     . LYS A 1 162 ? 13.028 2.711   -4.302  1.00 16.45 ?  168 LYS A N     1 
ATOM   1195 C CA    . LYS A 1 162 ? 13.948 1.733   -3.734  1.00 17.46 ?  168 LYS A CA    1 
ATOM   1196 C C     . LYS A 1 162 ? 13.184 0.685   -2.917  1.00 20.35 ?  168 LYS A C     1 
ATOM   1197 O O     . LYS A 1 162 ? 12.045 0.891   -2.502  1.00 19.47 ?  168 LYS A O     1 
ATOM   1198 C CB    . LYS A 1 162 ? 15.008 2.427   -2.894  1.00 16.42 ?  168 LYS A CB    1 
ATOM   1199 C CG    . LYS A 1 162 ? 16.008 3.188   -3.761  1.00 16.77 ?  168 LYS A CG    1 
ATOM   1200 C CD    . LYS A 1 162 ? 17.000 3.953   -2.930  1.00 18.24 ?  168 LYS A CD    1 
ATOM   1201 C CE    . LYS A 1 162 ? 17.881 4.829   -3.818  1.00 18.83 ?  168 LYS A CE    1 
ATOM   1202 N NZ    . LYS A 1 162 ? 18.740 4.023   -4.759  1.00 20.55 ?  168 LYS A NZ    1 
ATOM   1203 N N     . GLU A 1 163 ? 13.810 -0.470  -2.740  1.00 18.36 ?  169 GLU A N     1 
ATOM   1204 C CA    . GLU A 1 163 ? 13.256 -1.553  -1.940  1.00 22.11 ?  169 GLU A CA    1 
ATOM   1205 C C     . GLU A 1 163 ? 13.942 -1.507  -0.584  1.00 20.93 ?  169 GLU A C     1 
ATOM   1206 O O     . GLU A 1 163 ? 15.168 -1.629  -0.507  1.00 20.69 ?  169 GLU A O     1 
ATOM   1207 C CB    . GLU A 1 163 ? 13.473 -2.914  -2.610  1.00 20.12 ?  169 GLU A CB    1 
ATOM   1208 C CG    . GLU A 1 163 ? 12.782 -3.081  -3.968  1.00 26.29 ?  169 GLU A CG    1 
ATOM   1209 C CD    . GLU A 1 163 ? 11.262 -3.083  -3.821  1.00 36.66 ?  169 GLU A CD    1 
ATOM   1210 O OE1   . GLU A 1 163 ? 10.745 -3.921  -3.033  1.00 44.25 ?  169 GLU A OE1   1 
ATOM   1211 O OE2   . GLU A 1 163 ? 10.593 -2.226  -4.453  1.00 40.95 -1 169 GLU A OE2   1 
ATOM   1212 N N     . VAL A 1 164 ? 13.166 -1.319  0.478   1.00 21.19 ?  170 VAL A N     1 
ATOM   1213 C CA    . VAL A 1 164 ? 13.721 -1.110  1.814   1.00 19.15 ?  170 VAL A CA    1 
ATOM   1214 C C     . VAL A 1 164 ? 13.118 -2.129  2.759   1.00 19.51 ?  170 VAL A C     1 
ATOM   1215 O O     . VAL A 1 164 ? 11.891 -2.239  2.866   1.00 18.61 ?  170 VAL A O     1 
ATOM   1216 C CB    . VAL A 1 164 ? 13.458 0.313   2.347   1.00 17.57 ?  170 VAL A CB    1 
ATOM   1217 C CG1   . VAL A 1 164 ? 13.981 0.437   3.768   1.00 16.41 ?  170 VAL A CG1   1 
ATOM   1218 C CG2   . VAL A 1 164 ? 14.152 1.332   1.465   1.00 17.31 ?  170 VAL A CG2   1 
ATOM   1219 N N     . THR A 1 165 ? 13.977 -2.853  3.462   1.00 19.58 ?  171 THR A N     1 
ATOM   1220 C CA    . THR A 1 165 ? 13.546 -3.809  4.468   1.00 21.58 ?  171 THR A CA    1 
ATOM   1221 C C     . THR A 1 165 ? 14.096 -3.369  5.811   1.00 20.26 ?  171 THR A C     1 
ATOM   1222 O O     . THR A 1 165 ? 15.273 -3.001  5.917   1.00 19.43 ?  171 THR A O     1 
ATOM   1223 C CB    . THR A 1 165 ? 14.018 -5.226  4.113   1.00 21.84 ?  171 THR A CB    1 
ATOM   1224 O OG1   . THR A 1 165 ? 13.398 -5.616  2.881   1.00 24.45 ?  171 THR A OG1   1 
ATOM   1225 C CG2   . THR A 1 165 ? 13.657 -6.219  5.204   1.00 21.83 ?  171 THR A CG2   1 
ATOM   1226 N N     . LEU A 1 166 ? 13.240 -3.385  6.822   1.00 19.37 ?  172 LEU A N     1 
ATOM   1227 C CA    . LEU A 1 166 ? 13.621 -3.073  8.189   1.00 19.88 ?  172 LEU A CA    1 
ATOM   1228 C C     . LEU A 1 166 ? 13.543 -4.361  8.982   1.00 20.00 ?  172 LEU A C     1 
ATOM   1229 O O     . LEU A 1 166 ? 12.490 -5.006  9.001   1.00 20.94 ?  172 LEU A O     1 
ATOM   1230 C CB    . LEU A 1 166 ? 12.692 -2.016  8.787   1.00 18.39 ?  172 LEU A CB    1 
ATOM   1231 C CG    . LEU A 1 166 ? 12.936 -1.605  10.236  1.00 20.16 ?  172 LEU A CG    1 
ATOM   1232 C CD1   . LEU A 1 166 ? 14.366 -1.183  10.415  1.00 19.86 ?  172 LEU A CD1   1 
ATOM   1233 C CD2   . LEU A 1 166 ? 11.982 -0.459  10.607  1.00 19.88 ?  172 LEU A CD2   1 
ATOM   1234 N N     . ILE A 1 167 ? 14.646 -4.743  9.617   1.00 20.52 ?  173 ILE A N     1 
ATOM   1235 C CA    . ILE A 1 167 ? 14.723 -5.980  10.388  1.00 22.28 ?  173 ILE A CA    1 
ATOM   1236 C C     . ILE A 1 167 ? 14.895 -5.620  11.860  1.00 23.44 ?  173 ILE A C     1 
ATOM   1237 O O     . ILE A 1 167 ? 15.861 -4.940  12.230  1.00 22.18 ?  173 ILE A O     1 
ATOM   1238 C CB    . ILE A 1 167 ? 15.866 -6.876  9.904   1.00 22.91 ?  173 ILE A CB    1 
ATOM   1239 C CG1   . ILE A 1 167 ? 15.699 -7.156  8.407   1.00 22.45 ?  173 ILE A CG1   1 
ATOM   1240 C CG2   . ILE A 1 167 ? 15.905 -8.168  10.728  1.00 24.95 ?  173 ILE A CG2   1 
ATOM   1241 C CD1   . ILE A 1 167 ? 16.854 -7.900  7.777   1.00 23.19 ?  173 ILE A CD1   1 
ATOM   1242 N N     . HIS A 1 168 ? 13.972 -6.104  12.698  1.00 24.04 ?  174 HIS A N     1 
ATOM   1243 C CA    . HIS A 1 168 ? 13.871 -5.698  14.092  1.00 25.38 ?  174 HIS A CA    1 
ATOM   1244 C C     . HIS A 1 168 ? 13.697 -6.927  14.976  1.00 26.95 ?  174 HIS A C     1 
ATOM   1245 O O     . HIS A 1 168 ? 12.935 -7.841  14.640  1.00 27.83 ?  174 HIS A O     1 
ATOM   1246 C CB    . HIS A 1 168 ? 12.697 -4.737  14.287  1.00 24.00 ?  174 HIS A CB    1 
ATOM   1247 C CG    . HIS A 1 168 ? 12.613 -4.161  15.662  1.00 26.58 ?  174 HIS A CG    1 
ATOM   1248 N ND1   . HIS A 1 168 ? 13.727 -3.769  16.373  1.00 25.77 ?  174 HIS A ND1   1 
ATOM   1249 C CD2   . HIS A 1 168 ? 11.548 -3.910  16.459  1.00 25.38 ?  174 HIS A CD2   1 
ATOM   1250 C CE1   . HIS A 1 168 ? 13.352 -3.293  17.547  1.00 27.47 ?  174 HIS A CE1   1 
ATOM   1251 N NE2   . HIS A 1 168 ? 12.035 -3.363  17.621  1.00 30.17 ?  174 HIS A NE2   1 
ATOM   1252 N N     . SER A 1 169 ? 14.410 -6.946  16.104  1.00 28.66 ?  175 SER A N     1 
ATOM   1253 C CA    . SER A 1 169 ? 14.429 -8.122  16.972  1.00 31.87 ?  175 SER A CA    1 
ATOM   1254 C C     . SER A 1 169 ? 13.202 -8.232  17.864  1.00 31.87 ?  175 SER A C     1 
ATOM   1255 O O     . SER A 1 169 ? 12.938 -9.321  18.381  1.00 33.26 ?  175 SER A O     1 
ATOM   1256 C CB    . SER A 1 169 ? 15.683 -8.129  17.855  1.00 32.15 ?  175 SER A CB    1 
ATOM   1257 O OG    . SER A 1 169 ? 15.754 -6.947  18.636  1.00 32.39 ?  175 SER A OG    1 
ATOM   1258 N N     . GLN A 1 170 ? 12.467 -7.142  18.070  1.00 31.85 ?  176 GLN A N     1 
ATOM   1259 C CA    . GLN A 1 170 ? 11.253 -7.154  18.880  1.00 34.12 ?  176 GLN A CA    1 
ATOM   1260 C C     . GLN A 1 170 ? 10.025 -7.298  17.987  1.00 32.25 ?  176 GLN A C     1 
ATOM   1261 O O     . GLN A 1 170 ? 10.104 -7.190  16.764  1.00 29.88 ?  176 GLN A O     1 
ATOM   1262 C CB    . GLN A 1 170 ? 11.139 -5.871  19.706  1.00 32.83 ?  176 GLN A CB    1 
ATOM   1263 C CG    . GLN A 1 170 ? 12.414 -5.481  20.395  1.00 34.10 ?  176 GLN A CG    1 
ATOM   1264 C CD    . GLN A 1 170 ? 12.944 -6.604  21.244  1.00 39.64 ?  176 GLN A CD    1 
ATOM   1265 O OE1   . GLN A 1 170 ? 14.101 -7.017  21.103  1.00 40.87 ?  176 GLN A OE1   1 
ATOM   1266 N NE2   . GLN A 1 170 ? 12.095 -7.123  22.127  1.00 39.66 ?  176 GLN A NE2   1 
ATOM   1267 N N     . VAL A 1 171 ? 8.868  -7.502  18.620  1.00 33.18 ?  177 VAL A N     1 
ATOM   1268 C CA    . VAL A 1 171 ? 7.623  -7.585  17.856  1.00 35.50 ?  177 VAL A CA    1 
ATOM   1269 C C     . VAL A 1 171 ? 7.010  -6.208  17.604  1.00 34.83 ?  177 VAL A C     1 
ATOM   1270 O O     . VAL A 1 171 ? 6.270  -6.039  16.623  1.00 34.67 ?  177 VAL A O     1 
ATOM   1271 C CB    . VAL A 1 171 ? 6.609  -8.529  18.544  1.00 40.13 ?  177 VAL A CB    1 
ATOM   1272 C CG1   . VAL A 1 171 ? 6.120  -7.963  19.893  1.00 36.33 ?  177 VAL A CG1   1 
ATOM   1273 C CG2   . VAL A 1 171 ? 5.442  -8.846  17.595  1.00 40.19 ?  177 VAL A CG2   1 
ATOM   1274 N N     . ALA A 1 172 ? 7.340  -5.210  18.423  1.00 33.21 ?  178 ALA A N     1 
ATOM   1275 C CA    . ALA A 1 172 ? 6.868  -3.844  18.232  1.00 33.07 ?  178 ALA A CA    1 
ATOM   1276 C C     . ALA A 1 172 ? 8.035  -2.904  17.953  1.00 33.25 ?  178 ALA A C     1 
ATOM   1277 O O     . ALA A 1 172 ? 9.156  -3.112  18.433  1.00 33.08 ?  178 ALA A O     1 
ATOM   1278 C CB    . ALA A 1 172 ? 6.091  -3.344  19.453  1.00 32.97 ?  178 ALA A CB    1 
ATOM   1279 N N     . LEU A 1 173 ? 7.740  -1.844  17.200  1.00 32.28 ?  179 LEU A N     1 
ATOM   1280 C CA    . LEU A 1 173 ? 8.724  -0.877  16.735  1.00 29.32 ?  179 LEU A CA    1 
ATOM   1281 C C     . LEU A 1 173 ? 8.871  0.282   17.712  1.00 30.93 ?  179 LEU A C     1 
ATOM   1282 O O     . LEU A 1 173 ? 7.949  0.599   18.465  1.00 33.89 ?  179 LEU A O     1 
ATOM   1283 C CB    . LEU A 1 173 ? 8.316  -0.343  15.365  1.00 27.40 ?  179 LEU A CB    1 
ATOM   1284 C CG    . LEU A 1 173 ? 8.256  -1.394  14.256  1.00 27.70 ?  179 LEU A CG    1 
ATOM   1285 C CD1   . LEU A 1 173 ? 7.524  -0.850  13.036  1.00 25.02 ?  179 LEU A CD1   1 
ATOM   1286 C CD2   . LEU A 1 173 ? 9.655  -1.851  13.852  1.00 28.68 ?  179 LEU A CD2   1 
ATOM   1287 N N     . ALA A 1 174 ? 10.052 0.916   17.686  1.00 30.46 ?  180 ALA A N     1 
ATOM   1288 C CA    . ALA A 1 174 ? 10.350 2.120   18.463  1.00 30.27 ?  180 ALA A CA    1 
ATOM   1289 C C     . ALA A 1 174 ? 10.260 1.879   19.968  1.00 32.21 ?  180 ALA A C     1 
ATOM   1290 O O     . ALA A 1 174 ? 10.040 0.745   20.408  1.00 35.92 ?  180 ALA A O     1 
ATOM   1291 C CB    . ALA A 1 174 ? 9.430  3.272   18.036  1.00 28.33 ?  180 ALA A CB    1 
ATOM   1292 N N     . ASP A 1 175 ? 10.412 2.943   20.761  1.00 34.42 ?  181 ASP A N     1 
ATOM   1293 C CA    . ASP A 1 175 ? 10.703 2.805   22.189  1.00 36.23 ?  181 ASP A CA    1 
ATOM   1294 C C     . ASP A 1 175 ? 9.624  2.064   22.957  1.00 37.84 ?  181 ASP A C     1 
ATOM   1295 O O     . ASP A 1 175 ? 8.427  2.333   22.811  1.00 36.67 ?  181 ASP A O     1 
ATOM   1296 C CB    . ASP A 1 175 ? 10.899 4.171   22.835  1.00 39.04 ?  181 ASP A CB    1 
ATOM   1297 C CG    . ASP A 1 175 ? 12.330 4.619   22.783  1.00 40.78 ?  181 ASP A CG    1 
ATOM   1298 O OD1   . ASP A 1 175 ? 12.803 4.908   21.672  1.00 38.32 ?  181 ASP A OD1   1 
ATOM   1299 O OD2   . ASP A 1 175 ? 12.980 4.652   23.846  1.00 44.13 -1 181 ASP A OD2   1 
ATOM   1300 N N     . LYS A 1 176 ? 10.074 1.151   23.823  1.00 37.56 ?  182 LYS A N     1 
ATOM   1301 C CA    . LYS A 1 176 ? 9.175  0.474   24.745  1.00 39.21 ?  182 LYS A CA    1 
ATOM   1302 C C     . LYS A 1 176 ? 8.406  1.457   25.610  1.00 40.57 ?  182 LYS A C     1 
ATOM   1303 O O     . LYS A 1 176 ? 7.315  1.128   26.094  1.00 40.92 ?  182 LYS A O     1 
ATOM   1304 C CB    . LYS A 1 176 ? 9.967  -0.486  25.642  1.00 39.93 ?  182 LYS A CB    1 
ATOM   1305 N N     . GLU A 1 177 ? 8.943  2.655   25.818  1.00 42.35 ?  183 GLU A N     1 
ATOM   1306 C CA    . GLU A 1 177 ? 8.291  3.591   26.723  1.00 43.60 ?  183 GLU A CA    1 
ATOM   1307 C C     . GLU A 1 177 ? 7.131  4.344   26.075  1.00 39.84 ?  183 GLU A C     1 
ATOM   1308 O O     . GLU A 1 177 ? 6.364  4.990   26.800  1.00 38.80 ?  183 GLU A O     1 
ATOM   1309 C CB    . GLU A 1 177 ? 9.325  4.583   27.273  1.00 43.61 ?  183 GLU A CB    1 
ATOM   1310 C CG    . GLU A 1 177 ? 10.496 3.922   28.008  1.00 46.96 ?  183 GLU A CG    1 
ATOM   1311 N N     . LEU A 1 178 ? 6.967  4.256   24.751  1.00 34.35 ?  184 LEU A N     1 
ATOM   1312 C CA    . LEU A 1 178 ? 5.972  5.063   24.054  1.00 32.10 ?  184 LEU A CA    1 
ATOM   1313 C C     . LEU A 1 178 ? 4.560  4.547   24.297  1.00 34.69 ?  184 LEU A C     1 
ATOM   1314 O O     . LEU A 1 178 ? 4.341  3.365   24.588  1.00 33.58 ?  184 LEU A O     1 
ATOM   1315 C CB    . LEU A 1 178 ? 6.235  5.061   22.553  1.00 29.94 ?  184 LEU A CB    1 
ATOM   1316 C CG    . LEU A 1 178 ? 7.511  5.758   22.092  1.00 30.61 ?  184 LEU A CG    1 
ATOM   1317 C CD1   . LEU A 1 178 ? 7.685  5.588   20.592  1.00 30.90 ?  184 LEU A CD1   1 
ATOM   1318 C CD2   . LEU A 1 178 ? 7.467  7.219   22.452  1.00 29.23 ?  184 LEU A CD2   1 
ATOM   1319 N N     . LEU A 1 179 ? 3.586  5.448   24.141  1.00 32.36 ?  185 LEU A N     1 
ATOM   1320 C CA    . LEU A 1 179 ? 2.189  5.031   24.091  1.00 34.44 ?  185 LEU A CA    1 
ATOM   1321 C C     . LEU A 1 179 ? 2.009  3.929   23.047  1.00 32.92 ?  185 LEU A C     1 
ATOM   1322 O O     . LEU A 1 179 ? 2.517  4.060   21.921  1.00 30.10 ?  185 LEU A O     1 
ATOM   1323 C CB    . LEU A 1 179 ? 1.277  6.209   23.732  1.00 35.71 ?  185 LEU A CB    1 
ATOM   1324 C CG    . LEU A 1 179 ? 1.072  7.393   24.676  1.00 34.81 ?  185 LEU A CG    1 
ATOM   1325 C CD1   . LEU A 1 179 ? 0.457  8.552   23.890  1.00 32.51 ?  185 LEU A CD1   1 
ATOM   1326 C CD2   . LEU A 1 179 ? 0.194  6.999   25.852  1.00 35.60 ?  185 LEU A CD2   1 
ATOM   1327 N N     . PRO A 1 180 ? 1.289  2.853   23.358  1.00 35.18 ?  186 PRO A N     1 
ATOM   1328 C CA    . PRO A 1 180 ? 1.055  1.808   22.344  1.00 34.96 ?  186 PRO A CA    1 
ATOM   1329 C C     . PRO A 1 180 ? 0.453  2.348   21.054  1.00 34.65 ?  186 PRO A C     1 
ATOM   1330 O O     . PRO A 1 180 ? 0.846  1.917   19.960  1.00 35.09 ?  186 PRO A O     1 
ATOM   1331 C CB    . PRO A 1 180 ? 0.105  0.836   23.064  1.00 36.36 ?  186 PRO A CB    1 
ATOM   1332 C CG    . PRO A 1 180 ? 0.388  1.057   24.514  1.00 37.65 ?  186 PRO A CG    1 
ATOM   1333 C CD    . PRO A 1 180 ? 0.657  2.530   24.648  1.00 36.37 ?  186 PRO A CD    1 
ATOM   1334 N N     . SER A 1 181 ? -0.466 3.316   21.152  1.00 33.56 ?  187 SER A N     1 
ATOM   1335 C CA    . SER A 1 181 ? -1.035 3.915   19.946  1.00 34.11 ?  187 SER A CA    1 
ATOM   1336 C C     . SER A 1 181 ? 0.050  4.527   19.065  1.00 30.68 ?  187 SER A C     1 
ATOM   1337 O O     . SER A 1 181 ? -0.037 4.476   17.829  1.00 31.16 ?  187 SER A O     1 
ATOM   1338 C CB    . SER A 1 181 ? -2.077 4.964   20.332  1.00 33.15 ?  187 SER A CB    1 
ATOM   1339 O OG    . SER A 1 181 ? -1.474 5.963   21.125  1.00 33.13 ?  187 SER A OG    1 
ATOM   1340 N N     . VAL A 1 182 ? 1.087  5.103   19.679  1.00 28.62 ?  188 VAL A N     1 
ATOM   1341 C CA    . VAL A 1 182 ? 2.174  5.660   18.888  1.00 28.91 ?  188 VAL A CA    1 
ATOM   1342 C C     . VAL A 1 182 ? 2.937  4.552   18.175  1.00 26.82 ?  188 VAL A C     1 
ATOM   1343 O O     . VAL A 1 182 ? 3.275  4.678   16.995  1.00 25.87 ?  188 VAL A O     1 
ATOM   1344 C CB    . VAL A 1 182 ? 3.115  6.511   19.758  1.00 27.23 ?  188 VAL A CB    1 
ATOM   1345 C CG1   . VAL A 1 182 ? 4.390  6.844   18.976  1.00 23.78 ?  188 VAL A CG1   1 
ATOM   1346 C CG2   . VAL A 1 182 ? 2.428  7.774   20.195  1.00 27.15 ?  188 VAL A CG2   1 
ATOM   1347 N N     . ARG A 1 183 ? 3.235  3.462   18.880  1.00 28.72 ?  189 ARG A N     1 
ATOM   1348 C CA    . ARG A 1 183 ? 4.042  2.394   18.293  1.00 27.85 ?  189 ARG A CA    1 
ATOM   1349 C C     . ARG A 1 183 ? 3.300  1.693   17.164  1.00 26.25 ?  189 ARG A C     1 
ATOM   1350 O O     . ARG A 1 183 ? 3.905  1.305   16.160  1.00 27.93 ?  189 ARG A O     1 
ATOM   1351 C CB    . ARG A 1 183 ? 4.441  1.393   19.376  1.00 27.54 ?  189 ARG A CB    1 
ATOM   1352 C CG    . ARG A 1 183 ? 5.173  2.017   20.547  1.00 30.57 ?  189 ARG A CG    1 
ATOM   1353 C CD    . ARG A 1 183 ? 5.584  0.954   21.554  1.00 32.97 ?  189 ARG A CD    1 
ATOM   1354 N NE    . ARG A 1 183 ? 6.740  0.190   21.093  1.00 34.98 ?  189 ARG A NE    1 
ATOM   1355 C CZ    . ARG A 1 183 ? 7.223  -0.875  21.723  1.00 35.89 ?  189 ARG A CZ    1 
ATOM   1356 N NH1   . ARG A 1 183 ? 6.639  -1.356  22.804  1.00 37.42 ?  189 ARG A NH1   1 
ATOM   1357 N NH2   . ARG A 1 183 ? 8.317  -1.474  21.252  1.00 36.22 ?  189 ARG A NH2   1 
ATOM   1358 N N     . GLN A 1 184 ? 1.989  1.528   17.308  1.00 27.78 ?  190 GLN A N     1 
ATOM   1359 C CA    . GLN A 1 184 ? 1.193  0.936   16.239  1.00 29.23 ?  190 GLN A CA    1 
ATOM   1360 C C     . GLN A 1 184 ? 1.135  1.857   15.028  1.00 29.13 ?  190 GLN A C     1 
ATOM   1361 O O     . GLN A 1 184 ? 1.196  1.395   13.881  1.00 25.96 ?  190 GLN A O     1 
ATOM   1362 C CB    . GLN A 1 184 ? -0.219 0.619   16.756  1.00 32.35 ?  190 GLN A CB    1 
ATOM   1363 C CG    . GLN A 1 184 ? -1.100 -0.161  15.762  1.00 35.21 ?  190 GLN A CG    1 
ATOM   1364 C CD    . GLN A 1 184 ? -0.369 -1.312  15.054  1.00 38.96 ?  190 GLN A CD    1 
ATOM   1365 O OE1   . GLN A 1 184 ? 0.449  -2.016  15.654  1.00 41.70 ?  190 GLN A OE1   1 
ATOM   1366 N NE2   . GLN A 1 184 ? -0.669 -1.504  13.768  1.00 36.48 ?  190 GLN A NE2   1 
ATOM   1367 N N     . GLU A 1 185 ? 1.033  3.165   15.261  1.00 27.47 ?  191 GLU A N     1 
ATOM   1368 C CA    . GLU A 1 185 ? 0.957  4.080   14.134  1.00 27.39 ?  191 GLU A CA    1 
ATOM   1369 C C     . GLU A 1 185 ? 2.281  4.114   13.373  1.00 28.70 ?  191 GLU A C     1 
ATOM   1370 O O     . GLU A 1 185 ? 2.293  4.207   12.136  1.00 24.30 ?  191 GLU A O     1 
ATOM   1371 C CB    . GLU A 1 185 ? 0.525  5.464   14.627  1.00 27.20 ?  191 GLU A CB    1 
ATOM   1372 C CG    . GLU A 1 185 ? 0.186  6.481   13.531  1.00 30.12 ?  191 GLU A CG    1 
ATOM   1373 C CD    . GLU A 1 185 ? -0.960 6.055   12.610  1.00 38.31 ?  191 GLU A CD    1 
ATOM   1374 O OE1   . GLU A 1 185 ? -1.545 4.959   12.797  1.00 38.98 ?  191 GLU A OE1   1 
ATOM   1375 O OE2   . GLU A 1 185 ? -1.283 6.834   11.679  1.00 40.11 -1 191 GLU A OE2   1 
ATOM   1376 N N     . VAL A 1 186 ? 3.404  3.996   14.086  1.00 26.18 ?  192 VAL A N     1 
ATOM   1377 C CA    . VAL A 1 186 ? 4.695  3.942   13.411  1.00 23.07 ?  192 VAL A CA    1 
ATOM   1378 C C     . VAL A 1 186 ? 4.717  2.780   12.434  1.00 24.33 ?  192 VAL A C     1 
ATOM   1379 O O     . VAL A 1 186 ? 5.113  2.929   11.272  1.00 22.59 ?  192 VAL A O     1 
ATOM   1380 C CB    . VAL A 1 186 ? 5.845  3.832   14.428  1.00 24.37 ?  192 VAL A CB    1 
ATOM   1381 C CG1   . VAL A 1 186 ? 7.120  3.365   13.716  1.00 21.61 ?  192 VAL A CG1   1 
ATOM   1382 C CG2   . VAL A 1 186 ? 6.090  5.168   15.117  1.00 23.27 ?  192 VAL A CG2   1 
ATOM   1383 N N     . LYS A 1 187 ? 4.270  1.613   12.891  1.00 23.77 ?  193 LYS A N     1 
ATOM   1384 C CA    . LYS A 1 187 ? 4.189  0.429   12.038  1.00 22.95 ?  193 LYS A CA    1 
ATOM   1385 C C     . LYS A 1 187 ? 3.305  0.679   10.824  1.00 24.05 ?  193 LYS A C     1 
ATOM   1386 O O     . LYS A 1 187 ? 3.677  0.355   9.689   1.00 21.75 ?  193 LYS A O     1 
ATOM   1387 C CB    . LYS A 1 187 ? 3.644  -0.742  12.861  1.00 25.66 ?  193 LYS A CB    1 
ATOM   1388 C CG    . LYS A 1 187 ? 3.762  -2.141  12.248  1.00 27.38 ?  193 LYS A CG    1 
ATOM   1389 C CD    . LYS A 1 187 ? 3.043  -3.117  13.182  1.00 29.19 ?  193 LYS A CD    1 
ATOM   1390 C CE    . LYS A 1 187 ? 3.453  -4.563  12.993  1.00 40.02 ?  193 LYS A CE    1 
ATOM   1391 N NZ    . LYS A 1 187 ? 3.015  -5.108  11.688  1.00 42.69 ?  193 LYS A NZ    1 
ATOM   1392 N N     . GLU A 1 188 ? 2.107  1.227   11.047  1.00 23.35 ?  194 GLU A N     1 
ATOM   1393 C CA    . GLU A 1 188 ? 1.184  1.403   9.931   1.00 24.41 ?  194 GLU A CA    1 
ATOM   1394 C C     . GLU A 1 188 ? 1.721  2.392   8.902   1.00 26.34 ?  194 GLU A C     1 
ATOM   1395 O O     . GLU A 1 188 ? 1.442  2.250   7.707   1.00 24.39 ?  194 GLU A O     1 
ATOM   1396 C CB    . GLU A 1 188 ? -0.190 1.844   10.444  1.00 26.39 ?  194 GLU A CB    1 
ATOM   1397 C CG    . GLU A 1 188 ? -1.082 0.662   10.906  1.00 33.52 ?  194 GLU A CG    1 
ATOM   1398 N N     . ILE A 1 189 ? 2.490  3.393   9.338   1.00 21.72 ?  195 ILE A N     1 
ATOM   1399 C CA    . ILE A 1 189 ? 3.054  4.349   8.393   1.00 24.05 ?  195 ILE A CA    1 
ATOM   1400 C C     . ILE A 1 189 ? 4.180  3.707   7.589   1.00 24.03 ?  195 ILE A C     1 
ATOM   1401 O O     . ILE A 1 189 ? 4.282  3.903   6.371   1.00 21.63 ?  195 ILE A O     1 
ATOM   1402 C CB    . ILE A 1 189 ? 3.530  5.619   9.127   1.00 24.88 ?  195 ILE A CB    1 
ATOM   1403 C CG1   . ILE A 1 189 ? 2.338  6.368   9.742   1.00 25.87 ?  195 ILE A CG1   1 
ATOM   1404 C CG2   . ILE A 1 189 ? 4.301  6.535   8.177   1.00 24.12 ?  195 ILE A CG2   1 
ATOM   1405 C CD1   . ILE A 1 189 ? 2.737  7.354   10.882  1.00 25.58 ?  195 ILE A CD1   1 
ATOM   1406 N N     . LEU A 1 190 ? 5.058  2.944   8.245   1.00 23.32 ?  196 LEU A N     1 
ATOM   1407 C CA    . LEU A 1 190 ? 6.098  2.260   7.478   1.00 22.52 ?  196 LEU A CA    1 
ATOM   1408 C C     . LEU A 1 190 ? 5.485  1.339   6.428   1.00 22.37 ?  196 LEU A C     1 
ATOM   1409 O O     . LEU A 1 190 ? 5.922  1.322   5.268   1.00 20.77 ?  196 LEU A O     1 
ATOM   1410 C CB    . LEU A 1 190 ? 7.020  1.482   8.415   1.00 21.03 ?  196 LEU A CB    1 
ATOM   1411 C CG    . LEU A 1 190 ? 7.859  2.352   9.356   1.00 21.56 ?  196 LEU A CG    1 
ATOM   1412 C CD1   . LEU A 1 190 ? 8.638  1.472   10.317  1.00 21.67 ?  196 LEU A CD1   1 
ATOM   1413 C CD2   . LEU A 1 190 ? 8.824  3.191   8.537   1.00 19.81 ?  196 LEU A CD2   1 
ATOM   1414 N N     . LEU A 1 191 ? 4.448  0.587   6.808   1.00 22.96 ?  197 LEU A N     1 
ATOM   1415 C CA    . LEU A 1 191 ? 3.811  -0.316  5.853   1.00 23.67 ?  197 LEU A CA    1 
ATOM   1416 C C     . LEU A 1 191 ? 3.159  0.452   4.708   1.00 23.64 ?  197 LEU A C     1 
ATOM   1417 O O     . LEU A 1 191 ? 3.289  0.063   3.544   1.00 22.44 ?  197 LEU A O     1 
ATOM   1418 C CB    . LEU A 1 191 ? 2.793  -1.196  6.574   1.00 22.42 ?  197 LEU A CB    1 
ATOM   1419 C CG    . LEU A 1 191 ? 3.461  -2.238  7.478   1.00 22.99 ?  197 LEU A CG    1 
ATOM   1420 C CD1   . LEU A 1 191 ? 2.446  -2.927  8.388   1.00 24.92 ?  197 LEU A CD1   1 
ATOM   1421 C CD2   . LEU A 1 191 ? 4.231  -3.254  6.611   1.00 22.87 ?  197 LEU A CD2   1 
ATOM   1422 N N     . ARG A 1 192 ? 2.478  1.555   5.007   1.00 22.56 ?  198 ARG A N     1 
ATOM   1423 C CA    . ARG A 1 192 ? 1.885  2.354   3.937   1.00 24.03 ?  198 ARG A CA    1 
ATOM   1424 C C     . ARG A 1 192 ? 2.940  2.956   3.015   1.00 24.47 ?  198 ARG A C     1 
ATOM   1425 O O     . ARG A 1 192 ? 2.675  3.143   1.823   1.00 25.46 ?  198 ARG A O     1 
ATOM   1426 C CB    . ARG A 1 192 ? 1.007  3.461   4.526   1.00 23.54 ?  198 ARG A CB    1 
ATOM   1427 C CG    . ARG A 1 192 ? -0.357 2.970   5.024   1.00 31.42 ?  198 ARG A CG    1 
ATOM   1428 C CD    . ARG A 1 192 ? -1.310 4.138   5.344   1.00 33.41 ?  198 ARG A CD    1 
ATOM   1429 N NE    . ARG A 1 192 ? -0.994 4.794   6.609   1.00 32.51 ?  198 ARG A NE    1 
ATOM   1430 C CZ    . ARG A 1 192 ? -1.708 4.638   7.717   1.00 36.81 ?  198 ARG A CZ    1 
ATOM   1431 N NH1   . ARG A 1 192 ? -2.781 3.860   7.745   1.00 39.77 ?  198 ARG A NH1   1 
ATOM   1432 N NH2   . ARG A 1 192 ? -1.339 5.277   8.825   1.00 36.01 ?  198 ARG A NH2   1 
ATOM   1433 N N     . LYS A 1 193 ? 4.131  3.279   3.536   1.00 22.41 ?  199 LYS A N     1 
ATOM   1434 C CA    . LYS A 1 193 ? 5.209  3.757   2.672   1.00 23.58 ?  199 LYS A CA    1 
ATOM   1435 C C     . LYS A 1 193 ? 5.849  2.641   1.858   1.00 24.01 ?  199 LYS A C     1 
ATOM   1436 O O     . LYS A 1 193 ? 6.663  2.939   0.978   1.00 24.99 ?  199 LYS A O     1 
ATOM   1437 C CB    . LYS A 1 193 ? 6.302  4.448   3.486   1.00 19.57 ?  199 LYS A CB    1 
ATOM   1438 C CG    . LYS A 1 193 ? 5.945  5.845   3.991   1.00 21.29 ?  199 LYS A CG    1 
ATOM   1439 C CD    . LYS A 1 193 ? 7.168  6.540   4.588   1.00 22.38 ?  199 LYS A CD    1 
ATOM   1440 C CE    . LYS A 1 193 ? 6.809  7.866   5.253   1.00 18.93 ?  199 LYS A CE    1 
ATOM   1441 N NZ    . LYS A 1 193 ? 6.539  8.963   4.290   1.00 15.45 ?  199 LYS A NZ    1 
ATOM   1442 N N     . GLY A 1 194 ? 5.519  1.376   2.128   1.00 22.54 ?  200 GLY A N     1 
ATOM   1443 C CA    . GLY A 1 194 ? 6.090  0.275   1.363   1.00 23.74 ?  200 GLY A CA    1 
ATOM   1444 C C     . GLY A 1 194 ? 7.343  -0.338  1.951   1.00 21.69 ?  200 GLY A C     1 
ATOM   1445 O O     . GLY A 1 194 ? 8.003  -1.130  1.272   1.00 22.78 ?  200 GLY A O     1 
ATOM   1446 N N     . VAL A 1 195 ? 7.708  0.018   3.182   1.00 21.75 ?  201 VAL A N     1 
ATOM   1447 C CA    . VAL A 1 195 ? 8.835  -0.627  3.839   1.00 18.42 ?  201 VAL A CA    1 
ATOM   1448 C C     . VAL A 1 195 ? 8.426  -2.049  4.178   1.00 22.20 ?  201 VAL A C     1 
ATOM   1449 O O     . VAL A 1 195 ? 7.320  -2.283  4.677   1.00 22.86 ?  201 VAL A O     1 
ATOM   1450 C CB    . VAL A 1 195 ? 9.245  0.167   5.092   1.00 20.37 ?  201 VAL A CB    1 
ATOM   1451 C CG1   . VAL A 1 195 ? 10.411 -0.471  5.820   1.00 19.80 ?  201 VAL A CG1   1 
ATOM   1452 C CG2   . VAL A 1 195 ? 9.595  1.579   4.719   1.00 19.45 ?  201 VAL A CG2   1 
ATOM   1453 N N     . GLN A 1 196 ? 9.284  -3.013  3.853   1.00 20.17 ?  202 GLN A N     1 
ATOM   1454 C CA    . GLN A 1 196 ? 9.042  -4.391  4.249   1.00 23.41 ?  202 GLN A CA    1 
ATOM   1455 C C     . GLN A 1 196 ? 9.568  -4.583  5.667   1.00 24.42 ?  202 GLN A C     1 
ATOM   1456 O O     . GLN A 1 196 ? 10.695 -4.180  5.984   1.00 22.56 ?  202 GLN A O     1 
ATOM   1457 C CB    . GLN A 1 196 ? 9.705  -5.360  3.264   1.00 26.37 ?  202 GLN A CB    1 
ATOM   1458 C CG    . GLN A 1 196 ? 9.191  -5.221  1.819   1.00 27.76 ?  202 GLN A CG    1 
ATOM   1459 C CD    . GLN A 1 196 ? 9.526  -6.427  0.941   1.00 42.58 ?  202 GLN A CD    1 
ATOM   1460 O OE1   . GLN A 1 196 ? 9.427  -7.595  1.372   1.00 39.97 ?  202 GLN A OE1   1 
ATOM   1461 N NE2   . GLN A 1 196 ? 9.921  -6.152  -0.304  1.00 41.61 ?  202 GLN A NE2   1 
ATOM   1462 N N     . LEU A 1 197 ? 8.737  -5.146  6.534   1.00 24.76 ?  203 LEU A N     1 
ATOM   1463 C CA    . LEU A 1 197 ? 9.064  -5.273  7.948   1.00 24.66 ?  203 LEU A CA    1 
ATOM   1464 C C     . LEU A 1 197 ? 9.342  -6.737  8.259   1.00 26.41 ?  203 LEU A C     1 
ATOM   1465 O O     . LEU A 1 197 ? 8.511  -7.604  7.980   1.00 28.32 ?  203 LEU A O     1 
ATOM   1466 C CB    . LEU A 1 197 ? 7.934  -4.741  8.827   1.00 23.18 ?  203 LEU A CB    1 
ATOM   1467 C CG    . LEU A 1 197 ? 7.469  -3.289  8.678   1.00 23.72 ?  203 LEU A CG    1 
ATOM   1468 C CD1   . LEU A 1 197 ? 6.338  -3.007  9.662   1.00 25.75 ?  203 LEU A CD1   1 
ATOM   1469 C CD2   . LEU A 1 197 ? 8.597  -2.314  8.914   1.00 19.95 ?  203 LEU A CD2   1 
ATOM   1470 N N     . LEU A 1 198 ? 10.508 -7.015  8.817   1.00 26.80 ?  204 LEU A N     1 
ATOM   1471 C CA    . LEU A 1 198 ? 10.821 -8.338  9.348   1.00 29.92 ?  204 LEU A CA    1 
ATOM   1472 C C     . LEU A 1 198 ? 10.950 -8.191  10.861  1.00 29.36 ?  204 LEU A C     1 
ATOM   1473 O O     . LEU A 1 198 ? 12.020 -7.837  11.366  1.00 27.94 ?  204 LEU A O     1 
ATOM   1474 C CB    . LEU A 1 198 ? 12.092 -8.900  8.716   1.00 29.84 ?  204 LEU A CB    1 
ATOM   1475 C CG    . LEU A 1 198 ? 11.911 -9.834  7.523   1.00 33.50 ?  204 LEU A CG    1 
ATOM   1476 C CD1   . LEU A 1 198 ? 11.075 -11.039 7.933   1.00 36.82 ?  204 LEU A CD1   1 
ATOM   1477 C CD2   . LEU A 1 198 ? 11.272 -9.121  6.347   1.00 33.39 ?  204 LEU A CD2   1 
ATOM   1478 N N     . LEU A 1 199 ? 9.856  -8.464  11.579  1.00 29.11 ?  205 LEU A N     1 
ATOM   1479 C CA    . LEU A 1 199 ? 9.785  -8.292  13.022  1.00 29.63 ?  205 LEU A CA    1 
ATOM   1480 C C     . LEU A 1 199 ? 10.095 -9.600  13.747  1.00 32.03 ?  205 LEU A C     1 
ATOM   1481 O O     . LEU A 1 199 ? 9.946  -10.685 13.190  1.00 31.89 ?  205 LEU A O     1 
ATOM   1482 C CB    . LEU A 1 199 ? 8.404  -7.777  13.437  1.00 29.91 ?  205 LEU A CB    1 
ATOM   1483 C CG    . LEU A 1 199 ? 8.070  -6.422  12.800  1.00 30.34 ?  205 LEU A CG    1 
ATOM   1484 C CD1   . LEU A 1 199 ? 6.736  -5.873  13.271  1.00 31.40 ?  205 LEU A CD1   1 
ATOM   1485 C CD2   . LEU A 1 199 ? 9.179  -5.435  13.092  1.00 28.54 ?  205 LEU A CD2   1 
ATOM   1486 N N     . SER A 1 200 ? 10.529 -9.473  15.009  1.00 31.02 ?  206 SER A N     1 
ATOM   1487 C CA    . SER A 1 200 ? 10.963 -10.602 15.838  1.00 34.67 ?  206 SER A CA    1 
ATOM   1488 C C     . SER A 1 200 ? 12.070 -11.417 15.169  1.00 35.46 ?  206 SER A C     1 
ATOM   1489 O O     . SER A 1 200 ? 12.075 -12.645 15.239  1.00 36.18 ?  206 SER A O     1 
ATOM   1490 C CB    . SER A 1 200 ? 9.786  -11.511 16.224  1.00 35.26 ?  206 SER A CB    1 
ATOM   1491 O OG    . SER A 1 200 ? 8.807  -10.776 16.942  1.00 35.37 ?  206 SER A OG    1 
ATOM   1492 N N     . GLU A 1 201 ? 13.033 -10.729 14.541  1.00 34.32 ?  207 GLU A N     1 
ATOM   1493 C CA    . GLU A 1 201 ? 14.182 -11.381 13.912  1.00 35.75 ?  207 GLU A CA    1 
ATOM   1494 C C     . GLU A 1 201 ? 15.445 -10.588 14.203  1.00 31.25 ?  207 GLU A C     1 
ATOM   1495 O O     . GLU A 1 201 ? 15.442 -9.358  14.112  1.00 28.94 ?  207 GLU A O     1 
ATOM   1496 C CB    . GLU A 1 201 ? 14.023 -11.499 12.390  1.00 33.21 ?  207 GLU A CB    1 
ATOM   1497 C CG    . GLU A 1 201 ? 12.697 -12.082 11.955  1.00 39.15 ?  207 GLU A CG    1 
ATOM   1498 C CD    . GLU A 1 201 ? 12.850 -13.160 10.903  1.00 43.89 ?  207 GLU A CD    1 
ATOM   1499 O OE1   . GLU A 1 201 ? 13.881 -13.874 10.930  1.00 40.72 ?  207 GLU A OE1   1 
ATOM   1500 O OE2   . GLU A 1 201 ? 11.932 -13.289 10.054  1.00 45.92 -1 207 GLU A OE2   1 
ATOM   1501 N N     . ARG A 1 202 ? 16.524 -11.292 14.530  1.00 31.93 ?  208 ARG A N     1 
ATOM   1502 C CA    . ARG A 1 202 ? 17.815 -10.673 14.815  1.00 32.99 ?  208 ARG A CA    1 
ATOM   1503 C C     . ARG A 1 202 ? 18.786 -10.999 13.682  1.00 33.70 ?  208 ARG A C     1 
ATOM   1504 O O     . ARG A 1 202 ? 18.990 -12.173 13.354  1.00 32.47 ?  208 ARG A O     1 
ATOM   1505 C CB    . ARG A 1 202 ? 18.373 -11.147 16.163  1.00 33.31 ?  208 ARG A CB    1 
ATOM   1506 C CG    . ARG A 1 202 ? 19.609 -10.364 16.620  1.00 35.73 ?  208 ARG A CG    1 
ATOM   1507 C CD    . ARG A 1 202 ? 19.983 -10.611 18.096  1.00 40.05 ?  208 ARG A CD    1 
ATOM   1508 N NE    . ARG A 1 202 ? 19.158 -9.837  19.025  1.00 41.37 ?  208 ARG A NE    1 
ATOM   1509 C CZ    . ARG A 1 202 ? 19.399 -8.583  19.405  1.00 42.09 ?  208 ARG A CZ    1 
ATOM   1510 N NH1   . ARG A 1 202 ? 20.445 -7.906  18.949  1.00 37.03 ?  208 ARG A NH1   1 
ATOM   1511 N NH2   . ARG A 1 202 ? 18.569 -7.993  20.267  1.00 40.83 ?  208 ARG A NH2   1 
ATOM   1512 N N     . VAL A 1 203 ? 19.372 -9.964  13.076  1.00 30.14 ?  209 VAL A N     1 
ATOM   1513 C CA    . VAL A 1 203 ? 20.390 -10.198 12.060  1.00 32.03 ?  209 VAL A CA    1 
ATOM   1514 C C     . VAL A 1 203 ? 21.604 -10.820 12.733  1.00 33.69 ?  209 VAL A C     1 
ATOM   1515 O O     . VAL A 1 203 ? 22.101 -10.303 13.744  1.00 31.72 ?  209 VAL A O     1 
ATOM   1516 C CB    . VAL A 1 203 ? 20.750 -8.895  11.333  1.00 28.21 ?  209 VAL A CB    1 
ATOM   1517 C CG1   . VAL A 1 203 ? 22.043 -9.073  10.532  1.00 28.08 ?  209 VAL A CG1   1 
ATOM   1518 C CG2   . VAL A 1 203 ? 19.605 -8.466  10.409  1.00 26.54 ?  209 VAL A CG2   1 
ATOM   1519 N N     . SER A 1 204 ? 22.087 -11.936 12.178  1.00 32.06 ?  210 SER A N     1 
ATOM   1520 C CA    . SER A 1 204 ? 23.048 -12.780 12.872  1.00 34.25 ?  210 SER A CA    1 
ATOM   1521 C C     . SER A 1 204 ? 24.437 -12.834 12.248  1.00 35.02 ?  210 SER A C     1 
ATOM   1522 O O     . SER A 1 204 ? 25.341 -13.386 12.877  1.00 39.57 ?  210 SER A O     1 
ATOM   1523 C CB    . SER A 1 204 ? 22.500 -14.211 12.991  1.00 36.35 ?  210 SER A CB    1 
ATOM   1524 O OG    . SER A 1 204 ? 22.018 -14.666 11.743  1.00 35.96 ?  210 SER A OG    1 
ATOM   1525 N N     . ASN A 1 205 ? 24.654 -12.281 11.058  1.00 34.68 ?  211 ASN A N     1 
ATOM   1526 C CA    . ASN A 1 205 ? 25.984 -12.301 10.452  1.00 36.07 ?  211 ASN A CA    1 
ATOM   1527 C C     . ASN A 1 205 ? 26.569 -10.888 10.340  1.00 36.53 ?  211 ASN A C     1 
ATOM   1528 O O     . ASN A 1 205 ? 27.236 -10.546 9.362   1.00 36.59 ?  211 ASN A O     1 
ATOM   1529 C CB    . ASN A 1 205 ? 25.962 -13.022 9.093   1.00 33.64 ?  211 ASN A CB    1 
ATOM   1530 C CG    . ASN A 1 205 ? 25.056 -12.347 8.050   1.00 35.91 ?  211 ASN A CG    1 
ATOM   1531 O OD1   . ASN A 1 205 ? 24.161 -11.556 8.380   1.00 31.16 ?  211 ASN A OD1   1 
ATOM   1532 N ND2   . ASN A 1 205 ? 25.286 -12.674 6.776   1.00 32.83 ?  211 ASN A ND2   1 
ATOM   1533 N N     . LEU A 1 206 ? 26.356 -10.061 11.372  1.00 37.52 ?  212 LEU A N     1 
ATOM   1534 C CA    . LEU A 1 206 ? 26.740 -8.651  11.297  1.00 35.47 ?  212 LEU A CA    1 
ATOM   1535 C C     . LEU A 1 206 ? 28.236 -8.475  11.064  1.00 37.36 ?  212 LEU A C     1 
ATOM   1536 O O     . LEU A 1 206 ? 28.650 -7.551  10.352  1.00 35.60 ?  212 LEU A O     1 
ATOM   1537 C CB    . LEU A 1 206 ? 26.326 -7.919  12.574  1.00 34.80 ?  212 LEU A CB    1 
ATOM   1538 C CG    . LEU A 1 206 ? 24.871 -7.497  12.654  1.00 32.03 ?  212 LEU A CG    1 
ATOM   1539 C CD1   . LEU A 1 206 ? 24.639 -6.734  13.939  1.00 37.16 ?  212 LEU A CD1   1 
ATOM   1540 C CD2   . LEU A 1 206 ? 24.527 -6.644  11.457  1.00 32.75 ?  212 LEU A CD2   1 
ATOM   1541 N N     . GLU A 1 207 ? 29.062 -9.342  11.664  1.00 38.50 ?  213 GLU A N     1 
ATOM   1542 C CA    . GLU A 1 207 ? 30.511 -9.221  11.501  1.00 41.58 ?  213 GLU A CA    1 
ATOM   1543 C C     . GLU A 1 207 ? 30.945 -9.438  10.060  1.00 40.27 ?  213 GLU A C     1 
ATOM   1544 O O     . GLU A 1 207 ? 31.998 -8.940  9.645   1.00 43.75 ?  213 GLU A O     1 
ATOM   1545 C CB    . GLU A 1 207 ? 31.242 -10.224 12.393  1.00 45.55 ?  213 GLU A CB    1 
ATOM   1546 C CG    . GLU A 1 207 ? 31.830 -9.622  13.653  1.00 50.23 ?  213 GLU A CG    1 
ATOM   1547 C CD    . GLU A 1 207 ? 30.980 -9.915  14.871  1.00 58.76 ?  213 GLU A CD    1 
ATOM   1548 O OE1   . GLU A 1 207 ? 29.779 -10.220 14.684  1.00 60.52 ?  213 GLU A OE1   1 
ATOM   1549 O OE2   . GLU A 1 207 ? 31.514 -9.863  16.005  1.00 56.95 -1 213 GLU A OE2   1 
ATOM   1550 N N     . GLU A 1 208 ? 30.164 -10.187 9.292   1.00 37.88 ?  214 GLU A N     1 
ATOM   1551 C CA    . GLU A 1 208 ? 30.520 -10.553 7.934   1.00 35.20 ?  214 GLU A CA    1 
ATOM   1552 C C     . GLU A 1 208 ? 29.911 -9.618  6.906   1.00 34.19 ?  214 GLU A C     1 
ATOM   1553 O O     . GLU A 1 208 ? 30.029 -9.874  5.709   1.00 37.43 ?  214 GLU A O     1 
ATOM   1554 C CB    . GLU A 1 208 ? 30.088 -11.996 7.657   1.00 36.42 ?  214 GLU A CB    1 
ATOM   1555 N N     . LEU A 1 209 ? 29.269 -8.542  7.335   1.00 32.15 ?  215 LEU A N     1 
ATOM   1556 C CA    . LEU A 1 209 ? 28.558 -7.709  6.385   1.00 31.57 ?  215 LEU A CA    1 
ATOM   1557 C C     . LEU A 1 209 ? 29.333 -6.434  6.092   1.00 28.79 ?  215 LEU A C     1 
ATOM   1558 O O     . LEU A 1 209 ? 29.801 -5.775  7.025   1.00 29.56 ?  215 LEU A O     1 
ATOM   1559 C CB    . LEU A 1 209 ? 27.165 -7.352  6.916   1.00 30.76 ?  215 LEU A CB    1 
ATOM   1560 C CG    . LEU A 1 209 ? 26.115 -8.454  7.055   1.00 31.71 ?  215 LEU A CG    1 
ATOM   1561 C CD1   . LEU A 1 209 ? 24.894 -7.866  7.727   1.00 30.46 ?  215 LEU A CD1   1 
ATOM   1562 C CD2   . LEU A 1 209 ? 25.738 -9.020  5.715   1.00 27.21 ?  215 LEU A CD2   1 
ATOM   1563 N N     . PRO A 1 210 ? 29.490 -6.062  4.825   1.00 29.50 ?  216 PRO A N     1 
ATOM   1564 C CA    . PRO A 1 210 ? 29.921 -4.694  4.507   1.00 28.07 ?  216 PRO A CA    1 
ATOM   1565 C C     . PRO A 1 210 ? 28.848 -3.712  4.947   1.00 26.94 ?  216 PRO A C     1 
ATOM   1566 O O     . PRO A 1 210 ? 27.662 -3.888  4.644   1.00 27.07 ?  216 PRO A O     1 
ATOM   1567 C CB    . PRO A 1 210 ? 30.085 -4.710  2.980   1.00 28.79 ?  216 PRO A CB    1 
ATOM   1568 C CG    . PRO A 1 210 ? 29.972 -6.167  2.560   1.00 28.10 ?  216 PRO A CG    1 
ATOM   1569 C CD    . PRO A 1 210 ? 29.165 -6.846  3.622   1.00 26.46 ?  216 PRO A CD    1 
ATOM   1570 N N     . LEU A 1 211 ? 29.262 -2.674  5.672   1.00 25.58 ?  217 LEU A N     1 
ATOM   1571 C CA    . LEU A 1 211 ? 28.336 -1.700  6.238   1.00 24.00 ?  217 LEU A CA    1 
ATOM   1572 C C     . LEU A 1 211 ? 28.471 -0.365  5.527   1.00 24.42 ?  217 LEU A C     1 
ATOM   1573 O O     . LEU A 1 211 ? 29.582 0.049   5.184   1.00 24.76 ?  217 LEU A O     1 
ATOM   1574 C CB    . LEU A 1 211 ? 28.597 -1.501  7.736   1.00 22.62 ?  217 LEU A CB    1 
ATOM   1575 C CG    . LEU A 1 211 ? 28.470 -2.763  8.582   1.00 24.53 ?  217 LEU A CG    1 
ATOM   1576 C CD1   . LEU A 1 211 ? 28.716 -2.444  10.058  1.00 24.86 ?  217 LEU A CD1   1 
ATOM   1577 C CD2   . LEU A 1 211 ? 27.091 -3.364  8.382   1.00 24.78 ?  217 LEU A CD2   1 
ATOM   1578 N N     . ASN A 1 212 ? 27.338 0.314   5.331   1.00 20.89 ?  218 ASN A N     1 
ATOM   1579 C CA    . ASN A 1 212 ? 27.312 1.663   4.766   1.00 21.25 ?  218 ASN A CA    1 
ATOM   1580 C C     . ASN A 1 212 ? 28.010 1.750   3.415   1.00 21.87 ?  218 ASN A C     1 
ATOM   1581 O O     . ASN A 1 212 ? 28.543 2.798   3.053   1.00 23.86 ?  218 ASN A O     1 
ATOM   1582 C CB    . ASN A 1 212 ? 27.940 2.666   5.724   1.00 23.33 ?  218 ASN A CB    1 
ATOM   1583 C CG    . ASN A 1 212 ? 27.240 2.716   7.049   1.00 21.32 ?  218 ASN A CG    1 
ATOM   1584 O OD1   . ASN A 1 212 ? 26.017 2.600   7.124   1.00 20.67 ?  218 ASN A OD1   1 
ATOM   1585 N ND2   . ASN A 1 212 ? 28.010 2.894   8.112   1.00 23.59 ?  218 ASN A ND2   1 
ATOM   1586 N N     . GLU A 1 213 ? 28.017 0.667   2.648   1.00 20.83 ?  219 GLU A N     1 
ATOM   1587 C CA    . GLU A 1 213 ? 28.686 0.678   1.353   1.00 21.34 ?  219 GLU A CA    1 
ATOM   1588 C C     . GLU A 1 213 ? 27.880 -0.133  0.354   1.00 21.56 ?  219 GLU A C     1 
ATOM   1589 O O     . GLU A 1 213 ? 27.483 -1.263  0.649   1.00 20.53 ?  219 GLU A O     1 
ATOM   1590 C CB    . GLU A 1 213 ? 30.107 0.107   1.467   1.00 24.49 ?  219 GLU A CB    1 
ATOM   1591 N N     . TYR A 1 214 ? 27.664 0.438   -0.828  1.00 21.73 ?  220 TYR A N     1 
ATOM   1592 C CA    . TYR A 1 214 ? 26.998 -0.281  -1.899  1.00 20.09 ?  220 TYR A CA    1 
ATOM   1593 C C     . TYR A 1 214 ? 27.832 -1.475  -2.355  1.00 24.60 ?  220 TYR A C     1 
ATOM   1594 O O     . TYR A 1 214 ? 29.058 -1.392  -2.492  1.00 23.02 ?  220 TYR A O     1 
ATOM   1595 C CB    . TYR A 1 214 ? 26.732 0.649   -3.083  1.00 22.26 ?  220 TYR A CB    1 
ATOM   1596 C CG    . TYR A 1 214 ? 26.385 -0.110  -4.346  1.00 22.43 ?  220 TYR A CG    1 
ATOM   1597 C CD1   . TYR A 1 214 ? 25.095 -0.554  -4.578  1.00 21.34 ?  220 TYR A CD1   1 
ATOM   1598 C CD2   . TYR A 1 214 ? 27.360 -0.415  -5.289  1.00 23.51 ?  220 TYR A CD2   1 
ATOM   1599 C CE1   . TYR A 1 214 ? 24.782 -1.271  -5.728  1.00 22.18 ?  220 TYR A CE1   1 
ATOM   1600 C CE2   . TYR A 1 214 ? 27.058 -1.132  -6.424  1.00 22.41 ?  220 TYR A CE2   1 
ATOM   1601 C CZ    . TYR A 1 214 ? 25.770 -1.563  -6.634  1.00 21.23 ?  220 TYR A CZ    1 
ATOM   1602 O OH    . TYR A 1 214 ? 25.466 -2.273  -7.770  1.00 25.05 ?  220 TYR A OH    1 
ATOM   1603 N N     . ARG A 1 215 ? 27.156 -2.593  -2.572  1.00 21.37 ?  221 ARG A N     1 
ATOM   1604 C CA    . ARG A 1 215 ? 27.732 -3.767  -3.200  1.00 22.87 ?  221 ARG A CA    1 
ATOM   1605 C C     . ARG A 1 215 ? 26.676 -4.337  -4.126  1.00 22.31 ?  221 ARG A C     1 
ATOM   1606 O O     . ARG A 1 215 ? 25.473 -4.192  -3.872  1.00 20.04 ?  221 ARG A O     1 
ATOM   1607 C CB    . ARG A 1 215 ? 28.164 -4.850  -2.189  1.00 22.92 ?  221 ARG A CB    1 
ATOM   1608 C CG    . ARG A 1 215 ? 29.140 -4.394  -1.095  1.00 26.17 ?  221 ARG A CG    1 
ATOM   1609 C CD    . ARG A 1 215 ? 30.552 -4.170  -1.629  1.00 29.63 ?  221 ARG A CD    1 
ATOM   1610 N NE    . ARG A 1 215 ? 31.570 -4.734  -0.741  1.00 34.83 ?  221 ARG A NE    1 
ATOM   1611 C CZ    . ARG A 1 215 ? 32.306 -4.037  0.118   1.00 36.27 ?  221 ARG A CZ    1 
ATOM   1612 N NH1   . ARG A 1 215 ? 32.180 -2.722  0.240   1.00 34.80 ?  221 ARG A NH1   1 
ATOM   1613 N NH2   . ARG A 1 215 ? 33.198 -4.678  0.875   1.00 36.32 ?  221 ARG A NH2   1 
ATOM   1614 N N     . GLU A 1 216 ? 27.137 -4.983  -5.208  1.00 21.33 ?  222 GLU A N     1 
ATOM   1615 C CA    . GLU A 1 216 ? 26.208 -5.616  -6.133  1.00 19.73 ?  222 GLU A CA    1 
ATOM   1616 C C     . GLU A 1 216 ? 25.372 -6.676  -5.433  1.00 21.70 ?  222 GLU A C     1 
ATOM   1617 O O     . GLU A 1 216 ? 24.195 -6.853  -5.763  1.00 19.23 ?  222 GLU A O     1 
ATOM   1618 C CB    . GLU A 1 216 ? 26.967 -6.228  -7.315  1.00 22.72 ?  222 GLU A CB    1 
ATOM   1619 C CG    . GLU A 1 216 ? 27.730 -5.220  -8.182  1.00 22.97 ?  222 GLU A CG    1 
ATOM   1620 N N     . TYR A 1 217 ? 25.942 -7.365  -4.438  1.00 23.17 ?  223 TYR A N     1 
ATOM   1621 C CA    . TYR A 1 217 ? 25.192 -8.400  -3.733  1.00 24.87 ?  223 TYR A CA    1 
ATOM   1622 C C     . TYR A 1 217 ? 25.689 -8.592  -2.308  1.00 22.75 ?  223 TYR A C     1 
ATOM   1623 O O     . TYR A 1 217 ? 26.881 -8.828  -2.101  1.00 24.08 ?  223 TYR A O     1 
ATOM   1624 C CB    . TYR A 1 217 ? 25.278 -9.727  -4.472  1.00 24.92 ?  223 TYR A CB    1 
ATOM   1625 C CG    . TYR A 1 217 ? 24.568 -10.832 -3.741  1.00 24.59 ?  223 TYR A CG    1 
ATOM   1626 C CD1   . TYR A 1 217 ? 25.249 -11.636 -2.829  1.00 25.01 ?  223 TYR A CD1   1 
ATOM   1627 C CD2   . TYR A 1 217 ? 23.232 -11.092 -3.975  1.00 23.52 ?  223 TYR A CD2   1 
ATOM   1628 C CE1   . TYR A 1 217 ? 24.613 -12.652 -2.159  1.00 28.13 ?  223 TYR A CE1   1 
ATOM   1629 C CE2   . TYR A 1 217 ? 22.584 -12.123 -3.308  1.00 25.79 ?  223 TYR A CE2   1 
ATOM   1630 C CZ    . TYR A 1 217 ? 23.277 -12.895 -2.400  1.00 27.41 ?  223 TYR A CZ    1 
ATOM   1631 O OH    . TYR A 1 217 ? 22.655 -13.927 -1.723  1.00 31.18 ?  223 TYR A OH    1 
ATOM   1632 N N     . ILE A 1 218 ? 24.762 -8.537  -1.348  1.00 21.60 ?  224 ILE A N     1 
ATOM   1633 C CA    . ILE A 1 218 ? 25.026 -8.784  0.068   1.00 22.13 ?  224 ILE A CA    1 
ATOM   1634 C C     . ILE A 1 218 ? 23.892 -9.660  0.587   1.00 25.18 ?  224 ILE A C     1 
ATOM   1635 O O     . ILE A 1 218 ? 22.718 -9.387  0.312   1.00 21.83 ?  224 ILE A O     1 
ATOM   1636 C CB    . ILE A 1 218 ? 25.108 -7.476  0.887   1.00 23.47 ?  224 ILE A CB    1 
ATOM   1637 C CG1   . ILE A 1 218 ? 26.216 -6.549  0.368   1.00 21.10 ?  224 ILE A CG1   1 
ATOM   1638 C CG2   . ILE A 1 218 ? 25.295 -7.768  2.386   1.00 24.46 ?  224 ILE A CG2   1 
ATOM   1639 C CD1   . ILE A 1 218 ? 26.179 -5.157  0.996   1.00 20.34 ?  224 ILE A CD1   1 
ATOM   1640 N N     . LYS A 1 219 ? 24.234 -10.730 1.305   1.00 24.01 ?  225 LYS A N     1 
ATOM   1641 C CA    . LYS A 1 219 ? 23.238 -11.620 1.883   1.00 26.85 ?  225 LYS A CA    1 
ATOM   1642 C C     . LYS A 1 219 ? 23.191 -11.389 3.381   1.00 29.60 ?  225 LYS A C     1 
ATOM   1643 O O     . LYS A 1 219 ? 24.180 -11.634 4.084   1.00 28.42 ?  225 LYS A O     1 
ATOM   1644 C CB    . LYS A 1 219 ? 23.531 -13.091 1.605   1.00 27.87 ?  225 LYS A CB    1 
ATOM   1645 C CG    . LYS A 1 219 ? 22.539 -14.015 2.301   1.00 29.13 ?  225 LYS A CG    1 
ATOM   1646 C CD    . LYS A 1 219 ? 22.731 -15.472 1.866   1.00 37.03 ?  225 LYS A CD    1 
ATOM   1647 C CE    . LYS A 1 219 ? 23.271 -16.320 3.014   1.00 39.28 ?  225 LYS A CE    1 
ATOM   1648 N NZ    . LYS A 1 219 ? 23.151 -17.805 2.749   1.00 41.08 ?  225 LYS A NZ    1 
ATOM   1649 N N     . VAL A 1 220 ? 22.043 -10.931 3.861   1.00 27.28 ?  226 VAL A N     1 
ATOM   1650 C CA    . VAL A 1 220 ? 21.799 -10.734 5.279   1.00 26.89 ?  226 VAL A CA    1 
ATOM   1651 C C     . VAL A 1 220 ? 21.128 -11.991 5.812   1.00 29.29 ?  226 VAL A C     1 
ATOM   1652 O O     . VAL A 1 220 ? 20.216 -12.530 5.178   1.00 31.06 ?  226 VAL A O     1 
ATOM   1653 C CB    . VAL A 1 220 ? 20.940 -9.478  5.510   1.00 27.01 ?  226 VAL A CB    1 
ATOM   1654 C CG1   . VAL A 1 220 ? 20.646 -9.288  6.974   1.00 24.83 ?  226 VAL A CG1   1 
ATOM   1655 C CG2   . VAL A 1 220 ? 21.663 -8.259  4.965   1.00 22.85 ?  226 VAL A CG2   1 
ATOM   1656 N N     . GLN A 1 221 ? 21.603 -12.487 6.949   1.00 29.28 ?  227 GLN A N     1 
ATOM   1657 C CA    . GLN A 1 221 ? 21.001 -13.649 7.582   1.00 31.61 ?  227 GLN A CA    1 
ATOM   1658 C C     . GLN A 1 221 ? 20.421 -13.266 8.932   1.00 31.72 ?  227 GLN A C     1 
ATOM   1659 O O     . GLN A 1 221 ? 20.923 -12.364 9.610   1.00 30.03 ?  227 GLN A O     1 
ATOM   1660 C CB    . GLN A 1 221 ? 22.013 -14.775 7.781   1.00 35.19 ?  227 GLN A CB    1 
ATOM   1661 C CG    . GLN A 1 221 ? 22.643 -15.269 6.520   1.00 37.80 ?  227 GLN A CG    1 
ATOM   1662 C CD    . GLN A 1 221 ? 23.420 -16.545 6.743   1.00 42.44 ?  227 GLN A CD    1 
ATOM   1663 O OE1   . GLN A 1 221 ? 23.119 -17.568 6.137   1.00 48.27 ?  227 GLN A OE1   1 
ATOM   1664 N NE2   . GLN A 1 221 ? 24.428 -16.493 7.618   1.00 40.71 ?  227 GLN A NE2   1 
ATOM   1665 N N     . THR A 1 222 ? 19.359 -13.966 9.317   1.00 31.40 ?  228 THR A N     1 
ATOM   1666 C CA    . THR A 1 222 ? 18.788 -13.826 10.647  1.00 35.47 ?  228 THR A CA    1 
ATOM   1667 C C     . THR A 1 222 ? 18.845 -15.165 11.377  1.00 35.24 ?  228 THR A C     1 
ATOM   1668 O O     . THR A 1 222 ? 19.039 -16.222 10.768  1.00 35.49 ?  228 THR A O     1 
ATOM   1669 C CB    . THR A 1 222 ? 17.337 -13.324 10.597  1.00 36.00 ?  228 THR A CB    1 
ATOM   1670 O OG1   . THR A 1 222 ? 16.477 -14.378 10.138  1.00 36.59 ?  228 THR A OG1   1 
ATOM   1671 C CG2   . THR A 1 222 ? 17.210 -12.120 9.667   1.00 32.06 ?  228 THR A CG2   1 
ATOM   1672 N N     . ASP A 1 223 ? 18.658 -15.102 12.698  1.00 35.88 ?  229 ASP A N     1 
ATOM   1673 C CA    . ASP A 1 223 ? 18.723 -16.279 13.560  1.00 39.58 ?  229 ASP A CA    1 
ATOM   1674 C C     . ASP A 1 223 ? 17.569 -17.251 13.338  1.00 41.23 ?  229 ASP A C     1 
ATOM   1675 O O     . ASP A 1 223 ? 17.630 -18.374 13.849  1.00 41.88 ?  229 ASP A O     1 
ATOM   1676 C CB    . ASP A 1 223 ? 18.773 -15.855 15.041  1.00 39.36 ?  229 ASP A CB    1 
ATOM   1677 C CG    . ASP A 1 223 ? 17.554 -15.008 15.480  1.00 44.77 ?  229 ASP A CG    1 
ATOM   1678 O OD1   . ASP A 1 223 ? 16.778 -14.543 14.609  1.00 43.73 ?  229 ASP A OD1   1 
ATOM   1679 O OD2   . ASP A 1 223 ? 17.373 -14.801 16.712  1.00 47.40 -1 229 ASP A OD2   1 
ATOM   1680 N N     . LYS A 1 224 ? 16.530 -16.860 12.600  1.00 40.47 ?  230 LYS A N     1 
ATOM   1681 C CA    . LYS A 1 224 ? 15.459 -17.775 12.226  1.00 41.22 ?  230 LYS A CA    1 
ATOM   1682 C C     . LYS A 1 224 ? 15.646 -18.356 10.826  1.00 41.29 ?  230 LYS A C     1 
ATOM   1683 O O     . LYS A 1 224 ? 14.738 -19.014 10.308  1.00 46.14 ?  230 LYS A O     1 
ATOM   1684 C CB    . LYS A 1 224 ? 14.099 -17.075 12.343  1.00 40.38 ?  230 LYS A CB    1 
ATOM   1685 C CG    . LYS A 1 224 ? 13.647 -16.861 13.802  1.00 46.66 ?  230 LYS A CG    1 
ATOM   1686 C CD    . LYS A 1 224 ? 12.434 -15.927 13.913  1.00 42.89 ?  230 LYS A CD    1 
ATOM   1687 C CE    . LYS A 1 224 ? 11.751 -16.061 15.279  1.00 48.34 ?  230 LYS A CE    1 
ATOM   1688 N NZ    . LYS A 1 224 ? 10.568 -15.140 15.417  1.00 44.57 ?  230 LYS A NZ    1 
ATOM   1689 N N     . GLY A 1 225 ? 16.806 -18.150 10.208  1.00 38.70 ?  231 GLY A N     1 
ATOM   1690 C CA    . GLY A 1 225 ? 17.046 -18.674 8.878   1.00 38.63 ?  231 GLY A CA    1 
ATOM   1691 C C     . GLY A 1 225 ? 16.525 -17.823 7.739   1.00 35.46 ?  231 GLY A C     1 
ATOM   1692 O O     . GLY A 1 225 ? 16.635 -18.242 6.583   1.00 39.84 ?  231 GLY A O     1 
ATOM   1693 N N     . THR A 1 226 ? 15.962 -16.648 8.011   1.00 36.04 ?  232 THR A N     1 
ATOM   1694 C CA    . THR A 1 226 ? 15.575 -15.757 6.923   1.00 35.07 ?  232 THR A CA    1 
ATOM   1695 C C     . THR A 1 226 ? 16.820 -15.165 6.271   1.00 34.41 ?  232 THR A C     1 
ATOM   1696 O O     . THR A 1 226 ? 17.770 -14.761 6.953   1.00 35.07 ?  232 THR A O     1 
ATOM   1697 C CB    . THR A 1 226 ? 14.666 -14.624 7.417   1.00 33.01 ?  232 THR A CB    1 
ATOM   1698 O OG1   . THR A 1 226 ? 13.728 -15.129 8.369   1.00 36.90 ?  232 THR A OG1   1 
ATOM   1699 C CG2   . THR A 1 226 ? 13.885 -14.038 6.259   1.00 30.82 ?  232 THR A CG2   1 
ATOM   1700 N N     . GLU A 1 227 ? 16.808 -15.111 4.942   1.00 30.24 ?  233 GLU A N     1 
ATOM   1701 C CA    . GLU A 1 227 ? 17.917 -14.592 4.154   1.00 30.47 ?  233 GLU A CA    1 
ATOM   1702 C C     . GLU A 1 227 ? 17.391 -13.486 3.256   1.00 30.24 ?  233 GLU A C     1 
ATOM   1703 O O     . GLU A 1 227 ? 16.371 -13.668 2.585   1.00 29.48 ?  233 GLU A O     1 
ATOM   1704 C CB    . GLU A 1 227 ? 18.565 -15.699 3.315   1.00 33.57 ?  233 GLU A CB    1 
ATOM   1705 C CG    . GLU A 1 227 ? 19.215 -16.793 4.141   1.00 36.18 ?  233 GLU A CG    1 
ATOM   1706 C CD    . GLU A 1 227 ? 19.601 -18.002 3.310   1.00 42.74 ?  233 GLU A CD    1 
ATOM   1707 O OE1   . GLU A 1 227 ? 18.761 -18.491 2.514   1.00 44.42 ?  233 GLU A OE1   1 
ATOM   1708 O OE2   . GLU A 1 227 ? 20.753 -18.462 3.455   1.00 46.90 -1 233 GLU A OE2   1 
ATOM   1709 N N     . VAL A 1 228 ? 18.072 -12.339 3.260   1.00 29.06 ?  234 VAL A N     1 
ATOM   1710 C CA    . VAL A 1 228 ? 17.658 -11.169 2.497   1.00 25.49 ?  234 VAL A CA    1 
ATOM   1711 C C     . VAL A 1 228 ? 18.834 -10.736 1.636   1.00 25.38 ?  234 VAL A C     1 
ATOM   1712 O O     . VAL A 1 228 ? 19.912 -10.429 2.166   1.00 24.85 ?  234 VAL A O     1 
ATOM   1713 C CB    . VAL A 1 228 ? 17.194 -10.014 3.406   1.00 28.77 ?  234 VAL A CB    1 
ATOM   1714 C CG1   . VAL A 1 228 ? 16.864 -8.748  2.578   1.00 26.16 ?  234 VAL A CG1   1 
ATOM   1715 C CG2   . VAL A 1 228 ? 15.995 -10.430 4.261   1.00 27.22 ?  234 VAL A CG2   1 
ATOM   1716 N N     . ALA A 1 229 ? 18.638 -10.729 0.317   1.00 23.42 ?  235 ALA A N     1 
ATOM   1717 C CA    . ALA A 1 229 ? 19.603 -10.143 -0.610  1.00 24.85 ?  235 ALA A CA    1 
ATOM   1718 C C     . ALA A 1 229 ? 19.418 -8.626  -0.690  1.00 23.38 ?  235 ALA A C     1 
ATOM   1719 O O     . ALA A 1 229 ? 18.284 -8.127  -0.737  1.00 24.59 ?  235 ALA A O     1 
ATOM   1720 C CB    . ALA A 1 229 ? 19.451 -10.773 -1.999  1.00 24.08 ?  235 ALA A CB    1 
ATOM   1721 N N     . THR A 1 230 ? 20.536 -7.885  -0.670  1.00 20.97 ?  236 THR A N     1 
ATOM   1722 C CA    . THR A 1 230 ? 20.472 -6.426  -0.634  1.00 20.76 ?  236 THR A CA    1 
ATOM   1723 C C     . THR A 1 230 ? 21.740 -5.824  -1.237  1.00 21.25 ?  236 THR A C     1 
ATOM   1724 O O     . THR A 1 230 ? 22.748 -6.510  -1.438  1.00 20.75 ?  236 THR A O     1 
ATOM   1725 C CB    . THR A 1 230 ? 20.262 -5.900  0.801   1.00 21.91 ?  236 THR A CB    1 
ATOM   1726 O OG1   . THR A 1 230 ? 20.086 -4.473  0.775   1.00 20.15 ?  236 THR A OG1   1 
ATOM   1727 C CG2   . THR A 1 230 ? 21.458 -6.224  1.669   1.00 19.55 ?  236 THR A CG2   1 
ATOM   1728 N N     . ASN A 1 231 ? 21.682 -4.509  -1.503  1.00 18.89 ?  237 ASN A N     1 
ATOM   1729 C CA    . ASN A 1 231 ? 22.848 -3.753  -1.965  1.00 19.28 ?  237 ASN A CA    1 
ATOM   1730 C C     . ASN A 1 231 ? 23.524 -2.943  -0.876  1.00 18.17 ?  237 ASN A C     1 
ATOM   1731 O O     . ASN A 1 231 ? 24.659 -2.504  -1.083  1.00 18.76 ?  237 ASN A O     1 
ATOM   1732 C CB    . ASN A 1 231 ? 22.490 -2.766  -3.085  1.00 19.09 ?  237 ASN A CB    1 
ATOM   1733 C CG    . ASN A 1 231 ? 21.943 -3.442  -4.318  1.00 21.06 ?  237 ASN A CG    1 
ATOM   1734 O OD1   . ASN A 1 231 ? 20.863 -3.094  -4.780  1.00 19.80 ?  237 ASN A OD1   1 
ATOM   1735 N ND2   . ASN A 1 231 ? 22.683 -4.414  -4.862  1.00 22.43 ?  237 ASN A ND2   1 
ATOM   1736 N N     . LEU A 1 232 ? 22.853 -2.707  0.252   1.00 17.31 ?  238 LEU A N     1 
ATOM   1737 C CA    . LEU A 1 232 ? 23.351 -1.785  1.271   1.00 17.25 ?  238 LEU A CA    1 
ATOM   1738 C C     . LEU A 1 232 ? 22.780 -2.194  2.620   1.00 17.78 ?  238 LEU A C     1 
ATOM   1739 O O     . LEU A 1 232 ? 21.586 -2.489  2.728   1.00 17.91 ?  238 LEU A O     1 
ATOM   1740 C CB    . LEU A 1 232 ? 22.956 -0.342  0.949   1.00 16.35 ?  238 LEU A CB    1 
ATOM   1741 C CG    . LEU A 1 232 ? 23.426 0.752   1.905   1.00 17.74 ?  238 LEU A CG    1 
ATOM   1742 C CD1   . LEU A 1 232 ? 24.948 0.915   1.839   1.00 18.87 ?  238 LEU A CD1   1 
ATOM   1743 C CD2   . LEU A 1 232 ? 22.766 2.045   1.547   1.00 18.42 ?  238 LEU A CD2   1 
ATOM   1744 N N     . VAL A 1 233 ? 23.629 -2.206  3.647   1.00 18.49 ?  239 VAL A N     1 
