data_8QRA
# 
_entry.id   8QRA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QRA         pdb_00008qra 10.2210/pdb8qra/pdb 
WWPDB D_1292133754 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QRA 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              gilles.labesse@cbs.cnrs.fr 
_pdbx_contact_author.name_first         Gilles 
_pdbx_contact_author.name_last          Labesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6861-3300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gelin, M.'   1 ? 
'Labesse, G.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Guichou, J.-F.' 3 ? 
primary 'Pons, J.-L.'    4 ? 
primary 'Barluenga, S.'  5 ? 
primary 'Katickeyan, G.' 6 ? 
primary 'Winssinger, N.' 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 'Mitogen-activated protein kinase 1' 42311.668 1   ? ? ? ? 
2 non-polymer syn 'SULFATE ION' 96.063    2   ? ? ? ? 
3 non-polymer syn 
'(4~{R},5~{S},6~{S})-4,5,6,15,17-pentakis(oxidanyl)-2,12-dioxabicyclo[12.4.0]octadeca-1(14),15,17-triene-7,13-dione' 356.325   1   
? ? ? ? 
4 water       nat water 18.015    255 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;HHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILL
RFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLL
LNTT(CME)DLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKH
YLDQLNHILGILGSPSQEDLN(CME)IINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQAL
AHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILL
RFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLL
LNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQ
LNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQY
YDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_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 '(4~{R},5~{S},6~{S})-4,5,6,15,17-pentakis(oxidanyl)-2,12-dioxabicyclo[12.4.0]octadeca-1(14),15,17-triene-7,13-dione' WM6 
4 water                                                                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   MET n 
1 8   ALA n 
1 9   ALA n 
1 10  ALA n 
1 11  ALA n 
1 12  ALA n 
1 13  ALA n 
1 14  GLY n 
1 15  PRO n 
1 16  GLU n 
1 17  MET n 
1 18  VAL n 
1 19  ARG n 
1 20  GLY n 
1 21  GLN n 
1 22  VAL n 
1 23  PHE n 
1 24  ASP n 
1 25  VAL n 
1 26  GLY n 
1 27  PRO n 
1 28  ARG n 
1 29  TYR n 
1 30  THR n 
1 31  ASN n 
1 32  LEU n 
1 33  SER n 
1 34  TYR n 
1 35  ILE n 
1 36  GLY n 
1 37  GLU n 
1 38  GLY n 
1 39  ALA n 
1 40  TYR n 
1 41  GLY n 
1 42  MET n 
1 43  VAL n 
1 44  CYS n 
1 45  SER n 
1 46  ALA n 
1 47  TYR n 
1 48  ASP n 
1 49  ASN n 
1 50  LEU n 
1 51  ASN n 
1 52  LYS n 
1 53  VAL n 
1 54  ARG n 
1 55  VAL n 
1 56  ALA n 
1 57  ILE n 
1 58  LYS n 
1 59  LYS n 
1 60  ILE n 
1 61  SER n 
1 62  PRO n 
1 63  PHE n 
1 64  GLU n 
1 65  HIS n 
1 66  GLN n 
1 67  THR n 
1 68  TYR n 
1 69  CYS n 
1 70  GLN n 
1 71  ARG n 
1 72  THR n 
1 73  LEU n 
1 74  ARG n 
1 75  GLU n 
1 76  ILE n 
1 77  LYS n 
1 78  ILE n 
1 79  LEU n 
1 80  LEU n 
1 81  ARG n 
1 82  PHE n 
1 83  ARG n 
1 84  HIS n 
1 85  GLU n 
1 86  ASN n 
1 87  ILE n 
1 88  ILE n 
1 89  GLY n 
1 90  ILE n 
1 91  ASN n 
1 92  ASP n 
1 93  ILE n 
1 94  ILE n 
1 95  ARG n 
1 96  ALA n 
1 97  PRO n 
1 98  THR n 
1 99  ILE n 
1 100 GLU n 
1 101 GLN n 
1 102 MET n 
1 103 LYS n 
1 104 ASP n 
1 105 VAL n 
1 106 TYR n 
1 107 ILE n 
1 108 VAL n 
1 109 GLN n 
1 110 ASP n 
1 111 LEU n 
1 112 MET n 
1 113 GLU n 
1 114 THR n 
1 115 ASP n 
1 116 LEU n 
1 117 TYR n 
1 118 LYS n 
1 119 LEU n 
1 120 LEU n 
1 121 LYS n 
1 122 THR n 
1 123 GLN n 
1 124 HIS n 
1 125 LEU n 
1 126 SER n 
1 127 ASN n 
1 128 ASP n 
1 129 HIS n 
1 130 ILE n 
1 131 CYS n 
1 132 TYR n 
1 133 PHE n 
1 134 LEU n 
1 135 TYR n 
1 136 GLN n 
1 137 ILE n 
1 138 LEU n 
1 139 ARG n 
1 140 GLY n 
1 141 LEU n 
1 142 LYS n 
1 143 TYR n 
1 144 ILE n 
1 145 HIS n 
1 146 SER n 
1 147 ALA n 
1 148 ASN n 
1 149 VAL n 
1 150 LEU n 
1 151 HIS n 
1 152 ARG n 
1 153 ASP n 
1 154 LEU n 
1 155 LYS n 
1 156 PRO n 
1 157 SER n 
1 158 ASN n 
1 159 LEU n 
1 160 LEU n 
1 161 LEU n 
1 162 ASN n 
1 163 THR n 
1 164 THR n 
1 165 CME n 
1 166 ASP n 
1 167 LEU n 
1 168 LYS n 
1 169 ILE n 
1 170 CYS n 
1 171 ASP n 
1 172 PHE n 
1 173 GLY n 
1 174 LEU n 
1 175 ALA n 
1 176 ARG n 
1 177 VAL n 
1 178 ALA n 
1 179 ASP n 
1 180 PRO n 
1 181 ASP n 
1 182 HIS n 
1 183 ASP n 
1 184 HIS n 
1 185 THR n 
1 186 GLY n 
1 187 PHE n 
1 188 LEU n 
1 189 THR n 
1 190 GLU n 
1 191 TYR n 
1 192 VAL n 
1 193 ALA n 
1 194 THR n 
1 195 ARG n 
1 196 TRP n 
1 197 TYR n 
1 198 ARG n 
1 199 ALA n 
1 200 PRO n 
1 201 GLU n 
1 202 ILE n 
1 203 MET n 
1 204 LEU n 
1 205 ASN n 
1 206 SER n 
1 207 LYS n 
1 208 GLY n 
1 209 TYR n 
1 210 THR n 
1 211 LYS n 
1 212 SER n 
1 213 ILE n 
1 214 ASP n 
1 215 ILE n 
1 216 TRP n 
1 217 SER n 
1 218 VAL n 
1 219 GLY n 
1 220 CYS n 
1 221 ILE n 
1 222 LEU n 
1 223 ALA n 
1 224 GLU n 
1 225 MET n 
1 226 LEU n 
1 227 SER n 
1 228 ASN n 
1 229 ARG n 
1 230 PRO n 
1 231 ILE n 
1 232 PHE n 
1 233 PRO n 
1 234 GLY n 
1 235 LYS n 
1 236 HIS n 
1 237 TYR n 
1 238 LEU n 
1 239 ASP n 
1 240 GLN n 
1 241 LEU n 
1 242 ASN n 
1 243 HIS n 
1 244 ILE n 
1 245 LEU n 
1 246 GLY n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 SER n 
1 251 PRO n 
1 252 SER n 
1 253 GLN n 
1 254 GLU n 
1 255 ASP n 
1 256 LEU n 
1 257 ASN n 
1 258 CME n 
1 259 ILE n 
1 260 ILE n 
1 261 ASN n 
1 262 LEU n 
1 263 LYS n 
1 264 ALA n 
1 265 ARG n 
1 266 ASN n 
1 267 TYR n 
1 268 LEU n 
1 269 LEU n 
1 270 SER n 
1 271 LEU n 
1 272 PRO n 
1 273 HIS n 
1 274 LYS n 
1 275 ASN n 
1 276 LYS n 
1 277 VAL n 
1 278 PRO n 
1 279 TRP n 
1 280 ASN n 
1 281 ARG n 
1 282 LEU n 
1 283 PHE n 
1 284 PRO n 
1 285 ASN n 
1 286 ALA n 
1 287 ASP n 
1 288 SER n 
1 289 LYS n 
1 290 ALA n 
1 291 LEU n 
1 292 ASP n 
1 293 LEU n 
1 294 LEU n 
1 295 ASP n 
1 296 LYS n 
1 297 MET n 
1 298 LEU n 
1 299 THR n 
1 300 PHE n 
1 301 ASN n 
1 302 PRO n 
1 303 HIS n 
1 304 LYS n 
1 305 ARG n 
1 306 ILE n 
1 307 GLU n 
1 308 VAL n 
1 309 GLU n 
1 310 GLN n 
1 311 ALA n 
1 312 LEU n 
1 313 ALA n 
1 314 HIS n 
1 315 PRO n 
1 316 TYR n 
1 317 LEU n 
1 318 GLU n 
1 319 GLN n 
1 320 TYR n 
1 321 TYR n 
1 322 ASP n 
1 323 PRO n 
1 324 SER n 
1 325 ASP n 
1 326 GLU n 
1 327 PRO n 
1 328 ILE n 
1 329 ALA n 
1 330 GLU n 
1 331 ALA n 
1 332 PRO n 
1 333 PHE n 
1 334 LYS n 
1 335 PHE n 
1 336 ASP n 
1 337 MET n 
1 338 GLU n 
1 339 LEU n 
1 340 ASP n 
1 341 ASP n 
1 342 LEU n 
1 343 PRO n 
1 344 LYS n 
1 345 GLU n 
1 346 LYS n 
1 347 LEU n 
1 348 LYS n 
1 349 GLU n 
1 350 LEU n 
1 351 ILE n 
1 352 PHE n 
1 353 GLU n 
1 354 GLU n 
1 355 THR n 
1 356 ALA n 
1 357 ARG n 
1 358 PHE n 
1 359 GLN n 
1 360 PRO n 
1 361 GLY n 
1 362 TYR n 
1 363 ARG n 
1 364 SER 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                   364 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Mapk1 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ? 'C5 H11 N O3 S2' 197.276 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION' ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
WM6 non-polymer         . 
'(4~{R},5~{S},6~{S})-4,5,6,15,17-pentakis(oxidanyl)-2,12-dioxabicyclo[12.4.0]octadeca-1(14),15,17-triene-7,13-dione' ? 
'C16 H20 O9'     356.325 
# 
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   HIS 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   MET 7   1   ?   ?   ?   A . n 
A 1 8   ALA 8   2   ?   ?   ?   A . n 
A 1 9   ALA 9   3   ?   ?   ?   A . n 
A 1 10  ALA 10  4   ?   ?   ?   A . n 
A 1 11  ALA 11  5   ?   ?   ?   A . n 
A 1 12  ALA 12  6   ?   ?   ?   A . n 
A 1 13  ALA 13  7   ?   ?   ?   A . n 
A 1 14  GLY 14  8   ?   ?   ?   A . n 
A 1 15  PRO 15  9   9   PRO PRO A . n 
A 1 16  GLU 16  10  10  GLU GLU A . n 
A 1 17  MET 17  11  11  MET MET A . n 
A 1 18  VAL 18  12  12  VAL VAL A . n 
A 1 19  ARG 19  13  13  ARG ARG A . n 
A 1 20  GLY 20  14  14  GLY GLY A . n 
A 1 21  GLN 21  15  15  GLN GLN A . n 
A 1 22  VAL 22  16  16  VAL VAL A . n 
A 1 23  PHE 23  17  17  PHE PHE A . n 
A 1 24  ASP 24  18  18  ASP ASP A . n 
A 1 25  VAL 25  19  19  VAL VAL A . n 
A 1 26  GLY 26  20  20  GLY GLY A . n 
A 1 27  PRO 27  21  21  PRO PRO A . n 
A 1 28  ARG 28  22  22  ARG ARG A . n 
A 1 29  TYR 29  23  23  TYR TYR A . n 
A 1 30  THR 30  24  24  THR THR A . n 
A 1 31  ASN 31  25  25  ASN ASN A . n 
A 1 32  LEU 32  26  26  LEU LEU A . n 
A 1 33  SER 33  27  27  SER SER A . n 
A 1 34  TYR 34  28  28  TYR TYR A . n 
A 1 35  ILE 35  29  29  ILE ILE A . n 
A 1 36  GLY 36  30  30  GLY GLY A . n 
A 1 37  GLU 37  31  31  GLU GLU A . n 
A 1 38  GLY 38  32  32  GLY GLY A . n 
A 1 39  ALA 39  33  33  ALA ALA A . n 
A 1 40  TYR 40  34  34  TYR TYR A . n 
A 1 41  GLY 41  35  35  GLY GLY A . n 
A 1 42  MET 42  36  36  MET MET A . n 
A 1 43  VAL 43  37  37  VAL VAL A . n 
A 1 44  CYS 44  38  38  CYS CYS A . n 
A 1 45  SER 45  39  39  SER SER A . n 
A 1 46  ALA 46  40  40  ALA ALA A . n 
A 1 47  TYR 47  41  41  TYR TYR A . n 
A 1 48  ASP 48  42  42  ASP ASP A . n 
A 1 49  ASN 49  43  43  ASN ASN A . n 
A 1 50  LEU 50  44  44  LEU LEU A . n 
A 1 51  ASN 51  45  45  ASN ASN A . n 
A 1 52  LYS 52  46  46  LYS LYS A . n 
A 1 53  VAL 53  47  47  VAL VAL A . n 
A 1 54  ARG 54  48  48  ARG ARG A . n 
A 1 55  VAL 55  49  49  VAL VAL A . n 
A 1 56  ALA 56  50  50  ALA ALA A . n 
A 1 57  ILE 57  51  51  ILE ILE A . n 
A 1 58  LYS 58  52  52  LYS LYS A . n 
A 1 59  LYS 59  53  53  LYS LYS A . n 
A 1 60  ILE 60  54  54  ILE ILE A . n 
A 1 61  SER 61  55  55  SER SER A . n 
A 1 62  PRO 62  56  56  PRO PRO A . n 
A 1 63  PHE 63  57  57  PHE PHE A . n 
A 1 64  GLU 64  58  58  GLU GLU A . n 
A 1 65  HIS 65  59  59  HIS HIS A . n 
A 1 66  GLN 66  60  60  GLN GLN A . n 
A 1 67  THR 67  61  61  THR THR A . n 
A 1 68  TYR 68  62  62  TYR TYR A . n 
A 1 69  CYS 69  63  63  CYS CYS A . n 
A 1 70  GLN 70  64  64  GLN GLN A . n 
A 1 71  ARG 71  65  65  ARG ARG A . n 
A 1 72  THR 72  66  66  THR THR A . n 
A 1 73  LEU 73  67  67  LEU LEU A . n 
A 1 74  ARG 74  68  68  ARG ARG A . n 
A 1 75  GLU 75  69  69  GLU GLU A . n 
A 1 76  ILE 76  70  70  ILE ILE A . n 
A 1 77  LYS 77  71  71  LYS LYS A . n 
A 1 78  ILE 78  72  72  ILE ILE A . n 
A 1 79  LEU 79  73  73  LEU LEU A . n 
A 1 80  LEU 80  74  74  LEU LEU A . n 
A 1 81  ARG 81  75  75  ARG ARG A . n 
A 1 82  PHE 82  76  76  PHE PHE A . n 
A 1 83  ARG 83  77  77  ARG ARG A . n 
A 1 84  HIS 84  78  78  HIS HIS A . n 
A 1 85  GLU 85  79  79  GLU GLU A . n 
A 1 86  ASN 86  80  80  ASN ASN A . n 
A 1 87  ILE 87  81  81  ILE ILE A . n 
A 1 88  ILE 88  82  82  ILE ILE A . n 
A 1 89  GLY 89  83  83  GLY GLY A . n 
A 1 90  ILE 90  84  84  ILE ILE A . n 
A 1 91  ASN 91  85  85  ASN ASN A . n 
A 1 92  ASP 92  86  86  ASP ASP A . n 
A 1 93  ILE 93  87  87  ILE ILE A . n 
A 1 94  ILE 94  88  88  ILE ILE A . n 
A 1 95  ARG 95  89  89  ARG ARG A . n 
A 1 96  ALA 96  90  90  ALA ALA A . n 
A 1 97  PRO 97  91  91  PRO PRO A . n 
A 1 98  THR 98  92  92  THR THR A . n 
A 1 99  ILE 99  93  93  ILE ILE A . n 
A 1 100 GLU 100 94  94  GLU GLU A . n 
A 1 101 GLN 101 95  95  GLN GLN A . n 
A 1 102 MET 102 96  96  MET MET A . n 
A 1 103 LYS 103 97  97  LYS LYS A . n 
A 1 104 ASP 104 98  98  ASP ASP A . n 
A 1 105 VAL 105 99  99  VAL VAL A . n 
A 1 106 TYR 106 100 100 TYR TYR A . n 
A 1 107 ILE 107 101 101 ILE ILE A . n 
A 1 108 VAL 108 102 102 VAL VAL A . n 
A 1 109 GLN 109 103 103 GLN GLN A . n 
A 1 110 ASP 110 104 104 ASP ASP A . n 
A 1 111 LEU 111 105 105 LEU LEU A . n 
A 1 112 MET 112 106 106 MET MET A . n 
A 1 113 GLU 113 107 107 GLU GLU A . n 
A 1 114 THR 114 108 108 THR THR A . n 
A 1 115 ASP 115 109 109 ASP ASP A . n 
A 1 116 LEU 116 110 110 LEU LEU A . n 
A 1 117 TYR 117 111 111 TYR TYR A . n 
A 1 118 LYS 118 112 112 LYS LYS A . n 
A 1 119 LEU 119 113 113 LEU LEU A . n 
A 1 120 LEU 120 114 114 LEU LEU A . n 
A 1 121 LYS 121 115 115 LYS LYS A . n 
A 1 122 THR 122 116 116 THR THR A . n 
A 1 123 GLN 123 117 117 GLN GLN A . n 
A 1 124 HIS 124 118 118 HIS HIS A . n 
A 1 125 LEU 125 119 119 LEU LEU A . n 
A 1 126 SER 126 120 120 SER SER A . n 
A 1 127 ASN 127 121 121 ASN ASN A . n 
A 1 128 ASP 128 122 122 ASP ASP A . n 
A 1 129 HIS 129 123 123 HIS HIS A . n 
A 1 130 ILE 130 124 124 ILE ILE A . n 
A 1 131 CYS 131 125 125 CYS CYS A . n 
A 1 132 TYR 132 126 126 TYR TYR A . n 
A 1 133 PHE 133 127 127 PHE PHE A . n 
A 1 134 LEU 134 128 128 LEU LEU A . n 
A 1 135 TYR 135 129 129 TYR TYR A . n 
A 1 136 GLN 136 130 130 GLN GLN A . n 
A 1 137 ILE 137 131 131 ILE ILE A . n 
A 1 138 LEU 138 132 132 LEU LEU A . n 
A 1 139 ARG 139 133 133 ARG ARG A . n 
A 1 140 GLY 140 134 134 GLY GLY A . n 
A 1 141 LEU 141 135 135 LEU LEU A . n 
A 1 142 LYS 142 136 136 LYS LYS A . n 
A 1 143 TYR 143 137 137 TYR TYR A . n 
A 1 144 ILE 144 138 138 ILE ILE A . n 
A 1 145 HIS 145 139 139 HIS HIS A . n 
A 1 146 SER 146 140 140 SER SER A . n 
A 1 147 ALA 147 141 141 ALA ALA A . n 
A 1 148 ASN 148 142 142 ASN ASN A . n 
A 1 149 VAL 149 143 143 VAL VAL A . n 
A 1 150 LEU 150 144 144 LEU LEU A . n 
A 1 151 HIS 151 145 145 HIS HIS A . n 
A 1 152 ARG 152 146 146 ARG ARG A . n 
A 1 153 ASP 153 147 147 ASP ASP A . n 
A 1 154 LEU 154 148 148 LEU LEU A . n 
A 1 155 LYS 155 149 149 LYS LYS A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 SER 157 151 151 SER SER A . n 
A 1 158 ASN 158 152 152 ASN ASN A . n 
A 1 159 LEU 159 153 153 LEU LEU A . n 
A 1 160 LEU 160 154 154 LEU LEU A . n 
A 1 161 LEU 161 155 155 LEU LEU A . n 
A 1 162 ASN 162 156 156 ASN ASN A . n 
A 1 163 THR 163 157 157 THR THR A . n 
A 1 164 THR 164 158 158 THR THR A . n 
A 1 165 CME 165 159 159 CME CME A . n 
A 1 166 ASP 166 160 160 ASP ASP A . n 
A 1 167 LEU 167 161 161 LEU LEU A . n 
A 1 168 LYS 168 162 162 LYS LYS A . n 
A 1 169 ILE 169 163 163 ILE ILE A . n 
A 1 170 CYS 170 164 164 CYS CYS A . n 
A 1 171 ASP 171 165 165 ASP ASP A . n 
A 1 172 PHE 172 166 166 PHE PHE A . n 
A 1 173 GLY 173 167 167 GLY GLY A . n 
A 1 174 LEU 174 168 168 LEU LEU A . n 
A 1 175 ALA 175 169 169 ALA ALA A . n 
A 1 176 ARG 176 170 170 ARG ARG A . n 
A 1 177 VAL 177 171 171 VAL VAL A . n 
A 1 178 ALA 178 172 172 ALA ALA A . n 
A 1 179 ASP 179 173 173 ASP ASP A . n 
A 1 180 PRO 180 174 174 PRO PRO A . n 
A 1 181 ASP 181 175 175 ASP ASP A . n 
A 1 182 HIS 182 176 176 HIS HIS A . n 
A 1 183 ASP 183 177 177 ASP ASP A . n 
A 1 184 HIS 184 178 178 HIS HIS A . n 
A 1 185 THR 185 179 179 THR THR A . n 
A 1 186 GLY 186 180 180 GLY GLY A . n 
A 1 187 PHE 187 181 181 PHE PHE A . n 
A 1 188 LEU 188 182 182 LEU LEU A . n 
A 1 189 THR 189 183 183 THR THR A . n 
A 1 190 GLU 190 184 184 GLU GLU A . n 
A 1 191 TYR 191 185 185 TYR TYR A . n 
A 1 192 VAL 192 186 186 VAL VAL A . n 
A 1 193 ALA 193 187 187 ALA ALA A . n 
A 1 194 THR 194 188 188 THR THR A . n 
A 1 195 ARG 195 189 189 ARG ARG A . n 
A 1 196 TRP 196 190 190 TRP TRP A . n 
A 1 197 TYR 197 191 191 TYR TYR A . n 
A 1 198 ARG 198 192 192 ARG ARG A . n 
A 1 199 ALA 199 193 193 ALA ALA A . n 
A 1 200 PRO 200 194 194 PRO PRO A . n 
A 1 201 GLU 201 195 195 GLU GLU A . n 
A 1 202 ILE 202 196 196 ILE ILE A . n 
A 1 203 MET 203 197 197 MET MET A . n 
A 1 204 LEU 204 198 198 LEU LEU A . n 
A 1 205 ASN 205 199 199 ASN ASN A . n 
A 1 206 SER 206 200 200 SER SER A . n 
A 1 207 LYS 207 201 201 LYS LYS A . n 
A 1 208 GLY 208 202 202 GLY GLY A . n 
A 1 209 TYR 209 203 203 TYR TYR A . n 
A 1 210 THR 210 204 204 THR THR A . n 
A 1 211 LYS 211 205 205 LYS LYS A . n 
A 1 212 SER 212 206 206 SER SER A . n 
A 1 213 ILE 213 207 207 ILE ILE A . n 
A 1 214 ASP 214 208 208 ASP ASP A . n 
A 1 215 ILE 215 209 209 ILE ILE A . n 
A 1 216 TRP 216 210 210 TRP TRP A . n 
A 1 217 SER 217 211 211 SER SER A . n 
A 1 218 VAL 218 212 212 VAL VAL A . n 
A 1 219 GLY 219 213 213 GLY GLY A . n 
A 1 220 CYS 220 214 214 CYS CYS A . n 
A 1 221 ILE 221 215 215 ILE ILE A . n 
A 1 222 LEU 222 216 216 LEU LEU A . n 
A 1 223 ALA 223 217 217 ALA ALA A . n 
A 1 224 GLU 224 218 218 GLU GLU A . n 
A 1 225 MET 225 219 219 MET MET A . n 
A 1 226 LEU 226 220 220 LEU LEU A . n 
A 1 227 SER 227 221 221 SER SER A . n 
A 1 228 ASN 228 222 222 ASN ASN A . n 
A 1 229 ARG 229 223 223 ARG ARG A . n 
A 1 230 PRO 230 224 224 PRO PRO A . n 
A 1 231 ILE 231 225 225 ILE ILE A . n 
A 1 232 PHE 232 226 226 PHE PHE A . n 
A 1 233 PRO 233 227 227 PRO PRO A . n 
A 1 234 GLY 234 228 228 GLY GLY A . n 
A 1 235 LYS 235 229 229 LYS LYS A . n 
A 1 236 HIS 236 230 230 HIS HIS A . n 
A 1 237 TYR 237 231 231 TYR TYR A . n 
A 1 238 LEU 238 232 232 LEU LEU A . n 
A 1 239 ASP 239 233 233 ASP ASP A . n 
A 1 240 GLN 240 234 234 GLN GLN A . n 
A 1 241 LEU 241 235 235 LEU LEU A . n 
A 1 242 ASN 242 236 236 ASN ASN A . n 
A 1 243 HIS 243 237 237 HIS HIS A . n 
A 1 244 ILE 244 238 238 ILE ILE A . n 
A 1 245 LEU 245 239 239 LEU LEU A . n 
A 1 246 GLY 246 240 240 GLY GLY A . n 
A 1 247 ILE 247 241 241 ILE ILE A . n 
A 1 248 LEU 248 242 242 LEU LEU A . n 
A 1 249 GLY 249 243 243 GLY GLY A . n 
A 1 250 SER 250 244 244 SER SER A . n 
A 1 251 PRO 251 245 245 PRO PRO A . n 
A 1 252 SER 252 246 246 SER SER A . n 
A 1 253 GLN 253 247 247 GLN GLN A . n 
A 1 254 GLU 254 248 248 GLU GLU A . n 
A 1 255 ASP 255 249 249 ASP ASP A . n 
A 1 256 LEU 256 250 250 LEU LEU A . n 
A 1 257 ASN 257 251 251 ASN ASN A . n 
A 1 258 CME 258 252 252 CME CME A . n 
A 1 259 ILE 259 253 253 ILE ILE A . n 
A 1 260 ILE 260 254 254 ILE ILE A . n 
A 1 261 ASN 261 255 255 ASN ASN A . n 
A 1 262 LEU 262 256 256 LEU LEU A . n 
A 1 263 LYS 263 257 257 LYS LYS A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 ARG 265 259 259 ARG ARG A . n 
A 1 266 ASN 266 260 260 ASN ASN A . n 
A 1 267 TYR 267 261 261 TYR TYR A . n 
A 1 268 LEU 268 262 262 LEU LEU A . n 
A 1 269 LEU 269 263 263 LEU LEU A . n 
A 1 270 SER 270 264 264 SER SER A . n 
A 1 271 LEU 271 265 265 LEU LEU A . n 
A 1 272 PRO 272 266 266 PRO PRO A . n 
A 1 273 HIS 273 267 267 HIS HIS A . n 
A 1 274 LYS 274 268 268 LYS LYS A . n 
A 1 275 ASN 275 269 269 ASN ASN A . n 
A 1 276 LYS 276 270 270 LYS LYS A . n 
A 1 277 VAL 277 271 271 VAL VAL A . n 
A 1 278 PRO 278 272 272 PRO PRO A . n 
A 1 279 TRP 279 273 273 TRP TRP A . n 
A 1 280 ASN 280 274 274 ASN ASN A . n 
A 1 281 ARG 281 275 275 ARG ARG A . n 
A 1 282 LEU 282 276 276 LEU LEU A . n 
A 1 283 PHE 283 277 277 PHE PHE A . n 
A 1 284 PRO 284 278 278 PRO PRO A . n 
A 1 285 ASN 285 279 279 ASN ASN A . n 
A 1 286 ALA 286 280 280 ALA ALA A . n 
A 1 287 ASP 287 281 281 ASP ASP A . n 
A 1 288 SER 288 282 282 SER SER A . n 
A 1 289 LYS 289 283 283 LYS LYS A . n 
A 1 290 ALA 290 284 284 ALA ALA A . n 
A 1 291 LEU 291 285 285 LEU LEU A . n 
A 1 292 ASP 292 286 286 ASP ASP A . n 
A 1 293 LEU 293 287 287 LEU LEU A . n 
A 1 294 LEU 294 288 288 LEU LEU A . n 
A 1 295 ASP 295 289 289 ASP ASP A . n 
A 1 296 LYS 296 290 290 LYS LYS A . n 
A 1 297 MET 297 291 291 MET MET A . n 
A 1 298 LEU 298 292 292 LEU LEU A . n 
A 1 299 THR 299 293 293 THR THR A . n 
A 1 300 PHE 300 294 294 PHE PHE A . n 
A 1 301 ASN 301 295 295 ASN ASN A . n 
A 1 302 PRO 302 296 296 PRO PRO A . n 
A 1 303 HIS 303 297 297 HIS HIS A . n 
A 1 304 LYS 304 298 298 LYS LYS A . n 
A 1 305 ARG 305 299 299 ARG ARG A . n 
A 1 306 ILE 306 300 300 ILE ILE A . n 
A 1 307 GLU 307 301 301 GLU GLU A . n 
A 1 308 VAL 308 302 302 VAL VAL A . n 
A 1 309 GLU 309 303 303 GLU GLU A . n 
A 1 310 GLN 310 304 304 GLN GLN A . n 
A 1 311 ALA 311 305 305 ALA ALA A . n 
A 1 312 LEU 312 306 306 LEU LEU A . n 
A 1 313 ALA 313 307 307 ALA ALA A . n 
A 1 314 HIS 314 308 308 HIS HIS A . n 
A 1 315 PRO 315 309 309 PRO PRO A . n 
A 1 316 TYR 316 310 310 TYR TYR A . n 
A 1 317 LEU 317 311 311 LEU LEU A . n 
A 1 318 GLU 318 312 312 GLU GLU A . n 
A 1 319 GLN 319 313 313 GLN GLN A . n 
A 1 320 TYR 320 314 314 TYR TYR A . n 
A 1 321 TYR 321 315 315 TYR TYR A . n 
A 1 322 ASP 322 316 316 ASP ASP A . n 
A 1 323 PRO 323 317 317 PRO PRO A . n 
A 1 324 SER 324 318 318 SER SER A . n 
A 1 325 ASP 325 319 319 ASP ASP A . n 
A 1 326 GLU 326 320 320 GLU GLU A . n 
A 1 327 PRO 327 321 321 PRO PRO A . n 
A 1 328 ILE 328 322 322 ILE ILE A . n 
A 1 329 ALA 329 323 323 ALA ALA A . n 
A 1 330 GLU 330 324 324 GLU GLU A . n 
A 1 331 ALA 331 325 325 ALA ALA A . n 
A 1 332 PRO 332 326 326 PRO PRO A . n 
A 1 333 PHE 333 327 327 PHE PHE A . n 
A 1 334 LYS 334 328 328 LYS LYS A . n 
A 1 335 PHE 335 329 329 PHE PHE A . n 
A 1 336 ASP 336 330 ?   ?   ?   A . n 
A 1 337 MET 337 331 ?   ?   ?   A . n 
A 1 338 GLU 338 332 ?   ?   ?   A . n 
A 1 339 LEU 339 333 ?   ?   ?   A . n 
A 1 340 ASP 340 334 ?   ?   ?   A . n 
A 1 341 ASP 341 335 335 ASP ASP A . n 
A 1 342 LEU 342 336 336 LEU LEU A . n 
A 1 343 PRO 343 337 337 PRO PRO A . n 
A 1 344 LYS 344 338 338 LYS LYS A . n 
A 1 345 GLU 345 339 339 GLU GLU A . n 
A 1 346 LYS 346 340 340 LYS LYS A . n 
A 1 347 LEU 347 341 341 LEU LEU A . n 
A 1 348 LYS 348 342 342 LYS LYS A . n 
A 1 349 GLU 349 343 343 GLU GLU A . n 
A 1 350 LEU 350 344 344 LEU LEU A . n 
A 1 351 ILE 351 345 345 ILE ILE A . n 
A 1 352 PHE 352 346 346 PHE PHE A . n 
A 1 353 GLU 353 347 347 GLU GLU A . n 
A 1 354 GLU 354 348 348 GLU GLU A . n 
A 1 355 THR 355 349 349 THR THR A . n 
A 1 356 ALA 356 350 350 ALA ALA A . n 
A 1 357 ARG 357 351 351 ARG ARG A . n 
A 1 358 PHE 358 352 352 PHE PHE A . n 
A 1 359 GLN 359 353 353 GLN GLN A . n 
A 1 360 PRO 360 354 354 PRO PRO A . n 
A 1 361 GLY 361 355 ?   ?   ?   A . n 
A 1 362 TYR 362 356 ?   ?   ?   A . n 
A 1 363 ARG 363 357 ?   ?   ?   A . n 
A 1 364 SER 364 358 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WM6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WM6 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4 1   401 1   SO4 SO4 A . 
C 2 SO4 1   402 2   SO4 SO4 A . 
D 3 WM6 1   403 1   WM6 528 A . 
E 4 HOH 1   501 202 HOH HOH A . 
E 4 HOH 2   502 97  HOH HOH A . 
E 4 HOH 3   503 189 HOH HOH A . 
E 4 HOH 4   504 39  HOH HOH A . 
E 4 HOH 5   505 107 HOH HOH A . 
E 4 HOH 6   506 79  HOH HOH A . 
E 4 HOH 7   507 203 HOH HOH A . 
E 4 HOH 8   508 129 HOH HOH A . 
E 4 HOH 9   509 6   HOH HOH A . 
E 4 HOH 10  510 64  HOH HOH A . 
E 4 HOH 11  511 159 HOH HOH A . 
E 4 HOH 12  512 182 HOH HOH A . 
E 4 HOH 13  513 93  HOH HOH A . 
E 4 HOH 14  514 42  HOH HOH A . 
E 4 HOH 15  515 288 HOH HOH A . 
E 4 HOH 16  516 304 HOH HOH A . 
E 4 HOH 17  517 47  HOH HOH A . 
E 4 HOH 18  518 3   HOH HOH A . 
E 4 HOH 19  519 78  HOH HOH A . 
E 4 HOH 20  520 151 HOH HOH A . 
E 4 HOH 21  521 248 HOH HOH A . 
E 4 HOH 22  522 245 HOH HOH A . 
E 4 HOH 23  523 120 HOH HOH A . 
E 4 HOH 24  524 237 HOH HOH A . 
E 4 HOH 25  525 126 HOH HOH A . 
E 4 HOH 26  526 302 HOH HOH A . 
E 4 HOH 27  527 23  HOH HOH A . 
E 4 HOH 28  528 267 HOH HOH A . 
E 4 HOH 29  529 140 HOH HOH A . 
E 4 HOH 30  530 279 HOH HOH A . 
E 4 HOH 31  531 124 HOH HOH A . 
E 4 HOH 32  532 123 HOH HOH A . 
E 4 HOH 33  533 9   HOH HOH A . 
E 4 HOH 34  534 21  HOH HOH A . 
E 4 HOH 35  535 36  HOH HOH A . 
E 4 HOH 36  536 38  HOH HOH A . 
E 4 HOH 37  537 103 HOH HOH A . 
E 4 HOH 38  538 191 HOH HOH A . 
E 4 HOH 39  539 7   HOH HOH A . 
E 4 HOH 40  540 250 HOH HOH A . 
E 4 HOH 41  541 41  HOH HOH A . 
E 4 HOH 42  542 299 HOH HOH A . 
E 4 HOH 43  543 101 HOH HOH A . 
E 4 HOH 44  544 80  HOH HOH A . 
E 4 HOH 45  545 185 HOH HOH A . 
E 4 HOH 46  546 264 HOH HOH A . 
E 4 HOH 47  547 28  HOH HOH A . 
E 4 HOH 48  548 74  HOH HOH A . 
E 4 HOH 49  549 22  HOH HOH A . 
E 4 HOH 50  550 284 HOH HOH A . 
E 4 HOH 51  551 131 HOH HOH A . 
E 4 HOH 52  552 49  HOH HOH A . 
E 4 HOH 53  553 183 HOH HOH A . 
E 4 HOH 54  554 84  HOH HOH A . 
E 4 HOH 55  555 152 HOH HOH A . 
E 4 HOH 56  556 239 HOH HOH A . 
E 4 HOH 57  557 50  HOH HOH A . 
E 4 HOH 58  558 54  HOH HOH A . 
E 4 HOH 59  559 280 HOH HOH A . 
E 4 HOH 60  560 199 HOH HOH A . 
E 4 HOH 61  561 98  HOH HOH A . 