ATOM   1745 C CA    . VAL A 1 233 ? 23.201 -2.494  5.012   1.00 19.15 ?  239 VAL A CA    1 
ATOM   1746 C C     . VAL A 1 233 ? 23.494 -1.277  5.875   1.00 19.71 ?  239 VAL A C     1 
ATOM   1747 O O     . VAL A 1 233 ? 24.641 -0.812  5.934   1.00 19.21 ?  239 VAL A O     1 
ATOM   1748 C CB    . VAL A 1 233 ? 23.902 -3.730  5.590   1.00 20.46 ?  239 VAL A CB    1 
ATOM   1749 C CG1   . VAL A 1 233 ? 23.398 -3.980  7.000   1.00 21.26 ?  239 VAL A CG1   1 
ATOM   1750 C CG2   . VAL A 1 233 ? 23.699 -4.957  4.680   1.00 20.74 ?  239 VAL A CG2   1 
ATOM   1751 N N     . ILE A 1 234 ? 22.460 -0.775  6.555   1.00 18.81 ?  240 ILE A N     1 
ATOM   1752 C CA    . ILE A 1 234 ? 22.583 0.339   7.487   1.00 19.69 ?  240 ILE A CA    1 
ATOM   1753 C C     . ILE A 1 234 ? 22.214 -0.139  8.881   1.00 19.77 ?  240 ILE A C     1 
ATOM   1754 O O     . ILE A 1 234 ? 21.153 -0.737  9.077   1.00 19.99 ?  240 ILE A O     1 
ATOM   1755 C CB    . ILE A 1 234 ? 21.692 1.518   7.084   1.00 19.15 ?  240 ILE A CB    1 
ATOM   1756 C CG1   . ILE A 1 234 ? 22.042 1.958   5.659   1.00 19.96 ?  240 ILE A CG1   1 
ATOM   1757 C CG2   . ILE A 1 234 ? 21.827 2.637   8.117   1.00 18.92 ?  240 ILE A CG2   1 
ATOM   1758 C CD1   . ILE A 1 234 ? 21.107 3.042   5.117   1.00 19.28 ?  240 ILE A CD1   1 
ATOM   1759 N N     . LEU A 1 235 ? 23.076 0.154   9.847   1.00 20.47 ?  241 LEU A N     1 
ATOM   1760 C CA    . LEU A 1 235 ? 22.884 -0.275  11.229  1.00 22.23 ?  241 LEU A CA    1 
ATOM   1761 C C     . LEU A 1 235 ? 22.244 0.838   12.055  1.00 24.02 ?  241 LEU A C     1 
ATOM   1762 O O     . LEU A 1 235 ? 22.820 1.923   12.199  1.00 21.18 ?  241 LEU A O     1 
ATOM   1763 C CB    . LEU A 1 235 ? 24.216 -0.671  11.855  1.00 24.79 ?  241 LEU A CB    1 
ATOM   1764 C CG    . LEU A 1 235 ? 24.991 -1.851  11.289  1.00 23.62 ?  241 LEU A CG    1 
ATOM   1765 C CD1   . LEU A 1 235 ? 25.899 -2.386  12.387  1.00 26.54 ?  241 LEU A CD1   1 
ATOM   1766 C CD2   . LEU A 1 235 ? 24.061 -2.932  10.833  1.00 26.45 ?  241 LEU A CD2   1 
ATOM   1767 N N     . CYS A 1 236 ? 21.059 0.566   12.604  1.00 24.02 ?  242 CYS A N     1 
ATOM   1768 C CA    . CYS A 1 236 ? 20.494 1.418   13.642  1.00 22.10 ?  242 CYS A CA    1 
ATOM   1769 C C     . CYS A 1 236 ? 20.242 0.597   14.898  1.00 23.57 ?  242 CYS A C     1 
ATOM   1770 O O     . CYS A 1 236 ? 19.117 0.526   15.398  1.00 23.98 ?  242 CYS A O     1 
ATOM   1771 C CB    . CYS A 1 236 ? 19.212 2.065   13.156  1.00 22.47 ?  242 CYS A CB    1 
ATOM   1772 S SG    . CYS A 1 236 ? 19.459 3.073   11.695  1.00 23.62 ?  242 CYS A SG    1 
ATOM   1773 N N     . THR A 1 237 ? 21.296 -0.009  15.423  1.00 24.53 ?  243 THR A N     1 
ATOM   1774 C CA    . THR A 1 237 ? 21.178 -1.097  16.381  1.00 26.10 ?  243 THR A CA    1 
ATOM   1775 C C     . THR A 1 237 ? 21.268 -0.642  17.825  1.00 27.23 ?  243 THR A C     1 
ATOM   1776 O O     . THR A 1 237 ? 21.151 -1.479  18.719  1.00 28.95 ?  243 THR A O     1 
ATOM   1777 C CB    . THR A 1 237 ? 22.262 -2.142  16.103  1.00 26.76 ?  243 THR A CB    1 
ATOM   1778 O OG1   . THR A 1 237 ? 23.512 -1.462  15.931  1.00 31.20 ?  243 THR A OG1   1 
ATOM   1779 C CG2   . THR A 1 237 ? 21.954 -2.928  14.835  1.00 27.42 ?  243 THR A CG2   1 
ATOM   1780 N N     . GLY A 1 238 ? 21.485 0.643   18.085  1.00 26.71 ?  244 GLY A N     1 
ATOM   1781 C CA    . GLY A 1 238 ? 21.433 1.158   19.432  1.00 27.78 ?  244 GLY A CA    1 
ATOM   1782 C C     . GLY A 1 238 ? 22.667 1.957   19.780  1.00 29.16 ?  244 GLY A C     1 
ATOM   1783 O O     . GLY A 1 238 ? 23.640 2.025   19.034  1.00 27.90 ?  244 GLY A O     1 
ATOM   1784 N N     . ILE A 1 239 ? 22.617 2.576   20.956  1.00 30.12 ?  245 ILE A N     1 
ATOM   1785 C CA    . ILE A 1 239 ? 23.670 3.477   21.383  1.00 29.08 ?  245 ILE A CA    1 
ATOM   1786 C C     . ILE A 1 239 ? 24.061 3.119   22.810  1.00 31.02 ?  245 ILE A C     1 
ATOM   1787 O O     . ILE A 1 239 ? 23.379 2.345   23.484  1.00 32.04 ?  245 ILE A O     1 
ATOM   1788 C CB    . ILE A 1 239 ? 23.243 4.957   21.257  1.00 30.51 ?  245 ILE A CB    1 
ATOM   1789 C CG1   . ILE A 1 239 ? 22.029 5.263   22.129  1.00 33.62 ?  245 ILE A CG1   1 
ATOM   1790 C CG2   . ILE A 1 239 ? 22.949 5.317   19.783  1.00 27.38 ?  245 ILE A CG2   1 
ATOM   1791 C CD1   . ILE A 1 239 ? 21.597 6.729   22.054  1.00 34.22 ?  245 ILE A CD1   1 
ATOM   1792 N N     . LYS A 1 240 ? 25.211 3.643   23.237  1.00 31.59 ?  246 LYS A N     1 
ATOM   1793 C CA    . LYS A 1 240 ? 25.751 3.445   24.574  1.00 33.50 ?  246 LYS A CA    1 
ATOM   1794 C C     . LYS A 1 240 ? 26.211 4.794   25.092  1.00 33.59 ?  246 LYS A C     1 
ATOM   1795 O O     . LYS A 1 240 ? 26.734 5.609   24.323  1.00 32.50 ?  246 LYS A O     1 
ATOM   1796 C CB    . LYS A 1 240 ? 26.937 2.461   24.597  1.00 34.63 ?  246 LYS A CB    1 
ATOM   1797 C CG    . LYS A 1 240 ? 26.536 1.005   24.566  1.00 44.27 ?  246 LYS A CG    1 
ATOM   1798 C CD    . LYS A 1 240 ? 27.722 0.063   24.734  1.00 50.81 ?  246 LYS A CD    1 
ATOM   1799 C CE    . LYS A 1 240 ? 28.406 0.235   26.086  1.00 52.91 ?  246 LYS A CE    1 
ATOM   1800 N NZ    . LYS A 1 240 ? 29.420 -0.838  26.370  1.00 56.47 ?  246 LYS A NZ    1 
ATOM   1801 N N     . ILE A 1 241 ? 26.005 5.028   26.393  1.00 38.16 ?  247 ILE A N     1 
ATOM   1802 C CA    . ILE A 1 241 ? 26.544 6.228   27.019  1.00 35.92 ?  247 ILE A CA    1 
ATOM   1803 C C     . ILE A 1 241 ? 28.040 6.271   26.782  1.00 35.83 ?  247 ILE A C     1 
ATOM   1804 O O     . ILE A 1 241 ? 28.739 5.254   26.875  1.00 36.83 ?  247 ILE A O     1 
ATOM   1805 C CB    . ILE A 1 241 ? 26.236 6.272   28.524  1.00 38.65 ?  247 ILE A CB    1 
ATOM   1806 C CG1   . ILE A 1 241 ? 24.740 6.152   28.765  1.00 41.93 ?  247 ILE A CG1   1 
ATOM   1807 C CG2   . ILE A 1 241 ? 26.733 7.570   29.106  1.00 38.70 ?  247 ILE A CG2   1 
ATOM   1808 C CD1   . ILE A 1 241 ? 23.952 7.195   28.063  1.00 35.46 ?  247 ILE A CD1   1 
ATOM   1809 N N     . ASN A 1 242 ? 28.535 7.455   26.444  1.00 35.15 ?  248 ASN A N     1 
ATOM   1810 C CA    . ASN A 1 242 ? 29.949 7.629   26.153  1.00 35.56 ?  248 ASN A CA    1 
ATOM   1811 C C     . ASN A 1 242 ? 30.644 8.040   27.450  1.00 39.73 ?  248 ASN A C     1 
ATOM   1812 O O     . ASN A 1 242 ? 30.922 9.214   27.716  1.00 42.38 ?  248 ASN A O     1 
ATOM   1813 C CB    . ASN A 1 242 ? 30.117 8.639   25.027  1.00 33.96 ?  248 ASN A CB    1 
ATOM   1814 C CG    . ASN A 1 242 ? 31.519 8.705   24.523  1.00 34.33 ?  248 ASN A CG    1 
ATOM   1815 O OD1   . ASN A 1 242 ? 32.458 8.354   25.234  1.00 42.25 ?  248 ASN A OD1   1 
ATOM   1816 N ND2   . ASN A 1 242 ? 31.682 9.171   23.290  1.00 35.42 ?  248 ASN A ND2   1 
ATOM   1817 N N     . SER A 1 243 ? 30.900 7.034   28.289  1.00 39.98 ?  249 SER A N     1 
ATOM   1818 C CA    . SER A 1 243 ? 31.582 7.178   29.570  1.00 43.16 ?  249 SER A CA    1 
ATOM   1819 C C     . SER A 1 243 ? 33.088 7.251   29.420  1.00 43.81 ?  249 SER A C     1 
ATOM   1820 O O     . SER A 1 243 ? 33.797 7.130   30.416  1.00 44.74 ?  249 SER A O     1 
ATOM   1821 C CB    . SER A 1 243 ? 31.222 6.011   30.491  1.00 44.61 ?  249 SER A CB    1 
ATOM   1822 O OG    . SER A 1 243 ? 31.746 4.784   29.987  1.00 43.24 ?  249 SER A OG    1 
ATOM   1823 N N     . SER A 1 244 ? 33.578 7.454   28.198  1.00 41.91 ?  250 SER A N     1 
ATOM   1824 C CA    . SER A 1 244 ? 35.009 7.419   27.928  1.00 41.83 ?  250 SER A CA    1 
ATOM   1825 C C     . SER A 1 244 ? 35.777 8.361   28.852  1.00 45.81 ?  250 SER A C     1 
ATOM   1826 O O     . SER A 1 244 ? 36.698 7.946   29.565  1.00 45.38 ?  250 SER A O     1 
ATOM   1827 C CB    . SER A 1 244 ? 35.227 7.765   26.449  1.00 42.72 ?  250 SER A CB    1 
ATOM   1828 O OG    . SER A 1 244 ? 36.562 8.131   26.158  1.00 50.03 ?  250 SER A OG    1 
ATOM   1829 N N     . ALA A 1 245 ? 35.372 9.635   28.883  1.00 45.63 ?  251 ALA A N     1 
ATOM   1830 C CA    . ALA A 1 245 ? 36.167 10.668  29.547  1.00 43.79 ?  251 ALA A CA    1 
ATOM   1831 C C     . ALA A 1 245 ? 36.232 10.493  31.058  1.00 46.04 ?  251 ALA A C     1 
ATOM   1832 O O     . ALA A 1 245 ? 37.204 10.927  31.684  1.00 47.61 ?  251 ALA A O     1 
ATOM   1833 C CB    . ALA A 1 245 ? 35.599 12.050  29.227  1.00 42.44 ?  251 ALA A CB    1 
ATOM   1834 N N     . TYR A 1 246 ? 35.214 9.901   31.670  1.00 46.97 ?  252 TYR A N     1 
ATOM   1835 C CA    . TYR A 1 246 ? 35.102 9.946   33.119  1.00 48.32 ?  252 TYR A CA    1 
ATOM   1836 C C     . TYR A 1 246 ? 35.033 8.580   33.789  1.00 50.52 ?  252 TYR A C     1 
ATOM   1837 O O     . TYR A 1 246 ? 34.982 8.526   35.026  1.00 51.34 ?  252 TYR A O     1 
ATOM   1838 C CB    . TYR A 1 246 ? 33.872 10.778  33.517  1.00 47.14 ?  252 TYR A CB    1 
ATOM   1839 C CG    . TYR A 1 246 ? 32.548 10.263  32.974  1.00 45.48 ?  252 TYR A CG    1 
ATOM   1840 C CD1   . TYR A 1 246 ? 31.870 9.229   33.614  1.00 47.36 ?  252 TYR A CD1   1 
ATOM   1841 C CD2   . TYR A 1 246 ? 31.962 10.827  31.841  1.00 43.22 ?  252 TYR A CD2   1 
ATOM   1842 C CE1   . TYR A 1 246 ? 30.671 8.757   33.140  1.00 45.01 ?  252 TYR A CE1   1 
ATOM   1843 C CE2   . TYR A 1 246 ? 30.750 10.350  31.351  1.00 41.86 ?  252 TYR A CE2   1 
ATOM   1844 C CZ    . TYR A 1 246 ? 30.111 9.316   32.013  1.00 45.29 ?  252 TYR A CZ    1 
ATOM   1845 O OH    . TYR A 1 246 ? 28.908 8.829   31.569  1.00 41.82 ?  252 TYR A OH    1 
ATOM   1846 N N     . ARG A 1 247 ? 35.063 7.484   33.021  1.00 49.92 ?  253 ARG A N     1 
ATOM   1847 C CA    . ARG A 1 247 ? 34.709 6.165   33.552  1.00 50.52 ?  253 ARG A CA    1 
ATOM   1848 C C     . ARG A 1 247 ? 35.514 5.823   34.797  1.00 54.02 ?  253 ARG A C     1 
ATOM   1849 O O     . ARG A 1 247 ? 34.946 5.497   35.847  1.00 54.52 ?  253 ARG A O     1 
ATOM   1850 C CB    . ARG A 1 247 ? 34.902 5.094   32.473  1.00 49.27 ?  253 ARG A CB    1 
ATOM   1851 C CG    . ARG A 1 247 ? 34.268 3.741   32.794  1.00 51.37 ?  253 ARG A CG    1 
ATOM   1852 N N     . LYS A 1 248 ? 36.842 5.912   34.710  1.00 54.08 ?  254 LYS A N     1 
ATOM   1853 C CA    . LYS A 1 248 ? 37.661 5.497   35.839  1.00 57.00 ?  254 LYS A CA    1 
ATOM   1854 C C     . LYS A 1 248 ? 37.465 6.423   37.037  1.00 59.84 ?  254 LYS A C     1 
ATOM   1855 O O     . LYS A 1 248 ? 37.307 5.956   38.172  1.00 60.22 ?  254 LYS A O     1 
ATOM   1856 C CB    . LYS A 1 248 ? 39.135 5.444   35.435  1.00 59.00 ?  254 LYS A CB    1 
ATOM   1857 C CG    . LYS A 1 248 ? 39.975 4.613   36.392  1.00 63.88 ?  254 LYS A CG    1 
ATOM   1858 C CD    . LYS A 1 248 ? 41.467 4.698   36.103  1.00 64.81 ?  254 LYS A CD    1 
ATOM   1859 C CE    . LYS A 1 248 ? 42.174 3.349   36.327  1.00 64.78 ?  254 LYS A CE    1 
ATOM   1860 N NZ    . LYS A 1 248 ? 42.135 2.841   37.742  1.00 72.51 ?  254 LYS A NZ    1 
ATOM   1861 N N     . ALA A 1 249 ? 37.438 7.736   36.795  1.00 56.97 ?  255 ALA A N     1 
ATOM   1862 C CA    . ALA A 1 249 ? 37.403 8.697   37.889  1.00 58.22 ?  255 ALA A CA    1 
ATOM   1863 C C     . ALA A 1 249 ? 36.127 8.585   38.712  1.00 58.39 ?  255 ALA A C     1 
ATOM   1864 O O     . ALA A 1 249 ? 36.159 8.795   39.929  1.00 61.21 ?  255 ALA A O     1 
ATOM   1865 C CB    . ALA A 1 249 ? 37.556 10.112  37.336  1.00 56.78 ?  255 ALA A CB    1 
ATOM   1866 N N     . PHE A 1 250 ? 35.002 8.255   38.084  1.00 56.46 ?  256 PHE A N     1 
ATOM   1867 C CA    . PHE A 1 250 ? 33.710 8.307   38.757  1.00 56.47 ?  256 PHE A CA    1 
ATOM   1868 C C     . PHE A 1 250 ? 33.043 6.941   38.850  1.00 56.88 ?  256 PHE A C     1 
ATOM   1869 O O     . PHE A 1 250 ? 31.815 6.863   38.952  1.00 56.78 ?  256 PHE A O     1 
ATOM   1870 C CB    . PHE A 1 250 ? 32.772 9.284   38.053  1.00 54.03 ?  256 PHE A CB    1 
ATOM   1871 C CG    . PHE A 1 250 ? 33.202 10.711  38.145  1.00 53.86 ?  256 PHE A CG    1 
ATOM   1872 C CD1   . PHE A 1 250 ? 34.101 11.235  37.233  1.00 52.89 ?  256 PHE A CD1   1 
ATOM   1873 C CD2   . PHE A 1 250 ? 32.691 11.538  39.137  1.00 54.80 ?  256 PHE A CD2   1 
ATOM   1874 C CE1   . PHE A 1 250 ? 34.495 12.562  37.312  1.00 52.97 ?  256 PHE A CE1   1 
ATOM   1875 C CE2   . PHE A 1 250 ? 33.078 12.864  39.222  1.00 54.75 ?  256 PHE A CE2   1 
ATOM   1876 C CZ    . PHE A 1 250 ? 33.980 13.378  38.304  1.00 53.79 ?  256 PHE A CZ    1 
ATOM   1877 N N     . GLU A 1 251 ? 33.829 5.858   38.823  1.00 56.10 ?  257 GLU A N     1 
ATOM   1878 C CA    . GLU A 1 251 ? 33.238 4.521   38.816  1.00 53.78 ?  257 GLU A CA    1 
ATOM   1879 C C     . GLU A 1 251 ? 32.288 4.321   39.993  1.00 59.22 ?  257 GLU A C     1 
ATOM   1880 O O     . GLU A 1 251 ? 31.281 3.616   39.861  1.00 59.45 ?  257 GLU A O     1 
ATOM   1881 C CB    . GLU A 1 251 ? 34.339 3.457   38.822  1.00 53.99 ?  257 GLU A CB    1 
ATOM   1882 C CG    . GLU A 1 251 ? 33.858 2.051   38.472  1.00 55.26 ?  257 GLU A CG    1 
ATOM   1883 N N     . SER A 1 252 ? 32.566 4.971   41.132  1.00 57.45 ?  258 SER A N     1 
ATOM   1884 C CA    . SER A 1 252 ? 31.706 4.844   42.307  1.00 57.71 ?  258 SER A CA    1 
ATOM   1885 C C     . SER A 1 252 ? 30.280 5.310   42.026  1.00 60.08 ?  258 SER A C     1 
ATOM   1886 O O     . SER A 1 252 ? 29.315 4.668   42.454  1.00 60.45 ?  258 SER A O     1 
ATOM   1887 C CB    . SER A 1 252 ? 32.292 5.641   43.467  1.00 59.48 ?  258 SER A CB    1 
ATOM   1888 O OG    . SER A 1 252 ? 31.391 5.690   44.558  1.00 66.66 ?  258 SER A OG    1 
ATOM   1889 N N     . ARG A 1 253 ? 30.122 6.419   41.303  1.00 59.59 ?  259 ARG A N     1 
ATOM   1890 C CA    . ARG A 1 253 ? 28.836 7.100   41.198  1.00 58.50 ?  259 ARG A CA    1 
ATOM   1891 C C     . ARG A 1 253 ? 28.164 6.895   39.841  1.00 56.43 ?  259 ARG A C     1 
ATOM   1892 O O     . ARG A 1 253 ? 27.351 7.723   39.422  1.00 52.99 ?  259 ARG A O     1 
ATOM   1893 C CB    . ARG A 1 253 ? 29.011 8.591   41.493  1.00 57.26 ?  259 ARG A CB    1 
ATOM   1894 N N     . LEU A 1 254 ? 28.464 5.783   39.163  1.00 57.55 ?  260 LEU A N     1 
ATOM   1895 C CA    . LEU A 1 254 ? 27.899 5.487   37.851  1.00 56.28 ?  260 LEU A CA    1 
ATOM   1896 C C     . LEU A 1 254 ? 26.660 4.622   37.983  1.00 56.78 ?  260 LEU A C     1 
ATOM   1897 O O     . LEU A 1 254 ? 26.617 3.696   38.797  1.00 58.10 ?  260 LEU A O     1 
ATOM   1898 C CB    . LEU A 1 254 ? 28.912 4.770   36.961  1.00 51.48 ?  260 LEU A CB    1 
ATOM   1899 C CG    . LEU A 1 254 ? 30.106 5.624   36.550  1.00 55.10 ?  260 LEU A CG    1 
ATOM   1900 C CD1   . LEU A 1 254 ? 30.977 4.886   35.546  1.00 55.72 ?  260 LEU A CD1   1 
ATOM   1901 C CD2   . LEU A 1 254 ? 29.630 6.959   35.990  1.00 54.17 ?  260 LEU A CD2   1 
ATOM   1902 N N     . ALA A 1 255 ? 25.653 4.926   37.177  1.00 52.32 ?  261 ALA A N     1 
ATOM   1903 C CA    . ALA A 1 255 ? 24.491 4.058   37.132  1.00 57.68 ?  261 ALA A CA    1 
ATOM   1904 C C     . ALA A 1 255 ? 24.836 2.794   36.352  1.00 59.66 ?  261 ALA A C     1 
ATOM   1905 O O     . ALA A 1 255 ? 25.938 2.641   35.809  1.00 57.99 ?  261 ALA A O     1 
ATOM   1906 C CB    . ALA A 1 255 ? 23.299 4.782   36.511  1.00 50.95 ?  261 ALA A CB    1 
ATOM   1907 N N     . SER A 1 256 ? 23.889 1.857   36.305  1.00 59.19 ?  262 SER A N     1 
ATOM   1908 C CA    . SER A 1 256 ? 24.007 0.790   35.322  1.00 58.13 ?  262 SER A CA    1 
ATOM   1909 C C     . SER A 1 256 ? 24.127 1.383   33.918  1.00 59.47 ?  262 SER A C     1 
ATOM   1910 O O     . SER A 1 256 ? 25.049 1.041   33.171  1.00 59.21 ?  262 SER A O     1 
ATOM   1911 C CB    . SER A 1 256 ? 22.822 -0.174  35.431  1.00 57.70 ?  262 SER A CB    1 
ATOM   1912 O OG    . SER A 1 256 ? 21.587 0.482   35.202  1.00 63.14 ?  262 SER A OG    1 
ATOM   1913 N N     . SER A 1 257 ? 23.259 2.353   33.584  1.00 58.19 ?  263 SER A N     1 
ATOM   1914 C CA    . SER A 1 257 ? 23.251 2.982   32.257  1.00 55.42 ?  263 SER A CA    1 
ATOM   1915 C C     . SER A 1 257 ? 24.636 3.379   31.751  1.00 48.33 ?  263 SER A C     1 
ATOM   1916 O O     . SER A 1 257 ? 24.832 3.490   30.537  1.00 51.04 ?  263 SER A O     1 
ATOM   1917 C CB    . SER A 1 257 ? 22.359 4.236   32.272  1.00 53.35 ?  263 SER A CB    1 
ATOM   1918 N N     . GLY A 1 258 ? 25.605 3.571   32.642  1.00 49.88 ?  264 GLY A N     1 
ATOM   1919 C CA    . GLY A 1 258 ? 26.845 4.238   32.310  1.00 49.09 ?  264 GLY A CA    1 
ATOM   1920 C C     . GLY A 1 258 ? 26.803 5.721   32.586  1.00 46.37 ?  264 GLY A C     1 
ATOM   1921 O O     . GLY A 1 258 ? 27.852 6.384   32.555  1.00 42.56 ?  264 GLY A O     1 
ATOM   1922 N N     . ALA A 1 259 ? 25.617 6.246   32.872  1.00 47.37 ?  265 ALA A N     1 
ATOM   1923 C CA    . ALA A 1 259 ? 25.420 7.634   33.226  1.00 44.11 ?  265 ALA A CA    1 
ATOM   1924 C C     . ALA A 1 259 ? 25.932 7.903   34.640  1.00 47.66 ?  265 ALA A C     1 
ATOM   1925 O O     . ALA A 1 259 ? 26.277 6.990   35.400  1.00 47.86 ?  265 ALA A O     1 
ATOM   1926 C CB    . ALA A 1 259 ? 23.939 7.991   33.114  1.00 44.58 ?  265 ALA A CB    1 
ATOM   1927 N N     . LEU A 1 260 ? 25.988 9.182   34.989  1.00 44.05 ?  266 LEU A N     1 
ATOM   1928 C CA    . LEU A 1 260 ? 26.387 9.606   36.321  1.00 43.28 ?  266 LEU A CA    1 
ATOM   1929 C C     . LEU A 1 260 ? 25.134 9.900   37.134  1.00 43.85 ?  266 LEU A C     1 
ATOM   1930 O O     . LEU A 1 260 ? 24.216 10.572  36.647  1.00 42.92 ?  266 LEU A O     1 
ATOM   1931 C CB    . LEU A 1 260 ? 27.289 10.838  36.248  1.00 42.34 ?  266 LEU A CB    1 
ATOM   1932 C CG    . LEU A 1 260 ? 28.624 10.711  35.503  1.00 42.53 ?  266 LEU A CG    1 
ATOM   1933 C CD1   . LEU A 1 260 ? 28.751 11.779  34.447  1.00 40.18 ?  266 LEU A CD1   1 
ATOM   1934 C CD2   . LEU A 1 260 ? 29.779 10.834  36.467  1.00 45.43 ?  266 LEU A CD2   1 
ATOM   1935 N N     . ARG A 1 261 ? 25.085 9.385   38.363  1.00 45.51 ?  267 ARG A N     1 
ATOM   1936 C CA    . ARG A 1 261 ? 23.977 9.729   39.238  1.00 46.24 ?  267 ARG A CA    1 
ATOM   1937 C C     . ARG A 1 261 ? 24.110 11.176  39.690  1.00 45.64 ?  267 ARG A C     1 
ATOM   1938 O O     . ARG A 1 261 ? 25.212 11.701  39.864  1.00 45.37 ?  267 ARG A O     1 
ATOM   1939 C CB    . ARG A 1 261 ? 23.919 8.805   40.448  1.00 48.43 ?  267 ARG A CB    1 
ATOM   1940 C CG    . ARG A 1 261 ? 23.657 7.353   40.110  1.00 52.50 ?  267 ARG A CG    1 
ATOM   1941 C CD    . ARG A 1 261 ? 23.480 6.538   41.394  1.00 57.26 ?  267 ARG A CD    1 
ATOM   1942 N NE    . ARG A 1 261 ? 24.072 5.209   41.290  1.00 64.53 ?  267 ARG A NE    1 
ATOM   1943 C CZ    . ARG A 1 261 ? 25.240 4.865   41.820  1.00 65.14 ?  267 ARG A CZ    1 
ATOM   1944 N NH1   . ARG A 1 261 ? 25.968 5.728   42.515  1.00 57.98 ?  267 ARG A NH1   1 
ATOM   1945 N NH2   . ARG A 1 261 ? 25.689 3.621   41.646  1.00 66.66 ?  267 ARG A NH2   1 
ATOM   1946 N N     . VAL A 1 262 ? 22.965 11.823  39.867  1.00 45.49 ?  268 VAL A N     1 
ATOM   1947 C CA    . VAL A 1 262 ? 22.891 13.252  40.133  1.00 47.70 ?  268 VAL A CA    1 
ATOM   1948 C C     . VAL A 1 262 ? 21.640 13.485  40.964  1.00 47.45 ?  268 VAL A C     1 
ATOM   1949 O O     . VAL A 1 262 ? 20.693 12.693  40.932  1.00 46.50 ?  268 VAL A O     1 
ATOM   1950 C CB    . VAL A 1 262 ? 22.828 14.080  38.823  1.00 44.65 ?  268 VAL A CB    1 
ATOM   1951 C CG1   . VAL A 1 262 ? 24.158 14.073  38.089  1.00 41.98 ?  268 VAL A CG1   1 
ATOM   1952 C CG2   . VAL A 1 262 ? 21.746 13.518  37.925  1.00 42.50 ?  268 VAL A CG2   1 
ATOM   1953 N N     . ASN A 1 263 ? 21.642 14.578  41.724  1.00 45.93 ?  269 ASN A N     1 
ATOM   1954 C CA    . ASN A 1 263 ? 20.456 15.003  42.452  1.00 46.79 ?  269 ASN A CA    1 
ATOM   1955 C C     . ASN A 1 263 ? 19.601 15.848  41.506  1.00 47.12 ?  269 ASN A C     1 
ATOM   1956 O O     . ASN A 1 263 ? 19.909 15.973  40.313  1.00 43.94 ?  269 ASN A O     1 
ATOM   1957 C CB    . ASN A 1 263 ? 20.852 15.734  43.743  1.00 47.86 ?  269 ASN A CB    1 
ATOM   1958 C CG    . ASN A 1 263 ? 21.482 17.086  43.481  1.00 46.89 ?  269 ASN A CG    1 
ATOM   1959 O OD1   . ASN A 1 263 ? 21.439 17.585  42.362  1.00 44.88 ?  269 ASN A OD1   1 
ATOM   1960 N ND2   . ASN A 1 263 ? 22.090 17.684  44.509  1.00 47.19 ?  269 ASN A ND2   1 
ATOM   1961 N N     . GLU A 1 264 ? 18.539 16.472  42.030  1.00 46.00 ?  270 GLU A N     1 
ATOM   1962 C CA    . GLU A 1 264 ? 17.668 17.283  41.181  1.00 46.31 ?  270 GLU A CA    1 
ATOM   1963 C C     . GLU A 1 264 ? 18.319 18.592  40.731  1.00 46.34 ?  270 GLU A C     1 
ATOM   1964 O O     . GLU A 1 264 ? 17.740 19.292  39.890  1.00 44.20 ?  270 GLU A O     1 
ATOM   1965 C CB    . GLU A 1 264 ? 16.334 17.560  41.899  1.00 46.14 ?  270 GLU A CB    1 
ATOM   1966 C CG    . GLU A 1 264 ? 16.430 18.431  43.146  1.00 50.66 ?  270 GLU A CG    1 
ATOM   1967 C CD    . GLU A 1 264 ? 16.710 17.631  44.421  1.00 53.25 ?  270 GLU A CD    1 
ATOM   1968 O OE1   . GLU A 1 264 ? 17.027 16.415  44.323  1.00 51.36 ?  270 GLU A OE1   1 
ATOM   1969 O OE2   . GLU A 1 264 ? 16.603 18.228  45.521  1.00 56.42 -1 270 GLU A OE2   1 
ATOM   1970 N N     . HIS A 1 265 ? 19.498 18.931  41.266  1.00 43.50 ?  271 HIS A N     1 
ATOM   1971 C CA    . HIS A 1 265 ? 20.290 20.069  40.816  1.00 43.29 ?  271 HIS A CA    1 
ATOM   1972 C C     . HIS A 1 265 ? 21.362 19.686  39.795  1.00 41.65 ?  271 HIS A C     1 
ATOM   1973 O O     . HIS A 1 265 ? 22.124 20.559  39.370  1.00 40.06 ?  271 HIS A O     1 
ATOM   1974 C CB    . HIS A 1 265 ? 20.964 20.754  42.015  1.00 43.94 ?  271 HIS A CB    1 
ATOM   1975 C CG    . HIS A 1 265 ? 20.074 20.927  43.204  1.00 45.38 ?  271 HIS A CG    1 
ATOM   1976 N ND1   . HIS A 1 265 ? 18.890 21.630  43.157  1.00 46.98 ?  271 HIS A ND1   1 
ATOM   1977 C CD2   . HIS A 1 265 ? 20.217 20.512  44.485  1.00 48.41 ?  271 HIS A CD2   1 
ATOM   1978 C CE1   . HIS A 1 265 ? 18.335 21.628  44.359  1.00 48.89 ?  271 HIS A CE1   1 
ATOM   1979 N NE2   . HIS A 1 265 ? 19.120 20.958  45.182  1.00 47.12 ?  271 HIS A NE2   1 
ATOM   1980 N N     . LEU A 1 266 ? 21.464 18.405  39.428  1.00 41.29 ?  272 LEU A N     1 
ATOM   1981 C CA    . LEU A 1 266 ? 22.375 17.891  38.401  1.00 43.67 ?  272 LEU A CA    1 
ATOM   1982 C C     . LEU A 1 266 ? 23.848 17.871  38.824  1.00 40.56 ?  272 LEU A C     1 
ATOM   1983 O O     . LEU A 1 266 ? 24.723 17.668  37.975  1.00 39.72 ?  272 LEU A O     1 
ATOM   1984 C CB    . LEU A 1 266 ? 22.214 18.657  37.086  1.00 38.75 ?  272 LEU A CB    1 
ATOM   1985 C CG    . LEU A 1 266 ? 20.819 18.538  36.466  1.00 38.55 ?  272 LEU A CG    1 
ATOM   1986 C CD1   . LEU A 1 266 ? 20.772 19.404  35.250  1.00 37.11 ?  272 LEU A CD1   1 
ATOM   1987 C CD2   . LEU A 1 266 ? 20.493 17.081  36.121  1.00 39.02 ?  272 LEU A CD2   1 
ATOM   1988 N N     . GLN A 1 267 ? 24.141 18.039  40.118  1.00 41.71 ?  273 GLN A N     1 
ATOM   1989 C CA    . GLN A 1 267 ? 25.487 17.825  40.631  1.00 42.23 ?  273 GLN A CA    1 
ATOM   1990 C C     . GLN A 1 267 ? 25.727 16.331  40.685  1.00 43.14 ?  273 GLN A C     1 
ATOM   1991 O O     . GLN A 1 267 ? 24.821 15.589  41.069  1.00 44.07 ?  273 GLN A O     1 
ATOM   1992 C CB    . GLN A 1 267 ? 25.617 18.421  42.029  1.00 45.06 ?  273 GLN A CB    1 
ATOM   1993 C CG    . GLN A 1 267 ? 25.158 19.905  42.086  1.00 42.68 ?  273 GLN A CG    1 
ATOM   1994 C CD    . GLN A 1 267 ? 24.982 20.412  43.526  1.00 46.57 ?  273 GLN A CD    1 
ATOM   1995 O OE1   . GLN A 1 267 ? 24.081 19.968  44.248  1.00 45.20 ?  273 GLN A OE1   1 
ATOM   1996 N NE2   . GLN A 1 267 ? 25.851 21.334  43.949  1.00 43.93 ?  273 GLN A NE2   1 
ATOM   1997 N N     . VAL A 1 268 ? 26.945 15.880  40.372  1.00 43.05 ?  274 VAL A N     1 
ATOM   1998 C CA    . VAL A 1 268 ? 27.186 14.441  40.430  1.00 44.04 ?  274 VAL A CA    1 
ATOM   1999 C C     . VAL A 1 268 ? 27.273 14.027  41.889  1.00 47.55 ?  274 VAL A C     1 
ATOM   2000 O O     . VAL A 1 268 ? 27.756 14.793  42.732  1.00 46.38 ?  274 VAL A O     1 
ATOM   2001 C CB    . VAL A 1 268 ? 28.448 14.048  39.647  1.00 43.54 ?  274 VAL A CB    1 
ATOM   2002 C CG1   . VAL A 1 268 ? 28.757 12.545  39.866  1.00 44.85 ?  274 VAL A CG1   1 
ATOM   2003 C CG2   . VAL A 1 268 ? 28.234 14.320  38.134  1.00 41.82 ?  274 VAL A CG2   1 
ATOM   2004 N N     . GLU A 1 269 ? 26.738 12.841  42.201  1.00 48.65 ?  275 GLU A N     1 
ATOM   2005 C CA    . GLU A 1 269 ? 26.696 12.353  43.576  1.00 49.37 ?  275 GLU A CA    1 
ATOM   2006 C C     . GLU A 1 269 ? 28.082 12.358  44.205  1.00 52.18 ?  275 GLU A C     1 
ATOM   2007 O O     . GLU A 1 269 ? 29.055 11.882  43.609  1.00 54.36 ?  275 GLU A O     1 
ATOM   2008 C CB    . GLU A 1 269 ? 26.108 10.937  43.627  1.00 51.63 ?  275 GLU A CB    1 
ATOM   2009 C CG    . GLU A 1 269 ? 26.840 9.976   44.590  1.00 56.08 ?  275 GLU A CG    1 
ATOM   2010 C CD    . GLU A 1 269 ? 26.234 8.583   44.591  1.00 57.51 ?  275 GLU A CD    1 
ATOM   2011 O OE1   . GLU A 1 269 ? 25.056 8.456   44.194  1.00 53.55 ?  275 GLU A OE1   1 
ATOM   2012 O OE2   . GLU A 1 269 ? 26.931 7.623   44.981  1.00 56.28 -1 275 GLU A OE2   1 
ATOM   2013 N N     . GLY A 1 270 ? 28.158 12.889  45.429  1.00 53.03 ?  276 GLY A N     1 
ATOM   2014 C CA    . GLY A 1 270 ? 29.416 13.049  46.133  1.00 52.64 ?  276 GLY A CA    1 
ATOM   2015 C C     . GLY A 1 270 ? 30.208 14.286  45.759  1.00 51.99 ?  276 GLY A C     1 
ATOM   2016 O O     . GLY A 1 270 ? 31.278 14.523  46.341  1.00 51.33 ?  276 GLY A O     1 
ATOM   2017 N N     . HIS A 1 271 ? 29.691 15.114  44.857  1.00 49.08 ?  277 HIS A N     1 
ATOM   2018 C CA    . HIS A 1 271 ? 30.361 16.341  44.453  1.00 49.08 ?  277 HIS A CA    1 
ATOM   2019 C C     . HIS A 1 271 ? 29.349 17.480  44.459  1.00 50.29 ?  277 HIS A C     1 
ATOM   2020 O O     . HIS A 1 271 ? 28.147 17.266  44.267  1.00 51.89 ?  277 HIS A O     1 
ATOM   2021 C CB    . HIS A 1 271 ? 31.003 16.191  43.059  1.00 46.11 ?  277 HIS A CB    1 
ATOM   2022 C CG    . HIS A 1 271 ? 32.193 15.277  43.033  1.00 48.08 ?  277 HIS A CG    1 
ATOM   2023 N ND1   . HIS A 1 271 ? 32.094 13.919  42.808  1.00 50.00 ?  277 HIS A ND1   1 
ATOM   2024 C CD2   . HIS A 1 271 ? 33.510 15.530  43.219  1.00 50.37 ?  277 HIS A CD2   1 
ATOM   2025 C CE1   . HIS A 1 271 ? 33.303 13.381  42.838  1.00 48.83 ?  277 HIS A CE1   1 
ATOM   2026 N NE2   . HIS A 1 271 ? 34.177 14.336  43.089  1.00 48.18 ?  277 HIS A NE2   1 
ATOM   2027 N N     . SER A 1 272 ? 29.836 18.693  44.703  1.00 46.26 ?  278 SER A N     1 
ATOM   2028 C CA    . SER A 1 272 ? 29.006 19.872  44.559  1.00 45.34 ?  278 SER A CA    1 
ATOM   2029 C C     . SER A 1 272 ? 29.445 20.763  43.412  1.00 43.79 ?  278 SER A C     1 
ATOM   2030 O O     . SER A 1 272 ? 28.695 21.674  43.044  1.00 43.63 ?  278 SER A O     1 
ATOM   2031 C CB    . SER A 1 272 ? 29.001 20.680  45.859  1.00 46.40 ?  278 SER A CB    1 
ATOM   2032 O OG    . SER A 1 272 ? 30.320 21.026  46.233  1.00 48.65 ?  278 SER A OG    1 
ATOM   2033 N N     . ASN A 1 273 ? 30.622 20.520  42.831  1.00 43.18 ?  279 ASN A N     1 
ATOM   2034 C CA    . ASN A 1 273 ? 31.137 21.311  41.719  1.00 41.67 ?  279 ASN A CA    1 
ATOM   2035 C C     . ASN A 1 273 ? 31.270 20.504  40.428  1.00 40.81 ?  279 ASN A C     1 
ATOM   2036 O O     . ASN A 1 273 ? 31.901 20.973  39.478  1.00 39.77 ?  279 ASN A O     1 
ATOM   2037 C CB    . ASN A 1 273 ? 32.492 21.911  42.095  1.00 41.97 ?  279 ASN A CB    1 
ATOM   2038 C CG    . ASN A 1 273 ? 33.560 20.860  42.201  1.00 42.85 ?  279 ASN A CG    1 
ATOM   2039 O OD1   . ASN A 1 273 ? 33.285 19.731  42.614  1.00 43.85 ?  279 ASN A OD1   1 
ATOM   2040 N ND2   . ASN A 1 273 ? 34.777 21.204  41.803  1.00 42.58 ?  279 ASN A ND2   1 
ATOM   2041 N N     . VAL A 1 274 ? 30.711 19.298  40.372  1.00 41.32 ?  280 VAL A N     1 
ATOM   2042 C CA    . VAL A 1 274 ? 30.678 18.505  39.151  1.00 40.56 ?  280 VAL A CA    1 
ATOM   2043 C C     . VAL A 1 274 ? 29.226 18.276  38.781  1.00 40.16 ?  280 VAL A C     1 
ATOM   2044 O O     . VAL A 1 274 ? 28.434 17.813  39.612  1.00 41.17 ?  280 VAL A O     1 
ATOM   2045 C CB    . VAL A 1 274 ? 31.418 17.170  39.303  1.00 41.59 ?  280 VAL A CB    1 
ATOM   2046 C CG1   . VAL A 1 274 ? 31.263 16.342  38.030  1.00 40.84 ?  280 VAL A CG1   1 
ATOM   2047 C CG2   . VAL A 1 274 ? 32.881 17.433  39.617  1.00 42.05 ?  280 VAL A CG2   1 
ATOM   2048 N N     . TYR A 1 275 ? 28.882 18.614  37.543  1.00 38.80 ?  281 TYR A N     1 
ATOM   2049 C CA    . TYR A 1 275 ? 27.544 18.427  37.018  1.00 38.36 ?  281 TYR A CA    1 
ATOM   2050 C C     . TYR A 1 275 ? 27.599 17.486  35.821  1.00 37.80 ?  281 TYR A C     1 
ATOM   2051 O O     . TYR A 1 275 ? 28.615 17.396  35.128  1.00 37.33 ?  281 TYR A O     1 
ATOM   2052 C CB    . TYR A 1 275 ? 26.928 19.771  36.616  1.00 37.34 ?  281 TYR A CB    1 
ATOM   2053 C CG    . TYR A 1 275 ? 26.776 20.756  37.753  1.00 37.90 ?  281 TYR A CG    1 
ATOM   2054 C CD1   . TYR A 1 275 ? 27.875 21.431  38.273  1.00 38.06 ?  281 TYR A CD1   1 
ATOM   2055 C CD2   . TYR A 1 275 ? 25.527 21.017  38.310  1.00 38.35 ?  281 TYR A CD2   1 
ATOM   2056 C CE1   . TYR A 1 275 ? 27.735 22.336  39.332  1.00 38.64 ?  281 TYR A CE1   1 
ATOM   2057 C CE2   . TYR A 1 275 ? 25.375 21.924  39.371  1.00 38.96 ?  281 TYR A CE2   1 
ATOM   2058 C CZ    . TYR A 1 275 ? 26.481 22.587  39.873  1.00 39.14 ?  281 TYR A CZ    1 
ATOM   2059 O OH    . TYR A 1 275 ? 26.324 23.490  40.931  1.00 39.74 ?  281 TYR A OH    1 
ATOM   2060 N N     . ALA A 1 276 ? 26.498 16.781  35.585  1.00 37.95 ?  282 ALA A N     1 
ATOM   2061 C CA    . ALA A 1 276 ? 26.322 15.976  34.386  1.00 37.38 ?  282 ALA A CA    1 
ATOM   2062 C C     . ALA A 1 276 ? 25.031 16.403  33.709  1.00 36.62 ?  282 ALA A C     1 
ATOM   2063 O O     . ALA A 1 276 ? 24.004 16.593  34.372  1.00 37.14 ?  282 ALA A O     1 
ATOM   2064 C CB    . ALA A 1 276 ? 26.289 14.467  34.701  1.00 38.50 ?  282 ALA A CB    1 
ATOM   2065 N N     . ILE A 1 277 ? 25.083 16.565  32.389  1.00 35.51 ?  283 ILE A N     1 
ATOM   2066 C CA    . ILE A 1 277 ? 23.945 17.064  31.637  1.00 34.78 ?  283 ILE A CA    1 
ATOM   2067 C C     . ILE A 1 277 ? 23.775 16.226  30.381  1.00 34.30 ?  283 ILE A C     1 
ATOM   2068 O O     . ILE A 1 277 ? 24.739 15.666  29.856  1.00 34.16 ?  283 ILE A O     1 
ATOM   2069 C CB    . ILE A 1 277 ? 24.110 18.556  31.271  1.00 33.84 ?  283 ILE A CB    1 
ATOM   2070 C CG1   . ILE A 1 277 ? 25.281 18.752  30.306  1.00 33.03 ?  283 ILE A CG1   1 
ATOM   2071 C CG2   . ILE A 1 277 ? 24.304 19.399  32.532  1.00 34.37 ?  283 ILE A CG2   1 
ATOM   2072 C CD1   . ILE A 1 277 ? 25.404 20.175  29.785  1.00 32.14 ?  283 ILE A CD1   1 
ATOM   2073 N N     . GLY A 1 278 ? 22.541 16.159  29.889  1.00 34.12 ?  284 GLY A N     1 
ATOM   2074 C CA    . GLY A 1 278 ? 22.278 15.438  28.657  1.00 33.68 ?  284 GLY A CA    1 
ATOM   2075 C C     . GLY A 1 278 ? 22.324 13.930  28.858  1.00 34.56 ?  284 GLY A C     1 
ATOM   2076 O O     . GLY A 1 278 ? 22.071 13.418  29.948  1.00 35.63 ?  284 GLY A O     1 
ATOM   2077 N N     . ASP A 1 279 ? 22.666 13.216  27.778  1.00 34.20 ?  285 ASP A N     1 
ATOM   2078 C CA    . ASP A 1 279 ? 22.606 11.755  27.789  1.00 35.04 ?  285 ASP A CA    1 
ATOM   2079 C C     . ASP A 1 279 ? 23.447 11.137  28.901  1.00 36.10 ?  285 ASP A C     1 
ATOM   2080 O O     . ASP A 1 279 ? 23.079 10.086  29.436  1.00 38.28 ?  285 ASP A O     1 
ATOM   2081 C CB    . ASP A 1 279 ? 23.066 11.184  26.449  1.00 34.49 ?  285 ASP A CB    1 
ATOM   2082 C CG    . ASP A 1 279 ? 22.060 11.396  25.321  1.00 33.77 ?  285 ASP A CG    1 
ATOM   2083 O OD1   . ASP A 1 279 ? 21.083 12.167  25.505  1.00 33.57 ?  285 ASP A OD1   1 
ATOM   2084 O OD2   . ASP A 1 279 ? 22.263 10.782  24.239  1.00 33.50 -1 285 ASP A OD2   1 
ATOM   2085 N N     . CYS A 1 280 ? 24.580 11.743  29.257  1.00 35.93 ?  286 CYS A N     1 
ATOM   2086 C CA    . CYS A 1 280 ? 25.436 11.124  30.270  1.00 37.05 ?  286 CYS A CA    1 
ATOM   2087 C C     . CYS A 1 280 ? 24.929 11.294  31.700  1.00 38.36 ?  286 CYS A C     1 
ATOM   2088 O O     . CYS A 1 280 ? 25.496 10.676  32.606  1.00 40.33 ?  286 CYS A O     1 
ATOM   2089 C CB    . CYS A 1 280 ? 26.866 11.666  30.188  1.00 36.70 ?  286 CYS A CB    1 
ATOM   2090 S SG    . CYS A 1 280 ? 27.082 13.348  30.813  1.00 36.13 ?  286 CYS A SG    1 
ATOM   2091 N N     . ALA A 1 281 ? 23.905 12.110  31.942  1.00 37.73 ?  287 ALA A N     1 
ATOM   2092 C CA    . ALA A 1 281 ? 23.318 12.188  33.275  1.00 38.82 ?  287 ALA A CA    1 
ATOM   2093 C C     . ALA A 1 281 ? 22.318 11.055  33.482  1.00 42.87 ?  287 ALA A C     1 
ATOM   2094 O O     . ALA A 1 281 ? 21.639 10.621  32.548  1.00 39.65 ?  287 ALA A O     1 
ATOM   2095 C CB    . ALA A 1 281 ? 22.623 13.535  33.486  1.00 38.25 ?  287 ALA A CB    1 
ATOM   2096 N N     . ASP A 1 282 ? 22.224 10.574  34.724  1.00 44.78 ?  288 ASP A N     1 
ATOM   2097 C CA    . ASP A 1 282 ? 21.309 9.476   35.042  1.00 48.20 ?  288 ASP A CA    1 
ATOM   2098 C C     . ASP A 1 282 ? 19.966 10.040  35.496  1.00 50.47 ?  288 ASP A C     1 
ATOM   2099 O O     . ASP A 1 282 ? 19.656 10.130  36.686  1.00 48.88 ?  288 ASP A O     1 
ATOM   2100 C CB    . ASP A 1 282 ? 21.903 8.559   36.099  1.00 47.87 ?  288 ASP A CB    1 
ATOM   2101 C CG    . ASP A 1 282 ? 20.966 7.410   36.470  1.00 58.01 ?  288 ASP A CG    1 
ATOM   2102 O OD1   . ASP A 1 282 ? 20.549 6.656   35.547  1.00 51.62 ?  288 ASP A OD1   1 
ATOM   2103 O OD2   . ASP A 1 282 ? 20.658 7.267   37.687  1.00 56.31 -1 288 ASP A OD2   1 
ATOM   2104 N N     . VAL A 1 283 ? 19.150 10.415  34.519  1.00 46.63 ?  289 VAL A N     1 
ATOM   2105 C CA    . VAL A 1 283 ? 17.780 10.828  34.771  1.00 50.18 ?  289 VAL A CA    1 
ATOM   2106 C C     . VAL A 1 283 ? 16.842 9.749   34.245  1.00 54.61 ?  289 VAL A C     1 
ATOM   2107 O O     . VAL A 1 283 ? 17.226 8.875   33.455  1.00 54.73 ?  289 VAL A O     1 
ATOM   2108 C CB    . VAL A 1 283 ? 17.459 12.199  34.142  1.00 53.19 ?  289 VAL A CB    1 
ATOM   2109 C CG1   . VAL A 1 283 ? 18.215 13.289  34.860  1.00 47.07 ?  289 VAL A CG1   1 
ATOM   2110 C CG2   . VAL A 1 283 ? 17.800 12.199  32.665  1.00 47.56 ?  289 VAL A CG2   1 
ATOM   2111 N N     . ARG A 1 284 ? 15.589 9.808   34.710  1.00 59.11 ?  290 ARG A N     1 
ATOM   2112 C CA    . ARG A 1 284 ? 14.597 8.790   34.369  1.00 60.07 ?  290 ARG A CA    1 
ATOM   2113 C C     . ARG A 1 284 ? 13.950 9.038   33.011  1.00 56.59 ?  290 ARG A C     1 
ATOM   2114 O O     . ARG A 1 284 ? 13.347 8.121   32.445  1.00 60.36 ?  290 ARG A O     1 
ATOM   2115 C CB    . ARG A 1 284 ? 13.524 8.718   35.465  1.00 56.84 ?  290 ARG A CB    1 
ATOM   2116 N N     . THR A 1 285 ? 14.072 10.252  32.485  1.00 57.45 ?  291 THR A N     1 
ATOM   2117 C CA    . THR A 1 285 ? 13.569 10.622  31.168  1.00 58.49 ?  291 THR A CA    1 
ATOM   2118 C C     . THR A 1 285 ? 14.397 9.937   30.077  1.00 57.49 ?  291 THR A C     1 
ATOM   2119 O O     . THR A 1 285 ? 15.471 9.393   30.351  1.00 59.21 ?  291 THR A O     1 
ATOM   2120 C CB    . THR A 1 285 ? 13.609 12.148  31.023  1.00 59.49 ?  291 THR A CB    1 
ATOM   2121 O OG1   . THR A 1 285 ? 14.878 12.646  31.474  1.00 59.57 ?  291 THR A OG1   1 
ATOM   2122 C CG2   . THR A 1 285 ? 12.513 12.805  31.866  1.00 58.65 ?  291 THR A CG2   1 
ATOM   2123 N N     . PRO A 1 286 ? 13.926 9.930   28.827  1.00 60.99 ?  292 PRO A N     1 
ATOM   2124 C CA    . PRO A 1 286 ? 14.741 9.379   27.742  1.00 54.36 ?  292 PRO A CA    1 
ATOM   2125 C C     . PRO A 1 286 ? 15.787 10.394  27.303  1.00 47.82 ?  292 PRO A C     1 
ATOM   2126 O O     . PRO A 1 286 ? 15.767 11.568  27.681  1.00 47.08 ?  292 PRO A O     1 
ATOM   2127 C CB    . PRO A 1 286 ? 13.721 9.125   26.635  1.00 52.72 ?  292 PRO A CB    1 
ATOM   2128 C CG    . PRO A 1 286 ? 12.832 10.307  26.778  1.00 50.73 ?  292 PRO A CG    1 
ATOM   2129 C CD    . PRO A 1 286 ? 12.677 10.506  28.283  1.00 57.23 ?  292 PRO A CD    1 
ATOM   2130 N N     . LYS A 1 287 ? 16.719 9.916   26.495  1.00 43.43 ?  293 LYS A N     1 
ATOM   2131 C CA    . LYS A 1 287 ? 17.871 10.719  26.116  1.00 37.99 ?  293 LYS A CA    1 
ATOM   2132 C C     . LYS A 1 287 ? 17.467 11.636  24.970  1.00 34.32 ?  293 LYS A C     1 
ATOM   2133 O O     . LYS A 1 287 ? 17.372 11.192  23.826  1.00 33.93 ?  293 LYS A O     1 
ATOM   2134 C CB    . LYS A 1 287 ? 19.029 9.806   25.727  1.00 43.59 ?  293 LYS A CB    1 
ATOM   2135 C CG    . LYS A 1 287 ? 19.425 8.822   26.820  1.00 44.79 ?  293 LYS A CG    1 
ATOM   2136 C CD    . LYS A 1 287 ? 19.592 9.520   28.166  1.00 46.68 ?  293 LYS A CD    1 
ATOM   2137 C CE    . LYS A 1 287 ? 19.874 8.525   29.283  1.00 45.42 ?  293 LYS A CE    1 
ATOM   2138 N NZ    . LYS A 1 287 ? 20.064 9.201   30.587  1.00 42.00 ?  293 LYS A NZ    1 
ATOM   2139 N N     . MET A 1 288 ? 17.271 12.923  25.261  1.00 33.89 ?  294 MET A N     1 
ATOM   2140 C CA    . MET A 1 288 ? 16.748 13.877  24.295  1.00 33.05 ?  294 MET A CA    1 
ATOM   2141 C C     . MET A 1 288 ? 17.640 15.114  24.210  1.00 32.19 ?  294 MET A C     1 
ATOM   2142 O O     . MET A 1 288 ? 18.186 15.586  25.212  1.00 32.38 ?  294 MET A O     1 
ATOM   2143 C CB    . MET A 1 288 ? 15.323 14.289  24.680  1.00 33.59 ?  294 MET A CB    1 
ATOM   2144 C CG    . MET A 1 288 ? 14.346 13.145  24.767  1.00 34.55 ?  294 MET A CG    1 
ATOM   2145 S SD    . MET A 1 288 ? 13.857 12.615  23.125  1.00 42.10 ?  294 MET A SD    1 
ATOM   2146 C CE    . MET A 1 288 ? 12.893 14.026  22.589  1.00 36.65 ?  294 MET A CE    1 
ATOM   2147 N N     . ALA A 1 289 ? 17.753 15.659  22.999  1.00 22.79 ?  295 ALA A N     1 
ATOM   2148 C CA    . ALA A 1 289 ? 18.561 16.856  22.797  1.00 22.69 ?  295 ALA A CA    1 
ATOM   2149 C C     . ALA A 1 289 ? 18.004 18.049  23.561  1.00 19.99 ?  295 ALA A C     1 
ATOM   2150 O O     . ALA A 1 289 ? 18.762 18.831  24.135  1.00 17.17 ?  295 ALA A O     1 
ATOM   2151 C CB    . ALA A 1 289 ? 18.643 17.197  21.311  1.00 22.49 ?  295 ALA A CB    1 
ATOM   2152 N N     . TYR A 1 290 ? 16.684 18.228  23.554  1.00 21.22 ?  296 TYR A N     1 
ATOM   2153 C CA    . TYR A 1 290 ? 16.128 19.394  24.231  1.00 22.49 ?  296 TYR A CA    1 
ATOM   2154 C C     . TYR A 1 290 ? 16.327 19.316  25.745  1.00 23.58 ?  296 TYR A C     1 
ATOM   2155 O O     . TYR A 1 290 ? 16.528 20.350  26.392  1.00 26.18 ?  296 TYR A O     1 
ATOM   2156 C CB    . TYR A 1 290 ? 14.652 19.564  23.857  1.00 24.10 ?  296 TYR A CB    1 
ATOM   2157 C CG    . TYR A 1 290 ? 13.653 18.736  24.650  1.00 26.66 ?  296 TYR A CG    1 
ATOM   2158 C CD1   . TYR A 1 290 ? 13.273 17.454  24.227  1.00 25.45 ?  296 TYR A CD1   1 
ATOM   2159 C CD2   . TYR A 1 290 ? 13.067 19.246  25.813  1.00 25.53 ?  296 TYR A CD2   1 
ATOM   2160 C CE1   . TYR A 1 290 ? 12.338 16.707  24.945  1.00 25.95 ?  296 TYR A CE1   1 
ATOM   2161 C CE2   . TYR A 1 290 ? 12.141 18.512  26.532  1.00 26.56 ?  296 TYR A CE2   1 
ATOM   2162 C CZ    . TYR A 1 290 ? 11.776 17.245  26.092  1.00 28.68 ?  296 TYR A CZ    1 
ATOM   2163 O OH    . TYR A 1 290 ? 10.851 16.515  26.808  1.00 26.85 ?  296 TYR A OH    1 
ATOM   2164 N N     . LEU A 1 291 ? 16.304 18.109  26.322  1.00 21.60 ?  297 LEU A N     1 
ATOM   2165 C CA    . LEU A 1 291 ? 16.608 17.956  27.745  1.00 26.10 ?  297 LEU A CA    1 
ATOM   2166 C C     . LEU A 1 291 ? 18.071 18.279  28.033  1.00 23.78 ?  297 LEU A C     1 
ATOM   2167 O O     . LEU A 1 291 ? 18.390 18.867  29.071  1.00 23.11 ?  297 LEU A O     1 
ATOM   2168 C CB    . LEU A 1 291 ? 16.268 16.536  28.206  1.00 23.08 ?  297 LEU A CB    1 
ATOM   2169 C CG    . LEU A 1 291 ? 14.792 16.131  28.211  1.00 29.20 ?  297 LEU A CG    1 
ATOM   2170 C CD1   . LEU A 1 291 ? 14.617 14.647  28.532  1.00 33.59 ?  297 LEU A CD1   1 
ATOM   2171 C CD2   . LEU A 1 291 ? 14.014 16.967  29.208  1.00 31.34 ?  297 LEU A CD2   1 
ATOM   2172 N N     . ALA A 1 292 ? 18.972 17.901  27.122  1.00 21.13 ?  298 ALA A N     1 
ATOM   2173 C CA    . ALA A 1 292 ? 20.374 18.266  27.257  1.00 19.06 ?  298 ALA A CA    1 
ATOM   2174 C C     . ALA A 1 292 ? 20.524 19.772  27.442  1.00 22.05 ?  298 ALA A C     1 
ATOM   2175 O O     . ALA A 1 292 ? 21.243 20.230  28.334  1.00 22.64 ?  298 ALA A O     1 
ATOM   2176 C CB    . ALA A 1 292 ? 21.157 17.778  26.025  1.00 19.64 ?  298 ALA A CB    1 
ATOM   2177 N N     . GLY A 1 293 ? 19.823 20.561  26.623  1.00 21.07 ?  299 GLY A N     1 
ATOM   2178 C CA    . GLY A 1 293 ? 19.922 22.010  26.747  1.00 22.22 ?  299 GLY A CA    1 
ATOM   2179 C C     . GLY A 1 293 ? 19.318 22.539  28.039  1.00 26.27 ?  299 GLY A C     1 
ATOM   2180 O O     . GLY A 1 293 ? 19.811 23.513  28.609  1.00 26.02 ?  299 GLY A O     1 
ATOM   2181 N N     . LEU A 1 294 ? 18.241 21.910  28.514  1.00 25.30 ?  300 LEU A N     1 
ATOM   2182 C CA    . LEU A 1 294 ? 17.635 22.331  29.777  1.00 26.97 ?  300 LEU A CA    1 
ATOM   2183 C C     . LEU A 1 294 ? 18.510 21.966  30.967  1.00 25.47 ?  300 LEU A C     1 
ATOM   2184 O O     . LEU A 1 294 ? 18.554 22.700  31.956  1.00 31.12 ?  300 LEU A O     1 
ATOM   2185 C CB    . LEU A 1 294 ? 16.242 21.713  29.949  1.00 26.95 ?  300 LEU A CB    1 
ATOM   2186 C CG    . LEU A 1 294 ? 15.116 22.067  28.971  1.00 32.81 ?  300 LEU A CG    1 
ATOM   2187 C CD1   . LEU A 1 294 ? 13.822 21.315  29.343  1.00 30.71 ?  300 LEU A CD1   1 
ATOM   2188 C CD2   . LEU A 1 294 ? 14.863 23.588  28.873  1.00 31.40 ?  300 LEU A CD2   1 
ATOM   2189 N N     . HIS A 1 295 ? 19.171 20.810  30.923  1.00 25.17 ?  301 HIS A N     1 
ATOM   2190 C CA    . HIS A 1 295 ? 20.147 20.508  31.960  1.00 25.53 ?  301 HIS A CA    1 
ATOM   2191 C C     . HIS A 1 295 ? 21.275 21.528  31.949  1.00 26.66 ?  301 HIS A C     1 
ATOM   2192 O O     . HIS A 1 295 ? 21.795 21.909  33.005  1.00 24.60 ?  301 HIS A O     1 
ATOM   2193 C CB    . HIS A 1 295 ? 20.710 19.104  31.772  1.00 25.61 ?  301 HIS A CB    1 
ATOM   2194 C CG    . HIS A 1 295 ? 19.681 18.018  31.812  1.00 29.75 ?  301 HIS A CG    1 
ATOM   2195 N ND1   . HIS A 1 295 ? 19.910 16.758  31.296  1.00 30.31 ?  301 HIS A ND1   1 
ATOM   2196 C CD2   . HIS A 1 295 ? 18.423 17.996  32.311  1.00 33.47 ?  301 HIS A CD2   1 
ATOM   2197 C CE1   . HIS A 1 295 ? 18.838 16.010  31.476  1.00 34.13 ?  301 HIS A CE1   1 
ATOM   2198 N NE2   . HIS A 1 295 ? 17.920 16.737  32.087  1.00 33.89 ?  301 HIS A NE2   1 
ATOM   2199 N N     . ALA A 1 296 ? 21.670 21.974  30.757  1.00 24.09 ?  302 ALA A N     1 
ATOM   2200 C CA    . ALA A 1 296 ? 22.730 22.964  30.635  1.00 24.79 ?  302 ALA A CA    1 
ATOM   2201 C C     . ALA A 1 296 ? 22.359 24.257  31.346  1.00 27.24 ?  302 ALA A C     1 
ATOM   2202 O O     . ALA A 1 296 ? 23.167 24.814  32.101  1.00 25.43 ?  302 ALA A O     1 
ATOM   2203 C CB    . ALA A 1 296 ? 23.032 23.228  29.162  1.00 19.35 ?  302 ALA A CB    1 
ATOM   2204 N N     . ASN A 1 297 ? 21.140 24.757  31.111  1.00 29.21 ?  303 ASN A N     1 
ATOM   2205 C CA    . ASN A 1 297 ? 20.693 25.957  31.817  1.00 29.24 ?  303 ASN A CA    1 
ATOM   2206 C C     . ASN A 1 297 ? 20.737 25.743  33.315  1.00 29.25 ?  303 ASN A C     1 
ATOM   2207 O O     . ASN A 1 297 ? 21.167 26.628  34.061  1.00 29.44 ?  303 ASN A O     1 
ATOM   2208 C CB    . ASN A 1 297 ? 19.274 26.344  31.401  1.00 31.02 ?  303 ASN A CB    1 
ATOM   2209 C CG    . ASN A 1 297 ? 19.167 26.741  29.943  1.00 38.99 ?  303 ASN A CG    1 
ATOM   2210 O OD1   . ASN A 1 297 ? 20.159 27.141  29.300  1.00 39.52 ?  303 ASN A OD1   1 
ATOM   2211 N ND2   . ASN A 1 297 ? 17.946 26.640  29.402  1.00 41.60 ?  303 ASN A ND2   1 
ATOM   2212 N N     . ILE A 1 298 ? 20.305 24.565  33.772  1.00 27.69 ?  304 ILE A N     1 
ATOM   2213 C CA    . ILE A 1 298 ? 20.238 24.300  35.205  1.00 28.52 ?  304 ILE A CA    1 
ATOM   2214 C C     . ILE A 1 298 ? 21.633 24.245  35.808  1.00 28.68 ?  304 ILE A C     1 
ATOM   2215 O O     . ILE A 1 298 ? 21.885 24.821  36.873  1.00 26.16 ?  304 ILE A O     1 
ATOM   2216 C CB    . ILE A 1 298 ? 19.461 23.000  35.466  1.00 29.88 ?  304 ILE A CB    1 
ATOM   2217 C CG1   . ILE A 1 298 ? 17.974 23.226  35.202  1.00 34.50 ?  304 ILE A CG1   1 
ATOM   2218 C CG2   . ILE A 1 298 ? 19.672 22.517  36.902  1.00 32.65 ?  304 ILE A CG2   1 
ATOM   2219 C CD1   . ILE A 1 298 ? 17.151 21.991  35.356  1.00 31.48 ?  304 ILE A CD1   1 
ATOM   2220 N N     . ALA A 1 299 ? 22.567 23.577  35.125  1.00 27.84 ?  305 ALA A N     1 
ATOM   2221 C CA    . ALA A 1 299 ? 23.906 23.396  35.677  1.00 25.50 ?  305 ALA A CA    1 
ATOM   2222 C C     . ALA A 1 299 ? 24.639 24.725  35.796  1.00 25.63 ?  305 ALA A C     1 
ATOM   2223 O O     . ALA A 1 299 ? 25.200 25.039  36.855  1.00 28.33 ?  305 ALA A O     1 
ATOM   2224 C CB    . ALA A 1 299 ? 24.700 22.411  34.823  1.00 25.43 ?  305 ALA A CB    1 
ATOM   2225 N N     . VAL A 1 300 ? 24.653 25.512  34.715  1.00 24.17 ?  306 VAL A N     1 
ATOM   2226 C CA    . VAL A 1 300 ? 25.305 26.823  34.735  1.00 25.47 ?  306 VAL A CA    1 
ATOM   2227 C C     . VAL A 1 300 ? 24.673 27.718  35.799  1.00 25.73 ?  306 VAL A C     1 
ATOM   2228 O O     . VAL A 1 300 ? 25.370 28.328  36.614  1.00 25.46 ?  306 VAL A O     1 
ATOM   2229 C CB    . VAL A 1 300 ? 25.243 27.477  33.342  1.00 23.63 ?  306 VAL A CB    1 
ATOM   2230 C CG1   . VAL A 1 300 ? 25.803 28.905  33.409  1.00 24.67 ?  306 VAL A CG1   1 
ATOM   2231 C CG2   . VAL A 1 300 ? 26.007 26.649  32.321  1.00 23.43 ?  306 VAL A CG2   1 
ATOM   2232 N N     . ALA A 1 301 ? 23.339 27.799  35.809  1.00 26.21 ?  307 ALA A N     1 
ATOM   2233 C CA    . ALA A 1 301 ? 22.635 28.565  36.833  1.00 27.45 ?  307 ALA A CA    1 
ATOM   2234 C C     . ALA A 1 301 ? 23.057 28.146  38.239  1.00 31.71 ?  307 ALA A C     1 
ATOM   2235 O O     . ALA A 1 301 ? 23.253 28.996  39.118  1.00 30.87 ?  307 ALA A O     1 
ATOM   2236 C CB    . ALA A 1 301 ? 21.119 28.398  36.666  1.00 26.87 ?  307 ALA A CB    1 
ATOM   2237 N N     . ASN A 1 302 ? 23.209 26.837  38.470  1.00 30.81 ?  308 ASN A N     1 
ATOM   2238 C CA    . ASN A 1 302 ? 23.564 26.370  39.808  1.00 30.50 ?  308 ASN A CA    1 
ATOM   2239 C C     . ASN A 1 302 ? 25.020 26.661  40.144  1.00 31.14 ?  308 ASN A C     1 
ATOM   2240 O O     . ASN A 1 302 ? 25.336 26.904  41.311  1.00 33.61 ?  308 ASN A O     1 
ATOM   2241 C CB    . ASN A 1 302 ? 23.266 24.879  39.952  1.00 31.56 ?  308 ASN A CB    1 
ATOM   2242 C CG    . ASN A 1 302 ? 21.795 24.610  40.154  1.00 37.69 ?  308 ASN A CG    1 
ATOM   2243 O OD1   . ASN A 1 302 ? 21.022 25.532  40.439  1.00 38.38 ?  308 ASN A OD1   1 
ATOM   2244 N ND2   . ASN A 1 302 ? 21.392 23.350  40.019  1.00 36.93 ?  308 ASN A ND2   1 
ATOM   2245 N N     . ILE A 1 303 ? 25.920 26.644  39.158  1.00 30.12 ?  309 ILE A N     1 
ATOM   2246 C CA    . ILE A 1 303 ? 27.282 27.114  39.415  1.00 31.16 ?  309 ILE A CA    1 
ATOM   2247 C C     . ILE A 1 303 ? 27.244 28.558  39.914  1.00 32.42 ?  309 ILE A C     1 
ATOM   2248 O O     . ILE A 1 303 ? 27.772 28.877  40.988  1.00 30.18 ?  309 ILE A O     1 
ATOM   2249 C CB    . ILE A 1 303 ? 28.166 26.950  38.161  1.00 28.95 ?  309 ILE A CB    1 
ATOM   2250 C CG1   . ILE A 1 303 ? 28.314 25.469  37.803  1.00 30.12 ?  309 ILE A CG1   1 
ATOM   2251 C CG2   . ILE A 1 303 ? 29.549 27.520  38.379  1.00 26.03 ?  309 ILE A CG2   1 
ATOM   2252 C CD1   . ILE A 1 303 ? 28.921 25.201  36.431  1.00 28.63 ?  309 ILE A CD1   1 
ATOM   2253 N N     . VAL A 1 304 ? 26.538 29.432  39.193  1.00 29.04 ?  310 VAL A N     1 
ATOM   2254 C CA    . VAL A 1 304 ? 26.410 30.822  39.644  1.00 31.38 ?  310 VAL A CA    1 
ATOM   2255 C C     . VAL A 1 304 ? 25.673 30.898  40.985  1.00 34.92 ?  310 VAL A C     1 
ATOM   2256 O O     . VAL A 1 304 ? 26.108 31.589  41.917  1.00 32.44 ?  310 VAL A O     1 
ATOM   2257 C CB    . VAL A 1 304 ? 25.716 31.674  38.566  1.00 30.73 ?  310 VAL A CB    1 
ATOM   2258 C CG1   . VAL A 1 304 ? 25.503 33.102  39.062  1.00 32.22 ?  310 VAL A CG1   1 
ATOM   2259 C CG2   . VAL A 1 304 ? 26.539 31.677  37.293  1.00 27.03 ?  310 VAL A CG2   1 
ATOM   2260 N N     . ASN A 1 305 ? 24.542 30.194  41.103  1.00 34.16 ?  311 ASN A N     1 
ATOM   2261 C CA    . ASN A 1 305 ? 23.766 30.269  42.344  1.00 36.42 ?  311 ASN A CA    1 
ATOM   2262 C C     . ASN A 1 305 ? 24.571 29.779  43.533  1.00 39.62 ?  311 ASN A C     1 
ATOM   2263 O O     . ASN A 1 305 ? 24.399 30.278  44.655  1.00 41.78 ?  311 ASN A O     1 
ATOM   2264 C CB    . ASN A 1 305 ? 22.476 29.454  42.238  1.00 38.48 ?  311 ASN A CB    1 
ATOM   2265 C CG    . ASN A 1 305 ? 21.367 30.207  41.544  1.00 41.16 ?  311 ASN A CG    1 
ATOM   2266 O OD1   . ASN A 1 305 ? 21.305 31.436  41.610  1.00 45.00 ?  311 ASN A OD1   1 
ATOM   2267 N ND2   . ASN A 1 305 ? 20.485 29.474  40.864  1.00 41.86 ?  311 ASN A ND2   1 
ATOM   2268 N N     . SER A 1 306 ? 25.438 28.786  43.323  1.00 36.38 ?  312 SER A N     1 
ATOM   2269 C CA    . SER A 1 306 ? 26.261 28.314  44.430  1.00 38.85 ?  312 SER A CA    1 
ATOM   2270 C C     . SER A 1 306 ? 27.222 29.403  44.880  1.00 37.61 ?  312 SER A C     1 
ATOM   2271 O O     . SER A 1 306 ? 27.440 29.591  46.082  1.00 44.73 ?  312 SER A O     1 
ATOM   2272 C CB    . SER A 1 306 ? 27.014 27.040  44.039  1.00 33.20 ?  312 SER A CB    1 
ATOM   2273 O OG    . SER A 1 306 ? 27.943 27.276  42.999  1.00 37.57 ?  312 SER A OG    1 
ATOM   2274 N N     . VAL A 1 307 ? 27.780 30.157  43.929  1.00 39.12 ?  313 VAL A N     1 
ATOM   2275 C CA    . VAL A 1 307 ? 28.710 31.230  44.277  1.00 39.48 ?  313 VAL A CA    1 
ATOM   2276 C C     . VAL A 1 307 ? 27.980 32.391  44.961  1.00 42.86 ?  313 VAL A C     1 
ATOM   2277 O O     . VAL A 1 307 ? 28.542 33.062  45.839  1.00 38.82 ?  313 VAL A O     1 
ATOM   2278 C CB    . VAL A 1 307 ? 29.470 31.680  43.014  1.00 39.46 ?  313 VAL A CB    1 
ATOM   2279 C CG1   . VAL A 1 307 ? 30.448 32.795  43.343  1.00 37.34 ?  313 VAL A CG1   1 
ATOM   2280 C CG2   . VAL A 1 307 ? 30.210 30.498  42.397  1.00 38.65 ?  313 VAL A CG2   1 
ATOM   2281 N N     . LYS A 1 308 ? 26.718 32.628  44.607  1.00 46.77 ?  314 LYS A N     1 
ATOM   2282 C CA    . LYS A 1 308 ? 25.928 33.705  45.197  1.00 47.26 ?  314 LYS A CA    1 
ATOM   2283 C C     . LYS A 1 308 ? 25.184 33.292  46.472  1.00 48.93 ?  314 LYS A C     1 
ATOM   2284 O O     . LYS A 1 308 ? 24.408 34.095  47.003  1.00 51.15 ?  314 LYS A O     1 
ATOM   2285 C CB    . LYS A 1 308 ? 24.925 34.239  44.165  1.00 47.18 ?  314 LYS A CB    1 
ATOM   2286 C CG    . LYS A 1 308 ? 25.552 34.963  42.986  1.00 44.13 ?  314 LYS A CG    1 
ATOM   2287 C CD    . LYS A 1 308 ? 24.486 35.571  42.087  1.00 42.75 ?  314 LYS A CD    1 
ATOM   2288 C CE    . LYS A 1 308 ? 25.111 36.390  40.976  1.00 42.05 ?  314 LYS A CE    1 
ATOM   2289 N NZ    . LYS A 1 308 ? 24.135 36.718  39.897  1.00 47.76 ?  314 LYS A NZ    1 
ATOM   2290 N N     . GLN A 1 309 ? 25.413 32.076  46.983  1.00 49.89 ?  315 GLN A N     1 
ATOM   2291 C CA    . GLN A 1 309 ? 24.704 31.560  48.161  1.00 51.60 ?  315 GLN A CA    1 
ATOM   2292 C C     . GLN A 1 309 ? 23.192 31.666  47.972  1.00 51.76 ?  315 GLN A C     1 
ATOM   2293 O O     . GLN A 1 309 ? 22.452 32.013  48.895  1.00 52.27 ?  315 GLN A O     1 
ATOM   2294 C CB    . GLN A 1 309 ? 25.123 32.277  49.446  1.00 53.61 ?  315 GLN A CB    1 
ATOM   2295 C CG    . GLN A 1 309 ? 26.626 32.453  49.659  1.00 55.87 ?  315 GLN A CG    1 
ATOM   2296 C CD    . GLN A 1 309 ? 27.378 31.136  49.742  1.00 56.42 ?  315 GLN A CD    1 