E 4 HOH 62  562 125 HOH HOH A . 
E 4 HOH 63  563 73  HOH HOH A . 
E 4 HOH 64  564 30  HOH HOH A . 
E 4 HOH 65  565 14  HOH HOH A . 
E 4 HOH 66  566 71  HOH HOH A . 
E 4 HOH 67  567 111 HOH HOH A . 
E 4 HOH 68  568 135 HOH HOH A . 
E 4 HOH 69  569 31  HOH HOH A . 
E 4 HOH 70  570 45  HOH HOH A . 
E 4 HOH 71  571 109 HOH HOH A . 
E 4 HOH 72  572 59  HOH HOH A . 
E 4 HOH 73  573 187 HOH HOH A . 
E 4 HOH 74  574 81  HOH HOH A . 
E 4 HOH 75  575 137 HOH HOH A . 
E 4 HOH 76  576 294 HOH HOH A . 
E 4 HOH 77  577 11  HOH HOH A . 
E 4 HOH 78  578 72  HOH HOH A . 
E 4 HOH 79  579 17  HOH HOH A . 
E 4 HOH 80  580 216 HOH HOH A . 
E 4 HOH 81  581 68  HOH HOH A . 
E 4 HOH 82  582 92  HOH HOH A . 
E 4 HOH 83  583 206 HOH HOH A . 
E 4 HOH 84  584 8   HOH HOH A . 
E 4 HOH 85  585 224 HOH HOH A . 
E 4 HOH 86  586 155 HOH HOH A . 
E 4 HOH 87  587 67  HOH HOH A . 
E 4 HOH 88  588 146 HOH HOH A . 
E 4 HOH 89  589 75  HOH HOH A . 
E 4 HOH 90  590 61  HOH HOH A . 
E 4 HOH 91  591 195 HOH HOH A . 
E 4 HOH 92  592 2   HOH HOH A . 
E 4 HOH 93  593 18  HOH HOH A . 
E 4 HOH 94  594 85  HOH HOH A . 
E 4 HOH 95  595 82  HOH HOH A . 
E 4 HOH 96  596 115 HOH HOH A . 
E 4 HOH 97  597 29  HOH HOH A . 
E 4 HOH 98  598 166 HOH HOH A . 
E 4 HOH 99  599 102 HOH HOH A . 
E 4 HOH 100 600 33  HOH HOH A . 
E 4 HOH 101 601 207 HOH HOH A . 
E 4 HOH 102 602 16  HOH HOH A . 
E 4 HOH 103 603 121 HOH HOH A . 
E 4 HOH 104 604 27  HOH HOH A . 
E 4 HOH 105 605 62  HOH HOH A . 
E 4 HOH 106 606 181 HOH HOH A . 
E 4 HOH 107 607 312 HOH HOH A . 
E 4 HOH 108 608 141 HOH HOH A . 
E 4 HOH 109 609 4   HOH HOH A . 
E 4 HOH 110 610 34  HOH HOH A . 
E 4 HOH 111 611 145 HOH HOH A . 
E 4 HOH 112 612 122 HOH HOH A . 
E 4 HOH 113 613 87  HOH HOH A . 
E 4 HOH 114 614 176 HOH HOH A . 
E 4 HOH 115 615 204 HOH HOH A . 
E 4 HOH 116 616 1   HOH HOH A . 
E 4 HOH 117 617 37  HOH HOH A . 
E 4 HOH 118 618 175 HOH HOH A . 
E 4 HOH 119 619 157 HOH HOH A . 
E 4 HOH 120 620 110 HOH HOH A . 
E 4 HOH 121 621 244 HOH HOH A . 
E 4 HOH 122 622 76  HOH HOH A . 
E 4 HOH 123 623 10  HOH HOH A . 
E 4 HOH 124 624 5   HOH HOH A . 
E 4 HOH 125 625 116 HOH HOH A . 
E 4 HOH 126 626 12  HOH HOH A . 
E 4 HOH 127 627 117 HOH HOH A . 
E 4 HOH 128 628 307 HOH HOH A . 
E 4 HOH 129 629 275 HOH HOH A . 
E 4 HOH 130 630 300 HOH HOH A . 
E 4 HOH 131 631 19  HOH HOH A . 
E 4 HOH 132 632 147 HOH HOH A . 
E 4 HOH 133 633 35  HOH HOH A . 
E 4 HOH 134 634 32  HOH HOH A . 
E 4 HOH 135 635 40  HOH HOH A . 
E 4 HOH 136 636 43  HOH HOH A . 
E 4 HOH 137 637 289 HOH HOH A . 
E 4 HOH 138 638 46  HOH HOH A . 
E 4 HOH 139 639 91  HOH HOH A . 
E 4 HOH 140 640 210 HOH HOH A . 
E 4 HOH 141 641 232 HOH HOH A . 
E 4 HOH 142 642 211 HOH HOH A . 
E 4 HOH 143 643 100 HOH HOH A . 
E 4 HOH 144 644 69  HOH HOH A . 
E 4 HOH 145 645 149 HOH HOH A . 
E 4 HOH 146 646 143 HOH HOH A . 
E 4 HOH 147 647 134 HOH HOH A . 
E 4 HOH 148 648 99  HOH HOH A . 
E 4 HOH 149 649 112 HOH HOH A . 
E 4 HOH 150 650 25  HOH HOH A . 
E 4 HOH 151 651 105 HOH HOH A . 
E 4 HOH 152 652 263 HOH HOH A . 
E 4 HOH 153 653 286 HOH HOH A . 
E 4 HOH 154 654 167 HOH HOH A . 
E 4 HOH 155 655 77  HOH HOH A . 
E 4 HOH 156 656 160 HOH HOH A . 
E 4 HOH 157 657 24  HOH HOH A . 
E 4 HOH 158 658 205 HOH HOH A . 
E 4 HOH 159 659 240 HOH HOH A . 
E 4 HOH 160 660 44  HOH HOH A . 
E 4 HOH 161 661 132 HOH HOH A . 
E 4 HOH 162 662 114 HOH HOH A . 
E 4 HOH 163 663 209 HOH HOH A . 
E 4 HOH 164 664 292 HOH HOH A . 
E 4 HOH 165 665 86  HOH HOH A . 
E 4 HOH 166 666 13  HOH HOH A . 
E 4 HOH 167 667 26  HOH HOH A . 
E 4 HOH 168 668 108 HOH HOH A . 
E 4 HOH 169 669 227 HOH HOH A . 
E 4 HOH 170 670 163 HOH HOH A . 
E 4 HOH 171 671 310 HOH HOH A . 
E 4 HOH 172 672 144 HOH HOH A . 
E 4 HOH 173 673 15  HOH HOH A . 
E 4 HOH 174 674 186 HOH HOH A . 
E 4 HOH 175 675 20  HOH HOH A . 
E 4 HOH 176 676 118 HOH HOH A . 
E 4 HOH 177 677 213 HOH HOH A . 
E 4 HOH 178 678 309 HOH HOH A . 
E 4 HOH 179 679 178 HOH HOH A . 
E 4 HOH 180 680 171 HOH HOH A . 
E 4 HOH 181 681 303 HOH HOH A . 
E 4 HOH 182 682 217 HOH HOH A . 
E 4 HOH 183 683 252 HOH HOH A . 
E 4 HOH 184 684 198 HOH HOH A . 
E 4 HOH 185 685 169 HOH HOH A . 
E 4 HOH 186 686 247 HOH HOH A . 
E 4 HOH 187 687 255 HOH HOH A . 
E 4 HOH 188 688 153 HOH HOH A . 
E 4 HOH 189 689 52  HOH HOH A . 
E 4 HOH 190 690 214 HOH HOH A . 
E 4 HOH 191 691 158 HOH HOH A . 
E 4 HOH 192 692 231 HOH HOH A . 
E 4 HOH 193 693 290 HOH HOH A . 
E 4 HOH 194 694 170 HOH HOH A . 
E 4 HOH 195 695 53  HOH HOH A . 
E 4 HOH 196 696 57  HOH HOH A . 
E 4 HOH 197 697 200 HOH HOH A . 
E 4 HOH 198 698 172 HOH HOH A . 
E 4 HOH 199 699 180 HOH HOH A . 
E 4 HOH 200 700 212 HOH HOH A . 
E 4 HOH 201 701 168 HOH HOH A . 
E 4 HOH 202 702 106 HOH HOH A . 
E 4 HOH 203 703 225 HOH HOH A . 
E 4 HOH 204 704 298 HOH HOH A . 
E 4 HOH 205 705 113 HOH HOH A . 
E 4 HOH 206 706 266 HOH HOH A . 
E 4 HOH 207 707 119 HOH HOH A . 
E 4 HOH 208 708 179 HOH HOH A . 
E 4 HOH 209 709 133 HOH HOH A . 
E 4 HOH 210 710 251 HOH HOH A . 
E 4 HOH 211 711 197 HOH HOH A . 
E 4 HOH 212 712 48  HOH HOH A . 
E 4 HOH 213 713 89  HOH HOH A . 
E 4 HOH 214 714 65  HOH HOH A . 
E 4 HOH 215 715 60  HOH HOH A . 
E 4 HOH 216 716 164 HOH HOH A . 
E 4 HOH 217 717 194 HOH HOH A . 
E 4 HOH 218 718 162 HOH HOH A . 
E 4 HOH 219 719 184 HOH HOH A . 
E 4 HOH 220 720 273 HOH HOH A . 
E 4 HOH 221 721 51  HOH HOH A . 
E 4 HOH 222 722 142 HOH HOH A . 
E 4 HOH 223 723 281 HOH HOH A . 
E 4 HOH 224 724 253 HOH HOH A . 
E 4 HOH 225 725 301 HOH HOH A . 
E 4 HOH 226 726 165 HOH HOH A . 
E 4 HOH 227 727 56  HOH HOH A . 
E 4 HOH 228 728 196 HOH HOH A . 
E 4 HOH 229 729 265 HOH HOH A . 
E 4 HOH 230 730 236 HOH HOH A . 
E 4 HOH 231 731 174 HOH HOH A . 
E 4 HOH 232 732 277 HOH HOH A . 
E 4 HOH 233 733 241 HOH HOH A . 
E 4 HOH 234 734 63  HOH HOH A . 
E 4 HOH 235 735 104 HOH HOH A . 
E 4 HOH 236 736 88  HOH HOH A . 
E 4 HOH 237 737 154 HOH HOH A . 
E 4 HOH 238 738 128 HOH HOH A . 
E 4 HOH 239 739 254 HOH HOH A . 
E 4 HOH 240 740 95  HOH HOH A . 
E 4 HOH 241 741 96  HOH HOH A . 
E 4 HOH 242 742 190 HOH HOH A . 
E 4 HOH 243 743 311 HOH HOH A . 
E 4 HOH 244 744 66  HOH HOH A . 
E 4 HOH 245 745 269 HOH HOH A . 
E 4 HOH 246 746 234 HOH HOH A . 
E 4 HOH 247 747 136 HOH HOH A . 
E 4 HOH 248 748 127 HOH HOH A . 
E 4 HOH 249 749 215 HOH HOH A . 
E 4 HOH 250 750 261 HOH HOH A . 
E 4 HOH 251 751 221 HOH HOH A . 
E 4 HOH 252 752 201 HOH HOH A . 
E 4 HOH 253 753 193 HOH HOH A . 
E 4 HOH 254 754 308 HOH HOH A . 
E 4 HOH 255 755 276 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 PHE 329 ? CG  ? A PHE 335 CG  
2 1 Y 1 A PHE 329 ? CD1 ? A PHE 335 CD1 
3 1 Y 1 A PHE 329 ? CD2 ? A PHE 335 CD2 
4 1 Y 1 A PHE 329 ? CE1 ? A PHE 335 CE1 
5 1 Y 1 A PHE 329 ? CE2 ? A PHE 335 CE2 
6 1 Y 1 A PHE 329 ? CZ  ? A PHE 335 CZ  
7 1 Y 1 A ASP 335 ? CG  ? A ASP 341 CG  
8 1 Y 1 A ASP 335 ? OD1 ? A ASP 341 OD1 
9 1 Y 1 A ASP 335 ? OD2 ? A ASP 341 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.380 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QRA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.650 
_cell.length_a_esd                 ? 
_cell.length_b                     69.840 
_cell.length_b_esd                 ? 
_cell.length_c                     59.770 
_cell.length_c_esd                 ? 
_cell.volume                       191574.593 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8QRA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 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                   8QRA 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.67 
_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              ? 
_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    'PEG MME 2000, 0.1M MES pH 6.5, 0.1M ammonium sulfate, 0.02M beta-mercaptoethanol' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-12-11 
_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   0.979288 
_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                        'ESRF BEAMLINE ID14-4' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979288 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID14-4 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          19.94 
_reflns.entry_id                                       8QRA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               29.69 
_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                                     53250 
_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                           97.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.85 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.104 
_reflns.pdbx_Rpim_I_all                                0.055 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       186447 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           9022 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2603 
_reflns_shell.percent_possible_obs                          96.6 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              0.59 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.0 
_reflns_shell.pdbx_Rrim_I_all                               0.943 
_reflns_shell.pdbx_Rpim_I_all                               0.493 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.711 
_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                                  0.801 
_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                               30.69 
_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                                 8QRA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.55 
_refine.ls_d_res_low                             28.63 
_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                     53221 
_refine.ls_number_reflns_R_free                  2727 
_refine.ls_number_reflns_R_work                  50494 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.20 
_refine.ls_percent_reflns_R_free                 5.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1443 
_refine.ls_R_factor_R_free                       0.1819 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1421 
_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                          1.37 
_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                      3QYZ 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 19.5658 
_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                            0.1649 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        28.63 
_refine_hist.number_atoms_solvent             255 
_refine_hist.number_atoms_total               3079 
_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        2789 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_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' ? 0.0111 ? 3056 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1852 ? 4157 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0664 ? 459  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0114 ? 526  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.4467 ? 425  ? f_dihedral_angle_d ? ? 
# 
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' 1.55 1.58  . . 135 2629 96.37 . . . . 0.2070 . . . . . . . . . . . 0.2880 
'X-RAY DIFFRACTION' 1.58 1.61  . . 156 2595 96.46 . . . . 0.1845 . . . . . . . . . . . 0.2353 
'X-RAY DIFFRACTION' 1.61 1.64  . . 126 2643 96.62 . . . . 0.1765 . . . . . . . . . . . 0.2312 
'X-RAY DIFFRACTION' 1.64 1.68  . . 135 2647 96.60 . . . . 0.1706 . . . . . . . . . . . 0.2342 
'X-RAY DIFFRACTION' 1.68 1.72  . . 116 2658 96.72 . . . . 0.1580 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 1.72 1.76  . . 134 2654 97.21 . . . . 0.1474 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 1.76 1.81  . . 136 2682 97.61 . . . . 0.1439 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.81 1.86  . . 155 2627 97.72 . . . . 0.1340 . . . . . . . . . . . 0.1979 
'X-RAY DIFFRACTION' 1.86 1.92  . . 144 2685 97.82 . . . . 0.1296 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 1.92 1.99  . . 133 2683 98.29 . . . . 0.1277 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 1.99 2.07  . . 140 2687 98.54 . . . . 0.1205 . . . . . . . . . . . 0.1714 
'X-RAY DIFFRACTION' 2.07 2.16  . . 109 2708 98.46 . . . . 0.1176 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 2.16 2.28  . . 152 2700 98.41 . . . . 0.1186 . . . . . . . . . . . 0.1721 
'X-RAY DIFFRACTION' 2.28 2.42  . . 156 2716 98.90 . . . . 0.1324 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 2.42 2.61  . . 144 2688 98.95 . . . . 0.1325 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 2.61 2.87  . . 171 2691 98.45 . . . . 0.1478 . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 2.87 3.28  . . 163 2696 98.62 . . . . 0.1517 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 3.28 4.13  . . 168 2671 98.34 . . . . 0.1342 . . . . . . . . . . . 0.1598 
'X-RAY DIFFRACTION' 4.13 28.63 . . 154 2434 87.17 . . . . 0.1604 . . . . . . . . . . . 0.1754 
# 
_struct.entry_id                     8QRA 
_struct.title                        'Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand' 
_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        8QRA 
_struct_keywords.text            'SERINE/THREONINE-PROTEIN KINASE, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK01_RAT 
_struct_ref.pdbx_db_accession          P63086 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHEN
IIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCD
LKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILG
ILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDE
PIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QRA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 7 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 364 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P63086 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  358 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       358 
# 
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 8QRA HIS A 1 ? UNP P63086 ? ? 'expression tag' -5 1 
1 8QRA HIS A 2 ? UNP P63086 ? ? 'expression tag' -4 2 
1 8QRA HIS A 3 ? UNP P63086 ? ? 'expression tag' -3 3 
1 8QRA HIS A 4 ? UNP P63086 ? ? 'expression tag' -2 4 
1 8QRA HIS A 5 ? UNP P63086 ? ? 'expression tag' -1 5 
1 8QRA HIS A 6 ? UNP P63086 ? ? 'expression tag' 0  6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 360   ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  16250 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                monomer 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 65  ? PHE A 82  ? HIS A 59  PHE A 76  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 116 ? GLN A 123 ? LEU A 110 GLN A 117 1 ? 8  
HELX_P HELX_P3  AA3 SER A 126 ? ALA A 147 ? SER A 120 ALA A 141 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 155 ? SER A 157 ? LYS A 149 SER A 151 5 ? 3  
HELX_P HELX_P5  AA5 ASP A 179 ? ASP A 183 ? ASP A 173 ASP A 177 5 ? 5  
HELX_P HELX_P6  AA6 THR A 194 ? ARG A 198 ? THR A 188 ARG A 192 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 199 ? ASN A 205 ? ALA A 193 ASN A 199 1 ? 7  
HELX_P HELX_P8  AA8 LYS A 211 ? ASN A 228 ? LYS A 205 ASN A 222 1 ? 18 
HELX_P HELX_P9  AA9 LEU A 238 ? GLY A 249 ? LEU A 232 GLY A 243 1 ? 12 
HELX_P HELX_P10 AB1 SER A 252 ? CME A 258 ? SER A 246 CME A 252 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 261 ? LEU A 271 ? ASN A 255 LEU A 265 1 ? 11 
HELX_P HELX_P12 AB3 PRO A 278 ? PHE A 283 ? PRO A 272 PHE A 277 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 287 ? LEU A 298 ? ASP A 281 LEU A 292 1 ? 12 
HELX_P HELX_P14 AB5 GLU A 307 ? ALA A 313 ? GLU A 301 ALA A 307 1 ? 7  
HELX_P HELX_P15 AB6 HIS A 314 ? GLU A 318 ? HIS A 308 GLU A 312 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 322 ? GLU A 326 ? ASP A 316 GLU A 320 5 ? 5  
HELX_P HELX_P17 AB8 PRO A 343 ? THR A 355 ? PRO A 337 THR A 349 1 ? 13 
HELX_P HELX_P18 AB9 ALA A 356 ? GLN A 359 ? ALA A 350 GLN A 353 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A THR 164 C  ? ? ? 1_555 A CME 165 N   ? ? A THR 158 A CME 159 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale2 covale both ? A CME 165 C  ? ? ? 1_555 A ASP 166 N   ? ? A CME 159 A ASP 160 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale3 covale none ? A CYS 170 SG A ? ? 1_555 D WM6 .   C12 ? ? A CYS 164 A WM6 403 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
covale4 covale both ? A ASN 257 C  ? ? ? 1_555 A CME 258 N   ? ? A ASN 251 A CME 252 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale5 covale both ? A CME 258 C  ? ? ? 1_555 A ILE 259 N   ? ? A CME 252 A ILE 253 1_555 ? ? ? ? ? ? ? 1.325 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CME A 165 ? .   . .   . CME A 159 ? 1_555 .   . .   . .     .   .  CYS 1 CME Beta-mercaptoethanol 'Named protein modification' 
2 CME A 258 ? .   . .   . CME A 252 ? 1_555 .   . .   . .     .   .  CYS 1 CME Beta-mercaptoethanol 'Named protein modification' 
3 WM6 D .   ? CYS A 170 A WM6 A 403 ? 1_555 CYS A 164 ? 1_555 C12 SG CYS 1 WM6 None                 
'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           26 
_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           GLY 
_struct_mon_prot_cis.auth_seq_id            20 
_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    27 
_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     21 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.00 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? 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 GLU A 16  ? MET A 17  ? GLU A 10  MET A 11  
AA1 2 VAL A 22  ? PHE A 23  ? VAL A 16  PHE A 17  
AA2 1 TYR A 29  ? GLU A 37  ? TYR A 23  GLU A 31  
AA2 2 MET A 42  ? ASP A 48  ? MET A 36  ASP A 42  
AA2 3 VAL A 53  ? ILE A 60  ? VAL A 47  ILE A 54  
AA2 4 VAL A 105 ? ASP A 110 ? VAL A 99  ASP A 104 
AA2 5 ASP A 92  ? ILE A 94  ? ASP A 86  ILE A 88  
AA3 1 THR A 114 ? ASP A 115 ? THR A 108 ASP A 109 
AA3 2 LEU A 159 ? LEU A 161 ? LEU A 153 LEU A 155 
AA3 3 LEU A 167 ? ILE A 169 ? LEU A 161 ILE A 163 
AA4 1 VAL A 149 ? LEU A 150 ? VAL A 143 LEU A 144 
AA4 2 ARG A 176 ? VAL A 177 ? ARG A 170 VAL A 171 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 16  ? N GLU A 10  O PHE A 23  ? O PHE A 17  
AA2 1 2 N THR A 30  ? N THR A 24  O TYR A 47  ? O TYR A 41  
AA2 2 3 N CYS A 44  ? N CYS A 38  O ILE A 57  ? O ILE A 51  
AA2 3 4 N ALA A 56  ? N ALA A 50  O GLN A 109 ? O GLN A 103 
AA2 4 5 O VAL A 108 ? O VAL A 102 N ASP A 92  ? N ASP A 86  
AA3 1 2 N THR A 114 ? N THR A 108 O LEU A 161 ? O LEU A 155 
AA3 2 3 N LEU A 160 ? N LEU A 154 O LYS A 168 ? O LYS A 162 
AA4 1 2 N LEU A 150 ? N LEU A 144 O ARG A 176 ? O ARG A 170 
# 
_pdbx_entry_details.entry_id                   8QRA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 147 ? ? -146.48 43.42  
2 1 ASP A 165 ? ? 67.93   95.61  
3 1 ASP A 173 ? ? -150.90 70.09  
4 1 ALA A 187 ? B 59.49   149.86 
5 1 THR A 188 ? ? -31.13  131.38 
6 1 ASN A 199 ? ? -159.57 16.27  
7 1 TYR A 231 ? A -54.10  -71.45 
8 1 LEU A 292 ? ? -98.37  46.49  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    187 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   THR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    188 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            141.43 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CME 165 A CME 159 ? CYS 'modified residue' 
2 A CME 258 A CME 252 ? CYS 'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS -5  ? A HIS 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A MET 1   ? A MET 7   
8  1 Y 1 A ALA 2   ? A ALA 8   
9  1 Y 1 A ALA 3   ? A ALA 9   
10 1 Y 1 A ALA 4   ? A ALA 10  
11 1 Y 1 A ALA 5   ? A ALA 11  
12 1 Y 1 A ALA 6   ? A ALA 12  
13 1 Y 1 A ALA 7   ? A ALA 13  
14 1 Y 1 A GLY 8   ? A GLY 14  
15 1 Y 1 A ASP 330 ? A ASP 336 
16 1 Y 1 A MET 331 ? A MET 337 
17 1 Y 1 A GLU 332 ? A GLU 338 
18 1 Y 1 A LEU 333 ? A LEU 339 
19 1 Y 1 A ASP 334 ? A ASP 340 
20 1 Y 1 A GLY 355 ? A GLY 361 
21 1 Y 1 A TYR 356 ? A TYR 362 
22 1 Y 1 A ARG 357 ? A ARG 363 
23 1 Y 1 A SER 358 ? A SER 364 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CME N    N N N 74  
CME CA   C N R 75  
CME CB   C N N 76  
CME SG   S N N 77  
CME SD   S N N 78  
CME CE   C N N 79  
CME CZ   C N N 80  
CME OH   O N N 81  
CME C    C N N 82  
CME O    O N N 83  
CME OXT  O N N 84  
CME H    H N N 85  
CME H2   H N N 86  
CME HA   H N N 87  
CME HB2  H N N 88  
CME HB3  H N N 89  
CME HE2  H N N 90  
CME HE3  H N N 91  
CME HZ2  H N N 92  
CME HZ3  H N N 93  
CME HH   H N N 94  
CME HXT  H N N 95  
CYS N    N N N 96  
CYS CA   C N R 97  
CYS C    C N N 98  
CYS O    O N N 99  
CYS CB   C N N 100 
CYS SG   S N N 101 
CYS OXT  O N N 102 
CYS H    H N N 103 
CYS H2   H N N 104 
CYS HA   H N N 105 
CYS HB2  H N N 106 
CYS HB3  H N N 107 
CYS HG   H N N 108 
CYS HXT  H N N 109 
GLN N    N N N 110 
GLN CA   C N S 111 
GLN C    C N N 112 
GLN O    O N N 113 
GLN CB   C N N 114 
GLN CG   C N N 115 
GLN CD   C N N 116 
GLN OE1  O N N 117 
GLN NE2  N N N 118 
GLN OXT  O N N 119 
GLN H    H N N 120 
GLN H2   H N N 121 
GLN HA   H N N 122 
GLN HB2  H N N 123 
GLN HB3  H N N 124 
GLN HG2  H N N 125 
GLN HG3  H N N 126 
GLN HE21 H N N 127 
GLN HE22 H N N 128 
GLN HXT  H N N 129 
GLU N    N N N 130 
GLU CA   C N S 131 
GLU C    C N N 132 
GLU O    O N N 133 
GLU CB   C N N 134 
GLU CG   C N N 135 
GLU CD   C N N 136 
GLU OE1  O N N 137 
GLU OE2  O N N 138 
GLU OXT  O N N 139 
GLU H    H N N 140 
GLU H2   H N N 141 
GLU HA   H N N 142 
GLU HB2  H N N 143 
GLU HB3  H N N 144 
GLU HG2  H N N 145 
GLU HG3  H N N 146 
GLU HE2  H N N 147 
GLU HXT  H N N 148 
GLY N    N N N 149 
GLY CA   C N N 150 
GLY C    C N N 151 
GLY O    O N N 152 
GLY OXT  O N N 153 
GLY H    H N N 154 
GLY H2   H N N 155 
GLY HA2  H N N 156 
GLY HA3  H N N 157 
GLY HXT  H N N 158 
HIS N    N N N 159 
HIS CA   C N S 160 
HIS C    C N N 161 
HIS O    O N N 162 
HIS CB   C N N 163 
HIS CG   C Y N 164 
HIS ND1  N Y N 165 
HIS CD2  C Y N 166 
HIS CE1  C Y N 167 
HIS NE2  N Y N 168 
HIS OXT  O N N 169 
HIS H    H N N 170 
HIS H2   H N N 171 
HIS HA   H N N 172 
HIS HB2  H N N 173 
HIS HB3  H N N 174 
HIS HD1  H N N 175 
HIS HD2  H N N 176 
HIS HE1  H N N 177 
HIS HE2  H N N 178 
HIS HXT  H N N 179 
HOH O    O N N 180 
HOH H1   H N N 181 
HOH H2   H N N 182 
ILE N    N N N 183 
ILE CA   C N S 184 
ILE C    C N N 185 
ILE O    O N N 186 
ILE CB   C N S 187 
ILE CG1  C N N 188 
ILE CG2  C N N 189 
ILE CD1  C N N 190 
ILE OXT  O N N 191 
ILE H    H N N 192 
ILE H2   H N N 193 
ILE HA   H N N 194 
ILE HB   H N N 195 
ILE HG12 H N N 196 
ILE HG13 H N N 197 
ILE HG21 H N N 198 
ILE HG22 H N N 199 
ILE HG23 H N N 200 
ILE HD11 H N N 201 
ILE HD12 H N N 202 
ILE HD13 H N N 203 
ILE HXT  H N N 204 
LEU N    N N N 205 
LEU CA   C N S 206 
LEU C    C N N 207 
LEU O    O N N 208 
LEU CB   C N N 209 
LEU CG   C N N 210 
LEU CD1  C N N 211 
LEU CD2  C N N 212 
LEU OXT  O N N 213 
LEU H    H N N 214 
LEU H2   H N N 215 
LEU HA   H N N 216 
LEU HB2  H N N 217 
LEU HB3  H N N 218 
LEU HG   H N N 219 
LEU HD11 H N N 220 
LEU HD12 H N N 221 
LEU HD13 H N N 222 
LEU HD21 H N N 223 
LEU HD22 H N N 224 
LEU HD23 H N N 225 
LEU HXT  H N N 226 
LYS N    N N N 227 
LYS CA   C N S 228 
LYS C    C N N 229 
LYS O    O N N 230 
LYS CB   C N N 231 
LYS CG   C N N 232 
LYS CD   C N N 233 
LYS CE   C N N 234 
LYS NZ   N N N 235 
LYS OXT  O N N 236 
LYS H    H N N 237 
LYS H2   H N N 238 
LYS HA   H N N 239 
LYS HB2  H N N 240 
LYS HB3  H N N 241 
LYS HG2  H N N 242 
LYS HG3  H N N 243 
LYS HD2  H N N 244 
LYS HD3  H N N 245 
LYS HE2  H N N 246 
LYS HE3  H N N 247 
LYS HZ1  H N N 248 
LYS HZ2  H N N 249 
LYS HZ3  H N N 250 
LYS HXT  H N N 251 
MET N    N N N 252 
MET CA   C N S 253 
MET C    C N N 254 
MET O    O N N 255 
MET CB   C N N 256 
MET CG   C N N 257 
MET SD   S N N 258 
MET CE   C N N 259 
MET OXT  O N N 260 
MET H    H N N 261 
MET H2   H N N 262 
MET HA   H N N 263 
MET HB2  H N N 264 
MET HB3  H N N 265 
MET HG2  H N N 266 
MET HG3  H N N 267 
MET HE1  H N N 268 
MET HE2  H N N 269 
MET HE3  H N N 270 
MET HXT  H N N 271 
PHE N    N N N 272 
PHE CA   C N S 273 
PHE C    C N N 274 
PHE O    O N N 275 
PHE CB   C N N 276 
PHE CG   C Y N 277 
PHE CD1  C Y N 278 
PHE CD2  C Y N 279 
PHE CE1  C Y N 280 
PHE CE2  C Y N 281 
PHE CZ   C Y N 282 
PHE OXT  O N N 283 
PHE H    H N N 284 
PHE H2   H N N 285 
PHE HA   H N N 286 
PHE HB2  H N N 287 
PHE HB3  H N N 288 
PHE HD1  H N N 289 
PHE HD2  H N N 290 
PHE HE1  H N N 291 