ATOM   2297 O OE1   . GLN A 1 309 ? 27.747 30.559  48.715  1.00 61.58 ?  315 GLN A OE1   1 
ATOM   2298 N NE2   . GLN A 1 309 ? 27.632 30.664  50.968  1.00 62.13 ?  315 GLN A NE2   1 
ATOM   2299 N N     . ARG A 1 310 ? 22.735 31.403  46.756  1.00 49.06 ?  316 ARG A N     1 
ATOM   2300 C CA    . ARG A 1 310 ? 21.319 31.338  46.423  1.00 49.35 ?  316 ARG A CA    1 
ATOM   2301 C C     . ARG A 1 310 ? 20.862 29.891  46.307  1.00 51.15 ?  316 ARG A C     1 
ATOM   2302 O O     . ARG A 1 310 ? 21.667 28.986  46.067  1.00 50.28 ?  316 ARG A O     1 
ATOM   2303 C CB    . ARG A 1 310 ? 21.035 32.063  45.098  1.00 47.97 ?  316 ARG A CB    1 
ATOM   2304 C CG    . ARG A 1 310 ? 20.966 33.588  45.181  1.00 47.24 ?  316 ARG A CG    1 
ATOM   2305 C CD    . ARG A 1 310 ? 20.700 34.213  43.803  1.00 48.39 ?  316 ARG A CD    1 
ATOM   2306 N N     . PRO A 1 311 ? 19.560 29.638  46.461  1.00 54.77 ?  317 PRO A N     1 
ATOM   2307 C CA    . PRO A 1 311 ? 19.051 28.269  46.286  1.00 49.86 ?  317 PRO A CA    1 
ATOM   2308 C C     . PRO A 1 311 ? 19.171 27.800  44.847  1.00 48.23 ?  317 PRO A C     1 
ATOM   2309 O O     . PRO A 1 311 ? 19.118 28.589  43.901  1.00 48.64 ?  317 PRO A O     1 
ATOM   2310 C CB    . PRO A 1 311 ? 17.581 28.364  46.737  1.00 52.54 ?  317 PRO A CB    1 
ATOM   2311 C CG    . PRO A 1 311 ? 17.284 29.827  46.822  1.00 54.35 ?  317 PRO A CG    1 
ATOM   2312 C CD    . PRO A 1 311 ? 18.564 30.535  47.069  1.00 52.29 ?  317 PRO A CD    1 
ATOM   2313 N N     . LEU A 1 312 ? 19.358 26.492  44.695  1.00 47.18 ?  318 LEU A N     1 
ATOM   2314 C CA    . LEU A 1 312 ? 19.646 25.895  43.403  1.00 44.65 ?  318 LEU A CA    1 
ATOM   2315 C C     . LEU A 1 312 ? 18.362 25.584  42.643  1.00 45.10 ?  318 LEU A C     1 
ATOM   2316 O O     . LEU A 1 312 ? 17.344 25.213  43.235  1.00 44.51 ?  318 LEU A O     1 
ATOM   2317 C CB    . LEU A 1 312 ? 20.471 24.623  43.583  1.00 45.34 ?  318 LEU A CB    1 
ATOM   2318 C CG    . LEU A 1 312 ? 21.787 24.766  44.352  1.00 46.69 ?  318 LEU A CG    1 
ATOM   2319 C CD1   . LEU A 1 312 ? 22.693 23.584  44.067  1.00 46.84 ?  318 LEU A CD1   1 
ATOM   2320 C CD2   . LEU A 1 312 ? 22.499 26.067  44.018  1.00 45.94 ?  318 LEU A CD2   1 
ATOM   2321 N N     . GLN A 1 313 ? 18.413 25.766  41.329  1.00 41.57 ?  319 GLN A N     1 
ATOM   2322 C CA    . GLN A 1 313 ? 17.297 25.406  40.470  1.00 44.65 ?  319 GLN A CA    1 
ATOM   2323 C C     . GLN A 1 313 ? 17.154 23.889  40.393  1.00 43.95 ?  319 GLN A C     1 
ATOM   2324 O O     . GLN A 1 313 ? 18.134 23.143  40.496  1.00 42.81 ?  319 GLN A O     1 
ATOM   2325 C CB    . GLN A 1 313 ? 17.488 25.986  39.063  1.00 39.99 ?  319 GLN A CB    1 
ATOM   2326 C CG    . GLN A 1 313 ? 17.536 27.509  39.009  1.00 40.98 ?  319 GLN A CG    1 
ATOM   2327 C CD    . GLN A 1 313 ? 17.394 28.028  37.590  1.00 43.46 ?  319 GLN A CD    1 
ATOM   2328 O OE1   . GLN A 1 313 ? 17.206 27.251  36.666  1.00 44.03 ?  319 GLN A OE1   1 
ATOM   2329 N NE2   . GLN A 1 313 ? 17.478 29.346  37.415  1.00 42.85 ?  319 GLN A NE2   1 
ATOM   2330 N N     . ALA A 1 314 ? 15.917 23.438  40.182  1.00 47.61 ?  320 ALA A N     1 
ATOM   2331 C CA    . ALA A 1 314 ? 15.571 22.025  40.256  1.00 45.66 ?  320 ALA A CA    1 
ATOM   2332 C C     . ALA A 1 314 ? 14.984 21.537  38.939  1.00 50.39 ?  320 ALA A C     1 
ATOM   2333 O O     . ALA A 1 314 ? 14.186 22.238  38.306  1.00 54.53 ?  320 ALA A O     1 
ATOM   2334 C CB    . ALA A 1 314 ? 14.578 21.780  41.389  1.00 46.09 ?  320 ALA A CB    1 
ATOM   2335 N N     . TYR A 1 315 ? 15.373 20.318  38.543  1.00 48.83 ?  321 TYR A N     1 
ATOM   2336 C CA    . TYR A 1 315 ? 14.911 19.677  37.314  1.00 49.24 ?  321 TYR A CA    1 
ATOM   2337 C C     . TYR A 1 315 ? 13.748 18.742  37.622  1.00 46.83 ?  321 TYR A C     1 
ATOM   2338 O O     . TYR A 1 315 ? 13.909 17.785  38.387  1.00 47.55 ?  321 TYR A O     1 
ATOM   2339 C CB    . TYR A 1 315 ? 16.047 18.892  36.653  1.00 45.03 ?  321 TYR A CB    1 
ATOM   2340 C CG    . TYR A 1 315 ? 15.581 17.953  35.561  1.00 44.45 ?  321 TYR A CG    1 
ATOM   2341 C CD1   . TYR A 1 315 ? 15.015 18.445  34.387  1.00 44.89 ?  321 TYR A CD1   1 
ATOM   2342 C CD2   . TYR A 1 315 ? 15.706 16.572  35.702  1.00 46.35 ?  321 TYR A CD2   1 
ATOM   2343 C CE1   . TYR A 1 315 ? 14.588 17.589  33.377  1.00 47.71 ?  321 TYR A CE1   1 
ATOM   2344 C CE2   . TYR A 1 315 ? 15.279 15.700  34.695  1.00 47.46 ?  321 TYR A CE2   1 
ATOM   2345 C CZ    . TYR A 1 315 ? 14.722 16.211  33.540  1.00 46.99 ?  321 TYR A CZ    1 
ATOM   2346 O OH    . TYR A 1 315 ? 14.298 15.351  32.546  1.00 47.63 ?  321 TYR A OH    1 
ATOM   2347 N N     . LYS A 1 316 ? 12.592 18.996  37.008  1.00 45.32 ?  322 LYS A N     1 
ATOM   2348 C CA    . LYS A 1 316 ? 11.366 18.250  37.301  1.00 45.59 ?  322 LYS A CA    1 
ATOM   2349 C C     . LYS A 1 316 ? 10.787 17.659  36.028  1.00 49.18 ?  322 LYS A C     1 
ATOM   2350 O O     . LYS A 1 316 ? 10.138 18.384  35.249  1.00 51.21 ?  322 LYS A O     1 
ATOM   2351 C CB    . LYS A 1 316 ? 10.331 19.151  37.969  1.00 42.48 ?  322 LYS A CB    1 
ATOM   2352 C CG    . LYS A 1 316 ? 9.616  18.526  39.161  1.00 42.99 ?  322 LYS A CG    1 
ATOM   2353 C CD    . LYS A 1 316 ? 8.446  17.628  38.804  1.00 42.63 ?  322 LYS A CD    1 
ATOM   2354 C CE    . LYS A 1 316 ? 7.639  17.301  40.068  1.00 44.06 ?  322 LYS A CE    1 
ATOM   2355 N NZ    . LYS A 1 316 ? 6.530  16.326  39.808  1.00 48.34 ?  322 LYS A NZ    1 
ATOM   2356 N N     . PRO A 1 317 ? 10.960 16.358  35.776  1.00 47.21 ?  323 PRO A N     1 
ATOM   2357 C CA    . PRO A 1 317 ? 10.391 15.760  34.562  1.00 46.54 ?  323 PRO A CA    1 
ATOM   2358 C C     . PRO A 1 317 ? 8.870  15.785  34.586  1.00 45.46 ?  323 PRO A C     1 
ATOM   2359 O O     . PRO A 1 317 ? 8.233  15.862  35.641  1.00 46.87 ?  323 PRO A O     1 
ATOM   2360 C CB    . PRO A 1 317 ? 10.912 14.319  34.588  1.00 42.13 ?  323 PRO A CB    1 
ATOM   2361 C CG    . PRO A 1 317 ? 11.143 14.040  36.060  1.00 45.72 ?  323 PRO A CG    1 
ATOM   2362 C CD    . PRO A 1 317 ? 11.607 15.352  36.642  1.00 46.18 ?  323 PRO A CD    1 
ATOM   2363 N N     . GLY A 1 318 ? 8.294  15.753  33.395  1.00 42.17 ?  324 GLY A N     1 
ATOM   2364 C CA    . GLY A 1 318 ? 6.872  15.553  33.246  1.00 36.19 ?  324 GLY A CA    1 
ATOM   2365 C C     . GLY A 1 318 ? 6.677  14.356  32.346  1.00 36.28 ?  324 GLY A C     1 
ATOM   2366 O O     . GLY A 1 318 ? 7.610  13.576  32.152  1.00 38.11 ?  324 GLY A O     1 
ATOM   2367 N N     . ALA A 1 319 ? 5.488  14.205  31.771  1.00 35.06 ?  325 ALA A N     1 
ATOM   2368 C CA    . ALA A 1 319 ? 5.236  13.053  30.936  1.00 34.31 ?  325 ALA A CA    1 
ATOM   2369 C C     . ALA A 1 319 ? 6.084  13.112  29.663  1.00 33.25 ?  325 ALA A C     1 
ATOM   2370 O O     . ALA A 1 319 ? 6.646  14.148  29.289  1.00 33.34 ?  325 ALA A O     1 
ATOM   2371 C CB    . ALA A 1 319 ? 3.743  12.950  30.618  1.00 36.32 ?  325 ALA A CB    1 
ATOM   2372 N N     . LEU A 1 320 ? 6.174  11.963  29.008  1.00 32.43 ?  326 LEU A N     1 
ATOM   2373 C CA    . LEU A 1 320 ? 7.106  11.752  27.908  1.00 33.40 ?  326 LEU A CA    1 
ATOM   2374 C C     . LEU A 1 320 ? 6.720  12.566  26.673  1.00 30.30 ?  326 LEU A C     1 
ATOM   2375 O O     . LEU A 1 320 ? 5.586  12.471  26.189  1.00 29.03 ?  326 LEU A O     1 
ATOM   2376 C CB    . LEU A 1 320 ? 7.136  10.263  27.575  1.00 32.42 ?  326 LEU A CB    1 
ATOM   2377 C CG    . LEU A 1 320 ? 7.950  9.782   26.384  1.00 32.70 ?  326 LEU A CG    1 
ATOM   2378 C CD1   . LEU A 1 320 ? 9.391  10.289  26.497  1.00 30.82 ?  326 LEU A CD1   1 
ATOM   2379 C CD2   . LEU A 1 320 ? 7.883  8.242   26.298  1.00 32.97 ?  326 LEU A CD2   1 
ATOM   2380 N N     . THR A 1 321 ? 7.660  13.370  26.175  1.00 26.52 ?  327 THR A N     1 
ATOM   2381 C CA    . THR A 1 321 ? 7.579  13.965  24.844  1.00 26.88 ?  327 THR A CA    1 
ATOM   2382 C C     . THR A 1 321 ? 8.540  13.219  23.930  1.00 24.08 ?  327 THR A C     1 
ATOM   2383 O O     . THR A 1 321 ? 9.724  13.091  24.249  1.00 25.14 ?  327 THR A O     1 
ATOM   2384 C CB    . THR A 1 321 ? 7.946  15.454  24.859  1.00 28.27 ?  327 THR A CB    1 
ATOM   2385 O OG1   . THR A 1 321 ? 6.913  16.210  25.492  1.00 30.39 ?  327 THR A OG1   1 
ATOM   2386 C CG2   . THR A 1 321 ? 8.159  15.975  23.420  1.00 24.01 ?  327 THR A CG2   1 
ATOM   2387 N N     . PHE A 1 322 ? 8.038  12.727  22.801  1.00 24.27 ?  328 PHE A N     1 
ATOM   2388 C CA    . PHE A 1 322 ? 8.871  11.915  21.908  1.00 24.16 ?  328 PHE A CA    1 
ATOM   2389 C C     . PHE A 1 322 ? 8.247  11.964  20.524  1.00 20.91 ?  328 PHE A C     1 
ATOM   2390 O O     . PHE A 1 322 ? 7.126  11.478  20.348  1.00 21.15 ?  328 PHE A O     1 
ATOM   2391 C CB    . PHE A 1 322 ? 8.951  10.482  22.431  1.00 26.64 ?  328 PHE A CB    1 
ATOM   2392 C CG    . PHE A 1 322 ? 10.077 9.671   21.846  1.00 27.74 ?  328 PHE A CG    1 
ATOM   2393 C CD1   . PHE A 1 322 ? 10.130 9.401   20.494  1.00 25.55 ?  328 PHE A CD1   1 
ATOM   2394 C CD2   . PHE A 1 322 ? 11.073 9.167   22.662  1.00 31.42 ?  328 PHE A CD2   1 
ATOM   2395 C CE1   . PHE A 1 322 ? 11.165 8.653   19.959  1.00 27.91 ?  328 PHE A CE1   1 
ATOM   2396 C CE2   . PHE A 1 322 ? 12.111 8.410   22.136  1.00 34.68 ?  328 PHE A CE2   1 
ATOM   2397 C CZ    . PHE A 1 322 ? 12.155 8.155   20.782  1.00 30.13 ?  328 PHE A CZ    1 
ATOM   2398 N N     . LEU A 1 323 ? 8.948  12.554  19.557  1.00 19.76 ?  329 LEU A N     1 
ATOM   2399 C CA    . LEU A 1 323 ? 8.428  12.728  18.205  1.00 18.71 ?  329 LEU A CA    1 
ATOM   2400 C C     . LEU A 1 323 ? 9.277  11.946  17.221  1.00 18.54 ?  329 LEU A C     1 
ATOM   2401 O O     . LEU A 1 323 ? 10.506 12.070  17.218  1.00 17.64 ?  329 LEU A O     1 
ATOM   2402 C CB    . LEU A 1 323 ? 8.410  14.200  17.787  1.00 18.23 ?  329 LEU A CB    1 
ATOM   2403 C CG    . LEU A 1 323 ? 7.688  15.167  18.733  1.00 22.11 ?  329 LEU A CG    1 
ATOM   2404 C CD1   . LEU A 1 323 ? 7.804  16.591  18.216  1.00 22.50 ?  329 LEU A CD1   1 
ATOM   2405 C CD2   . LEU A 1 323 ? 6.231  14.785  18.890  1.00 20.68 ?  329 LEU A CD2   1 
ATOM   2406 N N     . LEU A 1 324 ? 8.624  11.157  16.383  1.00 17.54 ?  330 LEU A N     1 
ATOM   2407 C CA    . LEU A 1 324 ? 9.289  10.391  15.341  1.00 18.68 ?  330 LEU A CA    1 
ATOM   2408 C C     . LEU A 1 324 ? 8.899  10.987  14.004  1.00 17.00 ?  330 LEU A C     1 
ATOM   2409 O O     . LEU A 1 324 ? 7.722  10.994  13.655  1.00 19.23 ?  330 LEU A O     1 
ATOM   2410 C CB    . LEU A 1 324 ? 8.900  8.916   15.392  1.00 21.32 ?  330 LEU A CB    1 
ATOM   2411 C CG    . LEU A 1 324 ? 9.206  8.207   16.702  1.00 23.83 ?  330 LEU A CG    1 
ATOM   2412 C CD1   . LEU A 1 324 ? 7.948  8.079   17.550  1.00 23.74 ?  330 LEU A CD1   1 
ATOM   2413 C CD2   . LEU A 1 324 ? 9.833  6.831   16.438  1.00 24.88 ?  330 LEU A CD2   1 
ATOM   2414 N N     . SER A 1 325 ? 9.872  11.520  13.279  1.00 17.30 ?  331 SER A N     1 
ATOM   2415 C CA    . SER A 1 325 ? 9.639  11.918  11.902  1.00 19.08 ?  331 SER A CA    1 
ATOM   2416 C C     . SER A 1 325 ? 9.660  10.673  11.036  1.00 21.71 ?  331 SER A C     1 
ATOM   2417 O O     . SER A 1 325 ? 10.471 9.774   11.251  1.00 26.02 ?  331 SER A O     1 
ATOM   2418 C CB    . SER A 1 325 ? 10.721 12.889  11.438  1.00 22.33 ?  331 SER A CB    1 
ATOM   2419 O OG    . SER A 1 325 ? 11.982 12.241  11.514  1.00 25.88 ?  331 SER A OG    1 
ATOM   2420 N N     . MET A 1 326 ? 8.757  10.605  10.073  1.00 18.22 ?  332 MET A N     1 
ATOM   2421 C CA    . MET A 1 326 ? 8.683  9.470   9.156   1.00 20.37 ?  332 MET A CA    1 
ATOM   2422 C C     . MET A 1 326 ? 8.890  10.041  7.759   1.00 17.36 ?  332 MET A C     1 
ATOM   2423 O O     . MET A 1 326 ? 7.932  10.219  7.012   1.00 16.13 ?  332 MET A O     1 
ATOM   2424 C CB    . MET A 1 326 ? 7.327  8.746   9.263   1.00 20.70 ?  332 MET A CB    1 
ATOM   2425 C CG    . MET A 1 326 ? 6.926  8.253   10.648  1.00 24.47 ?  332 MET A CG    1 
ATOM   2426 S SD    . MET A 1 326 ? 7.511  6.582   10.961  1.00 35.53 ?  332 MET A SD    1 
ATOM   2427 C CE    . MET A 1 326 ? 9.038  6.982   11.782  1.00 20.30 ?  332 MET A CE    1 
ATOM   2428 N N     . GLY A 1 327 ? 10.128 10.383  7.433   1.00 16.84 ?  333 GLY A N     1 
ATOM   2429 C CA    . GLY A 1 327 ? 10.393 11.159  6.236   1.00 15.70 ?  333 GLY A CA    1 
ATOM   2430 C C     . GLY A 1 327 ? 9.880  12.582  6.407   1.00 16.26 ?  333 GLY A C     1 
ATOM   2431 O O     . GLY A 1 327 ? 9.286  12.947  7.419   1.00 15.98 ?  333 GLY A O     1 
ATOM   2432 N N     . ARG A 1 328 ? 10.112 13.402  5.386   1.00 13.71 ?  334 ARG A N     1 
ATOM   2433 C CA    . ARG A 1 328 ? 9.814  14.815  5.553   1.00 14.98 ?  334 ARG A CA    1 
ATOM   2434 C C     . ARG A 1 328 ? 8.320  15.116  5.515   1.00 16.48 ?  334 ARG A C     1 
ATOM   2435 O O     . ARG A 1 328 ? 7.917  16.221  5.893   1.00 15.39 ?  334 ARG A O     1 
ATOM   2436 C CB    . ARG A 1 328 ? 10.546 15.632  4.486   1.00 14.18 ?  334 ARG A CB    1 
ATOM   2437 C CG    . ARG A 1 328 ? 9.965  15.480  3.090   1.00 15.63 ?  334 ARG A CG    1 
ATOM   2438 C CD    . ARG A 1 328 ? 10.704 16.296  2.056   1.00 17.75 ?  334 ARG A CD    1 
ATOM   2439 N NE    . ARG A 1 328 ? 12.080 15.846  1.896   1.00 15.54 ?  334 ARG A NE    1 
ATOM   2440 C CZ    . ARG A 1 328 ? 13.139 16.540  2.287   1.00 19.78 ?  334 ARG A CZ    1 
ATOM   2441 N NH1   . ARG A 1 328 ? 13.016 17.743  2.824   1.00 17.35 ?  334 ARG A NH1   1 
ATOM   2442 N NH2   . ARG A 1 328 ? 14.353 16.024  2.117   1.00 18.28 ?  334 ARG A NH2   1 
ATOM   2443 N N     . ASN A 1 329 ? 7.480  14.178  5.082   1.00 14.65 ?  335 ASN A N     1 
ATOM   2444 C CA    . ASN A 1 329 ? 6.057  14.467  4.943   1.00 17.48 ?  335 ASN A CA    1 
ATOM   2445 C C     . ASN A 1 329 ? 5.182  13.768  5.984   1.00 16.25 ?  335 ASN A C     1 
ATOM   2446 O O     . ASN A 1 329 ? 3.963  13.735  5.818   1.00 13.97 ?  335 ASN A O     1 
ATOM   2447 C CB    . ASN A 1 329 ? 5.588  14.092  3.526   1.00 14.55 ?  335 ASN A CB    1 
ATOM   2448 C CG    . ASN A 1 329 ? 5.757  12.612  3.231   1.00 16.62 ?  335 ASN A CG    1 
ATOM   2449 O OD1   . ASN A 1 329 ? 6.239  11.837  4.071   1.00 14.98 ?  335 ASN A OD1   1 
ATOM   2450 N ND2   . ASN A 1 329 ? 5.362  12.207  2.034   1.00 17.36 ?  335 ASN A ND2   1 
ATOM   2451 N N     . ASP A 1 330 ? 5.750  13.220  7.056   1.00 16.27 ?  336 ASP A N     1 
ATOM   2452 C CA    . ASP A 1 330 ? 4.943  12.352  7.906   1.00 17.52 ?  336 ASP A CA    1 
ATOM   2453 C C     . ASP A 1 330 ? 5.611  12.212  9.271   1.00 18.08 ?  336 ASP A C     1 
ATOM   2454 O O     . ASP A 1 330 ? 6.770  12.605  9.466   1.00 14.97 ?  336 ASP A O     1 
ATOM   2455 C CB    . ASP A 1 330 ? 4.735  10.972  7.240   1.00 18.66 ?  336 ASP A CB    1 
ATOM   2456 C CG    . ASP A 1 330 ? 3.335  10.367  7.527   1.00 23.35 ?  336 ASP A CG    1 
ATOM   2457 O OD1   . ASP A 1 330 ? 2.756  10.665  8.591   1.00 21.26 ?  336 ASP A OD1   1 
ATOM   2458 O OD2   . ASP A 1 330 ? 2.814  9.585   6.686   1.00 22.68 -1 336 ASP A OD2   1 
ATOM   2459 N N     . GLY A 1 331 ? 4.878  11.624  10.207  1.00 19.96 ?  337 GLY A N     1 
ATOM   2460 C CA    . GLY A 1 331 ? 5.402  11.426  11.546  1.00 18.78 ?  337 GLY A CA    1 
ATOM   2461 C C     . GLY A 1 331 ? 4.299  11.113  12.532  1.00 17.06 ?  337 GLY A C     1 
ATOM   2462 O O     . GLY A 1 331 ? 3.113  11.168  12.219  1.00 18.06 ?  337 GLY A O     1 
ATOM   2463 N N     . VAL A 1 332 ? 4.711  10.773  13.751  1.00 17.35 ?  338 VAL A N     1 
ATOM   2464 C CA    . VAL A 1 332 ? 3.761  10.555  14.844  1.00 17.94 ?  338 VAL A CA    1 
ATOM   2465 C C     . VAL A 1 332 ? 4.559  10.609  16.132  1.00 18.55 ?  338 VAL A C     1 
ATOM   2466 O O     . VAL A 1 332 ? 5.781  10.471  16.128  1.00 18.12 ?  338 VAL A O     1 
ATOM   2467 C CB    . VAL A 1 332 ? 2.991  9.216   14.683  1.00 19.40 ?  338 VAL A CB    1 
ATOM   2468 C CG1   . VAL A 1 332 ? 3.924  8.025   14.823  1.00 21.23 ?  338 VAL A CG1   1 
ATOM   2469 C CG2   . VAL A 1 332 ? 1.818  9.123   15.673  1.00 21.56 ?  338 VAL A CG2   1 
ATOM   2470 N N     . GLY A 1 333 ? 3.864  10.835  17.248  1.00 19.72 ?  339 GLY A N     1 
ATOM   2471 C CA    . GLY A 1 333 ? 4.532  10.841  18.529  1.00 20.53 ?  339 GLY A CA    1 
ATOM   2472 C C     . GLY A 1 333 ? 3.594  11.290  19.631  1.00 22.28 ?  339 GLY A C     1 
ATOM   2473 O O     . GLY A 1 333 ? 2.370  11.181  19.520  1.00 22.38 ?  339 GLY A O     1 
ATOM   2474 N N     . GLN A 1 334 ? 4.200  11.793  20.690  1.00 22.49 ?  340 GLN A N     1 
ATOM   2475 C CA    . GLN A 1 334 ? 3.460  12.224  21.855  1.00 24.64 ?  340 GLN A CA    1 
ATOM   2476 C C     . GLN A 1 334 ? 4.137  13.448  22.445  1.00 26.20 ?  340 GLN A C     1 
ATOM   2477 O O     . GLN A 1 334 ? 5.369  13.535  22.471  1.00 23.43 ?  340 GLN A O     1 
ATOM   2478 C CB    . GLN A 1 334 ? 3.370  11.113  22.907  1.00 26.41 ?  340 GLN A CB    1 
ATOM   2479 C CG    . GLN A 1 334 ? 4.700  10.552  23.366  1.00 25.25 ?  340 GLN A CG    1 
ATOM   2480 C CD    . GLN A 1 334 ? 4.507  9.374   24.311  1.00 31.25 ?  340 GLN A CD    1 
ATOM   2481 O OE1   . GLN A 1 334 ? 4.489  8.221   23.877  1.00 33.55 ?  340 GLN A OE1   1 
ATOM   2482 N NE2   . GLN A 1 334 ? 4.340  9.662   25.606  1.00 30.91 ?  340 GLN A NE2   1 
ATOM   2483 N N     . ILE A 1 335 ? 3.324  14.388  22.913  1.00 26.67 ?  341 ILE A N     1 
ATOM   2484 C CA    . ILE A 1 335 ? 3.812  15.595  23.560  1.00 28.46 ?  341 ILE A CA    1 
ATOM   2485 C C     . ILE A 1 335 ? 3.288  15.579  24.981  1.00 30.91 ?  341 ILE A C     1 
ATOM   2486 O O     . ILE A 1 335 ? 2.069  15.548  25.196  1.00 32.15 ?  341 ILE A O     1 
ATOM   2487 C CB    . ILE A 1 335 ? 3.389  16.863  22.803  1.00 29.94 ?  341 ILE A CB    1 
ATOM   2488 C CG1   . ILE A 1 335 ? 4.119  16.917  21.462  1.00 27.71 ?  341 ILE A CG1   1 
ATOM   2489 C CG2   . ILE A 1 335 ? 3.656  18.116  23.648  1.00 31.54 ?  341 ILE A CG2   1 
ATOM   2490 C CD1   . ILE A 1 335 ? 3.822  18.146  20.623  1.00 31.22 ?  341 ILE A CD1   1 
ATOM   2491 N N     . SER A 1 336 ? 4.209  15.542  25.948  1.00 30.05 ?  342 SER A N     1 
ATOM   2492 C CA    . SER A 1 336 ? 3.877  15.488  27.373  1.00 31.21 ?  342 SER A CA    1 
ATOM   2493 C C     . SER A 1 336 ? 2.851  14.404  27.681  1.00 34.83 ?  342 SER A C     1 
ATOM   2494 O O     . SER A 1 336 ? 1.934  14.597  28.482  1.00 33.75 ?  342 SER A O     1 
ATOM   2495 C CB    . SER A 1 336 ? 3.389  16.846  27.879  1.00 31.31 ?  342 SER A CB    1 
ATOM   2496 O OG    . SER A 1 336 ? 4.325  17.867  27.542  1.00 36.45 ?  342 SER A OG    1 
ATOM   2497 N N     . GLY A 1 337 ? 3.008  13.245  27.063  1.00 31.15 ?  343 GLY A N     1 
ATOM   2498 C CA    . GLY A 1 337 ? 2.238  12.108  27.512  1.00 34.23 ?  343 GLY A CA    1 
ATOM   2499 C C     . GLY A 1 337 ? 0.959  11.840  26.758  1.00 33.27 ?  343 GLY A C     1 
ATOM   2500 O O     . GLY A 1 337 ? 0.258  10.874  27.084  1.00 38.16 ?  343 GLY A O     1 
ATOM   2501 N N     . PHE A 1 338 ? 0.632  12.633  25.749  1.00 33.30 ?  344 PHE A N     1 
ATOM   2502 C CA    . PHE A 1 338 ? -0.506 12.293  24.914  1.00 34.89 ?  344 PHE A CA    1 
ATOM   2503 C C     . PHE A 1 338 ? -0.141 12.329  23.437  1.00 30.14 ?  344 PHE A C     1 
ATOM   2504 O O     . PHE A 1 338 ? 0.783  13.032  23.008  1.00 29.02 ?  344 PHE A O     1 
ATOM   2505 C CB    . PHE A 1 338 ? -1.675 13.220  25.166  1.00 37.96 ?  344 PHE A CB    1 
ATOM   2506 C CG    . PHE A 1 338 ? -1.298 14.649  25.151  1.00 36.27 ?  344 PHE A CG    1 
ATOM   2507 C CD1   . PHE A 1 338 ? -0.992 15.282  23.956  1.00 33.13 ?  344 PHE A CD1   1 
ATOM   2508 C CD2   . PHE A 1 338 ? -1.245 15.361  26.338  1.00 33.24 ?  344 PHE A CD2   1 
ATOM   2509 C CE1   . PHE A 1 338 ? -0.646 16.602  23.940  1.00 38.08 ?  344 PHE A CE1   1 
ATOM   2510 C CE2   . PHE A 1 338 ? -0.902 16.678  26.337  1.00 33.76 ?  344 PHE A CE2   1 
ATOM   2511 C CZ    . PHE A 1 338 ? -0.605 17.307  25.134  1.00 34.82 ?  344 PHE A CZ    1 
ATOM   2512 N N     . TYR A 1 339 ? -0.947 11.590  22.672  1.00 29.91 ?  345 TYR A N     1 
ATOM   2513 C CA    . TYR A 1 339 ? -0.738 11.368  21.248  1.00 26.97 ?  345 TYR A CA    1 
ATOM   2514 C C     . TYR A 1 339 ? -0.857 12.656  20.448  1.00 26.88 ?  345 TYR A C     1 
ATOM   2515 O O     . TYR A 1 339 ? -1.815 13.417  20.609  1.00 26.53 ?  345 TYR A O     1 
ATOM   2516 C CB    . TYR A 1 339 ? -1.778 10.362  20.762  1.00 27.85 ?  345 TYR A CB    1 
ATOM   2517 C CG    . TYR A 1 339 ? -1.721 9.981   19.300  1.00 28.02 ?  345 TYR A CG    1 
ATOM   2518 C CD1   . TYR A 1 339 ? -2.255 10.809  18.310  1.00 25.72 ?  345 TYR A CD1   1 
ATOM   2519 C CD2   . TYR A 1 339 ? -1.188 8.757   18.912  1.00 29.58 ?  345 TYR A CD2   1 
ATOM   2520 C CE1   . TYR A 1 339 ? -2.217 10.434  16.971  1.00 25.61 ?  345 TYR A CE1   1 
ATOM   2521 C CE2   . TYR A 1 339 ? -1.150 8.380   17.588  1.00 28.14 ?  345 TYR A CE2   1 
ATOM   2522 C CZ    . TYR A 1 339 ? -1.664 9.213   16.622  1.00 26.28 ?  345 TYR A CZ    1 
ATOM   2523 O OH    . TYR A 1 339 ? -1.609 8.809   15.301  1.00 25.58 ?  345 TYR A OH    1 
ATOM   2524 N N     . VAL A 1 340 ? 0.089  12.866  19.536  1.00 23.54 ?  346 VAL A N     1 
ATOM   2525 C CA    . VAL A 1 340 ? -0.011 13.921  18.541  1.00 23.51 ?  346 VAL A CA    1 
ATOM   2526 C C     . VAL A 1 340 ? 0.130  13.301  17.155  1.00 24.12 ?  346 VAL A C     1 
ATOM   2527 O O     . VAL A 1 340 ? 0.931  12.377  16.939  1.00 22.01 ?  346 VAL A O     1 
ATOM   2528 C CB    . VAL A 1 340 ? 1.031  15.034  18.786  1.00 24.35 ?  346 VAL A CB    1 
ATOM   2529 C CG1   . VAL A 1 340 ? 0.756  15.726  20.132  1.00 24.16 ?  346 VAL A CG1   1 
ATOM   2530 C CG2   . VAL A 1 340 ? 2.446  14.479  18.750  1.00 23.13 ?  346 VAL A CG2   1 
ATOM   2531 N N     . GLY A 1 341 ? -0.647 13.815  16.209  1.00 23.35 ?  347 GLY A N     1 
ATOM   2532 C CA    . GLY A 1 341 ? -0.796 13.189  14.913  1.00 21.66 ?  347 GLY A CA    1 
ATOM   2533 C C     . GLY A 1 341 ? 0.251  13.598  13.895  1.00 22.35 ?  347 GLY A C     1 
ATOM   2534 O O     . GLY A 1 341 ? 1.278  14.206  14.203  1.00 21.16 ?  347 GLY A O     1 
ATOM   2535 N N     . ARG A 1 342 ? -0.049 13.273  12.639  1.00 20.18 ?  348 ARG A N     1 
ATOM   2536 C CA    . ARG A 1 342 ? 0.945  13.336  11.574  1.00 19.10 ?  348 ARG A CA    1 
ATOM   2537 C C     . ARG A 1 342 ? 1.175  14.762  11.095  1.00 17.12 ?  348 ARG A C     1 
ATOM   2538 O O     . ARG A 1 342 ? 2.323  15.156  10.845  1.00 16.98 ?  348 ARG A O     1 
ATOM   2539 C CB    . ARG A 1 342 ? 0.506  12.420  10.434  1.00 18.02 ?  348 ARG A CB    1 
ATOM   2540 C CG    . ARG A 1 342 ? 0.197  11.027  10.958  1.00 21.22 ?  348 ARG A CG    1 
ATOM   2541 C CD    . ARG A 1 342 ? -0.713 10.243  10.054  1.00 22.68 ?  348 ARG A CD    1 
ATOM   2542 N NE    . ARG A 1 342 ? -0.025 9.844   8.835   1.00 20.80 ?  348 ARG A NE    1 
ATOM   2543 C CZ    . ARG A 1 342 ? -0.578 9.110   7.882   1.00 24.17 ?  348 ARG A CZ    1 
ATOM   2544 N NH1   . ARG A 1 342 ? -1.838 8.710   7.966   1.00 24.01 ?  348 ARG A NH1   1 
ATOM   2545 N NH2   . ARG A 1 342 ? 0.145  8.778   6.816   1.00 24.56 ?  348 ARG A NH2   1 
ATOM   2546 N N     . LEU A 1 343 ? 0.108  15.546  10.956  1.00 17.55 ?  349 LEU A N     1 
ATOM   2547 C CA    . LEU A 1 343 ? 0.283  16.954  10.632  1.00 19.57 ?  349 LEU A CA    1 
ATOM   2548 C C     . LEU A 1 343 ? 1.120  17.647  11.697  1.00 19.96 ?  349 LEU A C     1 
ATOM   2549 O O     . LEU A 1 343 ? 2.046  18.398  11.372  1.00 17.19 ?  349 LEU A O     1 
ATOM   2550 C CB    . LEU A 1 343 ? -1.074 17.645  10.478  1.00 20.24 ?  349 LEU A CB    1 
ATOM   2551 C CG    . LEU A 1 343 ? -1.059 19.187  10.379  1.00 21.21 ?  349 LEU A CG    1 
ATOM   2552 C CD1   . LEU A 1 343 ? -0.310 19.703  9.155   1.00 26.34 ?  349 LEU A CD1   1 
ATOM   2553 C CD2   . LEU A 1 343 ? -2.453 19.730  10.359  1.00 24.66 ?  349 LEU A CD2   1 
ATOM   2554 N N     . MET A 1 344 ? 0.826  17.379  12.978  1.00 20.02 ?  350 MET A N     1 
ATOM   2555 C CA    . MET A 1 344 ? 1.539  18.043  14.062  1.00 19.28 ?  350 MET A CA    1 
ATOM   2556 C C     . MET A 1 344 ? 3.026  17.714  14.025  1.00 17.92 ?  350 MET A C     1 
ATOM   2557 O O     . MET A 1 344 ? 3.875  18.607  14.100  1.00 17.69 ?  350 MET A O     1 
ATOM   2558 C CB    . MET A 1 344 ? 0.929  17.638  15.402  1.00 22.59 ?  350 MET A CB    1 
ATOM   2559 C CG    . MET A 1 344 ? 1.572  18.314  16.592  1.00 23.40 ?  350 MET A CG    1 
ATOM   2560 S SD    . MET A 1 344 ? 1.414  20.115  16.416  1.00 37.56 ?  350 MET A SD    1 
ATOM   2561 C CE    . MET A 1 344 ? 2.026  20.694  18.008  1.00 37.55 ?  350 MET A CE    1 
ATOM   2562 N N     . VAL A 1 345 ? 3.356  16.428  13.907  1.00 17.50 ?  351 VAL A N     1 
ATOM   2563 C CA    . VAL A 1 345 ? 4.750  16.014  13.903  1.00 17.11 ?  351 VAL A CA    1 
ATOM   2564 C C     . VAL A 1 345 ? 5.465  16.527  12.654  1.00 16.29 ?  351 VAL A C     1 
ATOM   2565 O O     . VAL A 1 345 ? 6.611  16.997  12.733  1.00 15.51 ?  351 VAL A O     1 
ATOM   2566 C CB    . VAL A 1 345 ? 4.846  14.481  14.036  1.00 19.38 ?  351 VAL A CB    1 
ATOM   2567 C CG1   . VAL A 1 345 ? 6.302  14.030  13.949  1.00 17.48 ?  351 VAL A CG1   1 
ATOM   2568 C CG2   . VAL A 1 345 ? 4.228  14.018  15.379  1.00 19.00 ?  351 VAL A CG2   1 
ATOM   2569 N N     . ARG A 1 346 ? 4.807  16.452  11.487  1.00 15.47 ?  352 ARG A N     1 
ATOM   2570 C CA    . ARG A 1 346 ? 5.398  17.006  10.271  1.00 18.14 ?  352 ARG A CA    1 
ATOM   2571 C C     . ARG A 1 346 ? 5.783  18.467  10.469  1.00 16.74 ?  352 ARG A C     1 
ATOM   2572 O O     . ARG A 1 346 ? 6.919  18.856  10.190  1.00 15.95 ?  352 ARG A O     1 
ATOM   2573 C CB    . ARG A 1 346 ? 4.442  16.859  9.076   1.00 15.95 ?  352 ARG A CB    1 
ATOM   2574 C CG    . ARG A 1 346 ? 4.998  17.426  7.789   1.00 16.68 ?  352 ARG A CG    1 
ATOM   2575 C CD    . ARG A 1 346 ? 4.142  17.092  6.555   1.00 16.99 ?  352 ARG A CD    1 
ATOM   2576 N NE    . ARG A 1 346 ? 2.763  17.558  6.677   1.00 17.20 ?  352 ARG A NE    1 
ATOM   2577 C CZ    . ARG A 1 346 ? 1.698  16.765  6.715   1.00 18.08 ?  352 ARG A CZ    1 
ATOM   2578 N NH1   . ARG A 1 346 ? 1.806  15.443  6.631   1.00 16.69 ?  352 ARG A NH1   1 
ATOM   2579 N NH2   . ARG A 1 346 ? 0.493  17.308  6.818   1.00 18.09 ?  352 ARG A NH2   1 
ATOM   2580 N N     . LEU A 1 347 ? 4.859  19.286  10.985  1.00 16.37 ?  353 LEU A N     1 
ATOM   2581 C CA    . LEU A 1 347 ? 5.156  20.707  11.168  1.00 19.12 ?  353 LEU A CA    1 
ATOM   2582 C C     . LEU A 1 347 ? 6.178  20.941  12.277  1.00 18.50 ?  353 LEU A C     1 
ATOM   2583 O O     . LEU A 1 347 ? 7.058  21.793  12.133  1.00 19.05 ?  353 LEU A O     1 
ATOM   2584 C CB    . LEU A 1 347 ? 3.879  21.494  11.469  1.00 18.99 ?  353 LEU A CB    1 
ATOM   2585 C CG    . LEU A 1 347 ? 2.891  21.642  10.309  1.00 25.84 ?  353 LEU A CG    1 
ATOM   2586 C CD1   . LEU A 1 347 ? 1.819  22.664  10.652  1.00 26.61 ?  353 LEU A CD1   1 
ATOM   2587 C CD2   . LEU A 1 347 ? 3.627  22.016  8.990   1.00 29.03 ?  353 LEU A CD2   1 
ATOM   2588 N N     . THR A 1 348 ? 6.076  20.211  13.396  1.00 16.78 ?  354 THR A N     1 
ATOM   2589 C CA    . THR A 1 348 ? 6.976  20.465  14.519  1.00 16.95 ?  354 THR A CA    1 
ATOM   2590 C C     . THR A 1 348 ? 8.381  19.918  14.270  1.00 18.96 ?  354 THR A C     1 
ATOM   2591 O O     . THR A 1 348 ? 9.374  20.588  14.588  1.00 16.57 ?  354 THR A O     1 
ATOM   2592 C CB    . THR A 1 348 ? 6.410  19.853  15.794  1.00 18.44 ?  354 THR A CB    1 
ATOM   2593 O OG1   . THR A 1 348 ? 5.030  20.198  15.904  1.00 18.51 ?  354 THR A OG1   1 
ATOM   2594 C CG2   . THR A 1 348 ? 7.149  20.371  17.019  1.00 18.35 ?  354 THR A CG2   1 
ATOM   2595 N N     . LYS A 1 349 ? 8.492  18.701  13.728  1.00 14.57 ?  355 LYS A N     1 
ATOM   2596 C CA    . LYS A 1 349 ? 9.789  18.042  13.591  1.00 16.16 ?  355 LYS A CA    1 
ATOM   2597 C C     . LYS A 1 349 ? 10.181 17.706  12.157  1.00 16.85 ?  355 LYS A C     1 
ATOM   2598 O O     . LYS A 1 349 ? 11.297 18.043  11.741  1.00 13.34 ?  355 LYS A O     1 
ATOM   2599 C CB    . LYS A 1 349 ? 9.833  16.746  14.410  1.00 14.05 ?  355 LYS A CB    1 
ATOM   2600 C CG    . LYS A 1 349 ? 11.175 16.009  14.224  1.00 16.97 ?  355 LYS A CG    1 
ATOM   2601 C CD    . LYS A 1 349 ? 11.381 14.888  15.216  1.00 17.16 ?  355 LYS A CD    1 
ATOM   2602 C CE    . LYS A 1 349 ? 12.666 14.134  14.921  1.00 19.49 ?  355 LYS A CE    1 
ATOM   2603 N NZ    . LYS A 1 349 ? 12.894 13.047  15.892  1.00 22.86 ?  355 LYS A NZ    1 
ATOM   2604 N N     . SER A 1 350 ? 9.321  17.011  11.398  1.00 13.66 ?  356 SER A N     1 
ATOM   2605 C CA    . SER A 1 350 ? 9.790  16.331  10.186  1.00 17.22 ?  356 SER A CA    1 
ATOM   2606 C C     . SER A 1 350 ? 10.332 17.295  9.132   1.00 15.93 ?  356 SER A C     1 
ATOM   2607 O O     . SER A 1 350 ? 11.236 16.929  8.374   1.00 13.91 ?  356 SER A O     1 
ATOM   2608 C CB    . SER A 1 350 ? 8.671  15.483  9.573   1.00 15.99 ?  356 SER A CB    1 
ATOM   2609 O OG    . SER A 1 350 ? 8.144  14.578  10.519  1.00 13.53 ?  356 SER A OG    1 
ATOM   2610 N N     . ARG A 1 351 ? 9.777  18.504  9.028   1.00 20.04 ?  357 ARG A N     1 
ATOM   2611 C CA    . ARG A 1 351 ? 10.193 19.404  7.947   1.00 19.04 ?  357 ARG A CA    1 
ATOM   2612 C C     . ARG A 1 351 ? 11.608 19.928  8.153   1.00 19.88 ?  357 ARG A C     1 
ATOM   2613 O O     . ARG A 1 351 ? 12.433 19.848  7.233   1.00 18.80 ?  357 ARG A O     1 
ATOM   2614 C CB    . ARG A 1 351 ? 9.205  20.564  7.788   1.00 21.69 ?  357 ARG A CB    1 
ATOM   2615 C CG    . ARG A 1 351 ? 7.941  20.158  7.065   1.00 25.44 ?  357 ARG A CG    1 
ATOM   2616 C CD    . ARG A 1 351 ? 6.970  21.319  6.833   1.00 32.33 ?  357 ARG A CD    1 
ATOM   2617 N NE    . ARG A 1 351 ? 7.282  22.100  5.641   1.00 36.18 ?  357 ARG A NE    1 
ATOM   2618 C CZ    . ARG A 1 351 ? 8.092  23.152  5.628   1.00 36.22 ?  357 ARG A CZ    1 
ATOM   2619 N NH1   . ARG A 1 351 ? 8.709  23.567  6.729   1.00 37.10 ?  357 ARG A NH1   1 
ATOM   2620 N NH2   . ARG A 1 351 ? 8.280  23.812  4.486   1.00 34.75 ?  357 ARG A NH2   1 
ATOM   2621 N N     . ASP A 1 352 ? 11.909 20.494  9.336   1.00 15.77 ?  358 ASP A N     1 
ATOM   2622 C CA    . ASP A 1 352 ? 13.193 21.148  9.572   1.00 18.51 ?  358 ASP A CA    1 
ATOM   2623 C C     . ASP A 1 352 ? 14.090 20.419  10.562  1.00 18.72 ?  358 ASP A C     1 
ATOM   2624 O O     . ASP A 1 352 ? 15.266 20.786  10.674  1.00 15.02 ?  358 ASP A O     1 
ATOM   2625 C CB    . ASP A 1 352 ? 12.982 22.596  10.074  1.00 21.69 ?  358 ASP A CB    1 
ATOM   2626 C CG    . ASP A 1 352 ? 14.322 23.413  10.180  1.00 30.29 ?  358 ASP A CG    1 
ATOM   2627 O OD1   . ASP A 1 352 ? 15.023 23.542  9.134   1.00 35.22 ?  358 ASP A OD1   1 
ATOM   2628 O OD2   . ASP A 1 352 ? 14.672 23.940  11.294  1.00 29.75 -1 358 ASP A OD2   1 
ATOM   2629 N N     . LEU A 1 353 ? 13.567 19.425  11.294  1.00 15.65 ?  359 LEU A N     1 
ATOM   2630 C CA    . LEU A 1 353 ? 14.348 18.610  12.250  1.00 16.13 ?  359 LEU A CA    1 
ATOM   2631 C C     . LEU A 1 353 ? 15.099 19.472  13.265  1.00 15.81 ?  359 LEU A C     1 
ATOM   2632 O O     . LEU A 1 353 ? 16.214 19.139  13.693  1.00 12.64 ?  359 LEU A O     1 
ATOM   2633 C CB    . LEU A 1 353 ? 15.313 17.671  11.512  1.00 15.26 ?  359 LEU A CB    1 
ATOM   2634 C CG    . LEU A 1 353 ? 14.620 16.629  10.636  1.00 16.90 ?  359 LEU A CG    1 
ATOM   2635 C CD1   . LEU A 1 353 ? 15.568 16.086  9.592   1.00 17.71 ?  359 LEU A CD1   1 
ATOM   2636 C CD2   . LEU A 1 353 ? 14.062 15.490  11.493  1.00 15.37 ?  359 LEU A CD2   1 
ATOM   2637 N N     . PHE A 1 354 ? 14.500 20.606  13.623  1.00 15.96 ?  360 PHE A N     1 
ATOM   2638 C CA    . PHE A 1 354 ? 15.005 21.549  14.621  1.00 20.20 ?  360 PHE A CA    1 
ATOM   2639 C C     . PHE A 1 354 ? 16.344 22.175  14.239  1.00 16.77 ?  360 PHE A C     1 
ATOM   2640 O O     . PHE A 1 354 ? 16.997 22.781  15.091  1.00 16.65 ?  360 PHE A O     1 
ATOM   2641 C CB    . PHE A 1 354 ? 15.102 20.897  16.015  1.00 19.08 ?  360 PHE A CB    1 
ATOM   2642 C CG    . PHE A 1 354 ? 13.853 20.177  16.427  1.00 18.76 ?  360 PHE A CG    1 
ATOM   2643 C CD1   . PHE A 1 354 ? 12.669 20.865  16.590  1.00 19.16 ?  360 PHE A CD1   1 
ATOM   2644 C CD2   . PHE A 1 354 ? 13.864 18.806  16.643  1.00 19.23 ?  360 PHE A CD2   1 
ATOM   2645 C CE1   . PHE A 1 354 ? 11.510 20.190  16.969  1.00 21.27 ?  360 PHE A CE1   1 
ATOM   2646 C CE2   . PHE A 1 354 ? 12.707 18.114  17.018  1.00 18.22 ?  360 PHE A CE2   1 
ATOM   2647 C CZ    . PHE A 1 354 ? 11.530 18.797  17.166  1.00 19.59 ?  360 PHE A CZ    1 
ATOM   2648 N N     . VAL A 1 355 ? 16.742 22.088  12.967  1.00 18.29 ?  361 VAL A N     1 
ATOM   2649 C CA    . VAL A 1 355 ? 18.089 22.502  12.565  1.00 19.10 ?  361 VAL A CA    1 
ATOM   2650 C C     . VAL A 1 355 ? 18.333 23.980  12.886  1.00 18.22 ?  361 VAL A C     1 
ATOM   2651 O O     . VAL A 1 355 ? 19.414 24.351  13.358  1.00 17.31 ?  361 VAL A O     1 
ATOM   2652 C CB    . VAL A 1 355 ? 18.332 22.184  11.075  1.00 18.80 ?  361 VAL A CB    1 
ATOM   2653 C CG1   . VAL A 1 355 ? 19.571 22.902  10.553  1.00 18.33 ?  361 VAL A CG1   1 
ATOM   2654 C CG2   . VAL A 1 355 ? 18.468 20.649  10.843  1.00 15.66 ?  361 VAL A CG2   1 
ATOM   2655 N N     . SER A 1 356 ? 17.335 24.843  12.665  1.00 19.90 ?  362 SER A N     1 
ATOM   2656 C CA    . SER A 1 356 ? 17.557 26.275  12.861  1.00 19.56 ?  362 SER A CA    1 
ATOM   2657 C C     . SER A 1 356 ? 17.902 26.619  14.313  1.00 20.21 ?  362 SER A C     1 
ATOM   2658 O O     . SER A 1 356 ? 18.609 27.607  14.559  1.00 18.16 ?  362 SER A O     1 
ATOM   2659 C CB    . SER A 1 356 ? 16.323 27.058  12.418  1.00 22.88 ?  362 SER A CB    1 
ATOM   2660 O OG    . SER A 1 356 ? 15.209 26.700  13.240  1.00 32.08 ?  362 SER A OG    1 
ATOM   2661 N N     . THR A 1 357 ? 17.415 25.836  15.290  1.00 20.74 ?  363 THR A N     1 
ATOM   2662 C CA    . THR A 1 357 ? 17.650 26.197  16.692  1.00 22.19 ?  363 THR A CA    1 
ATOM   2663 C C     . THR A 1 357 ? 19.124 26.090  17.063  1.00 20.68 ?  363 THR A C     1 
ATOM   2664 O O     . THR A 1 357 ? 19.584 26.798  17.972  1.00 20.50 ?  363 THR A O     1 
ATOM   2665 C CB    . THR A 1 357 ? 16.817 25.328  17.658  1.00 25.17 ?  363 THR A CB    1 
ATOM   2666 O OG1   . THR A 1 357 ? 17.341 23.982  17.708  1.00 24.18 ?  363 THR A OG1   1 
ATOM   2667 C CG2   . THR A 1 357 ? 15.324 25.305  17.264  1.00 21.77 ?  363 THR A CG2   1 
ATOM   2668 N N     . SER A 1 358 ? 19.867 25.212  16.391  1.00 17.06 ?  364 SER A N     1 
ATOM   2669 C CA    . SER A 1 358 ? 21.291 25.055  16.667  1.00 19.65 ?  364 SER A CA    1 
ATOM   2670 C C     . SER A 1 358 ? 22.103 26.181  16.047  1.00 19.13 ?  364 SER A C     1 
ATOM   2671 O O     . SER A 1 358 ? 23.013 26.714  16.689  1.00 18.66 ?  364 SER A O     1 
ATOM   2672 C CB    . SER A 1 358 ? 21.804 23.710  16.153  1.00 18.48 ?  364 SER A CB    1 
ATOM   2673 O OG    . SER A 1 358 ? 21.236 22.631  16.867  1.00 18.71 ?  364 SER A OG    1 
ATOM   2674 N N     . TRP A 1 359 ? 21.801 26.548  14.799  1.00 18.53 ?  365 TRP A N     1 
ATOM   2675 C CA    . TRP A 1 359 ? 22.444 27.721  14.214  1.00 17.71 ?  365 TRP A CA    1 
ATOM   2676 C C     . TRP A 1 359 ? 22.162 28.968  15.046  1.00 19.87 ?  365 TRP A C     1 
ATOM   2677 O O     . TRP A 1 359 ? 23.057 29.795  15.257  1.00 20.79 ?  365 TRP A O     1 
ATOM   2678 C CB    . TRP A 1 359 ? 21.990 27.893  12.762  1.00 18.92 ?  365 TRP A CB    1 
ATOM   2679 C CG    . TRP A 1 359 ? 22.540 26.807  11.905  1.00 17.47 ?  365 TRP A CG    1 
ATOM   2680 C CD1   . TRP A 1 359 ? 21.915 25.645  11.546  1.00 18.57 ?  365 TRP A CD1   1 
ATOM   2681 C CD2   . TRP A 1 359 ? 23.857 26.741  11.349  1.00 17.86 ?  365 TRP A CD2   1 
ATOM   2682 N NE1   . TRP A 1 359 ? 22.752 24.877  10.772  1.00 15.92 ?  365 TRP A NE1   1 
ATOM   2683 C CE2   . TRP A 1 359 ? 23.956 25.521  10.646  1.00 18.23 ?  365 TRP A CE2   1 
ATOM   2684 C CE3   . TRP A 1 359 ? 24.954 27.603  11.357  1.00 17.54 ?  365 TRP A CE3   1 
ATOM   2685 C CZ2   . TRP A 1 359 ? 25.117 25.142  9.959   1.00 17.80 ?  365 TRP A CZ2   1 
ATOM   2686 C CZ3   . TRP A 1 359 ? 26.105 27.220  10.686  1.00 18.06 ?  365 TRP A CZ3   1 
ATOM   2687 C CH2   . TRP A 1 359 ? 26.176 26.002  9.995   1.00 17.34 ?  365 TRP A CH2   1 
ATOM   2688 N N     . LYS A 1 360 ? 20.938 29.106  15.568  1.00 20.70 ?  366 LYS A N     1 
ATOM   2689 C CA    . LYS A 1 360 ? 20.640 30.257  16.421  1.00 22.18 ?  366 LYS A CA    1 
ATOM   2690 C C     . LYS A 1 360 ? 21.480 30.222  17.701  1.00 21.66 ?  366 LYS A C     1 
ATOM   2691 O O     . LYS A 1 360 ? 22.124 31.215  18.062  1.00 22.77 ?  366 LYS A O     1 
ATOM   2692 C CB    . LYS A 1 360 ? 19.145 30.301  16.741  1.00 22.54 ?  366 LYS A CB    1 
ATOM   2693 C CG    . LYS A 1 360 ? 18.725 31.541  17.518  1.00 30.46 ?  366 LYS A CG    1 
ATOM   2694 C CD    . LYS A 1 360 ? 17.255 31.461  17.995  1.00 32.93 ?  366 LYS A CD    1 
ATOM   2695 C CE    . LYS A 1 360 ? 16.820 32.734  18.711  1.00 41.81 ?  366 LYS A CE    1 
ATOM   2696 N NZ    . LYS A 1 360 ? 15.446 32.602  19.342  1.00 52.55 ?  366 LYS A NZ    1 
ATOM   2697 N N     . THR A 1 361 ? 21.509 29.075  18.387  1.00 18.59 ?  367 THR A N     1 
ATOM   2698 C CA    . THR A 1 361 ? 22.320 28.958  19.596  1.00 23.03 ?  367 THR A CA    1 
ATOM   2699 C C     . THR A 1 361 ? 23.766 29.352  19.323  1.00 23.35 ?  367 THR A C     1 
ATOM   2700 O O     . THR A 1 361 ? 24.371 30.107  20.097  1.00 23.05 ?  367 THR A O     1 
ATOM   2701 C CB    . THR A 1 361 ? 22.244 27.525  20.161  1.00 22.71 ?  367 THR A CB    1 
ATOM   2702 O OG1   . THR A 1 361 ? 20.924 27.261  20.669  1.00 22.61 ?  367 THR A OG1   1 
ATOM   2703 C CG2   . THR A 1 361 ? 23.242 27.320  21.307  1.00 22.37 ?  367 THR A CG2   1 
ATOM   2704 N N     . MET A 1 362 ? 24.328 28.875  18.211  1.00 21.08 ?  368 MET A N     1 
ATOM   2705 C CA    . MET A 1 362 ? 25.712 29.159  17.842  1.00 21.35 ?  368 MET A CA    1 
ATOM   2706 C C     . MET A 1 362 ? 25.889 30.525  17.206  1.00 23.26 ?  368 MET A C     1 
ATOM   2707 O O     . MET A 1 362 ? 27.020 30.883  16.864  1.00 21.72 ?  368 MET A O     1 
ATOM   2708 C CB    . MET A 1 362 ? 26.233 28.079  16.888  1.00 19.55 ?  368 MET A CB    1 
ATOM   2709 C CG    . MET A 1 362 ? 26.250 26.686  17.526  1.00 19.58 ?  368 MET A CG    1 
ATOM   2710 S SD    . MET A 1 362 ? 27.486 26.529  18.831  1.00 19.28 ?  368 MET A SD    1 
ATOM   2711 C CE    . MET A 1 362 ? 28.959 26.351  17.809  1.00 16.46 ?  368 MET A CE    1 
ATOM   2712 N N     . ARG A 1 363 ? 24.810 31.286  17.044  1.00 22.38 ?  369 ARG A N     1 
ATOM   2713 C CA    . ARG A 1 363 ? 24.868 32.611  16.431  1.00 23.40 ?  369 ARG A CA    1 
ATOM   2714 C C     . ARG A 1 363 ? 25.672 32.571  15.135  1.00 24.10 ?  369 ARG A C     1 
ATOM   2715 O O     . ARG A 1 363 ? 26.591 33.365  14.894  1.00 24.21 ?  369 ARG A O     1 
ATOM   2716 C CB    . ARG A 1 363 ? 25.416 33.640  17.419  1.00 26.69 ?  369 ARG A CB    1 
ATOM   2717 C CG    . ARG A 1 363 ? 24.379 33.997  18.483  1.00 27.12 ?  369 ARG A CG    1 
ATOM   2718 C CD    . ARG A 1 363 ? 24.949 34.796  19.636  1.00 38.64 ?  369 ARG A CD    1 
ATOM   2719 N NE    . ARG A 1 363 ? 25.913 33.992  20.379  1.00 42.50 ?  369 ARG A NE    1 
ATOM   2720 C CZ    . ARG A 1 363 ? 27.229 34.141  20.312  1.00 40.98 ?  369 ARG A CZ    1 
ATOM   2721 N NH1   . ARG A 1 363 ? 27.782 35.115  19.597  1.00 46.06 ?  369 ARG A NH1   1 
ATOM   2722 N NH2   . ARG A 1 363 ? 28.012 33.291  20.974  1.00 35.76 ?  369 ARG A NH2   1 
ATOM   2723 N N     . GLN A 1 364 ? 25.337 31.593  14.307  1.00 23.01 ?  370 GLN A N     1 
ATOM   2724 C CA    . GLN A 1 364 ? 25.881 31.482  12.967  1.00 22.70 ?  370 GLN A CA    1 
ATOM   2725 C C     . GLN A 1 364 ? 24.728 31.259  11.998  1.00 22.26 ?  370 GLN A C     1 
ATOM   2726 O O     . GLN A 1 364 ? 23.611 30.908  12.390  1.00 22.97 ?  370 GLN A O     1 
ATOM   2727 C CB    . GLN A 1 364 ? 26.904 30.342  12.858  1.00 19.90 ?  370 GLN A CB    1 
ATOM   2728 C CG    . GLN A 1 364 ? 28.229 30.590  13.548  1.00 20.59 ?  370 GLN A CG    1 
ATOM   2729 C CD    . GLN A 1 364 ? 29.151 29.398  13.421  1.00 20.52 ?  370 GLN A CD    1 
ATOM   2730 O OE1   . GLN A 1 364 ? 29.397 28.902  12.317  1.00 20.38 ?  370 GLN A OE1   1 
ATOM   2731 N NE2   . GLN A 1 364 ? 29.644 28.910  14.550  1.00 19.34 ?  370 GLN A NE2   1 
ATOM   2732 N N     . SER A 1 365 ? 25.015 31.478  10.730  1.00 22.97 ?  371 SER A N     1 
ATOM   2733 C CA    . SER A 1 365 ? 24.075 31.310  9.650   1.00 24.06 ?  371 SER A CA    1 
ATOM   2734 C C     . SER A 1 365 ? 24.518 30.151  8.770   1.00 24.23 ?  371 SER A C     1 
ATOM   2735 O O     . SER A 1 365 ? 25.698 30.080  8.386   1.00 24.34 ?  371 SER A O     1 
ATOM   2736 C CB    . SER A 1 365 ? 23.980 32.601  8.826   1.00 26.33 ?  371 SER A CB    1 
ATOM   2737 O OG    . SER A 1 365 ? 23.303 33.628  9.552   1.00 29.69 ?  371 SER A OG    1 
ATOM   2738 N N     . PRO A 1 366 ? 23.619 29.229  8.442   1.00 22.92 ?  372 PRO A N     1 
ATOM   2739 C CA    . PRO A 1 366 ? 24.021 28.024  7.719   1.00 23.89 ?  372 PRO A CA    1 
ATOM   2740 C C     . PRO A 1 366 ? 24.481 28.358  6.313   1.00 26.96 ?  372 PRO A C     1 
ATOM   2741 O O     . PRO A 1 366 ? 24.103 29.395  5.742   1.00 29.52 ?  372 PRO A O     1 
ATOM   2742 C CB    . PRO A 1 366 ? 22.745 27.162  7.719   1.00 24.55 ?  372 PRO A CB    1 
ATOM   2743 C CG    . PRO A 1 366 ? 21.630 28.089  8.024   1.00 23.90 ?  372 PRO A CG    1 
ATOM   2744 C CD    . PRO A 1 366 ? 22.212 29.184  8.875   1.00 24.03 ?  372 PRO A CD    1 
ATOM   2745 N N     . PRO A 1 367 ? 25.349 27.528  5.729   1.00 29.77 ?  373 PRO A N     1 
ATOM   2746 C CA    . PRO A 1 367 ? 25.821 27.820  4.377   1.00 31.90 ?  373 PRO A CA    1 
ATOM   2747 C C     . PRO A 1 367 ? 24.788 27.329  3.351   1.00 37.39 ?  373 PRO A C     1 
ATOM   2748 O O     . PRO A 1 367 ? 23.942 26.481  3.686   1.00 40.16 ?  373 PRO A O     1 
ATOM   2749 C CB    . PRO A 1 367 ? 27.135 27.040  4.288   1.00 31.76 ?  373 PRO A CB    1 
ATOM   2750 C CG    . PRO A 1 367 ? 26.910 25.849  5.207   1.00 28.80 ?  373 PRO A CG    1 
ATOM   2751 C CD    . PRO A 1 367 ? 25.950 26.304  6.290   1.00 27.22 ?  373 PRO A CD    1 
ATOM   2752 O OXT   . PRO A 1 367 ? 24.742 27.769  2.194   1.00 43.29 -1 373 PRO A OXT   1 
HETATM 2753 S S     . SO4 B 2 .   ? -3.675 13.130  11.730  1.00 31.97 ?  401 SO4 A S     1 
HETATM 2754 O O1    . SO4 B 2 .   ? -3.034 14.423  11.407  1.00 23.59 ?  401 SO4 A O1    1 
HETATM 2755 O O2    . SO4 B 2 .   ? -3.996 12.425  10.490  1.00 31.69 ?  401 SO4 A O2    1 
HETATM 2756 O O3    . SO4 B 2 .   ? -2.821 12.252  12.535  1.00 24.36 -1 401 SO4 A O3    1 
HETATM 2757 O O4    . SO4 B 2 .   ? -4.931 13.399  12.430  1.00 34.52 ?  401 SO4 A O4    1 
HETATM 2758 N N1    . 6FA C 3 .   ? 16.362 14.487  20.872  1.00 23.12 ?  402 6FA A N1    1 
HETATM 2759 C C2    . 6FA C 3 .   ? 15.372 15.400  21.029  1.00 22.59 ?  402 6FA A C2    1 
HETATM 2760 O O2    . 6FA C 3 .   ? 15.303 16.095  22.039  1.00 23.74 ?  402 6FA A O2    1 
HETATM 2761 N N3    . 6FA C 3 .   ? 14.378 15.547  20.124  1.00 22.16 ?  402 6FA A N3    1 
HETATM 2762 C C4    . 6FA C 3 .   ? 14.334 14.807  18.972  1.00 20.81 ?  402 6FA A C4    1 
HETATM 2763 O O4    . 6FA C 3 .   ? 13.422 14.981  18.178  1.00 17.24 ?  402 6FA A O4    1 
HETATM 2764 C C4A   . 6FA C 3 .   ? 15.387 13.902  18.730  1.00 22.60 ?  402 6FA A C4A   1 
HETATM 2765 N N5    . 6FA C 3 .   ? 15.385 13.224  17.608  1.00 20.83 ?  402 6FA A N5    1 
HETATM 2766 C C5A   . 6FA C 3 .   ? 16.428 12.405  17.358  1.00 22.48 ?  402 6FA A C5A   1 
HETATM 2767 C C6    . 6FA C 3 .   ? 16.469 11.712  16.105  1.00 24.67 ?  402 6FA A C6    1 
HETATM 2768 O O6    . 6FA C 3 .   ? 15.486 11.915  15.190  1.00 20.22 ?  402 6FA A O6    1 
HETATM 2769 C C7    . 6FA C 3 .   ? 17.537 10.892  15.809  1.00 26.00 ?  402 6FA A C7    1 
HETATM 2770 C C7M   . 6FA C 3 .   ? 17.586 10.183  14.479  1.00 23.03 ?  402 6FA A C7M   1 
HETATM 2771 C C8    . 6FA C 3 .   ? 18.570 10.702  16.744  1.00 27.86 ?  402 6FA A C8    1 
HETATM 2772 C C8M   . 6FA C 3 .   ? 19.718 9.782   16.418  1.00 26.70 ?  402 6FA A C8M   1 
HETATM 2773 C C9    . 6FA C 3 .   ? 18.516 11.326  17.985  1.00 25.95 ?  402 6FA A C9    1 
HETATM 2774 C C9A   . 6FA C 3 .   ? 17.473 12.209  18.307  1.00 25.07 ?  402 6FA A C9A   1 
HETATM 2775 N N10   . 6FA C 3 .   ? 17.419 12.897  19.519  1.00 24.24 ?  402 6FA A N10   1 
HETATM 2776 C C10   . 6FA C 3 .   ? 16.389 13.791  19.757  1.00 22.24 ?  402 6FA A C10   1 
HETATM 2777 C "C1'" . 6FA C 3 .   ? 18.456 12.678  20.546  1.00 22.03 ?  402 6FA A "C1'" 1 
HETATM 2778 C "C2'" . 6FA C 3 .   ? 19.646 13.602  20.476  1.00 23.41 ?  402 6FA A "C2'" 1 
HETATM 2779 O "O2'" . 6FA C 3 .   ? 20.374 13.317  19.299  1.00 23.06 ?  402 6FA A "O2'" 1 
HETATM 2780 C "C3'" . 6FA C 3 .   ? 20.546 13.325  21.683  1.00 21.25 ?  402 6FA A "C3'" 1 
HETATM 2781 O "O3'" . 6FA C 3 .   ? 19.743 13.165  22.852  1.00 23.09 ?  402 6FA A "O3'" 1 
HETATM 2782 C "C4'" . 6FA C 3 .   ? 21.565 14.432  21.954  1.00 20.77 ?  402 6FA A "C4'" 1 
HETATM 2783 O "O4'" . 6FA C 3 .   ? 22.605 14.397  20.974  1.00 18.31 ?  402 6FA A "O4'" 1 
HETATM 2784 C "C5'" . 6FA C 3 .   ? 22.199 14.307  23.317  1.00 19.27 ?  402 6FA A "C5'" 1 
HETATM 2785 O "O5'" . 6FA C 3 .   ? 22.925 15.542  23.524  1.00 19.81 ?  402 6FA A "O5'" 1 
HETATM 2786 P P     . 6FA C 3 .   ? 24.207 15.555  24.470  1.00 20.78 ?  402 6FA A P     1 
HETATM 2787 O O1P   . 6FA C 3 .   ? 24.675 16.970  24.504  1.00 18.57 -1 402 6FA A O1P   1 
HETATM 2788 O O2P   . 6FA C 3 .   ? 23.816 14.837  25.723  1.00 20.46 ?  402 6FA A O2P   1 
HETATM 2789 O O3P   . 6FA C 3 .   ? 25.243 14.640  23.666  1.00 20.61 ?  402 6FA A O3P   1 
HETATM 2790 P PA    . 6FA C 3 .   ? 25.781 14.615  22.152  1.00 22.29 ?  402 6FA A PA    1 
HETATM 2791 O O1A   . 6FA C 3 .   ? 25.936 13.189  21.744  1.00 21.44 -1 402 6FA A O1A   1 
HETATM 2792 O O2A   . 6FA C 3 .   ? 24.892 15.514  21.374  1.00 17.18 ?  402 6FA A O2A   1 
HETATM 2793 O O5B   . 6FA C 3 .   ? 27.234 15.282  22.255  1.00 17.39 ?  402 6FA A O5B   1 
HETATM 2794 C C5B   . 6FA C 3 .   ? 28.279 14.724  23.082  1.00 19.15 ?  402 6FA A C5B   1 
HETATM 2795 C C4B   . 6FA C 3 .   ? 29.593 15.266  22.579  1.00 21.19 ?  402 6FA A C4B   1 
HETATM 2796 O O4B   . 6FA C 3 .   ? 30.658 14.834  23.458  1.00 20.47 ?  402 6FA A O4B   1 
HETATM 2797 C C3B   . 6FA C 3 .   ? 30.024 14.819  21.171  1.00 19.16 ?  402 6FA A C3B   1 
HETATM 2798 O O3B   . 6FA C 3 .   ? 30.414 15.952  20.409  1.00 20.37 ?  402 6FA A O3B   1 
HETATM 2799 C C2B   . 6FA C 3 .   ? 31.244 13.934  21.448  1.00 22.06 ?  402 6FA A C2B   1 
HETATM 2800 O O2B   . 6FA C 3 .   ? 32.139 13.871  20.361  1.00 25.23 ?  402 6FA A O2B   1 
HETATM 2801 C C1B   . 6FA C 3 .   ? 31.811 14.615  22.687  1.00 21.65 ?  402 6FA A C1B   1 
HETATM 2802 N N9A   . 6FA C 3 .   ? 32.690 13.772  23.487  1.00 26.11 ?  402 6FA A N9A   1 
HETATM 2803 C C8A   . 6FA C 3 .   ? 32.298 12.652  24.177  1.00 26.77 ?  402 6FA A C8A   1 
HETATM 2804 N N7A   . 6FA C 3 .   ? 33.274 12.076  24.827  1.00 28.02 ?  402 6FA A N7A   1 
HETATM 2805 C C5X   . 6FA C 3 .   ? 34.377 12.878  24.570  1.00 27.44 ?  402 6FA A C5X   1 
HETATM 2806 C C6A   . 6FA C 3 .   ? 35.717 12.794  24.990  1.00 30.23 ?  402 6FA A C6A   1 
HETATM 2807 N N6A   . 6FA C 3 .   ? 36.177 11.822  25.773  1.00 32.03 ?  402 6FA A N6A   1 
HETATM 2808 N N1A   . 6FA C 3 .   ? 36.573 13.751  24.552  1.00 28.21 ?  402 6FA A N1A   1 
HETATM 2809 C C2A   . 6FA C 3 .   ? 36.095 14.720  23.760  1.00 26.09 ?  402 6FA A C2A   1 
HETATM 2810 N N3A   . 6FA C 3 .   ? 34.857 14.899  23.307  1.00 25.47 ?  402 6FA A N3A   1 
HETATM 2811 C C4X   . 6FA C 3 .   ? 34.032 13.932  23.749  1.00 25.54 ?  402 6FA A C4X   1 
HETATM 2812 P PA    . NAD D 4 .   ? 17.311 1.441   20.482  1.00 26.07 ?  403 NAD A PA    1 
HETATM 2813 O O1A   . NAD D 4 .   ? 18.152 0.636   21.416  1.00 24.36 -1 403 NAD A O1A   1 
HETATM 2814 O O2A   . NAD D 4 .   ? 16.117 2.181   20.995  1.00 26.74 ?  403 NAD A O2A   1 
HETATM 2815 O O5B   . NAD D 4 .   ? 16.837 0.519   19.267  1.00 28.16 ?  403 NAD A O5B   1 
HETATM 2816 C C5B   . NAD D 4 .   ? 17.774 -0.377  18.633  1.00 26.10 ?  403 NAD A C5B   1 
HETATM 2817 C C4B   . NAD D 4 .   ? 17.057 -1.685  18.425  1.00 25.45 ?  403 NAD A C4B   1 
HETATM 2818 O O4B   . NAD D 4 .   ? 17.812 -2.512  17.505  1.00 26.34 ?  403 NAD A O4B   1 
HETATM 2819 C C3B   . NAD D 4 .   ? 16.844 -2.540  19.688  1.00 24.51 ?  403 NAD A C3B   1 
HETATM 2820 O O3B   . NAD D 4 .   ? 15.476 -2.918  19.774  1.00 26.35 ?  403 NAD A O3B   1 
HETATM 2821 C C2B   . NAD D 4 .   ? 17.718 -3.771  19.425  1.00 27.12 ?  403 NAD A C2B   1 
HETATM 2822 O O2B   . NAD D 4 .   ? 17.241 -4.951  20.032  1.00 30.05 ?  403 NAD A O2B   1 
HETATM 2823 C C1B   . NAD D 4 .   ? 17.641 -3.846  17.905  1.00 28.39 ?  403 NAD A C1B   1 
HETATM 2824 N N9A   . NAD D 4 .   ? 18.699 -4.654  17.320  1.00 27.95 ?  403 NAD A N9A   1 
HETATM 2825 C C8A   . NAD D 4 .   ? 20.014 -4.682  17.712  1.00 29.92 ?  403 NAD A C8A   1 
HETATM 2826 N N7A   . NAD D 4 .   ? 20.742 -5.520  17.017  1.00 31.07 ?  403 NAD A N7A   1 
HETATM 2827 C C5A   . NAD D 4 .   ? 19.844 -6.103  16.133  1.00 30.44 ?  403 NAD A C5A   1 
HETATM 2828 C C6A   . NAD D 4 .   ? 20.000 -7.088  15.137  1.00 30.90 ?  403 NAD A C6A   1 
HETATM 2829 N N6A   . NAD D 4 .   ? 21.157 -7.690  14.866  1.00 28.57 ?  403 NAD A N6A   1 
HETATM 2830 N N1A   . NAD D 4 .   ? 18.896 -7.447  14.439  1.00 28.31 ?  403 NAD A N1A   1 
HETATM 2831 C C2A   . NAD D 4 .   ? 17.733 -6.841  14.716  1.00 27.98 ?  403 NAD A C2A   1 
HETATM 2832 N N3A   . NAD D 4 .   ? 17.469 -5.909  15.628  1.00 27.47 ?  403 NAD A N3A   1 
HETATM 2833 C C4A   . NAD D 4 .   ? 18.578 -5.578  16.312  1.00 27.55 ?  403 NAD A C4A   1 
HETATM 2834 O O3    . NAD D 4 .   ? 18.277 2.459   19.711  1.00 29.72 ?  403 NAD A O3    1 
HETATM 2835 P PN    . NAD D 4 .   ? 17.978 3.791   18.867  1.00 25.62 ?  403 NAD A PN    1 
HETATM 2836 O O1N   . NAD D 4 .   ? 16.840 3.495   17.942  1.00 22.73 -1 403 NAD A O1N   1 
HETATM 2837 O O2N   . NAD D 4 .   ? 19.288 4.263   18.332  1.00 24.42 ?  403 NAD A O2N   1 
HETATM 2838 O O5D   . NAD D 4 .   ? 17.494 4.804   20.024  1.00 29.53 ?  403 NAD A O5D   1 
HETATM 2839 C C5D   . NAD D 4 .   ? 18.401 5.090   21.123  1.00 30.44 ?  403 NAD A C5D   1 
HETATM 2840 C C4D   . NAD D 4 .   ? 17.887 6.264   21.924  1.00 32.03 ?  403 NAD A C4D   1 
HETATM 2841 O O4D   . NAD D 4 .   ? 18.220 7.507   21.265  1.00 33.76 ?  403 NAD A O4D   1 
HETATM 2842 C C3D   . NAD D 4 .   ? 16.372 6.342   22.141  1.00 34.54 ?  403 NAD A C3D   1 
HETATM 2843 O O3D   . NAD D 4 .   ? 15.962 5.486   23.197  1.00 36.33 ?  403 NAD A O3D   1 
HETATM 2844 C C2D   . NAD D 4 .   ? 16.220 7.826   22.475  1.00 37.41 ?  403 NAD A C2D   1 
HETATM 2845 O O2D   . NAD D 4 .   ? 16.738 8.068   23.773  1.00 44.03 ?  403 NAD A O2D   1 
HETATM 2846 C C1D   . NAD D 4 .   ? 17.153 8.455   21.446  1.00 33.07 ?  403 NAD A C1D   1 
HETATM 2847 N N1N   . NAD D 4 .   ? 16.480 8.710   20.133  1.00 33.41 ?  403 NAD A N1N   1 