PHE HE2  H N N 292 
PHE HZ   H N N 293 
PHE HXT  H N N 294 
PRO N    N N N 295 
PRO CA   C N S 296 
PRO C    C N N 297 
PRO O    O N N 298 
PRO CB   C N N 299 
PRO CG   C N N 300 
PRO CD   C N N 301 
PRO OXT  O N N 302 
PRO H    H N N 303 
PRO HA   H N N 304 
PRO HB2  H N N 305 
PRO HB3  H N N 306 
PRO HG2  H N N 307 
PRO HG3  H N N 308 
PRO HD2  H N N 309 
PRO HD3  H N N 310 
PRO HXT  H N N 311 
SER N    N N N 312 
SER CA   C N S 313 
SER C    C N N 314 
SER O    O N N 315 
SER CB   C N N 316 
SER OG   O N N 317 
SER OXT  O N N 318 
SER H    H N N 319 
SER H2   H N N 320 
SER HA   H N N 321 
SER HB2  H N N 322 
SER HB3  H N N 323 
SER HG   H N N 324 
SER HXT  H N N 325 
SO4 S    S N N 326 
SO4 O1   O N N 327 
SO4 O2   O N N 328 
SO4 O3   O N N 329 
SO4 O4   O N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
WM6 C15  C N S 418 
WM6 C1   C N R 419 
WM6 C2   C N N 420 
WM6 C3   C Y N 421 
WM6 C8   C Y N 422 
WM6 C4   C Y N 423 
WM6 C5   C Y N 424 
WM6 C6   C Y N 425 
WM6 C7   C Y N 426 
WM6 C9   C N N 427 
WM6 C10  C N N 428 
WM6 C11  C N N 429 
WM6 C12  C N N 430 
WM6 C13  C N N 431 
WM6 C14  C N N 432 
WM6 C16  C N S 433 
WM6 O1   O N N 434 
WM6 O2   O N N 435 
WM6 O3   O N N 436 
WM6 O4   O N N 437 
WM6 O5   O N N 438 
WM6 O6   O N N 439 
WM6 O7   O N N 440 
WM6 O8   O N N 441 
WM6 O9   O N N 442 
WM6 H15  H N N 443 
WM6 H2   H N N 444 
WM6 H3   H N N 445 
WM6 H4   H N N 446 
WM6 H5   H N N 447 
WM6 H7   H N N 448 
WM6 H9   H N N 449 
WM6 H10  H N N 450 
WM6 H12  H N N 451 
WM6 H11  H N N 452 
WM6 H13  H N N 453 
WM6 H121 H N N 454 
WM6 H14  H N N 455 
WM6 H131 H N N 456 
WM6 H17  H N N 457 
WM6 H1   H N N 458 
WM6 H6   H N N 459 
WM6 H8   H N N 460 
WM6 H16  H N N 461 
WM6 H18  H N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CME N   CA   sing N N 70  
CME N   H    sing N N 71  
CME N   H2   sing N N 72  
CME CA  CB   sing N N 73  
CME CA  C    sing N N 74  
CME CA  HA   sing N N 75  
CME CB  SG   sing N N 76  
CME CB  HB2  sing N N 77  
CME CB  HB3  sing N N 78  
CME SG  SD   sing N N 79  
CME SD  CE   sing N N 80  
CME CE  CZ   sing N N 81  
CME CE  HE2  sing N N 82  
CME CE  HE3  sing N N 83  
CME CZ  OH   sing N N 84  
CME CZ  HZ2  sing N N 85  
CME CZ  HZ3  sing N N 86  
CME OH  HH   sing N N 87  
CME C   O    doub N N 88  
CME C   OXT  sing N N 89  
CME OXT HXT  sing N N 90  
CYS N   CA   sing N N 91  
CYS N   H    sing N N 92  
CYS N   H2   sing N N 93  
CYS CA  C    sing N N 94  
CYS CA  CB   sing N N 95  
CYS CA  HA   sing N N 96  
CYS C   O    doub N N 97  
CYS C   OXT  sing N N 98  
CYS CB  SG   sing N N 99  
CYS CB  HB2  sing N N 100 
CYS CB  HB3  sing N N 101 
CYS SG  HG   sing N N 102 
CYS OXT HXT  sing N N 103 
GLN N   CA   sing N N 104 
GLN N   H    sing N N 105 
GLN N   H2   sing N N 106 
GLN CA  C    sing N N 107 
GLN CA  CB   sing N N 108 
GLN CA  HA   sing N N 109 
GLN C   O    doub N N 110 
GLN C   OXT  sing N N 111 
GLN CB  CG   sing N N 112 
GLN CB  HB2  sing N N 113 
GLN CB  HB3  sing N N 114 
GLN CG  CD   sing N N 115 
GLN CG  HG2  sing N N 116 
GLN CG  HG3  sing N N 117 
GLN CD  OE1  doub N N 118 
GLN CD  NE2  sing N N 119 
GLN NE2 HE21 sing N N 120 
GLN NE2 HE22 sing N N 121 
GLN OXT HXT  sing N N 122 
GLU N   CA   sing N N 123 
GLU N   H    sing N N 124 
GLU N   H2   sing N N 125 
GLU CA  C    sing N N 126 
GLU CA  CB   sing N N 127 
GLU CA  HA   sing N N 128 
GLU C   O    doub N N 129 
GLU C   OXT  sing N N 130 
GLU CB  CG   sing N N 131 
GLU CB  HB2  sing N N 132 
GLU CB  HB3  sing N N 133 
GLU CG  CD   sing N N 134 
GLU CG  HG2  sing N N 135 
GLU CG  HG3  sing N N 136 
GLU CD  OE1  doub N N 137 
GLU CD  OE2  sing N N 138 
GLU OE2 HE2  sing N N 139 
GLU OXT HXT  sing N N 140 
GLY N   CA   sing N N 141 
GLY N   H    sing N N 142 
GLY N   H2   sing N N 143 
GLY CA  C    sing N N 144 
GLY CA  HA2  sing N N 145 
GLY CA  HA3  sing N N 146 
GLY C   O    doub N N 147 
GLY C   OXT  sing N N 148 
GLY OXT HXT  sing N N 149 
HIS N   CA   sing N N 150 
HIS N   H    sing N N 151 
HIS N   H2   sing N N 152 
HIS CA  C    sing N N 153 
HIS CA  CB   sing N N 154 
HIS CA  HA   sing N N 155 
HIS C   O    doub N N 156 
HIS C   OXT  sing N N 157 
HIS CB  CG   sing N N 158 
HIS CB  HB2  sing N N 159 
HIS CB  HB3  sing N N 160 
HIS CG  ND1  sing Y N 161 
HIS CG  CD2  doub Y N 162 
HIS ND1 CE1  doub Y N 163 
HIS ND1 HD1  sing N N 164 
HIS CD2 NE2  sing Y N 165 
HIS CD2 HD2  sing N N 166 
HIS CE1 NE2  sing Y N 167 
HIS CE1 HE1  sing N N 168 
HIS NE2 HE2  sing N N 169 
HIS OXT HXT  sing N N 170 
HOH O   H1   sing N N 171 
HOH O   H2   sing N N 172 
ILE N   CA   sing N N 173 
ILE N   H    sing N N 174 
ILE N   H2   sing N N 175 
ILE CA  C    sing N N 176 
ILE CA  CB   sing N N 177 
ILE CA  HA   sing N N 178 
ILE C   O    doub N N 179 
ILE C   OXT  sing N N 180 
ILE CB  CG1  sing N N 181 
ILE CB  CG2  sing N N 182 
ILE CB  HB   sing N N 183 
ILE CG1 CD1  sing N N 184 
ILE CG1 HG12 sing N N 185 
ILE CG1 HG13 sing N N 186 
ILE CG2 HG21 sing N N 187 
ILE CG2 HG22 sing N N 188 
ILE CG2 HG23 sing N N 189 
ILE CD1 HD11 sing N N 190 
ILE CD1 HD12 sing N N 191 
ILE CD1 HD13 sing N N 192 
ILE OXT HXT  sing N N 193 
LEU N   CA   sing N N 194 
LEU N   H    sing N N 195 
LEU N   H2   sing N N 196 
LEU CA  C    sing N N 197 
LEU CA  CB   sing N N 198 
LEU CA  HA   sing N N 199 
LEU C   O    doub N N 200 
LEU C   OXT  sing N N 201 
LEU CB  CG   sing N N 202 
LEU CB  HB2  sing N N 203 
LEU CB  HB3  sing N N 204 
LEU CG  CD1  sing N N 205 
LEU CG  CD2  sing N N 206 
LEU CG  HG   sing N N 207 
LEU CD1 HD11 sing N N 208 
LEU CD1 HD12 sing N N 209 
LEU CD1 HD13 sing N N 210 
LEU CD2 HD21 sing N N 211 
LEU CD2 HD22 sing N N 212 
LEU CD2 HD23 sing N N 213 
LEU OXT HXT  sing N N 214 
LYS N   CA   sing N N 215 
LYS N   H    sing N N 216 
LYS N   H2   sing N N 217 
LYS CA  C    sing N N 218 
LYS CA  CB   sing N N 219 
LYS CA  HA   sing N N 220 
LYS C   O    doub N N 221 
LYS C   OXT  sing N N 222 
LYS CB  CG   sing N N 223 
LYS CB  HB2  sing N N 224 
LYS CB  HB3  sing N N 225 
LYS CG  CD   sing N N 226 
LYS CG  HG2  sing N N 227 
LYS CG  HG3  sing N N 228 
LYS CD  CE   sing N N 229 
LYS CD  HD2  sing N N 230 
LYS CD  HD3  sing N N 231 
LYS CE  NZ   sing N N 232 
LYS CE  HE2  sing N N 233 
LYS CE  HE3  sing N N 234 
LYS NZ  HZ1  sing N N 235 
LYS NZ  HZ2  sing N N 236 
LYS NZ  HZ3  sing N N 237 
LYS OXT HXT  sing N N 238 
MET N   CA   sing N N 239 
MET N   H    sing N N 240 
MET N   H2   sing N N 241 
MET CA  C    sing N N 242 
MET CA  CB   sing N N 243 
MET CA  HA   sing N N 244 
MET C   O    doub N N 245 
MET C   OXT  sing N N 246 
MET CB  CG   sing N N 247 
MET CB  HB2  sing N N 248 
MET CB  HB3  sing N N 249 
MET CG  SD   sing N N 250 
MET CG  HG2  sing N N 251 
MET CG  HG3  sing N N 252 
MET SD  CE   sing N N 253 
MET CE  HE1  sing N N 254 
MET CE  HE2  sing N N 255 
MET CE  HE3  sing N N 256 
MET OXT HXT  sing N N 257 
PHE N   CA   sing N N 258 
PHE N   H    sing N N 259 
PHE N   H2   sing N N 260 
PHE CA  C    sing N N 261 
PHE CA  CB   sing N N 262 
PHE CA  HA   sing N N 263 
PHE C   O    doub N N 264 
PHE C   OXT  sing N N 265 
PHE CB  CG   sing N N 266 
PHE CB  HB2  sing N N 267 
PHE CB  HB3  sing N N 268 
PHE CG  CD1  doub Y N 269 
PHE CG  CD2  sing Y N 270 
PHE CD1 CE1  sing Y N 271 
PHE CD1 HD1  sing N N 272 
PHE CD2 CE2  doub Y N 273 
PHE CD2 HD2  sing N N 274 
PHE CE1 CZ   doub Y N 275 
PHE CE1 HE1  sing N N 276 
PHE CE2 CZ   sing Y N 277 
PHE CE2 HE2  sing N N 278 
PHE CZ  HZ   sing N N 279 
PHE OXT HXT  sing N N 280 
PRO N   CA   sing N N 281 
PRO N   CD   sing N N 282 
PRO N   H    sing N N 283 
PRO CA  C    sing N N 284 
PRO CA  CB   sing N N 285 
PRO CA  HA   sing N N 286 
PRO C   O    doub N N 287 
PRO C   OXT  sing N N 288 
PRO CB  CG   sing N N 289 
PRO CB  HB2  sing N N 290 
PRO CB  HB3  sing N N 291 
PRO CG  CD   sing N N 292 
PRO CG  HG2  sing N N 293 
PRO CG  HG3  sing N N 294 
PRO CD  HD2  sing N N 295 
PRO CD  HD3  sing N N 296 
PRO OXT HXT  sing N N 297 
SER N   CA   sing N N 298 
SER N   H    sing N N 299 
SER N   H2   sing N N 300 
SER CA  C    sing N N 301 
SER CA  CB   sing N N 302 
SER CA  HA   sing N N 303 
SER C   O    doub N N 304 
SER C   OXT  sing N N 305 
SER CB  OG   sing N N 306 
SER CB  HB2  sing N N 307 
SER CB  HB3  sing N N 308 
SER OG  HG   sing N N 309 
SER OXT HXT  sing N N 310 
SO4 S   O1   doub N N 311 
SO4 S   O2   doub N N 312 
SO4 S   O3   sing N N 313 
SO4 S   O4   sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TRP N   CA   sing N N 331 
TRP N   H    sing N N 332 
TRP N   H2   sing N N 333 
TRP CA  C    sing N N 334 
TRP CA  CB   sing N N 335 
TRP CA  HA   sing N N 336 
TRP C   O    doub N N 337 
TRP C   OXT  sing N N 338 
TRP CB  CG   sing N N 339 
TRP CB  HB2  sing N N 340 
TRP CB  HB3  sing N N 341 
TRP CG  CD1  doub Y N 342 
TRP CG  CD2  sing Y N 343 
TRP CD1 NE1  sing Y N 344 
TRP CD1 HD1  sing N N 345 
TRP CD2 CE2  doub Y N 346 
TRP CD2 CE3  sing Y N 347 
TRP NE1 CE2  sing Y N 348 
TRP NE1 HE1  sing N N 349 
TRP CE2 CZ2  sing Y N 350 
TRP CE3 CZ3  doub Y N 351 
TRP CE3 HE3  sing N N 352 
TRP CZ2 CH2  doub Y N 353 
TRP CZ2 HZ2  sing N N 354 
TRP CZ3 CH2  sing Y N 355 
TRP CZ3 HZ3  sing N N 356 
TRP CH2 HH2  sing N N 357 
TRP OXT HXT  sing N N 358 
TYR N   CA   sing N N 359 
TYR N   H    sing N N 360 
TYR N   H2   sing N N 361 
TYR CA  C    sing N N 362 
TYR CA  CB   sing N N 363 
TYR CA  HA   sing N N 364 
TYR C   O    doub N N 365 
TYR C   OXT  sing N N 366 
TYR CB  CG   sing N N 367 
TYR CB  HB2  sing N N 368 
TYR CB  HB3  sing N N 369 
TYR CG  CD1  doub Y N 370 
TYR CG  CD2  sing Y N 371 
TYR CD1 CE1  sing Y N 372 
TYR CD1 HD1  sing N N 373 
TYR CD2 CE2  doub Y N 374 
TYR CD2 HD2  sing N N 375 
TYR CE1 CZ   doub Y N 376 
TYR CE1 HE1  sing N N 377 
TYR CE2 CZ   sing Y N 378 
TYR CE2 HE2  sing N N 379 
TYR CZ  OH   sing N N 380 
TYR OH  HH   sing N N 381 
TYR OXT HXT  sing N N 382 
VAL N   CA   sing N N 383 
VAL N   H    sing N N 384 
VAL N   H2   sing N N 385 
VAL CA  C    sing N N 386 
VAL CA  CB   sing N N 387 
VAL CA  HA   sing N N 388 
VAL C   O    doub N N 389 
VAL C   OXT  sing N N 390 
VAL CB  CG1  sing N N 391 
VAL CB  CG2  sing N N 392 
VAL CB  HB   sing N N 393 
VAL CG1 HG11 sing N N 394 
VAL CG1 HG12 sing N N 395 
VAL CG1 HG13 sing N N 396 
VAL CG2 HG21 sing N N 397 
VAL CG2 HG22 sing N N 398 
VAL CG2 HG23 sing N N 399 
VAL OXT HXT  sing N N 400 
WM6 O1  C1   sing N N 401 
WM6 C1  C2   sing N N 402 
WM6 C1  C16  sing N N 403 
WM6 C2  O2   sing N N 404 
WM6 O2  C3   sing N N 405 
WM6 C3  C4   sing Y N 406 
WM6 C3  C8   doub Y N 407 
WM6 C4  C5   doub Y N 408 
WM6 C5  O3   sing N N 409 
WM6 C5  C6   sing Y N 410 
WM6 C6  C7   doub Y N 411 
WM6 C7  O4   sing N N 412 
WM6 C7  C8   sing Y N 413 
WM6 C8  C9   sing N N 414 
WM6 C9  O5   doub N N 415 
WM6 C9  O6   sing N N 416 
WM6 O6  C10  sing N N 417 
WM6 C10 C11  sing N N 418 
WM6 C11 C12  sing N N 419 
WM6 C12 C13  sing N N 420 
WM6 C13 C14  sing N N 421 
WM6 C14 O7   doub N N 422 
WM6 C14 C15  sing N N 423 
WM6 C15 O8   sing N N 424 
WM6 C15 C16  sing N N 425 
WM6 C16 O9   sing N N 426 
WM6 C15 H15  sing N N 427 
WM6 C1  H2   sing N N 428 
WM6 C2  H3   sing N N 429 
WM6 C2  H4   sing N N 430 
WM6 C4  H5   sing N N 431 
WM6 C6  H7   sing N N 432 
WM6 C10 H9   sing N N 433 
WM6 C10 H10  sing N N 434 
WM6 C11 H12  sing N N 435 
WM6 C11 H11  sing N N 436 
WM6 C12 H13  sing N N 437 
WM6 C12 H121 sing N N 438 
WM6 C13 H14  sing N N 439 
WM6 C13 H131 sing N N 440 
WM6 C16 H17  sing N N 441 
WM6 O1  H1   sing N N 442 
WM6 O3  H6   sing N N 443 
WM6 O4  H8   sing N N 444 
WM6 O8  H16  sing N N 445 
WM6 O9  H18  sing N N 446 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-20-CE18-0025 
_pdbx_audit_support.ordinal                1 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8QRA 
_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]   0.020555 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007230 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014318 
_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]   0.017736 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A 1 15  ? -22.96571 20.14035  21.29161 1.000 72.10122 ? 9   PRO A N   1 
ATOM   2    C CA  . PRO A 1 15  ? -21.98206 20.12799  22.38248 1.000 71.28146 ? 9   PRO A CA  1 
ATOM   3    C C   . PRO A 1 15  ? -22.40880 21.00950  23.56094 1.000 71.72740 ? 9   PRO A C   1 
ATOM   4    O O   . PRO A 1 15  ? -22.51315 22.23039  23.42101 1.000 71.99264 ? 9   PRO A O   1 
ATOM   5    C CB  . PRO A 1 15  ? -20.70091 20.66708  21.72205 1.000 70.22293 ? 9   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 15  ? -21.11474 21.23079  20.37713 1.000 70.70960 ? 9   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 15  ? -22.59966 21.07221  20.21210 1.000 71.48500 ? 9   PRO A CD  1 
ATOM   8    N N   . GLU A 1 16  ? -22.66546 20.39190  24.71117 1.000 71.32274 ? 10  GLU A N   1 
ATOM   9    C CA  . GLU A 1 16  ? -23.01596 21.15224  25.89997 1.000 70.61070 ? 10  GLU A CA  1 
ATOM   10   C C   . GLU A 1 16  ? -21.76804 21.79199  26.50544 1.000 71.74358 ? 10  GLU A C   1 
ATOM   11   O O   . GLU A 1 16  ? -20.66436 21.24257  26.44185 1.000 71.13192 ? 10  GLU A O   1 
ATOM   12   C CB  . GLU A 1 16  ? -23.72638 20.25613  26.92230 0.800 68.25044 ? 10  GLU A CB  1 
ATOM   13   C CG  . GLU A 1 16  ? -25.03958 19.65368  26.40793 0.700 65.46199 ? 10  GLU A CG  1 
ATOM   14   C CD  . GLU A 1 16  ? -25.86902 18.98362  27.49457 0.700 62.80454 ? 10  GLU A CD  1 