HETATM 2848 C C2N   . NAD D 4 .   ? 15.395 9.567   20.067  1.00 33.10 ?  403 NAD A C2N   1 
HETATM 2849 C C3N   . NAD D 4 .   ? 14.732 9.772   18.856  1.00 30.23 ?  403 NAD A C3N   1 
HETATM 2850 C C7N   . NAD D 4 .   ? 13.524 10.683  18.824  1.00 32.95 ?  403 NAD A C7N   1 
HETATM 2851 O O7N   . NAD D 4 .   ? 13.224 11.334  19.829  1.00 29.40 ?  403 NAD A O7N   1 
HETATM 2852 N N7N   . NAD D 4 .   ? 12.813 10.720  17.701  1.00 28.77 ?  403 NAD A N7N   1 
HETATM 2853 C C4N   . NAD D 4 .   ? 15.205 9.136   17.700  1.00 29.61 ?  403 NAD A C4N   1 
HETATM 2854 C C5N   . NAD D 4 .   ? 16.335 8.351   17.767  1.00 29.22 ?  403 NAD A C5N   1 
HETATM 2855 C C6N   . NAD D 4 .   ? 16.937 8.125   18.993  1.00 32.42 ?  403 NAD A C6N   1 
HETATM 2856 O O     . HOH E 5 .   ? 21.814 27.946  29.734  1.00 53.97 ?  501 HOH A O     1 
HETATM 2857 O O     . HOH E 5 .   ? 31.031 12.189  43.583  1.00 74.30 ?  502 HOH A O     1 
HETATM 2858 O O     . HOH E 5 .   ? 6.410  18.319  27.210  1.00 42.86 ?  503 HOH A O     1 
HETATM 2859 O O     . HOH E 5 .   ? 23.930 26.809  0.425   1.00 42.24 ?  504 HOH A O     1 
HETATM 2860 O O     . HOH E 5 .   ? 34.431 33.013  23.718  1.00 30.98 ?  505 HOH A O     1 
HETATM 2861 O O     . HOH E 5 .   ? 43.261 34.537  20.827  1.00 44.47 ?  506 HOH A O     1 
HETATM 2862 O O     . HOH E 5 .   ? 28.531 -11.465 16.179  1.00 49.71 ?  507 HOH A O     1 
HETATM 2863 O O     . HOH E 5 .   ? 29.734 7.413   18.033  1.00 29.59 ?  508 HOH A O     1 
HETATM 2864 O O     . HOH E 5 .   ? 31.957 19.222  45.526  1.00 48.42 ?  509 HOH A O     1 
HETATM 2865 O O     . HOH E 5 .   ? 25.935 13.270  -1.879  1.00 21.32 ?  510 HOH A O     1 
HETATM 2866 O O     . HOH E 5 .   ? 14.561 3.833   20.323  1.00 30.09 ?  511 HOH A O     1 
HETATM 2867 O O     . HOH E 5 .   ? 23.209 -2.817  -8.430  1.00 28.21 ?  512 HOH A O     1 
HETATM 2868 O O     . HOH E 5 .   ? 30.625 -6.185  9.778   1.00 34.06 ?  513 HOH A O     1 
HETATM 2869 O O     . HOH E 5 .   ? 35.062 15.468  12.758  1.00 40.66 ?  514 HOH A O     1 
HETATM 2870 O O     . HOH E 5 .   ? 33.051 10.465  27.415  1.00 36.91 ?  515 HOH A O     1 
HETATM 2871 O O     . HOH E 5 .   ? 26.699 31.308  21.727  1.00 44.19 ?  516 HOH A O     1 
HETATM 2872 O O     . HOH E 5 .   ? 3.615  8.532   4.556   1.00 25.28 ?  517 HOH A O     1 
HETATM 2873 O O     . HOH E 5 .   ? 28.539 24.179  41.928  1.00 34.44 ?  518 HOH A O     1 
HETATM 2874 O O     . HOH E 5 .   ? 24.505 -0.540  18.087  1.00 27.75 ?  519 HOH A O     1 
HETATM 2875 O O     . HOH E 5 .   ? 24.403 13.070  -4.085  1.00 25.83 ?  520 HOH A O     1 
HETATM 2876 O O     . HOH E 5 .   ? -0.045 14.062  30.019  1.00 26.86 ?  521 HOH A O     1 
HETATM 2877 O O     . HOH E 5 .   ? 21.202 31.635  12.881  1.00 31.00 ?  522 HOH A O     1 
HETATM 2878 O O     . HOH E 5 .   ? 17.014 5.247   -7.392  1.00 25.38 ?  523 HOH A O     1 
HETATM 2879 O O     . HOH E 5 .   ? 20.719 24.714  20.889  1.00 20.68 ?  524 HOH A O     1 
HETATM 2880 O O     . HOH E 5 .   ? 43.864 15.586  22.880  1.00 38.54 ?  525 HOH A O     1 
HETATM 2881 O O     . HOH E 5 .   ? 6.280  4.659   -0.922  1.00 34.47 ?  526 HOH A O     1 
HETATM 2882 O O     . HOH E 5 .   ? 36.142 24.683  15.144  1.00 24.82 ?  527 HOH A O     1 
HETATM 2883 O O     . HOH E 5 .   ? 19.668 23.062  18.891  1.00 23.93 ?  528 HOH A O     1 
HETATM 2884 O O     . HOH E 5 .   ? -3.940 9.887   9.933   1.00 33.34 ?  529 HOH A O     1 
HETATM 2885 O O     . HOH E 5 .   ? 26.493 -1.999  3.267   1.00 20.26 ?  530 HOH A O     1 
HETATM 2886 O O     . HOH E 5 .   ? 25.906 16.334  19.098  1.00 17.30 ?  531 HOH A O     1 
HETATM 2887 O O     . HOH E 5 .   ? 33.903 18.115  12.732  1.00 26.18 ?  532 HOH A O     1 
HETATM 2888 O O     . HOH E 5 .   ? 27.068 17.929  25.049  1.00 15.84 ?  533 HOH A O     1 
HETATM 2889 O O     . HOH E 5 .   ? 42.342 34.885  24.164  1.00 43.20 ?  534 HOH A O     1 
HETATM 2890 O O     . HOH E 5 .   ? 16.535 21.568  8.247   1.00 20.87 ?  535 HOH A O     1 
HETATM 2891 O O     . HOH E 5 .   ? 10.318 -1.282  0.010   1.00 22.97 ?  536 HOH A O     1 
HETATM 2892 O O     . HOH E 5 .   ? 12.291 10.462  9.428   1.00 27.23 ?  537 HOH A O     1 
HETATM 2893 O O     . HOH E 5 .   ? 39.095 27.900  18.946  1.00 28.49 ?  538 HOH A O     1 
HETATM 2894 O O     . HOH E 5 .   ? 25.448 1.588   9.667   1.00 18.59 ?  539 HOH A O     1 
HETATM 2895 O O     . HOH E 5 .   ? 37.371 28.572  42.663  1.00 33.21 ?  540 HOH A O     1 
HETATM 2896 O O     . HOH E 5 .   ? 43.584 21.158  20.004  1.00 37.50 ?  541 HOH A O     1 
HETATM 2897 O O     . HOH E 5 .   ? 27.162 -14.546 6.374   1.00 41.96 ?  542 HOH A O     1 
HETATM 2898 O O     . HOH E 5 .   ? 42.189 22.543  39.535  1.00 39.94 ?  543 HOH A O     1 
HETATM 2899 O O     . HOH E 5 .   ? 10.760 13.837  26.628  1.00 33.70 ?  544 HOH A O     1 
HETATM 2900 O O     . HOH E 5 .   ? 16.620 1.840   15.838  1.00 20.73 ?  545 HOH A O     1 
HETATM 2901 O O     . HOH E 5 .   ? 29.985 26.750  10.818  1.00 21.84 ?  546 HOH A O     1 
HETATM 2902 O O     . HOH E 5 .   ? -3.159 6.749   23.077  1.00 35.30 ?  547 HOH A O     1 
HETATM 2903 O O     . HOH E 5 .   ? 27.459 0.000   32.543  0.50 40.20 ?  548 HOH A O     1 
HETATM 2904 O O     . HOH E 5 .   ? 29.106 33.889  15.738  1.00 37.48 ?  549 HOH A O     1 
HETATM 2905 O O     . HOH E 5 .   ? 24.086 11.214  21.872  1.00 31.18 ?  550 HOH A O     1 
HETATM 2906 O O     . HOH E 5 .   ? 21.500 -0.857  -7.162  1.00 23.87 ?  551 HOH A O     1 
HETATM 2907 O O     . HOH E 5 .   ? 23.065 31.936  21.620  1.00 26.94 ?  552 HOH A O     1 
HETATM 2908 O O     . HOH E 5 .   ? 25.453 31.738  5.451   1.00 34.62 ?  553 HOH A O     1 
HETATM 2909 O O     . HOH E 5 .   ? 25.669 14.323  27.677  1.00 23.45 ?  554 HOH A O     1 
HETATM 2910 O O     . HOH E 5 .   ? 32.685 6.152   19.157  1.00 44.07 ?  555 HOH A O     1 
HETATM 2911 O O     . HOH E 5 .   ? 19.138 17.770  -2.659  1.00 24.71 ?  556 HOH A O     1 
HETATM 2912 O O     . HOH E 5 .   ? 26.419 19.179  2.249   1.00 22.38 ?  557 HOH A O     1 
HETATM 2913 O O     . HOH E 5 .   ? 40.607 31.210  18.557  1.00 37.85 ?  558 HOH A O     1 
HETATM 2914 O O     . HOH E 5 .   ? 47.013 28.880  40.198  1.00 32.87 ?  559 HOH A O     1 
HETATM 2915 O O     . HOH E 5 .   ? 18.634 -20.050 6.034   1.00 48.66 ?  560 HOH A O     1 
HETATM 2916 O O     . HOH E 5 .   ? 12.196 12.491  3.823   1.00 14.68 ?  561 HOH A O     1 
HETATM 2917 O O     . HOH E 5 .   ? 27.197 11.794  19.730  1.00 30.07 ?  562 HOH A O     1 
HETATM 2918 O O     . HOH E 5 .   ? 7.831  18.493  4.333   1.00 26.99 ?  563 HOH A O     1 
HETATM 2919 O O     . HOH E 5 .   ? 24.510 9.365   -6.904  1.00 38.91 ?  564 HOH A O     1 
HETATM 2920 O O     . HOH E 5 .   ? 28.820 23.565  7.828   1.00 19.98 ?  565 HOH A O     1 
HETATM 2921 O O     . HOH E 5 .   ? 22.485 4.629   12.618  1.00 22.63 ?  566 HOH A O     1 
HETATM 2922 O O     . HOH E 5 .   ? 28.076 28.768  7.894   1.00 26.91 ?  567 HOH A O     1 
HETATM 2923 O O     . HOH E 5 .   ? 19.367 12.912  29.714  1.00 40.85 ?  568 HOH A O     1 
HETATM 2924 O O     . HOH E 5 .   ? 7.156  23.635  10.078  1.00 28.39 ?  569 HOH A O     1 
HETATM 2925 O O     . HOH E 5 .   ? 18.738 29.750  12.822  1.00 25.79 ?  570 HOH A O     1 
HETATM 2926 O O     . HOH E 5 .   ? 20.398 1.839   22.494  1.00 25.35 ?  571 HOH A O     1 
HETATM 2927 O O     . HOH E 5 .   ? 34.893 5.766   42.403  1.00 49.89 ?  572 HOH A O     1 
HETATM 2928 O O     . HOH E 5 .   ? 29.442 30.255  9.900   1.00 21.48 ?  573 HOH A O     1 
HETATM 2929 O O     . HOH E 5 .   ? 29.312 10.822  22.446  1.00 26.64 ?  574 HOH A O     1 
HETATM 2930 O O     . HOH E 5 .   ? 32.567 36.094  27.076  1.00 39.52 ?  575 HOH A O     1 
HETATM 2931 O O     . HOH E 5 .   ? 24.270 0.983   -8.787  1.00 33.86 ?  576 HOH A O     1 
HETATM 2932 O O     . HOH E 5 .   ? 8.751  -11.347 10.771  1.00 41.96 ?  577 HOH A O     1 
HETATM 2933 O O     . HOH E 5 .   ? 33.156 18.447  2.421   1.00 27.32 ?  578 HOH A O     1 
HETATM 2934 O O     . HOH E 5 .   ? 4.784  -1.337  16.240  1.00 28.02 ?  579 HOH A O     1 
HETATM 2935 O O     . HOH E 5 .   ? 26.777 33.545  24.148  1.00 25.21 ?  580 HOH A O     1 
HETATM 2936 O O     . HOH E 5 .   ? 9.380  17.956  28.705  1.00 44.26 ?  581 HOH A O     1 
HETATM 2937 O O     . HOH E 5 .   ? 24.413 30.540  1.965   1.00 41.26 ?  582 HOH A O     1 
HETATM 2938 O O     . HOH E 5 .   ? 16.866 13.303  -1.303  1.00 20.73 ?  583 HOH A O     1 
HETATM 2939 O O     . HOH E 5 .   ? 41.556 35.501  44.285  1.00 24.22 ?  584 HOH A O     1 
HETATM 2940 O O     . HOH E 5 .   ? 12.427 -8.226  2.556   1.00 35.13 ?  585 HOH A O     1 
HETATM 2941 O O     . HOH E 5 .   ? 19.801 14.123  27.053  1.00 28.02 ?  586 HOH A O     1 
HETATM 2942 O O     . HOH E 5 .   ? 36.227 26.406  11.641  1.00 36.06 ?  587 HOH A O     1 
HETATM 2943 O O     . HOH E 5 .   ? 34.523 30.317  44.360  1.00 34.53 ?  588 HOH A O     1 
HETATM 2944 O O     . HOH E 5 .   ? 7.186  6.365   -0.042  1.00 26.02 ?  589 HOH A O     1 
HETATM 2945 O O     . HOH E 5 .   ? 9.966  20.855  11.357  1.00 17.79 ?  590 HOH A O     1 
HETATM 2946 O O     . HOH E 5 .   ? -1.573 16.051  13.700  1.00 25.57 ?  591 HOH A O     1 
HETATM 2947 O O     . HOH E 5 .   ? 30.744 3.644   8.024   1.00 38.72 ?  592 HOH A O     1 
HETATM 2948 O O     . HOH E 5 .   ? 21.201 3.345   16.440  1.00 22.56 ?  593 HOH A O     1 
HETATM 2949 O O     . HOH E 5 .   ? 30.138 5.067   3.687   1.00 36.78 ?  594 HOH A O     1 
HETATM 2950 O O     . HOH E 5 .   ? 18.881 14.340  -2.637  1.00 19.16 ?  595 HOH A O     1 
HETATM 2951 O O     . HOH E 5 .   ? 23.847 15.376  2.947   1.00 13.00 ?  596 HOH A O     1 
HETATM 2952 O O     . HOH E 5 .   ? 20.489 -4.078  -7.436  1.00 49.83 ?  597 HOH A O     1 
HETATM 2953 O O     . HOH E 5 .   ? 25.550 -3.470  15.931  1.00 44.12 ?  598 HOH A O     1 
HETATM 2954 O O     . HOH E 5 .   ? 6.123  8.992   1.459   1.00 29.65 ?  599 HOH A O     1 
HETATM 2955 O O     . HOH E 5 .   ? 24.738 14.747  9.684   1.00 12.33 ?  600 HOH A O     1 
HETATM 2956 O O     . HOH E 5 .   ? 11.796 21.508  13.328  1.00 19.06 ?  601 HOH A O     1 
HETATM 2957 O O     . HOH E 5 .   ? -4.262 13.269  22.109  1.00 39.29 ?  602 HOH A O     1 
HETATM 2958 O O     . HOH E 5 .   ? 16.050 21.034  2.434   1.00 37.90 ?  603 HOH A O     1 
HETATM 2959 O O     . HOH E 5 .   ? 40.007 15.708  8.105   1.00 38.53 ?  604 HOH A O     1 
HETATM 2960 O O     . HOH E 5 .   ? 17.418 12.713  10.661  1.00 17.56 ?  605 HOH A O     1 
HETATM 2961 O O     . HOH E 5 .   ? 26.929 12.475  16.555  1.00 22.77 ?  606 HOH A O     1 
HETATM 2962 O O     . HOH E 5 .   ? 20.063 10.185  39.548  1.00 44.25 ?  607 HOH A O     1 
HETATM 2963 O O     . HOH E 5 .   ? 28.256 17.828  18.652  1.00 16.83 ?  608 HOH A O     1 
HETATM 2964 O O     . HOH E 5 .   ? 32.332 -0.770  4.767   1.00 35.67 ?  609 HOH A O     1 
HETATM 2965 O O     . HOH E 5 .   ? 39.842 31.569  35.871  1.00 33.63 ?  610 HOH A O     1 
HETATM 2966 O O     . HOH E 5 .   ? 10.747 13.943  -0.821  1.00 23.80 ?  611 HOH A O     1 
HETATM 2967 O O     . HOH E 5 .   ? 30.391 7.390   4.633   1.00 28.29 ?  612 HOH A O     1 
HETATM 2968 O O     . HOH E 5 .   ? 12.655 -6.445  -1.258  1.00 42.21 ?  613 HOH A O     1 
HETATM 2969 O O     . HOH E 5 .   ? 16.076 -11.350 -0.925  1.00 29.76 ?  614 HOH A O     1 
HETATM 2970 O O     . HOH E 5 .   ? 3.800  6.320   27.193  1.00 37.08 ?  615 HOH A O     1 
HETATM 2971 O O     . HOH E 5 .   ? 23.465 2.951   28.018  1.00 36.01 ?  616 HOH A O     1 
HETATM 2972 O O     . HOH E 5 .   ? 14.985 28.522  15.507  1.00 32.62 ?  617 HOH A O     1 
HETATM 2973 O O     . HOH E 5 .   ? 11.393 19.657  4.320   1.00 27.56 ?  618 HOH A O     1 
HETATM 2974 O O     . HOH E 5 .   ? 17.689 28.255  19.682  1.00 39.69 ?  619 HOH A O     1 
HETATM 2975 O O     . HOH E 5 .   ? 5.212  9.558   30.398  1.00 40.12 ?  620 HOH A O     1 
HETATM 2976 O O     . HOH E 5 .   ? 9.376  23.211  15.918  1.00 28.38 ?  621 HOH A O     1 
HETATM 2977 O O     . HOH E 5 .   ? 14.680 -16.775 3.755   1.00 32.62 ?  622 HOH A O     1 
HETATM 2978 O O     . HOH E 5 .   ? 40.519 15.970  18.952  1.00 30.27 ?  623 HOH A O     1 
HETATM 2979 O O     . HOH E 5 .   ? 1.778  20.313  6.165   1.00 24.99 ?  624 HOH A O     1 
HETATM 2980 O O     . HOH E 5 .   ? 17.832 2.529   -7.161  1.00 20.74 ?  625 HOH A O     1 
HETATM 2981 O O     . HOH E 5 .   ? 19.709 6.861   32.702  1.00 44.46 ?  626 HOH A O     1 
HETATM 2982 O O     . HOH E 5 .   ? 27.096 20.957  -1.220  1.00 37.72 ?  627 HOH A O     1 
HETATM 2983 O O     . HOH E 5 .   ? 39.936 9.181   35.200  1.00 45.06 ?  628 HOH A O     1 
HETATM 2984 O O     . HOH E 5 .   ? 21.246 23.204  22.773  1.00 21.42 ?  629 HOH A O     1 
HETATM 2985 O O     . HOH E 5 .   ? 30.403 5.801   2.012   1.00 51.43 ?  630 HOH A O     1 
HETATM 2986 O O     . HOH E 5 .   ? 30.141 6.995   15.000  1.00 34.54 ?  631 HOH A O     1 
HETATM 2987 O O     . HOH E 5 .   ? 30.931 0.916   -2.949  1.00 34.77 ?  632 HOH A O     1 
HETATM 2988 O O     . HOH E 5 .   ? 40.105 17.447  13.231  1.00 41.16 ?  633 HOH A O     1 
HETATM 2989 O O     . HOH E 5 .   ? 6.126  -6.296  5.539   1.00 26.49 ?  634 HOH A O     1 
HETATM 2990 O O     . HOH E 5 .   ? 14.809 11.720  10.579  1.00 22.30 ?  635 HOH A O     1 
HETATM 2991 O O     . HOH E 5 .   ? 12.846 13.132  -3.270  1.00 24.20 ?  636 HOH A O     1 
HETATM 2992 O O     . HOH E 5 .   ? 27.750 32.582  10.009  1.00 22.09 ?  637 HOH A O     1 
HETATM 2993 O O     . HOH E 5 .   ? 14.954 -4.602  0.477   1.00 24.11 ?  638 HOH A O     1 
HETATM 2994 O O     . HOH E 5 .   ? 23.112 5.129   15.797  1.00 26.30 ?  639 HOH A O     1 
HETATM 2995 O O     . HOH E 5 .   ? 4.872  -2.512  2.888   1.00 31.49 ?  640 HOH A O     1 
HETATM 2996 O O     . HOH E 5 .   ? 13.095 0.794   23.756  1.00 40.18 ?  641 HOH A O     1 
HETATM 2997 O O     . HOH E 5 .   ? 35.080 17.592  0.430   1.00 39.24 ?  642 HOH A O     1 
HETATM 2998 O O     . HOH E 5 .   ? -2.805 3.945   16.668  1.00 40.40 ?  643 HOH A O     1 
HETATM 2999 O O     . HOH E 5 .   ? 31.310 13.116  49.046  1.00 51.15 ?  644 HOH A O     1 
HETATM 3000 O O     . HOH E 5 .   ? 30.169 -4.869  -5.528  1.00 29.33 ?  645 HOH A O     1 
HETATM 3001 O O     . HOH E 5 .   ? 32.225 -2.269  6.284   1.00 36.20 ?  646 HOH A O     1 
HETATM 3002 O O     . HOH E 5 .   ? 42.639 27.436  45.555  1.00 35.65 ?  647 HOH A O     1 
HETATM 3003 O O     . HOH E 5 .   ? 11.935 -1.868  20.289  1.00 34.05 ?  648 HOH A O     1 
HETATM 3004 O O     . HOH E 5 .   ? -1.982 16.378  17.219  1.00 33.33 ?  649 HOH A O     1 
HETATM 3005 O O     . HOH E 5 .   ? 19.002 21.778  23.341  1.00 27.67 ?  650 HOH A O     1 
HETATM 3006 O O     . HOH E 5 .   ? 35.878 24.615  43.448  1.00 35.78 ?  651 HOH A O     1 
HETATM 3007 O O     . HOH E 5 .   ? -3.186 10.115  24.158  1.00 39.55 ?  652 HOH A O     1 
HETATM 3008 O O     . HOH E 5 .   ? 30.464 22.030  2.279   1.00 34.23 ?  653 HOH A O     1 
HETATM 3009 O O     . HOH E 5 .   ? 37.432 21.377  7.201   1.00 26.36 ?  654 HOH A O     1 
HETATM 3010 O O     . HOH E 5 .   ? 39.960 20.247  12.328  1.00 33.74 ?  655 HOH A O     1 
HETATM 3011 O O     . HOH E 5 .   ? 10.875 20.463  33.098  1.00 44.01 ?  656 HOH A O     1 
HETATM 3012 O O     . HOH E 5 .   ? 27.185 -11.249 2.025   1.00 31.25 ?  657 HOH A O     1 
HETATM 3013 O O     . HOH E 5 .   ? 29.229 2.487   12.117  1.00 32.26 ?  658 HOH A O     1 
HETATM 3014 O O     . HOH E 5 .   ? 18.835 7.022   -6.547  1.00 25.51 ?  659 HOH A O     1 
HETATM 3015 O O     . HOH E 5 .   ? 2.549  6.223   5.182   1.00 37.50 ?  660 HOH A O     1 
HETATM 3016 O O     . HOH E 5 .   ? 23.080 -8.305  17.281  1.00 42.88 ?  661 HOH A O     1 
HETATM 3017 O O     . HOH E 5 .   ? 23.611 -10.641 16.490  1.00 38.21 ?  662 HOH A O     1 
HETATM 3018 O O     . HOH E 5 .   ? 26.669 -13.557 3.870   1.00 48.45 ?  663 HOH A O     1 
HETATM 3019 O O     . HOH E 5 .   ? 41.524 23.812  19.221  1.00 35.75 ?  664 HOH A O     1 
HETATM 3020 O O     . HOH E 5 .   ? -3.125 7.329   5.426   1.00 34.98 ?  665 HOH A O     1 
HETATM 3021 O O     . HOH E 5 .   ? 12.713 24.402  13.750  1.00 29.63 ?  666 HOH A O     1 
HETATM 3022 O O     . HOH E 5 .   ? 23.751 14.663  44.104  1.00 44.32 ?  667 HOH A O     1 
HETATM 3023 O O     . HOH E 5 .   ? 33.164 7.646   3.597   1.00 38.22 ?  668 HOH A O     1 
HETATM 3024 O O     . HOH E 5 .   ? 19.481 28.443  4.812   1.00 42.60 ?  669 HOH A O     1 
HETATM 3025 O O     . HOH E 5 .   ? 39.755 6.346   28.959  1.00 51.30 ?  670 HOH A O     1 
HETATM 3026 O O     . HOH E 5 .   ? 3.340  8.526   28.463  1.00 36.79 ?  671 HOH A O     1 
HETATM 3027 O O     . HOH E 5 .   ? 23.981 -5.471  17.431  1.00 39.80 ?  672 HOH A O     1 
HETATM 3028 O O     . HOH E 5 .   ? 4.713  20.139  5.149   1.00 43.13 ?  673 HOH A O     1 
HETATM 3029 O O     . HOH E 5 .   ? 15.651 12.332  -3.687  1.00 31.36 ?  674 HOH A O     1 
HETATM 3030 O O     . HOH E 5 .   ? 30.478 24.207  5.719   1.00 30.43 ?  675 HOH A O     1 
HETATM 3031 O O     . HOH E 5 .   ? 16.523 -5.628  0.493   1.00 32.13 ?  676 HOH A O     1 
HETATM 3032 O O     . HOH E 5 .   ? 19.671 14.428  -5.445  1.00 36.15 ?  677 HOH A O     1 
HETATM 3033 O O     . HOH E 5 .   ? 32.674 27.170  9.230   1.00 29.43 ?  678 HOH A O     1 
HETATM 3034 O O     . HOH E 5 .   ? 13.679 26.010  40.371  1.00 40.23 ?  679 HOH A O     1 
HETATM 3035 O O     . HOH E 5 .   ? 20.136 -9.420  22.967  1.00 45.48 ?  680 HOH A O     1 
HETATM 3036 O O     . HOH E 5 .   ? 12.465 16.141  -1.745  1.00 29.59 ?  681 HOH A O     1 
HETATM 3037 O O     . HOH E 5 .   ? 13.534 -0.325  21.048  1.00 39.41 ?  682 HOH A O     1 
HETATM 3038 O O     . HOH E 5 .   ? 11.859 18.459  -0.476  1.00 27.86 ?  683 HOH A O     1 
HETATM 3039 O O     . HOH E 5 .   ? 20.020 9.626   -7.123  1.00 35.88 ?  684 HOH A O     1 
HETATM 3040 O O     . HOH E 5 .   ? 23.846 6.130   -8.303  1.00 33.42 ?  685 HOH A O     1 
HETATM 3041 O O     . HOH E 5 .   ? 28.332 0.866   11.096  1.00 30.80 ?  686 HOH A O     1 
HETATM 3042 O O     . HOH E 5 .   ? 19.875 1.743   -8.789  1.00 38.80 ?  687 HOH A O     1 
HETATM 3043 O O     . HOH E 5 .   ? 7.988  13.835  0.000   0.50 22.46 ?  688 HOH A O     1 
HETATM 3044 O O     . HOH E 5 .   ? -4.220 11.991  24.416  1.00 50.63 ?  689 HOH A O     1 
HETATM 3045 O O     . HOH E 5 .   ? 42.354 17.506  17.838  1.00 42.75 ?  690 HOH A O     1 
HETATM 3046 O O     . HOH E 5 .   ? 29.371 26.275  8.271   1.00 21.90 ?  691 HOH A O     1 
HETATM 3047 O O     . HOH E 5 .   ? 0.437  11.194  30.883  1.00 37.01 ?  692 HOH A O     1 
HETATM 3048 O O     . HOH E 5 .   ? -4.862 7.970   21.167  1.00 45.87 ?  693 HOH A O     1 
HETATM 3049 O O     . HOH E 5 .   ? 27.743 36.193  24.155  1.00 38.59 ?  694 HOH A O     1 
HETATM 3050 O O     . HOH E 5 .   ? 34.724 28.322  43.546  1.00 40.86 ?  695 HOH A O     1 
HETATM 3051 O O     . HOH E 5 .   ? 43.404 24.607  45.523  1.00 38.92 ?  696 HOH A O     1 
HETATM 3052 O O     . HOH E 5 .   ? 19.816 25.495  24.283  1.00 39.57 ?  697 HOH A O     1 
HETATM 3053 O O     . HOH E 5 .   ? 13.779 27.602  39.175  1.00 41.90 ?  698 HOH A O     1 
HETATM 3054 O O     . HOH E 5 .   ? 28.702 20.118  1.050   1.00 27.32 ?  699 HOH A O     1 
HETATM 3055 O O     . HOH E 5 .   ? 29.907 24.126  3.310   1.00 34.43 ?  700 HOH A O     1 
HETATM 3056 O O     . HOH E 5 .   ? 27.411 -0.638  17.781  1.00 41.02 ?  701 HOH A O     1 
HETATM 3057 O O     . HOH E 5 .   ? 10.989 23.877  17.053  1.00 45.01 ?  702 HOH A O     1 
HETATM 3058 O O     . HOH E 5 .   ? 22.930 -12.746 17.389  1.00 35.77 ?  703 HOH A O     1 
HETATM 3059 O O     . HOH E 5 .   ? 24.919 7.576   -8.639  1.00 41.99 ?  704 HOH A O     1 
HETATM 3060 O O     . HOH E 5 .   ? 32.044 31.319  8.889   1.00 34.85 ?  705 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 1   ? 0.5695 0.6355 0.4967 0.0254  -0.2786 -0.1277 7   PRO A N   
2    C CA  . PRO A 1   ? 0.5572 0.6036 0.4498 0.0096  -0.2732 -0.1233 7   PRO A CA  
3    C C   . PRO A 1   ? 0.5210 0.5827 0.4240 -0.0079 -0.2504 -0.1254 7   PRO A C   
4    O O   . PRO A 1   ? 0.4998 0.5952 0.4361 -0.0155 -0.2450 -0.1347 7   PRO A O   
5    C CB  . PRO A 1   ? 0.5809 0.6411 0.4816 0.0103  -0.2892 -0.1314 7   PRO A CB  
6    C CG  . PRO A 1   ? 0.5659 0.6648 0.5169 0.0220  -0.2967 -0.1430 7   PRO A CG  
7    C CD  . PRO A 1   ? 0.5830 0.6881 0.5526 0.0302  -0.2874 -0.1415 7   PRO A CD  
8    N N   . HIS A 2   ? 0.5170 0.5516 0.3907 -0.0148 -0.2367 -0.1168 8   HIS A N   
9    C CA  . HIS A 2   ? 0.4870 0.5307 0.3680 -0.0306 -0.2159 -0.1188 8   HIS A CA  
10   C C   . HIS A 2   ? 0.5019 0.5344 0.3601 -0.0455 -0.2107 -0.1207 8   HIS A C   
11   O O   . HIS A 2   ? 0.4801 0.5218 0.3484 -0.0591 -0.1954 -0.1245 8   HIS A O   
12   C CB  . HIS A 2   ? 0.4743 0.4964 0.3395 -0.0301 -0.2028 -0.1105 8   HIS A CB  
13   C CG  . HIS A 2   ? 0.4938 0.5327 0.3872 -0.0176 -0.2044 -0.1107 8   HIS A CG  
14   N ND1 . HIS A 2   ? 0.4370 0.5080 0.3685 -0.0214 -0.1916 -0.1166 8   HIS A ND1 
15   C CD2 . HIS A 2   ? 0.5013 0.5298 0.3915 -0.0014 -0.2170 -0.1066 8   HIS A CD2 
16   C CE1 . HIS A 2   ? 0.4755 0.5567 0.4259 -0.0081 -0.1952 -0.1166 8   HIS A CE1 
17   N NE2 . HIS A 2   ? 0.5499 0.6052 0.4763 0.0047  -0.2111 -0.1108 8   HIS A NE2 
18   N N   . MET A 3   ? 0.5401 0.5526 0.3690 -0.0432 -0.2233 -0.1188 9   MET A N   
19   C CA  . MET A 3   ? 0.5575 0.5617 0.3663 -0.0558 -0.2197 -0.1224 9   MET A CA  
20   C C   . MET A 3   ? 0.5461 0.5322 0.3378 -0.0675 -0.1977 -0.1204 9   MET A C   
21   O O   . MET A 3   ? 0.5371 0.5321 0.3364 -0.0791 -0.1880 -0.1278 9   MET A O   
22   C CB  . MET A 3   ? 0.5480 0.5870 0.3889 -0.0630 -0.2243 -0.1335 9   MET A CB  
23   C CG  . MET A 3   ? 0.5613 0.6185 0.4226 -0.0503 -0.2456 -0.1368 9   MET A CG  
24   S SD  . MET A 3   ? 0.5597 0.6519 0.4529 -0.0600 -0.2515 -0.1491 9   MET A SD  
25   C CE  . MET A 3   ? 0.5756 0.6865 0.4942 -0.0395 -0.2757 -0.1535 9   MET A CE  
26   N N   . GLY A 4   ? 0.5480 0.5071 0.3178 -0.0641 -0.1896 -0.1104 10  GLY A N   
27   C CA  . GLY A 4   ? 0.5422 0.4799 0.2940 -0.0741 -0.1683 -0.1068 10  GLY A CA  
28   C C   . GLY A 4   ? 0.5028 0.4534 0.2805 -0.0777 -0.1533 -0.1071 10  GLY A C   
29   O O   . GLY A 4   ? 0.5470 0.4772 0.3095 -0.0832 -0.1359 -0.1012 10  GLY A O   
30   N N   . ALA A 5   ? 0.4752 0.4601 0.2921 -0.0759 -0.1585 -0.1139 11  ALA A N   
31   C CA  . ALA A 5   ? 0.4493 0.4472 0.2910 -0.0815 -0.1443 -0.1138 11  ALA A CA  
32   C C   . ALA A 5   ? 0.4358 0.4244 0.2756 -0.0713 -0.1387 -0.1040 11  ALA A C   
33   O O   . ALA A 5   ? 0.4468 0.4263 0.2741 -0.0591 -0.1543 -0.1009 11  ALA A O   
34   C CB  . ALA A 5   ? 0.4150 0.4554 0.3020 -0.0823 -0.1490 -0.1236 11  ALA A CB  
35   N N   . LEU A 6   ? 0.4359 0.4256 0.2883 -0.0761 -0.1174 -0.0993 12  LEU A N   
36   C CA  . LEU A 6   ? 0.4521 0.4368 0.3076 -0.0677 -0.1105 -0.0909 12  LEU A CA  
37   C C   . LEU A 6   ? 0.4095 0.4291 0.3056 -0.0611 -0.1133 -0.0946 12  LEU A C   
38   O O   . LEU A 6   ? 0.4133 0.4587 0.3380 -0.0689 -0.1066 -0.1004 12  LEU A O   
39   C CB  . LEU A 6   ? 0.4436 0.4134 0.2942 -0.0754 -0.0872 -0.0849 12  LEU A CB  
40   C CG  . LEU A 6   ? 0.4719 0.4093 0.2865 -0.0831 -0.0782 -0.0826 12  LEU A CG  
41   C CD1 . LEU A 6   ? 0.4528 0.3819 0.2719 -0.0861 -0.0574 -0.0776 12  LEU A CD1 
42   C CD2 . LEU A 6   ? 0.5201 0.4314 0.2966 -0.0777 -0.0907 -0.0784 12  LEU A CD2 
43   N N   . HIS A 7   ? 0.4038 0.4226 0.3008 -0.0476 -0.1225 -0.0914 13  HIS A N   
44   C CA  . HIS A 7   ? 0.3592 0.4062 0.2913 -0.0413 -0.1194 -0.0935 13  HIS A CA  
45   C C   . HIS A 7   ? 0.4180 0.4439 0.3352 -0.0307 -0.1188 -0.0845 13  HIS A C   
46   O O   . HIS A 7   ? 0.3633 0.3754 0.2646 -0.0191 -0.1365 -0.0835 13  HIS A O   
47   C CB  . HIS A 7   ? 0.3612 0.4433 0.3238 -0.0342 -0.1366 -0.1058 13  HIS A CB  
48   C CG  . HIS A 7   ? 0.4100 0.5242 0.4099 -0.0307 -0.1297 -0.1101 13  HIS A CG  
49   N ND1 . HIS A 7   ? 0.4163 0.5464 0.4340 -0.0153 -0.1433 -0.1157 13  HIS A ND1 
50   C CD2 . HIS A 7   ? 0.3661 0.4966 0.3861 -0.0409 -0.1105 -0.1094 13  HIS A CD2 
51   C CE1 . HIS A 7   ? 0.3823 0.5397 0.4304 -0.0169 -0.1313 -0.1194 13  HIS A CE1 
52   N NE2 . HIS A 7   ? 0.3796 0.5368 0.4280 -0.0328 -0.1115 -0.1149 13  HIS A NE2 
53   N N   . VAL A 8   ? 0.3529 0.3743 0.2740 -0.0349 -0.0998 -0.0779 14  VAL A N   
54   C CA  . VAL A 8   ? 0.3645 0.3656 0.2720 -0.0273 -0.0963 -0.0693 14  VAL A CA  
55   C C   . VAL A 8   ? 0.3634 0.3903 0.3021 -0.0173 -0.0991 -0.0729 14  VAL A C   
56   O O   . VAL A 8   ? 0.3019 0.3590 0.2716 -0.0221 -0.0908 -0.0782 14  VAL A O   
57   C CB  . VAL A 8   ? 0.3477 0.3314 0.2443 -0.0369 -0.0747 -0.0619 14  VAL A CB  
58   C CG1 . VAL A 8   ? 0.3336 0.2933 0.2119 -0.0306 -0.0716 -0.0534 14  VAL A CG1 
59   C CG2 . VAL A 8   ? 0.3328 0.2978 0.2056 -0.0480 -0.0698 -0.0621 14  VAL A CG2 
60   N N   . VAL A 9   ? 0.3324 0.3460 0.2614 -0.0042 -0.1105 -0.0701 15  VAL A N   
61   C CA  . VAL A 9   ? 0.3010 0.3349 0.2569 0.0060  -0.1119 -0.0735 15  VAL A CA  
62   C C   . VAL A 9   ? 0.2984 0.3064 0.2371 0.0076  -0.1014 -0.0631 15  VAL A C   
63   O O   . VAL A 9   ? 0.3256 0.2979 0.2295 0.0092  -0.1059 -0.0553 15  VAL A O   
64   C CB  . VAL A 9   ? 0.3354 0.3785 0.3005 0.0220  -0.1365 -0.0819 15  VAL A CB  
65   C CG1 . VAL A 9   ? 0.3100 0.3747 0.3044 0.0331  -0.1369 -0.0873 15  VAL A CG1 
66   C CG2 . VAL A 9   ? 0.3298 0.4014 0.3143 0.0193  -0.1466 -0.0937 15  VAL A CG2 
67   N N   . ILE A 10  ? 0.2931 0.3185 0.2544 0.0053  -0.0867 -0.0630 16  ILE A N   
68   C CA  . ILE A 10  ? 0.2928 0.3004 0.2452 0.0073  -0.0769 -0.0551 16  ILE A CA  
69   C C   . ILE A 10  ? 0.2993 0.3227 0.2727 0.0208  -0.0852 -0.0605 16  ILE A C   
70   O O   . ILE A 10  ? 0.2872 0.3458 0.2931 0.0210  -0.0825 -0.0693 16  ILE A O   
71   C CB  . ILE A 10  ? 0.2912 0.3057 0.2533 -0.0046 -0.0555 -0.0515 16  ILE A CB  
72   C CG1 . ILE A 10  ? 0.2699 0.2741 0.2182 -0.0173 -0.0478 -0.0493 16  ILE A CG1 
73   C CG2 . ILE A 10  ? 0.2709 0.2661 0.2229 -0.0025 -0.0465 -0.0439 16  ILE A CG2 
74   C CD1 . ILE A 10  ? 0.2545 0.2675 0.2163 -0.0278 -0.0306 -0.0475 16  ILE A CD1 
75   N N   . VAL A 11  ? 0.3185 0.3154 0.2727 0.0311  -0.0946 -0.0559 17  VAL A N   
76   C CA  . VAL A 11  ? 0.3176 0.3254 0.2904 0.0451  -0.1029 -0.0615 17  VAL A CA  
77   C C   . VAL A 11  ? 0.2656 0.2621 0.2348 0.0421  -0.0873 -0.0544 17  VAL A C   
78   O O   . VAL A 11  ? 0.3289 0.2902 0.2685 0.0409  -0.0858 -0.0448 17  VAL A O   
79   C CB  . VAL A 11  ? 0.3818 0.3671 0.3376 0.0600  -0.1274 -0.0624 17  VAL A CB  
80   C CG1 . VAL A 11  ? 0.3422 0.3314 0.3139 0.0751  -0.1351 -0.0674 17  VAL A CG1 
81   C CG2 . VAL A 11  ? 0.3203 0.3265 0.2897 0.0644  -0.1437 -0.0726 17  VAL A CG2 
82   N N   . GLY A 12  ? 0.2591 0.2859 0.2576 0.0391  -0.0752 -0.0595 18  GLY A N   
83   C CA  . GLY A 12  ? 0.2626 0.2838 0.2618 0.0361  -0.0609 -0.0543 18  GLY A CA  
84   C C   . GLY A 12  ? 0.2560 0.2889 0.2624 0.0210  -0.0421 -0.0510 18  GLY A C   
85   O O   . GLY A 12  ? 0.2124 0.2310 0.2026 0.0116  -0.0366 -0.0453 18  GLY A O   
86   N N   . GLY A 13  ? 0.2114 0.2687 0.2407 0.0186  -0.0328 -0.0550 19  GLY A N   
87   C CA  . GLY A 13  ? 0.1833 0.2497 0.2185 0.0048  -0.0174 -0.0516 19  GLY A CA  
88   C C   . GLY A 13  ? 0.1932 0.2467 0.2232 0.0023  -0.0063 -0.0449 19  GLY A C   
89   O O   . GLY A 13  ? 0.1653 0.2348 0.2090 -0.0032 0.0026  -0.0459 19  GLY A O   
90   N N   . GLY A 14  ? 0.2193 0.2431 0.2282 0.0055  -0.0073 -0.0382 20  GLY A N   
91   C CA  . GLY A 14  ? 0.2086 0.2183 0.2117 0.0028  0.0026  -0.0324 20  GLY A CA  
92   C C   . GLY A 14  ? 0.2022 0.2012 0.1974 -0.0083 0.0130  -0.0269 20  GLY A C   
93   O O   . GLY A 14  ? 0.1922 0.1995 0.1911 -0.0149 0.0145  -0.0279 20  GLY A O   
94   N N   . PHE A 15  ? 0.1919 0.1726 0.1776 -0.0103 0.0203  -0.0221 21  PHE A N   
95   C CA  . PHE A 15  ? 0.2073 0.1780 0.1878 -0.0195 0.0300  -0.0190 21  PHE A CA  
96   C C   . PHE A 15  ? 0.2523 0.2109 0.2168 -0.0230 0.0278  -0.0190 21  PHE A C   
97   O O   . PHE A 15  ? 0.2127 0.1746 0.1807 -0.0300 0.0324  -0.0199 21  PHE A O   
98   C CB  . PHE A 15  ? 0.2363 0.1904 0.2099 -0.0206 0.0373  -0.0159 21  PHE A CB  
99   C CG  . PHE A 15  ? 0.2237 0.1897 0.2137 -0.0198 0.0413  -0.0160 21  PHE A CG  
100  C CD1 . PHE A 15  ? 0.2138 0.1880 0.2162 -0.0258 0.0477  -0.0156 21  PHE A CD1 
101  C CD2 . PHE A 15  ? 0.2459 0.2136 0.2379 -0.0127 0.0373  -0.0169 21  PHE A CD2 
102  C CE1 . PHE A 15  ? 0.2113 0.1945 0.2258 -0.0256 0.0500  -0.0153 21  PHE A CE1 
103  C CE2 . PHE A 15  ? 0.1982 0.1768 0.2037 -0.0127 0.0411  -0.0175 21  PHE A CE2 
104  C CZ  . PHE A 15  ? 0.2118 0.1978 0.2273 -0.0195 0.0473  -0.0164 21  PHE A CZ  
105  N N   . GLY A 16  ? 0.2280 0.1706 0.1733 -0.0185 0.0199  -0.0181 22  GLY A N   
106  C CA  . GLY A 16  ? 0.2584 0.1886 0.1853 -0.0224 0.0168  -0.0183 22  GLY A CA  
107  C C   . GLY A 16  ? 0.2655 0.2156 0.2045 -0.0223 0.0099  -0.0226 22  GLY A C   
108  O O   . GLY A 16  ? 0.2540 0.2041 0.1906 -0.0295 0.0134  -0.0240 22  GLY A O   
109  N N   . GLY A 17  ? 0.2547 0.2237 0.2089 -0.0146 0.0006  -0.0262 23  GLY A N   
110  C CA  . GLY A 17  ? 0.2373 0.2263 0.2031 -0.0150 -0.0067 -0.0318 23  GLY A CA  
111  C C   . GLY A 17  ? 0.2576 0.2646 0.2406 -0.0247 0.0023  -0.0334 23  GLY A C   
112  O O   . GLY A 17  ? 0.2327 0.2459 0.2167 -0.0301 0.0001  -0.0363 23  GLY A O   
113  N N   . ILE A 18  ? 0.1912 0.2050 0.1864 -0.0275 0.0115  -0.0314 24  ILE A N   
114  C CA  . ILE A 18  ? 0.1889 0.2150 0.1965 -0.0372 0.0179  -0.0319 24  ILE A CA  
115  C C   . ILE A 18  ? 0.2191 0.2269 0.2160 -0.0441 0.0240  -0.0291 24  ILE A C   
116  O O   . ILE A 18  ? 0.1995 0.2117 0.2012 -0.0518 0.0255  -0.0305 24  ILE A O   
117  C CB  . ILE A 18  ? 0.1711 0.2091 0.1930 -0.0392 0.0241  -0.0305 24  ILE A CB  
118  C CG1 . ILE A 18  ? 0.1912 0.2122 0.2072 -0.0374 0.0306  -0.0254 24  ILE A CG1 
119  C CG2 . ILE A 18  ? 0.1426 0.2031 0.1778 -0.0338 0.0195  -0.0359 24  ILE A CG2 
120  C CD1 . ILE A 18  ? 0.1707 0.1996 0.1980 -0.0419 0.0364  -0.0232 24  ILE A CD1 
121  N N   . ALA A 19  ? 0.2002 0.1872 0.1828 -0.0422 0.0280  -0.0264 25  ALA A N   
122  C CA  . ALA A 19  ? 0.2564 0.2282 0.2300 -0.0485 0.0342  -0.0267 25  ALA A CA  
123  C C   . ALA A 19  ? 0.2581 0.2259 0.2194 -0.0509 0.0285  -0.0299 25  ALA A C   
124  O O   . ALA A 19  ? 0.2585 0.2252 0.2214 -0.0574 0.0311  -0.0325 25  ALA A O   
125  C CB  . ALA A 19  ? 0.2522 0.2054 0.2137 -0.0475 0.0411  -0.0249 25  ALA A CB  
126  N N   . ALA A 20  ? 0.2579 0.2220 0.2062 -0.0453 0.0196  -0.0301 26  ALA A N   
127  C CA  . ALA A 20  ? 0.2968 0.2575 0.2324 -0.0472 0.0118  -0.0333 26  ALA A CA  
128  C C   . ALA A 20  ? 0.2577 0.2403 0.2115 -0.0508 0.0077  -0.0376 26  ALA A C   
129  O O   . ALA A 20  ? 0.2752 0.2553 0.2249 -0.0575 0.0080  -0.0407 26  ALA A O   
130  C CB  . ALA A 20  ? 0.2479 0.2002 0.1672 -0.0391 -0.0004 -0.0325 26  ALA A CB  
131  N N   . ALA A 21  ? 0.2462 0.2507 0.2199 -0.0477 0.0049  -0.0387 27  ALA A N   
132  C CA  . ALA A 21  ? 0.2168 0.2441 0.2076 -0.0531 0.0018  -0.0437 27  ALA A CA  
133  C C   . ALA A 21  ? 0.2459 0.2707 0.2418 -0.0640 0.0107  -0.0425 27  ALA A C   
134  O O   . ALA A 21  ? 0.2128 0.2437 0.2119 -0.0716 0.0088  -0.0462 27  ALA A O   
135  C CB  . ALA A 21  ? 0.1942 0.2460 0.2048 -0.0489 -0.0004 -0.0464 27  ALA A CB  
136  N N   . SER A 22  ? 0.2158 0.2309 0.2131 -0.0647 0.0194  -0.0377 28  SER A N   
137  C CA  . SER A 22  ? 0.2607 0.2697 0.2626 -0.0733 0.0256  -0.0364 28  SER A CA  
138  C C   . SER A 22  ? 0.3046 0.2968 0.2948 -0.0770 0.0267  -0.0391 28  SER A C   
139  O O   . SER A 22  ? 0.2739 0.2646 0.2677 -0.0849 0.0270  -0.0410 28  SER A O   
140  C CB  . SER A 22  ? 0.2739 0.2755 0.2799 -0.0712 0.0323  -0.0315 28  SER A CB  
141  O OG  . SER A 22  ? 0.3851 0.3770 0.3947 -0.0779 0.0358  -0.0306 28  SER A OG  
142  N N   . GLN A 23  ? 0.2561 0.2341 0.2309 -0.0724 0.0277  -0.0397 29  GLN A N   
143  C CA  . GLN A 23  ? 0.3434 0.3063 0.3057 -0.0769 0.0299  -0.0439 29  GLN A CA  
144  C C   . GLN A 23  ? 0.3167 0.2860 0.2739 -0.0805 0.0216  -0.0482 29  GLN A C   
145  O O   . GLN A 23  ? 0.2971 0.2611 0.2533 -0.0874 0.0225  -0.0523 29  GLN A O   
146  C CB  . GLN A 23  ? 0.3434 0.2894 0.2874 -0.0737 0.0346  -0.0439 29  GLN A CB  
147  C CG  . GLN A 23  ? 0.4491 0.3809 0.3777 -0.0793 0.0375  -0.0499 29  GLN A CG  
148  C CD  . GLN A 23  ? 0.5278 0.4459 0.4532 -0.0811 0.0495  -0.0531 29  GLN A CD  
149  O OE1 . GLN A 23  ? 0.6352 0.5505 0.5612 -0.0777 0.0548  -0.0502 29  GLN A OE1 
150  N NE2 . GLN A 23  ? 0.5731 0.4835 0.4964 -0.0865 0.0539  -0.0605 29  GLN A NE2 
151  N N   . LEU A 24  ? 0.2914 0.2717 0.2464 -0.0756 0.0124  -0.0483 30  LEU A N   
152  C CA  . LEU A 24  ? 0.2693 0.2586 0.2224 -0.0785 0.0028  -0.0536 30  LEU A CA  
153  C C   . LEU A 24  ? 0.2860 0.2912 0.2577 -0.0872 0.0033  -0.0563 30  LEU A C   
154  O O   . LEU A 24  ? 0.2544 0.2586 0.2235 -0.0944 0.0007  -0.0610 30  LEU A O   
155  C CB  . LEU A 24  ? 0.2793 0.2795 0.2313 -0.0697 -0.0089 -0.0543 30  LEU A CB  
156  C CG  . LEU A 24  ? 0.2768 0.2558 0.2023 -0.0631 -0.0137 -0.0519 30  LEU A CG  
157  C CD1 . LEU A 24  ? 0.2853 0.2724 0.2137 -0.0520 -0.0248 -0.0510 30  LEU A CD1 
158  C CD2 . LEU A 24  ? 0.2724 0.2396 0.1774 -0.0673 -0.0200 -0.0560 30  LEU A CD2 
159  N N   . GLN A 25  ? 0.2626 0.2808 0.2511 -0.0881 0.0071  -0.0532 31  GLN A N   
160  C CA  . GLN A 25  ? 0.2615 0.2914 0.2638 -0.0989 0.0088  -0.0546 31  GLN A CA  
161  C C   . GLN A 25  ? 0.2813 0.2912 0.2783 -0.1067 0.0137  -0.0540 31  GLN A C   
162  O O   . GLN A 25  ? 0.3139 0.3259 0.3136 -0.1166 0.0119  -0.0574 31  GLN A O   
163  C CB  . GLN A 25  ? 0.2528 0.2955 0.2685 -0.0991 0.0130  -0.0506 31  GLN A CB  
164  C CG  . GLN A 25  ? 0.2721 0.3297 0.2994 -0.1113 0.0142  -0.0521 31  GLN A CG  
165  C CD  . GLN A 25  ? 0.3192 0.3877 0.3545 -0.1085 0.0182  -0.0475 31  GLN A CD  
166  O OE1 . GLN A 25  ? 0.3728 0.4262 0.4037 -0.1058 0.0225  -0.0402 31  GLN A OE1 
167  N NE2 . GLN A 25  ? 0.2604 0.3551 0.3075 -0.1077 0.0161  -0.0529 31  GLN A NE2 
168  N N   . ALA A 26  ? 0.3094 0.2999 0.3001 -0.1024 0.0198  -0.0509 32  ALA A N   
169  C CA  . ALA A 26  ? 0.3343 0.3063 0.3231 -0.1072 0.0235  -0.0520 32  ALA A CA  
170  C C   . ALA A 26  ? 0.3229 0.2849 0.2996 -0.1104 0.0216  -0.0592 32  ALA A C   
171  O O   . ALA A 26  ? 0.3411 0.2941 0.3188 -0.1120 0.0215  -0.0600 32  ALA A O   
172  C CB  . ALA A 26  ? 0.3340 0.2924 0.3234 -0.0998 0.0299  -0.0486 32  ALA A CB  
173  N N   . LEU A 27  ? 0.3190 0.2825 0.2831 -0.1055 0.0187  -0.0615 33  LEU A N   
174  C CA  . LEU A 27  ? 0.3278 0.2826 0.2772 -0.1089 0.0159  -0.0683 33  LEU A CA  
175  C C   . LEU A 27  ? 0.3248 0.2944 0.2779 -0.1151 0.0066  -0.0722 33  LEU A C   
176  O O   . LEU A 27  ? 0.3689 0.3320 0.3103 -0.1190 0.0031  -0.0784 33  LEU A O   
177  C CB  . LEU A 27  ? 0.3139 0.2605 0.2431 -0.1024 0.0154  -0.0685 33  LEU A CB  
178  C CG  . LEU A 27  ? 0.3571 0.2885 0.2801 -0.0987 0.0260  -0.0671 33  LEU A CG  
179  C CD1 . LEU A 27  ? 0.3485 0.2719 0.2492 -0.0940 0.0248  -0.0652 33  LEU A CD1 
180  C CD2 . LEU A 27  ? 0.3110 0.2276 0.2322 -0.1040 0.0336  -0.0744 33  LEU A CD2 
181  N N   . ASN A 28  ? 0.2963 0.2868 0.2656 -0.1168 0.0032  -0.0700 34  ASN A N   
182  C CA  . ASN A 28  ? 0.3109 0.3218 0.2884 -0.1229 -0.0050 -0.0752 34  ASN A CA  
183  C C   . ASN A 28  ? 0.3475 0.3646 0.3149 -0.1160 -0.0154 -0.0794 34  ASN A C   
184  O O   . ASN A 28  ? 0.3353 0.3602 0.3020 -0.1209 -0.0233 -0.0862 34  ASN A O   
185  C CB  . ASN A 28  ? 0.3367 0.3406 0.3156 -0.1309 -0.0043 -0.0769 34  ASN A CB  
186  C CG  . ASN A 28  ? 0.3879 0.4145 0.3816 -0.1363 -0.0088 -0.0786 34  ASN A CG  
187  O OD1 . ASN A 28  ? 0.4081 0.4567 0.4146 -0.1350 -0.0100 -0.0783 34  ASN A OD1 
188  N ND2 . ASN A 28  ? 0.3952 0.4166 0.3876 -0.1424 -0.0104 -0.0811 34  ASN A ND2 
189  N N   . VAL A 29  ? 0.3155 0.3276 0.2737 -0.1048 -0.0167 -0.0754 35  VAL A N   
190  C CA  . VAL A 29  ? 0.3255 0.3383 0.2704 -0.0973 -0.0287 -0.0780 35  VAL A CA  
191  C C   . VAL A 29  ? 0.3230 0.3638 0.2882 -0.0913 -0.0374 -0.0800 35  VAL A C   
192  O O   . VAL A 29  ? 0.2780 0.3273 0.2562 -0.0875 -0.0319 -0.0760 35  VAL A O   
193  C CB  . VAL A 29  ? 0.3284 0.3168 0.2488 -0.0899 -0.0261 -0.0728 35  VAL A CB  
194  C CG1 . VAL A 29  ? 0.2985 0.2850 0.2036 -0.0811 -0.0409 -0.0733 35  VAL A CG1 
195  C CG2 . VAL A 29  ? 0.3390 0.3036 0.2402 -0.0968 -0.0179 -0.0746 35  VAL A CG2 
196  N N   . PRO A 30  ? 0.3021 0.3593 0.2725 -0.0904 -0.0508 -0.0876 36  PRO A N   
197  C CA  . PRO A 30  ? 0.3133 0.4005 0.3071 -0.0837 -0.0592 -0.0924 36  PRO A CA  
198  C C   . PRO A 30  ? 0.2810 0.3607 0.2683 -0.0689 -0.0633 -0.0873 36  PRO A C   
199  O O   . PRO A 30  ? 0.2899 0.3451 0.2512 -0.0620 -0.0698 -0.0833 36  PRO A O   
200  C CB  . PRO A 30  ? 0.3002 0.4006 0.2962 -0.0838 -0.0752 -0.1023 36  PRO A CB  
201  C CG  . PRO A 30  ? 0.3516 0.4374 0.3344 -0.0965 -0.0706 -0.1035 36  PRO A CG  
202  C CD  . PRO A 30  ? 0.3447 0.3971 0.3035 -0.0965 -0.0586 -0.0940 36  PRO A CD  
203  N N   . PHE A 31  ? 0.2583 0.3579 0.2677 -0.0652 -0.0594 -0.0876 37  PHE A N   
204  C CA  . PHE A 31  ? 0.2632 0.3561 0.2684 -0.0513 -0.0633 -0.0835 37  PHE A CA  
205  C C   . PHE A 31  ? 0.2568 0.3829 0.2933 -0.0474 -0.0636 -0.0900 37  PHE A C   
206  O O   . PHE A 31  ? 0.2229 0.3734 0.2807 -0.0580 -0.0561 -0.0951 37  PHE A O   
207  C CB  . PHE A 31  ? 0.2557 0.3211 0.2433 -0.0516 -0.0501 -0.0725 37  PHE A CB  
208  C CG  . PHE A 31  ? 0.2426 0.3183 0.2471 -0.0586 -0.0351 -0.0697 37  PHE A CG  
209  C CD1 . PHE A 31  ? 0.2684 0.3445 0.2768 -0.0721 -0.0258 -0.0695 37  PHE A CD1 
210  C CD2 . PHE A 31  ? 0.2308 0.3136 0.2456 -0.0518 -0.0316 -0.0672 37  PHE A CD2 
211  C CE1 . PHE A 31  ? 0.2287 0.3102 0.2490 -0.0788 -0.0142 -0.0660 37  PHE A CE1 
212  C CE2 . PHE A 31  ? 0.2093 0.3001 0.2368 -0.0587 -0.0190 -0.0644 37  PHE A CE2 
213  C CZ  . PHE A 31  ? 0.2369 0.3260 0.2660 -0.0722 -0.0108 -0.0632 37  PHE A CZ  
214  N N   . MET A 32  ? 0.2587 0.3835 0.2958 -0.0328 -0.0717 -0.0898 38  MET A N   
215  C CA  . MET A 32  ? 0.2600 0.4126 0.3246 -0.0267 -0.0710 -0.0961 38  MET A CA  
216  C C   . MET A 32  ? 0.2514 0.3829 0.3038 -0.0173 -0.0673 -0.0874 38  MET A C   
217  O O   . MET A 32  ? 0.2467 0.3514 0.2764 -0.0074 -0.0771 -0.0824 38  MET A O   
218  C CB  . MET A 32  ? 0.2689 0.4463 0.3528 -0.0156 -0.0896 -0.1095 38  MET A CB  
219  C CG  . MET A 32  ? 0.3155 0.5295 0.4339 -0.0108 -0.0878 -0.1205 38  MET A CG  
220  S SD  . MET A 32  ? 0.3550 0.5978 0.4948 -0.0314 -0.0673 -0.1241 38  MET A SD  
221  C CE  . MET A 32  ? 0.3297 0.5761 0.4685 -0.0381 -0.0751 -0.1285 38  MET A CE  
222  N N   . LEU A 33  ? 0.2261 0.3675 0.2908 -0.0216 -0.0535 -0.0854 39  LEU A N   
223  C CA  . LEU A 33  ? 0.2420 0.3687 0.3000 -0.0129 -0.0502 -0.0793 39  LEU A CA  
224  C C   . LEU A 33  ? 0.2325 0.3864 0.3159 -0.0021 -0.0566 -0.0897 39  LEU A C   
225  O O   . LEU A 33  ? 0.2223 0.4102 0.3319 -0.0083 -0.0514 -0.0992 39  LEU A O   
226  C CB  . LEU A 33  ? 0.2291 0.3477 0.2837 -0.0232 -0.0322 -0.0708 39  LEU A CB  
227  C CG  . LEU A 33  ? 0.2408 0.3528 0.2956 -0.0166 -0.0267 -0.0666 39  LEU A CG  
228  C CD1 . LEU A 33  ? 0.2140 0.2921 0.2435 -0.0076 -0.0318 -0.0589 39  LEU A CD1 
229  C CD2 . LEU A 33  ? 0.1782 0.2899 0.2352 -0.0282 -0.0109 -0.0608 39  LEU A CD2 
230  N N   . VAL A 34  ? 0.2523 0.3907 0.3275 0.0132  -0.0677 -0.0888 40  VAL A N   
231  C CA  . VAL A 34  ? 0.2223 0.3833 0.3214 0.0264  -0.0764 -0.1002 40  VAL A CA  
232  C C   . VAL A 34  ? 0.2311 0.3773 0.3243 0.0318  -0.0694 -0.0941 40  VAL A C   
233  O O   . VAL A 34  ? 0.2436 0.3534 0.3088 0.0343  -0.0699 -0.0825 40  VAL A O   
234  C CB  . VAL A 34  ? 0.2252 0.3801 0.3217 0.0423  -0.1002 -0.1063 40  VAL A CB  
235  C CG1 . VAL A 34  ? 0.2374 0.4229 0.3667 0.0564  -0.1101 -0.1222 40  VAL A CG1 
236  C CG2 . VAL A 34  ? 0.2615 0.4234 0.3568 0.0361  -0.1075 -0.1099 40  VAL A CG2 
237  N N   . ASP A 35  ? 0.1857 0.3605 0.3044 0.0324  -0.0624 -0.1029 41  ASP A N   
238  C CA  . ASP A 35  ? 0.1861 0.3510 0.3028 0.0387  -0.0576 -0.1000 41  ASP A CA  
239  C C   . ASP A 35  ? 0.1868 0.3875 0.3362 0.0472  -0.0605 -0.1168 41  ASP A C   
240  O O   . ASP A 35  ? 0.1999 0.4378 0.3744 0.0405  -0.0567 -0.1288 41  ASP A O   
241  C CB  . ASP A 35  ? 0.1708 0.3280 0.2785 0.0245  -0.0381 -0.0897 41  ASP A CB  
242  C CG  . ASP A 35  ? 0.2040 0.3421 0.3026 0.0310  -0.0347 -0.0842 41  ASP A CG  
243  O OD1 . ASP A 35  ? 0.2234 0.3262 0.2966 0.0340  -0.0376 -0.0735 41  ASP A OD1 
244  O OD2 . ASP A 35  ? 0.1698 0.3284 0.2860 0.0322  -0.0289 -0.0913 41  ASP A OD2 
245  N N   . MET A 36  ? 0.1895 0.3796 0.3390 0.0609  -0.0662 -0.1185 42  MET A N   
246  C CA  . MET A 36  ? 0.2102 0.4307 0.3888 0.0695  -0.0680 -0.1354 42  MET A CA  
247  C C   . MET A 36  ? 0.1713 0.4097 0.3563 0.0540  -0.0461 -0.1367 42  MET A C   
248  O O   . MET A 36  ? 0.1751 0.4329 0.3729 0.0516  -0.0415 -0.1481 42  MET A O   
249  C CB  . MET A 36  ? 0.2199 0.4174 0.3926 0.0881  -0.0808 -0.1362 42  MET A CB  
250  C CG  . MET A 36  ? 0.2383 0.4123 0.3933 0.0844  -0.0694 -0.1243 42  MET A CG  
251  S SD  . MET A 36  ? 0.3044 0.4541 0.4555 0.1051  -0.0833 -0.1276 42  MET A SD  
252  C CE  . MET A 36  ? 0.2700 0.3745 0.3893 0.1149  -0.1053 -0.1167 42  MET A CE  
253  N N   . LYS A 37  ? 0.1653 0.3951 0.3393 0.0434  -0.0334 -0.1253 43  LYS A N   
254  C CA  . LYS A 37  ? 0.1626 0.4008 0.3343 0.0275  -0.0150 -0.1234 43  LYS A CA  
255  C C   . LYS A 37  ? 0.1798 0.4277 0.3486 0.0095  -0.0059 -0.1205 43  LYS A C   
256  O O   . LYS A 37  ? 0.1373 0.3856 0.3062 0.0079  -0.0118 -0.1190 43  LYS A O   
257  C CB  . LYS A 37  ? 0.1484 0.3681 0.3068 0.0242  -0.0063 -0.1118 43  LYS A CB  
258  C CG  . LYS A 37  ? 0.1990 0.3961 0.3504 0.0400  -0.0143 -0.1098 43  LYS A CG  
259  C CD  . LYS A 37  ? 0.1687 0.3413 0.3005 0.0325  -0.0033 -0.0962 43  LYS A CD  
260  C CE  . LYS A 37  ? 0.1454 0.2799 0.2507 0.0317  -0.0062 -0.0809 43  LYS A CE  
261  N NZ  . LYS A 37  ? 0.1307 0.2643 0.2294 0.0212  -0.0043 -0.0753 43  LYS A NZ  
262  N N   . ASP A 38  ? 0.1347 0.3872 0.2980 -0.0043 0.0073  -0.1193 44  ASP A N   
263  C CA  . ASP A 38  ? 0.1583 0.4119 0.3133 -0.0213 0.0155  -0.1141 44  ASP A CA  
264  C C   . ASP A 38  ? 0.1509 0.3818 0.2871 -0.0313 0.0227  -0.0983 44  ASP A C   
265  O O   . ASP A 38  ? 0.1425 0.3680 0.2689 -0.0444 0.0278  -0.0923 44  ASP A O   
266  C CB  . ASP A 38  ? 0.2038 0.4738 0.3615 -0.0309 0.0233  -0.1227 44  ASP A CB  
267  C CG  . ASP A 38  ? 0.2398 0.5017 0.3850 -0.0385 0.0325  -0.1179 44  ASP A CG  
268  O OD1 . ASP A 38  ? 0.2479 0.4922 0.3841 -0.0351 0.0331  -0.1085 44  ASP A OD1 
269  O OD2 . ASP A 38  ? 0.2617 0.5357 0.4060 -0.0485 0.0392  -0.1243 44  ASP A OD2 
270  N N   . SER A 39  ? 0.1146 0.3308 0.2457 -0.0249 0.0225  -0.0918 45  SER A N   
271  C CA  . SER A 39  ? 0.1201 0.3139 0.2344 -0.0334 0.0289  -0.0778 45  SER A CA  
272  C C   . SER A 39  ? 0.1479 0.3267 0.2598 -0.0238 0.0257  -0.0730 45  SER A C   
273  O O   . SER A 39  ? 0.1226 0.2978 0.2374 -0.0098 0.0191  -0.0770 45  SER A O   
274  C CB  . SER A 39  ? 0.1549 0.3406 0.2580 -0.0402 0.0361  -0.0730 45  SER A CB  
275  O OG  . SER A 39  ? 0.2308 0.4343 0.3417 -0.0394 0.0370  -0.0837 45  SER A OG  
276  N N   . PHE A 40  ? 0.1300 0.2841 0.2255 -0.0302 0.0283  -0.0611 46  PHE A N   
277  C CA  . PHE A 40  ? 0.1255 0.2493 0.2056 -0.0232 0.0267  -0.0521 46  PHE A CA  
278  C C   . PHE A 40  ? 0.1297 0.2500 0.2094 -0.0210 0.0316  -0.0505 46  PHE A C   
279  O O   . PHE A 40  ? 0.1218 0.2538 0.2054 -0.0299 0.0386  -0.0509 46  PHE A O   
280  C CB  . PHE A 40  ? 0.1287 0.2326 0.1959 -0.0320 0.0302  -0.0426 46  PHE A CB  
281  C CG  . PHE A 40  ? 0.1422 0.2188 0.1962 -0.0283 0.0320  -0.0347 46  PHE A CG  
282  C CD1 . PHE A 40  ? 0.1518 0.2097 0.1942 -0.0208 0.0270  -0.0330 46  PHE A CD1 
283  C CD2 . PHE A 40  ? 0.1425 0.2121 0.1949 -0.0331 0.0385  -0.0296 46  PHE A CD2 
284  C CE1 . PHE A 40  ? 0.1847 0.2193 0.2152 -0.0196 0.0305  -0.0271 46  PHE A CE1 
285  C CE2 . PHE A 40  ? 0.1461 0.1942 0.1899 -0.0302 0.0406  -0.0244 46  PHE A CE2 
286  C CZ  . PHE A 40  ? 0.1606 0.1920 0.1939 -0.0241 0.0376  -0.0235 46  PHE A CZ  
287  N N   . HIS A 41  ? 0.1164 0.2189 0.1891 -0.0103 0.0277  -0.0485 47  HIS A N   
288  C CA  . HIS A 41  ? 0.1439 0.2403 0.2154 -0.0076 0.0315  -0.0472 47  HIS A CA  
289  C C   . HIS A 41  ? 0.1421 0.2104 0.1990 -0.0092 0.0344  -0.0373 47  HIS A C   
290  O O   . HIS A 41  ? 0.1595 0.2080 0.2054 -0.0037 0.0302  -0.0344 47  HIS A O   
291  C CB  . HIS A 41  ? 0.1144 0.2129 0.1911 0.0060  0.0245  -0.0548 47  HIS A CB  
292  C CG  . HIS A 41  ? 0.1257 0.2196 0.2021 0.0083  0.0284  -0.0549 47  HIS A CG  
293  N ND1 . HIS A 41  ? 0.1502 0.2302 0.2233 0.0199  0.0225  -0.0572 47  HIS A ND1 
294  C CD2 . HIS A 41  ? 0.1228 0.2221 0.2001 0.0000  0.0367  -0.0530 47  HIS A CD2 
295  C CE1 . HIS A 41  ? 0.1592 0.2386 0.2331 0.0186  0.0279  -0.0576 47  HIS A CE1 
296  N NE2 . HIS A 41  ? 0.1521 0.2434 0.2283 0.0067  0.0363  -0.0550 47  HIS A NE2 
297  N N   . HIS A 42  ? 0.1263 0.1926 0.1826 -0.0173 0.0411  -0.0327 48  HIS A N   
298  C CA  . HIS A 42  ? 0.1424 0.1863 0.1898 -0.0187 0.0442  -0.0257 48  HIS A CA  
299  C C   . HIS A 42  ? 0.1707 0.2067 0.2164 -0.0117 0.0439  -0.0270 48  HIS A C   
300  O O   . HIS A 42  ? 0.1394 0.1786 0.1885 -0.0138 0.0471  -0.0270 48  HIS A O   
301  C CB  . HIS A 42  ? 0.1364 0.1809 0.1854 -0.0285 0.0486  -0.0213 48  HIS A CB  
302  C CG  . HIS A 42  ? 0.1852 0.2106 0.2299 -0.0297 0.0511  -0.0165 48  HIS A CG  
303  N ND1 . HIS A 42  ? 0.1807 0.1961 0.2223 -0.0329 0.0517  -0.0142 48  HIS A ND1 
304  C CD2 . HIS A 42  ? 0.1709 0.1868 0.2154 -0.0280 0.0528  -0.0152 48  HIS A CD2 
305  C CE1 . HIS A 42  ? 0.1937 0.1952 0.2328 -0.0313 0.0520  -0.0124 48  HIS A CE1 
306  N NE2 . HIS A 42  ? 0.1827 0.1846 0.2238 -0.0287 0.0526  -0.0129 48  HIS A NE2 
307  N N   . ASN A 43  ? 0.1486 0.1724 0.1872 -0.0035 0.0389  -0.0283 49  ASN A N   
308  C CA  . ASN A 43  ? 0.1799 0.1977 0.2177 0.0040  0.0367  -0.0312 49  ASN A CA  
309  C C   . ASN A 43  ? 0.2022 0.2013 0.2328 0.0010  0.0417  -0.0266 49  ASN A C   
310  O O   . ASN A 43  ? 0.1789 0.1726 0.2091 0.0054  0.0409  -0.0289 49  ASN A O   
311  C CB  . ASN A 43  ? 0.1903 0.1982 0.2213 0.0143  0.0271  -0.0341 49  ASN A CB  
312  C CG  . ASN A 43  ? 0.2581 0.2423 0.2713 0.0124  0.0254  -0.0279 49  ASN A CG  
313  O OD1 . ASN A 43  ? 0.2624 0.2355 0.2688 0.0044  0.0328  -0.0226 49  ASN A OD1 
314  N ND2 . ASN A 43  ? 0.2715 0.2478 0.2767 0.0200  0.0150  -0.0296 49  ASN A ND2 
315  N N   . VAL A 44  ? 0.1723 0.1624 0.1989 -0.0063 0.0468  -0.0215 50  VAL A N   
316  C CA  . VAL A 44  ? 0.2313 0.2100 0.2569 -0.0104 0.0524  -0.0193 50  VAL A CA  
317  C C   . VAL A 44  ? 0.1989 0.1908 0.2353 -0.0119 0.0538  -0.0209 50  VAL A C   
318  O O   . VAL A 44  ? 0.2187 0.2036 0.2557 -0.0125 0.0562  -0.0213 50  VAL A O   
319  C CB  . VAL A 44  ? 0.2322 0.2043 0.2566 -0.0174 0.0573  -0.0163 50  VAL A CB  
320  C CG1 . VAL A 44  ? 0.2511 0.2173 0.2804 -0.0216 0.0628  -0.0163 50  VAL A CG1 
321  C CG2 . VAL A 44  ? 0.2589 0.2149 0.2683 -0.0175 0.0571  -0.0151 50  VAL A CG2 
322  N N   . ALA A 45  ? 0.1494 0.1599 0.1929 -0.0136 0.0526  -0.0224 51  ALA A N   
323  C CA  . ALA A 45  ? 0.1381 0.1595 0.1874 -0.0167 0.0538  -0.0236 51  ALA A CA  
324  C C   . ALA A 45  ? 0.1552 0.1890 0.2074 -0.0116 0.0522  -0.0303 51  ALA A C   
325  O O   . ALA A 45  ? 0.1311 0.1770 0.1862 -0.0155 0.0536  -0.0324 51  ALA A O   
326  C CB  . ALA A 45  ? 0.1288 0.1587 0.1790 -0.0240 0.0526  -0.0203 51  ALA A CB  
327  N N   . ALA A 46  ? 0.1367 0.1669 0.1874 -0.0031 0.0485  -0.0342 52  ALA A N   
328  C CA  . ALA A 46  ? 0.1559 0.2008 0.2132 0.0032  0.0461  -0.0430 52  ALA A CA  
329  C C   . ALA A 46  ? 0.1522 0.1942 0.2099 0.0048  0.0476  -0.0463 52  ALA A C   
330  O O   . ALA A 46  ? 0.1315 0.1906 0.1959 0.0062  0.0484  -0.0542 52  ALA A O   
331  C CB  . ALA A 46  ? 0.1382 0.1768 0.1942 0.0138  0.0389  -0.0467 52  ALA A CB  
332  N N   . LEU A 47  ? 0.1496 0.1713 0.2006 0.0037  0.0487  -0.0414 53  LEU A N   
333  C CA  . LEU A 47  ? 0.1588 0.1770 0.2102 0.0045  0.0497  -0.0448 53  LEU A CA  
334  C C   . LEU A 47  ? 0.1754 0.2062 0.2297 -0.0041 0.0533  -0.0439 53  LEU A C   
335  O O   . LEU A 47  ? 0.1788 0.2197 0.2350 -0.0041 0.0540  -0.0500 53  LEU A O   
336  C CB  . LEU A 47  ? 0.1461 0.1388 0.1896 0.0049  0.0499  -0.0409 53  LEU A CB  
337  C CG  . LEU A 47  ? 0.2098 0.1839 0.2440 0.0119  0.0452  -0.0402 53  LEU A CG  
338  C CD1 . LEU A 47  ? 0.1896 0.1365 0.2123 0.0094  0.0467  -0.0367 53  LEU A CD1 
339  C CD2 . LEU A 47  ? 0.1804 0.1602 0.2180 0.0229  0.0385  -0.0485 53  LEU A CD2 
340  N N   . ARG A 48  ? 0.1527 0.1822 0.2063 -0.0115 0.0547  -0.0369 54  ARG A N   
341  C CA  . ARG A 48  ? 0.1476 0.1867 0.2009 -0.0197 0.0554  -0.0351 54  ARG A CA  
342  C C   . ARG A 48  ? 0.1738 0.2315 0.2256 -0.0222 0.0552  -0.0390 54  ARG A C   
343  O O   . ARG A 48  ? 0.1783 0.2436 0.2262 -0.0272 0.0556  -0.0412 54  ARG A O   
344  C CB  . ARG A 48  ? 0.1538 0.1858 0.2070 -0.0253 0.0545  -0.0274 54  ARG A CB  
345  C CG  . ARG A 48  ? 0.1721 0.2069 0.2219 -0.0334 0.0518  -0.0234 54  ARG A CG  
346  C CD  . ARG A 48  ? 0.2013 0.2301 0.2524 -0.0347 0.0499  -0.0238 54  ARG A CD  
347  N NE  . ARG A 48  ? 0.1881 0.2049 0.2463 -0.0306 0.0505  -0.0241 54  ARG A NE  
348  C CZ  . ARG A 48  ? 0.2011 0.2101 0.2650 -0.0316 0.0491  -0.0210 54  ARG A CZ  
349  N NH1 . ARG A 48  ? 0.1531 0.1622 0.2158 -0.0349 0.0450  -0.0164 54  ARG A NH1 
350  N NH2 . ARG A 48  ? 0.1678 0.1677 0.2361 -0.0285 0.0508  -0.0230 54  ARG A NH2 
351  N N   . ALA A 49  ? 0.1261 0.1908 0.1802 -0.0193 0.0541  -0.0405 55  ALA A N   
352  C CA  . ALA A 49  ? 0.1342 0.2164 0.1882 -0.0217 0.0537  -0.0454 55  ALA A CA  
353  C C   . ALA A 49  ? 0.1305 0.2217 0.1887 -0.0160 0.0537  -0.0554 55  ALA A C   
354  O O   . ALA A 49  ? 0.1301 0.2362 0.1886 -0.0196 0.0543  -0.0609 55  ALA A O   
355  C CB  . ALA A 49  ? 0.1340 0.2232 0.1922 -0.0201 0.0522  -0.0461 55  ALA A CB  
356  N N   . SER A 50  ? 0.1428 0.2239 0.2038 -0.0077 0.0531  -0.0585 56  SER A N   
357  C CA  . SER A 50  ? 0.1638 0.2504 0.2281 -0.0018 0.0519  -0.0680 56  SER A CA  
358  C C   . SER A 50  ? 0.1877 0.2737 0.2467 -0.0075 0.0545  -0.0691 56  SER A C   
359  O O   . SER A 50  ? 0.1644 0.2557 0.2256 -0.0039 0.0539  -0.0774 56  SER A O   
360  C CB  . SER A 50  ? 0.1566 0.2287 0.2242 0.0108  0.0481  -0.0714 56  SER A CB  
361  O OG  . SER A 50  ? 0.1728 0.2466 0.2451 0.0171  0.0445  -0.0725 56  SER A OG  
362  N N   . VAL A 51  ? 0.1674 0.2470 0.2199 -0.0160 0.0566  -0.0618 57  VAL A N   
363  C CA  . VAL A 51  ? 0.1998 0.2787 0.2470 -0.0215 0.0585  -0.0636 57  VAL A CA  
364  C C   . VAL A 51  ? 0.2133 0.2979 0.2506 -0.0345 0.0598  -0.0583 57  VAL A C   
365  O O   . VAL A 51  ? 0.2007 0.2877 0.2305 -0.0410 0.0613  -0.0607 57  VAL A O   
366  C CB  . VAL A 51  ? 0.1837 0.2442 0.2325 -0.0184 0.0577  -0.0606 57  VAL A CB  