ATOM   15   O OE1 . GLU A 1 16  ? -25.76694 19.39138  28.67383 0.700 62.32965 ? 10  GLU A OE1 1 
ATOM   16   O OE2 . GLU A 1 16  ? -26.63221 18.05072  27.16417 0.700 61.37177 ? 10  GLU A OE2 1 
ATOM   17   N N   . MET A 1 17  ? -21.94788 22.98541  27.06493 1.000 73.25310 ? 11  MET A N   1 
ATOM   18   C CA  . MET A 1 17  ? -20.88005 23.71496  27.73124 1.000 73.93164 ? 11  MET A CA  1 
ATOM   19   C C   . MET A 1 17  ? -21.21278 23.86590  29.20607 1.000 71.78349 ? 11  MET A C   1 
ATOM   20   O O   . MET A 1 17  ? -22.35850 24.14574  29.56660 1.000 71.08913 ? 11  MET A O   1 
ATOM   21   C CB  . MET A 1 17  ? -20.67965 25.09284  27.12001 0.700 76.83362 ? 11  MET A CB  1 
ATOM   22   C CG  . MET A 1 17  ? -19.27768 25.61505  27.28245 0.700 79.11897 ? 11  MET A CG  1 
ATOM   23   S SD  . MET A 1 17  ? -18.90819 26.92464  26.11023 0.700 81.61486 ? 11  MET A SD  1 
ATOM   24   C CE  . MET A 1 17  ? -19.23768 26.10504  24.54705 0.700 82.72843 ? 11  MET A CE  1 
ATOM   25   N N   . VAL A 1 18  ? -20.21241 23.68214  30.05946 1.000 70.96697 ? 12  VAL A N   1 
ATOM   26   C CA  . VAL A 1 18  ? -20.38183 23.83497  31.49882 1.000 70.00054 ? 12  VAL A CA  1 
ATOM   27   C C   . VAL A 1 18  ? -19.30453 24.80225  31.96301 1.000 70.21045 ? 12  VAL A C   1 
ATOM   28   O O   . VAL A 1 18  ? -18.10927 24.50340  31.84270 1.000 70.70169 ? 12  VAL A O   1 
ATOM   29   C CB  . VAL A 1 18  ? -20.28409 22.49911  32.25365 1.000 68.18111 ? 12  VAL A CB  1 
ATOM   30   C CG1 . VAL A 1 18  ? -20.27833 22.74306  33.75890 1.000 68.05168 ? 12  VAL A CG1 1 
ATOM   31   C CG2 . VAL A 1 18  ? -21.41801 21.57386  31.87162 1.000 67.01599 ? 12  VAL A CG2 1 
ATOM   32   N N   . ARG A 1 19  ? -19.72510 25.96002  32.47713 1.000 69.95956 ? 13  ARG A N   1 
ATOM   33   C CA  . ARG A 1 19  ? -18.84023 27.00392  33.00158 1.000 70.13273 ? 13  ARG A CA  1 
ATOM   34   C C   . ARG A 1 19  ? -17.69956 27.29836  32.02768 1.000 72.10878 ? 13  ARG A C   1 
ATOM   35   O O   . ARG A 1 19  ? -16.51642 27.17287  32.35555 1.000 72.15328 ? 13  ARG A O   1 
ATOM   36   C CB  . ARG A 1 19  ? -18.28296 26.62040  34.37541 0.800 68.46244 ? 13  ARG A CB  1 
ATOM   37   C CG  . ARG A 1 19  ? -19.27843 25.95803  35.30837 0.700 66.57135 ? 13  ARG A CG  1 
ATOM   38   C CD  . ARG A 1 19  ? -18.95188 26.21847  36.76943 0.600 64.67703 ? 13  ARG A CD  1 
ATOM   39   N NE  . ARG A 1 19  ? -20.15497 26.20308  37.59156 0.500 63.04802 ? 13  ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 19  ? -20.15595 26.10318  38.91278 0.500 61.63481 ? 13  ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 19  ? -19.03056 26.12936  39.60805 0.500 61.75328 ? 13  ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 19  ? -21.31448 25.97059  39.55252 0.500 60.41507 ? 13  ARG A NH2 1 
ATOM   43   N N   . GLY A 1 20  ? -18.08042 27.68190  30.80781 1.000 73.67458 ? 14  GLY A N   1 
ATOM   44   C CA  . GLY A 1 20  ? -17.11807 27.96875  29.75814 1.000 75.35775 ? 14  GLY A CA  1 
ATOM   45   C C   . GLY A 1 20  ? -16.18217 26.81597  29.43683 1.000 77.07407 ? 14  GLY A C   1 
ATOM   46   O O   . GLY A 1 20  ? -14.96607 27.00567  29.31167 1.000 78.55445 ? 14  GLY A O   1 
ATOM   47   N N   . GLN A 1 21  ? -16.73119 25.61057  29.30601 1.000 76.12624 ? 15  GLN A N   1 
ATOM   48   C CA  . GLN A 1 21  ? -15.92301 24.44233  28.97114 1.000 74.60739 ? 15  GLN A CA  1 
ATOM   49   C C   . GLN A 1 21  ? -16.76815 23.49079  28.13927 1.000 73.08279 ? 15  GLN A C   1 
ATOM   50   O O   . GLN A 1 21  ? -17.78128 22.97354  28.62475 1.000 74.04802 ? 15  GLN A O   1 
ATOM   51   C CB  . GLN A 1 21  ? -15.40077 23.74938  30.23509 0.800 73.96583 ? 15  GLN A CB  1 
ATOM   52   C CG  . GLN A 1 21  ? -14.60356 22.48430  29.96153 0.700 72.83891 ? 15  GLN A CG  1 
ATOM   53   C CD  . GLN A 1 21  ? -13.25699 22.48695  30.66007 0.600 71.54446 ? 15  GLN A CD  1 
ATOM   54   O OE1 . GLN A 1 21  ? -12.43129 23.36349  30.41990 0.600 70.88425 ? 15  GLN A OE1 1 
ATOM   55   N NE2 . GLN A 1 21  ? -13.01643 21.48881  31.50494 0.600 71.37840 ? 15  GLN A NE2 1 
ATOM   56   N N   . VAL A 1 22  ? -16.35853 23.27969  26.88627 1.000 69.57557 ? 16  VAL A N   1 
ATOM   57   C CA  . VAL A 1 22  ? -17.03650 22.32864  26.01207 1.000 65.89644 ? 16  VAL A CA  1 
ATOM   58   C C   . VAL A 1 22  ? -16.92068 20.91978  26.58002 1.000 62.56947 ? 16  VAL A C   1 
ATOM   59   O O   . VAL A 1 22  ? -15.83965 20.49057  26.99929 1.000 62.55157 ? 16  VAL A O   1 
ATOM   60   C CB  . VAL A 1 22  ? -16.43594 22.38248  24.59762 1.000 65.04142 ? 16  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 22  ? -16.88965 21.17500  23.78195 1.000 64.29505 ? 16  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 22  ? -16.78229 23.69817  23.90676 1.000 65.77616 ? 16  VAL A CG2 1 
ATOM   63   N N   . PHE A 1 23  ? -18.03539 20.18340  26.56618 1.000 60.31183 ? 17  PHE A N   1 
ATOM   64   C CA  . PHE A 1 23  ? -18.10403 18.77396  26.96325 1.000 57.47903 ? 17  PHE A CA  1 
ATOM   65   C C   . PHE A 1 23  ? -18.68689 17.97202  25.79761 1.000 56.52879 ? 17  PHE A C   1 
ATOM   66   O O   . PHE A 1 23  ? -19.90835 17.83834  25.67637 1.000 57.97540 ? 17  PHE A O   1 
ATOM   67   C CB  . PHE A 1 23  ? -18.95200 18.61137  28.22544 1.000 57.06073 ? 17  PHE A CB  1 
ATOM   68   C CG  . PHE A 1 23  ? -18.16598 18.27665  29.46436 1.000 54.81118 ? 17  PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 23  ? -17.39247 19.23729  30.08799 1.000 54.14046 ? 17  PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 23  ? -18.21113 16.99888  30.00640 1.000 53.70717 ? 17  PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 23  ? -16.67465 18.93377  31.22397 1.000 53.24598 ? 17  PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 23  ? -17.49178 16.68226  31.14652 1.000 52.40457 ? 17  PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 23  ? -16.72086 17.64772  31.75624 1.000 52.24361 ? 17  PHE A CZ  1 
ATOM   74   N N   . ASP A 1 24  ? -17.82192 17.42297  24.94386 1.000 55.00263 ? 18  ASP A N   1 
ATOM   75   C CA  . ASP A 1 24  ? -18.27635 16.72840  23.73295 1.000 53.73992 ? 18  ASP A CA  1 
ATOM   76   C C   . ASP A 1 24  ? -18.55232 15.25855  24.02676 1.000 47.85044 ? 18  ASP A C   1 
ATOM   77   O O   . ASP A 1 24  ? -17.82776 14.36189  23.60852 1.000 48.94216 ? 18  ASP A O   1 
ATOM   78   C CB  . ASP A 1 24  ? -17.26011 16.87238  22.60682 0.800 56.47301 ? 18  ASP A CB  1 
ATOM   79   C CG  . ASP A 1 24  ? -17.76245 17.73555  21.48582 0.800 58.76462 ? 18  ASP A CG  1 
ATOM   80   O OD1 . ASP A 1 24  ? -18.46003 17.18582  20.60386 0.600 59.26029 ? 18  ASP A OD1 1 
ATOM   81   O OD2 . ASP A 1 24  ? -17.46947 18.94832  21.47980 0.600 60.24007 ? 18  ASP A OD2 1 
ATOM   82   N N   . VAL A 1 25  ? -19.65783 15.01653  24.73192 1.000 44.23109 ? 19  VAL A N   1 
ATOM   83   C CA  . VAL A 1 25  ? -19.94770 13.67960  25.22418 1.000 41.55671 ? 19  VAL A CA  1 
ATOM   84   C C   . VAL A 1 25  ? -21.23611 13.11977  24.63939 1.000 42.69486 ? 19  VAL A C   1 
ATOM   85   O O   . VAL A 1 25  ? -21.67606 12.04182  25.03248 1.000 41.58766 ? 19  VAL A O   1 
ATOM   86   C CB  . VAL A 1 25  ? -19.96722 13.65543  26.76887 1.000 39.38844 ? 19  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 25  ? -18.60992 14.11483  27.30063 1.000 37.99897 ? 19  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 25  ? -21.08412 14.53615  27.32480 1.000 42.29505 ? 19  VAL A CG2 1 
ATOM   89   N N   . GLY A 1 26  ? -21.82748 13.80497  23.66944 1.000 44.40594 ? 20  GLY A N   1 
ATOM   90   C CA  . GLY A 1 26  ? -23.07269 13.35179  23.09242 1.000 46.28949 ? 20  GLY A CA  1 
ATOM   91   C C   . GLY A 1 26  ? -22.86639 12.31631  22.00922 1.000 46.57825 ? 20  GLY A C   1 
ATOM   92   O O   . GLY A 1 26  ? -21.76322 12.12146  21.46792 1.000 46.26823 ? 20  GLY A O   1 
ATOM   93   N N   . PRO A 1 27  ? -23.96445 11.64596  21.63704 1.000 46.07657 ? 21  PRO A N   1 
ATOM   94   C CA  . PRO A 1 27  ? -25.31107 11.85920  22.17860 1.000 44.74947 ? 21  PRO A CA  1 
ATOM   95   C C   . PRO A 1 27  ? -25.64765 11.01894  23.41399 1.000 43.76645 ? 21  PRO A C   1 
ATOM   96   O O   . PRO A 1 27  ? -26.72642 11.20065  24.00438 1.000 43.67718 ? 21  PRO A O   1 
ATOM   97   C CB  . PRO A 1 27  ? -26.20420 11.44666  21.01202 1.000 45.90975 ? 21  PRO A CB  1 
ATOM   98   C CG  . PRO A 1 27  ? -25.42555 10.32457  20.35553 1.000 46.29063 ? 21  PRO A CG  1 
ATOM   99   C CD  . PRO A 1 27  ? -23.97385 10.75894  20.45972 1.000 45.99581 ? 21  PRO A CD  1 
ATOM   100  N N   . ARG A 1 28  ? -24.75004 10.10491  23.79765 1.000 41.52000 ? 22  ARG A N   1 
ATOM   101  C CA  . ARG A 1 28  ? -25.09777 9.15874   24.85948 1.000 39.30886 ? 22  ARG A CA  1 
ATOM   102  C C   . ARG A 1 28  ? -25.30733 9.86428   26.19122 1.000 38.84316 ? 22  ARG A C   1 
ATOM   103  O O   . ARG A 1 28  ? -26.17806 9.46528   26.97869 1.000 41.03521 ? 22  ARG A O   1 
ATOM   104  C CB  . ARG A 1 28  ? -24.02758 8.07438   24.99629 1.000 38.30870 ? 22  ARG A CB  1 
ATOM   105  C CG  . ARG A 1 28  ? -24.32003 7.13657   26.14724 1.000 37.60666 ? 22  ARG A CG  1 
ATOM   106  C CD  . ARG A 1 28  ? -23.48268 5.87311   26.11295 1.000 37.17560 ? 22  ARG A CD  1 
ATOM   107  N NE  . ARG A 1 28  ? -23.67592 5.06479   27.31048 1.000 36.85437 ? 22  ARG A NE  1 
ATOM   108  C CZ  . ARG A 1 28  ? -22.89739 4.04489   27.63540 1.000 38.72697 ? 22  ARG A CZ  1 
ATOM   109  N NH1 . ARG A 1 28  ? -21.89451 3.66959   26.85500 1.000 39.14423 ? 22  ARG A NH1 1 
ATOM   110  N NH2 . ARG A 1 28  ? -23.12780 3.38664   28.76734 1.000 39.82463 ? 22  ARG A NH2 1 
ATOM   111  N N   . TYR A 1 29  ? -24.53145 10.91334  26.46438 1.000 36.94300 ? 23  TYR A N   1 
ATOM   112  C CA  . TYR A 1 29  ? -24.54715 11.58693  27.76369 1.000 37.26849 ? 23  TYR A CA  1 
ATOM   113  C C   . TYR A 1 29  ? -25.07733 13.00252  27.59044 1.000 40.67940 ? 23  TYR A C   1 
ATOM   114  O O   . TYR A 1 29  ? -24.54781 13.77084  26.77598 1.000 42.57996 ? 23  TYR A O   1 
ATOM   115  C CB  . TYR A 1 29  ? -23.14820 11.58395  28.38450 1.000 34.83375 ? 23  TYR A CB  1 
ATOM   116  C CG  . TYR A 1 29  ? -22.58354 10.19997  28.50484 1.000 34.06674 ? 23  TYR A CG  1 
ATOM   117  C CD1 . TYR A 1 29  ? -23.01414 9.33580   29.52009 1.000 31.83013 ? 23  TYR A CD1 1 
ATOM   118  C CD2 . TYR A 1 29  ? -21.61547 9.74256   27.61188 1.000 31.26848 ? 23  TYR A CD2 1 
ATOM   119  C CE1 . TYR A 1 29  ? -22.49087 8.04764   29.64036 1.000 30.93495 ? 23  TYR A CE1 1 
ATOM   120  C CE2 . TYR A 1 29  ? -21.10943 8.46147   27.69731 1.000 32.46318 ? 23  TYR A CE2 1 
ATOM   121  C CZ  . TYR A 1 29  ? -21.52917 7.61819   28.72755 1.000 31.11834 ? 23  TYR A CZ  1 
ATOM   122  O OH  . TYR A 1 29  ? -21.00037 6.35228   28.83953 1.000 30.44131 ? 23  TYR A OH  1 
ATOM   123  N N   . THR A 1 30  ? -26.13177 13.33507  28.33629 1.000 42.67994 ? 24  THR A N   1 
ATOM   124  C CA  . THR A 1 30  ? -26.80684 14.62085  28.20690 1.000 44.27676 ? 24  THR A CA  1 
ATOM   125  C C   . THR A 1 30  ? -27.12061 15.16888  29.58916 1.000 45.18587 ? 24  THR A C   1 
ATOM   126  O O   . THR A 1 30  ? -26.91885 14.49551  30.59310 1.000 44.75745 ? 24  THR A O   1 
ATOM   127  C CB  . THR A 1 30  ? -28.10631 14.50981  27.39160 1.000 46.35926 ? 24  THR A CB  1 
ATOM   128  O OG1 . THR A 1 30  ? -28.94286 13.48592  27.94812 1.000 46.62895 ? 24  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 30  ? -27.80810 14.19657  25.92461 1.000 48.19227 ? 24  THR A CG2 1 
ATOM   130  N N   . ASN A 1 31  ? -27.61127 16.41463  29.62373 1.000 47.87284 ? 25  ASN A N   1 
ATOM   131  C CA  . ASN A 1 31  ? -28.08486 17.10263  30.83739 1.000 48.41284 ? 25  ASN A CA  1 
ATOM   132  C C   . ASN A 1 31  ? -26.98905 17.20676  31.90654 1.000 47.62908 ? 25  ASN A C   1 
ATOM   133  O O   . ASN A 1 31  ? -27.11757 16.71571  33.02968 1.000 46.66213 ? 25  ASN A O   1 
ATOM   134  C CB  . ASN A 1 31  ? -29.34384 16.43115  31.40213 0.700 50.00855 ? 25  ASN A CB  1 
ATOM   135  C CG  . ASN A 1 31  ? -30.11180 17.34452  32.34455 0.600 51.62726 ? 25  ASN A CG  1 
ATOM   136  O OD1 . ASN A 1 31  ? -30.02298 18.56772  32.24247 0.600 52.68628 ? 25  ASN A OD1 1 
ATOM   137  N ND2 . ASN A 1 31  ? -30.90441 16.75501  33.23855 0.600 52.50876 ? 25  ASN A ND2 1 
ATOM   138  N N   . LEU A 1 32  ? -25.94451 17.94721  31.54474 1.000 47.40315 ? 26  LEU A N   1 
ATOM   139  C CA  . LEU A 1 32  ? -24.72510 18.02766  32.33571 1.000 47.87087 ? 26  LEU A CA  1 
ATOM   140  C C   . LEU A 1 32  ? -24.86586 18.99198  33.51843 1.000 48.86075 ? 26  LEU A C   1 
ATOM   141  O O   . LEU A 1 32  ? -25.60772 19.98158  33.45623 1.000 51.16191 ? 26  LEU A O   1 
ATOM   142  C CB  . LEU A 1 32  ? -23.56490 18.45863  31.43664 1.000 48.80101 ? 26  LEU A CB  1 
ATOM   143  C CG  . LEU A 1 32  ? -22.87020 17.42920  30.53266 1.000 50.19210 ? 26  LEU A CG  1 
ATOM   144  C CD1 . LEU A 1 32  ? -23.80365 16.39530  29.93726 1.000 48.62803 ? 26  LEU A CD1 1 
ATOM   145  C CD2 . LEU A 1 32  ? -22.14702 18.16728  29.40277 1.000 52.00384 ? 26  LEU A CD2 1 
ATOM   146  N N   . SER A 1 33  ? -24.14124 18.68570  34.60758 1.000 46.93728 ? 27  SER A N   1 
ATOM   147  C CA  . SER A 1 33  ? -24.03080 19.54888  35.78409 1.000 46.02544 ? 27  SER A CA  1 
ATOM   148  C C   . SER A 1 33  ? -22.60453 19.54432  36.31444 1.000 46.65894 ? 27  SER A C   1 
ATOM   149  O O   . SER A 1 33  ? -22.00068 18.47860  36.46879 1.000 45.76611 ? 27  SER A O   1 
ATOM   150  C CB  . SER A 1 33  ? -24.97844 19.11437  36.91481 1.000 47.16923 ? 27  SER A CB  1 
ATOM   151  O OG  . SER A 1 33  ? -26.32738 19.06674  36.48414 1.000 49.03696 ? 27  SER A OG  1 
ATOM   152  N N   . TYR A 1 34  ? -22.09072 20.73036  36.64332 1.000 46.86115 ? 28  TYR A N   1 
ATOM   153  C CA  . TYR A 1 34  ? -20.76648 20.83886  37.24571 1.000 47.66400 ? 28  TYR A CA  1 
ATOM   154  C C   . TYR A 1 34  ? -20.70738 20.11124  38.58716 1.000 49.64514 ? 28  TYR A C   1 
ATOM   155  O O   . TYR A 1 34  ? -21.67061 20.10938  39.36353 1.000 50.69566 ? 28  TYR A O   1 
ATOM   156  C CB  . TYR A 1 34  ? -20.39506 22.30793  37.45221 0.800 47.30570 ? 28  TYR A CB  1 
ATOM   157  C CG  . TYR A 1 34  ? -18.97794 22.51063  37.93496 0.600 46.96832 ? 28  TYR A CG  1 
ATOM   158  C CD1 . TYR A 1 34  ? -17.90398 22.37083  37.06855 0.600 48.93896 ? 28  TYR A CD1 1 
ATOM   159  C CD2 . TYR A 1 34  ? -18.71344 22.83397  39.25847 0.600 45.44923 ? 28  TYR A CD2 1 
ATOM   160  C CE1 . TYR A 1 34  ? -16.60351 22.55134  37.50473 0.600 49.50946 ? 28  TYR A CE1 1 
ATOM   161  C CE2 . TYR A 1 34  ? -17.41691 23.01689  39.70453 0.600 46.78583 ? 28  TYR A CE2 1 
ATOM   162  C CZ  . TYR A 1 34  ? -16.36784 22.87576  38.82319 0.600 48.98956 ? 28  TYR A CZ  1 
ATOM   163  O OH  . TYR A 1 34  ? -15.07730 23.06159  39.25755 0.600 50.03995 ? 28  TYR A OH  1 
ATOM   164  N N   . ILE A 1 35  ? -19.55046 19.49870  38.86431 1.000 50.05390 ? 29  ILE A N   1 
ATOM   165  C CA  . ILE A 1 35  ? -19.25654 18.90241  40.16321 1.000 52.40983 ? 29  ILE A CA  1 
ATOM   166  C C   . ILE A 1 35  ? -17.99810 19.50148  40.78823 1.000 57.01092 ? 29  ILE A C   1 
ATOM   167  O O   . ILE A 1 35  ? -18.00196 19.88897  41.96154 1.000 58.74233 ? 29  ILE A O   1 
ATOM   168  C CB  . ILE A 1 35  ? -19.14074 17.36156  40.07112 1.000 50.44966 ? 29  ILE A CB  1 
ATOM   169  C CG1 . ILE A 1 35  ? -20.48897 16.73029  39.73393 1.000 49.68232 ? 29  ILE A CG1 1 
ATOM   170  C CG2 . ILE A 1 35  ? -18.60183 16.77109  41.38439 1.000 50.26052 ? 29  ILE A CG2 1 
ATOM   171  C CD1 . ILE A 1 35  ? -20.43821 15.22071  39.69335 1.000 48.41825 ? 29  ILE A CD1 1 
ATOM   172  N N   . GLY A 1 36  ? -16.91036 19.57421  40.02737 1.000 59.12233 ? 30  GLY A N   1 
ATOM   173  C CA  . GLY A 1 36  ? -15.64678 20.02935  40.58714 1.000 61.85187 ? 30  GLY A CA  1 
ATOM   174  C C   . GLY A 1 36  ? -14.51233 19.91164  39.59050 1.000 63.91604 ? 30  GLY A C   1 
ATOM   175  O O   . GLY A 1 36  ? -14.73660 19.85063  38.37896 1.000 64.04881 ? 30  GLY A O   1 
ATOM   176  N N   . GLU A 1 37  ? -13.28342 19.86562  40.10913 1.000 65.41748 ? 31  GLU A N   1 
ATOM   177  C CA  . GLU A 1 37  ? -12.08070 19.89638  39.28280 1.000 68.32846 ? 31  GLU A CA  1 
ATOM   178  C C   . GLU A 1 37  ? -11.23900 18.64632  39.50896 1.000 70.98055 ? 31  GLU A C   1 
ATOM   179  O O   . GLU A 1 37  ? -11.00832 18.24415  40.65401 1.000 70.40279 ? 31  GLU A O   1 
ATOM   180  C CB  . GLU A 1 37  ? -11.24170 21.14580  39.58100 1.000 69.27680 ? 31  GLU A CB  1 
ATOM   181  C CG  . GLU A 1 37  ? -11.95509 22.45026  39.28344 1.000 70.62816 ? 31  GLU A CG  1 
ATOM   182  C CD  . GLU A 1 37  ? -12.06779 22.72310  37.79794 1.000 72.22150 ? 31  GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 37  ? -11.22787 22.19439  37.03424 1.000 71.65007 ? 31  GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 37  ? -13.00751 23.44655  37.39338 1.000 73.73401 ? 31  GLU A OE2 1 
ATOM   185  N N   . GLY A 1 38  ? -10.76738 18.05192  38.42034 1.000 73.34074 ? 32  GLY A N   1 
ATOM   186  C CA  . GLY A 1 38  ? -9.79335  16.96575  38.44736 1.000 74.26767 ? 32  GLY A CA  1 
ATOM   187  C C   . GLY A 1 38  ? -8.38927  17.46134  38.16390 1.000 75.52899 ? 32  GLY A C   1 
ATOM   188  O O   . GLY A 1 38  ? -8.00454  18.56906  38.55820 1.000 76.11076 ? 32  GLY A O   1 
ATOM   189  N N   . ALA A 1 39  ? -7.61169  16.63770  37.46185 1.000 76.07531 ? 33  ALA A N   1 
ATOM   190  C CA  . ALA A 1 39  ? -6.22511  16.99515  37.18159 1.000 76.53920 ? 33  ALA A CA  1 
ATOM   191  C C   . ALA A 1 39  ? -6.12797  18.00961  36.04241 1.000 75.92716 ? 33  ALA A C   1 
ATOM   192  O O   . ALA A 1 39  ? -5.67186  19.14231  36.24242 1.000 75.80769 ? 33  ALA A O   1 
ATOM   193  C CB  . ALA A 1 39  ? -5.41302  15.73498  36.86233 1.000 76.89934 ? 33  ALA A CB  1 
ATOM   194  N N   . TYR A 1 40  ? -6.55322  17.61749  34.83426 1.000 73.75784 ? 34  TYR A N   1 
ATOM   195  C CA  . TYR A 1 40  ? -6.39847  18.43337  33.63087 1.000 70.80115 ? 34  TYR A CA  1 
ATOM   196  C C   . TYR A 1 40  ? -7.75066  18.85029  33.06905 1.000 67.02965 ? 34  TYR A C   1 
ATOM   197  O O   . TYR A 1 40  ? -7.91919  18.96858  31.84981 1.000 66.61968 ? 34  TYR A O   1 
ATOM   198  C CB  . TYR A 1 40  ? -5.57174  17.68840  32.58066 1.000 71.50166 ? 34  TYR A CB  1 
ATOM   199  C CG  . TYR A 1 40  ? -4.30663  17.15152  33.19097 1.000 73.34777 ? 34  TYR A CG  1 
ATOM   200  C CD1 . TYR A 1 40  ? -3.51062  17.97555  33.98195 1.000 74.64191 ? 34  TYR A CD1 1 
ATOM   201  C CD2 . TYR A 1 40  ? -3.93741  15.81509  33.04759 1.000 73.81371 ? 34  TYR A CD2 1 
ATOM   202  C CE1 . TYR A 1 40  ? -2.36762  17.50272  34.58891 1.000 75.20513 ? 34  TYR A CE1 1 
ATOM   203  C CE2 . TYR A 1 40  ? -2.78172  15.32658  33.65267 1.000 74.58150 ? 34  TYR A CE2 1 
ATOM   204  C CZ  . TYR A 1 40  ? -2.00101  16.18618  34.42142 1.000 75.14273 ? 34  TYR A CZ  1 
ATOM   205  O OH  . TYR A 1 40  ? -0.84826  15.75756  35.03306 1.000 75.38804 ? 34  TYR A OH  1 
ATOM   206  N N   . GLY A 1 41  ? -8.71087  19.08426  33.95333 1.000 63.32670 ? 35  GLY A N   1 
ATOM   207  C CA  . GLY A 1 41  ? -10.05544 19.42802  33.54059 1.000 59.26732 ? 35  GLY A CA  1 
ATOM   208  C C   . GLY A 1 41  ? -11.02953 19.18764  34.67681 1.000 54.71340 ? 35  GLY A C   1 
ATOM   209  O O   . GLY A 1 41  ? -10.63734 18.87199  35.80296 1.000 53.72612 ? 35  GLY A O   1 
ATOM   210  N N   . MET A 1 42  ? -12.31028 19.33242  34.34650 1.000 51.24301 ? 36  MET A N   1 
ATOM   211  C CA  . MET A 1 42  ? -13.37346 19.34650  35.33662 1.000 47.95461 ? 36  MET A CA  1 
ATOM   212  C C   . MET A 1 42  ? -14.17107 18.04858  35.33548 1.000 41.49644 ? 36  MET A C   1 
ATOM   213  O O   . MET A 1 42  ? -14.11276 17.23976  34.40208 1.000 40.93165 ? 36  MET A O   1 
ATOM   214  C CB  . MET A 1 42  ? -14.30834 20.53694  35.10354 1.000 50.72557 ? 36  MET A CB  1 
ATOM   215  C CG  . MET A 1 42  ? -14.97135 20.56160  33.75663 0.900 51.78343 ? 36  MET A CG  1 
ATOM   216  S SD  . MET A 1 42  ? -16.44660 21.60630  33.71722 0.700 53.56249 ? 36  MET A SD  1 
ATOM   217  C CE  . MET A 1 42  ? -15.69190 23.22206  33.80614 0.650 53.64547 ? 36  MET A CE  1 
ATOM   218  N N   . VAL A 1 43  ? -14.93070 17.86987  36.41078 1.000 37.64894 ? 37  VAL A N   1 
ATOM   219  C CA  . VAL A 1 43  ? -15.79922 16.71743  36.59827 1.000 37.11532 ? 37  VAL A CA  1 
ATOM   220  C C   . VAL A 1 43  ? -17.23681 17.21055  36.56816 1.000 37.86728 ? 37  VAL A C   1 
ATOM   221  O O   . VAL A 1 43  ? -17.56681 18.21151  37.21733 1.000 38.96845 ? 37  VAL A O   1 
ATOM   222  C CB  . VAL A 1 43  ? -15.47881 15.99604  37.91626 1.000 37.71906 ? 37  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 43  ? -16.37915 14.80647  38.10148 1.000 37.33813 ? 37  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 43  ? -14.02230 15.55932  37.91329 1.000 38.45596 ? 37  VAL A CG2 1 
ATOM   225  N N   . CYS A 1 44  ? -18.07809 16.52811  35.79049 1.000 36.28515 ? 38  CYS A N   1 
ATOM   226  C CA  . CYS A 1 44  ? -19.49727 16.82937  35.69247 1.000 36.11461 ? 38  CYS A CA  1 
ATOM   227  C C   . CYS A 1 44  ? -20.30924 15.56034  35.88973 1.000 34.99805 ? 38  CYS A C   1 
ATOM   228  O O   . CYS A 1 44  ? -19.81174 14.44511  35.71475 1.000 33.43081 ? 38  CYS A O   1 
ATOM   229  C CB  . CYS A 1 44  ? -19.84788 17.43640  34.34437 0.900 37.49143 ? 38  CYS A CB  1 
ATOM   230  S SG  . CYS A 1 44  ? -19.11382 19.04081  34.08051 0.700 38.74815 ? 38  CYS A SG  1 
ATOM   231  N N   . SER A 1 45  ? -21.57009 15.74133  36.27266 1.000 35.73590 ? 39  SER A N   1 
ATOM   232  C CA  . SER A 1 45  ? -22.55392 14.67630  36.17646 1.000 37.23187 ? 39  SER A CA  1 
ATOM   233  C C   . SER A 1 45  ? -23.32140 14.81695  34.86388 1.000 36.53719 ? 39  SER A C   1 
ATOM   234  O O   . SER A 1 45  ? -23.36601 15.88502  34.25231 1.000 38.90327 ? 39  SER A O   1 
ATOM   235  C CB  . SER A 1 45  ? -23.51464 14.69340  37.36911 1.000 38.24846 ? 39  SER A CB  1 
ATOM   236  O OG  . SER A 1 45  ? -24.24078 15.91634  37.41823 1.000 39.24767 ? 39  SER A OG  1 
ATOM   237  N N   . ALA A 1 46  ? -23.90369 13.70928  34.42266 1.000 34.64204 ? 40  ALA A N   1 
ATOM   238  C CA  . ALA A 1 46  ? -24.58207 13.65346  33.13497 1.000 33.02177 ? 40  ALA A CA  1 
ATOM   239  C C   . ALA A 1 46  ? -25.54973 12.48504  33.17714 1.000 33.65801 ? 40  ALA A C   1 
ATOM   240  O O   . ALA A 1 46  ? -25.38741 11.56577  33.97306 1.000 33.44399 ? 40  ALA A O   1 
ATOM   241  C CB  . ALA A 1 46  ? -23.58765 13.48928  31.97624 1.000 33.47643 ? 40  ALA A CB  1 
ATOM   242  N N   . TYR A 1 47  ? -26.57260 12.53330  32.32395 1.000 33.43919 ? 41  TYR A N   1 
ATOM   243  C CA  . TYR A 1 47  ? -27.47260 11.39764  32.18507 1.000 34.99616 ? 41  TYR A CA  1 
ATOM   244  C C   . TYR A 1 47  ? -27.01937 10.46756  31.06337 1.000 35.94729 ? 41  TYR A C   1 
ATOM   245  O O   . TYR A 1 47  ? -26.74769 10.90847  29.94246 1.000 36.96742 ? 41  TYR A O   1 
ATOM   246  C CB  . TYR A 1 47  ? -28.90637 11.87447  31.95526 0.800 34.65550 ? 41  TYR A CB  1 
ATOM   247  C CG  . TYR A 1 47  ? -29.91154 10.75871  31.78978 0.700 32.30214 ? 41  TYR A CG  1 
ATOM   248  C CD1 . TYR A 1 47  ? -30.39001 10.06133  32.89818 0.600 33.49688 ? 41  TYR A CD1 1 
ATOM   249  C CD2 . TYR A 1 47  ? -30.45884 10.46095  30.54549 0.600 32.83559 ? 41  TYR A CD2 1 
ATOM   250  C CE1 . TYR A 1 47  ? -31.34245 9.05819   32.76373 0.600 35.21152 ? 41  TYR A CE1 1 
ATOM   251  C CE2 . TYR A 1 47  ? -31.42129 9.46112   30.40398 0.600 33.08082 ? 41  TYR A CE2 1 
ATOM   252  C CZ  . TYR A 1 47  ? -31.84852 8.75895   31.51576 0.600 35.46125 ? 41  TYR A CZ  1 
ATOM   253  O OH  . TYR A 1 47  ? -32.80216 7.76563   31.37867 0.600 37.62074 ? 41  TYR A OH  1 
ATOM   254  N N   . ASP A 1 48  ? -26.92898 9.17697   31.38666 1.000 36.47975 ? 42  ASP A N   1 
ATOM   255  C CA  . ASP A 1 48  ? -26.52681 8.11408   30.46516 1.000 36.64304 ? 42  ASP A CA  1 
ATOM   256  C C   . ASP A 1 48  ? -27.79372 7.57143   29.80452 1.000 39.26249 ? 42  ASP A C   1 
ATOM   257  O O   . ASP A 1 48  ? -28.54232 6.80002   30.40916 1.000 40.41304 ? 42  ASP A O   1 
ATOM   258  C CB  . ASP A 1 48  ? -25.77205 7.03497   31.23430 1.000 37.69496 ? 42  ASP A CB  1 
ATOM   259  C CG  . ASP A 1 48  ? -25.30593 5.88337   30.36708 1.000 38.99492 ? 42  ASP A CG  1 
ATOM   260  O OD1 . ASP A 1 48  ? -25.78183 5.73863   29.22168 1.000 39.64411 ? 42  ASP A OD1 1 
ATOM   261  O OD2 . ASP A 1 48  ? -24.44637 5.09952   30.85528 1.000 40.45026 ? 42  ASP A OD2 1 
ATOM   262  N N   . ASN A 1 49  ? -28.03668 7.97794   28.55422 1.000 40.09697 ? 43  ASN A N   1 
ATOM   263  C CA  . ASN A 1 49  ? -29.26773 7.59807   27.85562 1.000 41.17005 ? 43  ASN A CA  1 
ATOM   264  C C   . ASN A 1 49  ? -29.35784 6.11109   27.53146 1.000 41.75962 ? 43  ASN A C   1 
ATOM   265  O O   . ASN A 1 49  ? -30.47135 5.60648   27.29296 1.000 43.88585 ? 43  ASN A O   1 
ATOM   266  C CB  . ASN A 1 49  ? -29.39659 8.43637   26.59346 1.000 42.55828 ? 43  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 49  ? -29.74909 9.88053   26.89085 1.000 43.66508 ? 43  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 49  ? -30.92014 10.18700  27.13812 1.000 46.16009 ? 43  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 49  ? -28.77375 10.76419  26.87346 1.000 44.17866 ? 43  ASN A ND2 1 
ATOM   270  N N   . LEU A 1 50  ? -28.22682 5.40359   27.53332 1.000 43.62031 ? 44  LEU A N   1 
ATOM   271  C CA  . LEU A 1 50  ? -28.22290 3.95930   27.34924 1.000 45.45642 ? 44  LEU A CA  1 
ATOM   272  C C   . LEU A 1 50  ? -28.62816 3.24428   28.63418 1.000 47.25558 ? 44  LEU A C   1 
ATOM   273  O O   . LEU A 1 50  ? -29.56219 2.43443   28.63010 1.000 48.03027 ? 44  LEU A O   1 
ATOM   274  C CB  . LEU A 1 50  ? -26.83552 3.50342   26.88424 1.000 48.46043 ? 44  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 50  ? -26.60514 2.10657   26.29795 1.000 52.05597 ? 44  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 50  ? -25.32694 2.09496   25.49264 1.000 52.38584 ? 44  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 50  ? -26.53304 1.03489   27.36135 1.000 54.46201 ? 44  LEU A CD2 1 
ATOM   278  N N   . ASN A 1 51  ? -27.94910 3.53306   29.75009 1.000 47.34302 ? 45  ASN A N   1 
ATOM   279  C CA  . ASN A 1 51  ? -28.22548 2.82545   30.99437 1.000 48.30723 ? 45  ASN A CA  1 
ATOM   280  C C   . ASN A 1 51  ? -29.23880 3.53344   31.88326 1.000 49.00251 ? 45  ASN A C   1 
ATOM   281  O O   . ASN A 1 51  ? -29.52796 3.03067   32.97315 1.000 50.24741 ? 45  ASN A O   1 
ATOM   282  C CB  . ASN A 1 51  ? -26.93283 2.60274   31.78487 1.000 51.61025 ? 45  ASN A CB  1 
ATOM   283  C CG  . ASN A 1 51  ? -25.97431 1.66784   31.08164 1.000 55.34532 ? 45  ASN A CG  1 
ATOM   284  O OD1 . ASN A 1 51  ? -26.36983 0.61599   30.57986 1.000 57.86866 ? 45  ASN A OD1 1 
ATOM   285  N ND2 . ASN A 1 51  ? -24.69943 2.03776   31.05762 1.000 56.98194 ? 45  ASN A ND2 1 
ATOM   286  N N   . LYS A 1 52  ? -29.75104 4.69393   31.46057 1.000 48.24252 ? 46  LYS A N   1 
ATOM   287  C CA  . LYS A 1 52  ? -30.85028 5.39534   32.13487 1.000 45.79449 ? 46  LYS A CA  1 