367  C CG1 . VAL A 51  ? 0.1740 0.2244 0.2277 -0.0071 0.0564  -0.0661 57  VAL A CG1 
368  C CG2 . VAL A 51  ? 0.1743 0.2237 0.2228 -0.0218 0.0559  -0.0498 57  VAL A CG2 
369  N N   . GLU A 52  ? 0.1691 0.2539 0.2039 -0.0391 0.0587  -0.0512 58  GLU A N   
370  C CA  . GLU A 52  ? 0.2067 0.2909 0.2292 -0.0518 0.0581  -0.0446 58  GLU A CA  
371  C C   . GLU A 52  ? 0.1705 0.2661 0.1866 -0.0577 0.0589  -0.0466 58  GLU A C   
372  O O   . GLU A 52  ? 0.1473 0.2450 0.1686 -0.0549 0.0580  -0.0454 58  GLU A O   
373  C CB  . GLU A 52  ? 0.1839 0.2544 0.2080 -0.0536 0.0548  -0.0342 58  GLU A CB  
374  C CG  . GLU A 52  ? 0.2471 0.3131 0.2571 -0.0662 0.0517  -0.0264 58  GLU A CG  
375  C CD  . GLU A 52  ? 0.2688 0.3185 0.2816 -0.0660 0.0456  -0.0170 58  GLU A CD  
376  O OE1 . GLU A 52  ? 0.2553 0.2974 0.2805 -0.0569 0.0444  -0.0170 58  GLU A OE1 
377  O OE2 . GLU A 52  ? 0.2749 0.3183 0.2765 -0.0753 0.0418  -0.0103 58  GLU A OE2 
378  N N   . THR A 53  ? 0.2023 0.3050 0.2067 -0.0671 0.0608  -0.0504 59  THR A N   
379  C CA  . THR A 53  ? 0.2150 0.3280 0.2126 -0.0754 0.0625  -0.0532 59  THR A CA  
380  C C   . THR A 53  ? 0.2319 0.3361 0.2222 -0.0818 0.0597  -0.0435 59  THR A C   
381  O O   . THR A 53  ? 0.2140 0.3031 0.1951 -0.0865 0.0561  -0.0336 59  THR A O   
382  C CB  . THR A 53  ? 0.2324 0.3498 0.2138 -0.0877 0.0648  -0.0569 59  THR A CB  
383  O OG1 . THR A 53  ? 0.2745 0.4005 0.2634 -0.0816 0.0673  -0.0672 59  THR A OG1 
384  C CG2 . THR A 53  ? 0.2236 0.3514 0.1981 -0.0983 0.0674  -0.0607 59  THR A CG2 
385  N N   . GLY A 54  ? 0.2070 0.3205 0.2019 -0.0824 0.0610  -0.0469 60  GLY A N   
386  C CA  . GLY A 54  ? 0.1981 0.3041 0.1858 -0.0888 0.0588  -0.0393 60  GLY A CA  
387  C C   . GLY A 54  ? 0.2221 0.3180 0.2198 -0.0799 0.0554  -0.0325 60  GLY A C   
388  O O   . GLY A 54  ? 0.2277 0.3179 0.2215 -0.0841 0.0535  -0.0272 60  GLY A O   
389  N N   . PHE A 55  ? 0.1803 0.2733 0.1902 -0.0685 0.0548  -0.0330 61  PHE A N   
390  C CA  . PHE A 55  ? 0.1635 0.2457 0.1810 -0.0619 0.0520  -0.0268 61  PHE A CA  
391  C C   . PHE A 55  ? 0.1693 0.2595 0.1967 -0.0558 0.0524  -0.0306 61  PHE A C   
392  O O   . PHE A 55  ? 0.1310 0.2134 0.1606 -0.0542 0.0503  -0.0254 61  PHE A O   
393  C CB  . PHE A 55  ? 0.1560 0.2302 0.1806 -0.0541 0.0516  -0.0263 61  PHE A CB  
394  C CG  . PHE A 55  ? 0.1589 0.2205 0.1895 -0.0494 0.0493  -0.0204 61  PHE A CG  
395  C CD1 . PHE A 55  ? 0.1954 0.2445 0.2219 -0.0546 0.0457  -0.0126 61  PHE A CD1 
396  C CD2 . PHE A 55  ? 0.1721 0.2331 0.2116 -0.0403 0.0503  -0.0233 61  PHE A CD2 
397  C CE1 . PHE A 55  ? 0.2093 0.2474 0.2424 -0.0502 0.0437  -0.0090 61  PHE A CE1 
398  C CE2 . PHE A 55  ? 0.1791 0.2278 0.2218 -0.0375 0.0489  -0.0188 61  PHE A CE2 
399  C CZ  . PHE A 55  ? 0.2028 0.2409 0.2430 -0.0420 0.0459  -0.0122 61  PHE A CZ  
400  N N   . ALA A 56  ? 0.1798 0.2857 0.2139 -0.0525 0.0545  -0.0403 62  ALA A N   
401  C CA  . ALA A 56  ? 0.1458 0.2595 0.1911 -0.0454 0.0536  -0.0448 62  ALA A CA  
402  C C   . ALA A 56  ? 0.1244 0.2398 0.1673 -0.0517 0.0530  -0.0420 62  ALA A C   
403  O O   . ALA A 56  ? 0.1189 0.2334 0.1683 -0.0470 0.0512  -0.0412 62  ALA A O   
404  C CB  . ALA A 56  ? 0.1562 0.2878 0.2109 -0.0408 0.0547  -0.0572 62  ALA A CB  
405  N N   . LYS A 57  ? 0.1328 0.2493 0.1651 -0.0630 0.0543  -0.0405 63  LYS A N   
406  C CA  . LYS A 57  ? 0.1867 0.3039 0.2157 -0.0699 0.0539  -0.0384 63  LYS A CA  
407  C C   . LYS A 57  ? 0.1969 0.2967 0.2238 -0.0685 0.0505  -0.0285 63  LYS A C   
408  O O   . LYS A 57  ? 0.1713 0.2711 0.1985 -0.0715 0.0496  -0.0274 63  LYS A O   
409  C CB  . LYS A 57  ? 0.1740 0.2932 0.1888 -0.0837 0.0562  -0.0387 63  LYS A CB  
410  C CG  . LYS A 57  ? 0.2300 0.3311 0.2293 -0.0902 0.0541  -0.0292 63  LYS A CG  
411  C CD  . LYS A 57  ? 0.3137 0.4155 0.2958 -0.1057 0.0558  -0.0295 63  LYS A CD  
412  C CE  . LYS A 57  ? 0.3791 0.4656 0.3437 -0.1130 0.0532  -0.0224 63  LYS A CE  
413  N NZ  . LYS A 57  ? 0.4369 0.5316 0.4034 -0.1104 0.0557  -0.0281 63  LYS A NZ  
414  N N   . LYS A 58  ? 0.1842 0.2701 0.2104 -0.0639 0.0487  -0.0225 64  LYS A N   
415  C CA  . LYS A 58  ? 0.1938 0.2644 0.2208 -0.0614 0.0457  -0.0151 64  LYS A CA  
416  C C   . LYS A 58  ? 0.1462 0.2182 0.1834 -0.0524 0.0459  -0.0176 64  LYS A C   
417  O O   . LYS A 58  ? 0.1318 0.1923 0.1695 -0.0508 0.0443  -0.0132 64  LYS A O   
418  C CB  . LYS A 58  ? 0.2005 0.2567 0.2233 -0.0617 0.0436  -0.0091 64  LYS A CB  
419  C CG  . LYS A 58  ? 0.2525 0.3049 0.2620 -0.0723 0.0424  -0.0059 64  LYS A CG  
420  C CD  . LYS A 58  ? 0.3743 0.4138 0.3803 -0.0733 0.0392  -0.0008 64  LYS A CD  
421  C CE  . LYS A 58  ? 0.4824 0.5112 0.4716 -0.0848 0.0350  0.0049  64  LYS A CE  
422  N NZ  . LYS A 58  ? 0.5901 0.6056 0.5781 -0.0866 0.0304  0.0105  64  LYS A NZ  
423  N N   . THR A 59  ? 0.1378 0.2229 0.1824 -0.0468 0.0476  -0.0253 65  THR A N   
424  C CA  . THR A 59  ? 0.1457 0.2305 0.1980 -0.0385 0.0476  -0.0281 65  THR A CA  
425  C C   . THR A 59  ? 0.1476 0.2478 0.2077 -0.0370 0.0467  -0.0349 65  THR A C   
426  O O   . THR A 59  ? 0.1183 0.2201 0.1852 -0.0299 0.0461  -0.0386 65  THR A O   
427  C CB  . THR A 59  ? 0.1319 0.2174 0.1886 -0.0307 0.0488  -0.0325 65  THR A CB  
428  O OG1 . THR A 59  ? 0.1231 0.2258 0.1850 -0.0286 0.0488  -0.0412 65  THR A OG1 
429  C CG2 . THR A 59  ? 0.1306 0.2032 0.1811 -0.0328 0.0493  -0.0271 65  THR A CG2 
430  N N   . PHE A 60  ? 0.1135 0.2251 0.1731 -0.0437 0.0467  -0.0377 66  PHE A N   
431  C CA  . PHE A 60  ? 0.1332 0.2610 0.2015 -0.0432 0.0453  -0.0450 66  PHE A CA  
432  C C   . PHE A 60  ? 0.1736 0.2976 0.2352 -0.0532 0.0453  -0.0406 66  PHE A C   
433  O O   . PHE A 60  ? 0.1436 0.2632 0.1958 -0.0615 0.0468  -0.0371 66  PHE A O   
434  C CB  . PHE A 60  ? 0.1393 0.2880 0.2161 -0.0414 0.0456  -0.0563 66  PHE A CB  
435  C CG  . PHE A 60  ? 0.0918 0.2456 0.1784 -0.0289 0.0435  -0.0632 66  PHE A CG  
436  C CD1 . PHE A 60  ? 0.1259 0.2864 0.2244 -0.0179 0.0384  -0.0694 66  PHE A CD1 
437  C CD2 . PHE A 60  ? 0.0950 0.2457 0.1785 -0.0275 0.0454  -0.0637 66  PHE A CD2 
438  C CE1 . PHE A 60  ? 0.1122 0.2732 0.2181 -0.0045 0.0344  -0.0758 66  PHE A CE1 
439  C CE2 . PHE A 60  ? 0.1164 0.2688 0.2080 -0.0155 0.0428  -0.0701 66  PHE A CE2 
440  C CZ  . PHE A 60  ? 0.1333 0.2893 0.2355 -0.0035 0.0370  -0.0760 66  PHE A CZ  
441  N N   . ILE A 61  ? 0.1559 0.2816 0.2219 -0.0527 0.0433  -0.0415 67  ILE A N   
442  C CA  . ILE A 61  ? 0.1660 0.2854 0.2255 -0.0615 0.0428  -0.0373 67  ILE A CA  
443  C C   . ILE A 61  ? 0.1788 0.3178 0.2483 -0.0626 0.0412  -0.0462 67  ILE A C   
444  O O   . ILE A 61  ? 0.1432 0.2901 0.2226 -0.0559 0.0381  -0.0511 67  ILE A O   
445  C CB  . ILE A 61  ? 0.1660 0.2644 0.2195 -0.0611 0.0417  -0.0291 67  ILE A CB  
446  C CG1 . ILE A 61  ? 0.1686 0.2504 0.2161 -0.0580 0.0424  -0.0223 67  ILE A CG1 
447  C CG2 . ILE A 61  ? 0.1860 0.2766 0.2329 -0.0695 0.0406  -0.0254 67  ILE A CG2 
448  C CD1 . ILE A 61  ? 0.1454 0.2078 0.1894 -0.0558 0.0418  -0.0168 67  ILE A CD1 
449  N N   . SER A 62  ? 0.1981 0.3452 0.2652 -0.0712 0.0429  -0.0490 68  SER A N   
450  C CA  . SER A 62  ? 0.1955 0.3628 0.2732 -0.0728 0.0415  -0.0586 68  SER A CA  
451  C C   . SER A 62  ? 0.1872 0.3504 0.2675 -0.0722 0.0375  -0.0572 68  SER A C   
452  O O   . SER A 62  ? 0.1735 0.3177 0.2428 -0.0780 0.0378  -0.0486 68  SER A O   
453  C CB  . SER A 62  ? 0.2008 0.3729 0.2718 -0.0851 0.0455  -0.0602 68  SER A CB  
454  O OG  . SER A 62  ? 0.2488 0.4366 0.3285 -0.0884 0.0443  -0.0680 68  SER A OG  
455  N N   . TYR A 63  ? 0.1714 0.3529 0.2669 -0.0647 0.0324  -0.0668 69  TYR A N   
456  C CA  . TYR A 63  ? 0.1812 0.3623 0.2796 -0.0652 0.0271  -0.0676 69  TYR A CA  
457  C C   . TYR A 63  ? 0.2133 0.3966 0.3083 -0.0761 0.0284  -0.0682 69  TYR A C   
458  O O   . TYR A 63  ? 0.1977 0.3663 0.2842 -0.0821 0.0277  -0.0626 69  TYR A O   
459  C CB  . TYR A 63  ? 0.1642 0.3653 0.2800 -0.0530 0.0174  -0.0789 69  TYR A CB  
460  C CG  . TYR A 63  ? 0.1563 0.3442 0.2687 -0.0387 0.0126  -0.0765 69  TYR A CG  
461  C CD1 . TYR A 63  ? 0.1201 0.2739 0.2115 -0.0361 0.0123  -0.0646 69  TYR A CD1 
462  C CD2 . TYR A 63  ? 0.1164 0.3196 0.2423 -0.0265 0.0082  -0.0854 69  TYR A CD2 
463  C CE1 . TYR A 63  ? 0.1166 0.2515 0.1989 -0.0236 0.0085  -0.0608 69  TYR A CE1 
464  C CE2 . TYR A 63  ? 0.1232 0.3055 0.2398 -0.0127 0.0029  -0.0814 69  TYR A CE2 
465  C CZ  . TYR A 63  ? 0.1380 0.2858 0.2318 -0.0122 0.0034  -0.0686 69  TYR A CZ  
466  O OH  . TYR A 63  ? 0.1168 0.2435 0.2002 -0.0007 -0.0009 -0.0649 69  TYR A OH  
467  N N   . SER A 64  ? 0.1820 0.3840 0.2840 -0.0790 0.0305  -0.0764 70  SER A N   
468  C CA  . SER A 64  ? 0.2171 0.4259 0.3193 -0.0888 0.0313  -0.0796 70  SER A CA  
469  C C   . SER A 64  ? 0.2260 0.4125 0.3096 -0.1009 0.0362  -0.0688 70  SER A C   
470  O O   . SER A 64  ? 0.2437 0.4253 0.3237 -0.1083 0.0353  -0.0676 70  SER A O   
471  C CB  . SER A 64  ? 0.1889 0.4241 0.3034 -0.0901 0.0338  -0.0924 70  SER A CB  
472  O OG  . SER A 64  ? 0.2819 0.5152 0.3884 -0.0946 0.0409  -0.0910 70  SER A OG  
473  N N   . VAL A 65  ? 0.2151 0.3866 0.2869 -0.1023 0.0400  -0.0610 71  VAL A N   
474  C CA  . VAL A 65  ? 0.2326 0.3810 0.2873 -0.1115 0.0419  -0.0508 71  VAL A CA  
475  C C   . VAL A 65  ? 0.2574 0.3855 0.3074 -0.1097 0.0379  -0.0437 71  VAL A C   
476  O O   . VAL A 65  ? 0.2507 0.3651 0.2920 -0.1173 0.0373  -0.0394 71  VAL A O   
477  C CB  . VAL A 65  ? 0.2300 0.3670 0.2745 -0.1114 0.0445  -0.0447 71  VAL A CB  
478  C CG1 . VAL A 65  ? 0.2141 0.3241 0.2427 -0.1172 0.0434  -0.0334 71  VAL A CG1 
479  C CG2 . VAL A 65  ? 0.2037 0.3585 0.2483 -0.1180 0.0496  -0.0522 71  VAL A CG2 
480  N N   . THR A 66  ? 0.2184 0.3436 0.2734 -0.1002 0.0353  -0.0433 72  THR A N   
481  C CA  . THR A 66  ? 0.2376 0.3434 0.2871 -0.0993 0.0326  -0.0382 72  THR A CA  
482  C C   . THR A 66  ? 0.2431 0.3585 0.2989 -0.1012 0.0288  -0.0449 72  THR A C   
483  O O   . THR A 66  ? 0.2638 0.3645 0.3127 -0.1060 0.0273  -0.0423 72  THR A O   
484  C CB  . THR A 66  ? 0.2407 0.3371 0.2902 -0.0905 0.0325  -0.0351 72  THR A CB  
485  O OG1 . THR A 66  ? 0.2551 0.3376 0.2973 -0.0893 0.0347  -0.0276 72  THR A OG1 
486  C CG2 . THR A 66  ? 0.2352 0.3150 0.2800 -0.0903 0.0307  -0.0333 72  THR A CG2 
487  N N   . PHE A 67  ? 0.2089 0.3490 0.2785 -0.0968 0.0258  -0.0545 73  PHE A N   
488  C CA  . PHE A 67  ? 0.2517 0.4007 0.3275 -0.0966 0.0190  -0.0616 73  PHE A CA  
489  C C   . PHE A 67  ? 0.2420 0.4127 0.3279 -0.1005 0.0171  -0.0702 73  PHE A C   
490  O O   . PHE A 67  ? 0.2464 0.4208 0.3349 -0.1019 0.0109  -0.0750 73  PHE A O   
491  C CB  . PHE A 67  ? 0.2052 0.3637 0.2892 -0.0861 0.0121  -0.0673 73  PHE A CB  
492  C CG  . PHE A 67  ? 0.1879 0.3160 0.2553 -0.0787 0.0142  -0.0572 73  PHE A CG  
493  C CD1 . PHE A 67  ? 0.1941 0.2964 0.2462 -0.0807 0.0143  -0.0518 73  PHE A CD1 
494  C CD2 . PHE A 67  ? 0.2034 0.3298 0.2717 -0.0700 0.0164  -0.0545 73  PHE A CD2 
495  C CE1 . PHE A 67  ? 0.2364 0.3140 0.2759 -0.0748 0.0175  -0.0446 73  PHE A CE1 
496  C CE2 . PHE A 67  ? 0.2094 0.3092 0.2637 -0.0643 0.0189  -0.0463 73  PHE A CE2 
497  C CZ  . PHE A 67  ? 0.2128 0.2896 0.2537 -0.0668 0.0198  -0.0417 73  PHE A CZ  
498  N N   . LYS A 68  ? 0.2038 0.3887 0.2949 -0.1026 0.0222  -0.0733 74  LYS A N   
499  C CA  . LYS A 68  ? 0.2582 0.4629 0.3581 -0.1088 0.0227  -0.0820 74  LYS A CA  
500  C C   . LYS A 68  ? 0.2673 0.4923 0.3839 -0.1004 0.0128  -0.0930 74  LYS A C   
501  O O   . LYS A 68  ? 0.2105 0.4452 0.3369 -0.0878 0.0071  -0.0977 74  LYS A O   
502  C CB  . LYS A 68  ? 0.2855 0.4733 0.3720 -0.1218 0.0260  -0.0757 74  LYS A CB  
503  C CG  . LYS A 68  ? 0.3267 0.4930 0.3965 -0.1275 0.0324  -0.0650 74  LYS A CG  
504  C CD  . LYS A 68  ? 0.4436 0.5872 0.4995 -0.1372 0.0326  -0.0577 74  LYS A CD  
505  C CE  . LYS A 68  ? 0.5293 0.6559 0.5702 -0.1436 0.0370  -0.0493 74  LYS A CE  
506  N NZ  . LYS A 68  ? 0.6030 0.7105 0.6317 -0.1541 0.0364  -0.0440 74  LYS A NZ  
507  N N   . ASP A 69  ? 0.2312 0.4613 0.3509 -0.1057 0.0087  -0.0974 75  ASP A N   
508  C CA  . ASP A 69  ? 0.2372 0.4878 0.3732 -0.0968 -0.0026 -0.1089 75  ASP A CA  
509  C C   . ASP A 69  ? 0.2464 0.4863 0.3781 -0.0862 -0.0150 -0.1078 75  ASP A C   
510  O O   . ASP A 69  ? 0.2209 0.4727 0.3621 -0.0767 -0.0279 -0.1163 75  ASP A O   
511  C CB  . ASP A 69  ? 0.3179 0.5762 0.4574 -0.1062 -0.0039 -0.1139 75  ASP A CB  
512  C CG  . ASP A 69  ? 0.3597 0.6400 0.5103 -0.1134 0.0043  -0.1218 75  ASP A CG  
513  O OD1 . ASP A 69  ? 0.3376 0.6272 0.4924 -0.1105 0.0104  -0.1243 75  ASP A OD1 
514  O OD2 . ASP A 69  ? 0.3887 0.6766 0.5427 -0.1227 0.0047  -0.1264 75  ASP A OD2 
515  N N   . ASN A 70  ? 0.2392 0.4551 0.3547 -0.0878 -0.0122 -0.0980 76  ASN A N   
516  C CA  . ASN A 70  ? 0.2466 0.4507 0.3538 -0.0786 -0.0230 -0.0978 76  ASN A CA  
517  C C   . ASN A 70  ? 0.2402 0.4477 0.3524 -0.0641 -0.0257 -0.0983 76  ASN A C   
518  O O   . ASN A 70  ? 0.2270 0.4098 0.3220 -0.0517 -0.0324 -0.0922 76  ASN A O   
519  C CB  . ASN A 70  ? 0.2504 0.4199 0.3338 -0.0846 -0.0165 -0.0859 76  ASN A CB  
520  C CG  . ASN A 70  ? 0.2965 0.4578 0.3722 -0.0959 -0.0179 -0.0870 76  ASN A CG  
521  O OD1 . ASN A 70  ? 0.2776 0.4266 0.3475 -0.1067 -0.0086 -0.0810 76  ASN A OD1 
522  N ND2 . ASN A 70  ? 0.2754 0.4374 0.3473 -0.0900 -0.0302 -0.0927 76  ASN A ND2 
523  N N   . PHE A 71  ? 0.2237 0.4512 0.3518 -0.0636 -0.0187 -0.1020 77  PHE A N   
524  C CA  . PHE A 71  ? 0.1844 0.4192 0.3210 -0.0502 -0.0216 -0.1051 77  PHE A CA  
525  C C   . PHE A 71  ? 0.1984 0.4580 0.3551 -0.0404 -0.0275 -0.1175 77  PHE A C   
526  O O   . PHE A 71  ? 0.1680 0.4428 0.3330 -0.0484 -0.0206 -0.1227 77  PHE A O   
527  C CB  . PHE A 71  ? 0.1831 0.4114 0.3152 -0.0558 -0.0070 -0.0976 77  PHE A CB  
528  C CG  . PHE A 71  ? 0.1775 0.4149 0.3195 -0.0430 -0.0086 -0.1020 77  PHE A CG  
529  C CD1 . PHE A 71  ? 0.1479 0.3661 0.2805 -0.0285 -0.0170 -0.0979 77  PHE A CD1 
530  C CD2 . PHE A 71  ? 0.1682 0.4207 0.3189 -0.0437 -0.0011 -0.1077 77  PHE A CD2 
531  C CE1 . PHE A 71  ? 0.1775 0.4019 0.3190 -0.0160 -0.0194 -0.1024 77  PHE A CE1 
532  C CE2 . PHE A 71  ? 0.1571 0.4162 0.3161 -0.0318 -0.0028 -0.1130 77  PHE A CE2 
533  C CZ  . PHE A 71  ? 0.1193 0.3691 0.2783 -0.0180 -0.0125 -0.1116 77  PHE A CZ  
534  N N   . ARG A 72  ? 0.1868 0.4481 0.3496 -0.0227 -0.0407 -0.1229 78  ARG A N   
535  C CA  . ARG A 72  ? 0.1986 0.4804 0.3811 -0.0113 -0.0458 -0.1354 78  ARG A CA  
536  C C   . ARG A 72  ? 0.1901 0.4667 0.3748 0.0033  -0.0496 -0.1362 78  ARG A C   
537  O O   . ARG A 72  ? 0.2099 0.4674 0.3836 0.0147  -0.0627 -0.1317 78  ARG A O   
538  C CB  . ARG A 72  ? 0.2510 0.5374 0.4398 -0.0014 -0.0635 -0.1431 78  ARG A CB  
539  C CG  . ARG A 72  ? 0.2582 0.5625 0.4677 0.0134  -0.0710 -0.1571 78  ARG A CG  
540  C CD  . ARG A 72  ? 0.2963 0.6216 0.5219 0.0121  -0.0757 -0.1687 78  ARG A CD  
541  N N   . GLN A 73  ? 0.2246 0.5150 0.4197 0.0023  -0.0387 -0.1420 79  GLN A N   
542  C CA  . GLN A 73  ? 0.1960 0.4832 0.3955 0.0167  -0.0427 -0.1455 79  GLN A CA  
543  C C   . GLN A 73  ? 0.2298 0.5208 0.4413 0.0356  -0.0612 -0.1568 79  GLN A C   
544  O O   . GLN A 73  ? 0.2119 0.5213 0.4375 0.0355  -0.0642 -0.1678 79  GLN A O   
545  C CB  . GLN A 73  ? 0.2001 0.5004 0.4049 0.0087  -0.0268 -0.1502 79  GLN A CB  
546  C CG  . GLN A 73  ? 0.2007 0.4973 0.4091 0.0215  -0.0293 -0.1544 79  GLN A CG  
547  C CD  . GLN A 73  ? 0.2545 0.5593 0.4615 0.0104  -0.0131 -0.1564 79  GLN A CD  
548  O OE1 . GLN A 73  ? 0.3339 0.6488 0.5382 -0.0056 -0.0017 -0.1568 79  GLN A OE1 
549  N NE2 . GLN A 73  ? 0.2336 0.5316 0.4399 0.0186  -0.0133 -0.1573 79  GLN A NE2 
550  N N   . GLY A 74  ? 0.2133 0.4841 0.4176 0.0519  -0.0744 -0.1540 80  GLY A N   
551  C CA  . GLY A 74  ? 0.2295 0.4963 0.4409 0.0708  -0.0935 -0.1634 80  GLY A CA  
552  C C   . GLY A 74  ? 0.2625 0.4962 0.4561 0.0862  -0.1076 -0.1555 80  GLY A C   
553  O O   . GLY A 74  ? 0.2458 0.4605 0.4213 0.0825  -0.1046 -0.1426 80  GLY A O   
554  N N   . LEU A 75  ? 0.2875 0.5125 0.4852 0.1033  -0.1239 -0.1635 81  LEU A N   
555  C CA  . LEU A 75  ? 0.2828 0.4706 0.4603 0.1186  -0.1392 -0.1564 81  LEU A CA  
556  C C   . LEU A 75  ? 0.3602 0.5212 0.5185 0.1278  -0.1615 -0.1519 81  LEU A C   
557  O O   . LEU A 75  ? 0.3809 0.5512 0.5522 0.1355  -0.1728 -0.1632 81  LEU A O   
558  C CB  . LEU A 75  ? 0.3336 0.5254 0.5255 0.1299  -0.1415 -0.1686 81  LEU A CB  
559  C CG  . LEU A 75  ? 0.3606 0.5117 0.5307 0.1438  -0.1555 -0.1613 81  LEU A CG  
560  C CD1 . LEU A 75  ? 0.3373 0.4706 0.4884 0.1369  -0.1445 -0.1459 81  LEU A CD1 
561  C CD2 . LEU A 75  ? 0.3518 0.5107 0.5389 0.1536  -0.1583 -0.1758 81  LEU A CD2 
562  N N   . VAL A 76  ? 0.3558 0.4821 0.4808 0.1260  -0.1678 -0.1357 82  VAL A N   
563  C CA  . VAL A 76  ? 0.3912 0.4859 0.4891 0.1316  -0.1878 -0.1292 82  VAL A CA  
564  C C   . VAL A 76  ? 0.4477 0.5066 0.5298 0.1482  -0.2055 -0.1284 82  VAL A C   
565  O O   . VAL A 76  ? 0.4342 0.4667 0.4987 0.1510  -0.2041 -0.1202 82  VAL A O   
566  C CB  . VAL A 76  ? 0.4056 0.4731 0.4670 0.1202  -0.1863 -0.1127 82  VAL A CB  
567  C CG1 . VAL A 76  ? 0.4141 0.4435 0.4410 0.1243  -0.2056 -0.1052 82  VAL A CG1 
568  C CG2 . VAL A 76  ? 0.3432 0.4429 0.4194 0.1017  -0.1672 -0.1143 82  VAL A CG2 
569  N N   . VAL A 77  ? 0.4329 0.4896 0.5207 0.1585  -0.2224 -0.1372 83  VAL A N   
570  C CA  . VAL A 77  ? 0.4906 0.5142 0.5654 0.1739  -0.2410 -0.1389 83  VAL A CA  
571  C C   . VAL A 77  ? 0.5203 0.4953 0.5525 0.1763  -0.2601 -0.1262 83  VAL A C   
572  O O   . VAL A 77  ? 0.5627 0.5032 0.5775 0.1872  -0.2768 -0.1256 83  VAL A O   
573  C CB  . VAL A 77  ? 0.4335 0.4871 0.5459 0.1854  -0.2480 -0.1605 83  VAL A CB  
574  C CG1 . VAL A 77  ? 0.4005 0.4916 0.5460 0.1828  -0.2294 -0.1725 83  VAL A CG1 
575  C CG2 . VAL A 77  ? 0.4334 0.5138 0.5632 0.1833  -0.2522 -0.1691 83  VAL A CG2 
576  N N   . GLY A 78  ? 0.5467 0.5163 0.5595 0.1651  -0.2581 -0.1163 84  GLY A N   
577  C CA  . GLY A 78  ? 0.5667 0.4900 0.5364 0.1653  -0.2747 -0.1048 84  GLY A CA  
578  C C   . GLY A 78  ? 0.5764 0.5062 0.5335 0.1517  -0.2701 -0.0987 84  GLY A C   
579  O O   . GLY A 78  ? 0.4965 0.4694 0.4830 0.1439  -0.2573 -0.1059 84  GLY A O   
580  N N   . ILE A 79  ? 0.6259 0.5105 0.5370 0.1475  -0.2804 -0.0857 85  ILE A N   
581  C CA  . ILE A 79  ? 0.6522 0.5338 0.5419 0.1334  -0.2764 -0.0787 85  ILE A CA  
582  C C   . ILE A 79  ? 0.6813 0.5404 0.5529 0.1391  -0.2975 -0.0789 85  ILE A C   
583  O O   . ILE A 79  ? 0.7578 0.5708 0.5956 0.1440  -0.3107 -0.0713 85  ILE A O   
584  C CB  . ILE A 79  ? 0.6891 0.5348 0.5333 0.1179  -0.2632 -0.0616 85  ILE A CB  
585  C CG1 . ILE A 79  ? 0.6430 0.5068 0.5035 0.1141  -0.2447 -0.0612 85  ILE A CG1 
586  C CG2 . ILE A 79  ? 0.6761 0.5199 0.4987 0.1022  -0.2572 -0.0566 85  ILE A CG2 
587  C CD1 . ILE A 79  ? 0.5663 0.4800 0.4617 0.1055  -0.2297 -0.0699 85  ILE A CD1 
588  N N   . ASP A 80  ? 0.6462 0.5374 0.5404 0.1378  -0.3008 -0.0881 86  ASP A N   
589  C CA  . ASP A 80  ? 0.6644 0.5394 0.5440 0.1423  -0.3207 -0.0892 86  ASP A CA  
590  C C   . ASP A 80  ? 0.7204 0.5691 0.5560 0.1253  -0.3156 -0.0758 86  ASP A C   
591  O O   . ASP A 80  ? 0.6850 0.5613 0.5313 0.1144  -0.3062 -0.0790 86  ASP A O   
592  C CB  . ASP A 80  ? 0.6399 0.5650 0.5683 0.1490  -0.3258 -0.1072 86  ASP A CB  
593  C CG  . ASP A 80  ? 0.7351 0.6474 0.6519 0.1541  -0.3472 -0.1098 86  ASP A CG  
594  O OD1 . ASP A 80  ? 0.7832 0.6478 0.6521 0.1511  -0.3579 -0.0970 86  ASP A OD1 
595  O OD2 . ASP A 80  ? 0.6991 0.6503 0.6555 0.1604  -0.3529 -0.1253 86  ASP A OD2 
596  N N   . LEU A 81  ? 0.7868 0.5809 0.5716 0.1218  -0.3208 -0.0618 87  LEU A N   
597  C CA  . LEU A 81  ? 0.7826 0.5494 0.5225 0.1033  -0.3110 -0.0491 87  LEU A CA  
598  C C   . LEU A 81  ? 0.7827 0.5511 0.5139 0.1005  -0.3227 -0.0518 87  LEU A C   
599  O O   . LEU A 81  ? 0.8352 0.6112 0.5549 0.0854  -0.3107 -0.0494 87  LEU A O   
600  C CB  . LEU A 81  ? 0.7876 0.4963 0.4761 0.0982  -0.3111 -0.0344 87  LEU A CB  
601  C CG  . LEU A 81  ? 0.8061 0.5103 0.4915 0.0920  -0.2916 -0.0284 87  LEU A CG  
602  C CD1 . LEU A 81  ? 0.8843 0.5344 0.5277 0.0902  -0.2952 -0.0172 87  LEU A CD1 
603  C CD2 . LEU A 81  ? 0.7971 0.5121 0.4721 0.0729  -0.2681 -0.0240 87  LEU A CD2 
604  N N   . LYS A 82  ? 0.8106 0.5715 0.5472 0.1149  -0.3465 -0.0575 88  LYS A N   
605  C CA  . LYS A 82  ? 0.8586 0.6174 0.5840 0.1128  -0.3599 -0.0596 88  LYS A CA  
606  C C   . LYS A 82  ? 0.8192 0.6325 0.5842 0.1078  -0.3514 -0.0711 88  LYS A C   
607  O O   . LYS A 82  ? 0.8430 0.6563 0.5910 0.0960  -0.3493 -0.0694 88  LYS A O   
608  C CB  . LYS A 82  ? 0.8362 0.5788 0.5647 0.1311  -0.3883 -0.0654 88  LYS A CB  
609  C CG  . LYS A 82  ? 0.8883 0.6070 0.5860 0.1285  -0.4057 -0.0625 88  LYS A CG  
610  N N   . ASN A 83  ? 0.7485 0.6078 0.5653 0.1151  -0.3453 -0.0835 89  ASN A N   
611  C CA  . ASN A 83  ? 0.7119 0.6232 0.5682 0.1088  -0.3360 -0.0953 89  ASN A CA  
612  C C   . ASN A 83  ? 0.6836 0.6176 0.5523 0.0954  -0.3102 -0.0940 89  ASN A C   
613  O O   . ASN A 83  ? 0.6569 0.6356 0.5633 0.0900  -0.3003 -0.1047 89  ASN A O   
614  C CB  . ASN A 83  ? 0.6743 0.6248 0.5825 0.1244  -0.3469 -0.1127 89  ASN A CB  
615  C CG  . ASN A 83  ? 0.7471 0.6761 0.6457 0.1387  -0.3742 -0.1159 89  ASN A CG  
616  O OD1 . ASN A 83  ? 0.7764 0.6885 0.6781 0.1546  -0.3873 -0.1184 89  ASN A OD1 
617  N ND2 . ASN A 83  ? 0.7339 0.6617 0.6200 0.1332  -0.3835 -0.1163 89  ASN A ND2 
618  N N   . GLN A 84  ? 0.7021 0.6052 0.5401 0.0896  -0.2991 -0.0817 90  GLN A N   
619  C CA  . GLN A 84  ? 0.6387 0.5545 0.4793 0.0757  -0.2754 -0.0789 90  GLN A CA  
620  C C   . GLN A 84  ? 0.5884 0.5559 0.4838 0.0786  -0.2657 -0.0918 90  GLN A C   
621  O O   . GLN A 84  ? 0.5558 0.5551 0.4721 0.0669  -0.2530 -0.0980 90  GLN A O   
622  C CB  . GLN A 84  ? 0.6275 0.5383 0.4443 0.0576  -0.2658 -0.0756 90  GLN A CB  
623  C CG  . GLN A 84  ? 0.7100 0.5709 0.4721 0.0529  -0.2726 -0.0637 90  GLN A CG  
624  C CD  . GLN A 84  ? 0.7118 0.5382 0.4356 0.0412  -0.2552 -0.0512 90  GLN A CD  
625  O OE1 . GLN A 84  ? 0.7435 0.5741 0.4593 0.0259  -0.2368 -0.0505 90  GLN A OE1 
626  N NE2 . GLN A 84  ? 0.7322 0.5235 0.4326 0.0476  -0.2603 -0.0422 90  GLN A NE2 
627  N N   . MET A 85  ? 0.5764 0.5507 0.4942 0.0934  -0.2708 -0.0962 91  MET A N   
628  C CA  . MET A 85  ? 0.5213 0.5434 0.4903 0.0966  -0.2608 -0.1092 91  MET A CA  
629  C C   . MET A 85  ? 0.5283 0.5417 0.4988 0.1023  -0.2533 -0.1055 91  MET A C   
630  O O   . MET A 85  ? 0.5737 0.5480 0.5163 0.1110  -0.2633 -0.0972 91  MET A O   
631  C CB  . MET A 85  ? 0.5246 0.5740 0.5299 0.1102  -0.2748 -0.1242 91  MET A CB  
632  C CG  . MET A 85  ? 0.5880 0.6541 0.5996 0.1040  -0.2810 -0.1302 91  MET A CG  
633  S SD  . MET A 85  ? 0.6519 0.7790 0.7132 0.0909  -0.2616 -0.1444 91  MET A SD  
634  C CE  . MET A 85  ? 0.5446 0.7011 0.6459 0.1070  -0.2777 -0.1631 91  MET A CE  
635  N N   . VAL A 86  ? 0.4533 0.5016 0.4546 0.0962  -0.2353 -0.1114 92  VAL A N   
636  C CA  . VAL A 86  ? 0.4698 0.5191 0.4813 0.1022  -0.2275 -0.1110 92  VAL A CA  
637  C C   . VAL A 86  ? 0.4521 0.5393 0.5103 0.1134  -0.2286 -0.1275 92  VAL A C   
638  O O   . VAL A 86  ? 0.4172 0.5461 0.5089 0.1066  -0.2187 -0.1386 92  VAL A O   
639  C CB  . VAL A 86  ? 0.4317 0.4918 0.4435 0.0872  -0.2061 -0.1067 92  VAL A CB  
640  C CG1 . VAL A 86  ? 0.4586 0.5331 0.4930 0.0933  -0.1969 -0.1102 92  VAL A CG1 
641  C CG2 . VAL A 86  ? 0.4450 0.4600 0.4059 0.0780  -0.2047 -0.0914 92  VAL A CG2 
642  N N   . LEU A 87  ? 0.4539 0.5242 0.5119 0.1294  -0.2393 -0.1294 93  LEU A N   
643  C CA  . LEU A 87  ? 0.4380 0.5361 0.5342 0.1421  -0.2438 -0.1466 93  LEU A CA  
644  C C   . LEU A 87  ? 0.4380 0.5601 0.5592 0.1410  -0.2260 -0.1524 93  LEU A C   
645  O O   . LEU A 87  ? 0.4371 0.5345 0.5412 0.1444  -0.2243 -0.1441 93  LEU A O   
646  C CB  . LEU A 87  ? 0.4565 0.5193 0.5367 0.1600  -0.2675 -0.1471 93  LEU A CB  
647  C CG  . LEU A 87  ? 0.5391 0.5650 0.5832 0.1613  -0.2868 -0.1378 93  LEU A CG  
648  C CD1 . LEU A 87  ? 0.5465 0.5397 0.5791 0.1791  -0.3104 -0.1407 93  LEU A CD1 
649  C CD2 . LEU A 87  ? 0.4938 0.5476 0.5526 0.1544  -0.2881 -0.1444 93  LEU A CD2 
650  N N   . LEU A 88  ? 0.4087 0.5773 0.5678 0.1351  -0.2121 -0.1665 94  LEU A N   
651  C CA  . LEU A 88  ? 0.3796 0.5737 0.5618 0.1313  -0.1933 -0.1733 94  LEU A CA  
652  C C   . LEU A 88  ? 0.4001 0.6064 0.6066 0.1459  -0.2002 -0.1903 94  LEU A C   
653  O O   . LEU A 88  ? 0.4104 0.6233 0.6292 0.1552  -0.2146 -0.2016 94  LEU A O   
654  C CB  . LEU A 88  ? 0.3782 0.6118 0.5816 0.1127  -0.1717 -0.1781 94  LEU A CB  
655  C CG  . LEU A 88  ? 0.3584 0.5893 0.5469 0.0949  -0.1552 -0.1647 94  LEU A CG  
656  C CD1 . LEU A 88  ? 0.3818 0.5729 0.5329 0.0957  -0.1674 -0.1489 94  LEU A CD1 
657  C CD2 . LEU A 88  ? 0.3444 0.6066 0.5488 0.0771  -0.1407 -0.1695 94  LEU A CD2 
658  N N   . GLN A 89  ? 0.3950 0.6046 0.6084 0.1476  -0.1901 -0.1930 95  GLN A N   
659  C CA  . GLN A 89  ? 0.4116 0.6406 0.6516 0.1576  -0.1922 -0.2121 95  GLN A CA  
660  C C   . GLN A 89  ? 0.3778 0.6525 0.6492 0.1484  -0.1805 -0.2282 95  GLN A C   
661  O O   . GLN A 89  ? 0.3768 0.6715 0.6512 0.1307  -0.1617 -0.2241 95  GLN A O   
662  C CB  . GLN A 89  ? 0.3821 0.6091 0.6227 0.1572  -0.1803 -0.2118 95  GLN A CB  
663  C CG  . GLN A 89  ? 0.3979 0.6455 0.6647 0.1657  -0.1813 -0.2325 95  GLN A CG  
664  C CD  . GLN A 89  ? 0.4801 0.7343 0.7495 0.1597  -0.1646 -0.2327 95  GLN A CD  
665  O OE1 . GLN A 89  ? 0.4557 0.6824 0.7107 0.1681  -0.1712 -0.2267 95  GLN A OE1 
666  N NE2 . GLN A 89  ? 0.4785 0.7673 0.7638 0.1439  -0.1428 -0.2389 95  GLN A NE2 
667  N N   . GLY A 90  ? 0.3824 0.6719 0.6760 0.1599  -0.1922 -0.2468 96  GLY A N   
668  C CA  . GLY A 90  ? 0.3419 0.6720 0.6640 0.1528  -0.1847 -0.2634 96  GLY A CA  
669  C C   . GLY A 90  ? 0.3881 0.7179 0.7115 0.1566  -0.2004 -0.2647 96  GLY A C   
670  O O   . GLY A 90  ? 0.4209 0.7823 0.7708 0.1558  -0.2002 -0.2821 96  GLY A O   
671  N N   . GLY A 91  ? 0.3964 0.6909 0.6905 0.1598  -0.2140 -0.2472 97  GLY A N   
672  C CA  . GLY A 91  ? 0.3936 0.6814 0.6833 0.1642  -0.2317 -0.2469 97  GLY A CA  
673  C C   . GLY A 91  ? 0.4117 0.7024 0.6882 0.1468  -0.2230 -0.2342 97  GLY A C   
674  O O   . GLY A 91  ? 0.4456 0.7278 0.7141 0.1491  -0.2380 -0.2322 97  GLY A O   
675  N N   . GLU A 92  ? 0.3866 0.6877 0.6595 0.1293  -0.2002 -0.2259 98  GLU A N   
676  C CA  . GLU A 92  ? 0.3706 0.6733 0.6309 0.1121  -0.1923 -0.2149 98  GLU A CA  
677  C C   . GLU A 92  ? 0.4231 0.6824 0.6443 0.1144  -0.2051 -0.1958 98  GLU A C   
678  O O   . GLU A 92  ? 0.4175 0.6460 0.6188 0.1241  -0.2121 -0.1875 98  GLU A O   
679  C CB  . GLU A 92  ? 0.3248 0.6478 0.5910 0.0925  -0.1651 -0.2118 98  GLU A CB  
680  N N   . ALA A 93  ? 0.3992 0.6543 0.6070 0.1043  -0.2081 -0.1894 99  ALA A N   
681  C CA  . ALA A 93  ? 0.4389 0.6527 0.6059 0.1039  -0.2197 -0.1727 99  ALA A CA  
682  C C   . ALA A 93  ? 0.4451 0.6609 0.5986 0.0831  -0.2052 -0.1635 99  ALA A C   
683  O O   . ALA A 93  ? 0.4177 0.6620 0.5899 0.0709  -0.1960 -0.1703 99  ALA A O   
684  C CB  . ALA A 93  ? 0.4101 0.6066 0.5659 0.1150  -0.2441 -0.1745 99  ALA A CB  
685  N N   . LEU A 94  ? 0.4090 0.5920 0.5285 0.0789  -0.2035 -0.1487 100 LEU A N   
686  C CA  . LEU A 94  ? 0.4028 0.5812 0.5050 0.0601  -0.1906 -0.1404 100 LEU A CA  
687  C C   . LEU A 94  ? 0.4261 0.5653 0.4857 0.0587  -0.2039 -0.1298 100 LEU A C   
688  O O   . LEU A 94  ? 0.4116 0.5125 0.4384 0.0657  -0.2116 -0.1195 100 LEU A O   
689  C CB  . LEU A 94  ? 0.3550 0.5297 0.4531 0.0537  -0.1739 -0.1340 100 LEU A CB  
690  C CG  . LEU A 94  ? 0.3461 0.5577 0.4818 0.0520  -0.1581 -0.1434 100 LEU A CG  
691  C CD1 . LEU A 94  ? 0.3719 0.5772 0.5010 0.0461  -0.1430 -0.1362 100 LEU A CD1 
692  C CD2 . LEU A 94  ? 0.3159 0.5599 0.4742 0.0372  -0.1459 -0.1512 100 LEU A CD2 
693  N N   . PRO A 95  ? 0.4450 0.5895 0.5008 0.0489  -0.2060 -0.1317 101 PRO A N   
694  C CA  . PRO A 95  ? 0.4467 0.5529 0.4586 0.0457  -0.2164 -0.1220 101 PRO A CA  
695  C C   . PRO A 95  ? 0.4381 0.5221 0.4205 0.0313  -0.2018 -0.1124 101 PRO A C   
696  O O   . PRO A 95  ? 0.4203 0.5246 0.4201 0.0200  -0.1841 -0.1151 101 PRO A O   
697  C CB  . PRO A 95  ? 0.4684 0.5944 0.4927 0.0396  -0.2220 -0.1299 101 PRO A CB  
698  C CG  . PRO A 95  ? 0.4405 0.6110 0.5072 0.0303  -0.2053 -0.1401 101 PRO A CG  
699  C CD  . PRO A 95  ? 0.4156 0.6000 0.5050 0.0390  -0.1977 -0.1428 101 PRO A CD  
700  N N   . PHE A 96  ? 0.4732 0.5127 0.4089 0.0312  -0.2083 -0.1013 102 PHE A N   
701  C CA  . PHE A 96  ? 0.4506 0.4636 0.3543 0.0182  -0.1938 -0.0929 102 PHE A CA  
702  C C   . PHE A 96  ? 0.4884 0.4649 0.3468 0.0112  -0.1983 -0.0854 102 PHE A C   
703  O O   . PHE A 96  ? 0.5384 0.4982 0.3804 0.0194  -0.2147 -0.0826 102 PHE A O   
704  C CB  . PHE A 96  ? 0.4471 0.4381 0.3386 0.0226  -0.1838 -0.0825 102 PHE A CB  
705  C CG  . PHE A 96  ? 0.4794 0.4368 0.3426 0.0367  -0.2040 -0.0766 102 PHE A CG  
706  C CD1 . PHE A 96  ? 0.5070 0.4182 0.3197 0.0314  -0.2055 -0.0648 102 PHE A CD1 
707  C CD2 . PHE A 96  ? 0.5184 0.4896 0.4080 0.0533  -0.2148 -0.0811 102 PHE A CD2 
708  C CE1 . PHE A 96  ? 0.5499 0.4277 0.3378 0.0418  -0.2189 -0.0568 102 PHE A CE1 
709  C CE2 . PHE A 96  ? 0.5083 0.4452 0.3741 0.0654  -0.2295 -0.0740 102 PHE A CE2 
710  C CZ  . PHE A 96  ? 0.5550 0.4444 0.3694 0.0593  -0.2320 -0.0614 102 PHE A CZ  
711  N N   . SER A 97  ? 0.4481 0.4129 0.2889 -0.0046 -0.1806 -0.0819 103 SER A N   
712  C CA  . SER A 97  ? 0.5167 0.4417 0.3084 -0.0129 -0.1805 -0.0745 103 SER A CA  
713  C C   . SER A 97  ? 0.5261 0.4164 0.2869 -0.0153 -0.1675 -0.0624 103 SER A C   
714  O O   . SER A 97  ? 0.5272 0.3815 0.2465 -0.0177 -0.1705 -0.0545 103 SER A O   
715  C CB  . SER A 97  ? 0.4971 0.4288 0.2882 -0.0292 -0.1665 -0.0787 103 SER A CB  
716  O OG  . SER A 97  ? 0.4620 0.4039 0.2718 -0.0375 -0.1408 -0.0765 103 SER A OG  
717  N N   . HIS A 98  ? 0.4546 0.3587 0.2402 -0.0156 -0.1493 -0.0601 104 HIS A N   
718  C CA  . HIS A 98  ? 0.5085 0.3861 0.2734 -0.0175 -0.1355 -0.0501 104 HIS A CA  
719  C C   . HIS A 98  ? 0.4570 0.3532 0.2536 -0.0065 -0.1342 -0.0499 104 HIS A C   
720  O O   . HIS A 98  ? 0.4235 0.3570 0.2614 -0.0040 -0.1314 -0.0574 104 HIS A O   
721  C CB  . HIS A 98  ? 0.5028 0.3760 0.2628 -0.0329 -0.1096 -0.0482 104 HIS A CB  
722  C CG  . HIS A 98  ? 0.5004 0.3563 0.2303 -0.0443 -0.1091 -0.0501 104 HIS A CG  
723  N ND1 . HIS A 98  ? 0.5003 0.3743 0.2415 -0.0469 -0.1175 -0.0585 104 HIS A ND1 
724  C CD2 . HIS A 98  ? 0.5595 0.3820 0.2474 -0.0544 -0.1010 -0.0458 104 HIS A CD2 
725  C CE1 . HIS A 98  ? 0.5468 0.3985 0.2542 -0.0574 -0.1151 -0.0591 104 HIS A CE1 
726  N NE2 . HIS A 98  ? 0.5914 0.4126 0.2666 -0.0622 -0.1043 -0.0516 104 HIS A NE2 
727  N N   . LEU A 99  ? 0.4739 0.3429 0.2490 -0.0010 -0.1363 -0.0419 105 LEU A N   
728  C CA  . LEU A 99  ? 0.4442 0.3254 0.2443 0.0100  -0.1361 -0.0416 105 LEU A CA  
729  C C   . LEU A 99  ? 0.4875 0.3509 0.2761 0.0029  -0.1153 -0.0332 105 LEU A C   
730  O O   . LEU A 99  ? 0.5175 0.3443 0.2661 -0.0038 -0.1119 -0.0254 105 LEU A O   
731  C CB  . LEU A 99  ? 0.4894 0.3546 0.2780 0.0261  -0.1624 -0.0413 105 LEU A CB  
732  C CG  . LEU A 99  ? 0.4994 0.3697 0.3074 0.0386  -0.1643 -0.0412 105 LEU A CG  
733  C CD1 . LEU A 99  ? 0.4067 0.3273 0.2687 0.0449  -0.1620 -0.0532 105 LEU A CD1 
734  C CD2 . LEU A 99  ? 0.5211 0.3602 0.3034 0.0526  -0.1916 -0.0385 105 LEU A CD2 
735  N N   . ILE A 100 ? 0.4315 0.3208 0.2543 0.0035  -0.1015 -0.0353 106 ILE A N   
736  C CA  . ILE A 100 ? 0.4069 0.2845 0.2256 -0.0013 -0.0835 -0.0288 106 ILE A CA  
737  C C   . ILE A 100 ? 0.4349 0.3192 0.2710 0.0118  -0.0903 -0.0292 106 ILE A C   
738  O O   . ILE A 100 ? 0.3697 0.2881 0.2425 0.0180  -0.0916 -0.0365 106 ILE A O   
739  C CB  . ILE A 100 ? 0.3983 0.2976 0.2405 -0.0119 -0.0621 -0.0308 106 ILE A CB  
740  C CG1 . ILE A 100 ? 0.3820 0.2733 0.2078 -0.0243 -0.0551 -0.0318 106 ILE A CG1 
741  C CG2 . ILE A 100 ? 0.3975 0.2882 0.2402 -0.0148 -0.0461 -0.0255 106 ILE A CG2 
742  C CD1 . ILE A 100 ? 0.3466 0.2557 0.1954 -0.0336 -0.0360 -0.0340 106 ILE A CD1 
743  N N   . LEU A 101 ? 0.4284 0.2799 0.2373 0.0149  -0.0939 -0.0220 107 LEU A N   
744  C CA  . LEU A 101 ? 0.4476 0.3009 0.2701 0.0272  -0.1003 -0.0224 107 LEU A CA  
745  C C   . LEU A 101 ? 0.3932 0.2477 0.2238 0.0204  -0.0791 -0.0186 107 LEU A C   
746  O O   . LEU A 101 ? 0.4119 0.2405 0.2162 0.0098  -0.0673 -0.0116 107 LEU A O   
747  C CB  . LEU A 101 ? 0.4754 0.2897 0.2635 0.0359  -0.1206 -0.0172 107 LEU A CB  
748  C CG  . LEU A 101 ? 0.5132 0.3275 0.2969 0.0462  -0.1464 -0.0222 107 LEU A CG  
749  C CD1 . LEU A 101 ? 0.6276 0.3921 0.3635 0.0501  -0.1659 -0.0140 107 LEU A CD1 
750  C CD2 . LEU A 101 ? 0.4833 0.3350 0.3113 0.0624  -0.1590 -0.0342 107 LEU A CD2 
751  N N   . ALA A 102 ? 0.3896 0.2757 0.2569 0.0256  -0.0740 -0.0241 108 ALA A N   
752  C CA  . ALA A 102 ? 0.3577 0.2506 0.2375 0.0193  -0.0551 -0.0218 108 ALA A CA  
753  C C   . ALA A 102 ? 0.3672 0.2758 0.2710 0.0308  -0.0592 -0.0262 108 ALA A C   
754  O O   . ALA A 102 ? 0.3104 0.2469 0.2422 0.0290  -0.0488 -0.0302 108 ALA A O   
755  C CB  . ALA A 102 ? 0.3229 0.2412 0.2227 0.0088  -0.0401 -0.0244 108 ALA A CB  
756  N N   . THR A 103 ? 0.3933 0.2818 0.2842 0.0425  -0.0753 -0.0258 109 THR A N   
757  C CA  . THR A 103 ? 0.3724 0.2768 0.2875 0.0564  -0.0838 -0.0332 109 THR A CA  
758  C C   . THR A 103 ? 0.3802 0.2770 0.2972 0.0555  -0.0727 -0.0301 109 THR A C   
759  O O   . THR A 103 ? 0.3765 0.2884 0.3151 0.0661  -0.0774 -0.0373 109 THR A O   
760  C CB  . THR A 103 ? 0.4186 0.3022 0.3197 0.0711  -0.1086 -0.0350 109 THR A CB  
761  O OG1 . THR A 103 ? 0.4812 0.3164 0.3386 0.0667  -0.1116 -0.0235 109 THR A OG1 
762  C CG2 . THR A 103 ? 0.4361 0.3347 0.3430 0.0741  -0.1219 -0.0410 109 THR A CG2 
763  N N   . GLY A 104 ? 0.3978 0.2732 0.2944 0.0432  -0.0583 -0.0212 110 GLY A N   
764  C CA  . GLY A 104 ? 0.4048 0.2768 0.3063 0.0408  -0.0466 -0.0192 110 GLY A CA  
765  C C   . GLY A 104 ? 0.4296 0.2776 0.3201 0.0514  -0.0583 -0.0187 110 GLY A C   
766  O O   . GLY A 104 ? 0.4398 0.2577 0.3049 0.0573  -0.0741 -0.0155 110 GLY A O   
767  N N   . SER A 105 ? 0.4150 0.2745 0.3237 0.0538  -0.0511 -0.0218 111 SER A N   
768  C CA  . SER A 105 ? 0.4389 0.2773 0.3408 0.0631  -0.0596 -0.0224 111 SER A CA  
769  C C   . SER A 105 ? 0.4304 0.3011 0.3673 0.0753  -0.0633 -0.0343 111 SER A C   
770  O O   . SER A 105 ? 0.4035 0.3117 0.3678 0.0720  -0.0532 -0.0402 111 SER A O   
771  C CB  . SER A 105 ? 0.4578 0.2753 0.3450 0.0520  -0.0453 -0.0154 111 SER A CB  
772  O OG  . SER A 105 ? 0.5615 0.3460 0.4140 0.0404  -0.0417 -0.0060 111 SER A OG  
773  N N   . THR A 106 ? 0.4174 0.2711 0.3513 0.0887  -0.0776 -0.0381 112 THR A N   
774  C CA  . THR A 106 ? 0.4076 0.2873 0.3724 0.1014  -0.0817 -0.0511 112 THR A CA  
775  C C   . THR A 106 ? 0.4026 0.2619 0.3605 0.1021  -0.0779 -0.0497 112 THR A C   
776  O O   . THR A 106 ? 0.4069 0.2246 0.3335 0.0980  -0.0803 -0.0398 112 THR A O   
777  C CB  . THR A 106 ? 0.4644 0.3450 0.4375 0.1200  -0.1053 -0.0607 112 THR A CB  
778  O OG1 . THR A 106 ? 0.5774 0.4917 0.5863 0.1315  -0.1070 -0.0766 112 THR A OG1 
779  C CG2 . THR A 106 ? 0.4675 0.2967 0.4076 0.1279  -0.1230 -0.0539 112 THR A CG2 
780  N N   . GLY A 107 ? 0.3449 0.2332 0.3309 0.1060  -0.0714 -0.0600 113 GLY A N   
781  C CA  . GLY A 107 ? 0.3502 0.2220 0.3320 0.1070  -0.0681 -0.0603 113 GLY A CA  
782  C C   . GLY A 107 ? 0.3512 0.2615 0.3660 0.1112  -0.0612 -0.0738 113 GLY A C   
783  O O   . GLY A 107 ? 0.3125 0.2616 0.3528 0.1133  -0.0592 -0.0834 113 GLY A O   
784  N N   . PRO A 108 ? 0.3280 0.2155 0.3170 0.1227  -0.0218 0.0417  114 PRO A N   
785  C CA  . PRO A 108 ? 0.3229 0.2363 0.3439 0.1337  -0.0167 0.0312  114 PRO A CA  
786  C C   . PRO A 108 ? 0.2713 0.2122 0.3059 0.1226  -0.0034 0.0235  114 PRO A C   
787  O O   . PRO A 108 ? 0.2539 0.1849 0.2760 0.1077  0.0063  0.0241  114 PRO A O   
788  C CB  . PRO A 108 ? 0.3079 0.1940 0.3246 0.1356  -0.0114 0.0291  114 PRO A CB  
789  C CG  . PRO A 108 ? 0.3734 0.2201 0.3559 0.1245  -0.0072 0.0375  114 PRO A CG  
790  C CD  . PRO A 108 ? 0.3482 0.1927 0.3120 0.1193  -0.0184 0.0468  114 PRO A CD  
791  N N   . PHE A 109 ? 0.2435 0.2187 0.3046 0.1298  -0.0033 0.0160  115 PHE A N   
792  C CA  . PHE A 109 ? 0.2558 0.2525 0.3298 0.1219  0.0090  0.0083  115 PHE A CA  
793  C C   . PHE A 109 ? 0.2420 0.2188 0.3111 0.1183  0.0177  0.0040  115 PHE A C   
794  O O   . PHE A 109 ? 0.2666 0.2273 0.3347 0.1228  0.0138  0.0023  115 PHE A O   
795  C CB  . PHE A 109 ? 0.2033 0.2369 0.3041 0.1295  0.0079  0.0002  115 PHE A CB  
796  C CG  . PHE A 109 ? 0.2081 0.2639 0.3174 0.1187  0.0191  -0.0060 115 PHE A CG  
797  C CD1 . PHE A 109 ? 0.1862 0.2588 0.2953 0.1069  0.0204  -0.0036 115 PHE A CD1 
798  C CD2 . PHE A 109 ? 0.2384 0.2937 0.3521 0.1144  0.0265  -0.0141 115 PHE A CD2 
799  C CE1 . PHE A 109 ? 0.1860 0.2747 0.3001 0.0963  0.0295  -0.0076 115 PHE A CE1 
800  C CE2 . PHE A 109 ? 0.2188 0.2907 0.3351 0.1045  0.0352  -0.0182 115 PHE A CE2 
801  C CZ  . PHE A 109 ? 0.1888 0.2786 0.3063 0.0976  0.0372  -0.0141 115 PHE A CZ  
802  N N   . PRO A 110 ? 0.2550 0.2339 0.3226 0.1064  0.0272  0.0015  116 PRO A N   
803  C CA  . PRO A 110 ? 0.2281 0.2243 0.2990 0.0957  0.0319  0.0025  116 PRO A CA  
804  C C   . PRO A 110 ? 0.2324 0.2137 0.2887 0.0843  0.0321  0.0083  116 PRO A C   
805  O O   . PRO A 110 ? 0.1926 0.1880 0.2518 0.0748  0.0335  0.0085  116 PRO A O   
806  C CB  . PRO A 110 ? 0.2090 0.2057 0.2830 0.0885  0.0392  -0.0029 116 PRO A CB  
807  C CG  . PRO A 110 ? 0.2404 0.2106 0.3034 0.0876  0.0379  -0.0044 116 PRO A CG  
808  C CD  . PRO A 110 ? 0.2337 0.1986 0.2970 0.0997  0.0309  -0.0041 116 PRO A CD  
809  N N   . GLY A 111 ? 0.2823 0.2344 0.3218 0.0835  0.0318  0.0123  117 GLY A N   
810  C CA  . GLY A 111 ? 0.2632 0.2003 0.2878 0.0702  0.0358  0.0152  117 GLY A CA  
811  C C   . GLY A 111 ? 0.3010 0.2487 0.3186 0.0656  0.0295  0.0189  117 GLY A C   
812  O O   . GLY A 111 ? 0.2721 0.2156 0.2822 0.0527  0.0347  0.0184  117 GLY A O   
813  N N   . LYS A 112 ? 0.2351 0.1967 0.2565 0.0760  0.0181  0.0216  118 LYS A N   
814  C CA  . LYS A 112 ? 0.2898 0.2661 0.3077 0.0725  0.0096  0.0245  118 LYS A CA  
815  C C   . LYS A 112 ? 0.2751 0.2865 0.3182 0.0818  0.0036  0.0209  118 LYS A C   
816  O O   . LYS A 112 ? 0.2638 0.2814 0.3208 0.0949  0.0021  0.0180  118 LYS A O   
817  C CB  . LYS A 112 ? 0.3040 0.2585 0.2979 0.0751  -0.0021 0.0328  118 LYS A CB  
818  C CG  . LYS A 112 ? 0.3424 0.2611 0.3068 0.0634  0.0049  0.0362  118 LYS A CG  
819  C CD  . LYS A 112 ? 0.4100 0.3315 0.3691 0.0455  0.0159  0.0319  118 LYS A CD  
820  C CE  . LYS A 112 ? 0.4281 0.3163 0.3571 0.0320  0.0240  0.0335  118 LYS A CE  
821  N NZ  . LYS A 112 ? 0.4061 0.2962 0.3367 0.0157  0.0384  0.0256  118 LYS A NZ  
822  N N   . PHE A 113 ? 0.2313 0.2658 0.2807 0.0742  0.0014  0.0197  119 PHE A N   
823  C CA  . PHE A 113 ? 0.2388 0.3096 0.3131 0.0800  -0.0029 0.0152  119 PHE A CA  
824  C C   . PHE A 113 ? 0.2690 0.3545 0.3422 0.0773  -0.0154 0.0178  119 PHE A C   
825  O O   . PHE A 113 ? 0.3030 0.3974 0.3729 0.0635  -0.0129 0.0169  119 PHE A O   
826  C CB  . PHE A 113 ? 0.1936 0.2826 0.2809 0.0707  0.0086  0.0096  119 PHE A CB  
827  C CG  . PHE A 113 ? 0.2059 0.3317 0.3173 0.0740  0.0074  0.0039  119 PHE A CG  
828  C CD1 . PHE A 113 ? 0.2186 0.3565 0.3463 0.0856  0.0103  -0.0019 119 PHE A CD1 
829  C CD2 . PHE A 113 ? 0.1894 0.3386 0.3080 0.0646  0.0044  0.0028  119 PHE A CD2 
830  C CE1 . PHE A 113 ? 0.1932 0.3673 0.3447 0.0876  0.0115  -0.0093 119 PHE A CE1 
831  C CE2 . PHE A 113 ? 0.2047 0.3897 0.3473 0.0663  0.0047  -0.0036 119 PHE A CE2 
832  C CZ  . PHE A 113 ? 0.1953 0.3938 0.3551 0.0777  0.0089  -0.0100 119 PHE A CZ  
833  N N   . ASN A 114 ? 0.2706 0.3585 0.3474 0.0905  -0.0298 0.0207  120 ASN A N   
834  C CA  . ASN A 114 ? 0.3233 0.4234 0.3978 0.0886  -0.0453 0.0239  120 ASN A CA  
835  C C   . ASN A 114 ? 0.2875 0.4242 0.3967 0.1028  -0.0554 0.0186  120 ASN A C   
836  O O   . ASN A 114 ? 0.3317 0.4665 0.4460 0.1173  -0.0718 0.0220  120 ASN A O   
837  C CB  . ASN A 114 ? 0.3777 0.4425 0.4196 0.0894  -0.0570 0.0340  120 ASN A CB  
838  C CG  . ASN A 114 ? 0.4024 0.4375 0.4125 0.0718  -0.0451 0.0365  120 ASN A CG  
839  O OD1 . ASN A 114 ? 0.3974 0.4419 0.4043 0.0567  -0.0387 0.0331  120 ASN A OD1 
840  N ND2 . ASN A 114 ? 0.4015 0.4013 0.3905 0.0731  -0.0406 0.0410  120 ASN A ND2 
841  N N   . GLU A 115 ? 0.2965 0.4660 0.4303 0.0980  -0.0453 0.0098  121 GLU A N   
842  C CA  . GLU A 115 ? 0.2934 0.5033 0.4644 0.1083  -0.0503 0.0015  121 GLU A CA  
843  C C   . GLU A 115 ? 0.2781 0.5198 0.4603 0.0936  -0.0504 -0.0024 121 GLU A C   
844  O O   . GLU A 115 ? 0.2736 0.5083 0.4401 0.0760  -0.0399 -0.0015 121 GLU A O   
845  C CB  . GLU A 115 ? 0.2697 0.4915 0.4607 0.1147  -0.0353 -0.0076 121 GLU A CB  
846  C CG  . GLU A 115 ? 0.3499 0.5447 0.5361 0.1312  -0.0364 -0.0062 121 GLU A CG  
847  C CD  . GLU A 115 ? 0.4968 0.6954 0.6939 0.1311  -0.0191 -0.0151 121 GLU A CD  
848  O OE1 . GLU A 115 ? 0.5241 0.7496 0.7427 0.1264  -0.0121 -0.0233 121 GLU A OE1 
849  O OE2 . GLU A 115 ? 0.5253 0.6950 0.7050 0.1322  -0.0118 -0.0131 121 GLU A OE2 
850  N N   . VAL A 116 ? 0.2430 0.5187 0.4536 0.1010  -0.0632 -0.0072 122 VAL A N   
851  C CA  . VAL A 116 ? 0.2619 0.5743 0.4907 0.0869  -0.0604 -0.0139 122 VAL A CA  
852  C C   . VAL A 116 ? 0.3103 0.6464 0.5609 0.0834  -0.0407 -0.0242 122 VAL A C   
853  O O   . VAL A 116 ? 0.2878 0.6247 0.5546 0.0936  -0.0364 -0.0291 122 VAL A O   
854  C CB  . VAL A 116 ? 0.2175 0.5624 0.4736 0.0950  -0.0809 -0.0170 122 VAL A CB  
855  C CG1 . VAL A 116 ? 0.1773 0.5569 0.4504 0.0770  -0.0760 -0.0243 122 VAL A CG1 
856  C CG2 . VAL A 116 ? 0.2359 0.5524 0.4639 0.0982  -0.1026 -0.0051 122 VAL A CG2 
857  N N   . SER A 117 ? 0.3047 0.6402 0.5437 0.0636  -0.0266 -0.0246 123 SER A N   
858  C CA  . SER A 117 ? 0.3104 0.6576 0.5594 0.0552  -0.0082 -0.0318 123 SER A CA  
859  C C   . SER A 117 ? 0.3106 0.6569 0.5454 0.0333  0.0019  -0.0299 123 SER A C   
860  O O   . SER A 117 ? 0.3378 0.6634 0.5512 0.0247  -0.0033 -0.0229 123 SER A O   
861  C CB  . SER A 117 ? 0.3115 0.6364 0.5527 0.0646  0.0019  -0.0322 123 SER A CB  
862  O OG  . SER A 117 ? 0.3235 0.6252 0.5403 0.0571  0.0099  -0.0264 123 SER A OG  
863  N N   . SER A 118 ? 0.2310 0.5792 0.4662 0.0224  0.0165  -0.0339 124 SER A N   
864  C CA  . SER A 118 ? 0.1980 0.5398 0.4187 0.0014  0.0256  -0.0313 124 SER A CA  
865  C C   . SER A 118 ? 0.1535 0.4662 0.3520 -0.0009 0.0329  -0.0250 124 SER A C   
866  O O   . SER A 118 ? 0.1490 0.4484 0.3436 0.0125  0.0340  -0.0241 124 SER A O   
867  C CB  . SER A 118 ? 0.1574 0.5123 0.3852 -0.0095 0.0364  -0.0372 124 SER A CB  
868  O OG  . SER A 118 ? 0.1323 0.4810 0.3586 -0.0025 0.0455  -0.0400 124 SER A OG  
869  N N   . GLN A 119 ? 0.1229 0.4234 0.3073 -0.0185 0.0375  -0.0207 125 GLN A N   
870  C CA  . GLN A 119 ? 0.1390 0.4028 0.3008 -0.0217 0.0423  -0.0138 125 GLN A CA  
871  C C   . GLN A 119 ? 0.1335 0.3967 0.2937 -0.0191 0.0517  -0.0153 125 GLN A C   
872  O O   . GLN A 119 ? 0.1111 0.3476 0.2583 -0.0120 0.0521  -0.0114 125 GLN A O   
873  C CB  . GLN A 119 ? 0.1856 0.4362 0.3362 -0.0411 0.0449  -0.0099 125 GLN A CB  
874  C CG  . GLN A 119 ? 0.1816 0.3934 0.3133 -0.0427 0.0467  -0.0031 125 GLN A CG  
875  C CD  . GLN A 119 ? 0.2414 0.4377 0.3650 -0.0600 0.0479  0.0002  125 GLN A CD  
876  O OE1 . GLN A 119 ? 0.3865 0.5843 0.5072 -0.0731 0.0532  0.0021  125 GLN A OE1 
877  N NE2 . GLN A 119 ? 0.2370 0.4170 0.3555 -0.0611 0.0434  0.0006  125 GLN A NE2 
878  N N   . GLN A 120 ? 0.1263 0.4048 0.2920 -0.0248 0.0576  -0.0204 126 GLN A N   
879  C CA  . GLN A 120 ? 0.1495 0.4213 0.3066 -0.0246 0.0663  -0.0218 126 GLN A CA  
880  C C   . GLN A 120 ? 0.1311 0.4066 0.2978 -0.0051 0.0655  -0.0273 126 GLN A C   
881  O O   . GLN A 120 ? 0.1256 0.3869 0.2818 -0.0011 0.0699  -0.0269 126 GLN A O   
882  C CB  . GLN A 120 ? 0.1426 0.4274 0.2988 -0.0388 0.0744  -0.0256 126 GLN A CB  
883  C CG  . GLN A 120 ? 0.2072 0.4772 0.3461 -0.0591 0.0764  -0.0184 126 GLN A CG  
884  C CD  . GLN A 120 ? 0.2922 0.5321 0.4138 -0.0616 0.0737  -0.0088 126 GLN A CD  
885  O OE1 . GLN A 120 ? 0.2228 0.4512 0.3335 -0.0591 0.0769  -0.0069 126 GLN A OE1 
886  N NE2 . GLN A 120 ? 0.2169 0.4448 0.3373 -0.0670 0.0678  -0.0038 126 GLN A NE2 
887  N N   . ALA A 121 ? 0.1247 0.4177 0.3113 0.0069  0.0590  -0.0324 127 ALA A N   
888  C CA  . ALA A 121 ? 0.1262 0.4165 0.3214 0.0262  0.0562  -0.0363 127 ALA A CA  
889  C C   . ALA A 121 ? 0.1183 0.3834 0.3013 0.0363  0.0508  -0.0301 127 ALA A C   
890  O O   . ALA A 121 ? 0.1213 0.3712 0.2993 0.0460  0.0532  -0.0315 127 ALA A O   
891  C CB  . ALA A 121 ? 0.1311 0.4434 0.3510 0.0371  0.0476  -0.0415 127 ALA A CB  
892  N N   . ALA A 122 ? 0.1190 0.3786 0.2963 0.0330  0.0443  -0.0236 128 ALA A N   
893  C CA  . ALA A 122 ? 0.1231 0.3454 0.2815 0.0395  0.0394  -0.0162 128 ALA A CA  
894  C C   . ALA A 122 ? 0.1108 0.3098 0.2531 0.0336  0.0471  -0.0135 128 ALA A C   
895  O O   . ALA A 122 ? 0.1128 0.2910 0.2480 0.0431  0.0469  -0.0128 128 ALA A O   
896  C CB  . ALA A 122 ? 0.1137 0.3226 0.2617 0.0324  0.0320  -0.0098 128 ALA A CB  
897  N N   . ILE A 123 ? 0.1100 0.3100 0.2458 0.0172  0.0524  -0.0114 129 ILE A N   
898  C CA  . ILE A 123 ? 0.1229 0.3019 0.2437 0.0107  0.0571  -0.0081 129 ILE A CA  
899  C C   . ILE A 123 ? 0.1359 0.3214 0.2575 0.0178  0.0630  -0.0143 129 ILE A C   
900  O O   . ILE A 123 ? 0.1191 0.2826 0.2303 0.0221  0.0628  -0.0129 129 ILE A O   
901  C CB  . ILE A 123 ? 0.1361 0.3171 0.2502 -0.0084 0.0603  -0.0044 129 ILE A CB  
902  C CG1 . ILE A 123 ? 0.1396 0.3047 0.2503 -0.0154 0.0549  0.0013  129 ILE A CG1 
903  C CG2 . ILE A 123 ? 0.1535 0.3169 0.2518 -0.0154 0.0634  -0.0010 129 ILE A CG2 
904  C CD1 . ILE A 123 ? 0.1378 0.3077 0.2452 -0.0339 0.0573  0.0040  129 ILE A CD1 
905  N N   . GLN A 124 ? 0.1191 0.3358 0.2547 0.0187  0.0688  -0.0228 130 GLN A N   
906  C CA  . GLN A 124 ? 0.1327 0.3532 0.2684 0.0244  0.0756  -0.0307 130 GLN A CA  
907  C C   . GLN A 124 ? 0.1478 0.3541 0.2881 0.0436  0.0708  -0.0332 130 GLN A C   
908  O O   . GLN A 124 ? 0.1431 0.3401 0.2769 0.0478  0.0754  -0.0377 130 GLN A O   
909  C CB  . GLN A 124 ? 0.1496 0.3939 0.2971 0.0206  0.0806  -0.0380 130 GLN A CB  
910  C CG  . GLN A 124 ? 0.2266 0.4729 0.3701 0.0223  0.0896  -0.0464 130 GLN A CG  
911  C CD  . GLN A 124 ? 0.2622 0.4996 0.3813 0.0065  0.0972  -0.0443 130 GLN A CD  
912  O OE1 . GLN A 124 ? 0.3123 0.5531 0.4213 -0.0109 0.0996  -0.0395 130 GLN A OE1 
913  N NE2 . GLN A 124 ? 0.2466 0.4702 0.3541 0.0114  0.0999  -0.0473 130 GLN A NE2 
914  N N   . ALA A 125 ? 0.1279 0.3312 0.2774 0.0543  0.0616  -0.0304 131 ALA A N   
915  C CA  . ALA A 125 ? 0.1698 0.3534 0.3197 0.0703  0.0563  -0.0309 131 ALA A CA  
916  C C   . ALA A 125 ? 0.1576 0.3138 0.2904 0.0707  0.0572  -0.0267 131 ALA A C   
917  O O   . ALA A 125 ? 0.1471 0.2855 0.2760 0.0784  0.0576  -0.0296 131 ALA A O   
918  C CB  . ALA A 125 ? 0.1545 0.3390 0.3129 0.0800  0.0449  -0.0272 131 ALA A CB  
919  N N   . TYR A 126 ? 0.1216 0.2637 0.2418 0.0582  0.0559  -0.0186 132 TYR A N   
920  C CA  . TYR A 126 ? 0.1260 0.2382 0.2318 0.0556  0.0553  -0.0143 132 TYR A CA  
921  C C   . TYR A 126 ? 0.1808 0.2925 0.2782 0.0483  0.0609  -0.0172 132 TYR A C   
922  O O   . TYR A 126 ? 0.1687 0.2623 0.2589 0.0519  0.0609  -0.0185 132 TYR A O   
923  C CB  . TYR A 126 ? 0.1281 0.2259 0.2280 0.0463  0.0515  -0.0065 132 TYR A CB  
924  C CG  . TYR A 126 ? 0.1186 0.2051 0.2183 0.0533  0.0465  -0.0038 132 TYR A CG  
925  C CD1 . TYR A 126 ? 0.1446 0.2052 0.2372 0.0584  0.0456  -0.0025 132 TYR A CD1 
926  C CD2 . TYR A 126 ? 0.1190 0.2206 0.2240 0.0537  0.0423  -0.0029 132 TYR A CD2 
927  C CE1 . TYR A 126 ? 0.1444 0.1920 0.2316 0.0628  0.0417  0.0005  132 TYR A CE1 
928  C CE2 . TYR A 126 ? 0.1264 0.2151 0.2258 0.0588  0.0363  0.0004  132 TYR A CE2 
929  C CZ  . TYR A 126 ? 0.1530 0.2137 0.2418 0.0630  0.0366  0.0024  132 TYR A CZ  
930  O OH  . TYR A 126 ? 0.2059 0.2506 0.2840 0.0658  0.0316  0.0063  132 TYR A OH  
931  N N   . GLU A 127 ? 0.1773 0.3081 0.2734 0.0370  0.0655  -0.0184 133 GLU A N   
932  C CA  . GLU A 127 ? 0.1775 0.3076 0.2607 0.0290  0.0709  -0.0214 133 GLU A CA  
933  C C   . GLU A 127 ? 0.2090 0.3463 0.2961 0.0398  0.0769  -0.0326 133 GLU A C   
934  O O   . GLU A 127 ? 0.2186 0.3430 0.2925 0.0379  0.0786  -0.0353 133 GLU A O   
935  C CB  . GLU A 127 ? 0.1545 0.3031 0.2327 0.0128  0.0762  -0.0206 133 GLU A CB  
936  C CG  . GLU A 127 ? 0.2169 0.3524 0.2877 0.0000  0.0701  -0.0094 133 GLU A CG  
937  C CD  . GLU A 127 ? 0.2974 0.4026 0.3530 -0.0044 0.0630  -0.0021 133 GLU A CD  
938  O OE1 . GLU A 127 ? 0.2841 0.3808 0.3295 -0.0023 0.0636  -0.0053 133 GLU A OE1 
939  O OE2 . GLU A 127 ? 0.2934 0.3836 0.3489 -0.0099 0.0563  0.0059  133 GLU A OE2 
940  N N   . ASP A 128 ? 0.1820 0.3398 0.2884 0.0515  0.0793  -0.0400 134 ASP A N   
941  C CA  . ASP A 128 ? 0.2141 0.3697 0.3250 0.0627  0.0827  -0.0491 134 ASP A CA  
942  C C   . ASP A 128 ? 0.2332 0.3597 0.3385 0.0731  0.0774  -0.0474 134 ASP A C   
943  O O   . ASP A 128 ? 0.2244 0.3407 0.3226 0.0760  0.0811  -0.0537 134 ASP A O   
944  C CB  . ASP A 128 ? 0.2083 0.3777 0.3387 0.0713  0.0807  -0.0516 134 ASP A CB  
945  C CG  . ASP A 128 ? 0.2968 0.4948 0.4341 0.0615  0.0884  -0.0573 134 ASP A CG  
946  O OD1 . ASP A 128 ? 0.2943 0.4985 0.4171 0.0469  0.0965  -0.0592 134 ASP A OD1 
947  O OD2 . ASP A 128 ? 0.3433 0.5574 0.5002 0.0675  0.0860  -0.0598 134 ASP A OD2 
948  N N   . MET A 129 ? 0.1983 0.3102 0.3055 0.0773  0.0691  -0.0393 135 MET A N   
949  C CA  . MET A 129 ? 0.2274 0.3095 0.3275 0.0828  0.0637  -0.0374 135 MET A CA  
950  C C   . MET A 129 ? 0.2050 0.2720 0.2901 0.0751  0.0664  -0.0364 135 MET A C   
951  O O   . MET A 129 ? 0.1944 0.2458 0.2747 0.0798  0.0673  -0.0414 135 MET A O   
952  C CB  . MET A 129 ? 0.1990 0.2679 0.2978 0.0834  0.0557  -0.0278 135 MET A CB  
953  C CG  . MET A 129 ? 0.2078 0.2464 0.2969 0.0861  0.0498  -0.0258 135 MET A CG  
954  S SD  . MET A 129 ? 0.2892 0.3209 0.3850 0.0978  0.0445  -0.0330 135 MET A SD  
955  C CE  . MET A 129 ? 0.3165 0.3176 0.3963 0.0953  0.0421  -0.0327 135 MET A CE  
956  N N   . VAL A 130 ? 0.2044 0.2733 0.2818 0.0611  0.0649  -0.0299 136 VAL A N   
957  C CA  . VAL A 130 ? 0.1924 0.2469 0.2557 0.0514  0.0631  -0.0283 136 VAL A CA  
958  C C   . VAL A 130 ? 0.2140 0.2741 0.2680 0.0507  0.0693  -0.0383 136 VAL A C   
959  O O   . VAL A 130 ? 0.1971 0.2406 0.2414 0.0496  0.0673  -0.0408 136 VAL A O   
960  C CB  . VAL A 130 ? 0.2156 0.2726 0.2726 0.0369  0.0596  -0.0197 136 VAL A CB  
961  C CG1 . VAL A 130 ? 0.2300 0.2718 0.2721 0.0272  0.0545  -0.0171 136 VAL A CG1 
962  C CG2 . VAL A 130 ? 0.2005 0.2503 0.2668 0.0371  0.0546  -0.0121 136 VAL A CG2 
963  N N   . ARG A 131 ? 0.2052 0.2900 0.2625 0.0500  0.0777  -0.0453 137 ARG A N   
964  C CA  . ARG A 131 ? 0.2407 0.3317 0.2884 0.0480  0.0861  -0.0572 137 ARG A CA  
965  C C   . ARG A 131 ? 0.2308 0.3113 0.2862 0.0634  0.0880  -0.0671 137 ARG A C   
966  O O   . ARG A 131 ? 0.2212 0.2935 0.2640 0.0609  0.0917  -0.0754 137 ARG A O   
967  C CB  . ARG A 131 ? 0.2382 0.3604 0.2911 0.0431  0.0972  -0.0649 137 ARG A CB  
968  C CG  . ARG A 131 ? 0.3050 0.4348 0.3439 0.0240  0.0971  -0.0561 137 ARG A CG  
969  C CD  . ARG A 131 ? 0.3826 0.5459 0.4300 0.0181  0.1098  -0.0648 137 ARG A CD  
970  N N   . GLN A 132 ? 0.2194 0.2964 0.2919 0.0780  0.0843  -0.0653 138 GLN A N   
971  C CA  . GLN A 132 ? 0.2474 0.3040 0.3180 0.0891  0.0819  -0.0673 138 GLN A CA  
972  C C   . GLN A 132 ? 0.2332 0.2641 0.2934 0.0870  0.0766  -0.0665 138 GLN A C   
973  O O   . GLN A 132 ? 0.2242 0.2418 0.2763 0.0888  0.0779  -0.0735 138 GLN A O   
974  C CB  . GLN A 132 ? 0.2371 0.2878 0.3200 0.1001  0.0767  -0.0592 138 GLN A CB  
975  C CG  . GLN A 132 ? 0.2517 0.3278 0.3524 0.1015  0.0790  -0.0601 138 GLN A CG  
976  C CD  . GLN A 132 ? 0.3110 0.4032 0.4172 0.1041  0.0871  -0.0715 138 GLN A CD  
977  O OE1 . GLN A 132 ? 0.2845 0.3652 0.3837 0.1079  0.0907  -0.0788 138 GLN A OE1 
978  N NE2 . GLN A 132 ? 0.3690 0.4885 0.4886 0.1015  0.0902  -0.0740 138 GLN A NE2 
979  N N   . VAL A 133 ? 0.2320 0.2535 0.2939 0.0819  0.0715  -0.0571 139 VAL A N   
980  C CA  . VAL A 133 ? 0.1983 0.1953 0.2527 0.0772  0.0667  -0.0542 139 VAL A CA  
981  C C   . VAL A 133 ? 0.2323 0.2287 0.2709 0.0660  0.0669  -0.0587 139 VAL A C   
982  O O   . VAL A 133 ? 0.2201 0.2000 0.2522 0.0656  0.0656  -0.0642 139 VAL A O   
983  C CB  . VAL A 133 ? 0.2277 0.2178 0.2859 0.0718  0.0602  -0.0421 139 VAL A CB  
984  C CG1 . VAL A 133 ? 0.2016 0.1738 0.2555 0.0637  0.0546  -0.0399 139 VAL A CG1 
985  C CG2 . VAL A 133 ? 0.2080 0.1925 0.2700 0.0775  0.0538  -0.0375 139 VAL A CG2 
986  N N   . GLN A 134 ? 0.2098 0.2231 0.2396 0.0556  0.0684  -0.0568 140 GLN A N   
987  C CA  . GLN A 134 ? 0.2489 0.2588 0.2578 0.0427  0.0667  -0.0591 140 GLN A CA  
988  C C   . GLN A 134 ? 0.2605 0.2709 0.2606 0.0454  0.0752  -0.0742 140 GLN A C   
989  O O   . GLN A 134 ? 0.2839 0.2807 0.2682 0.0386  0.0717  -0.0781 140 GLN A O   
990  C CB  . GLN A 134 ? 0.2384 0.2632 0.2361 0.0293  0.0668  -0.0525 140 GLN A CB  
991  C CG  . GLN A 134 ? 0.2671 0.2825 0.2690 0.0239  0.0553  -0.0383 140 GLN A CG  
992  C CD  . GLN A 134 ? 0.3054 0.3319 0.2993 0.0119  0.0545  -0.0299 140 GLN A CD  
993  O OE1 . GLN A 134 ? 0.2740 0.3197 0.2629 0.0079  0.0643  -0.0344 140 GLN A OE1 
994  N NE2 . GLN A 134 ? 0.3347 0.3492 0.3301 0.0059  0.0431  -0.0184 140 GLN A NE2 
995  N N   . ARG A 135 ? 0.2482 0.2738 0.2603 0.0559  0.0858  -0.0840 141 ARG A N   
996  C CA  . ARG A 135 ? 0.3047 0.3314 0.3117 0.0594  0.0956  -0.1010 141 ARG A CA  
997  C C   . ARG A 135 ? 0.2758 0.2779 0.2872 0.0695  0.0927  -0.1064 141 ARG A C   
998  O O   . ARG A 135 ? 0.2976 0.2935 0.2990 0.0692  0.0974  -0.1184 141 ARG A O   
999  C CB  . ARG A 135 ? 0.2703 0.3202 0.2931 0.0683  0.1049  -0.1076 141 ARG A CB  
1000 C CG  . ARG A 135 ? 0.4296 0.5018 0.4400 0.0556  0.1163  -0.1161 141 ARG A CG  
1001 C CD  . ARG A 135 ? 0.4629 0.5548 0.4932 0.0643  0.1212  -0.1178 141 ARG A CD  
1002 N NE  . ARG A 135 ? 0.4464 0.5522 0.4936 0.0668  0.1169  -0.1068 141 ARG A NE  
1003 C CZ  . ARG A 135 ? 0.4916 0.6095 0.5613 0.0772  0.1161  -0.1049 141 ARG A CZ  
1004 N NH1 . ARG A 135 ? 0.5048 0.6229 0.5856 0.0879  0.1195  -0.1128 141 ARG A NH1 
1005 N NH2 . ARG A 135 ? 0.4319 0.5618 0.5135 0.0765  0.1116  -0.0954 141 ARG A NH2 
1006 N N   . SER A 136 ? 0.2473 0.1851 0.2465 0.0577  0.0270  -0.0667 142 SER A N   
1007 C CA  . SER A 136 ? 0.2833 0.2075 0.2822 0.0595  0.0240  -0.0669 142 SER A CA  
1008 C C   . SER A 136 ? 0.3020 0.2162 0.2959 0.0540  0.0206  -0.0674 142 SER A C   
1009 O O   . SER A 136 ? 0.2630 0.1816 0.2598 0.0507  0.0186  -0.0638 142 SER A O   
1010 C CB  . SER A 136 ? 0.2606 0.1875 0.2665 0.0625  0.0220  -0.0623 142 SER A CB  
1011 O OG  . SER A 136 ? 0.2448 0.1824 0.2572 0.0681  0.0231  -0.0629 142 SER A OG  
1012 N N   . ARG A 137 ? 0.2605 0.1610 0.2476 0.0529  0.0195  -0.0726 143 ARG A N   
1013 C CA  . ARG A 137 ? 0.3126 0.2031 0.2963 0.0470  0.0148  -0.0742 143 ARG A CA  
1014 C C   . ARG A 137 ? 0.3042 0.1841 0.2909 0.0459  0.0125  -0.0709 143 ARG A C   
1015 O O   . ARG A 137 ? 0.2931 0.1715 0.2825 0.0406  0.0091  -0.0701 143 ARG A O   
1016 C CB  . ARG A 137 ? 0.3223 0.2001 0.2967 0.0449  0.0138  -0.0817 143 ARG A CB  
1017 C CG  . ARG A 137 ? 0.3321 0.1978 0.3038 0.0377  0.0074  -0.0845 143 ARG A CG  
1018 C CD  . ARG A 137 ? 0.3338 0.2107 0.3088 0.0334  0.0027  -0.0848 143 ARG A CD  
1019 N NE  . ARG A 137 ? 0.4051 0.2836 0.3703 0.0327  0.0022  -0.0902 143 ARG A NE  
1020 C CZ  . ARG A 137 ? 0.3829 0.2672 0.3467 0.0294  -0.0034 -0.0924 143 ARG A CZ  
1021 N NH1 . ARG A 137 ? 0.3589 0.2504 0.3347 0.0267  -0.0091 -0.0903 143 ARG A NH1 
1022 N NH2 . ARG A 137 ? 0.3672 0.2497 0.3176 0.0289  -0.0035 -0.0974 143 ARG A NH2 
1023 N N   . PHE A 138 ? 0.2773 0.1490 0.2646 0.0506  0.0140  -0.0698 144 PHE A N   
1024 C CA  . PHE A 138 ? 0.2899 0.1468 0.2776 0.0497  0.0123  -0.0668 144 PHE A CA  
1025 C C   . PHE A 138 ? 0.2839 0.1496 0.2775 0.0556  0.0130  -0.0615 144 PHE A C   
1026 O O   . PHE A 138 ? 0.2768 0.1510 0.2733 0.0624  0.0138  -0.0619 144 PHE A O   
1027 C CB  . PHE A 138 ? 0.3007 0.1373 0.2838 0.0510  0.0112  -0.0704 144 PHE A CB  
1028 C CG  . PHE A 138 ? 0.3438 0.1700 0.3204 0.0445  0.0100  -0.0768 144 PHE A CG  
1029 C CD1 . PHE A 138 ? 0.3364 0.1687 0.3091 0.0462  0.0116  -0.0825 144 PHE A CD1 
1030 C CD2 . PHE A 138 ? 0.3396 0.1492 0.3134 0.0355  0.0071  -0.0777 144 PHE A CD2 
1031 C CE1 . PHE A 138 ? 0.3428 0.1651 0.3079 0.0400  0.0094  -0.0892 144 PHE A CE1 
1032 C CE2 . PHE A 138 ? 0.4045 0.2055 0.3725 0.0284  0.0047  -0.0843 144 PHE A CE2 
1033 C CZ  . PHE A 138 ? 0.4049 0.2122 0.3680 0.0312  0.0054  -0.0902 144 PHE A CZ  
1034 N N   . ILE A 139 ? 0.2616 0.1250 0.2565 0.0528  0.0122  -0.0572 145 ILE A N   
1035 C CA  . ILE A 139 ? 0.2500 0.1214 0.2485 0.0575  0.0119  -0.0527 145 ILE A CA  
1036 C C   . ILE A 139 ? 0.2898 0.1411 0.2826 0.0563  0.0090  -0.0490 145 ILE A C   
1037 O O   . ILE A 139 ? 0.2978 0.1372 0.2885 0.0483  0.0095  -0.0490 145 ILE A O   
1038 C CB  . ILE A 139 ? 0.2326 0.1240 0.2358 0.0552  0.0146  -0.0511 145 ILE A CB  
1039 C CG1 . ILE A 139 ? 0.2339 0.1404 0.2387 0.0551  0.0163  -0.0535 145 ILE A CG1 
1040 C CG2 . ILE A 139 ? 0.2055 0.1046 0.2116 0.0595  0.0138  -0.0477 145 ILE A CG2 
1041 C CD1 . ILE A 139 ? 0.2408 0.1641 0.2490 0.0524  0.0177  -0.0515 145 ILE A CD1 
1042 N N   . VAL A 140 ? 0.2735 0.1191 0.2611 0.0639  0.0053  -0.0451 146 VAL A N   
1043 C CA  . VAL A 140 ? 0.2828 0.1044 0.2560 0.0634  0.0027  -0.0387 146 VAL A CA  
1044 C C   . VAL A 140 ? 0.2751 0.1058 0.2452 0.0674  0.0024  -0.0350 146 VAL A C   
1045 O O   . VAL A 140 ? 0.2650 0.1126 0.2410 0.0754  -0.0004 -0.0361 146 VAL A O   
1046 C CB  . VAL A 140 ? 0.3126 0.1121 0.2751 0.0696  -0.0023 -0.0360 146 VAL A CB  
1047 C CG1 . VAL A 140 ? 0.3389 0.1138 0.2813 0.0707  -0.0053 -0.0268 146 VAL A CG1 
1048 C CG2 . VAL A 140 ? 0.3272 0.1109 0.2887 0.0633  -0.0014 -0.0393 146 VAL A CG2 
1049 N N   . VAL A 141 ? 0.2804 0.0993 0.2403 0.0608  0.0064  -0.0309 147 VAL A N   
1050 C CA  . VAL A 141 ? 0.2813 0.1028 0.2324 0.0630  0.0072  -0.0259 147 VAL A CA  
1051 C C   . VAL A 141 ? 0.3171 0.1081 0.2445 0.0615  0.0052  -0.0166 147 VAL A C   
1052 O O   . VAL A 141 ? 0.3680 0.1399 0.2874 0.0503  0.0097  -0.0128 147 VAL A O   
1053 C CB  . VAL A 141 ? 0.2644 0.1069 0.2256 0.0516  0.0156  -0.0262 147 VAL A CB  
1054 C CG1 . VAL A 141 ? 0.2887 0.1360 0.2400 0.0514  0.0171  -0.0212 147 VAL A CG1 
1055 C CG2 . VAL A 141 ? 0.2283 0.0969 0.2100 0.0532  0.0167  -0.0344 147 VAL A CG2 
1056 N N   . VAL A 142 ? 0.3308 0.1162 0.2462 0.0724  -0.0020 -0.0128 148 VAL A N   
1057 C CA  . VAL A 142 ? 0.3700 0.1235 0.2583 0.0727  -0.0057 -0.0027 148 VAL A CA  
1058 C C   . VAL A 142 ? 0.3831 0.1432 0.2595 0.0658  -0.0016 0.0031  148 VAL A C   
1059 O O   . VAL A 142 ? 0.3588 0.1404 0.2407 0.0725  -0.0051 0.0004  148 VAL A O   
1060 C CB  . VAL A 142 ? 0.3885 0.1330 0.2712 0.0894  -0.0184 -0.0019 148 VAL A CB  
1061 C CG1 . VAL A 142 ? 0.4373 0.1444 0.2899 0.0885  -0.0225 0.0095  148 VAL A CG1 
1062 C CG2 . VAL A 142 ? 0.3757 0.1341 0.2803 0.0925  -0.0199 -0.0098 148 VAL A CG2 
1063 N N   . GLY A 143 ? 0.3991 0.1405 0.2588 0.0518  0.0064  0.0104  149 GLY A N   
1064 C CA  . GLY A 143 ? 0.4072 0.1511 0.2517 0.0439  0.0123  0.0157  149 GLY A CA  
1065 C C   . GLY A 143 ? 0.3992 0.1660 0.2613 0.0295  0.0261  0.0112  149 GLY A C   
1066 O O   . GLY A 143 ? 0.3766 0.1724 0.2638 0.0322  0.0271  0.0027  149 GLY A O   
1067 N N   . GLY A 144 ? 0.4355 0.1890 0.2851 0.0142  0.0370  0.0165  150 GLY A N   
1068 C CA  . GLY A 144 ? 0.3974 0.1728 0.2656 0.0008  0.0505  0.0119  150 GLY A CA  
1069 C C   . GLY A 144 ? 0.4166 0.1986 0.2718 -0.0058 0.0596  0.0142  150 GLY A C   
1070 O O   . GLY A 144 ? 0.4427 0.2277 0.2993 -0.0202 0.0734  0.0146  150 GLY A O   
1071 N N   . GLY A 145 ? 0.3988 0.1835 0.2413 0.0045  0.0523  0.0151  151 GLY A N   
1072 C CA  . GLY A 145 ? 0.4100 0.2075 0.2450 0.0003  0.0599  0.0138  151 GLY A CA  
1073 C C   . GLY A 145 ? 0.3839 0.2155 0.2517 -0.0004 0.0661  0.0033  151 GLY A C   
1074 O O   . GLY A 145 ? 0.3188 0.1629 0.2127 0.0008  0.0650  -0.0018 151 GLY A O   
1075 N N   . SER A 146 ? 0.3932 0.2382 0.2576 -0.0018 0.0719  -0.0001 152 SER A N   
1076 C CA  . SER A 146 ? 0.3477 0.2217 0.2415 -0.0019 0.0779  -0.0096 152 SER A CA  
1077 C C   . SER A 146 ? 0.3379 0.2262 0.2520 0.0099  0.0664  -0.0150 152 SER A C   
1078 O O   . SER A 146 ? 0.3151 0.2208 0.2553 0.0099  0.0689  -0.0209 152 SER A O   
1079 C CB  . SER A 146 ? 0.4254 0.3080 0.3097 -0.0051 0.0865  -0.0131 152 SER A CB  
1080 O OG  . SER A 146 ? 0.4878 0.3645 0.3515 0.0024  0.0765  -0.0118 152 SER A OG  
1081 N N   . ALA A 147 ? 0.3535 0.2348 0.2563 0.0199  0.0538  -0.0130 153 ALA A N   
1082 C CA  . ALA A 147 ? 0.3271 0.2231 0.2496 0.0298  0.0447  -0.0186 153 ALA A CA  
1083 C C   . ALA A 147 ? 0.2936 0.1860 0.2304 0.0311  0.0421  -0.0188 153 ALA A C   
1084 O O   . ALA A 147 ? 0.2451 0.1531 0.2035 0.0333  0.0417  -0.0246 153 ALA A O   
1085 C CB  . ALA A 147 ? 0.3039 0.1964 0.2136 0.0401  0.0322  -0.0175 153 ALA A CB  
1086 N N   . GLY A 148 ? 0.2969 0.1664 0.2194 0.0296  0.0399  -0.0124 154 GLY A N   
1087 C CA  . GLY A 148 ? 0.2749 0.1383 0.2085 0.0304  0.0371  -0.0133 154 GLY A CA  
1088 C C   . GLY A 148 ? 0.2608 0.1360 0.2142 0.0207  0.0457  -0.0171 154 GLY A C   
1089 O O   . GLY A 148 ? 0.2335 0.1163 0.2036 0.0231  0.0425  -0.0219 154 GLY A O   
1090 N N   . VAL A 149 ? 0.2795 0.1568 0.2313 0.0097  0.0565  -0.0156 155 VAL A N   
1091 C CA  . VAL A 149 ? 0.2478 0.1397 0.2222 0.0014  0.0637  -0.0200 155 VAL A CA  
1092 C C   . VAL A 149 ? 0.2490 0.1662 0.2449 0.0072  0.0626  -0.0272 155 VAL A C   
1093 O O   . VAL A 149 ? 0.2157 0.1437 0.2311 0.0064  0.0612  -0.0314 155 VAL A O   
1094 C CB  . VAL A 149 ? 0.2912 0.1821 0.2613 -0.0118 0.0769  -0.0176 155 VAL A CB  
1095 C CG1 . VAL A 149 ? 0.2928 0.1539 0.2369 -0.0183 0.0779  -0.0092 155 VAL A CG1 
1096 C CG2 . VAL A 149 ? 0.2864 0.1881 0.2507 -0.0110 0.0836  -0.0191 155 VAL A CG2 
1097 N N   . GLU A 150 ? 0.2195 0.1441 0.2102 0.0132  0.0618  -0.0286 156 GLU A N   
1098 C CA  . GLU A 150 ? 0.2304 0.1741 0.2383 0.0187  0.0601  -0.0348 156 GLU A CA  
1099 C C   . GLU A 150 ? 0.2287 0.1728 0.2422 0.0264  0.0504  -0.0368 156 GLU A C   
1100 O O   . GLU A 150 ? 0.1968 0.1518 0.2262 0.0275  0.0492  -0.0408 156 GLU A O   
1101 C CB  . GLU A 150 ? 0.2139 0.1634 0.2135 0.0216  0.0620  -0.0365 156 GLU A CB  
1102 C CG  . GLU A 150 ? 0.2572 0.2116 0.2563 0.0145  0.0738  -0.0377 156 GLU A CG  
1103 C CD  . GLU A 150 ? 0.3303 0.2900 0.3213 0.0169  0.0760  -0.0411 156 GLU A CD  
1104 O OE1 . GLU A 150 ? 0.3596 0.3165 0.3405 0.0227  0.0679  -0.0410 156 GLU A OE1 
1105 O OE2 . GLU A 150 ? 0.2955 0.2629 0.2915 0.0131  0.0859  -0.0449 156 GLU A OE2 
1106 N N   . MET A 151 ? 0.2053 0.1372 0.2055 0.0322  0.0434  -0.0343 157 MET A N   
1107 C CA  . MET A 151 ? 0.1928 0.1262 0.1988 0.0398  0.0359  -0.0374 157 MET A CA  
1108 C C   . MET A 151 ? 0.2205 0.1507 0.2358 0.0364  0.0353  -0.0389 157 MET A C   
1109 O O   . MET A 151 ? 0.2216 0.1613 0.2478 0.0389  0.0331  -0.0434 157 MET A O   
1110 C CB  . MET A 151 ? 0.2395 0.1598 0.2313 0.0474  0.0286  -0.0348 157 MET A CB  
1111 C CG  . MET A 151 ? 0.2275 0.1512 0.2260 0.0565  0.0220  -0.0393 157 MET A CG  
1112 S SD  . MET A 151 ? 0.3532 0.3024 0.3636 0.0582  0.0217  -0.0435 157 MET A SD  
1113 C CE  . MET A 151 ? 0.2198 0.1780 0.2364 0.0514  0.0252  -0.0420 157 MET A CE  
1114 N N   . ALA A 152 ? 0.2198 0.1355 0.2293 0.0299  0.0372  -0.0353 158 ALA A N   
1115 C CA  . ALA A 152 ? 0.2431 0.1547 0.2605 0.0253  0.0358  -0.0373 158 ALA A CA  
1116 C C   . ALA A 152 ? 0.2301 0.1605 0.2664 0.0205  0.0388  -0.0412 158 ALA A C   
1117 O O   . ALA A 152 ? 0.1940 0.1291 0.2391 0.0215  0.0344  -0.0451 158 ALA A O   
1118 C CB  . ALA A 152 ? 0.2227 0.1140 0.2295 0.0170  0.0384  -0.0325 158 ALA A CB  
1119 N N   . ALA A 153 ? 0.1761 0.1172 0.2181 0.0161  0.0459  -0.0404 159 ALA A N   
1120 C CA  . ALA A 153 ? 0.2152 0.1747 0.2769 0.0135  0.0481  -0.0442 159 ALA A CA  
1121 C C   . ALA A 153 ? 0.1872 0.1568 0.2543 0.0216  0.0433  -0.0475 159 ALA A C   
1122 O O   . ALA A 153 ? 0.1574 0.1349 0.2363 0.0219  0.0396  -0.0504 159 ALA A O   
1123 C CB  . ALA A 153 ? 0.1948 0.1629 0.2608 0.0085  0.0580  -0.0435 159 ALA A CB  
1124 N N   . GLU A 154 ? 0.1534 0.1223 0.2095 0.0273  0.0421  -0.0462 160 GLU A N   
1125 C CA  . GLU A 154 ? 0.1858 0.1642 0.2382 0.0308  0.0352  -0.0444 160 GLU A CA  
1126 C C   . GLU A 154 ? 0.1845 0.1593 0.2343 0.0326  0.0289  -0.0450 160 GLU A C   
1127 O O   . GLU A 154 ? 0.1609 0.1414 0.2136 0.0325  0.0260  -0.0451 160 GLU A O   
1128 C CB  . GLU A 154 ? 0.1599 0.1388 0.2002 0.0344  0.0339  -0.0425 160 GLU A CB  
1129 C CG  . GLU A 154 ? 0.2099 0.1938 0.2500 0.0328  0.0388  -0.0425 160 GLU A CG  
1130 C CD  . GLU A 154 ? 0.2196 0.2124 0.2642 0.0315  0.0379  -0.0415 160 GLU A CD  
1131 O OE1 . GLU A 154 ? 0.1981 0.1923 0.2423 0.0326  0.0334  -0.0403 160 GLU A OE1 
1132 O OE2 . GLU A 154 ? 0.2260 0.2222 0.2736 0.0296  0.0427  -0.0423 160 GLU A OE2 
1133 N N   . ILE A 155 ? 0.1642 0.1275 0.2069 0.0346  0.0271  -0.0457 161 ILE A N   
1134 C CA  . ILE A 155 ? 0.1676 0.1263 0.2058 0.0363  0.0223  -0.0470 161 ILE A CA  
1135 C C   . ILE A 155 ? 0.1632 0.1223 0.2122 0.0321  0.0208  -0.0508 161 ILE A C   
1136 O O   . ILE A 155 ? 0.1711 0.1331 0.2189 0.0329  0.0172  -0.0523 161 ILE A O   
1137 C CB  . ILE A 155 ? 0.2086 0.1526 0.2371 0.0399  0.0207  -0.0473 161 ILE A CB  
1138 C CG1 . ILE A 155 ? 0.1880 0.1337 0.2086 0.0456  0.0212  -0.0445 161 ILE A CG1 
1139 C CG2 . ILE A 155 ? 0.1793 0.1177 0.2029 0.0409  0.0174  -0.0495 161 ILE A CG2 
1140 C CD1 . ILE A 155 ? 0.1921 0.1214 0.2052 0.0505  0.0200  -0.0444 161 ILE A CD1 
1141 N N   . LYS A 156 ? 0.1381 0.0930 0.1984 0.0272  0.0240  -0.0535 162 LYS A N   
1142 C CA  . LYS A 156 ? 0.1738 0.1315 0.2450 0.0219  0.0204  -0.0568 162 LYS A CA  
1143 C C   . LYS A 156 ? 0.1832 0.1576 0.2679 0.0228  0.0194  -0.0578 162 LYS A C   
1144 O O   . LYS A 156 ? 0.1712 0.1499 0.2622 0.0213  0.0130  -0.0603 162 LYS A O   
1145 C CB  . LYS A 156 ? 0.2069 0.1597 0.2828 0.0124  0.0231  -0.0554 162 LYS A CB  
1146 C CG  . LYS A 156 ? 0.2575 0.1913 0.3232 0.0090  0.0197  -0.0565 162 LYS A CG  
1147 C CD  . LYS A 156 ? 0.2436 0.1767 0.3095 0.0096  0.0116  -0.0619 162 LYS A CD  
1148 C CE  . LYS A 156 ? 0.2668 0.1924 0.3367 -0.0010 0.0087  -0.0644 162 LYS A CE  
1149 N NZ  . LYS A 156 ? 0.2204 0.1374 0.2829 -0.0006 0.0006  -0.0702 162 LYS A NZ  
1150 N N   . THR A 157 ? 0.1462 0.1290 0.2342 0.0255  0.0246  -0.0558 163 THR A N   
1151 C CA  . THR A 157 ? 0.1554 0.1510 0.2531 0.0273  0.0227  -0.0556 163 THR A CA  
1152 C C   . THR A 157 ? 0.1804 0.1734 0.2649 0.0313  0.0170  -0.0534 163 THR A C   
1153 O O   . THR A 157 ? 0.1639 0.1606 0.2554 0.0335  0.0117  -0.0557 163 THR A O   
1154 C CB  . THR A 157 ? 0.1562 0.1587 0.2547 0.0268  0.0291  -0.0521 163 THR A CB  
1155 O OG1 . THR A 157 ? 0.1653 0.1691 0.2742 0.0222  0.0372  -0.0545 163 THR A OG1 
1156 C CG2 . THR A 157 ? 0.1419 0.1547 0.2502 0.0291  0.0268  -0.0519 163 THR A CG2 
1157 N N   . GLU A 158 ? 0.1458 0.1330 0.2126 0.0326  0.0183  -0.0497 164 GLU A N   
1158 C CA  . GLU A 158 ? 0.1849 0.1694 0.2407 0.0350  0.0159  -0.0487 164 GLU A CA  
1159 C C   . GLU A 158 ? 0.1859 0.1634 0.2372 0.0356  0.0115  -0.0530 164 GLU A C   
1160 O O   . GLU A 158 ? 0.1916 0.1669 0.2382 0.0374  0.0084  -0.0549 164 GLU A O   
1161 C CB  . GLU A 158 ? 0.1730 0.1563 0.2161 0.0357  0.0193  -0.0447 164 GLU A CB  
1162 C CG  . GLU A 158 ? 0.1972 0.1855 0.2418 0.0351  0.0224  -0.0418 164 GLU A CG  
1163 C CD  . GLU A 158 ? 0.2404 0.2312 0.2899 0.0358  0.0219  -0.0417 164 GLU A CD  
1164 O OE1 . GLU A 158 ? 0.2914 0.2786 0.3347 0.0371  0.0212  -0.0417 164 GLU A OE1 
1165 O OE2 . GLU A 158 ? 0.2308 0.2264 0.2909 0.0355  0.0227  -0.0422 164 GLU A OE2 
1166 N N   . TYR A 159 ? 0.1819 0.1536 0.2329 0.0342  0.0109  -0.0554 165 TYR A N   
1167 C CA  . TYR A 159 ? 0.1959 0.1583 0.2388 0.0343  0.0069  -0.0599 165 TYR A CA  
1168 C C   . TYR A 159 ? 0.1982 0.1550 0.2506 0.0306  0.0030  -0.0653 165 TYR A C   
1169 O O   . TYR A 159 ? 0.1882 0.1346 0.2349 0.0291  0.0039  -0.0658 165 TYR A O   
1170 C CB  . TYR A 159 ? 0.1904 0.1470 0.2197 0.0362  0.0105  -0.0575 165 TYR A CB  
1171 C CG  . TYR A 159 ? 0.2209 0.1837 0.2445 0.0381  0.0146  -0.0534 165 TYR A CG  
1172 C CD1 . TYR A 159 ? 0.2442 0.2067 0.2604 0.0387  0.0155  -0.0551 165 TYR A CD1 
1173 C CD2 . TYR A 159 ? 0.1982 0.1659 0.2234 0.0386  0.0176  -0.0489 165 TYR A CD2 
1174 C CE1 . TYR A 159 ? 0.2337 0.2011 0.2465 0.0391  0.0197  -0.0524 165 TYR A CE1 
1175 C CE2 . TYR A 159 ? 0.2306 0.2037 0.2521 0.0393  0.0205  -0.0463 165 TYR A CE2 
1176 C CZ  . TYR A 159 ? 0.2476 0.2207 0.2640 0.0393  0.0217  -0.0481 165 TYR A CZ  
1177 O OH  . TYR A 159 ? 0.2235 0.2019 0.2381 0.0392  0.0247  -0.0467 165 TYR A OH  
1178 N N   . PRO A 160 ? 0.1933 0.1573 0.2579 0.0277  -0.0021 -0.0668 166 PRO A N   
1179 C CA  . PRO A 160 ? 0.2111 0.1743 0.2846 0.0200  -0.0058 -0.0687 166 PRO A CA  
1180 C C   . PRO A 160 ? 0.2381 0.1857 0.2984 0.0176  -0.0098 -0.0731 166 PRO A C   
1181 O O   . PRO A 160 ? 0.2095 0.1501 0.2729 0.0107  -0.0101 -0.0745 166 PRO A O   
1182 C CB  . PRO A 160 ? 0.2086 0.1855 0.2954 0.0187  -0.0133 -0.0693 166 PRO A CB  
1183 C CG  . PRO A 160 ? 0.2201 0.2036 0.3068 0.0259  -0.0114 -0.0662 166 PRO A CG  
1184 C CD  . PRO A 160 ? 0.1635 0.1376 0.2337 0.0305  -0.0053 -0.0652 166 PRO A CD  
1185 N N   . GLU A 161 ? 0.2226 0.1632 0.2670 0.0223  -0.0121 -0.0759 167 GLU A N   
1186 C CA  . GLU A 161 ? 0.2631 0.1883 0.2936 0.0207  -0.0155 -0.0816 167 GLU A CA  
1187 C C   . GLU A 161 ? 0.2472 0.1604 0.2683 0.0231  -0.0088 -0.0797 167 GLU A C   
1188 O O   . GLU A 161 ? 0.2443 0.1440 0.2537 0.0217  -0.0101 -0.0829 167 GLU A O   
1189 C CB  . GLU A 161 ? 0.2760 0.1990 0.2905 0.0244  -0.0189 -0.0849 167 GLU A CB  
1190 C CG  . GLU A 161 ? 0.2526 0.1773 0.2562 0.0306  -0.0099 -0.0809 167 GLU A CG  
1191 C CD  . GLU A 161 ? 0.2826 0.2200 0.2942 0.0337  -0.0061 -0.0755 167 GLU A CD  
1192 O OE1 . GLU A 161 ? 0.2210 0.1662 0.2475 0.0329  -0.0091 -0.0744 167 GLU A OE1 
1193 O OE2 . GLU A 161 ? 0.2752 0.2151 0.2787 0.0362  0.0006  -0.0721 167 GLU A OE2 
1194 N N   . LYS A 162 ? 0.2277 0.1457 0.2516 0.0267  -0.0021 -0.0734 168 LYS A N   
1195 C CA  . LYS A 162 ? 0.2476 0.1542 0.2615 0.0298  0.0020  -0.0705 168 LYS A CA  
1196 C C   . LYS A 162 ? 0.2875 0.1804 0.3052 0.0244  0.0014  -0.0708 168 LYS A C   
1197 O O   . LYS A 162 ? 0.2701 0.1671 0.3024 0.0175  0.0006  -0.0721 168 LYS A O   
1198 C CB  . LYS A 162 ? 0.2316 0.1478 0.2446 0.0356  0.0074  -0.0642 168 LYS A CB  
1199 C CG  . LYS A 162 ? 0.2350 0.1599 0.2421 0.0389  0.0096  -0.0641 168 LYS A CG  
1200 C CD  . LYS A 162 ? 0.2497 0.1850 0.2584 0.0421  0.0140  -0.0586 168 LYS A CD  
1201 C CE  . LYS A 162 ? 0.2558 0.1990 0.2606 0.0430  0.0168  -0.0591 168 LYS A CE  
1202 N NZ  . LYS A 162 ? 0.2823 0.2193 0.2794 0.0451  0.0188  -0.0633 168 LYS A NZ  
1203 N N   . GLU A 163 ? 0.2722 0.1478 0.2777 0.0267  0.0026  -0.0700 169 GLU A N   
1204 C CA  . GLU A 163 ? 0.3264 0.1829 0.3306 0.0214  0.0026  -0.0691 169 GLU A CA  
1205 C C   . GLU A 163 ? 0.3135 0.1669 0.3147 0.0272  0.0066  -0.0627 169 GLU A C   
1206 O O   . GLU A 163 ? 0.3129 0.1665 0.3067 0.0359  0.0088  -0.0606 169 GLU A O   
1207 C CB  . GLU A 163 ? 0.3132 0.1479 0.3034 0.0205  0.0012  -0.0723 169 GLU A CB  
1208 C CG  . GLU A 163 ? 0.3914 0.2263 0.3813 0.0141  -0.0038 -0.0795 169 GLU A CG  
1209 C CD  . GLU A 163 ? 0.5174 0.3542 0.5212 0.0011  -0.0079 -0.0819 169 GLU A CD  
1210 O OE1 . GLU A 163 ? 0.6187 0.4400 0.6228 -0.0065 -0.0063 -0.0798 169 GLU A OE1 
1211 O OE2 . GLU A 163 ? 0.5619 0.4164 0.5777 -0.0021 -0.0121 -0.0855 169 GLU A OE2 
1212 N N   . VAL A 164 ? 0.3138 0.1668 0.3244 0.0209  0.0094  -0.0602 170 VAL A N   
1213 C CA  . VAL A 164 ? 0.2898 0.1406 0.2971 0.0255  0.0133  -0.0544 170 VAL A CA  
1214 C C   . VAL A 164 ? 0.3046 0.1340 0.3029 0.0171  0.0159  -0.0487 170 VAL A C   
1215 O O   . VAL A 164 ? 0.2900 0.1217 0.2954 0.0040  0.0190  -0.0479 170 VAL A O   
1216 C CB  . VAL A 164 ? 0.2577 0.1335 0.2765 0.0246  0.0175  -0.0520 170 VAL A CB  
1217 C CG1 . VAL A 164 ? 0.2467 0.1193 0.2576 0.0278  0.0208  -0.0456 170 VAL A CG1 
1218 C CG2 . VAL A 164 ? 0.2470 0.1419 0.2690 0.0317  0.0150  -0.0548 170 VAL A CG2 
1219 N N   . THR A 165 ? 0.3174 0.1263 0.3001 0.0243  0.0145  -0.0446 171 THR A N   
1220 C CA  . THR A 165 ? 0.3559 0.1396 0.3244 0.0170  0.0170  -0.0373 171 THR A CA  
1221 C C   . THR A 165 ? 0.3417 0.1269 0.3011 0.0220  0.0190  -0.0298 171 THR A C   
1222 O O   . THR A 165 ? 0.3297 0.1211 0.2873 0.0357  0.0147  -0.0306 171 THR A O   
1223 C CB  . THR A 165 ? 0.3714 0.1299 0.3286 0.0207  0.0109  -0.0376 171 THR A CB  
1224 O OG1 . THR A 165 ? 0.4012 0.1609 0.3669 0.0141  0.0088  -0.0450 171 THR A OG1 
1225 C CG2 . THR A 165 ? 0.3873 0.1160 0.3260 0.0136  0.0132  -0.0288 171 THR A CG2 
1226 N N   . LEU A 166 ? 0.3336 0.1147 0.2878 0.0103  0.0258  -0.0234 172 LEU A N   
1227 C CA  . LEU A 166 ? 0.3454 0.1238 0.2859 0.0128  0.0283  -0.0159 172 LEU A CA  
1228 C C   . LEU A 166 ? 0.3679 0.1090 0.2831 0.0083  0.0283  -0.0076 172 LEU A C   
1229 O O   . LEU A 166 ? 0.3849 0.1129 0.2979 -0.0066 0.0341  -0.0058 172 LEU A O   
1230 C CB  . LEU A 166 ? 0.3152 0.1172 0.2666 0.0026  0.0378  -0.0153 172 LEU A CB  
1231 C CG  . LEU A 166 ? 0.3435 0.1435 0.2790 0.0028  0.0420  -0.0086 172 LEU A CG  
1232 C CD1 . LEU A 166 ? 0.3403 0.1444 0.2700 0.0190  0.0334  -0.0088 172 LEU A CD1 
1233 C CD2 . LEU A 166 ? 0.3260 0.1525 0.2767 -0.0061 0.0522  -0.0110 172 LEU A CD2 
1234 N N   . ILE A 167 ? 0.3865 0.1102 0.2829 0.0209  0.0213  -0.0025 173 ILE A N   
1235 C CA  . ILE A 167 ? 0.4317 0.1149 0.2998 0.0194  0.0192  0.0067  173 ILE A CA  
1236 C C   . ILE A 167 ? 0.4544 0.1336 0.3025 0.0187  0.0214  0.0158  173 ILE A C   
1237 O O   . ILE A 167 ? 0.4336 0.1273 0.2817 0.0315  0.0153  0.0154  173 ILE A O   
1238 C CB  . ILE A 167 ? 0.4447 0.1161 0.3097 0.0352  0.0071  0.0053  173 ILE A CB  
1239 C CG1 . ILE A 167 ? 0.4270 0.1116 0.3143 0.0345  0.0058  -0.0049 173 ILE A CG1 
1240 C CG2 . ILE A 167 ? 0.4906 0.1275 0.3298 0.0332  0.0040  0.0152  173 ILE A CG2 
1241 C CD1 . ILE A 167 ? 0.4344 0.1201 0.3268 0.0490  -0.0033 -0.0086 173 ILE A CD1 
1242 N N   . HIS A 168 ? 0.4750 0.1336 0.3047 0.0029  0.0302  0.0238  174 HIS A N   
1243 C CA  . HIS A 168 ? 0.4998 0.1556 0.3089 -0.0019 0.0355  0.0318  174 HIS A CA  
1244 C C   . HIS A 168 ? 0.5475 0.1568 0.3195 -0.0089 0.0362  0.0440  174 HIS A C   
1245 O O   . HIS A 168 ? 0.5655 0.1561 0.3358 -0.0211 0.0409  0.0452  174 HIS A O   
1246 C CB  . HIS A 168 ? 0.4669 0.1520 0.2930 -0.0176 0.0503  0.0280  174 HIS A CB  
1247 C CG  . HIS A 168 ? 0.5057 0.1920 0.3121 -0.0221 0.0571  0.0338  174 HIS A CG  
1248 N ND1 . HIS A 168 ? 0.5013 0.1865 0.2913 -0.0083 0.0479  0.0370  174 HIS A ND1 
1249 C CD2 . HIS A 168 ? 0.4915 0.1810 0.2920 -0.0390 0.0725  0.0363  174 HIS A CD2 
1250 C CE1 . HIS A 168 ? 0.5287 0.2143 0.3007 -0.0167 0.0569  0.0413  174 HIS A CE1 
1251 N NE2 . HIS A 168 ? 0.5600 0.2483 0.3380 -0.0352 0.0727  0.0408  174 HIS A NE2 
1252 N N   . SER A 169 ? 0.5842 0.1774 0.3274 -0.0013 0.0305  0.0528  175 SER A N   
1253 C CA  . SER A 169 ? 0.6486 0.2044 0.3579 -0.0048 0.0278  0.0640  175 SER A CA  
1254 C C   . SER A 169 ? 0.6571 0.2041 0.3497 -0.0277 0.0444  0.0700  175 SER A C   
1255 O O   . SER A 169 ? 0.6902 0.2115 0.3619 -0.0346 0.0446  0.0770  175 SER A O   
1256 C CB  . SER A 169 ? 0.6633 0.2091 0.3491 0.0126  0.0134  0.0702  175 SER A CB  
1257 O OG  . SER A 169 ? 0.6655 0.2237 0.3415 0.0119  0.0177  0.0720  175 SER A OG  
1258 N N   . GLN A 170 ? 0.6461 0.2154 0.3485 -0.0393 0.0587  0.0669  176 GLN A N   
1259 C CA  . GLN A 170 ? 0.6775 0.2479 0.3711 -0.0612 0.0765  0.0698  176 GLN A CA  
1260 C C   . GLN A 170 ? 0.6374 0.2251 0.3630 -0.0772 0.0879  0.0619  176 GLN A C   
1261 O O   . GLN A 170 ? 0.5938 0.1942 0.3473 -0.0718 0.0827  0.0539  176 GLN A O   
1262 C CB  . GLN A 170 ? 0.6550 0.2476 0.3448 -0.0638 0.0860  0.0687  176 GLN A CB  
1263 C CG  . GLN A 170 ? 0.6798 0.2680 0.3478 -0.0458 0.0719  0.0727  176 GLN A CG  
1264 C CD  . GLN A 170 ? 0.7771 0.3245 0.4044 -0.0423 0.0622  0.0847  176 GLN A CD  
1265 O OE1 . GLN A 170 ? 0.7995 0.3342 0.4194 -0.0236 0.0436  0.0872  176 GLN A OE1 
1266 N NE2 . GLN A 170 ? 0.7883 0.3229 0.3959 -0.0591 0.0739  0.0897  176 GLN A NE2 
1267 N N   . VAL A 171 ? 0.6488 0.2401 0.3716 -0.0969 0.1032  0.0632  177 VAL A N   
1268 C CA  . VAL A 171 ? 0.6598 0.2730 0.4160 -0.1126 0.1136  0.0549  177 VAL A CA  
1269 C C   . VAL A 171 ? 0.6266 0.2818 0.4151 -0.1169 0.1250  0.0453  177 VAL A C   
1270 O O   . VAL A 171 ? 0.6045 0.2841 0.4287 -0.1230 0.1278  0.0361  177 VAL A O   
1271 C CB  . VAL A 171 ? 0.7270 0.3273 0.4704 -0.1315 0.1242  0.0592  177 VAL A CB  
1272 C CG1 . VAL A 171 ? 0.6816 0.2900 0.4088 -0.1410 0.1387  0.0620  177 VAL A CG1 
1273 C CG2 . VAL A 171 ? 0.7094 0.3295 0.4879 -0.1457 0.1303  0.0506  177 VAL A CG2 
1274 N N   . ALA A 172 ? 0.6063 0.2714 0.3840 -0.1125 0.1301  0.0465  178 ALA A N   
1275 C CA  . ALA A 172 ? 0.5785 0.2886 0.3895 -0.1117 0.1380  0.0359  178 ALA A CA  
1276 C C   . ALA A 172 ? 0.5730 0.2999 0.3906 -0.0892 0.1235  0.0319  178 ALA A C   
1277 O O   . ALA A 172 ? 0.5876 0.2925 0.3767 -0.0771 0.1122  0.0387  178 ALA A O   
1278 C CB  . ALA A 172 ? 0.5770 0.2976 0.3781 -0.1244 0.1562  0.0362  178 ALA A CB  
1279 N N   . LEU A 173 ? 0.5348 0.3011 0.3906 -0.0843 0.1240  0.0208  179 LEU A N   
1280 C CA  . LEU A 173 ? 0.4867 0.2723 0.3548 -0.0654 0.1117  0.0154  179 LEU A CA  
1281 C C   . LEU A 173 ? 0.5044 0.3055 0.3655 -0.0626 0.1181  0.0134  179 LEU A C   
1282 O O   . LEU A 173 ? 0.5395 0.3486 0.3995 -0.0750 0.1342  0.0123  179 LEU A O   
1283 C CB  . LEU A 173 ? 0.4386 0.2544 0.3480 -0.0620 0.1084  0.0051  179 LEU A CB  
1284 C CG  . LEU A 173 ? 0.4443 0.2467 0.3616 -0.0634 0.1002  0.0050  179 LEU A CG  
1285 C CD1 . LEU A 173 ? 0.3869 0.2203 0.3433 -0.0644 0.0996  -0.0051 179 LEU A CD1 
1286 C CD2 . LEU A 173 ? 0.4682 0.2512 0.3704 -0.0471 0.0840  0.0080  179 LEU A CD2 
1287 N N   . ALA A 174 ? 0.4981 0.3041 0.3551 -0.0466 0.1059  0.0121  180 ALA A N   
1288 C CA  . ALA A 174 ? 0.4921 0.3137 0.3445 -0.0422 0.1092  0.0084  180 ALA A CA  
1289 C C   . ALA A 174 ? 0.5364 0.3371 0.3502 -0.0505 0.1177  0.0156  180 ALA A C   
1290 O O   . ALA A 174 ? 0.6015 0.3732 0.3901 -0.0592 0.1202  0.0248  180 ALA A O   
1291 C CB  . ALA A 174 ? 0.4444 0.3005 0.3316 -0.0452 0.1196  -0.0023 180 ALA A CB  
1292 N N   . ASP A 175 ? 0.5626 0.3758 0.3693 -0.0487 0.1225  0.0114  181 ASP A N   
1293 C CA  . ASP A 175 ? 0.6072 0.3986 0.3710 -0.0527 0.1257  0.0181  181 ASP A CA  
1294 C C   . ASP A 175 ? 0.6404 0.4140 0.3834 -0.0710 0.1432  0.0242  181 ASP A C   
1295 O O   . ASP A 175 ? 0.6117 0.4038 0.3776 -0.0825 0.1601  0.0181  181 ASP A O   
1296 C CB  . ASP A 175 ? 0.6366 0.4471 0.3995 -0.0492 0.1298  0.0101  181 ASP A CB  
1297 C CG  . ASP A 175 ? 0.6602 0.4720 0.4172 -0.0337 0.1109  0.0091  181 ASP A CG  
1298 O OD1 . ASP A 175 ? 0.6138 0.4417 0.4005 -0.0237 0.1008  0.0043  181 ASP A OD1 
1299 O OD2 . ASP A 175 ? 0.7193 0.5160 0.4414 -0.0321 0.1061  0.0132  181 ASP A OD2 
1300 N N   . LYS A 176 ? 0.6638 0.4011 0.3622 -0.0738 0.1391  0.0362  182 LYS A N   
1301 C CA  . LYS A 176 ? 0.7004 0.4174 0.3722 -0.0917 0.1552  0.0427  182 LYS A CA  
1302 C C   . LYS A 176 ? 0.7064 0.4487 0.3863 -0.0983 0.1694  0.0332  182 LYS A C   
1303 O O   . LYS A 176 ? 0.7084 0.4539 0.3924 -0.1117 0.1825  0.0319  182 LYS A O   
1304 C CB  . LYS A 176 ? 0.7388 0.4158 0.3626 -0.0888 0.1426  0.0558  182 LYS A CB  
1305 N N   . GLU A 177 ? 0.7220 0.4821 0.4049 -0.0888 0.1667  0.0259  183 GLU A N   
1306 C CA  . GLU A 177 ? 0.7295 0.5095 0.4177 -0.0934 0.1782  0.0170  183 GLU A CA  
1307 C C   . GLU A 177 ? 0.6530 0.4699 0.3909 -0.0965 0.1904  0.0045  183 GLU A C   
1308 O O   . GLU A 177 ? 0.6321 0.4646 0.3774 -0.1011 0.2010  -0.0026 183 GLU A O   
1309 C CB  . GLU A 177 ? 0.7341 0.5172 0.4058 -0.0822 0.1687  0.0134  183 GLU A CB  
1310 C CG  . GLU A 177 ? 0.8038 0.5534 0.4272 -0.0772 0.1534  0.0250  183 GLU A CG  
1311 N N   . LEU A 178 ? 0.5678 0.3981 0.3392 -0.0934 0.1881  0.0019  184 LEU A N   
1312 C CA  . LEU A 178 ? 0.5111 0.3775 0.3310 -0.0929 0.1950  -0.0101 184 LEU A CA  
1313 C C   . LEU A 178 ? 0.5363 0.4109 0.3707 -0.1068 0.2080  -0.0118 184 LEU A C   
1314 O O   . LEU A 178 ? 0.5365 0.3888 0.3505 -0.1177 0.2111  -0.0034 184 LEU A O   
1315 C CB  . LEU A 178 ? 0.4702 0.3475 0.3199 -0.0856 0.1874  -0.0121 184 LEU A CB  
1316 C CG  . LEU A 178 ? 0.4795 0.3575 0.3261 -0.0704 0.1747  -0.0136 184 LEU A CG  
1317 C CD1 . LEU A 178 ? 0.4683 0.3575 0.3483 -0.0621 0.1612  -0.0152 184 LEU A CD1 
1318 C CD2 . LEU A 178 ? 0.4498 0.3504 0.3104 -0.0631 0.1754  -0.0240 184 LEU A CD2 
1319 N N   . LEU A 179 ? 0.4841 0.3906 0.3547 -0.1056 0.2147  -0.0229 185 LEU A N   
1320 C CA  . LEU A 179 ? 0.4978 0.4190 0.3916 -0.1170 0.2257  -0.0264 185 LEU A CA  
1321 C C   . LEU A 179 ? 0.4764 0.3918 0.3827 -0.1229 0.2217  -0.0218 185 LEU A C   
1322 O O   . LEU A 179 ? 0.4331 0.3538 0.3569 -0.1144 0.2114  -0.0227 185 LEU A O   
1323 C CB  . LEU A 179 ? 0.4877 0.4453 0.4239 -0.1107 0.2286  -0.0388 185 LEU A CB  
1324 C CG  . LEU A 179 ? 0.4733 0.4421 0.4073 -0.1058 0.2344  -0.0459 185 LEU A CG  
1325 C CD1 . LEU A 179 ? 0.4192 0.4195 0.3967 -0.0950 0.2307  -0.0562 185 LEU A CD1 
1326 C CD2 . LEU A 179 ? 0.4894 0.4547 0.4087 -0.1192 0.2503  -0.0459 185 LEU A CD2 
1327 N N   . PRO A 180 ? 0.5113 0.4158 0.4096 -0.1377 0.2295  -0.0175 186 PRO A N   
1328 C CA  . PRO A 180 ? 0.5059 0.4048 0.4175 -0.1440 0.2250  -0.0140 186 PRO A CA  
1329 C C   . PRO A 180 ? 0.4741 0.4069 0.4356 -0.1385 0.2204  -0.0238 186 PRO A C   
1330 O O   . PRO A 180 ? 0.4776 0.4061 0.4495 -0.1358 0.2105  -0.0219 186 PRO A O   
1331 C CB  . PRO A 180 ? 0.5307 0.4198 0.4309 -0.1615 0.2368  -0.0108 186 PRO A CB  
1332 C CG  . PRO A 180 ? 0.5650 0.4380 0.4276 -0.1633 0.2441  -0.0071 186 PRO A CG  
1333 C CD  . PRO A 180 ? 0.5368 0.4324 0.4126 -0.1497 0.2428  -0.0156 186 PRO A CD  
1334 N N   . SER A 181 ? 0.4394 0.4046 0.4309 -0.1355 0.2262  -0.0341 187 SER A N   
1335 C CA  . SER A 181 ? 0.4208 0.4174 0.4578 -0.1281 0.2194  -0.0428 187 SER A CA  
1336 C C   . SER A 181 ? 0.3762 0.3719 0.4174 -0.1129 0.2057  -0.0429 187 SER A C   
1337 O O   . SER A 181 ? 0.3697 0.3771 0.4372 -0.1090 0.1965  -0.0456 187 SER A O   
1338 C CB  . SER A 181 ? 0.3899 0.4169 0.4526 -0.1247 0.2265  -0.0528 187 SER A CB  
1339 O OG  . SER A 181 ? 0.3967 0.4199 0.4421 -0.1153 0.2276  -0.0539 187 SER A OG  
1340 N N   . VAL A 182 ? 0.3635 0.3455 0.3785 -0.1046 0.2039  -0.0402 188 VAL A N   
1341 C CA  . VAL A 182 ? 0.3668 0.3474 0.3842 -0.0908 0.1918  -0.0402 188 VAL A CA  
1342 C C   . VAL A 182 ? 0.3522 0.3101 0.3569 -0.0941 0.1857  -0.0322 188 VAL A C   
1343 O O   . VAL A 182 ? 0.3309 0.2964 0.3556 -0.0870 0.1765  -0.0342 188 VAL A O   
1344 C CB  . VAL A 182 ? 0.3571 0.3286 0.3488 -0.0820 0.1908  -0.0395 188 VAL A CB  
1345 C CG1 . VAL A 182 ? 0.3165 0.2820 0.3050 -0.0696 0.1787  -0.0381 188 VAL A CG1 
1346 C CG2 . VAL A 182 ? 0.3426 0.3368 0.3521 -0.0764 0.1938  -0.0483 188 VAL A CG2 
1347 N N   . ARG A 183 ? 0.3981 0.3255 0.3676 -0.1042 0.1897  -0.0225 189 ARG A N   
1348 C CA  . ARG A 183 ? 0.4024 0.3013 0.3544 -0.1051 0.1806  -0.0136 189 ARG A CA  
1349 C C   . ARG A 183 ? 0.3698 0.2768 0.3510 -0.1123 0.1774  -0.0162 189 ARG A C   
1350 O O   . ARG A 183 ? 0.3923 0.2913 0.3776 -0.1038 0.1612  -0.0149 189 ARG A O   
1351 C CB  . ARG A 183 ? 0.4271 0.2874 0.3318 -0.1139 0.1844  -0.0017 189 ARG A CB  
1352 C CG  . ARG A 183 ? 0.4797 0.3303 0.3517 -0.1075 0.1859  0.0010  189 ARG A CG  
1353 C CD  . ARG A 183 ? 0.5391 0.3501 0.3634 -0.1140 0.1849  0.0133  189 ARG A CD  
1354 N NE  . ARG A 183 ? 0.5810 0.3629 0.3851 -0.1045 0.1673  0.0223  189 ARG A NE  
1355 C CZ  . ARG A 183 ? 0.6197 0.3614 0.3823 -0.1078 0.1632  0.0346  189 ARG A CZ  
1356 N NH1 . ARG A 183 ? 0.6510 0.3801 0.3907 -0.1197 0.1724  0.0386  189 ARG A NH1 
1357 N NH2 . ARG A 183 ? 0.6346 0.3555 0.3860 -0.0942 0.1435  0.0402  189 ARG A NH2 
1358 N N   . GLN A 184 ? 0.3763 0.3016 0.3776 -0.1231 0.1859  -0.0212 190 GLN A N   
1359 C CA  . GLN A 184 ? 0.3807 0.3180 0.4118 -0.1298 0.1815  -0.0252 190 GLN A CA  
1360 C C   . GLN A 184 ? 0.3568 0.3239 0.4260 -0.1181 0.1723  -0.0341 190 GLN A C   
1361 O O   . GLN A 184 ? 0.3121 0.2784 0.3961 -0.1185 0.1625  -0.0353 190 GLN A O   
1362 C CB  . GLN A 184 ? 0.4109 0.3636 0.4547 -0.1430 0.1921  -0.0289 190 GLN A CB  
1363 C CG  . GLN A 184 ? 0.4347 0.3978 0.5053 -0.1524 0.1876  -0.0325 190 GLN A CG  
1364 C CD  . GLN A 184 ? 0.4988 0.4295 0.5520 -0.1556 0.1773  -0.0256 190 GLN A CD  
1365 O OE1 . GLN A 184 ? 0.5588 0.4524 0.5732 -0.1574 0.1773  -0.0156 190 GLN A OE1 
1366 N NE2 . GLN A 184 ? 0.4540 0.3974 0.5347 -0.1552 0.1668  -0.0311 190 GLN A NE2 
1367 N N   . GLU A 185 ? 0.3234 0.3141 0.4063 -0.1070 0.1738  -0.0404 191 GLU A N   
1368 C CA  . GLU A 185 ? 0.3029 0.3192 0.4187 -0.0945 0.1634  -0.0480 191 GLU A CA  
1369 C C   . GLU A 185 ? 0.3285 0.3292 0.4327 -0.0829 0.1498  -0.0443 191 GLU A C   
1370 O O   . GLU A 185 ? 0.2632 0.2732 0.3869 -0.0763 0.1367  -0.0476 191 GLU A O   
1371 C CB  . GLU A 185 ? 0.2891 0.3276 0.4169 -0.0843 0.1657  -0.0544 191 GLU A CB  
1372 C CG  . GLU A 185 ? 0.3069 0.3704 0.4671 -0.0712 0.1538  -0.0615 191 GLU A CG  
1373 C CD  . GLU A 185 ? 0.3937 0.4767 0.5852 -0.0768 0.1492  -0.0661 191 GLU A CD  
1374 O OE1 . GLU A 185 ? 0.4038 0.4827 0.5946 -0.0917 0.1554  -0.0646 191 GLU A OE1 
1375 O OE2 . GLU A 185 ? 0.4025 0.5037 0.6178 -0.0662 0.1382  -0.0710 191 GLU A OE2 
1376 N N   . VAL A 186 ? 0.3171 0.2923 0.3854 -0.0779 0.1479  -0.0372 192 VAL A N   
1377 C CA  . VAL A 186 ? 0.2874 0.2473 0.3417 -0.0643 0.1309  -0.0337 192 VAL A CA  
1378 C C   . VAL A 186 ? 0.3075 0.2536 0.3632 -0.0681 0.1212  -0.0314 192 VAL A C   
1379 O O   . VAL A 186 ? 0.2800 0.2309 0.3472 -0.0589 0.1082  -0.0342 192 VAL A O   
1380 C CB  . VAL A 186 ? 0.3249 0.2601 0.3411 -0.0597 0.1300  -0.0264 192 VAL A CB  
1381 C CG1 . VAL A 186 ? 0.3004 0.2176 0.3032 -0.0483 0.1131  -0.0224 192 VAL A CG1 
1382 C CG2 . VAL A 186 ? 0.3065 0.2556 0.3219 -0.0522 0.1350  -0.0305 192 VAL A CG2 
1383 N N   . LYS A 187 ? 0.3110 0.2385 0.3535 -0.0826 0.1280  -0.0266 193 LYS A N   
1384 C CA  . LYS A 187 ? 0.3061 0.2173 0.3486 -0.0885 0.1202  -0.0251 193 LYS A CA  
1385 C C   . LYS A 187 ? 0.2985 0.2369 0.3784 -0.0904 0.1154  -0.0340 193 LYS A C   
1386 O O   . LYS A 187 ? 0.2696 0.2032 0.3536 -0.0846 0.1021  -0.0359 193 LYS A O   
1387 C CB  . LYS A 187 ? 0.3546 0.2423 0.3781 -0.1067 0.1315  -0.0189 193 LYS A CB  
1388 C CG  . LYS A 187 ? 0.3900 0.2486 0.4019 -0.1134 0.1240  -0.0153 193 LYS A CG  
1389 C CD  . LYS A 187 ? 0.4257 0.2630 0.4203 -0.1342 0.1384  -0.0094 193 LYS A CD  
1390 C CE  . LYS A 187 ? 0.5858 0.3809 0.5538 -0.1389 0.1316  -0.0024 193 LYS A CE  
1391 N NZ  . LYS A 187 ? 0.6100 0.4113 0.6006 -0.1420 0.1222  -0.0094 193 LYS A NZ  
1392 N N   . GLU A 188 ? 0.2706 0.2381 0.3783 -0.0986 0.1261  -0.0401 194 GLU A N   
1393 C CA  . GLU A 188 ? 0.2629 0.2573 0.4074 -0.1009 0.1202  -0.0486 194 GLU A CA  
1394 C C   . GLU A 188 ? 0.2789 0.2869 0.4351 -0.0827 0.1057  -0.0525 194 GLU A C   
1395 O O   . GLU A 188 ? 0.2459 0.2622 0.4187 -0.0815 0.0942  -0.0570 194 GLU A O   
1396 C CB  . GLU A 188 ? 0.2680 0.2935 0.4413 -0.1106 0.1337  -0.0548 194 GLU A CB  
1397 C CG  . GLU A 188 ? 0.3632 0.3802 0.5303 -0.1284 0.1409  -0.0527 194 GLU A CG  
1398 N N   . ILE A 189 ? 0.2233 0.2325 0.3694 -0.0695 0.1061  -0.0510 195 ILE A N   
1399 C CA  . ILE A 189 ? 0.2470 0.2658 0.4009 -0.0536 0.0935  -0.0539 195 ILE A CA  
1400 C C   . ILE A 189 ? 0.2615 0.2568 0.3946 -0.0473 0.0805  -0.0504 195 ILE A C   
1401 O O   . ILE A 189 ? 0.2261 0.2271 0.3687 -0.0411 0.0688  -0.0537 195 ILE A O   
1402 C CB  . ILE A 189 ? 0.2568 0.2826 0.4060 -0.0432 0.0986  -0.0541 195 ILE A CB  
1403 C CG1 . ILE A 189 ? 0.2521 0.3043 0.4266 -0.0472 0.1111  -0.0600 195 ILE A CG1 
1404 C CG2 . ILE A 189 ? 0.2454 0.2746 0.3965 -0.0280 0.0860  -0.0557 195 ILE A CG2 
1405 C CD1 . ILE A 189 ? 0.2523 0.3049 0.4148 -0.0413 0.1210  -0.0601 195 ILE A CD1 
1406 N N   . LEU A 190 ? 0.2713 0.2395 0.3751 -0.0481 0.0822  -0.0438 196 LEU A N   
1407 C CA  . LEU A 190 ? 0.2739 0.2209 0.3607 -0.0415 0.0706  -0.0416 196 LEU A CA  
1408 C C   . LEU A 190 ? 0.2700 0.2135 0.3665 -0.0493 0.0643  -0.0450 196 LEU A C   
1409 O O   . LEU A 190 ? 0.2498 0.1919 0.3475 -0.0422 0.0532  -0.0482 196 LEU A O   
1410 C CB  . LEU A 190 ? 0.2752 0.1933 0.3306 -0.0409 0.0728  -0.0340 196 LEU A CB  
1411 C CG  . LEU A 190 ? 0.2858 0.2055 0.3281 -0.0318 0.0756  -0.0312 196 LEU A CG  
1412 C CD1 . LEU A 190 ? 0.3072 0.1979 0.3181 -0.0320 0.0763  -0.0232 196 LEU A CD1 
1413 C CD2 . LEU A 190 ? 0.2591 0.1878 0.3057 -0.0174 0.0659  -0.0345 196 LEU A CD2 
1414 N N   . LEU A 191 ? 0.2756 0.2179 0.3789 -0.0650 0.0717  -0.0451 197 LEU A N   
1415 C CA  . LEU A 191 ? 0.2826 0.2214 0.3954 -0.0745 0.0656  -0.0493 197 LEU A CA  
1416 C C   . LEU A 191 ? 0.2629 0.2307 0.4044 -0.0709 0.0570  -0.0572 197 LEU A C   
1417 O O   . LEU A 191 ? 0.2495 0.2120 0.3909 -0.0692 0.0455  -0.0609 197 LEU A O   
1418 C CB  . LEU A 191 ? 0.2674 0.2011 0.3834 -0.0941 0.0768  -0.0481 197 LEU A CB  
1419 C CG  . LEU A 191 ? 0.2989 0.1944 0.3803 -0.0985 0.0821  -0.0392 197 LEU A CG  
1420 C CD1 . LEU A 191 ? 0.3251 0.2154 0.4066 -0.1192 0.0966  -0.0368 197 LEU A CD1 
1421 C CD2 . LEU A 191 ? 0.3132 0.1790 0.3767 -0.0943 0.0702  -0.0389 197 LEU A CD2 
1422 N N   . ARG A 192 ? 0.2319 0.2290 0.3964 -0.0689 0.0618  -0.0601 198 ARG A N   
1423 C CA  . ARG A 192 ? 0.2332 0.2563 0.4235 -0.0632 0.0518  -0.0668 198 ARG A CA  
1424 C C   . ARG A 192 ? 0.2454 0.2617 0.4228 -0.0475 0.0400  -0.0662 198 ARG A C   
1425 O O   . ARG A 192 ? 0.2518 0.2766 0.4389 -0.0444 0.0281  -0.0706 198 ARG A O   
1426 C CB  . ARG A 192 ? 0.2079 0.2617 0.4250 -0.0618 0.0597  -0.0699 198 ARG A CB  
1427 C CG  . ARG A 192 ? 0.2934 0.3652 0.5352 -0.0784 0.0695  -0.0741 198 ARG A CG  
1428 C CD  . ARG A 192 ? 0.2959 0.4031 0.5702 -0.0741 0.0750  -0.0796 198 ARG A CD  
1429 N NE  . ARG A 192 ? 0.2895 0.3942 0.5516 -0.0695 0.0887  -0.0763 198 ARG A NE  
1430 C CZ  . ARG A 192 ? 0.3432 0.4520 0.6036 -0.0776 0.1023  -0.0757 198 ARG A CZ  
1431 N NH1 . ARG A 192 ? 0.3737 0.4912 0.6460 -0.0907 0.1051  -0.0779 198 ARG A NH1 
1432 N NH2 . ARG A 192 ? 0.3396 0.4436 0.5850 -0.0729 0.1129  -0.0731 198 ARG A NH2 
1433 N N   . LYS A 193 ? 0.2316 0.2332 0.3868 -0.0381 0.0429  -0.0612 199 LYS A N   
1434 C CA  . LYS A 193 ? 0.2531 0.2476 0.3953 -0.0251 0.0334  -0.0609 199 LYS A CA  
1435 C C   . LYS A 193 ? 0.2719 0.2439 0.3964 -0.0259 0.0259  -0.0614 199 LYS A C   
1436 O O   . LYS A 193 ? 0.2891 0.2565 0.4040 -0.0166 0.0185  -0.0626 199 LYS A O   
1437 C CB  . LYS A 193 ? 0.2094 0.1980 0.3363 -0.0157 0.0387  -0.0566 199 LYS A CB  
1438 C CG  . LYS A 193 ? 0.2198 0.2285 0.3608 -0.0106 0.0437  -0.0576 199 LYS A CG  
1439 C CD  . LYS A 193 ? 0.2417 0.2429 0.3657 -0.0015 0.0464  -0.0544 199 LYS A CD  
1440 C CE  . LYS A 193 ? 0.1889 0.2060 0.3242 0.0024  0.0529  -0.0559 199 LYS A CE  
1441 N NZ  . LYS A 193 ? 0.1359 0.1658 0.2852 0.0100  0.0458  -0.0591 199 LYS A NZ  
1442 N N   . GLY A 194 ? 0.2603 0.2169 0.3793 -0.0370 0.0285  -0.0609 200 GLY A N   
1443 C CA  . GLY A 194 ? 0.2891 0.2219 0.3912 -0.0375 0.0217  -0.0624 200 GLY A CA  
1444 C C   . GLY A 194 ? 0.2803 0.1869 0.3569 -0.0312 0.0243  -0.0574 200 GLY A C   
1445 O O   . GLY A 194 ? 0.3055 0.1924 0.3677 -0.0278 0.0186  -0.0594 200 GLY A O   
1446 N N   . VAL A 195 ? 0.2834 0.1893 0.3537 -0.0286 0.0323  -0.0515 201 VAL A N   
1447 C CA  . VAL A 195 ? 0.2574 0.1385 0.3039 -0.0226 0.0333  -0.0463 201 VAL A CA  
1448 C C   . VAL A 195 ? 0.3178 0.1728 0.3529 -0.0338 0.0355  -0.0438 201 VAL A C   
1449 O O   . VAL A 195 ? 0.3221 0.1810 0.3656 -0.0479 0.0423  -0.0428 201 VAL A O   
1450 C CB  . VAL A 195 ? 0.2815 0.1694 0.3232 -0.0180 0.0402  -0.0410 201 VAL A CB  
1451 C CG1 . VAL A 195 ? 0.2904 0.1542 0.3078 -0.0109 0.0391  -0.0354 201 VAL A CG1 
1452 C CG2 . VAL A 195 ? 0.2583 0.1695 0.3112 -0.0085 0.0382  -0.0440 201 VAL A CG2 
1453 N N   . GLN A 196 ? 0.3071 0.1353 0.3239 -0.0281 0.0301  -0.0434 202 GLN A N   
1454 C CA  . GLN A 196 ? 0.3639 0.1606 0.3651 -0.0374 0.0319  -0.0400 202 GLN A CA  
1455 C C   . GLN A 196 ? 0.3889 0.1686 0.3703 -0.0349 0.0372  -0.0304 202 GLN A C   
1456 O O   . GLN A 196 ? 0.3683 0.1480 0.3407 -0.0204 0.0339  -0.0280 202 GLN A O   
1457 C CB  . GLN A 196 ? 0.4133 0.1860 0.4028 -0.0313 0.0234  -0.0446 202 GLN A CB  
1458 C CG  . GLN A 196 ? 0.4212 0.2080 0.4256 -0.0344 0.0174  -0.0545 202 GLN A CG  
1459 C CD  . GLN A 196 ? 0.6222 0.3827 0.6131 -0.0331 0.0103  -0.0593 202 GLN A CD  
1460 O OE1 . GLN A 196 ? 0.6013 0.3373 0.5800 -0.0384 0.0101  -0.0552 202 GLN A OE1 
1461 N NE2 . GLN A 196 ? 0.6060 0.3762 0.5988 -0.0252 0.0032  -0.0666 202 GLN A NE2 
1462 N N   . LEU A 197 ? 0.3996 0.1667 0.3745 -0.0499 0.0454  -0.0250 203 LEU A N   
1463 C CA  . LEU A 197 ? 0.4109 0.1619 0.3643 -0.0499 0.0513  -0.0152 203 LEU A CA  
1464 C C   . LEU A 197 ? 0.4571 0.1633 0.3831 -0.0531 0.0493  -0.0091 203 LEU A C   
1465 O O   . LEU A 197 ? 0.4859 0.1776 0.4123 -0.0679 0.0519  -0.0101 203 LEU A O   
1466 C CB  . LEU A 197 ? 0.3831 0.1518 0.3458 -0.0648 0.0643  -0.0131 203 LEU A CB  
1467 C CG  . LEU A 197 ? 0.3667 0.1777 0.3567 -0.0628 0.0678  -0.0189 203 LEU A CG  
1468 C CD1 . LEU A 197 ? 0.3861 0.2095 0.3828 -0.0781 0.0825  -0.0171 203 LEU A CD1 
1469 C CD2 . LEU A 197 ? 0.3172 0.1385 0.3023 -0.0454 0.0633  -0.0181 203 LEU A CD2 
1470 N N   . LEU A 198 ? 0.4767 0.1617 0.3799 -0.0390 0.0436  -0.0029 204 LEU A N   
1471 C CA  . LEU A 198 ? 0.5371 0.1853 0.4144 -0.0391 0.0400  0.0051  204 LEU A CA  
1472 C C   . LEU A 198 ? 0.5427 0.1772 0.3956 -0.0412 0.0458  0.0161  204 LEU A C   
1473 O O   . LEU A 198 ? 0.5301 0.1611 0.3703 -0.0256 0.0397  0.0198  204 LEU A O   
1474 C CB  . LEU A 198 ? 0.5397 0.1802 0.4138 -0.0193 0.0265  0.0026  204 LEU A CB  
1475 C CG  . LEU A 198 ? 0.5844 0.2199 0.4685 -0.0209 0.0212  -0.0045 204 LEU A CG  
1476 C CD1 . LEU A 198 ? 0.6396 0.2486 0.5107 -0.0365 0.0251  0.0011  204 LEU A CD1 
1477 C CD2 . LEU A 198 ? 0.5659 0.2279 0.4751 -0.0264 0.0224  -0.0153 204 LEU A CD2 
1478 N N   . LEU A 199 ? 0.5434 0.1724 0.3901 -0.0607 0.0575  0.0210  205 LEU A N   
1479 C CA  . LEU A 199 ? 0.5616 0.1800 0.3842 -0.0661 0.0654  0.0310  205 LEU A CA  
1480 C C   . LEU A 199 ? 0.6145 0.1968 0.4059 -0.0658 0.0607  0.0411  205 LEU A C   
1481 O O   . LEU A 199 ? 0.6175 0.1845 0.4096 -0.0682 0.0561  0.0401  205 LEU A O   
1482 C CB  . LEU A 199 ? 0.5538 0.1929 0.3897 -0.0873 0.0825  0.0294  205 LEU A CB  
1483 C CG  . LEU A 199 ? 0.5320 0.2167 0.4040 -0.0849 0.0854  0.0187  205 LEU A CG  
1484 C CD1 . LEU A 199 ? 0.5313 0.2415 0.4204 -0.1033 0.1020  0.0161  205 LEU A CD1 
1485 C CD2 . LEU A 199 ? 0.5050 0.2051 0.3744 -0.0654 0.0782  0.0187  205 LEU A CD2 
1486 N N   . SER A 200 ? 0.6158 0.1842 0.3788 -0.0627 0.0618  0.0506  206 SER A N   
1487 C CA  . SER A 200 ? 0.6847 0.2181 0.4146 -0.0600 0.0560  0.0609  206 SER A CA  
1488 C C   . SER A 200 ? 0.7001 0.2180 0.4291 -0.0409 0.0392  0.0598  206 SER A C   
1489 O O   . SER A 200 ? 0.7231 0.2139 0.4379 -0.0425 0.0355  0.0641  206 SER A O   
1490 C CB  . SER A 200 ? 0.6999 0.2184 0.4212 -0.0817 0.0671  0.0648  206 SER A CB  
1491 O OG  . SER A 200 ? 0.6946 0.2312 0.4181 -0.0984 0.0835  0.0651  206 SER A OG  
1492 N N   . GLU A 201 ? 0.6743 0.2106 0.4190 -0.0225 0.0296  0.0534  207 GLU A N   
1493 C CA  . GLU A 201 ? 0.6934 0.2231 0.4418 -0.0029 0.0147  0.0505  207 GLU A CA  
1494 C C   . GLU A 201 ? 0.6318 0.1755 0.3800 0.0172  0.0047  0.0500  207 GLU A C   
1495 O O   . GLU A 201 ? 0.5900 0.1587 0.3511 0.0183  0.0083  0.0456  207 GLU A O   
1496 C CB  . GLU A 201 ? 0.6458 0.1917 0.4245 -0.0018 0.0133  0.0387  207 GLU A CB  
1497 C CG  . GLU A 201 ? 0.7209 0.2605 0.5062 -0.0226 0.0226  0.0367  207 GLU A CG  
1498 C CD  . GLU A 201 ? 0.7817 0.3105 0.5756 -0.0189 0.0162  0.0309  207 GLU A CD  
1499 O OE1 . GLU A 201 ? 0.7501 0.2630 0.5340 -0.0033 0.0064  0.0327  207 GLU A OE1 
1500 O OE2 . GLU A 201 ? 0.7989 0.3359 0.6100 -0.0318 0.0209  0.0239  207 GLU A OE2 
1501 N N   . ARG A 202 ? 0.6498 0.1786 0.3850 0.0330  -0.0079 0.0538  208 ARG A N   
1502 C CA  . ARG A 202 ? 0.6573 0.2015 0.3947 0.0527  -0.0193 0.0525  208 ARG A CA  
1503 C C   . ARG A 202 ? 0.6527 0.2124 0.4153 0.0690  -0.0284 0.0428  208 ARG A C   
1504 O O   . ARG A 202 ? 0.6444 0.1852 0.4040 0.0724  -0.0326 0.0431  208 ARG A O   
1505 C CB  . ARG A 202 ? 0.6805 0.2002 0.3848 0.0585  -0.0273 0.0638  208 ARG A CB  
1506 C CG  . ARG A 202 ? 0.7043 0.2429 0.4104 0.0765  -0.0391 0.0626  208 ARG A CG  
1507 C CD  . ARG A 202 ? 0.7782 0.2947 0.4487 0.0792  -0.0463 0.0741  208 ARG A CD  
1508 N NE  . ARG A 202 ? 0.8029 0.3164 0.4527 0.0641  -0.0356 0.0802  208 ARG A NE  
1509 C CZ  . ARG A 202 ? 0.8042 0.3393 0.4556 0.0667  -0.0355 0.0783  208 ARG A CZ  
1510 N NH1 . ARG A 202 ? 0.7232 0.2862 0.3975 0.0837  -0.0461 0.0703  208 ARG A NH1 
1511 N NH2 . ARG A 202 ? 0.7969 0.3272 0.4273 0.0511  -0.0235 0.0840  208 ARG A NH2 
1512 N N   . VAL A 203 ? 0.5878 0.1820 0.3752 0.0781  -0.0302 0.0337  209 VAL A N   
1513 C CA  . VAL A 203 ? 0.5975 0.2105 0.4090 0.0926  -0.0372 0.0242  209 VAL A CA  
1514 C C   . VAL A 203 ? 0.6257 0.2287 0.4259 0.1089  -0.0500 0.0283  209 VAL A C   
1515 O O   . VAL A 203 ? 0.6039 0.2094 0.3918 0.1149  -0.0560 0.0333  209 VAL A O   
1516 C CB  . VAL A 203 ? 0.5263 0.1798 0.3656 0.0967  -0.0350 0.0140  209 VAL A CB  
1517 C CG1 . VAL A 203 ? 0.5103 0.1854 0.3713 0.1120  -0.0418 0.0054  209 VAL A CG1 
1518 C CG2 . VAL A 203 ? 0.4970 0.1604 0.3508 0.0823  -0.0239 0.0083  209 VAL A CG2 
1519 N N   . SER A 204 ? 0.6075 0.1989 0.4118 0.1165  -0.0545 0.0258  210 SER A N   
1520 C CA  . SER A 204 ? 0.6460 0.2194 0.4360 0.1305  -0.0664 0.0311  210 SER A CA  
1521 C C   . SER A 204 ? 0.6398 0.2372 0.4537 0.1488  -0.0742 0.0220  210 SER A C   
1522 O O   . SER A 204 ? 0.7036 0.2911 0.5088 0.1622  -0.0853 0.0256  210 SER A O   
1523 C CB  . SER A 204 ? 0.6935 0.2254 0.4624 0.1250  -0.0658 0.0377  210 SER A CB  
1524 O OG  . SER A 204 ? 0.6827 0.2156 0.4682 0.1190  -0.0587 0.0298  210 SER A OG  
1525 N N   . ASN A 205 ? 0.6152 0.2440 0.4585 0.1493  -0.0686 0.0105  211 ASN A N   
1526 C CA  . ASN A 205 ? 0.6169 0.2702 0.4834 0.1647  -0.0737 0.0015  211 ASN A CA  
1527 C C   . ASN A 205 ? 0.6018 0.2969 0.4891 0.1669  -0.0729 -0.0049 211 ASN A C   
1528 O O   . ASN A 205 ? 0.5848 0.3082 0.4974 0.1709  -0.0696 -0.0150 211 ASN A O   
1529 C CB  . ASN A 205 ? 0.5815 0.2337 0.4629 0.1646  -0.0676 -0.0070 211 ASN A CB  
1530 C CG  . ASN A 205 ? 0.6003 0.2690 0.4951 0.1502  -0.0555 -0.0134 211 ASN A CG  
1531 O OD1 . ASN A 205 ? 0.5407 0.2130 0.4303 0.1383  -0.0508 -0.0101 211 ASN A OD1 
1532 N ND2 . ASN A 205 ? 0.5529 0.2305 0.4641 0.1516  -0.0504 -0.0229 211 ASN A ND2 
1533 N N   . LEU A 206 ? 0.6174 0.3154 0.4927 0.1638  -0.0757 0.0009  212 LEU A N   
1534 C CA  . LEU A 206 ? 0.5729 0.3083 0.4664 0.1635  -0.0739 -0.0051 212 LEU A CA  
1535 C C   . LEU A 206 ? 0.5800 0.3439 0.4955 0.1774  -0.0809 -0.0128 212 LEU A C   
1536 O O   . LEU A 206 ? 0.5386 0.3364 0.4778 0.1757  -0.0756 -0.0216 212 LEU A O   
1537 C CB  . LEU A 206 ? 0.5735 0.3022 0.4464 0.1595  -0.0770 0.0029  212 LEU A CB  
1538 C CG  . LEU A 206 ? 0.5472 0.2626 0.4072 0.1434  -0.0662 0.0074  212 LEU A CG  
1539 C CD1 . LEU A 206 ? 0.6211 0.3309 0.4598 0.1412  -0.0690 0.0147  212 LEU A CD1 
1540 C CD2 . LEU A 206 ? 0.5379 0.2820 0.4243 0.1362  -0.0557 -0.0024 212 LEU A CD2 
1541 N N   . GLU A 207 ? 0.6015 0.3521 0.5094 0.1905  -0.0924 -0.0096 213 GLU A N   
1542 C CA  . GLU A 207 ? 0.6239 0.4019 0.5539 0.2042  -0.0995 -0.0173 213 GLU A CA  
1543 C C   . GLU A 207 ? 0.5930 0.3886 0.5486 0.2055  -0.0910 -0.0278 213 GLU A C   
1544 O O   . GLU A 207 ? 0.6185 0.4460 0.5979 0.2116  -0.0914 -0.0363 213 GLU A O   
1545 C CB  . GLU A 207 ? 0.6857 0.4430 0.6021 0.2187  -0.1141 -0.0115 213 GLU A CB  
1546 C CG  . GLU A 207 ? 0.7446 0.5108 0.6531 0.2247  -0.1265 -0.0077 213 GLU A CG  
1547 C CD  . GLU A 207 ? 0.8775 0.6071 0.7479 0.2197  -0.1313 0.0059  213 GLU A CD  
1548 O OE1 . GLU A 207 ? 0.9137 0.6182 0.7677 0.2076  -0.1218 0.0113  213 GLU A OE1 
1549 O OE2 . GLU A 207 ? 0.8606 0.5862 0.7170 0.2270  -0.1443 0.0112  213 GLU A OE2 
1550 N N   . GLU A 208 ? 0.5715 0.3462 0.5216 0.1994  -0.0832 -0.0275 214 GLU A N   
1551 C CA  . GLU A 208 ? 0.5277 0.3128 0.4968 0.2009  -0.0753 -0.0369 214 GLU A CA  
1552 C C   . GLU A 208 ? 0.5042 0.3098 0.4852 0.1869  -0.0620 -0.0426 214 GLU A C   
1553 O O   . GLU A 208 ? 0.5393 0.3508 0.5320 0.1857  -0.0541 -0.0498 214 GLU A O   
1554 C CB  . GLU A 208 ? 0.5600 0.3085 0.5153 0.2033  -0.0754 -0.0341 214 GLU A CB  
1555 N N   . LEU A 209 ? 0.4951 0.2432 0.4831 0.1273  -0.0679 -0.0475 215 LEU A N   
1556 C CA  . LEU A 209 ? 0.4755 0.2485 0.4756 0.1205  -0.0508 -0.0520 215 LEU A CA  
1557 C C   . LEU A 209 ? 0.4249 0.2260 0.4428 0.1224  -0.0533 -0.0552 215 LEU A C   
1558 O O   . LEU A 209 ? 0.4405 0.2338 0.4486 0.1242  -0.0652 -0.0523 215 LEU A O   
1559 C CB  . LEU A 209 ? 0.4800 0.2349 0.4537 0.1106  -0.0412 -0.0486 215 LEU A CB  
1560 C CG  . LEU A 209 ? 0.5064 0.2359 0.4626 0.1049  -0.0342 -0.0471 215 LEU A CG  
1561 C CD1 . LEU A 209 ? 0.5048 0.2193 0.4334 0.0952  -0.0264 -0.0446 215 LEU A CD1 
1562 C CD2 . LEU A 209 ? 0.4356 0.1840 0.4143 0.1034  -0.0211 -0.0542 215 LEU A CD2 
1563 N N   . PRO A 210 ? 0.4156 0.2479 0.4574 0.1213  -0.0428 -0.0611 216 PRO A N   
1564 C CA  . PRO A 210 ? 0.3856 0.2416 0.4393 0.1197  -0.0415 -0.0637 216 PRO A CA  
1565 C C   . PRO A 210 ? 0.3810 0.2284 0.4143 0.1123  -0.0339 -0.0606 216 PRO A C   
1566 O O   . PRO A 210 ? 0.3874 0.2304 0.4107 0.1063  -0.0210 -0.0600 216 PRO A O   
1567 C CB  . PRO A 210 ? 0.3775 0.2629 0.4534 0.1183  -0.0296 -0.0692 216 PRO A CB  
1568 C CG  . PRO A 210 ? 0.3706 0.2484 0.4488 0.1213  -0.0278 -0.0702 216 PRO A CG  
1569 C CD  . PRO A 210 ? 0.3692 0.2130 0.4230 0.1202  -0.0309 -0.0649 216 PRO A CD  
1570 N N   . LEU A 211 ? 0.3666 0.2116 0.3937 0.1128  -0.0424 -0.0594 217 LEU A N   
1571 C CA  . LEU A 211 ? 0.3577 0.1917 0.3623 0.1068  -0.0372 -0.0566 217 LEU A CA  
1572 C C   . LEU A 211 ? 0.3514 0.2087 0.3679 0.1040  -0.0305 -0.0603 217 LEU A C   
1573 O O   . LEU A 211 ? 0.3434 0.2173 0.3800 0.1074  -0.0369 -0.0640 217 LEU A O   
1574 C CB  . LEU A 211 ? 0.3578 0.1642 0.3376 0.1087  -0.0524 -0.0514 217 LEU A CB  
1575 C CG  . LEU A 211 ? 0.3979 0.1754 0.3587 0.1106  -0.0604 -0.0460 217 LEU A CG  
1576 C CD1 . LEU A 211 ? 0.4212 0.1708 0.3524 0.1111  -0.0751 -0.0398 217 LEU A CD1 
1577 C CD2 . LEU A 211 ? 0.4093 0.1761 0.3560 0.1040  -0.0456 -0.0450 217 LEU A CD2 
1578 N N   . ASN A 212 ? 0.3105 0.1686 0.3145 0.0976  -0.0178 -0.0597 218 ASN A N   
1579 C CA  . ASN A 212 ? 0.3084 0.1824 0.3166 0.0943  -0.0115 -0.0618 218 ASN A CA  
1580 C C   . ASN A 212 ? 0.2989 0.1994 0.3326 0.0949  -0.0064 -0.0656 218 ASN A C   
1581 O O   . ASN A 212 ? 0.3179 0.2297 0.3589 0.0941  -0.0064 -0.0682 218 ASN A O   
1582 C CB  . ASN A 212 ? 0.3422 0.2046 0.3397 0.0961  -0.0234 -0.0613 218 ASN A CB  
1583 C CG  . ASN A 212 ? 0.3368 0.1711 0.3023 0.0945  -0.0276 -0.0566 218 ASN A CG  
1584 O OD1 . ASN A 212 ? 0.3353 0.1642 0.2859 0.0900  -0.0170 -0.0551 218 ASN A OD1 
1585 N ND2 . ASN A 212 ? 0.3751 0.1916 0.3295 0.0977  -0.0433 -0.0545 218 ASN A ND2 
1586 N N   . GLU A 213 ? 0.2790 0.1881 0.3243 0.0958  -0.0018 -0.0662 219 GLU A N   
1587 C CA  . GLU A 213 ? 0.2708 0.2039 0.3361 0.0959  0.0027  -0.0696 219 GLU A CA  
1588 C C   . GLU A 213 ? 0.2729 0.2108 0.3356 0.0932  0.0138  -0.0681 219 GLU A C   
1589 O O   . GLU A 213 ? 0.2651 0.1912 0.3236 0.0948  0.0132  -0.0672 219 GLU A O   
1590 C CB  . GLU A 213 ? 0.3007 0.2420 0.3880 0.1023  -0.0093 -0.0740 219 GLU A CB  
1591 N N   . TYR A 214 ? 0.2696 0.2227 0.3333 0.0896  0.0225  -0.0678 220 TYR A N   
1592 C CA  . TYR A 214 ? 0.2481 0.2067 0.3086 0.0879  0.0301  -0.0665 220 TYR A CA  
1593 C C   . TYR A 214 ? 0.2974 0.2630 0.3743 0.0919  0.0265  -0.0704 220 TYR A C   
1594 O O   . TYR A 214 ? 0.2673 0.2447 0.3625 0.0946  0.0212  -0.0747 220 TYR A O   
1595 C CB  . TYR A 214 ? 0.2726 0.2439 0.3292 0.0843  0.0371  -0.0648 220 TYR A CB  
1596 C CG  . TYR A 214 ? 0.2719 0.2515 0.3290 0.0836  0.0416  -0.0646 220 TYR A CG  
1597 C CD1 . TYR A 214 ? 0.2627 0.2382 0.3098 0.0819  0.0445  -0.0641 220 TYR A CD1 
1598 C CD2 . TYR A 214 ? 0.2752 0.2698 0.3485 0.0846  0.0413  -0.0690 220 TYR A CD2 
1599 C CE1 . TYR A 214 ? 0.2682 0.2533 0.3212 0.0809  0.0464  -0.0678 220 TYR A CE1 
1600 C CE2 . TYR A 214 ? 0.2569 0.2598 0.3348 0.0836  0.0440  -0.0724 220 TYR A CE2 
1601 C CZ  . TYR A 214 ? 0.2472 0.2447 0.3147 0.0818  0.0462  -0.0717 220 TYR A CZ  
1602 O OH  . TYR A 214 ? 0.2912 0.2967 0.3637 0.0807  0.0484  -0.0758 220 TYR A OH  
1603 N N   . ARG A 215 ? 0.2609 0.2190 0.3320 0.0923  0.0292  -0.0698 221 ARG A N   
1604 C CA  . ARG A 215 ? 0.2740 0.2373 0.3576 0.0958  0.0276  -0.0736 221 ARG A CA  
1605 C C   . ARG A 215 ? 0.2702 0.2338 0.3438 0.0929  0.0349  -0.0728 221 ARG A C   
1606 O O   . ARG A 215 ? 0.2498 0.2044 0.3072 0.0898  0.0387  -0.0698 221 ARG A O   
1607 C CB  . ARG A 215 ? 0.2787 0.2258 0.3666 0.1017  0.0192  -0.0753 221 ARG A CB  
1608 C CG  . ARG A 215 ? 0.3182 0.2619 0.4141 0.1058  0.0080  -0.0758 221 ARG A CG  
1609 C CD  . ARG A 215 ? 0.3470 0.3123 0.4665 0.1092  0.0030  -0.0812 221 ARG A CD  
1610 N NE  . ARG A 215 ? 0.4110 0.3703 0.5419 0.1170  -0.0109 -0.0837 221 ARG A NE  
1611 C CZ  . ARG A 215 ? 0.4270 0.3871 0.5641 0.1197  -0.0215 -0.0846 221 ARG A CZ  
1612 N NH1 . ARG A 215 ? 0.4075 0.3735 0.5414 0.1149  -0.0190 -0.0838 221 ARG A NH1 
1613 N NH2 . ARG A 215 ? 0.4269 0.3806 0.5727 0.1278  -0.0361 -0.0865 221 ARG A NH2 
1614 N N   . GLU A 216 ? 0.2497 0.2252 0.3355 0.0940  0.0357  -0.0773 222 GLU A N   
1615 C CA  . GLU A 216 ? 0.2296 0.2078 0.3124 0.0915  0.0399  -0.0802 222 GLU A CA  
1616 C C   . GLU A 216 ? 0.2650 0.2231 0.3362 0.0927  0.0398  -0.0796 222 GLU A C   
1617 O O   . GLU A 216 ? 0.2370 0.1940 0.2996 0.0890  0.0433  -0.0804 222 GLU A O   
1618 C CB  . GLU A 216 ? 0.2575 0.2496 0.3562 0.0930  0.0403  -0.0866 222 GLU A CB  
1619 C CG  . GLU A 216 ? 0.2512 0.2623 0.3593 0.0909  0.0423  -0.0882 222 GLU A CG  
1620 N N   . TYR A 217 ? 0.2891 0.2307 0.3606 0.0976  0.0352  -0.0789 223 TYR A N   
1621 C CA  . TYR A 217 ? 0.3220 0.2402 0.3825 0.0983  0.0349  -0.0799 223 TYR A CA  
1622 C C   . TYR A 217 ? 0.3027 0.2000 0.3617 0.1019  0.0281  -0.0782 223 TYR A C   
1623 O O   . TYR A 217 ? 0.3141 0.2136 0.3873 0.1077  0.0205  -0.0793 223 TYR A O   
1624 C CB  . TYR A 217 ? 0.3218 0.2371 0.3878 0.1010  0.0352  -0.0849 223 TYR A CB  
1625 C CG  . TYR A 217 ? 0.3313 0.2182 0.3848 0.1013  0.0348  -0.0864 223 TYR A CG  
1626 C CD1 . TYR A 217 ? 0.3438 0.2079 0.3986 0.1067  0.0285  -0.0862 223 TYR A CD1 
1627 C CD2 . TYR A 217 ? 0.3237 0.2058 0.3643 0.0960  0.0394  -0.0886 223 TYR A CD2 
1628 C CE1 . TYR A 217 ? 0.3987 0.2310 0.4390 0.1056  0.0287  -0.0868 223 TYR A CE1 
1629 C CE2 . TYR A 217 ? 0.3663 0.2196 0.3939 0.0950  0.0388  -0.0913 223 TYR A CE2 
1630 C CZ  . TYR A 217 ? 0.3971 0.2223 0.4219 0.0993  0.0345  -0.0896 223 TYR A CZ  
1631 O OH  . TYR A 217 ? 0.4626 0.2521 0.4700 0.0968  0.0345  -0.0910 223 TYR A OH  
1632 N N   . ILE A 218 ? 0.3006 0.1775 0.3425 0.0985  0.0300  -0.0759 224 ILE A N   
1633 C CA  . ILE A 218 ? 0.3173 0.1691 0.3544 0.1000  0.0235  -0.0735 224 ILE A CA  
1634 C C   . ILE A 218 ? 0.3711 0.1948 0.3909 0.0952  0.0286  -0.0745 224 ILE A C   
1635 O O   . ILE A 218 ? 0.3322 0.1593 0.3378 0.0895  0.0352  -0.0757 224 ILE A O   
1636 C CB  . ILE A 218 ? 0.3341 0.1891 0.3684 0.0978  0.0210  -0.0701 224 ILE A CB  
1637 C CG1 . ILE A 218 ? 0.2901 0.1710 0.3405 0.1012  0.0166  -0.0702 224 ILE A CG1 
1638 C CG2 . ILE A 218 ? 0.3588 0.1864 0.3843 0.0990  0.0105  -0.0672 224 ILE A CG2 
1639 C CD1 . ILE A 218 ? 0.2808 0.1654 0.3265 0.0984  0.0154  -0.0676 224 ILE A CD1 
1640 N N   . LYS A 219 ? 0.3648 0.1632 0.3843 0.0972  0.0219  -0.0740 225 LYS A N   
1641 C CA  . LYS A 219 ? 0.4136 0.1840 0.4223 0.0898  0.0257  -0.0759 225 LYS A CA  
1642 C C   . LYS A 219 ? 0.4602 0.2089 0.4554 0.0877  0.0137  -0.0710 225 LYS A C   
1643 O O   . LYS A 219 ? 0.4526 0.1865 0.4410 0.0950  0.0004  -0.0648 225 LYS A O   
1644 C CB  . LYS A 219 ? 0.4327 0.1845 0.4418 0.0933  0.0230  -0.0776 225 LYS A CB  
1645 C CG  . LYS A 219 ? 0.4608 0.1840 0.4622 0.0838  0.0221  -0.0803 225 LYS A CG  
1646 C CD  . LYS A 219 ? 0.5669 0.2712 0.5688 0.0861  0.0223  -0.0826 225 LYS A CD  
1647 C CE  . LYS A 219 ? 0.6134 0.2812 0.5977 0.0900  0.0066  -0.0747 225 LYS A CE  
1648 N NZ  . LYS A 219 ? 0.6453 0.2886 0.6269 0.0893  0.0064  -0.0775 225 LYS A NZ  
1649 N N   . VAL A 220 ? 0.4370 0.1813 0.4181 0.0790  0.0170  -0.0728 226 VAL A N   
1650 C CA  . VAL A 220 ? 0.4543 0.1674 0.4001 0.0757  0.0111  -0.0640 226 VAL A CA  
1651 C C   . VAL A 220 ? 0.5057 0.1815 0.4257 0.0683  0.0122  -0.0613 226 VAL A C   
1652 O O   . VAL A 220 ? 0.5262 0.2048 0.4490 0.0614  0.0219  -0.0681 226 VAL A O   
1653 C CB  . VAL A 220 ? 0.4551 0.1811 0.3899 0.0699  0.0193  -0.0651 226 VAL A CB  
1654 C CG1 . VAL A 220 ? 0.4523 0.1440 0.3473 0.0645  0.0172  -0.0559 226 VAL A CG1 
1655 C CG2 . VAL A 220 ? 0.3828 0.1433 0.3423 0.0762  0.0176  -0.0670 226 VAL A CG2 
1656 N N   . GLN A 221 ? 0.5259 0.1669 0.4199 0.0692  0.0018  -0.0512 227 GLN A N   
1657 C CA  . GLN A 221 ? 0.5786 0.1798 0.4425 0.0602  0.0031  -0.0464 227 GLN A CA  
1658 C C   . GLN A 221 ? 0.6038 0.1762 0.4251 0.0503  0.0052  -0.0373 227 GLN A C   
1659 O O   . GLN A 221 ? 0.5846 0.1589 0.3977 0.0547  -0.0020 -0.0323 227 GLN A O   
1660 C CB  . GLN A 221 ? 0.6304 0.2110 0.4954 0.0689  -0.0109 -0.0417 227 GLN A CB  
1661 C CG  . GLN A 221 ? 0.6425 0.2478 0.5461 0.0782  -0.0112 -0.0503 227 GLN A CG  
1662 C CD  . GLN A 221 ? 0.7113 0.2910 0.6104 0.0854  -0.0223 -0.0463 227 GLN A CD  
1663 O OE1 . GLN A 221 ? 0.7858 0.3571 0.6911 0.0832  -0.0178 -0.0511 227 GLN A OE1 
1664 N NE2 . GLN A 221 ? 0.6975 0.2644 0.5851 0.0944  -0.0379 -0.0383 227 GLN A NE2 
1665 N N   . THR A 222 ? 0.6180 0.1635 0.4116 0.0355  0.0160  -0.0357 228 THR A N   
1666 C CA  . THR A 222 ? 0.6952 0.2085 0.4441 0.0235  0.0198  -0.0269 228 THR A CA  
1667 C C   . THR A 222 ? 0.7165 0.1868 0.4357 0.0178  0.0139  -0.0182 228 THR A C   
1668 O O   . THR A 222 ? 0.7168 0.1819 0.4495 0.0206  0.0108  -0.0208 228 THR A O   
1669 C CB  . THR A 222 ? 0.7032 0.2238 0.4410 0.0071  0.0421  -0.0330 228 THR A CB  
1670 O OG1 . THR A 222 ? 0.7141 0.2258 0.4505 -0.0053 0.0539  -0.0377 228 THR A OG1 
1671 C CG2 . THR A 222 ? 0.6267 0.1933 0.3979 0.0138  0.0485  -0.0432 228 THR A CG2 
1672 N N   . ASP A 223 ? 0.7493 0.1880 0.4259 0.0097  0.0126  -0.0083 229 ASP A N   
1673 C CA  . ASP A 223 ? 0.8223 0.2175 0.4639 0.0039  0.0063  0.0011  229 ASP A CA  
1674 C C   . ASP A 223 ? 0.8535 0.2315 0.4814 -0.0142 0.0229  -0.0016 229 ASP A C   
1675 O O   . ASP A 223 ? 0.8819 0.2246 0.4848 -0.0186 0.0180  0.0051  229 ASP A O   
1676 C CB  . ASP A 223 ? 0.8433 0.2114 0.4406 -0.0012 0.0015  0.0116  229 ASP A CB  
1677 C CG  . ASP A 223 ? 0.9185 0.2888 0.4937 -0.0186 0.0221  0.0095  229 ASP A CG  
1678 O OD1 . ASP A 223 ? 0.8881 0.2865 0.4870 -0.0241 0.0385  -0.0007 229 ASP A OD1 
1679 O OD2 . ASP A 223 ? 0.9742 0.3186 0.5080 -0.0267 0.0221  0.0172  229 ASP A OD2 
1680 N N   . LYS A 224 ? 0.8305 0.2329 0.4742 -0.0249 0.0423  -0.0117 230 LYS A N   
1681 C CA  . LYS A 224 ? 0.8450 0.2380 0.4830 -0.0424 0.0584  -0.0168 230 LYS A CA  
1682 C C   . LYS A 224 ? 0.8250 0.2399 0.5038 -0.0342 0.0566  -0.0267 230 LYS A C   
1683 O O   . LYS A 224 ? 0.8855 0.3004 0.5669 -0.0480 0.0703  -0.0336 230 LYS A O   
1684 C CB  . LYS A 224 ? 0.8328 0.2396 0.4617 -0.0618 0.0825  -0.0236 230 LYS A CB  
1685 C CG  . LYS A 224 ? 0.9386 0.3154 0.5190 -0.0762 0.0889  -0.0145 230 LYS A CG  
1686 C CD  . LYS A 224 ? 0.8851 0.2825 0.4623 -0.0928 0.1125  -0.0232 230 LYS A CD  
1687 C CE  . LYS A 224 ? 0.9811 0.3469 0.5085 -0.1128 0.1236  -0.0161 230 LYS A CE  
1688 N NZ  . LYS A 224 ? 0.9262 0.3144 0.4527 -0.1294 0.1478  -0.0262 230 LYS A NZ  
1689 N N   . GLY A 225 ? 0.7751 0.2095 0.4858 -0.0131 0.0405  -0.0284 231 GLY A N   
1690 C CA  . GLY A 225 ? 0.7542 0.2104 0.5031 -0.0048 0.0387  -0.0384 231 GLY A CA  
1691 C C   . GLY A 225 ? 0.6876 0.1896 0.4701 -0.0042 0.0502  -0.0517 231 GLY A C   
1692 O O   . GLY A 225 ? 0.7264 0.2482 0.5392 0.0015  0.0496  -0.0610 231 GLY A O   
1693 N N   . THR A 226 ? 0.6904 0.2105 0.4684 -0.0095 0.0605  -0.0533 232 THR A N   
1694 C CA  . THR A 226 ? 0.6515 0.2184 0.4627 -0.0061 0.0694  -0.0655 232 THR A CA  
1695 C C   . THR A 226 ? 0.6233 0.2177 0.4666 0.0150  0.0543  -0.0668 232 THR A C   
1696 O O   . THR A 226 ? 0.6366 0.2221 0.4736 0.0246  0.0415  -0.0585 232 THR A O   
1697 C CB  . THR A 226 ? 0.6249 0.2053 0.4240 -0.0161 0.0842  -0.0675 232 THR A CB  
1698 O OG1 . THR A 226 ? 0.6969 0.2456 0.4597 -0.0365 0.0966  -0.0639 232 THR A OG1 
1699 C CG2 . THR A 226 ? 0.5709 0.1984 0.4018 -0.0172 0.0966  -0.0815 232 THR A CG2 
1700 N N   . GLU A 227 ? 0.5473 0.1769 0.4248 0.0212  0.0561  -0.0776 233 GLU A N   
1701 C CA  . GLU A 227 ? 0.5292 0.1891 0.4394 0.0386  0.0441  -0.0808 233 GLU A CA  
1702 C C   . GLU A 227 ? 0.5044 0.2097 0.4348 0.0397  0.0524  -0.0888 233 GLU A C   
1703 O O   . GLU A 227 ? 0.4882 0.2089 0.4232 0.0314  0.0640  -0.0960 233 GLU A O   
1704 C CB  . GLU A 227 ? 0.5619 0.2207 0.4928 0.0464  0.0353  -0.0857 233 GLU A CB  
1705 C CG  . GLU A 227 ? 0.6141 0.2316 0.5291 0.0478  0.0258  -0.0771 233 GLU A CG  
1706 C CD  . GLU A 227 ? 0.6920 0.3059 0.6261 0.0528  0.0214  -0.0835 233 GLU A CD  
1707 O OE1 . GLU A 227 ? 0.7104 0.3301 0.6474 0.0460  0.0283  -0.0922 233 GLU A OE1 
1708 O OE2 . GLU A 227 ? 0.7443 0.3497 0.6881 0.0636  0.0124  -0.0794 233 GLU A OE2 
1709 N N   . VAL A 228 ? 0.4782 0.2055 0.4203 0.0491  0.0461  -0.0869 234 VAL A N   
1710 C CA  . VAL A 228 ? 0.4142 0.1831 0.3713 0.0510  0.0512  -0.0916 234 VAL A CA  
1711 C C   . VAL A 228 ? 0.3973 0.1909 0.3762 0.0653  0.0385  -0.0929 234 VAL A C   
1712 O O   . VAL A 228 ? 0.3897 0.1781 0.3763 0.0717  0.0286  -0.0896 234 VAL A O   
1713 C CB  . VAL A 228 ? 0.4605 0.2305 0.4023 0.0462  0.0574  -0.0874 234 VAL A CB  
1714 C CG1 . VAL A 228 ? 0.4069 0.2210 0.3659 0.0498  0.0593  -0.0908 234 VAL A CG1 
1715 C CG2 . VAL A 228 ? 0.4583 0.2034 0.3726 0.0309  0.0714  -0.0868 234 VAL A CG2 
1716 N N   . ALA A 229 ? 0.3613 0.1804 0.3483 0.0684  0.0414  -0.0962 235 ALA A N   
1717 C CA  . ALA A 229 ? 0.3711 0.2098 0.3632 0.0785  0.0384  -0.0919 235 ALA A CA  
1718 C C   . ALA A 229 ? 0.3439 0.2072 0.3370 0.0781  0.0407  -0.0883 235 ALA A C   
1719 O O   . ALA A 229 ? 0.3542 0.2324 0.3478 0.0713  0.0463  -0.0905 235 ALA A O   
1720 C CB  . ALA A 229 ? 0.3525 0.2073 0.3550 0.0779  0.0435  -0.0949 235 ALA A CB  
1721 N N   . THR A 230 ? 0.3118 0.1790 0.3061 0.0829  0.0389  -0.0809 236 THR A N   
1722 C CA  . THR A 230 ? 0.3036 0.1883 0.2969 0.0817  0.0400  -0.0765 236 THR A CA  
1723 C C   . THR A 230 ? 0.3018 0.1981 0.3077 0.0845  0.0419  -0.0713 236 THR A C   
1724 O O   . THR A 230 ? 0.2928 0.1851 0.3105 0.0886  0.0403  -0.0723 236 THR A O   
1725 C CB  . THR A 230 ? 0.3246 0.1977 0.3101 0.0802  0.0328  -0.0778 236 THR A CB  
1726 O OG1 . THR A 230 ? 0.2969 0.1876 0.2810 0.0792  0.0335  -0.0748 236 THR A OG1 
1727 C CG2 . THR A 230 ? 0.3001 0.1481 0.2947 0.0758  0.0428  -0.0700 236 THR A CG2 
1728 N N   . ASN A 231 ? 0.2667 0.1786 0.2725 0.0824  0.0436  -0.0674 237 ASN A N   
1729 C CA  . ASN A 231 ? 0.2634 0.1870 0.2820 0.0842  0.0434  -0.0652 237 ASN A CA  
1730 C C   . ASN A 231 ? 0.2513 0.1672 0.2719 0.0844  0.0406  -0.0635 237 ASN A C   
1731 O O   . ASN A 231 ? 0.2510 0.1767 0.2851 0.0867  0.0365  -0.0640 237 ASN A O   
1732 C CB  . ASN A 231 ? 0.2539 0.1973 0.2742 0.0816  0.0464  -0.0640 237 ASN A CB  
1733 C CG  . ASN A 231 ? 0.2724 0.2280 0.2998 0.0803  0.0482  -0.0685 237 ASN A CG  
1734 O OD1 . ASN A 231 ? 0.2553 0.2182 0.2786 0.0772  0.0507  -0.0692 237 ASN A OD1 
1735 N ND2 . ASN A 231 ? 0.2850 0.2432 0.3242 0.0823  0.0468  -0.0719 237 ASN A ND2 
1736 N N   . LEU A 232 ? 0.2485 0.1505 0.2587 0.0803  0.0413  -0.0627 238 LEU A N   
1737 C CA  . LEU A 232 ? 0.2479 0.1450 0.2626 0.0793  0.0376  -0.0631 238 LEU A CA  
1738 C C   . LEU A 232 ? 0.2622 0.1409 0.2723 0.0768  0.0334  -0.0670 238 LEU A C   
1739 O O   . LEU A 232 ? 0.2632 0.1455 0.2717 0.0711  0.0354  -0.0721 238 LEU A O   
1740 C CB  . LEU A 232 ? 0.2329 0.1434 0.2450 0.0744  0.0416  -0.0610 238 LEU A CB  
1741 C CG  . LEU A 232 ? 0.2519 0.1578 0.2645 0.0751  0.0356  -0.0631 238 LEU A CG  
1742 C CD1 . LEU A 232 ? 0.2629 0.1710 0.2831 0.0820  0.0265  -0.0623 238 LEU A CD1 
1743 C CD2 . LEU A 232 ? 0.2567 0.1754 0.2678 0.0690  0.0397  -0.0630 238 LEU A CD2 
1744 N N   . VAL A 233 ? 0.2797 0.1412 0.2817 0.0824  0.0209  -0.0644 239 VAL A N   
1745 C CA  . VAL A 233 ? 0.3058 0.1393 0.2827 0.0822  0.0141  -0.0621 239 VAL A CA  
1746 C C   . VAL A 233 ? 0.3203 0.1472 0.2812 0.0832  0.0080  -0.0586 239 VAL A C   
1747 O O   . VAL A 233 ? 0.3102 0.1408 0.2789 0.0879  -0.0010 -0.0571 239 VAL A O   
1748 C CB  . VAL A 233 ? 0.3322 0.1417 0.3035 0.0871  0.0037  -0.0587 239 VAL A CB  
1749 C CG1 . VAL A 233 ? 0.3659 0.1402 0.3017 0.0846  -0.0013 -0.0533 239 VAL A CG1 
1750 C CG2 . VAL A 233 ? 0.3289 0.1433 0.3157 0.0867  0.0099  -0.0625 239 VAL A CG2 
1751 N N   . ILE A 234 ? 0.3200 0.1371 0.2577 0.0786  0.0130  -0.0578 240 ILE A N   
1752 C CA  . ILE A 234 ? 0.3418 0.1478 0.2587 0.0786  0.0085  -0.0544 240 ILE A CA  
1753 C C   . ILE A 234 ? 0.3666 0.1366 0.2479 0.0764  0.0050  -0.0495 240 ILE A C   
1754 O O   . ILE A 234 ? 0.3774 0.1375 0.2445 0.0710  0.0145  -0.0503 240 ILE A O   
1755 C CB  . ILE A 234 ? 0.3275 0.1539 0.2460 0.0744  0.0184  -0.0574 240 ILE A CB  
1756 C CG1 . ILE A 234 ? 0.3169 0.1747 0.2667 0.0744  0.0218  -0.0609 240 ILE A CG1 
1757 C CG2 . ILE A 234 ? 0.3374 0.1492 0.2324 0.0744  0.0138  -0.0542 240 ILE A CG2 
1758 C CD1 . ILE A 234 ? 0.3004 0.1786 0.2537 0.0699  0.0293  -0.0632 240 ILE A CD1 
1759 N N   . LEU A 235 ? 0.3875 0.1375 0.2529 0.0794  -0.0083 -0.0446 241 LEU A N   
1760 C CA  . LEU A 235 ? 0.4347 0.1473 0.2628 0.0765  -0.0139 -0.0385 241 LEU A CA  
1761 C C   . LEU A 235 ? 0.4696 0.1728 0.2703 0.0719  -0.0090 -0.0382 241 LEU A C   
1762 O O   . LEU A 235 ? 0.4306 0.1405 0.2336 0.0745  -0.0154 -0.0386 241 LEU A O   
1763 C CB  . LEU A 235 ? 0.4728 0.1699 0.2993 0.0824  -0.0337 -0.0332 241 LEU A CB  
1764 C CG  . LEU A 235 ? 0.4481 0.1508 0.2984 0.0881  -0.0412 -0.0331 241 LEU A CG  
1765 C CD1 . LEU A 235 ? 0.4996 0.1763 0.3325 0.0920  -0.0603 -0.0263 241 LEU A CD1 
1766 C CD2 . LEU A 235 ? 0.4858 0.1838 0.3354 0.0838  -0.0293 -0.0343 241 LEU A CD2 
1767 N N   . CYS A 236 ? 0.4836 0.1710 0.2581 0.0645  0.0029  -0.0383 242 CYS A N   
1768 C CA  . CYS A 236 ? 0.4750 0.1472 0.2174 0.0597  0.0068  -0.0378 242 CYS A CA  
1769 C C   . CYS A 236 ? 0.5179 0.1547 0.2229 0.0522  0.0048  -0.0306 242 CYS A C   
1770 O O   . CYS A 236 ? 0.5327 0.1624 0.2158 0.0431  0.0187  -0.0320 242 CYS A O   
1771 C CB  . CYS A 236 ? 0.4679 0.1673 0.2187 0.0553  0.0246  -0.0443 242 CYS A CB  
1772 S SG  . CYS A 236 ? 0.4521 0.1977 0.2475 0.0613  0.0252  -0.0489 242 CYS A SG  
1773 N N   . THR A 237 ? 0.5403 0.1547 0.2372 0.0559  -0.0127 -0.0234 243 THR A N   
1774 C CA  . THR A 237 ? 0.5835 0.1609 0.2471 0.0502  -0.0164 -0.0155 243 THR A CA  
1775 C C   . THR A 237 ? 0.6209 0.1706 0.2432 0.0457  -0.0233 -0.0094 243 THR A C   
1776 O O   . THR A 237 ? 0.6657 0.1806 0.2539 0.0400  -0.0265 -0.0020 243 THR A O   
1777 C CB  . THR A 237 ? 0.5902 0.1585 0.2682 0.0584  -0.0328 -0.0111 243 THR A CB  
1778 O OG1 . THR A 237 ? 0.6326 0.2190 0.3337 0.0682  -0.0491 -0.0119 243 THR A OG1 
1779 C CG2 . THR A 237 ? 0.5804 0.1702 0.2911 0.0596  -0.0234 -0.0163 243 THR A CG2 
1780 N N   . GLY A 238 ? 0.6105 0.1720 0.2325 0.0478  -0.0262 -0.0123 244 GLY A N   
1781 C CA  . GLY A 238 ? 0.6457 0.1825 0.2273 0.0427  -0.0306 -0.0081 244 GLY A CA  
1782 C C   . GLY A 238 ? 0.6619 0.1989 0.2472 0.0503  -0.0508 -0.0068 244 GLY A C   
1783 O O   . GLY A 238 ? 0.6286 0.1837 0.2476 0.0590  -0.0622 -0.0084 244 GLY A O   
1784 N N   . ILE A 239 ? 0.6926 0.2096 0.2420 0.0460  -0.0548 -0.0045 245 ILE A N   
1785 C CA  . ILE A 239 ? 0.6793 0.1965 0.2290 0.0511  -0.0729 -0.0045 245 ILE A CA  
1786 C C   . ILE A 239 ? 0.7318 0.2103 0.2365 0.0486  -0.0878 0.0036  245 ILE A C   
1787 O O   . ILE A 239 ? 0.7655 0.2167 0.2354 0.0415  -0.0809 0.0091  245 ILE A O   
1788 C CB  . ILE A 239 ? 0.6896 0.2258 0.2437 0.0494  -0.0632 -0.0125 245 ILE A CB  
1789 C CG1 . ILE A 239 ? 0.7470 0.2678 0.2624 0.0404  -0.0474 -0.0139 245 ILE A CG1 
1790 C CG2 . ILE A 239 ? 0.6234 0.1961 0.2210 0.0532  -0.0509 -0.0199 245 ILE A CG2 
1791 C CD1 . ILE A 239 ? 0.7486 0.2852 0.2664 0.0405  -0.0389 -0.0224 245 ILE A CD1 
1792 N N   . LYS A 240 ? 0.7395 0.2154 0.2453 0.0542  -0.1090 0.0045  246 LYS A N   
1793 C CA  . LYS A 240 ? 0.7870 0.2312 0.2547 0.0530  -0.1264 0.0104  246 LYS A CA  
1794 C C   . LYS A 240 ? 0.7889 0.2373 0.2501 0.0527  -0.1350 0.0059  246 LYS A C   
1795 O O   . LYS A 240 ? 0.7543 0.2304 0.2500 0.0570  -0.1380 0.0000  246 LYS A O   
1796 C CB  . LYS A 240 ? 0.7950 0.2395 0.2812 0.0607  -0.1475 0.0130  246 LYS A CB  
1797 C CG  . LYS A 240 ? 0.9240 0.3548 0.4031 0.0589  -0.1421 0.0178  246 LYS A CG  
1798 C CD  . LYS A 240 ? 1.0033 0.4316 0.4956 0.0674  -0.1640 0.0199  246 LYS A CD  
1799 C CE  . LYS A 240 ? 1.0469 0.4532 0.5104 0.0671  -0.1822 0.0215  246 LYS A CE  
1800 N NZ  . LYS A 240 ? 1.0928 0.4907 0.5622 0.0754  -0.2025 0.0239  246 LYS A NZ  
1801 N N   . ILE A 241 ? 0.8651 0.2924 0.2924 0.0457  -0.1355 0.0062  247 ILE A N   
1802 C CA  . ILE A 241 ? 0.8369 0.2666 0.2612 0.0450  -0.1447 0.0020  247 ILE A CA  
1803 C C   . ILE A 241 ? 0.8235 0.2643 0.2736 0.0535  -0.1702 0.0013  247 ILE A C   
1804 O O   . ILE A 241 ? 0.8358 0.2711 0.2926 0.0587  -0.1845 0.0051  247 ILE A O   
1805 C CB  . ILE A 241 ? 0.8927 0.2960 0.2798 0.0375  -0.1436 0.0043  247 ILE A CB  
1806 C CG1 . ILE A 241 ? 0.9434 0.3398 0.3100 0.0284  -0.1175 0.0046  247 ILE A CG1 
1807 C CG2 . ILE A 241 ? 0.8920 0.2995 0.2787 0.0367  -0.1514 0.0000  247 ILE A CG2 
1808 C CD1 . ILE A 241 ? 0.8469 0.2688 0.2317 0.0274  -0.0992 -0.0018 247 ILE A CD1 
1809 N N   . ASN A 242 ? 0.8029 0.2620 0.2708 0.0547  -0.1754 -0.0045 248 ASN A N   
1810 C CA  . ASN A 242 ? 0.7931 0.2680 0.2900 0.0613  -0.1985 -0.0068 248 ASN A CA  
1811 C C   . ASN A 242 ? 0.8567 0.3169 0.3358 0.0587  -0.2139 -0.0073 248 ASN A C   
1812 O O   . ASN A 242 ? 0.8880 0.3542 0.3680 0.0550  -0.2165 -0.0121 248 ASN A O   
1813 C CB  . ASN A 242 ? 0.7517 0.2569 0.2818 0.0617  -0.1935 -0.0140 248 ASN A CB  
1814 C CG  . ASN A 242 ? 0.7343 0.2641 0.3059 0.0670  -0.2123 -0.0177 248 ASN A CG  
1815 O OD1 . ASN A 242 ? 0.8402 0.3602 0.4048 0.0712  -0.2359 -0.0157 248 ASN A OD1 
1816 N ND2 . ASN A 242 ? 0.7229 0.2855 0.3376 0.0669  -0.2023 -0.0237 248 ASN A ND2 
1817 N N   . SER A 243 ? 0.8729 0.3122 0.3341 0.0605  -0.2236 -0.0022 249 SER A N   
1818 C CA  . SER A 243 ? 0.9254 0.3475 0.3668 0.0595  -0.2399 -0.0015 249 SER A CA  
1819 C C   . SER A 243 ? 0.9173 0.3573 0.3898 0.0671  -0.2652 -0.0051 249 SER A C   
1820 O O   . SER A 243 ? 0.9377 0.3647 0.3974 0.0686  -0.2819 -0.0043 249 SER A O   
1821 C CB  . SER A 243 ? 0.9653 0.3564 0.3732 0.0584  -0.2399 0.0051  249 SER A CB  
1822 O OG  . SER A 243 ? 0.9409 0.3354 0.3666 0.0666  -0.2500 0.0078  249 SER A OG  
1823 N N   . SER A 244 ? 0.8694 0.3401 0.3830 0.0718  -0.2681 -0.0094 250 SER A N   
1824 C CA  . SER A 244 ? 0.8484 0.3420 0.3987 0.0792  -0.2908 -0.0140 250 SER A CA  
1825 C C   . SER A 244 ? 0.9013 0.3939 0.4452 0.0754  -0.3052 -0.0181 250 SER A C   
1826 O O   . SER A 244 ? 0.8970 0.3853 0.4418 0.0804  -0.3248 -0.0182 250 SER A O   
1827 C CB  . SER A 244 ? 0.8336 0.3622 0.4275 0.0817  -0.2870 -0.0191 250 SER A CB  
1828 O OG  . SER A 244 ? 0.9037 0.4609 0.5363 0.0852  -0.3058 -0.0264 250 SER A OG  
1829 N N   . ALA A 245 ? 0.9008 0.3961 0.4367 0.0664  -0.2950 -0.0216 251 ALA A N   
1830 C CA  . ALA A 245 ? 0.8754 0.3756 0.4127 0.0619  -0.3077 -0.0269 251 ALA A CA  
1831 C C   . ALA A 245 ? 0.9263 0.3970 0.4260 0.0610  -0.3163 -0.0230 251 ALA A C   
1832 O O   . ALA A 245 ? 0.9430 0.4184 0.4477 0.0609  -0.3341 -0.0267 251 ALA A O   
1833 C CB  . ALA A 245 ? 0.8570 0.3637 0.3919 0.0522  -0.2920 -0.0315 251 ALA A CB  
1834 N N   . TYR A 246 ? 0.9605 0.4017 0.4224 0.0594  -0.3038 -0.0161 252 TYR A N   
1835 C CA  . TYR A 246 ? 1.0007 0.4127 0.4225 0.0561  -0.3082 -0.0131 252 TYR A CA  
1836 C C   . TYR A 246 ? 1.0454 0.4313 0.4430 0.0609  -0.3144 -0.0061 252 TYR A C   
1837 O O   . TYR A 246 ? 1.0762 0.4360 0.4385 0.0583  -0.3194 -0.0033 252 TYR A O   
1838 C CB  . TYR A 246 ? 1.0003 0.3983 0.3926 0.0465  -0.2856 -0.0127 252 TYR A CB  
1839 C CG  . TYR A 246 ? 0.9844 0.3764 0.3671 0.0445  -0.2614 -0.0089 252 TYR A CG  
1840 C CD1 . TYR A 246 ? 1.0274 0.3931 0.3789 0.0434  -0.2549 -0.0024 252 TYR A CD1 
1841 C CD2 . TYR A 246 ? 0.9418 0.3545 0.3459 0.0428  -0.2449 -0.0123 252 TYR A CD2 
1842 C CE1 . TYR A 246 ? 1.0013 0.3634 0.3453 0.0404  -0.2328 0.0002  252 TYR A CE1 
1843 C CE2 . TYR A 246 ? 0.9281 0.3375 0.3247 0.0412  -0.2230 -0.0095 252 TYR A CE2 
1844 C CZ  . TYR A 246 ? 0.9896 0.3745 0.3569 0.0396  -0.2170 -0.0034 252 TYR A CZ  
1845 O OH  . TYR A 246 ? 0.9486 0.3314 0.3091 0.0367  -0.1951 -0.0013 252 TYR A OH  
1846 N N   . ARG A 247 ? 1.0300 0.4217 0.4451 0.0677  -0.3147 -0.0036 253 ARG A N   
1847 C CA  . ARG A 247 ? 1.0560 0.4196 0.4438 0.0701  -0.3147 0.0034  253 ARG A CA  
1848 C C   . ARG A 247 ? 1.1147 0.4573 0.4805 0.0738  -0.3362 0.0052  253 ARG A C   
1849 O O   . ARG A 247 ? 1.1464 0.4562 0.4687 0.0689  -0.3321 0.0104  253 ARG A O   
1850 C CB  . ARG A 247 ? 1.0255 0.4035 0.4430 0.0784  -0.3159 0.0044  253 ARG A CB  
1851 C CG  . ARG A 247 ? 1.0710 0.4206 0.4604 0.0787  -0.3098 0.0116  253 ARG A CG  
1852 N N   . LYS A 248 ? 1.0991 0.4610 0.4947 0.0822  -0.3593 0.0005  254 LYS A N   
1853 C CA  . LYS A 248 ? 1.1487 0.4918 0.5254 0.0876  -0.3815 0.0019  254 LYS A CA  
1854 C C   . LYS A 248 ? 1.2027 0.5270 0.5438 0.0792  -0.3816 0.0019  254 LYS A C   
1855 O O   . LYS A 248 ? 1.2322 0.5234 0.5324 0.0782  -0.3865 0.0069  254 LYS A O   
1856 C CB  . LYS A 248 ? 1.1492 0.5223 0.5702 0.0987  -0.4056 -0.0047 254 LYS A CB  
1857 C CG  . LYS A 248 ? 1.2225 0.5765 0.6281 0.1080  -0.4292 -0.0028 254 LYS A CG  
1858 C CD  . LYS A 248 ? 1.2082 0.5953 0.6591 0.1188  -0.4532 -0.0110 254 LYS A CD  
1859 C CE  . LYS A 248 ? 1.2106 0.5872 0.6634 0.1330  -0.4719 -0.0094 254 LYS A CE  
1860 N NZ  . LYS A 248 ? 1.3400 0.6736 0.7414 0.1342  -0.4833 -0.0031 254 LYS A NZ  
1861 N N   . ALA A 249 ? 1.1552 0.4993 0.5101 0.0726  -0.3753 -0.0037 255 ALA A N   
1862 C CA  . ALA A 249 ? 1.1850 0.5156 0.5115 0.0655  -0.3773 -0.0052 255 ALA A CA  
1863 C C   . ALA A 249 ? 1.2151 0.5113 0.4920 0.0571  -0.3584 0.0008  255 ALA A C   
1864 O O   . ALA A 249 ? 1.2703 0.5432 0.5123 0.0540  -0.3646 0.0023  255 ALA A O   
1865 C CB  . ALA A 249 ? 1.1486 0.5076 0.5012 0.0595  -0.3722 -0.0128 255 ALA A CB  
1866 N N   . PHE A 250 ? 1.1926 0.4864 0.4661 0.0531  -0.3352 0.0039  256 PHE A N   
1867 C CA  . PHE A 250 ? 1.2149 0.4832 0.4474 0.0437  -0.3138 0.0078  256 PHE A CA  
1868 C C   . PHE A 250 ? 1.2355 0.4802 0.4456 0.0436  -0.3059 0.0151  256 PHE A C   
1869 O O   . PHE A 250 ? 1.2455 0.4784 0.4336 0.0354  -0.2829 0.0175  256 PHE A O   
1870 C CB  . PHE A 250 ? 1.1740 0.4602 0.4186 0.0368  -0.2899 0.0039  256 PHE A CB  
1871 C CG  . PHE A 250 ? 1.1625 0.4649 0.4191 0.0342  -0.2938 -0.0030 256 PHE A CG  
1872 C CD1 . PHE A 250 ? 1.1260 0.4589 0.4246 0.0383  -0.3047 -0.0085 256 PHE A CD1 
1873 C CD2 . PHE A 250 ? 1.1894 0.4772 0.4155 0.0270  -0.2860 -0.0044 256 PHE A CD2 
1874 C CE1 . PHE A 250 ? 1.1191 0.4658 0.4277 0.0343  -0.3079 -0.0153 256 PHE A CE1 
1875 C CE2 . PHE A 250 ? 1.1809 0.4823 0.4172 0.0242  -0.2895 -0.0112 256 PHE A CE2 
1876 C CZ  . PHE A 250 ? 1.1455 0.4757 0.4226 0.0274  -0.3004 -0.0165 256 PHE A CZ  
1877 N N   . GLU A 251 ? 1.2775 0.4102 0.4438 -0.1004 -0.2108 0.0146  257 GLU A N   
1878 C CA  . GLU A 251 ? 1.2783 0.3638 0.4013 -0.1080 -0.2154 0.0251  257 GLU A CA  
1879 C C   . GLU A 251 ? 1.3654 0.4279 0.4568 -0.1263 -0.2059 0.0291  257 GLU A C   
1880 O O   . GLU A 251 ? 1.3737 0.4320 0.4532 -0.1387 -0.1950 0.0313  257 GLU A O   
1881 C CB  . GLU A 251 ? 1.2970 0.3511 0.4034 -0.0920 -0.2411 0.0239  257 GLU A CB  
1882 C CG  . GLU A 251 ? 1.3266 0.3605 0.4125 -0.0959 -0.2432 0.0262  257 GLU A CG  
1883 N N   . SER A 252 ? 1.3522 0.4006 0.4299 -0.1290 -0.2092 0.0296  258 SER A N   
1884 C CA  . SER A 252 ? 1.3738 0.3989 0.4201 -0.1474 -0.2004 0.0327  258 SER A CA  
1885 C C   . SER A 252 ? 1.3892 0.4438 0.4497 -0.1647 -0.1742 0.0326  258 SER A C   
1886 O O   . SER A 252 ? 1.4067 0.4456 0.4443 -0.1801 -0.1651 0.0346  258 SER A O   
1887 C CB  . SER A 252 ? 1.4055 0.4153 0.4390 -0.1471 -0.2075 0.0325  258 SER A CB  
1888 O OG  . SER A 252 ? 1.5115 0.5035 0.5176 -0.1668 -0.1963 0.0348  258 SER A OG  
1889 N N   . ARG A 253 ? 1.3565 0.4532 0.4543 -0.1623 -0.1623 0.0298  259 ARG A N   
1890 C CA  . ARG A 253 ? 1.3285 0.4534 0.4410 -0.1776 -0.1390 0.0285  259 ARG A CA  
1891 C C   . ARG A 253 ? 1.2831 0.4388 0.4221 -0.1776 -0.1278 0.0270  259 ARG A C   
1892 O O   . ARG A 253 ? 1.2240 0.4072 0.3820 -0.1855 -0.1117 0.0249  259 ARG A O   
1893 C CB  . ARG A 253 ? 1.2998 0.4460 0.4299 -0.1775 -0.1331 0.0257  259 ARG A CB  
1894 N N   . LEU A 254 ? 1.3024 0.4475 0.4368 -0.1704 -0.1371 0.0281  260 LEU A N   
1895 C CA  . LEU A 254 ? 1.2707 0.4408 0.4267 -0.1705 -0.1282 0.0268  260 LEU A CA  
1896 C C   . LEU A 254 ? 1.2856 0.4474 0.4242 -0.1861 -0.1164 0.0278  260 LEU A C   
1897 O O   . LEU A 254 ? 1.3266 0.4516 0.4293 -0.1919 -0.1229 0.0307  260 LEU A O   
1898 C CB  . LEU A 254 ? 1.2102 0.3746 0.3714 -0.1543 -0.1444 0.0267  260 LEU A CB  
1899 C CG  . LEU A 254 ? 1.2402 0.4244 0.4291 -0.1381 -0.1546 0.0213  260 LEU A CG  
1900 C CD1 . LEU A 254 ? 1.2410 0.4310 0.4452 -0.1229 -0.1676 0.0169  260 LEU A CD1 
1901 C CD2 . LEU A 254 ? 1.2007 0.4306 0.4271 -0.1412 -0.1386 0.0151  260 LEU A CD2 
1902 N N   . ALA A 255 ? 1.2116 0.4040 0.3723 -0.1935 -0.0998 0.0255  261 ALA A N   
1903 C CA  . ALA A 255 ? 1.2858 0.4731 0.4329 -0.2073 -0.0887 0.0255  261 ALA A CA  
1904 C C   . ALA A 255 ? 1.3187 0.4916 0.4565 -0.2007 -0.0985 0.0272  261 ALA A C   
1905 O O   . ALA A 255 ? 1.2959 0.4661 0.4412 -0.1852 -0.1131 0.0276  261 ALA A O   
1906 C CB  . ALA A 255 ? 1.1801 0.4032 0.3526 -0.2171 -0.0691 0.0217  261 ALA A CB  
1907 N N   . SER A 256 ? 1.3223 0.4846 0.4422 -0.2129 -0.0906 0.0276  262 SER A N   
1908 C CA  . SER A 256 ? 1.3114 0.4686 0.4288 -0.2081 -0.0958 0.0281  262 SER A CA  
1909 C C   . SER A 256 ? 1.3016 0.4978 0.4600 -0.1991 -0.0917 0.0251  262 SER A C   
1910 O O   . SER A 256 ? 1.2982 0.4903 0.4612 -0.1863 -0.1043 0.0255  262 SER A O   
1911 C CB  . SER A 256 ? 1.3177 0.4623 0.4122 -0.2245 -0.0849 0.0281  262 SER A CB  
1912 O OG  . SER A 256 ? 1.3692 0.5454 0.4845 -0.2366 -0.0648 0.0243  262 SER A OG  
1913 N N   . SER A 257 ? 1.2678 0.4946 0.4487 -0.2070 -0.0757 0.0222  263 SER A N   
1914 C CA  . SER A 257 ? 1.2127 0.4694 0.4237 -0.2023 -0.0712 0.0200  263 SER A CA  
1915 C C   . SER A 257 ? 1.1189 0.3759 0.3414 -0.1856 -0.0860 0.0208  263 SER A C   
1916 O O   . SER A 257 ? 1.1373 0.4167 0.3853 -0.1792 -0.0858 0.0171  263 SER A O   
1917 C CB  . SER A 257 ? 1.1697 0.4557 0.4017 -0.2108 -0.0554 0.0167  263 SER A CB  
1918 N N   . GLY A 258 ? 1.1483 0.3871 0.3599 -0.1775 -0.0988 0.0224  264 GLY A N   
1919 C CA  . GLY A 258 ? 1.1257 0.3782 0.3612 -0.1614 -0.1104 0.0183  264 GLY A CA  
1920 C C   . GLY A 258 ? 1.0742 0.3538 0.3338 -0.1615 -0.1030 0.0144  264 GLY A C   
1921 O O   . GLY A 258 ? 1.0147 0.3076 0.2946 -0.1488 -0.1119 0.0095  264 GLY A O   
1922 N N   . ALA A 259 ? 1.0847 0.3730 0.3422 -0.1757 -0.0870 0.0157  265 ALA A N   
1923 C CA  . ALA A 259 ? 1.0290 0.3408 0.3060 -0.1775 -0.0790 0.0118  265 ALA A CA  
1924 C C   . ALA A 259 ? 1.0897 0.3772 0.3442 -0.1778 -0.0858 0.0146  265 ALA A C   
1925 O O   . ALA A 259 ? 1.1161 0.3658 0.3367 -0.1788 -0.0955 0.0205  265 ALA A O   
1926 C CB  . ALA A 259 ? 1.0286 0.3558 0.3095 -0.1928 -0.0604 0.0110  265 ALA A CB  
1927 N N   . LEU A 260 ? 1.0307 0.3393 0.3037 -0.1770 -0.0811 0.0101  266 LEU A N   
1928 C CA  . LEU A 260 ? 1.0332 0.3234 0.2880 -0.1785 -0.0856 0.0115  266 LEU A CA  
1929 C C   . LEU A 260 ? 1.0475 0.3324 0.2864 -0.1969 -0.0701 0.0130  266 LEU A C   
1930 O O   . LEU A 260 ? 1.0188 0.3326 0.2792 -0.2030 -0.0561 0.0086  266 LEU A O   
1931 C CB  . LEU A 260 ? 1.0026 0.3195 0.2865 -0.1664 -0.0902 0.0046  266 LEU A CB  
1932 C CG  . LEU A 260 ? 0.9954 0.3218 0.2988 -0.1486 -0.1047 0.0007  266 LEU A CG  
1933 C CD1 . LEU A 260 ? 0.9377 0.3066 0.2822 -0.1423 -0.0989 -0.0067 266 LEU A CD1 
1934 C CD2 . LEU A 260 ? 1.0418 0.3511 0.3334 -0.1401 -0.1190 0.0000  266 LEU A CD2 
1935 N N   . ARG A 261 ? 1.0933 0.3411 0.2949 -0.2059 -0.0729 0.0184  267 ARG A N   
1936 C CA  . ARG A 261 ? 1.1055 0.3542 0.2975 -0.2228 -0.0581 0.0164  267 ARG A CA  
1937 C C   . ARG A 261 ? 1.0858 0.3542 0.2939 -0.2220 -0.0537 0.0116  267 ARG A C   
1938 O O   . ARG A 261 ? 1.0780 0.3504 0.2954 -0.2090 -0.0651 0.0096  267 ARG A O   
1939 C CB  . ARG A 261 ? 1.1559 0.3708 0.3137 -0.2305 -0.0624 0.0188  267 ARG A CB  
1940 C CG  . ARG A 261 ? 1.2163 0.4170 0.3614 -0.2315 -0.0655 0.0208  267 ARG A CG  
1941 C CD  . ARG A 261 ? 1.3048 0.4641 0.4067 -0.2437 -0.0686 0.0233  267 ARG A CD  
1942 N NE  . ARG A 261 ? 1.4155 0.5430 0.4934 -0.2376 -0.0835 0.0274  267 ARG A NE  
1943 C CZ  . ARG A 261 ? 1.4402 0.5369 0.4979 -0.2275 -0.1027 0.0307  267 ARG A CZ  
1944 N NH1 . ARG A 261 ? 1.3508 0.4436 0.4084 -0.2226 -0.1093 0.0305  267 ARG A NH1 
1945 N NH2 . ARG A 261 ? 1.4759 0.5444 0.5125 -0.2219 -0.1160 0.0337  267 ARG A NH2 
1946 N N   . VAL A 262 ? 1.0751 0.3620 0.2912 -0.2349 -0.0369 0.0072  268 VAL A N   
1947 C CA  . VAL A 262 ? 1.0856 0.4014 0.3253 -0.2331 -0.0307 -0.0003 268 VAL A CA  
1948 C C   . VAL A 262 ? 1.0873 0.4014 0.3141 -0.2525 -0.0144 -0.0031 268 VAL A C   
1949 O O   . VAL A 262 ? 1.0840 0.3871 0.2955 -0.2662 -0.0053 -0.0010 268 VAL A O   
1950 C CB  . VAL A 262 ? 1.0184 0.3768 0.3011 -0.2222 -0.0275 -0.0066 268 VAL A CB  
1951 C CG1 . VAL A 262 ? 0.9775 0.3415 0.2760 -0.2036 -0.0427 -0.0060 268 VAL A CG1 
1952 C CG2 . VAL A 262 ? 0.9854 0.3542 0.2751 -0.2295 -0.0175 -0.0069 268 VAL A CG2 
1953 N N   . ASN A 263 ? 1.0621 0.3879 0.2950 -0.2543 -0.0103 -0.0086 269 ASN A N   
1954 C CA  . ASN A 263 ? 1.0728 0.4046 0.3002 -0.2716 0.0061  -0.0139 269 ASN A CA  
1955 C C   . ASN A 263 ? 1.0501 0.4248 0.3156 -0.2693 0.0174  -0.0227 269 ASN A C   
1956 O O   . ASN A 263 ? 0.9945 0.3891 0.2859 -0.2561 0.0123  -0.0232 269 ASN A O   
1957 C CB  . ASN A 263 ? 1.0938 0.4167 0.3080 -0.2749 0.0050  -0.0161 269 ASN A CB  
1958 C CG  . ASN A 263 ? 1.0608 0.4146 0.3063 -0.2601 0.0014  -0.0224 269 ASN A CG  
1959 O OD1 . ASN A 263 ? 1.0144 0.3982 0.2926 -0.2496 0.0020  -0.0261 269 ASN A OD1 
1960 N ND2 . ASN A 263 ? 1.0709 0.4165 0.3054 -0.2597 -0.0028 -0.0235 269 ASN A ND2 
1961 N N   . GLU A 264 ? 1.0296 0.4189 0.2995 -0.2819 0.0322  -0.0305 270 GLU A N   
1962 C CA  . GLU A 264 ? 1.0084 0.4371 0.3140 -0.2793 0.0420  -0.0400 270 GLU A CA  
1963 C C   . GLU A 264 ? 0.9894 0.4452 0.3261 -0.2626 0.0359  -0.0450 270 GLU A C   
1964 O O   . GLU A 264 ? 0.9419 0.4285 0.3091 -0.2576 0.0409  -0.0523 270 GLU A O   
1965 C CB  . GLU A 264 ? 1.0046 0.4417 0.3067 -0.2973 0.0594  -0.0487 270 GLU A CB  
1966 C CG  . GLU A 264 ? 1.0653 0.5005 0.3591 -0.3026 0.0631  -0.0534 270 GLU A CG  
1967 C CD  . GLU A 264 ? 1.1261 0.5207 0.3766 -0.3165 0.0619  -0.0464 270 GLU A CD  
1968 O OE1 . GLU A 264 ? 1.1201 0.4850 0.3463 -0.3193 0.0553  -0.0366 270 GLU A OE1 
1969 O OE2 . GLU A 264 ? 1.1708 0.5621 0.4107 -0.3249 0.0674  -0.0508 270 GLU A OE2 
1970 N N   . HIS A 265 ? 0.9600 0.4041 0.2888 -0.2542 0.0251  -0.0415 271 HIS A N   
1971 C CA  . HIS A 265 ? 0.9411 0.4074 0.2965 -0.2384 0.0181  -0.0451 271 HIS A CA  
1972 C C   . HIS A 265 ? 0.9171 0.3828 0.2828 -0.2233 0.0046  -0.0394 271 HIS A C   
1973 O O   . HIS A 265 ? 0.8844 0.3669 0.2709 -0.2107 -0.0016 -0.0420 271 HIS A O   
1974 C CB  . HIS A 265 ? 0.9566 0.4137 0.2994 -0.2384 0.0149  -0.0462 271 HIS A CB  
1975 C CG  . HIS A 265 ? 0.9830 0.4333 0.3081 -0.2550 0.0272  -0.0505 271 HIS A CG  
1976 N ND1 . HIS A 265 ? 0.9893 0.4641 0.3317 -0.2618 0.0411  -0.0603 271 HIS A ND1 
1977 C CD2 . HIS A 265 ? 1.0419 0.4638 0.3336 -0.2662 0.0274  -0.0473 271 HIS A CD2 
1978 C CE1 . HIS A 265 ? 1.0245 0.4875 0.3456 -0.2772 0.0504  -0.0632 271 HIS A CE1 
1979 N NE2 . HIS A 265 ? 1.0237 0.4539 0.3129 -0.2807 0.0424  -0.0550 271 HIS A NE2 
1980 N N   . LEU A 266 ? 0.9241 0.3702 0.2746 -0.2248 0.0000  -0.0323 272 LEU A N   
1981 C CA  . LEU A 266 ? 0.9513 0.3970 0.3112 -0.2116 -0.0118 -0.0278 272 LEU A CA  
1982 C C   . LEU A 266 ? 0.9197 0.3505 0.2710 -0.2008 -0.0265 -0.0246 272 LEU A C   
1983 O O   . LEU A 266 ? 0.9030 0.3390 0.2673 -0.1884 -0.0364 -0.0232 272 LEU A O   
1984 C CB  . LEU A 266 ? 0.8653 0.3451 0.2619 -0.2024 -0.0098 -0.0330 272 LEU A CB  
1985 C CG  . LEU A 266 ? 0.8541 0.3492 0.2614 -0.2109 0.0023  -0.0367 272 LEU A CG  
1986 C CD1 . LEU A 266 ? 0.8142 0.3401 0.2558 -0.2009 0.0021  -0.0417 272 LEU A CD1 
1987 C CD2 . LEU A 266 ? 0.8722 0.3486 0.2618 -0.2171 0.0022  -0.0305 272 LEU A CD2 
1988 N N   . GLN A 267 ? 0.9475 0.3602 0.2770 -0.2056 -0.0283 -0.0239 273 GLN A N   
1989 C CA  . GLN A 267 ? 0.9646 0.3587 0.2811 -0.1965 -0.0433 -0.0208 273 GLN A CA  
1990 C C   . GLN A 267 ? 0.9963 0.3570 0.2858 -0.1979 -0.0518 -0.0130 273 GLN A C   
1991 O O   . GLN A 267 ? 1.0220 0.3637 0.2889 -0.2117 -0.0445 -0.0093 273 GLN A O   
1992 C CB  . GLN A 267 ? 1.0099 0.3933 0.3089 -0.2026 -0.0422 -0.0226 273 GLN A CB  
1993 C CG  . GLN A 267 ? 0.9613 0.3761 0.2841 -0.2036 -0.0316 -0.0309 273 GLN A CG  
1994 C CD  . GLN A 267 ? 1.0210 0.4247 0.3236 -0.2136 -0.0270 -0.0330 273 GLN A CD  
1995 O OE1 . GLN A 267 ? 1.0165 0.4042 0.2968 -0.2289 -0.0182 -0.0319 273 GLN A OE1 
1996 N NE2 . GLN A 267 ? 0.9824 0.3946 0.2921 -0.2059 -0.0327 -0.0366 273 GLN A NE2 
1997 N N   . VAL A 268 ? 0.9978 0.3501 0.2880 -0.1844 -0.0672 -0.0110 274 VAL A N   
1998 C CA  . VAL A 268 ? 1.0304 0.3490 0.2940 -0.1848 -0.0766 -0.0038 274 VAL A CA  
1999 C C   . VAL A 268 ? 1.1003 0.3815 0.3251 -0.1936 -0.0809 0.0005  274 VAL A C   
2000 O O   . VAL A 268 ? 1.0859 0.3681 0.3082 -0.1923 -0.0836 -0.0025 274 VAL A O   
2001 C CB  . VAL A 268 ? 1.0187 0.3401 0.2956 -0.1673 -0.0922 -0.0044 274 VAL A CB  
2002 C CG1 . VAL A 268 ? 1.0588 0.3408 0.3045 -0.1668 -0.1040 0.0027  274 VAL A CG1 
2003 C CG2 . VAL A 268 ? 0.9738 0.3292 0.2860 -0.1613 -0.0866 -0.0082 274 VAL A CG2 
2004 N N   . GLU A 269 ? 1.1358 0.3835 0.3290 -0.2042 -0.0805 0.0074  275 GLU A N   
2005 C CA  . GLU A 269 ? 1.1720 0.3795 0.3243 -0.2154 -0.0837 0.0121  275 GLU A CA  
2006 C C   . GLU A 269 ? 1.2168 0.4070 0.3589 -0.2027 -0.1027 0.0123  275 GLU A C   
2007 O O   . GLU A 269 ? 1.2425 0.4304 0.3925 -0.1871 -0.1174 0.0128  275 GLU A O   
2008 C CB  . GLU A 269 ? 1.2238 0.3946 0.3435 -0.2264 -0.0835 0.0200  275 GLU A CB  
2009 C CG  . GLU A 269 ? 1.3070 0.4335 0.3903 -0.2249 -0.0999 0.0247  275 GLU A CG  
2010 C CD  . GLU A 269 ? 1.3405 0.4443 0.4003 -0.2330 -0.0997 0.0267  275 GLU A CD  
2011 O OE1 . GLU A 269 ? 1.2813 0.4033 0.3501 -0.2443 -0.0833 0.0246  275 GLU A OE1 
2012 O OE2 . GLU A 269 ? 1.3465 0.4137 0.3783 -0.2281 -0.1163 0.0302  275 GLU A OE2 
2013 N N   . GLY A 270 ? 1.2372 0.4159 0.3619 -0.2098 -0.1022 0.0112  276 GLY A N   
2014 C CA  . GLY A 270 ? 1.2396 0.4051 0.3552 -0.1988 -0.1191 0.0101  276 GLY A CA  
2015 C C   . GLY A 270 ? 1.2059 0.4115 0.3581 -0.1846 -0.1213 0.0020  276 GLY A C   
2016 O O   . GLY A 270 ? 1.2011 0.4006 0.3486 -0.1754 -0.1347 -0.0002 276 GLY A O   
2017 N N   . HIS A 271 ? 1.1441 0.3896 0.3312 -0.1837 -0.1082 -0.0029 277 HIS A N   
2018 C CA  . HIS A 271 ? 1.1202 0.4031 0.3416 -0.1721 -0.1087 -0.0108 277 HIS A CA  
2019 C C   . HIS A 271 ? 1.1205 0.4313 0.3588 -0.1818 -0.0902 -0.0153 277 HIS A C   
2020 O O   . HIS A 271 ? 1.1415 0.4530 0.3770 -0.1938 -0.0769 -0.0137 277 HIS A O   
2021 C CB  . HIS A 271 ? 1.0649 0.3699 0.3171 -0.1568 -0.1150 -0.0133 277 HIS A CB  
2022 C CG  . HIS A 271 ? 1.1000 0.3844 0.3423 -0.1441 -0.1346 -0.0118 277 HIS A CG  
2023 N ND1 . HIS A 271 ? 1.1406 0.3960 0.3630 -0.1442 -0.1417 -0.0055 277 HIS A ND1 
2024 C CD2 . HIS A 271 ? 1.1250 0.4139 0.3749 -0.1306 -0.1491 -0.0167 277 HIS A CD2 
2025 C CE1 . HIS A 271 ? 1.1312 0.3740 0.3501 -0.1304 -0.1603 -0.0067 277 HIS A CE1 
2026 N NE2 . HIS A 271 ? 1.1104 0.3739 0.3463 -0.1221 -0.1649 -0.0138 277 HIS A NE2 
2027 N N   . SER A 272 ? 1.0560 0.3899 0.3117 -0.1767 -0.0895 -0.0218 278 SER A N   
2028 C CA  . SER A 272 ? 1.0275 0.3909 0.3042 -0.1826 -0.0738 -0.0273 278 SER A CA  
2029 C C   . SER A 272 ? 0.9826 0.3826 0.2987 -0.1702 -0.0735 -0.0331 278 SER A C   
2030 O O   . SER A 272 ? 0.9656 0.3903 0.3018 -0.1736 -0.0613 -0.0375 278 SER A O   
2031 C CB  . SER A 272 ? 1.0470 0.4066 0.3095 -0.1899 -0.0704 -0.0304 278 SER A CB  
2032 O OG  . SER A 272 ? 1.0752 0.4348 0.3385 -0.1788 -0.0838 -0.0327 278 SER A OG  
2033 N N   . ASN A 273 ? 0.9700 0.3734 0.2973 -0.1562 -0.0867 -0.0339 279 ASN A N   
2034 C CA  . ASN A 273 ? 0.9280 0.3643 0.2911 -0.1454 -0.0868 -0.0396 279 ASN A CA  
2035 C C   . ASN A 273 ? 0.9111 0.3518 0.2879 -0.1386 -0.0906 -0.0377 279 ASN A C   
2036 O O   . ASN A 273 ? 0.8811 0.3453 0.2849 -0.1291 -0.0930 -0.0423 279 ASN A O   
2037 C CB  . ASN A 273 ? 0.9273 0.3707 0.2966 -0.1354 -0.0975 -0.0448 279 ASN A CB  
2038 C CG  . ASN A 273 ? 0.9492 0.3729 0.3060 -0.1266 -0.1141 -0.0430 279 ASN A CG  
2039 O OD1 . ASN A 273 ? 0.9808 0.3743 0.3110 -0.1308 -0.1186 -0.0365 279 ASN A OD1 
2040 N ND2 . ASN A 273 ? 0.9340 0.3742 0.3096 -0.1146 -0.1233 -0.0493 279 ASN A ND2 
2041 N N   . VAL A 274 ? 0.9313 0.3494 0.2892 -0.1439 -0.0910 -0.0313 280 VAL A N   
2042 C CA  . VAL A 274 ? 0.9165 0.3385 0.2860 -0.1390 -0.0931 -0.0294 280 VAL A CA  
2043 C C   . VAL A 274 ? 0.9114 0.3352 0.2793 -0.1506 -0.0793 -0.0263 280 VAL A C   
2044 O O   . VAL A 274 ? 0.9400 0.3422 0.2821 -0.1625 -0.0741 -0.0221 280 VAL A O   
2045 C CB  . VAL A 274 ? 0.9459 0.3393 0.2951 -0.1334 -0.1077 -0.0252 280 VAL A CB  
2046 C CG1 . VAL A 274 ? 0.9310 0.3291 0.2918 -0.1297 -0.1083 -0.0236 280 VAL A CG1 
2047 C CG2 . VAL A 274 ? 0.9493 0.3448 0.3036 -0.1209 -0.1219 -0.0302 280 VAL A CG2 
2048 N N   . TYR A 275 ? 0.8765 0.3262 0.2717 -0.1478 -0.0733 -0.0288 281 TYR A N   
2049 C CA  . TYR A 275 ? 0.8678 0.3237 0.2660 -0.1572 -0.0611 -0.0273 281 TYR A CA  
2050 C C   . TYR A 275 ? 0.8579 0.3148 0.2637 -0.1528 -0.0645 -0.0249 281 TYR A C   
2051 O O   . TYR A 275 ? 0.8446 0.3091 0.2646 -0.1415 -0.0737 -0.0268 281 TYR A O   
2052 C CB  . TYR A 275 ? 0.8362 0.3227 0.2601 -0.1584 -0.0504 -0.0332 281 TYR A CB  
2053 C CG  . TYR A 275 ? 0.8447 0.3325 0.2627 -0.1631 -0.0458 -0.0367 281 TYR A CG  
2054 C CD1 . TYR A 275 ? 0.8454 0.3352 0.2656 -0.1558 -0.0533 -0.0394 281 TYR A CD1 
2055 C CD2 . TYR A 275 ? 0.8526 0.3410 0.2635 -0.1753 -0.0334 -0.0382 281 TYR A CD2 
2056 C CE1 . TYR A 275 ? 0.8544 0.3454 0.2683 -0.1606 -0.0488 -0.0428 281 TYR A CE1 
2057 C CE2 . TYR A 275 ? 0.8616 0.3517 0.2670 -0.1801 -0.0287 -0.0422 281 TYR A CE2 
2058 C CZ  . TYR A 275 ? 0.8632 0.3543 0.2698 -0.1727 -0.0364 -0.0441 281 TYR A CZ  
2059 O OH  . TYR A 275 ? 0.8721 0.3650 0.2727 -0.1778 -0.0315 -0.0483 281 TYR A OH  
2060 N N   . ALA A 276 ? 0.8652 0.3152 0.2617 -0.1624 -0.0566 -0.0215 282 ALA A N   
2061 C CA  . ALA A 276 ? 0.8536 0.3079 0.2587 -0.1601 -0.0572 -0.0198 282 ALA A CA  
2062 C C   . ALA A 276 ? 0.8317 0.3073 0.2526 -0.1675 -0.0437 -0.0223 282 ALA A C   
2063 O O   . ALA A 276 ? 0.8423 0.3155 0.2534 -0.1788 -0.0336 -0.0228 282 ALA A O   
2064 C CB  . ALA A 276 ? 0.8888 0.3103 0.2639 -0.1642 -0.0625 -0.0131 282 ALA A CB  
2065 N N   . ILE A 277 ? 0.8021 0.2992 0.2478 -0.1614 -0.0435 -0.0246 283 ILE A N   
2066 C CA  . ILE A 277 ? 0.7796 0.2987 0.2431 -0.1664 -0.0327 -0.0278 283 ILE A CA  
2067 C C   . ILE A 277 ? 0.7696 0.2930 0.2407 -0.1650 -0.0335 -0.0263 283 ILE A C   
2068 O O   . ILE A 277 ? 0.7688 0.2874 0.2416 -0.1570 -0.0426 -0.0248 283 ILE A O   
2069 C CB  . ILE A 277 ? 0.7500 0.2956 0.2399 -0.1604 -0.0309 -0.0337 283 ILE A CB  
2070 C CG1 . ILE A 277 ? 0.7302 0.2867 0.2380 -0.1487 -0.0395 -0.0348 283 ILE A CG1 
2071 C CG2 . ILE A 277 ? 0.7606 0.3024 0.2429 -0.1619 -0.0301 -0.0359 283 ILE A CG2 
2072 C CD1 . ILE A 277 ? 0.7026 0.2836 0.2349 -0.1438 -0.0374 -0.0400 283 ILE A CD1 
2073 N N   . GLY A 278 ? 0.7619 0.2958 0.2388 -0.1727 -0.0238 -0.0277 284 GLY A N   
2074 C CA  . GLY A 278 ? 0.7515 0.2915 0.2366 -0.1722 -0.0236 -0.0268 284 GLY A CA  
2075 C C   . GLY A 278 ? 0.7797 0.2940 0.2396 -0.1765 -0.0265 -0.0213 284 GLY A C   
2076 O O   . GLY A 278 ? 0.8093 0.3012 0.2434 -0.1841 -0.0250 -0.0180 284 GLY A O   
2077 N N   . ASP A 279 ? 0.7722 0.2885 0.2388 -0.1719 -0.0308 -0.0203 285 ASP A N   
2078 C CA  . ASP A 279 ? 0.7980 0.2913 0.2421 -0.1759 -0.0333 -0.0156 285 ASP A CA  
2079 C C   . ASP A 279 ? 0.8305 0.2935 0.2478 -0.1737 -0.0426 -0.0112 285 ASP A C   
2080 O O   . ASP A 279 ? 0.8759 0.3134 0.2651 -0.1814 -0.0421 -0.0065 285 ASP A O   
2081 C CB  . ASP A 279 ? 0.7836 0.2852 0.2416 -0.1693 -0.0380 -0.0166 285 ASP A CB  
2082 C CG  . ASP A 279 ? 0.7607 0.2850 0.2375 -0.1738 -0.0291 -0.0195 285 ASP A CG  
2083 O OD1 . ASP A 279 ? 0.7512 0.2889 0.2353 -0.1800 -0.0202 -0.0221 285 ASP A OD1 
2084 O OD2 . ASP A 279 ? 0.7531 0.2819 0.2377 -0.1710 -0.0315 -0.0200 285 ASP A OD2 
2085 N N   . CYS A 280 ? 0.8258 0.2898 0.2497 -0.1637 -0.0514 -0.0128 286 CYS A N   
2086 C CA  . CYS A 280 ? 0.8581 0.2927 0.2569 -0.1603 -0.0623 -0.0092 286 CYS A CA  
2087 C C   . CYS A 280 ? 0.8895 0.3049 0.2631 -0.1700 -0.0580 -0.0059 286 CYS A C   
2088 O O   . CYS A 280 ? 0.9330 0.3190 0.2804 -0.1692 -0.0668 -0.0018 286 CYS A O   
2089 C CB  . CYS A 280 ? 0.8457 0.2885 0.2603 -0.1462 -0.0738 -0.0133 286 CYS A CB  
2090 S SG  . CYS A 280 ? 0.8268 0.2888 0.2571 -0.1442 -0.0704 -0.0176 286 CYS A SG  
2091 N N   . ALA A 281 ? 0.8743 0.3046 0.2547 -0.1791 -0.0454 -0.0082 287 ALA A N   
2092 C CA  . ALA A 281 ? 0.9022 0.3145 0.2582 -0.1906 -0.0396 -0.0061 287 ALA A CA  
2093 C C   . ALA A 281 ? 0.9692 0.3608 0.2989 -0.2046 -0.0324 -0.0016 287 ALA A C   
2094 O O   . ALA A 281 ? 0.9217 0.3246 0.2603 -0.2079 -0.0265 -0.0025 287 ALA A O   
2095 C CB  . ALA A 281 ? 0.8801 0.3180 0.2551 -0.1948 -0.0288 -0.0122 287 ALA A CB  
2096 N N   . ASP A 282 ? 1.0150 0.3753 0.3109 -0.2137 -0.0327 0.0030  288 ASP A N   
2097 C CA  . ASP A 282 ? 1.0763 0.4128 0.3424 -0.2289 -0.0255 0.0077  288 ASP A CA  
2098 C C   . ASP A 282 ? 1.0993 0.4499 0.3683 -0.2445 -0.0082 0.0028  288 ASP A C   
2099 O O   . ASP A 282 ? 1.0891 0.4270 0.3410 -0.2539 -0.0040 0.0020  288 ASP A O   
2100 C CB  . ASP A 282 ? 1.0940 0.3956 0.3294 -0.2284 -0.0361 0.0117  288 ASP A CB  
2101 C CG  . ASP A 282 ? 1.2333 0.5215 0.4491 -0.2408 -0.0295 0.0115  288 ASP A CG  
2102 O OD1 . ASP A 282 ? 1.1484 0.4433 0.3697 -0.2412 -0.0271 0.0111  288 ASP A OD1 
2103 O OD2 . ASP A 282 ? 1.2251 0.4953 0.4190 -0.2508 -0.0267 0.0116  288 ASP A OD2 
2104 N N   . VAL A 283 ? 1.0313 0.4131 0.3271 -0.2458 0.0013  -0.0028 289 VAL A N   
2105 C CA  . VAL A 283 ? 1.0693 0.4670 0.3704 -0.2603 0.0178  -0.0090 289 VAL A CA  
2106 C C   . VAL A 283 ? 1.1282 0.5245 0.4223 -0.2699 0.0252  -0.0092 289 VAL A C   
2107 O O   . VAL A 283 ? 1.1317 0.5226 0.4251 -0.2631 0.0179  -0.0059 289 VAL A O   
2108 C CB  . VAL A 283 ? 1.0802 0.5188 0.4218 -0.2532 0.0223  -0.0183 289 VAL A CB  
2109 C CG1 . VAL A 283 ? 0.9995 0.4414 0.3474 -0.2457 0.0170  -0.0200 289 VAL A CG1 
2110 C CG2 . VAL A 283 ? 0.9935 0.4522 0.3615 -0.2405 0.0162  -0.0191 289 VAL A CG2 
2111 N N   . ARG A 284 ? 1.1831 0.5876 0.4754 -0.2851 0.0398  -0.0152 290 ARG A N   
2112 C CA  . ARG A 284 ? 1.1962 0.6025 0.4839 -0.2948 0.0476  -0.0180 290 ARG A CA  
2113 C C   . ARG A 284 ? 1.1339 0.5686 0.4475 -0.2939 0.0538  -0.0222 290 ARG A C   
2114 O O   . ARG A 284 ? 1.1818 0.6180 0.4936 -0.2987 0.0574  -0.0234 290 ARG A O   
2115 C CB  . ARG A 284 ? 1.1607 0.5639 0.4351 -0.3126 0.0610  -0.0236 290 ARG A CB  
2116 N N   . THR A 285 ? 1.1264 0.5872 0.4692 -0.2852 0.0531  -0.0265 291 THR A N   
2117 C CA  . THR A 285 ? 1.1175 0.6108 0.4942 -0.2790 0.0548  -0.0331 291 THR A CA  
2118 C C   . THR A 285 ? 1.1057 0.5937 0.4848 -0.2676 0.0437  -0.0270 291 THR A C   
2119 O O   . THR A 285 ? 1.1422 0.6053 0.5021 -0.2615 0.0333  -0.0190 291 THR A O   
2120 C CB  . THR A 285 ? 1.1094 0.6319 0.5190 -0.2691 0.0536  -0.0408 291 THR A CB  
2121 O OG1 . THR A 285 ? 1.1153 0.6269 0.5213 -0.2580 0.0427  -0.0358 291 THR A OG1 
2122 C CG2 . THR A 285 ? 1.0934 0.6284 0.5068 -0.2809 0.0665  -0.0502 291 THR A CG2 
2123 N N   . PRO A 286 ? 1.1347 0.6455 0.5373 -0.2644 0.0451  -0.0313 292 PRO A N   
2124 C CA  . PRO A 286 ? 1.0497 0.5581 0.4576 -0.2535 0.0350  -0.0267 292 PRO A CA  
2125 C C   . PRO A 286 ? 0.9546 0.4766 0.3860 -0.2371 0.0246  -0.0270 292 PRO A C   
2126 O O   . PRO A 286 ? 0.9354 0.4717 0.3818 -0.2339 0.0256  -0.0313 292 PRO A O   
2127 C CB  . PRO A 286 ? 1.0163 0.5457 0.4413 -0.2580 0.0418  -0.0322 292 PRO A CB  
2128 C CG  . PRO A 286 ? 0.9744 0.5304 0.4229 -0.2603 0.0492  -0.0416 292 PRO A CG  
2129 C CD  . PRO A 286 ? 1.0682 0.6096 0.4966 -0.2693 0.0549  -0.0415 292 PRO A CD  
2130 N N   . LYS A 287 ? 0.8995 0.4169 0.3336 -0.2273 0.0149  -0.0229 293 LYS A N   
2131 C CA  . LYS A 287 ? 0.8214 0.3482 0.2739 -0.2127 0.0049  -0.0228 293 LYS A CA  
2132 C C   . LYS A 287 ? 0.7535 0.3117 0.2388 -0.2080 0.0070  -0.0288 293 LYS A C   
2133 O O   . LYS A 287 ? 0.7426 0.3089 0.2376 -0.2063 0.0060  -0.0291 293 LYS A O   
2134 C CB  . LYS A 287 ? 0.9012 0.4110 0.3440 -0.2047 -0.0061 -0.0177 293 LYS A CB  
2135 C CG  . LYS A 287 ? 0.9397 0.4148 0.3475 -0.2086 -0.0102 -0.0116 293 LYS A CG  
2136 C CD  . LYS A 287 ? 0.9703 0.4361 0.3672 -0.2104 -0.0100 -0.0108 293 LYS A CD  
2137 C CE  . LYS A 287 ? 0.9796 0.4079 0.3381 -0.2159 -0.0140 -0.0042 293 LYS A CE  
2138 N NZ  . LYS A 287 ? 0.9434 0.3617 0.2906 -0.2181 -0.0140 -0.0034 293 LYS A NZ  
2139 N N   . MET A 288 ? 0.7371 0.3117 0.2386 -0.2055 0.0090  -0.0335 294 MET A N   
2140 C CA  . MET A 288 ? 0.7079 0.3100 0.2380 -0.2017 0.0107  -0.0396 294 MET A CA  
2141 C C   . MET A 288 ? 0.6882 0.3006 0.2344 -0.1904 0.0041  -0.0407 294 MET A C   
2142 O O   . MET A 288 ? 0.6958 0.3002 0.2344 -0.1884 0.0022  -0.0398 294 MET A O   
2143 C CB  . MET A 288 ? 0.7087 0.3232 0.2444 -0.2110 0.0208  -0.0469 294 MET A CB  
2144 C CG  . MET A 288 ? 0.7283 0.3352 0.2492 -0.2237 0.0289  -0.0472 294 MET A CG  
2145 S SD  . MET A 288 ? 0.8139 0.4352 0.3506 -0.2229 0.0284  -0.0488 294 MET A SD  
2146 C CE  . MET A 288 ? 0.7235 0.3762 0.2929 -0.2198 0.0304  -0.0596 294 MET A CE  
2147 N N   . ALA A 289 ? 0.2697 0.3157 0.2807 -0.0597 0.0464  -0.0247 295 ALA A N   
2148 C CA  . ALA A 289 ? 0.2630 0.3154 0.2839 -0.0530 0.0425  -0.0246 295 ALA A CA  
2149 C C   . ALA A 289 ? 0.2258 0.2807 0.2530 -0.0595 0.0538  -0.0366 295 ALA A C   
2150 O O   . ALA A 289 ? 0.1939 0.2458 0.2126 -0.0621 0.0526  -0.0369 295 ALA A O   
2151 C CB  . ALA A 289 ? 0.2492 0.3114 0.2941 -0.0394 0.0360  -0.0213 295 ALA A CB  
2152 N N   . TYR A 290 ? 0.2328 0.2957 0.2777 -0.0614 0.0642  -0.0487 296 TYR A N   
2153 C CA  . TYR A 290 ? 0.2438 0.3119 0.2989 -0.0650 0.0735  -0.0638 296 TYR A CA  
2154 C C   . TYR A 290 ? 0.2694 0.3300 0.2965 -0.0817 0.0827  -0.0676 296 TYR A C   
2155 O O   . TYR A 290 ? 0.3027 0.3629 0.3291 -0.0839 0.0858  -0.0749 296 TYR A O   
2156 C CB  . TYR A 290 ? 0.2490 0.3323 0.3344 -0.0614 0.0810  -0.0807 296 TYR A CB  
2157 C CG  . TYR A 290 ? 0.2819 0.3706 0.3604 -0.0761 0.0943  -0.0913 296 TYR A CG  
2158 C CD1 . TYR A 290 ? 0.2692 0.3557 0.3421 -0.0789 0.0932  -0.0851 296 TYR A CD1 
2159 C CD2 . TYR A 290 ? 0.2689 0.3595 0.3418 -0.0866 0.1040  -0.1069 296 TYR A CD2 
2160 C CE1 . TYR A 290 ? 0.2804 0.3650 0.3404 -0.0931 0.1022  -0.0940 296 TYR A CE1 
2161 C CE2 . TYR A 290 ? 0.2859 0.3763 0.3471 -0.1009 0.1128  -0.1162 296 TYR A CE2 
2162 C CZ  . TYR A 290 ? 0.3163 0.4030 0.3702 -0.1047 0.1122  -0.1097 296 TYR A CZ  
2163 O OH  . TYR A 290 ? 0.2983 0.3834 0.3383 -0.1216 0.1219  -0.1202 296 TYR A OH  
2164 N N   . LEU A 291 ? 0.2569 0.3072 0.2566 -0.0942 0.0857  -0.0623 297 LEU A N   
2165 C CA  . LEU A 291 ? 0.3311 0.3663 0.2943 -0.1112 0.0916  -0.0634 297 LEU A CA  
2166 C C   . LEU A 291 ? 0.3118 0.3349 0.2567 -0.1061 0.0778  -0.0526 297 LEU A C   
2167 O O   . LEU A 291 ? 0.3112 0.3279 0.2390 -0.1144 0.0814  -0.0574 297 LEU A O   
2168 C CB  . LEU A 291 ? 0.3097 0.3276 0.2399 -0.1266 0.0949  -0.0585 297 LEU A CB  
2169 C CG  . LEU A 291 ? 0.3800 0.4063 0.3230 -0.1332 0.1056  -0.0716 297 LEU A CG  
2170 C CD1 . LEU A 291 ? 0.4560 0.4582 0.3622 -0.1473 0.1041  -0.0638 297 LEU A CD1 
2171 C CD2 . LEU A 291 ? 0.4030 0.4370 0.3508 -0.1419 0.1170  -0.0906 297 LEU A CD2 
2172 N N   . ALA A 292 ? 0.2768 0.2995 0.2267 -0.0928 0.0621  -0.0403 298 ALA A N   
2173 C CA  . ALA A 292 ? 0.2545 0.2739 0.1957 -0.0873 0.0492  -0.0341 298 ALA A CA  
2174 C C   . ALA A 292 ? 0.2842 0.3125 0.2410 -0.0867 0.0543  -0.0421 298 ALA A C   
2175 O O   . ALA A 292 ? 0.2994 0.3213 0.2394 -0.0920 0.0520  -0.0437 298 ALA A O   
2176 C CB  . ALA A 292 ? 0.2547 0.2819 0.2095 -0.0731 0.0350  -0.0249 298 ALA A CB  
2177 N N   . GLY A 293 ? 0.2580 0.2979 0.2448 -0.0800 0.0595  -0.0477 299 GLY A N   
2178 C CA  . GLY A 293 ? 0.2680 0.3099 0.2665 -0.0788 0.0617  -0.0553 299 GLY A CA  
2179 C C   . GLY A 293 ? 0.3231 0.3624 0.3126 -0.0894 0.0736  -0.0688 299 GLY A C   
2180 O O   . GLY A 293 ? 0.3226 0.3582 0.3077 -0.0920 0.0732  -0.0732 299 GLY A O   
2181 N N   . LEU A 294 ? 0.3109 0.3531 0.2972 -0.0974 0.0852  -0.0768 300 LEU A N   
2182 C CA  . LEU A 294 ? 0.3354 0.3782 0.3113 -0.1104 0.0991  -0.0921 300 LEU A CA  
2183 C C   . LEU A 294 ? 0.3359 0.3613 0.2706 -0.1231 0.0973  -0.0858 300 LEU A C   
2184 O O   . LEU A 294 ? 0.4119 0.4346 0.3359 -0.1309 0.1035  -0.0955 300 LEU A O   
2185 C CB  . LEU A 294 ? 0.3290 0.3830 0.3122 -0.1194 0.1144  -0.1051 300 LEU A CB  
2186 C CG  . LEU A 294 ? 0.3825 0.4557 0.4084 -0.1069 0.1160  -0.1177 300 LEU A CG  
2187 C CD1 . LEU A 294 ? 0.3535 0.4320 0.3813 -0.1161 0.1229  -0.1284 300 LEU A CD1 
2188 C CD2 . LEU A 294 ? 0.3529 0.4342 0.4061 -0.0958 0.1150  -0.1335 300 LEU A CD2 
2189 N N   . HIS A 295 ? 0.3452 0.3566 0.2546 -0.1247 0.0873  -0.0711 301 HIS A N   
2190 C CA  . HIS A 295 ? 0.3699 0.3608 0.2395 -0.1326 0.0792  -0.0650 301 HIS A CA  
2191 C C   . HIS A 295 ? 0.3796 0.3748 0.2584 -0.1242 0.0689  -0.0642 301 HIS A C   
2192 O O   . HIS A 295 ? 0.3648 0.3496 0.2204 -0.1316 0.0676  -0.0676 301 HIS A O   
2193 C CB  . HIS A 295 ? 0.3855 0.3585 0.2292 -0.1310 0.0648  -0.0509 301 HIS A CB  
2194 C CG  . HIS A 295 ? 0.4465 0.4095 0.2744 -0.1423 0.0738  -0.0502 301 HIS A CG  
2195 N ND1 . HIS A 295 ? 0.4630 0.4118 0.2769 -0.1382 0.0613  -0.0384 301 HIS A ND1 
2196 C CD2 . HIS A 295 ? 0.4933 0.4594 0.3189 -0.1581 0.0935  -0.0617 301 HIS A CD2 
2197 C CE1 . HIS A 295 ? 0.5190 0.4593 0.3184 -0.1530 0.0738  -0.0409 301 HIS A CE1 
2198 N NE2 . HIS A 295 ? 0.5077 0.4605 0.3196 -0.1638 0.0917  -0.0556 301 HIS A NE2 
2199 N N   . ALA A 296 ? 0.3319 0.3414 0.2421 -0.1105 0.0619  -0.0602 302 ALA A N   
2200 C CA  . ALA A 296 ? 0.3361 0.3505 0.2554 -0.1059 0.0538  -0.0602 302 ALA A CA  
2201 C C   . ALA A 296 ? 0.3661 0.3799 0.2891 -0.1116 0.0634  -0.0726 302 ALA A C   
2202 O O   . ALA A 296 ? 0.3492 0.3580 0.2590 -0.1160 0.0592  -0.0750 302 ALA A O   
2203 C CB  . ALA A 296 ? 0.2533 0.2804 0.2014 -0.0947 0.0480  -0.0546 302 ALA A CB  
2204 N N   . ASN A 297 ? 0.3825 0.4022 0.3252 -0.1103 0.0748  -0.0826 303 ASN A N   
2205 C CA  . ASN A 297 ? 0.3813 0.4007 0.3289 -0.1140 0.0828  -0.0977 303 ASN A CA  
2206 C C   . ASN A 297 ? 0.3947 0.4060 0.3106 -0.1282 0.0899  -0.1039 303 ASN A C   
2207 O O   . ASN A 297 ? 0.4013 0.4078 0.3094 -0.1320 0.0896  -0.1106 303 ASN A O   
2208 C CB  . ASN A 297 ? 0.3913 0.4209 0.3664 -0.1087 0.0924  -0.1119 303 ASN A CB  
2209 C CG  . ASN A 297 ? 0.4827 0.5137 0.4849 -0.0940 0.0832  -0.1072 303 ASN A CG  
2210 O OD1 . ASN A 297 ? 0.4922 0.5159 0.4934 -0.0900 0.0721  -0.0960 303 ASN A OD1 
2211 N ND2 . ASN A 297 ? 0.5048 0.5454 0.5304 -0.0870 0.0877  -0.1172 303 ASN A ND2 
2212 N N   . ILE A 298 ? 0.3843 0.3904 0.2775 -0.1377 0.0958  -0.1014 304 ILE A N   
2213 C CA  . ILE A 298 ? 0.4121 0.4048 0.2668 -0.1545 0.1035  -0.1070 304 ILE A CA  
2214 C C   . ILE A 298 ? 0.4296 0.4052 0.2550 -0.1553 0.0879  -0.0974 304 ILE A C   
2215 O O   . ILE A 298 ? 0.4056 0.3737 0.2147 -0.1624 0.0894  -0.1033 304 ILE A O   
2216 C CB  . ILE A 298 ? 0.4374 0.4223 0.2755 -0.1651 0.1092  -0.1022 304 ILE A CB  
2217 C CG1 . ILE A 298 ? 0.4776 0.4833 0.3501 -0.1663 0.1237  -0.1168 304 ILE A CG1 
2218 C CG2 . ILE A 298 ? 0.4942 0.4552 0.2911 -0.1805 0.1080  -0.0981 304 ILE A CG2 
2219 C CD1 . ILE A 298 ? 0.4454 0.4445 0.3060 -0.1778 0.1283  -0.1144 304 ILE A CD1 
2220 N N   . ALA A 299 ? 0.4200 0.3925 0.2451 -0.1457 0.0709  -0.0830 305 ALA A N   
2221 C CA  . ALA A 299 ? 0.4030 0.3626 0.2034 -0.1445 0.0533  -0.0771 305 ALA A CA  
2222 C C   . ALA A 299 ? 0.3955 0.3652 0.2130 -0.1413 0.0502  -0.0837 305 ALA A C   
2223 O O   . ALA A 299 ? 0.4416 0.4000 0.2347 -0.1477 0.0458  -0.0881 305 ALA A O   
2224 C CB  . ALA A 299 ? 0.4006 0.3611 0.2045 -0.1329 0.0356  -0.0650 305 ALA A CB  
2225 N N   . VAL A 300 ? 0.3584 0.3458 0.2141 -0.1327 0.0516  -0.0843 306 VAL A N   
2226 C CA  . VAL A 300 ? 0.3683 0.3612 0.2381 -0.1321 0.0490  -0.0902 306 VAL A CA  
2227 C C   . VAL A 300 ? 0.3772 0.3628 0.2376 -0.1405 0.0605  -0.1035 306 VAL A C   
2228 O O   . VAL A 300 ? 0.3801 0.3601 0.2273 -0.1454 0.0561  -0.1086 306 VAL A O   
2229 C CB  . VAL A 300 ? 0.3296 0.3342 0.2339 -0.1242 0.0492  -0.0877 306 VAL A CB  
2230 C CG1 . VAL A 300 ? 0.3404 0.3437 0.2532 -0.1272 0.0475  -0.0942 306 VAL A CG1 
2231 C CG2 . VAL A 300 ? 0.3207 0.3358 0.2339 -0.1175 0.0386  -0.0767 306 VAL A CG2 
2232 N N   . ALA A 301 ? 0.3798 0.3678 0.2485 -0.1421 0.0751  -0.1117 307 ALA A N   
2233 C CA  . ALA A 301 ? 0.3985 0.3840 0.2604 -0.1500 0.0875  -0.1284 307 ALA A CA  
2234 C C   . ALA A 301 ? 0.4693 0.4416 0.2940 -0.1607 0.0864  -0.1260 307 ALA A C   
2235 O O   . ALA A 301 ? 0.4613 0.4305 0.2811 -0.1638 0.0875  -0.1330 307 ALA A O   
2236 C CB  . ALA A 301 ? 0.3821 0.3784 0.2604 -0.1505 0.1033  -0.1394 307 ALA A CB  
2237 N N   . ASN A 302 ? 0.4702 0.4316 0.2687 -0.1648 0.0819  -0.1143 308 ASN A N   
2238 C CA  . ASN A 302 ? 0.4853 0.4271 0.2465 -0.1735 0.0778  -0.1095 308 ASN A CA  
2239 C C   . ASN A 302 ? 0.5001 0.4341 0.2488 -0.1685 0.0592  -0.1058 308 ASN A C   
2240 O O   . ASN A 302 ? 0.5430 0.4645 0.2695 -0.1736 0.0568  -0.1076 308 ASN A O   
2241 C CB  . ASN A 302 ? 0.5133 0.4382 0.2474 -0.1793 0.0758  -0.0981 308 ASN A CB  
2242 C CG  . ASN A 302 ? 0.5872 0.5176 0.3273 -0.1907 0.0956  -0.1045 308 ASN A CG  
2243 O OD1 . ASN A 302 ? 0.5833 0.5300 0.3448 -0.1942 0.1099  -0.1188 308 ASN A OD1 
2244 N ND2 . ASN A 302 ? 0.5875 0.5049 0.3106 -0.1967 0.0953  -0.0957 308 ASN A ND2 
2245 N N   . ILE A 303 ? 0.4787 0.4222 0.2434 -0.1591 0.0458  -0.1021 309 ILE A N   
2246 C CA  . ILE A 303 ? 0.4917 0.4365 0.2558 -0.1548 0.0295  -0.1030 309 ILE A CA  
2247 C C   . ILE A 303 ? 0.5023 0.4517 0.2777 -0.1587 0.0373  -0.1140 309 ILE A C   
2248 O O   . ILE A 303 ? 0.4830 0.4230 0.2406 -0.1612 0.0317  -0.1166 309 ILE A O   
2249 C CB  . ILE A 303 ? 0.4499 0.4121 0.2380 -0.1465 0.0169  -0.1001 309 ILE A CB  
2250 C CG1 . ILE A 303 ? 0.4713 0.4272 0.2458 -0.1403 0.0055  -0.0901 309 ILE A CG1 
2251 C CG2 . ILE A 303 ? 0.4073 0.3785 0.2031 -0.1435 0.0022  -0.1043 309 ILE A CG2 
2252 C CD1 . ILE A 303 ? 0.4335 0.4123 0.2422 -0.1290 -0.0028 -0.0852 309 ILE A CD1 
2253 N N   . VAL A 304 ? 0.4464 0.4070 0.2498 -0.1584 0.0493  -0.1211 310 VAL A N   
2254 C CA  . VAL A 304 ? 0.4724 0.4335 0.2863 -0.1604 0.0551  -0.1321 310 VAL A CA  
2255 C C   . VAL A 304 ? 0.5268 0.4794 0.3208 -0.1668 0.0656  -0.1383 310 VAL A C   
2256 O O   . VAL A 304 ? 0.5007 0.4475 0.2844 -0.1697 0.0630  -0.1435 310 VAL A O   
2257 C CB  . VAL A 304 ? 0.4511 0.4194 0.2970 -0.1561 0.0623  -0.1386 310 VAL A CB  
2258 C CG1 . VAL A 304 ? 0.4686 0.4324 0.3232 -0.1562 0.0658  -0.1505 310 VAL A CG1 
2259 C CG2 . VAL A 304 ? 0.3957 0.3710 0.2604 -0.1515 0.0519  -0.1295 310 VAL A CG2 
2260 N N   . ASN A 305 ? 0.5185 0.4717 0.3078 -0.1706 0.0782  -0.1385 311 ASN A N   
2261 C CA  . ASN A 305 ? 0.5538 0.5027 0.3272 -0.1799 0.0905  -0.1457 311 ASN A CA  
2262 C C   . ASN A 305 ? 0.6143 0.5432 0.3479 -0.1864 0.0810  -0.1386 311 ASN A C   
2263 O O   . ASN A 305 ? 0.6481 0.5716 0.3678 -0.1934 0.0865  -0.1459 311 ASN A O   
2264 C CB  . ASN A 305 ? 0.5770 0.5319 0.3532 -0.1861 0.1051  -0.1468 311 ASN A CB  
2265 C CG  . ASN A 305 ? 0.5902 0.5667 0.4069 -0.1800 0.1168  -0.1612 311 ASN A CG  
2266 O OD1 . ASN A 305 ? 0.6306 0.6132 0.4661 -0.1740 0.1173  -0.1733 311 ASN A OD1 
2267 N ND2 . ASN A 305 ? 0.5911 0.5776 0.4219 -0.1801 0.1242  -0.1607 311 ASN A ND2 
2268 N N   . SER A 306 ? 0.5835 0.5004 0.2983 -0.1831 0.0652  -0.1254 312 SER A N   
2269 C CA  . SER A 306 ? 0.6349 0.5293 0.3118 -0.1858 0.0517  -0.1197 312 SER A CA  
2270 C C   . SER A 306 ? 0.6164 0.5140 0.2985 -0.1817 0.0423  -0.1268 312 SER A C   
2271 O O   . SER A 306 ? 0.7199 0.6033 0.3765 -0.1868 0.0400  -0.1295 312 SER A O   
2272 C CB  . SER A 306 ? 0.5733 0.4548 0.2335 -0.1788 0.0329  -0.1065 312 SER A CB  
2273 O OG  . SER A 306 ? 0.6138 0.5124 0.3013 -0.1668 0.0197  -0.1064 312 SER A OG  
2274 N N   . VAL A 307 ? 0.6189 0.5342 0.3335 -0.1741 0.0374  -0.1304 313 VAL A N   
2275 C CA  . VAL A 307 ? 0.6195 0.5386 0.3419 -0.1720 0.0288  -0.1376 313 VAL A CA  
2276 C C   . VAL A 307 ? 0.6608 0.5803 0.3874 -0.1777 0.0432  -0.1494 313 VAL A C   
2277 O O   . VAL A 307 ? 0.6149 0.5286 0.3315 -0.1792 0.0378  -0.1551 313 VAL A O   
2278 C CB  . VAL A 307 ? 0.6022 0.5393 0.3579 -0.1660 0.0211  -0.1376 313 VAL A CB  
2279 C CG1 . VAL A 307 ? 0.5708 0.5121 0.3358 -0.1665 0.0130  -0.1451 313 VAL A CG1 
2280 C CG2 . VAL A 307 ? 0.5912 0.5320 0.3451 -0.1594 0.0060  -0.1285 313 VAL A CG2 
2281 N N   . LYS A 308 ? 0.7165 0.6823 0.3781 -0.1545 0.0323  -0.2499 314 LYS A N   
2282 C CA  . LYS A 308 ? 0.7201 0.6888 0.3869 -0.1668 0.0555  -0.2540 314 LYS A CA  
2283 C C   . LYS A 308 ? 0.7592 0.7110 0.3887 -0.1805 0.0583  -0.2508 314 LYS A C   
2284 O O   . LYS A 308 ? 0.7855 0.7391 0.4187 -0.1919 0.0781  -0.2544 314 LYS A O   
2285 C CB  . LYS A 308 ? 0.7048 0.6828 0.4050 -0.1647 0.0769  -0.2518 314 LYS A CB  
2286 C CG  . LYS A 308 ? 0.6478 0.6425 0.3866 -0.1546 0.0795  -0.2555 314 LYS A CG  
2287 C CD  . LYS A 308 ? 0.6182 0.6189 0.3872 -0.1530 0.0996  -0.2529 314 LYS A CD  
2288 C CE  . LYS A 308 ? 0.5927 0.6075 0.3974 -0.1447 0.1028  -0.2559 314 LYS A CE  
2289 N NZ  . LYS A 308 ? 0.6552 0.6726 0.4868 -0.1399 0.1164  -0.2509 314 LYS A NZ  
2290 N N   . GLN A 309 ? 0.7888 0.7239 0.3829 -0.1801 0.0386  -0.2444 315 GLN A N   
2291 C CA  . GLN A 309 ? 0.8295 0.7460 0.3850 -0.1942 0.0408  -0.2397 315 GLN A CA  
2292 C C   . GLN A 309 ? 0.8291 0.7448 0.3927 -0.2033 0.0653  -0.2360 315 GLN A C   
2293 O O   . GLN A 309 ? 0.8420 0.7521 0.3918 -0.2186 0.0797  -0.2380 315 GLN A O   
2294 C CB  . GLN A 309 ? 0.8617 0.7759 0.3994 -0.2052 0.0414  -0.2474 315 GLN A CB  
2295 C CG  . GLN A 309 ? 0.8890 0.8083 0.4256 -0.1967 0.0196  -0.2543 315 GLN A CG  
2296 C CD  . GLN A 309 ? 0.9089 0.8149 0.4198 -0.1870 -0.0110 -0.2482 315 GLN A CD  
2297 O OE1 . GLN A 309 ? 0.9673 0.8781 0.4945 -0.1731 -0.0226 -0.2453 315 GLN A OE1 
2298 N NE2 . GLN A 309 ? 0.9999 0.8894 0.4715 -0.1940 -0.0247 -0.2467 315 GLN A NE2 
2299 N N   . ARG A 310 ? 0.7843 0.7068 0.3728 -0.1940 0.0701  -0.2317 316 ARG A N   
2300 C CA  . ARG A 310 ? 0.7846 0.7071 0.3834 -0.1999 0.0900  -0.2280 316 ARG A CA  
2301 C C   . ARG A 310 ? 0.8216 0.7273 0.3947 -0.2001 0.0804  -0.2167 316 ARG A C   
2302 O O   . ARG A 310 ? 0.8182 0.7159 0.3763 -0.1907 0.0582  -0.2113 316 ARG A O   
2303 C CB  . ARG A 310 ? 0.7454 0.6864 0.3909 -0.1892 0.1022  -0.2306 316 ARG A CB  
2304 C CG  . ARG A 310 ? 0.7215 0.6772 0.3960 -0.1923 0.1189  -0.2405 316 ARG A CG  
2305 C CD  . ARG A 310 ? 0.7168 0.6871 0.4349 -0.1807 0.1281  -0.2409 316 ARG A CD  
2306 N N   . PRO A 311 ? 0.8706 0.7709 0.4396 -0.2107 0.0966  -0.2135 317 PRO A N   
2307 C CA  . PRO A 311 ? 0.8214 0.7054 0.3675 -0.2119 0.0894  -0.2024 317 PRO A CA  
2308 C C   . PRO A 311 ? 0.7903 0.6820 0.3604 -0.1952 0.0827  -0.1977 317 PRO A C   
2309 O O   . PRO A 311 ? 0.7762 0.6864 0.3854 -0.1860 0.0920  -0.2026 317 PRO A O   
2310 C CB  . PRO A 311 ? 0.8567 0.7382 0.4015 -0.2282 0.1121  -0.2033 317 PRO A CB  
2311 C CG  . PRO A 311 ? 0.8626 0.7629 0.4397 -0.2311 0.1310  -0.2150 317 PRO A CG  
2312 C CD  . PRO A 311 ? 0.8339 0.7400 0.4128 -0.2249 0.1203  -0.2205 317 PRO A CD  
2313 N N   . LEU A 312 ? 0.7905 0.6663 0.3360 -0.1915 0.0656  -0.1878 318 LEU A N   
2314 C CA  . LEU A 312 ? 0.7509 0.6317 0.3139 -0.1756 0.0552  -0.1830 318 LEU A CA  
2315 C C   . LEU A 312 ? 0.7507 0.6339 0.3291 -0.1772 0.0713  -0.1788 318 LEU A C   
2316 O O   . LEU A 312 ? 0.7526 0.6250 0.3134 -0.1911 0.0823  -0.1756 318 LEU A O   
2317 C CB  . LEU A 312 ? 0.7763 0.6389 0.3077 -0.1699 0.0276  -0.1745 318 LEU A CB  
2318 C CG  . LEU A 312 ? 0.7997 0.6594 0.3151 -0.1668 0.0073  -0.1787 318 LEU A CG  
2319 C CD1 . LEU A 312 ? 0.8096 0.6593 0.3109 -0.1543 -0.0218 -0.1719 318 LEU A CD1 
2320 C CD2 . LEU A 312 ? 0.7713 0.6539 0.3203 -0.1600 0.0124  -0.1909 318 LEU A CD2 
2321 N N   . GLN A 313 ? 0.6897 0.5877 0.3020 -0.1634 0.0730  -0.1796 319 GLN A N   
2322 C CA  . GLN A 313 ? 0.7220 0.6234 0.3510 -0.1621 0.0851  -0.1756 319 GLN A CA  
2323 C C   . GLN A 313 ? 0.7295 0.6116 0.3289 -0.1627 0.0716  -0.1643 319 GLN A C   
2324 O O   . GLN A 313 ? 0.7260 0.5967 0.3040 -0.1566 0.0490  -0.1594 319 GLN A O   
2325 C CB  . GLN A 313 ? 0.6423 0.5631 0.3140 -0.1465 0.0885  -0.1787 319 GLN A CB  
2326 C CG  . GLN A 313 ? 0.6383 0.5765 0.3423 -0.1454 0.1024  -0.1884 319 GLN A CG  
2327 C CD  . GLN A 313 ? 0.6507 0.6046 0.3961 -0.1319 0.1085  -0.1891 319 GLN A CD  
2328 O OE1 . GLN A 313 ? 0.6565 0.6095 0.4070 -0.1240 0.1037  -0.1832 319 GLN A OE1 
2329 N NE2 . GLN A 313 ? 0.6290 0.5958 0.4033 -0.1297 0.1185  -0.1959 319 GLN A NE2 
2330 N N   . ALA A 314 ? 0.7765 0.6554 0.3771 -0.1694 0.0847  -0.1604 320 ALA A N   
2331 C CA  . ALA A 314 ? 0.7689 0.6270 0.3390 -0.1739 0.0755  -0.1493 320 ALA A CA  
2332 C C   . ALA A 314 ? 0.8190 0.6841 0.4116 -0.1645 0.0790  -0.1455 320 ALA A C   
2333 O O   . ALA A 314 ? 0.8538 0.7370 0.4810 -0.1625 0.0969  -0.1513 320 ALA A O   
2334 C CB  . ALA A 314 ? 0.7876 0.6317 0.3317 -0.1946 0.0880  -0.1481 320 ALA A CB  
2335 N N   . TYR A 315 ? 0.8107 0.6606 0.3840 -0.1585 0.0608  -0.1356 321 TYR A N   
2336 C CA  . TYR A 315 ? 0.8094 0.6628 0.3987 -0.1498 0.0612  -0.1308 321 TYR A CA  
2337 C C   . TYR A 315 ? 0.7910 0.6288 0.3594 -0.1631 0.0691  -0.1237 321 TYR A C   
2338 O O   . TYR A 315 ? 0.8214 0.6342 0.3510 -0.1712 0.0568  -0.1150 321 TYR A O   
2339 C CB  . TYR A 315 ? 0.7604 0.6070 0.3434 -0.1351 0.0359  -0.1248 321 TYR A CB  
2340 C CG  . TYR A 315 ? 0.7522 0.5955 0.3412 -0.1284 0.0332  -0.1175 321 TYR A CG  
2341 C CD1 . TYR A 315 ? 0.7385 0.6021 0.3650 -0.1210 0.0477  -0.1222 321 TYR A CD1 
2342 C CD2 . TYR A 315 ? 0.7947 0.6137 0.3527 -0.1291 0.0157  -0.1055 321 TYR A CD2 
2343 C CE1 . TYR A 315 ? 0.7734 0.6342 0.4052 -0.1150 0.0454  -0.1160 321 TYR A CE1 
2344 C CE2 . TYR A 315 ? 0.8083 0.6236 0.3716 -0.1231 0.0130  -0.0987 321 TYR A CE2 
2345 C CZ  . TYR A 315 ? 0.7832 0.6197 0.3825 -0.1165 0.0281  -0.1043 321 TYR A CZ  
2346 O OH  . TYR A 315 ? 0.7911 0.6239 0.3949 -0.1108 0.0255  -0.0979 321 TYR A OH  
2347 N N   . LYS A 316 ? 0.7583 0.6102 0.3535 -0.1650 0.0884  -0.1273 322 LYS A N   
2348 C CA  . LYS A 316 ? 0.7697 0.6112 0.3512 -0.1793 0.0994  -0.1236 322 LYS A CA  
2349 C C   . LYS A 316 ? 0.8064 0.6545 0.4077 -0.1705 0.1014  -0.1200 322 LYS A C   
2350 O O   . LYS A 316 ? 0.8111 0.6824 0.4524 -0.1643 0.1160  -0.1272 322 LYS A O   
2351 C CB  . LYS A 316 ? 0.7211 0.5751 0.3179 -0.1930 0.1224  -0.1339 322 LYS A CB  
2352 C CG  . LYS A 316 ? 0.7457 0.5799 0.3078 -0.2153 0.1285  -0.1317 322 LYS A CG  
2353 C CD  . LYS A 316 ? 0.7429 0.5724 0.3043 -0.2234 0.1371  -0.1286 322 LYS A CD  
2354 C CE  . LYS A 316 ? 0.7757 0.5894 0.3090 -0.2483 0.1477  -0.1305 322 LYS A CE  
2355 N NZ  . LYS A 316 ? 0.8338 0.6404 0.3626 -0.2585 0.1552  -0.1280 322 LYS A NZ  
2356 N N   . PRO A 317 ? 0.7968 0.6245 0.3724 -0.1694 0.0868  -0.1087 323 PRO A N   
2357 C CA  . PRO A 317 ? 0.7805 0.6140 0.3738 -0.1617 0.0890  -0.1053 323 PRO A CA  
2358 C C   . PRO A 317 ? 0.7589 0.6015 0.3667 -0.1738 0.1111  -0.1100 323 PRO A C   
2359 O O   . PRO A 317 ? 0.7838 0.6200 0.3770 -0.1913 0.1216  -0.1132 323 PRO A O   
2360 C CB  . PRO A 317 ? 0.7466 0.5514 0.3030 -0.1609 0.0673  -0.0916 323 PRO A CB  
2361 C CG  . PRO A 317 ? 0.8130 0.5944 0.3297 -0.1758 0.0615  -0.0879 323 PRO A CG  
2362 C CD  . PRO A 317 ? 0.8094 0.6064 0.3387 -0.1757 0.0676  -0.0982 323 PRO A CD  
2363 N N   . GLY A 318 ? 0.7015 0.5603 0.3407 -0.1642 0.1177  -0.1115 324 GLY A N   
2364 C CA  . GLY A 318 ? 0.6177 0.4851 0.2723 -0.1735 0.1346  -0.1153 324 GLY A CA  
2365 C C   . GLY A 318 ? 0.6242 0.4825 0.2718 -0.1689 0.1273  -0.1063 324 GLY A C   
2366 O O   . GLY A 318 ? 0.6623 0.5015 0.2841 -0.1625 0.1082  -0.0962 324 GLY A O   
2367 N N   . ALA A 319 ? 0.5960 0.4680 0.2680 -0.1711 0.1407  -0.1102 325 ALA A N   
2368 C CA  . ALA A 319 ? 0.5916 0.4551 0.2568 -0.1680 0.1348  -0.1020 325 ALA A CA  
2369 C C   . ALA A 319 ? 0.5701 0.4410 0.2523 -0.1464 0.1231  -0.0983 325 ALA A C   
2370 O O   . ALA A 319 ? 0.5570 0.4446 0.2652 -0.1337 0.1232  -0.1040 325 ALA A O   
2371 C CB  . ALA A 319 ? 0.6031 0.4826 0.2943 -0.1753 0.1521  -0.1088 325 ALA A CB  
2372 N N   . LEU A 320 ? 0.5696 0.4264 0.2362 -0.1431 0.1126  -0.0889 326 LEU A N   
2373 C CA  . LEU A 320 ? 0.5731 0.4344 0.2615 -0.1208 0.0934  -0.0799 326 LEU A CA  
2374 C C   . LEU A 320 ? 0.5049 0.3978 0.2486 -0.1051 0.1019  -0.0853 326 LEU A C   
2375 O O   . LEU A 320 ? 0.4781 0.3835 0.2415 -0.1078 0.1152  -0.0891 326 LEU A O   
2376 C CB  . LEU A 320 ? 0.5756 0.4150 0.2412 -0.1210 0.0791  -0.0669 326 LEU A CB  
2377 C CG  . LEU A 320 ? 0.5709 0.4137 0.2580 -0.0997 0.0597  -0.0576 326 LEU A CG  
2378 C CD1 . LEU A 320 ? 0.5464 0.3893 0.2353 -0.0871 0.0432  -0.0570 326 LEU A CD1 
2379 C CD2 . LEU A 320 ? 0.5933 0.4093 0.2503 -0.1035 0.0466  -0.0458 326 LEU A CD2 
2380 N N   . THR A 321 ? 0.4449 0.3500 0.2126 -0.0891 0.0940  -0.0861 327 THR A N   
2381 C CA  . THR A 321 ? 0.4262 0.3546 0.2405 -0.0719 0.0957  -0.0874 327 THR A CA  
2382 C C   . THR A 321 ? 0.3911 0.3144 0.2093 -0.0570 0.0750  -0.0762 327 THR A C   
2383 O O   . THR A 321 ? 0.4132 0.3262 0.2157 -0.0529 0.0598  -0.0728 327 THR A O   
2384 C CB  . THR A 321 ? 0.4301 0.3750 0.2689 -0.0656 0.1028  -0.0970 327 THR A CB  
2385 O OG1 . THR A 321 ? 0.4521 0.4060 0.2967 -0.0770 0.1234  -0.1091 327 THR A OG1 
2386 C CG2 . THR A 321 ? 0.3565 0.3190 0.2366 -0.0468 0.0996  -0.0956 327 THR A CG2 
2387 N N   . PHE A 322 ? 0.3837 0.3149 0.2235 -0.0489 0.0743  -0.0717 328 PHE A N   
2388 C CA  . PHE A 322 ? 0.3829 0.3091 0.2260 -0.0358 0.0557  -0.0619 328 PHE A CA  
2389 C C   . PHE A 322 ? 0.3240 0.2675 0.2028 -0.0253 0.0601  -0.0609 328 PHE A C   
2390 O O   . PHE A 322 ? 0.3259 0.2708 0.2067 -0.0315 0.0686  -0.0607 328 PHE A O   
2391 C CB  . PHE A 322 ? 0.4356 0.3360 0.2407 -0.0438 0.0440  -0.0531 328 PHE A CB  
2392 C CG  . PHE A 322 ? 0.4534 0.3449 0.2558 -0.0309 0.0219  -0.0448 328 PHE A CG  
2393 C CD1 . PHE A 322 ? 0.4120 0.3156 0.2431 -0.0175 0.0175  -0.0414 328 PHE A CD1 
2394 C CD2 . PHE A 322 ? 0.5174 0.3881 0.2883 -0.0323 0.0052  -0.0412 328 PHE A CD2 
2395 C CE1 . PHE A 322 ? 0.4443 0.3412 0.2747 -0.0060 -0.0019 -0.0356 328 PHE A CE1 
2396 C CE2 . PHE A 322 ? 0.5609 0.4247 0.3321 -0.0195 -0.0158 -0.0355 328 PHE A CE2 
2397 C CZ  . PHE A 322 ? 0.4884 0.3661 0.2903 -0.0065 -0.0187 -0.0332 328 PHE A CZ  
2398 N N   . LEU A 323 ? 0.2963 0.2526 0.2020 -0.0107 0.0546  -0.0610 329 LEU A N   
2399 C CA  . LEU A 323 ? 0.2670 0.2386 0.2053 -0.0004 0.0580  -0.0601 329 LEU A CA  
2400 C C   . LEU A 323 ? 0.2642 0.2332 0.2069 0.0110  0.0419  -0.0522 329 LEU A C   
2401 O O   . LEU A 323 ? 0.2543 0.2213 0.1945 0.0171  0.0311  -0.0519 329 LEU A O   
2402 C CB  . LEU A 323 ? 0.2460 0.2339 0.2126 0.0062  0.0672  -0.0675 329 LEU A CB  
2403 C CG  . LEU A 323 ? 0.2936 0.2860 0.2604 -0.0033 0.0832  -0.0776 329 LEU A CG  
2404 C CD1 . LEU A 323 ? 0.2852 0.2903 0.2796 0.0052  0.0895  -0.0840 329 LEU A CD1 
2405 C CD2 . LEU A 323 ? 0.2734 0.2695 0.2426 -0.0118 0.0949  -0.0806 329 LEU A CD2 
2406 N N   . LEU A 324 ? 0.2485 0.2188 0.1990 0.0136  0.0408  -0.0472 330 LEU A N   
2407 C CA  . LEU A 324 ? 0.2611 0.2304 0.2184 0.0242  0.0272  -0.0407 330 LEU A CA  
2408 C C   . LEU A 324 ? 0.2234 0.2095 0.2130 0.0335  0.0323  -0.0417 330 LEU A C   
2409 O O   . LEU A 324 ? 0.2458 0.2385 0.2465 0.0314  0.0413  -0.0425 330 LEU A O   
2410 C CB  . LEU A 324 ? 0.3057 0.2604 0.2439 0.0195  0.0203  -0.0336 330 LEU A CB  
2411 C CG  . LEU A 324 ? 0.3574 0.2899 0.2581 0.0092  0.0138  -0.0312 330 LEU A CG  
2412 C CD1 . LEU A 324 ? 0.3637 0.2902 0.2480 -0.0067 0.0278  -0.0332 330 LEU A CD1 
2413 C CD2 . LEU A 324 ? 0.3817 0.2973 0.2665 0.0136  -0.0041 -0.0233 330 LEU A CD2 
2414 N N   . SER A 325 ? 0.2202 0.2130 0.2240 0.0432  0.0268  -0.0425 331 SER A N   
2415 C CA  . SER A 325 ? 0.2306 0.2349 0.2596 0.0519  0.0288  -0.0418 331 SER A CA  
2416 C C   . SER A 325 ? 0.2648 0.2662 0.2938 0.0562  0.0192  -0.0352 331 SER A C   
2417 O O   . SER A 325 ? 0.3270 0.3195 0.3421 0.0570  0.0077  -0.0324 331 SER A O   
2418 C CB  . SER A 325 ? 0.2657 0.2762 0.3065 0.0584  0.0271  -0.0454 331 SER A CB  
2419 O OG  . SER A 325 ? 0.3153 0.3213 0.3468 0.0612  0.0145  -0.0445 331 SER A OG  
2420 N N   . MET A 326 ? 0.2132 0.2215 0.2576 0.0591  0.0232  -0.0333 332 MET A N   
2421 C CA  . MET A 326 ? 0.2404 0.2470 0.2865 0.0629  0.0153  -0.0276 332 MET A CA  
2422 C C   . MET A 326 ? 0.1920 0.2086 0.2591 0.0718  0.0148  -0.0275 332 MET A C   
2423 O O   . MET A 326 ? 0.1718 0.1929 0.2481 0.0706  0.0198  -0.0240 332 MET A O   
2424 C CB  . MET A 326 ? 0.2461 0.2514 0.2892 0.0566  0.0203  -0.0256 332 MET A CB  
2425 C CG  . MET A 326 ? 0.3053 0.2994 0.3252 0.0448  0.0237  -0.0262 332 MET A CG  
2426 S SD  . MET A 326 ? 0.4611 0.4350 0.4539 0.0420  0.0096  -0.0190 332 MET A SD  
2427 C CE  . MET A 326 ? 0.2753 0.2415 0.2545 0.0447  0.0005  -0.0208 332 MET A CE  
2428 N N   . GLY A 327 ? 0.1857 0.2019 0.2521 0.0722  0.0103  -0.0266 333 GLY A N   
2429 C CA  . GLY A 327 ? 0.1688 0.1872 0.2406 0.0683  0.0139  -0.0204 333 GLY A CA  
2430 C C   . GLY A 327 ? 0.1753 0.1951 0.2476 0.0680  0.0226  -0.0212 333 GLY A C   
2431 O O   . GLY A 327 ? 0.1711 0.1924 0.2437 0.0684  0.0272  -0.0271 333 GLY A O   
2432 N N   . ARG A 328 ? 0.1442 0.1635 0.2132 0.0670  0.0232  -0.0170 334 ARG A N   
2433 C CA  . ARG A 328 ? 0.1609 0.1809 0.2271 0.0681  0.0263  -0.0202 334 ARG A CA  
2434 C C   . ARG A 328 ? 0.1778 0.2014 0.2468 0.0695  0.0271  -0.0218 334 ARG A C   
2435 O O   . ARG A 328 ? 0.1627 0.1870 0.2349 0.0702  0.0306  -0.0258 334 ARG A O   
2436 C CB  . ARG A 328 ? 0.1530 0.1705 0.2154 0.0676  0.0250  -0.0183 334 ARG A CB  
2437 C CG  . ARG A 328 ? 0.1723 0.1894 0.2323 0.0682  0.0215  -0.0143 334 ARG A CG  
2438 C CD  . ARG A 328 ? 0.2005 0.2145 0.2593 0.0684  0.0209  -0.0151 334 ARG A CD  
2439 N NE  . ARG A 328 ? 0.1721 0.1861 0.2321 0.0659  0.0219  -0.0145 334 ARG A NE  
2440 C CZ  . ARG A 328 ? 0.2258 0.2394 0.2863 0.0652  0.0243  -0.0189 334 ARG A CZ  
2441 N NH1 . ARG A 328 ? 0.1959 0.2076 0.2557 0.0665  0.0268  -0.0232 334 ARG A NH1 
2442 N NH2 . ARG A 328 ? 0.2044 0.2209 0.2694 0.0635  0.0236  -0.0214 334 ARG A NH2 
2443 N N   . ASN A 329 ? 0.1533 0.1794 0.2240 0.0698  0.0249  -0.0193 335 ASN A N   
2444 C CA  . ASN A 329 ? 0.1854 0.2160 0.2628 0.0711  0.0265  -0.0211 335 ASN A CA  
2445 C C   . ASN A 329 ? 0.1652 0.2008 0.2515 0.0689  0.0317  -0.0256 335 ASN A C   
2446 O O   . ASN A 329 ? 0.1321 0.1726 0.2262 0.0685  0.0337  -0.0269 335 ASN A O   
2447 C CB  . ASN A 329 ? 0.1495 0.1797 0.2237 0.0717  0.0212  -0.0161 335 ASN A CB  
2448 C CG  . ASN A 329 ? 0.1765 0.2069 0.2480 0.0704  0.0183  -0.0126 335 ASN A CG  
2449 O OD1 . ASN A 329 ? 0.1556 0.1852 0.2284 0.0696  0.0195  -0.0134 335 ASN A OD1 
2450 N ND2 . ASN A 329 ? 0.1859 0.2164 0.2572 0.0706  0.0150  -0.0093 335 ASN A ND2 
2451 N N   . ASP A 330 ? 0.1661 0.2000 0.2520 0.0667  0.0350  -0.0292 336 ASP A N   
2452 C CA  . ASP A 330 ? 0.1788 0.2156 0.2714 0.0629  0.0417  -0.0345 336 ASP A CA  
2453 C C   . ASP A 330 ? 0.1892 0.2211 0.2767 0.0594  0.0484  -0.0414 336 ASP A C   
2454 O O   . ASP A 330 ? 0.1536 0.1811 0.2343 0.0613  0.0444  -0.0413 336 ASP A O   
2455 C CB  . ASP A 330 ? 0.1930 0.2292 0.2869 0.0645  0.0368  -0.0304 336 ASP A CB  
2456 C CG  . ASP A 330 ? 0.2468 0.2895 0.3509 0.0599  0.0447  -0.0349 336 ASP A CG  
2457 O OD1 . ASP A 330 ? 0.2194 0.2646 0.3239 0.0530  0.0554  -0.0422 336 ASP A OD1 
2458 O OD2 . ASP A 330 ? 0.2362 0.2814 0.3442 0.0612  0.0403  -0.0312 336 ASP A OD2 
2459 N N   . GLY A 331 ? 0.2175 0.2472 0.2938 0.0495  0.0537  -0.0434 337 GLY A N   
2460 C CA  . GLY A 331 ? 0.2140 0.2333 0.2663 0.0404  0.0546  -0.0446 337 GLY A CA  
2461 C C   . GLY A 331 ? 0.1954 0.2142 0.2385 0.0277  0.0650  -0.0493 337 GLY A C   
2462 O O   . GLY A 331 ? 0.1993 0.2286 0.2585 0.0264  0.0727  -0.0534 337 GLY A O   
2463 N N   . VAL A 332 ? 0.2125 0.2184 0.2284 0.0177  0.0651  -0.0493 338 VAL A N   
2464 C CA  . VAL A 332 ? 0.2255 0.2287 0.2276 0.0027  0.0767  -0.0548 338 VAL A CA  
2465 C C   . VAL A 332 ? 0.2480 0.2363 0.2205 -0.0058 0.0750  -0.0550 338 VAL A C   
2466 O O   . VAL A 332 ? 0.2493 0.2284 0.2107 0.0000  0.0626  -0.0497 338 VAL A O   
2467 C CB  . VAL A 332 ? 0.2493 0.2466 0.2412 -0.0048 0.0761  -0.0508 338 VAL A CB  
2468 C CG1 . VAL A 332 ? 0.2892 0.2652 0.2524 -0.0057 0.0615  -0.0406 338 VAL A CG1 
2469 C CG2 . VAL A 332 ? 0.2793 0.2779 0.2622 -0.0216 0.0915  -0.0590 338 VAL A CG2 
2470 N N   . GLY A 333 ? 0.2674 0.2542 0.2275 -0.0198 0.0878  -0.0623 339 GLY A N   
2471 C CA  . GLY A 333 ? 0.2937 0.2646 0.2219 -0.0296 0.0864  -0.0626 339 GLY A CA  
2472 C C   . GLY A 333 ? 0.3175 0.2912 0.2378 -0.0455 0.1040  -0.0731 339 GLY A C   
2473 O O   . GLY A 333 ? 0.3111 0.2953 0.2439 -0.0520 0.1163  -0.0793 339 GLY A O   
2474 N N   . GLN A 334 ? 0.3298 0.2949 0.2299 -0.0520 0.1051  -0.0762 340 GLN A N   
2475 C CA  . GLN A 334 ? 0.3609 0.3266 0.2488 -0.0687 0.1217  -0.0869 340 GLN A CA  
2476 C C   . GLN A 334 ? 0.3785 0.3479 0.2689 -0.0665 0.1243  -0.0933 340 GLN A C   
2477 O O   . GLN A 334 ? 0.3497 0.3104 0.2301 -0.0591 0.1106  -0.0874 340 GLN A O   
2478 C CB  . GLN A 334 ? 0.4070 0.3479 0.2486 -0.0873 0.1208  -0.0826 340 GLN A CB  
2479 C CG  . GLN A 334 ? 0.4120 0.3283 0.2191 -0.0858 0.1019  -0.0720 340 GLN A CG  
2480 C CD  . GLN A 334 ? 0.5137 0.4013 0.2725 -0.1042 0.0996  -0.0666 340 GLN A CD  
2481 O OE1 . GLN A 334 ? 0.5515 0.4253 0.2981 -0.1034 0.0897  -0.0572 340 GLN A OE1 
2482 N NE2 . GLN A 334 ? 0.5227 0.3996 0.2521 -0.1216 0.1092  -0.0727 340 GLN A NE2 
2483 N N   . ILE A 335 ? 0.3749 0.3583 0.2802 -0.0729 0.1418  -0.1067 341 ILE A N   
2484 C CA  . ILE A 335 ? 0.3956 0.3826 0.3032 -0.0729 0.1470  -0.1148 341 ILE A CA  
2485 C C   . ILE A 335 ? 0.4368 0.4164 0.3214 -0.0925 0.1554  -0.1198 341 ILE A C   
2486 O O   . ILE A 335 ? 0.4451 0.4335 0.3428 -0.1009 0.1648  -0.1253 341 ILE A O   
2487 C CB  . ILE A 335 ? 0.3914 0.3996 0.3466 -0.0587 0.1479  -0.1186 341 ILE A CB  
2488 C CG1 . ILE A 335 ? 0.3559 0.3678 0.3292 -0.0403 0.1375  -0.1120 341 ILE A CG1 
2489 C CG2 . ILE A 335 ? 0.4096 0.4202 0.3684 -0.0612 0.1509  -0.1246 341 ILE A CG2 
2490 C CD1 . ILE A 335 ? 0.3829 0.4088 0.3945 -0.0264 0.1341  -0.1120 341 ILE A CD1 
2491 N N   . SER A 336 ? 0.4434 0.4058 0.2927 -0.1003 0.1508  -0.1182 342 SER A N   
2492 C CA  . SER A 336 ? 0.4707 0.4223 0.2929 -0.1198 0.1570  -0.1216 342 SER A CA  
2493 C C   . SER A 336 ? 0.5249 0.4681 0.3302 -0.1354 0.1630  -0.1203 342 SER A C   
2494 O O   . SER A 336 ? 0.5094 0.4562 0.3166 -0.1496 0.1741  -0.1278 342 SER A O   
2495 C CB  . SER A 336 ? 0.4569 0.4253 0.3073 -0.1209 0.1670  -0.1322 342 SER A CB  
2496 O OG  . SER A 336 ? 0.5144 0.4895 0.3812 -0.1067 0.1612  -0.1328 342 SER A OG  
2497 N N   . GLY A 337 ? 0.4884 0.4192 0.2760 -0.1336 0.1555  -0.1113 343 GLY A N   
2498 C CA  . GLY A 337 ? 0.5409 0.4569 0.3026 -0.1508 0.1589  -0.1082 343 GLY A CA  
2499 C C   . GLY A 337 ? 0.5122 0.4464 0.3055 -0.1506 0.1687  -0.1130 343 GLY A C   
2500 O O   . GLY A 337 ? 0.5846 0.5072 0.3583 -0.1657 0.1724  -0.1115 343 GLY A O   
2501 N N   . PHE A 338 ? 0.4880 0.4486 0.3288 -0.1341 0.1715  -0.1184 344 PHE A N   
2502 C CA  . PHE A 338 ? 0.4927 0.4697 0.3631 -0.1317 0.1769  -0.1218 344 PHE A CA  
2503 C C   . PHE A 338 ? 0.4196 0.4082 0.3173 -0.1104 0.1691  -0.1166 344 PHE A C   
2504 O O   . PHE A 338 ? 0.4009 0.3925 0.3090 -0.0956 0.1621  -0.1142 344 PHE A O   
2505 C CB  . PHE A 338 ? 0.5125 0.5113 0.4185 -0.1341 0.1872  -0.1354 344 PHE A CB  
2506 C CG  . PHE A 338 ? 0.4784 0.4896 0.4099 -0.1217 0.1857  -0.1400 344 PHE A CG  
2507 C CD1 . PHE A 338 ? 0.4236 0.4478 0.3875 -0.1002 0.1779  -0.1369 344 PHE A CD1 
2508 C CD2 . PHE A 338 ? 0.4446 0.4525 0.3660 -0.1323 0.1915  -0.1469 344 PHE A CD2 
2509 C CE1 . PHE A 338 ? 0.4767 0.5089 0.4611 -0.0897 0.1756  -0.1401 344 PHE A CE1 
2510 C CE2 . PHE A 338 ? 0.4405 0.4583 0.3840 -0.1216 0.1901  -0.1509 344 PHE A CE2 
2511 C CZ  . PHE A 338 ? 0.4397 0.4690 0.4142 -0.1004 0.1820  -0.1473 344 PHE A CZ  
2512 N N   . TYR A 339 ? 0.4100 0.4056 0.3209 -0.1099 0.1708  -0.1158 345 TYR A N   
2513 C CA  . TYR A 339 ? 0.3620 0.3666 0.2963 -0.0921 0.1629  -0.1099 345 TYR A CA  
2514 C C   . TYR A 339 ? 0.3379 0.3649 0.3187 -0.0732 0.1600  -0.1142 345 TYR A C   
2515 O O   . TYR A 339 ? 0.3200 0.3616 0.3263 -0.0738 0.1646  -0.1228 345 TYR A O   
2516 C CB  . TYR A 339 ? 0.3699 0.3790 0.3094 -0.0988 0.1672  -0.1103 345 TYR A CB  
2517 C CG  . TYR A 339 ? 0.3609 0.3778 0.3258 -0.0812 0.1546  -0.1018 345 TYR A CG  
2518 C CD1 . TYR A 339 ? 0.3083 0.3504 0.3185 -0.0661 0.1566  -0.1085 345 TYR A CD1 
2519 C CD2 . TYR A 339 ? 0.3948 0.3924 0.3369 -0.0803 0.1405  -0.0876 345 TYR A CD2 
2520 C CE1 . TYR A 339 ? 0.2985 0.3461 0.3285 -0.0514 0.1450  -0.1006 345 TYR A CE1 
2521 C CE2 . TYR A 339 ? 0.3668 0.3715 0.3308 -0.0655 0.1299  -0.0807 345 TYR A CE2 
2522 C CZ  . TYR A 339 ? 0.3207 0.3503 0.3275 -0.0517 0.1324  -0.0870 345 TYR A CZ  
2523 O OH  . TYR A 339 ? 0.3040 0.3388 0.3292 -0.0381 0.1214  -0.0798 345 TYR A OH  
2524 N N   . VAL A 340 ? 0.2925 0.3191 0.2827 -0.0562 0.1491  -0.1068 346 VAL A N   
2525 C CA  . VAL A 340 ? 0.2737 0.3164 0.3032 -0.0381 0.1431  -0.1073 346 VAL A CA  
2526 C C   . VAL A 340 ? 0.2756 0.3216 0.3191 -0.0251 0.1344  -0.0997 346 VAL A C   
2527 O O   . VAL A 340 ? 0.2612 0.2919 0.2832 -0.0241 0.1221  -0.0877 346 VAL A O   
2528 C CB  . VAL A 340 ? 0.2856 0.3248 0.3150 -0.0305 0.1384  -0.1066 346 VAL A CB  
2529 C CG1 . VAL A 340 ? 0.2867 0.3247 0.3064 -0.0432 0.1471  -0.1149 346 VAL A CG1 
2530 C CG2 . VAL A 340 ? 0.2838 0.3069 0.2880 -0.0275 0.1284  -0.0975 346 VAL A CG2 
2531 N N   . GLY A 341 ? 0.2508 0.3105 0.3260 -0.0144 0.1288  -0.0994 347 GLY A N   
2532 C CA  . GLY A 341 ? 0.2234 0.2873 0.3122 -0.0044 0.1206  -0.0928 347 GLY A CA  
2533 C C   . GLY A 341 ? 0.2313 0.2913 0.3267 0.0116  0.1074  -0.0835 347 GLY A C   
2534 O O   . GLY A 341 ? 0.2214 0.2744 0.3084 0.0146  0.1050  -0.0820 347 GLY A O   
2535 N N   . ARG A 342 ? 0.1975 0.2621 0.3071 0.0209  0.0984  -0.0772 348 ARG A N   
2536 C CA  . ARG A 342 ? 0.1855 0.2445 0.2958 0.0332  0.0855  -0.0672 348 ARG A CA  
2537 C C   . ARG A 342 ? 0.1586 0.2171 0.2748 0.0412  0.0781  -0.0639 348 ARG A C   
2538 O O   . ARG A 342 ? 0.1616 0.2130 0.2705 0.0462  0.0721  -0.0589 348 ARG A O   
2539 C CB  . ARG A 342 ? 0.1680 0.2304 0.2862 0.0379  0.0788  -0.0617 348 ARG A CB  
2540 C CG  . ARG A 342 ? 0.2128 0.2729 0.3204 0.0275  0.0859  -0.0641 348 ARG A CG  
2541 C CD  . ARG A 342 ? 0.2241 0.2925 0.3452 0.0290  0.0839  -0.0631 348 ARG A CD  
2542 N NE  . ARG A 342 ? 0.2011 0.2651 0.3241 0.0400  0.0707  -0.0531 348 ARG A NE  
2543 C CZ  . ARG A 342 ? 0.2389 0.3079 0.3714 0.0429  0.0662  -0.0503 348 ARG A CZ  
2544 N NH1 . ARG A 342 ? 0.2301 0.3096 0.3726 0.0361  0.0731  -0.0567 348 ARG A NH1 
2545 N NH2 . ARG A 342 ? 0.2467 0.3100 0.3765 0.0514  0.0538  -0.0410 348 ARG A NH2 
2546 N N   . LEU A 343 ? 0.1576 0.2229 0.2863 0.0420  0.0790  -0.0673 349 LEU A N   
2547 C CA  . LEU A 343 ? 0.1832 0.2456 0.3148 0.0483  0.0745  -0.0657 349 LEU A CA  
2548 C C   . LEU A 343 ? 0.1925 0.2499 0.3158 0.0443  0.0797  -0.0696 349 LEU A C   
2549 O O   . LEU A 343 ? 0.1615 0.2122 0.2794 0.0491  0.0746  -0.0653 349 LEU A O   
2550 C CB  . LEU A 343 ? 0.1839 0.2540 0.3312 0.0495  0.0759  -0.0712 349 LEU A CB  
2551 C CG  . LEU A 343 ? 0.1960 0.2626 0.3474 0.0548  0.0739  -0.0723 349 LEU A CG  
2552 C CD1 . LEU A 343 ? 0.2665 0.3239 0.4106 0.0636  0.0638  -0.0626 349 LEU A CD1 
2553 C CD2 . LEU A 343 ? 0.2310 0.3060 0.3998 0.0558  0.0759  -0.0798 349 LEU A CD2 
2554 N N   . MET A 344 ? 0.1935 0.2537 0.3135 0.0341  0.0906  -0.0783 350 MET A N   
2555 C CA  . MET A 344 ? 0.1890 0.2443 0.2992 0.0290  0.0962  -0.0828 350 MET A CA  
2556 C C   . MET A 344 ? 0.1796 0.2262 0.2753 0.0313  0.0919  -0.0777 350 MET A C   
2557 O O   . MET A 344 ? 0.1792 0.2212 0.2717 0.0342  0.0891  -0.0766 350 MET A O   
2558 C CB  . MET A 344 ? 0.2322 0.2905 0.3357 0.0153  0.1090  -0.0928 350 MET A CB  
2559 C CG  . MET A 344 ? 0.2483 0.3015 0.3394 0.0085  0.1151  -0.0981 350 MET A CG  
2560 S SD  . MET A 344 ? 0.4216 0.4768 0.5288 0.0158  0.1120  -0.1000 350 MET A SD  
2561 C CE  . MET A 344 ? 0.4281 0.4786 0.5199 0.0047  0.1212  -0.1080 350 MET A CE  
2562 N N   . VAL A 345 ? 0.1779 0.2219 0.2650 0.0299  0.0914  -0.0754 351 VAL A N   
2563 C CA  . VAL A 345 ? 0.1799 0.2156 0.2544 0.0326  0.0869  -0.0724 351 VAL A CA  
2564 C C   . VAL A 345 ? 0.1676 0.2022 0.2492 0.0435  0.0747  -0.0637 351 VAL A C   
2565 O O   . VAL A 345 ? 0.1611 0.1912 0.2369 0.0456  0.0712  -0.0631 351 VAL A O   
2566 C CB  . VAL A 345 ? 0.2166 0.2455 0.2742 0.0276  0.0838  -0.0683 351 VAL A CB  
2567 C CG1 . VAL A 345 ? 0.2016 0.2199 0.2428 0.0311  0.0707  -0.0610 351 VAL A CG1 
2568 C CG2 . VAL A 345 ? 0.2203 0.2444 0.2575 0.0121  0.0926  -0.0730 351 VAL A CG2 
2569 N N   . ARG A 346 ? 0.1527 0.1910 0.2441 0.0490  0.0684  -0.0576 352 ARG A N   
2570 C CA  . ARG A 346 ? 0.1876 0.2228 0.2790 0.0564  0.0586  -0.0499 352 ARG A CA  
2571 C C   . ARG A 346 ? 0.1709 0.2032 0.2619 0.0568  0.0597  -0.0519 352 ARG A C   
2572 O O   . ARG A 346 ? 0.1645 0.1922 0.2495 0.0586  0.0559  -0.0496 352 ARG A O   
2573 C CB  . ARG A 346 ? 0.1565 0.1950 0.2547 0.0605  0.0534  -0.0449 352 ARG A CB  
2574 C CG  . ARG A 346 ? 0.1688 0.2026 0.2623 0.0660  0.0452  -0.0383 352 ARG A CG  
2575 C CD  . ARG A 346 ? 0.1713 0.2069 0.2675 0.0697  0.0400  -0.0336 352 ARG A CD  
2576 N NE  . ARG A 346 ? 0.1684 0.2091 0.2759 0.0702  0.0433  -0.0374 352 ARG A NE  
2577 C CZ  . ARG A 346 ? 0.1744 0.2223 0.2903 0.0687  0.0452  -0.0391 352 ARG A CZ  
2578 N NH1 . ARG A 346 ? 0.1568 0.2066 0.2706 0.0667  0.0441  -0.0370 352 ARG A NH1 
2579 N NH2 . ARG A 346 ? 0.1688 0.2221 0.2966 0.0693  0.0480  -0.0438 352 ARG A NH2 
2580 N N   . LEU A 347 ? 0.1628 0.1980 0.2610 0.0546  0.0654  -0.0571 353 LEU A N   
2581 C CA  . LEU A 347 ? 0.1987 0.2302 0.2976 0.0554  0.0666  -0.0595 353 LEU A CA  
2582 C C   . LEU A 347 ? 0.1945 0.2232 0.2853 0.0503  0.0713  -0.0642 353 LEU A C   
2583 O O   . LEU A 347 ? 0.2041 0.2280 0.2917 0.0516  0.0695  -0.0636 353 LEU A O   
2584 C CB  . LEU A 347 ? 0.1919 0.2273 0.3021 0.0550  0.0713  -0.0649 353 LEU A CB  
2585 C CG  . LEU A 347 ? 0.2753 0.3123 0.3942 0.0614  0.0659  -0.0615 353 LEU A CG  
2586 C CD1 . LEU A 347 ? 0.2799 0.3199 0.4112 0.0623  0.0699  -0.0683 353 LEU A CD1 
2587 C CD2 . LEU A 347 ? 0.3206 0.3496 0.4327 0.0678  0.0574  -0.0537 353 LEU A CD2 
2588 N N   . THR A 348 ? 0.1735 0.2046 0.2595 0.0436  0.0780  -0.0698 354 THR A N   
2589 C CA  . THR A 348 ? 0.1801 0.2080 0.2557 0.0380  0.0826  -0.0755 354 THR A CA  
2590 C C   . THR A 348 ? 0.2100 0.2339 0.2767 0.0406  0.0766  -0.0728 354 THR A C   
2591 O O   . THR A 348 ? 0.1822 0.2033 0.2443 0.0398  0.0760  -0.0752 354 THR A O   
2592 C CB  . THR A 348 ? 0.2012 0.2307 0.2688 0.0282  0.0923  -0.0832 354 THR A CB  
2593 O OG1 . THR A 348 ? 0.1963 0.2318 0.2753 0.0259  0.0974  -0.0863 354 THR A OG1 
2594 C CG2 . THR A 348 ? 0.2057 0.2313 0.2603 0.0211  0.0975  -0.0901 354 THR A CG2 
2595 N N   . LYS A 349 ? 0.1535 0.1927 0.2073 0.0483  0.0446  -0.0395 355 LYS A N   
2596 C CA  . LYS A 349 ? 0.1840 0.2158 0.2141 0.0451  0.0447  -0.0288 355 LYS A CA  
2597 C C   . LYS A 349 ? 0.1930 0.2183 0.2288 0.0428  0.0429  -0.0235 355 LYS A C   
2598 O O   . LYS A 349 ? 0.1474 0.1750 0.1845 0.0390  0.0389  -0.0279 355 LYS A O   
2599 C CB  . LYS A 349 ? 0.1592 0.1952 0.1793 0.0373  0.0481  -0.0298 355 LYS A CB  
2600 C CG  . LYS A 349 ? 0.2035 0.2320 0.2094 0.0338  0.0451  -0.0198 355 LYS A CG  
2601 C CD  . LYS A 349 ? 0.2063 0.2406 0.2050 0.0282  0.0466  -0.0199 355 LYS A CD  
2602 C CE  . LYS A 349 ? 0.2292 0.2777 0.2336 0.0190  0.0379  -0.0251 355 LYS A CE  
2603 N NZ  . LYS A 349 ? 0.2756 0.3237 0.2694 0.0187  0.0433  -0.0166 355 LYS A NZ  
2604 N N   . SER A 350 ? 0.1470 0.1810 0.1909 0.0458  0.0404  -0.0261 356 SER A N   
2605 C CA  . SER A 350 ? 0.1930 0.2322 0.2291 0.0454  0.0354  -0.0265 356 SER A CA  
2606 C C   . SER A 350 ? 0.1788 0.2197 0.2069 0.0578  0.0278  -0.0215 356 SER A C   
2607 O O   . SER A 350 ? 0.1613 0.2007 0.1664 0.0569  0.0310  -0.0165 356 SER A O   
2608 C CB  . SER A 350 ? 0.1720 0.2227 0.2128 0.0484  0.0320  -0.0299 356 SER A CB  
2609 O OG  . SER A 350 ? 0.1425 0.1893 0.1824 0.0414  0.0391  -0.0298 356 SER A OG  
2610 N N   . ARG A 351 ? 0.2250 0.2642 0.2722 0.0692  0.0182  -0.0202 357 ARG A N   
2611 C CA  . ARG A 351 ? 0.2221 0.2459 0.2556 0.0672  0.0041  -0.0049 357 ARG A CA  
2612 C C   . ARG A 351 ? 0.2430 0.2547 0.2576 0.0625  0.0124  0.0002  357 ARG A C   
2613 O O   . ARG A 351 ? 0.2410 0.2459 0.2277 0.0535  0.0120  0.0095  357 ARG A O   
2614 C CB  . ARG A 351 ? 0.2469 0.2647 0.3126 0.0758  -0.0139 -0.0009 357 ARG A CB  
2615 C CG  . ARG A 351 ? 0.2856 0.3143 0.3669 0.0779  -0.0302 0.0007  357 ARG A CG  
2616 C CD  . ARG A 351 ? 0.3607 0.3835 0.4842 0.0879  -0.0528 0.0068  357 ARG A CD  
2617 N NE  . ARG A 351 ? 0.4234 0.4252 0.5261 0.0821  -0.0765 0.0313  357 ARG A NE  
2618 C CZ  . ARG A 351 ? 0.4343 0.4135 0.5283 0.0808  -0.0787 0.0420  357 ARG A CZ  
2619 N NH1 . ARG A 351 ? 0.4430 0.4187 0.5479 0.0853  -0.0590 0.0292  357 ARG A NH1 
2620 N NH2 . ARG A 351 ? 0.4301 0.3888 0.5014 0.0720  -0.1022 0.0666  357 ARG A NH2 
2621 N N   . ASP A 352 ? 0.1868 0.1965 0.2159 0.0658  0.0210  -0.0073 358 ASP A N   
2622 C CA  . ASP A 352 ? 0.2294 0.2283 0.2456 0.0609  0.0264  -0.0028 358 ASP A CA  
2623 C C   . ASP A 352 ? 0.2314 0.2394 0.2406 0.0543  0.0392  -0.0097 358 ASP A C   
2624 O O   . ASP A 352 ? 0.1893 0.1923 0.1890 0.0509  0.0443  -0.0058 358 ASP A O   
2625 C CB  . ASP A 352 ? 0.2671 0.2525 0.3047 0.0654  0.0217  -0.0044 358 ASP A CB  
2626 C CG  . ASP A 352 ? 0.3851 0.3570 0.4087 0.0582  0.0255  0.0015  358 ASP A CG  
2627 O OD1 . ASP A 352 ? 0.4579 0.4210 0.4592 0.0509  0.0211  0.0152  358 ASP A OD1 
2628 O OD2 . ASP A 352 ? 0.3755 0.3460 0.4087 0.0571  0.0337  -0.0086 358 ASP A OD2 
2629 N N   . LEU A 353 ? 0.1865 0.2055 0.2027 0.0451  0.0380  -0.0181 359 LEU A N   
2630 C CA  . LEU A 353 ? 0.1923 0.2166 0.2041 0.0339  0.0392  -0.0205 359 LEU A CA  
2631 C C   . LEU A 353 ? 0.1889 0.2126 0.1992 0.0325  0.0416  -0.0225 359 LEU A C   
2632 O O   . LEU A 353 ? 0.1505 0.1754 0.1544 0.0282  0.0429  -0.0186 359 LEU A O   
2633 C CB  . LEU A 353 ? 0.1841 0.2082 0.1876 0.0309  0.0393  -0.0145 359 LEU A CB  
2634 C CG  . LEU A 353 ? 0.2043 0.2306 0.2074 0.0304  0.0386  -0.0156 359 LEU A CG  
2635 C CD1 . LEU A 353 ? 0.2164 0.2433 0.2131 0.0279  0.0417  -0.0141 359 LEU A CD1 
2636 C CD2 . LEU A 353 ? 0.1818 0.2115 0.1909 0.0263  0.0384  -0.0196 359 LEU A CD2 
2637 N N   . PHE A 354 ? 0.1892 0.2105 0.2068 0.0380  0.0423  -0.0287 360 PHE A N   
2638 C CA  . PHE A 354 ? 0.2459 0.2620 0.2598 0.0368  0.0472  -0.0319 360 PHE A CA  
2639 C C   . PHE A 354 ? 0.2074 0.2130 0.2168 0.0352  0.0516  -0.0256 360 PHE A C   
2640 O O   . PHE A 354 ? 0.2081 0.2102 0.2144 0.0294  0.0570  -0.0300 360 PHE A O   
2641 C CB  . PHE A 354 ? 0.2335 0.2560 0.2353 0.0289  0.0508  -0.0334 360 PHE A CB  
2642 C CG  . PHE A 354 ? 0.2284 0.2542 0.2303 0.0288  0.0514  -0.0352 360 PHE A CG  
2643 C CD1 . PHE A 354 ? 0.2296 0.2530 0.2453 0.0301  0.0543  -0.0445 360 PHE A CD1 
2644 C CD2 . PHE A 354 ? 0.2355 0.2665 0.2285 0.0262  0.0502  -0.0290 360 PHE A CD2 
2645 C CE1 . PHE A 354 ? 0.2532 0.2821 0.2728 0.0272  0.0566  -0.0483 360 PHE A CE1 
2646 C CE2 . PHE A 354 ? 0.2218 0.2544 0.2162 0.0235  0.0526  -0.0317 360 PHE A CE2 
2647 C CZ  . PHE A 354 ? 0.2347 0.2677 0.2419 0.0234  0.0558  -0.0417 360 PHE A CZ  
2648 N N   . VAL A 355 ? 0.2301 0.2295 0.2353 0.0397  0.0514  -0.0153 361 VAL A N   
2649 C CA  . VAL A 355 ? 0.2448 0.2387 0.2420 0.0354  0.0547  -0.0076 361 VAL A CA  
2650 C C   . VAL A 355 ? 0.2373 0.2160 0.2392 0.0320  0.0535  -0.0096 361 VAL A C   
2651 O O   . VAL A 355 ? 0.2265 0.2057 0.2256 0.0237  0.0560  -0.0097 361 VAL A O   
2652 C CB  . VAL A 355 ? 0.2451 0.2369 0.2321 0.0350  0.0532  0.0022  361 VAL A CB  
2653 C CG1 . VAL A 355 ? 0.2439 0.2289 0.2236 0.0257  0.0557  0.0087  361 VAL A CG1 
2654 C CG2 . VAL A 355 ? 0.2004 0.2075 0.1870 0.0338  0.0545  0.0004  361 VAL A CG2 
2655 N N   . SER A 356 ? 0.2590 0.2240 0.2733 0.0382  0.0486  -0.0118 362 SER A N   
2656 C CA  . SER A 356 ? 0.2577 0.2037 0.2816 0.0355  0.0469  -0.0136 362 SER A CA  
2657 C C   . SER A 356 ? 0.2633 0.2136 0.2909 0.0282  0.0558  -0.0296 362 SER A C   
2658 O O   . SER A 356 ? 0.2411 0.1792 0.2698 0.0209  0.0568  -0.0313 362 SER A O   
2659 C CB  . SER A 356 ? 0.2972 0.2275 0.3445 0.0457  0.0378  -0.0137 362 SER A CB  
2660 O OG  . SER A 356 ? 0.4029 0.3455 0.4705 0.0523  0.0432  -0.0309 362 SER A OG  
2661 N N   . THR A 357 ? 0.2651 0.2317 0.2913 0.0268  0.0622  -0.0416 363 THR A N   
2662 C CA  . THR A 357 ? 0.2836 0.2536 0.3061 0.0148  0.0704  -0.0577 363 THR A CA  
2663 C C   . THR A 357 ? 0.2685 0.2440 0.2732 0.0024  0.0681  -0.0504 363 THR A C   
2664 O O   . THR A 357 ? 0.2686 0.2411 0.2691 -0.0100 0.0716  -0.0609 363 THR A O   
2665 C CB  . THR A 357 ? 0.3178 0.3049 0.3335 0.0099  0.0713  -0.0644 363 THR A CB  
2666 O OG1 . THR A 357 ? 0.3069 0.3073 0.3046 0.0072  0.0681  -0.0533 363 THR A OG1 
2667 C CG2 . THR A 357 ? 0.2682 0.2565 0.3023 0.0204  0.0672  -0.0660 363 THR A CG2 
2668 N N   . SER A 358 ? 0.2218 0.2066 0.2197 0.0045  0.0626  -0.0347 364 SER A N   
2669 C CA  . SER A 358 ? 0.2537 0.2472 0.2459 -0.0057 0.0591  -0.0279 364 SER A CA  
2670 C C   . SER A 358 ? 0.2495 0.2305 0.2470 -0.0094 0.0593  -0.0242 364 SER A C   
2671 O O   . SER A 358 ? 0.2433 0.2260 0.2397 -0.0214 0.0584  -0.0273 364 SER A O   
2672 C CB  . SER A 358 ? 0.2332 0.2419 0.2273 -0.0014 0.0553  -0.0159 364 SER A CB  
2673 O OG  . SER A 358 ? 0.2346 0.2532 0.2230 -0.0013 0.0533  -0.0169 364 SER A OG  
2674 N N   . TRP A 359 ? 0.2453 0.2130 0.2458 -0.0019 0.0592  -0.0166 365 TRP A N   
2675 C CA  . TRP A 359 ? 0.2401 0.1907 0.2420 -0.0083 0.0592  -0.0117 365 TRP A CA  
2676 C C   . TRP A 359 ? 0.2706 0.2041 0.2801 -0.0128 0.0605  -0.0242 365 TRP A C   
2677 O O   . TRP A 359 ? 0.2844 0.2109 0.2946 -0.0242 0.0616  -0.0255 365 TRP A O   
2678 C CB  . TRP A 359 ? 0.2618 0.1979 0.2593 -0.0027 0.0560  0.0012  365 TRP A CB  
2679 C CG  . TRP A 359 ? 0.2410 0.1935 0.2293 -0.0039 0.0591  0.0092  365 TRP A CG  
2680 C CD1 . TRP A 359 ? 0.2519 0.2162 0.2374 0.0045  0.0590  0.0099  365 TRP A CD1 
2681 C CD2 . TRP A 359 ? 0.2441 0.2049 0.2298 -0.0152 0.0654  0.0137  365 TRP A CD2 
2682 N NE1 . TRP A 359 ? 0.2153 0.1929 0.1967 -0.0007 0.0653  0.0135  365 TRP A NE1 
2683 C CE2 . TRP A 359 ? 0.2441 0.2214 0.2274 -0.0127 0.0702  0.0151  365 TRP A CE2 
2684 C CE3 . TRP A 359 ? 0.2407 0.1972 0.2286 -0.0284 0.0689  0.0148  365 TRP A CE3 
2685 C CZ2 . TRP A 359 ? 0.2329 0.2239 0.2194 -0.0226 0.0803  0.0151  365 TRP A CZ2 
2686 C CZ3 . TRP A 359 ? 0.2415 0.2131 0.2315 -0.0386 0.0780  0.0166  365 TRP A CZ3 
2687 C CH2 . TRP A 359 ? 0.2263 0.2155 0.2171 -0.0354 0.0845  0.0156  365 TRP A CH2 
2688 N N   . LYS A 360 ? 0.2798 0.2081 0.2986 -0.0054 0.0622  -0.0364 366 LYS A N   
2689 C CA  . LYS A 360 ? 0.2994 0.2125 0.3308 -0.0106 0.0672  -0.0542 366 LYS A CA  
2690 C C   . LYS A 360 ? 0.2929 0.2195 0.3107 -0.0278 0.0720  -0.0662 366 LYS A C   
2691 O O   . LYS A 360 ? 0.3099 0.2252 0.3300 -0.0393 0.0740  -0.0732 366 LYS A O   
2692 C CB  . LYS A 360 ? 0.2985 0.2086 0.3494 0.0002  0.0712  -0.0691 366 LYS A CB  
2693 C CG  . LYS A 360 ? 0.3969 0.2900 0.4706 -0.0039 0.0795  -0.0922 366 LYS A CG  
2694 C CD  . LYS A 360 ? 0.4167 0.3247 0.5097 0.0036  0.0808  -0.1030 366 LYS A CD  
2695 C CE  . LYS A 360 ? 0.5233 0.4247 0.6407 -0.0008 0.0863  -0.1201 366 LYS A CE  
2696 N NZ  . LYS A 360 ? 0.6467 0.5664 0.7837 0.0013  0.0918  -0.1333 366 LYS A NZ  
2697 N N   . THR A 361 ? 0.2513 0.2012 0.2538 -0.0319 0.0717  -0.0671 367 THR A N   
2698 C CA  . THR A 361 ? 0.3089 0.2720 0.2943 -0.0510 0.0708  -0.0740 367 THR A CA  
2699 C C   . THR A 361 ? 0.3119 0.2767 0.2986 -0.0598 0.0644  -0.0637 367 THR A C   
2700 O O   . THR A 361 ? 0.3105 0.2728 0.2923 -0.0762 0.0651  -0.0741 367 THR A O   
2701 C CB  . THR A 361 ? 0.3029 0.2882 0.2717 -0.0538 0.0657  -0.0676 367 THR A CB  
2702 O OG1 . THR A 361 ? 0.3030 0.2883 0.2677 -0.0521 0.0747  -0.0816 367 THR A OG1 
2703 C CG2 . THR A 361 ? 0.3003 0.2994 0.2502 -0.0753 0.0576  -0.0673 367 THR A CG2 
2704 N N   . MET A 362 ? 0.2790 0.2487 0.2733 -0.0510 0.0599  -0.0458 368 MET A N   
2705 C CA  . MET A 362 ? 0.2783 0.2536 0.2791 -0.0597 0.0566  -0.0374 368 MET A CA  
2706 C C   . MET A 362 ? 0.3087 0.2592 0.3159 -0.0631 0.0615  -0.0385 368 MET A C   
2707 O O   . MET A 362 ? 0.2861 0.2400 0.2989 -0.0729 0.0611  -0.0328 368 MET A O   
2708 C CB  . MET A 362 ? 0.2472 0.2391 0.2564 -0.0514 0.0543  -0.0223 368 MET A CB  
2709 C CG  . MET A 362 ? 0.2402 0.2547 0.2493 -0.0488 0.0467  -0.0187 368 MET A CG  
2710 S SD  . MET A 362 ? 0.2282 0.2634 0.2409 -0.0669 0.0332  -0.0183 368 MET A SD  
2711 C CE  . MET A 362 ? 0.1760 0.2278 0.2217 -0.0662 0.0334  -0.0092 368 MET A CE  
2712 N N   . ARG A 363 ? 0.3046 0.2303 0.3153 -0.0558 0.0653  -0.0452 369 ARG A N   
2713 C CA  . ARG A 363 ? 0.3246 0.2204 0.3442 -0.0584 0.0668  -0.0435 369 ARG A CA  
2714 C C   . ARG A 363 ? 0.3352 0.2294 0.3511 -0.0609 0.0651  -0.0236 369 ARG A C   
2715 O O   . ARG A 363 ? 0.3393 0.2242 0.3565 -0.0743 0.0668  -0.0204 369 ARG A O   
2716 C CB  . ARG A 363 ? 0.3679 0.2554 0.3907 -0.0750 0.0703  -0.0599 369 ARG A CB  
2717 C CG  . ARG A 363 ? 0.3742 0.2541 0.4020 -0.0743 0.0767  -0.0837 369 ARG A CG  
2718 C CD  . ARG A 363 ? 0.5221 0.3997 0.5464 -0.0950 0.0819  -0.1044 369 ARG A CD  
2719 N NE  . ARG A 363 ? 0.5675 0.4762 0.5713 -0.1098 0.0760  -0.1020 369 ARG A NE  
2720 C CZ  . ARG A 363 ? 0.5452 0.4637 0.5480 -0.1229 0.0698  -0.0936 369 ARG A CZ  
2721 N NH1 . ARG A 363 ? 0.6119 0.5107 0.6275 -0.1265 0.0718  -0.0888 369 ARG A NH1 
2722 N NH2 . ARG A 363 ? 0.4727 0.4215 0.4643 -0.1336 0.0602  -0.0890 369 ARG A NH2 
2723 N N   . GLN A 364 ? 0.3199 0.2246 0.3297 -0.0505 0.0637  -0.0121 370 GLN A N   
2724 C CA  . GLN A 364 ? 0.3195 0.2221 0.3209 -0.0546 0.0651  0.0040  370 GLN A CA  
2725 C C   . GLN A 364 ? 0.3214 0.2098 0.3147 -0.0425 0.0600  0.0147  370 GLN A C   
2726 O O   . GLN A 364 ? 0.3282 0.2169 0.3277 -0.0288 0.0561  0.0088  370 GLN A O   
2727 C CB  . GLN A 364 ? 0.2721 0.2085 0.2757 -0.0586 0.0700  0.0050  370 GLN A CB  
2728 C CG  . GLN A 364 ? 0.2711 0.2238 0.2874 -0.0728 0.0720  -0.0013 370 GLN A CG  
2729 C CD  . GLN A 364 ? 0.2538 0.2410 0.2850 -0.0734 0.0747  -0.0007 370 GLN A CD  
2730 O OE1 . GLN A 364 ? 0.2499 0.2436 0.2808 -0.0735 0.0828  0.0046  370 GLN A OE1 
2731 N NE2 . GLN A 364 ? 0.2266 0.2358 0.2723 -0.0747 0.0672  -0.0066 370 GLN A NE2 
2732 N N   . SER A 365 ? 0.3393 0.2159 0.3176 -0.0505 0.0599  0.0302  371 SER A N   
2733 C CA  . SER A 365 ? 0.3624 0.2250 0.3269 -0.0446 0.0519  0.0439  371 SER A CA  
2734 C C   . SER A 365 ? 0.3627 0.2483 0.3097 -0.0496 0.0599  0.0479  371 SER A C   
2735 O O   . SER A 365 ? 0.3624 0.2591 0.3033 -0.0650 0.0713  0.0479  371 SER A O   
2736 C CB  . SER A 365 ? 0.4070 0.2316 0.3618 -0.0548 0.0428  0.0611  371 SER A CB  
2737 O OG  . SER A 365 ? 0.4496 0.2495 0.4291 -0.0461 0.0343  0.0558  371 SER A OG  
2738 N N   . PRO A 366 ? 0.3449 0.2391 0.2870 -0.0382 0.0561  0.0486  372 PRO A N   
2739 C CA  . PRO A 366 ? 0.3534 0.2707 0.2836 -0.0426 0.0662  0.0469  372 PRO A CA  
2740 C C   . PRO A 366 ? 0.4064 0.3120 0.3060 -0.0630 0.0705  0.0594  372 PRO A C   
2741 O O   . PRO A 366 ? 0.4547 0.3301 0.3370 -0.0709 0.0589  0.0756  372 PRO A O   
2742 C CB  . PRO A 366 ? 0.3596 0.2823 0.2909 -0.0266 0.0585  0.0452  372 PRO A CB  
2743 C CG  . PRO A 366 ? 0.3565 0.2552 0.2964 -0.0169 0.0431  0.0506  372 PRO A CG  
2744 C CD  . PRO A 366 ? 0.3572 0.2441 0.3117 -0.0206 0.0446  0.0462  372 PRO A CD  
2745 N N   . PRO A 367 ? 0.4360 0.3648 0.3302 -0.0739 0.0871  0.0519  373 PRO A N   
2746 C CA  . PRO A 367 ? 0.4707 0.3984 0.3429 -0.0904 0.0879  0.0572  373 PRO A CA  
2747 C C   . PRO A 367 ? 0.5508 0.4729 0.3970 -0.0901 0.0790  0.0643  373 PRO A C   
2748 O O   . PRO A 367 ? 0.5818 0.5107 0.4335 -0.0764 0.0759  0.0604  373 PRO A O   
2749 C CB  . PRO A 367 ? 0.4507 0.4113 0.3447 -0.0939 0.1046  0.0388  373 PRO A CB  
2750 C CG  . PRO A 367 ? 0.3966 0.3786 0.3192 -0.0753 0.1063  0.0266  373 PRO A CG  
2751 C CD  . PRO A 367 ? 0.3823 0.3461 0.3057 -0.0645 0.0974  0.0340  373 PRO A CD  
2752 O OXT . PRO A 367 ? 0.6385 0.5490 0.4573 -0.1043 0.0737  0.0740  373 PRO A OXT 
# 