ATOM   288  C C   . LYS A 1 52  ? -30.52557 5.69984   33.59940 1.000 45.35614 ? 46  LYS A C   1 
ATOM   289  O O   . LYS A 1 52  ? -31.36479 5.55134   34.49862 1.000 47.36569 ? 46  LYS A O   1 
ATOM   290  C CB  . LYS A 1 52  ? -32.15584 4.60743   31.99004 0.800 43.88862 ? 46  LYS A CB  1 
ATOM   291  C CG  . LYS A 1 52  ? -32.59008 4.54397   30.54065 0.700 46.36712 ? 46  LYS A CG  1 
ATOM   292  C CD  . LYS A 1 52  ? -33.92570 3.86496   30.34930 0.600 49.23209 ? 46  LYS A CD  1 
ATOM   293  C CE  . LYS A 1 52  ? -34.34065 3.91788   28.88446 0.600 51.07893 ? 46  LYS A CE  1 
ATOM   294  N NZ  . LYS A 1 52  ? -35.62506 3.19443   28.63053 0.600 51.44577 ? 46  LYS A NZ  1 
ATOM   295  N N   . VAL A 1 53  ? -29.28804 6.13091   33.83829 1.000 43.35097 ? 47  VAL A N   1 
ATOM   296  C CA  . VAL A 1 53  ? -28.81603 6.52701   35.15699 1.000 41.54376 ? 47  VAL A CA  1 
ATOM   297  C C   . VAL A 1 53  ? -27.89584 7.72114   34.95617 1.000 38.42155 ? 47  VAL A C   1 
ATOM   298  O O   . VAL A 1 53  ? -27.34297 7.92291   33.87538 1.000 36.77974 ? 47  VAL A O   1 
ATOM   299  C CB  . VAL A 1 53  ? -28.07793 5.37218   35.87445 1.000 43.45127 ? 47  VAL A CB  1 
ATOM   300  C CG1 . VAL A 1 53  ? -26.82131 4.98156   35.11718 1.000 41.84004 ? 47  VAL A CG1 1 
ATOM   301  C CG2 . VAL A 1 53  ? -27.74214 5.74164   37.30142 1.000 46.17218 ? 47  VAL A CG2 1 
ATOM   302  N N   . ARG A 1 54  ? -27.75090 8.53767   35.99603 1.000 36.70300 ? 48  ARG A N   1 
ATOM   303  C CA  . ARG A 1 54  ? -26.76023 9.60096   35.91972 1.000 35.23475 ? 48  ARG A CA  1 
ATOM   304  C C   . ARG A 1 54  ? -25.38002 9.06193   36.28211 1.000 32.53283 ? 48  ARG A C   1 
ATOM   305  O O   . ARG A 1 54  ? -25.24561 8.12400   37.08386 1.000 33.38230 ? 48  ARG A O   1 
ATOM   306  C CB  . ARG A 1 54  ? -27.15360 10.78165  36.81162 1.000 35.08780 ? 48  ARG A CB  1 
ATOM   307  C CG  . ARG A 1 54  ? -28.34510 11.57430  36.23042 1.000 37.02956 ? 48  ARG A CG  1 
ATOM   308  C CD  . ARG A 1 54  ? -28.56667 12.90661  36.94859 1.000 41.26219 ? 48  ARG A CD  1 
ATOM   309  N NE  . ARG A 1 54  ? -27.52984 13.90518  36.69285 1.000 43.22864 ? 48  ARG A NE  1 
ATOM   310  C CZ  . ARG A 1 54  ? -27.45833 14.66594  35.60571 1.000 44.21156 ? 48  ARG A CZ  1 
ATOM   311  N NH1 . ARG A 1 54  ? -28.33204 14.54859  34.61644 1.000 43.86197 ? 48  ARG A NH1 1 
ATOM   312  N NH2 . ARG A 1 54  ? -26.49081 15.57510  35.51140 1.000 45.24570 ? 48  ARG A NH2 1 
ATOM   313  N N   . VAL A 1 55  ? -24.35694 9.63805   35.63235 1.000 32.23515 ? 49  VAL A N   1 
ATOM   314  C CA  . VAL A 1 55  ? -22.96380 9.22023   35.75051 1.000 28.35808 ? 49  VAL A CA  1 
ATOM   315  C C   . VAL A 1 55  ? -22.10475 10.45035  36.02544 1.000 28.07393 ? 49  VAL A C   1 
ATOM   316  O O   . VAL A 1 55  ? -22.56104 11.58886  35.92446 1.000 28.91239 ? 49  VAL A O   1 
ATOM   317  C CB  . VAL A 1 55  ? -22.45429 8.50356   34.48257 1.000 27.99392 ? 49  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 55  ? -23.21444 7.21891   34.23113 1.000 29.83994 ? 49  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 55  ? -22.48989 9.42661   33.27586 1.000 27.33142 ? 49  VAL A CG2 1 
ATOM   320  N N   . ALA A 1 56  ? -20.85140 10.20434  36.40668 1.000 26.39367 ? 50  ALA A N   1 
ATOM   321  C CA  . ALA A 1 56  ? -19.83441 11.24457  36.49069 1.000 24.33497 ? 50  ALA A CA  1 
ATOM   322  C C   . ALA A 1 56  ? -18.91488 11.16918  35.27494 1.000 27.84625 ? 50  ALA A C   1 
ATOM   323  O O   . ALA A 1 56  ? -18.57844 10.07368  34.80856 1.000 30.40759 ? 50  ALA A O   1 
ATOM   324  C CB  . ALA A 1 56  ? -18.98817 11.08995  37.76235 1.000 25.78343 ? 50  ALA A CB  1 
ATOM   325  N N   . ILE A 1 57  ? -18.50303 12.33397  34.76572 1.000 26.60384 ? 51  ILE A N   1 
ATOM   326  C CA  . ILE A 1 57  ? -17.60317 12.41014  33.61646 1.000 26.69626 ? 51  ILE A CA  1 
ATOM   327  C C   . ILE A 1 57  ? -16.48718 13.39936  33.92218 1.000 28.40496 ? 51  ILE A C   1 
ATOM   328  O O   . ILE A 1 57  ? -16.75401 14.53345  34.34021 1.000 29.57904 ? 51  ILE A O   1 
ATOM   329  C CB  . ILE A 1 57  ? -18.32205 12.81982  32.31639 1.000 27.08087 ? 51  ILE A CB  1 
ATOM   330  C CG1 . ILE A 1 57  ? -19.54793 11.93158  32.07273 1.000 27.33117 ? 51  ILE A CG1 1 
ATOM   331  C CG2 . ILE A 1 57  ? -17.33423 12.77144  31.11178 1.000 26.96283 ? 51  ILE A CG2 1 
ATOM   332  C CD1 . ILE A 1 57  ? -20.31186 12.25829  30.76540 1.000 27.94711 ? 51  ILE A CD1 1 
ATOM   333  N N   . LYS A 1 58  ? -15.23910 12.96610  33.71362 1.000 27.83609 ? 52  LYS A N   1 
ATOM   334  C CA  . LYS A 1 58  ? -14.05279 13.77772  33.96893 1.000 28.09745 ? 52  LYS A CA  1 
ATOM   335  C C   . LYS A 1 58  ? -13.42505 14.12383  32.62001 1.000 29.11902 ? 52  LYS A C   1 
ATOM   336  O O   . LYS A 1 58  ? -13.09021 13.22092  31.84340 1.000 30.24089 ? 52  LYS A O   1 
ATOM   337  C CB  . LYS A 1 58  ? -13.05723 13.03116  34.86451 1.000 30.32137 ? 52  LYS A CB  1 
ATOM   338  C CG  . LYS A 1 58  ? -11.72744 13.76218  35.08780 1.000 33.92688 ? 52  LYS A CG  1 
ATOM   339  C CD  . LYS A 1 58  ? -10.82762 13.04751  36.11319 0.800 34.22498 ? 52  LYS A CD  1 
ATOM   340  C CE  . LYS A 1 58  ? -10.31845 11.69623  35.61640 0.700 34.31069 ? 52  LYS A CE  1 
ATOM   341  N NZ  . LYS A 1 58  ? -9.20898  11.21648  36.51110 0.600 36.35256 ? 52  LYS A NZ  1 
ATOM   342  N N   . LYS A 1 59  ? -13.27569 15.42142  32.34420 1.000 30.52221 ? 53  LYS A N   1 
ATOM   343  C CA  . LYS A 1 59  ? -12.61894 15.88414  31.12940 1.000 31.51126 ? 53  LYS A CA  1 
ATOM   344  C C   . LYS A 1 59  ? -11.12112 16.07841  31.38408 1.000 30.45383 ? 53  LYS A C   1 
ATOM   345  O O   . LYS A 1 59  ? -10.73170 16.69885  32.37895 1.000 32.95298 ? 53  LYS A O   1 
ATOM   346  C CB  . LYS A 1 59  ? -13.24769 17.19825  30.63627 1.000 34.15362 ? 53  LYS A CB  1 
ATOM   347  C CG  . LYS A 1 59  ? -12.57680 17.74433  29.37538 1.000 36.37327 ? 53  LYS A CG  1 
ATOM   348  C CD  . LYS A 1 59  ? -13.17997 19.06555  28.88668 1.000 38.76009 ? 53  LYS A CD  1 
ATOM   349  C CE  . LYS A 1 59  ? -12.65744 19.41262  27.49304 1.000 41.94547 ? 53  LYS A CE  1 
ATOM   350  N NZ  . LYS A 1 59  ? -13.15794 20.73649  27.01860 1.000 44.68433 ? 53  LYS A NZ  1 
ATOM   351  N N   . ILE A 1 60  ? -10.28864 15.55242  30.48576 1.000 29.55972 ? 54  ILE A N   1 
ATOM   352  C CA  . ILE A 1 60  ? -8.83165  15.62095  30.58427 1.000 30.12667 ? 54  ILE A CA  1 
ATOM   353  C C   . ILE A 1 60  ? -8.28821  16.19750  29.27401 1.000 31.58050 ? 54  ILE A C   1 
ATOM   354  O O   . ILE A 1 60  ? -8.66922  15.73993  28.18855 1.000 31.34715 ? 54  ILE A O   1 
ATOM   355  C CB  . ILE A 1 60  ? -8.22857  14.22647  30.82408 1.000 31.55644 ? 54  ILE A CB  1 
ATOM   356  C CG1 . ILE A 1 60  ? -8.94399  13.52957  31.96258 1.000 35.79097 ? 54  ILE A CG1 1 
ATOM   357  C CG2 . ILE A 1 60  ? -6.71303  14.30379  31.09718 1.000 33.21277 ? 54  ILE A CG2 1 
ATOM   358  C CD1 . ILE A 1 60  ? -8.42805  12.14841  32.16961 1.000 38.56713 ? 54  ILE A CD1 1 
ATOM   359  N N   . SER A 1 61  ? -7.35602  17.15232  29.37041 1.000 33.59857 ? 55  SER A N   1 
ATOM   360  C CA  . SER A 1 61  ? -6.70813  17.75005  28.19866 1.000 35.18143 ? 55  SER A CA  1 
ATOM   361  C C   . SER A 1 61  ? -5.19551  17.74633  28.38140 1.000 34.03135 ? 55  SER A C   1 
ATOM   362  O O   . SER A 1 61  ? -4.59411  18.79158  28.64586 1.000 37.21157 ? 55  SER A O   1 
ATOM   363  C CB  . SER A 1 61  ? -7.21201  19.17515  27.94596 1.000 38.12592 ? 55  SER A CB  1 
ATOM   364  O OG  . SER A 1 61  ? -8.63514  19.21782  27.88305 1.000 39.70282 ? 55  SER A OG  1 
ATOM   365  N N   . PRO A 1 62  ? -4.54371  16.59671  28.20877 1.000 33.73045 ? 56  PRO A N   1 
ATOM   366  C CA  . PRO A 1 62  ? -3.14171  16.43576  28.63579 1.000 34.79835 ? 56  PRO A CA  1 
ATOM   367  C C   . PRO A 1 62  ? -2.08551  16.53029  27.53889 1.000 34.48105 ? 56  PRO A C   1 
ATOM   368  O O   . PRO A 1 62  ? -0.88658  16.43671  27.85925 1.000 34.05127 ? 56  PRO A O   1 
ATOM   369  C CB  . PRO A 1 62  ? -3.16414  15.00987  29.19863 1.000 35.03675 ? 56  PRO A CB  1 
ATOM   370  C CG  . PRO A 1 62  ? -4.07642  14.29990  28.20343 1.000 36.06895 ? 56  PRO A CG  1 
ATOM   371  C CD  . PRO A 1 62  ? -5.13658  15.30950  27.80572 1.000 34.28495 ? 56  PRO A CD  1 
ATOM   372  N N   . PHE A 1 63  ? -2.47062  16.70712  26.27526 1.000 33.26893 ? 57  PHE A N   1 
ATOM   373  C CA  . PHE A 1 63  ? -1.56333  16.33231  25.19213 1.000 33.48652 ? 57  PHE A CA  1 
ATOM   374  C C   . PHE A 1 63  ? -0.47430  17.35216  24.91741 1.000 36.71306 ? 57  PHE A C   1 
ATOM   375  O O   . PHE A 1 63  ? 0.51141   17.00140  24.26014 1.000 39.20935 ? 57  PHE A O   1 
ATOM   376  C CB  . PHE A 1 63  ? -2.38057  16.01583  23.93467 1.000 32.59875 ? 57  PHE A CB  1 
ATOM   377  C CG  . PHE A 1 63  ? -3.32040  14.84964  24.14217 1.000 29.15513 ? 57  PHE A CG  1 
ATOM   378  C CD1 . PHE A 1 63  ? -2.80204  13.62286  24.53400 1.000 29.89740 ? 57  PHE A CD1 1 
ATOM   379  C CD2 . PHE A 1 63  ? -4.69570  14.96956  23.96499 1.000 29.71482 ? 57  PHE A CD2 1 
ATOM   380  C CE1 . PHE A 1 63  ? -3.61029  12.52821  24.73727 1.000 27.01705 ? 57  PHE A CE1 1 
ATOM   381  C CE2 . PHE A 1 63  ? -5.54164  13.86936  24.18154 1.000 28.47185 ? 57  PHE A CE2 1 
ATOM   382  C CZ  . PHE A 1 63  ? -4.99913  12.65140  24.58025 1.000 27.70544 ? 57  PHE A CZ  1 
ATOM   383  N N   . GLU A 1 64  ? -0.59263  18.56535  25.45437 1.000 37.48328 ? 58  GLU A N   1 
ATOM   384  C CA  . GLU A 1 64  ? 0.45844   19.56415  25.30544 1.000 40.84482 ? 58  GLU A CA  1 
ATOM   385  C C   . GLU A 1 64  ? 1.67609   19.27520  26.17916 1.000 41.61778 ? 58  GLU A C   1 
ATOM   386  O O   . GLU A 1 64  ? 2.75130   19.81074  25.90680 1.000 42.84408 ? 58  GLU A O   1 
ATOM   387  C CB  . GLU A 1 64  ? -0.09000  20.95925  25.62881 0.700 42.03912 ? 58  GLU A CB  1 
ATOM   388  C CG  . GLU A 1 64  ? -1.08636  21.46795  24.61018 0.600 44.73817 ? 58  GLU A CG  1 
ATOM   389  C CD  . GLU A 1 64  ? -0.55164  21.39750  23.19489 0.500 47.29064 ? 58  GLU A CD  1 
ATOM   390  O OE1 . GLU A 1 64  ? 0.46964   22.05898  22.88798 0.500 48.26937 ? 58  GLU A OE1 1 
ATOM   391  O OE2 . GLU A 1 64  ? -1.14512  20.65378  22.39000 0.500 49.66064 ? 58  GLU A OE2 1 
ATOM   392  N N   . HIS A 1 65  ? 1.54731   18.43161  27.20542 1.000 42.52401 ? 59  HIS A N   1 
ATOM   393  C CA  . HIS A 1 65  ? 2.59587   18.31168  28.20835 1.000 42.66486 ? 59  HIS A CA  1 
ATOM   394  C C   . HIS A 1 65  ? 2.88181   16.85662  28.53020 1.000 40.57041 ? 59  HIS A C   1 
ATOM   395  O O   . HIS A 1 65  ? 1.96502   16.07078  28.80954 1.000 39.98797 ? 59  HIS A O   1 
ATOM   396  C CB  . HIS A 1 65  ? 2.22839   19.07518  29.47740 0.900 43.79921 ? 59  HIS A CB  1 
ATOM   397  C CG  . HIS A 1 65  ? 2.10155   20.54574  29.25625 0.800 45.89733 ? 59  HIS A CG  1 
ATOM   398  N ND1 . HIS A 1 65  ? 3.19400   21.38766  29.21950 0.700 46.72671 ? 59  HIS A ND1 1 
ATOM   399  C CD2 . HIS A 1 65  ? 1.01600   21.32547  29.04574 0.700 46.93253 ? 59  HIS A CD2 1 
ATOM   400  C CE1 . HIS A 1 65  ? 2.78569   22.62402  29.00107 0.700 47.81787 ? 59  HIS A CE1 1 
ATOM   401  N NE2 . HIS A 1 65  ? 1.46863   22.61390  28.89284 0.700 47.67684 ? 59  HIS A NE2 1 
ATOM   402  N N   . GLN A 1 66  ? 4.17174   16.52446  28.52373 1.000 39.46499 ? 60  GLN A N   1 
ATOM   403  C CA  . GLN A 1 66  ? 4.59376   15.13937  28.67165 1.000 40.52341 ? 60  GLN A CA  1 
ATOM   404  C C   . GLN A 1 66  ? 4.19089   14.59001  30.04464 1.000 40.65965 ? 60  GLN A C   1 
ATOM   405  O O   . GLN A 1 66  ? 3.70376   13.45796  30.14220 1.000 39.89212 ? 60  GLN A O   1 
ATOM   406  C CB  . GLN A 1 66  ? 6.11072   15.07269  28.40992 1.000 43.22488 ? 60  GLN A CB  1 
ATOM   407  C CG  . GLN A 1 66  ? 6.75030   13.70005  28.27506 0.900 46.23460 ? 60  GLN A CG  1 
ATOM   408  C CD  . GLN A 1 66  ? 7.01967   12.98790  29.56438 0.800 49.97509 ? 60  GLN A CD  1 
ATOM   409  O OE1 . GLN A 1 66  ? 6.75227   13.49589  30.65481 0.700 51.41750 ? 60  GLN A OE1 1 
ATOM   410  N NE2 . GLN A 1 66  ? 7.55467   11.77686  29.44699 0.700 50.92369 ? 60  GLN A NE2 1 
ATOM   411  N N   . THR A 1 67  ? 4.32354   15.39776  31.11192 1.000 41.49500 ? 61  THR A N   1 
ATOM   412  C CA  . THR A 1 67  ? 3.96092   14.89802  32.44373 1.000 41.79650 ? 61  THR A CA  1 
ATOM   413  C C   . THR A 1 67  ? 2.45842   14.65064  32.54605 1.000 40.22604 ? 61  THR A C   1 
ATOM   414  O O   . THR A 1 67  ? 2.02267   13.69206  33.20153 1.000 40.48950 ? 61  THR A O   1 
ATOM   415  C CB  . THR A 1 67  ? 4.42129   15.86152  33.54975 0.600 41.35946 ? 61  THR A CB  1 
ATOM   416  O OG1 . THR A 1 67  ? 3.77886   17.13466  33.40990 0.600 42.28423 ? 61  THR A OG1 1 
ATOM   417  C CG2 . THR A 1 67  ? 5.91264   16.07880  33.45816 0.600 40.52157 ? 61  THR A CG2 1 
ATOM   418  N N   . TYR A 1 68  ? 1.65509   15.50988  31.91135 1.000 36.66066 ? 62  TYR A N   1 
ATOM   419  C CA  . TYR A 1 68  ? 0.20930   15.29680  31.88734 1.000 35.32049 ? 62  TYR A CA  1 
ATOM   420  C C   . TYR A 1 68  ? -0.12982  14.01015  31.16263 1.000 34.76177 ? 62  TYR A C   1 
ATOM   421  O O   . TYR A 1 68  ? -0.95594  13.22834  31.63738 1.000 34.79400 ? 62  TYR A O   1 
ATOM   422  C CB  . TYR A 1 68  ? -0.51500  16.46989  31.22425 0.900 36.87867 ? 62  TYR A CB  1 
ATOM   423  C CG  . TYR A 1 68  ? -0.32836  17.81657  31.89580 0.800 39.34972 ? 62  TYR A CG  1 
ATOM   424  C CD1 . TYR A 1 68  ? 0.42616   17.95222  33.05576 0.700 40.54475 ? 62  TYR A CD1 1 
ATOM   425  C CD2 . TYR A 1 68  ? -0.92168  18.95173  31.36850 0.700 40.54466 ? 62  TYR A CD2 1 
ATOM   426  C CE1 . TYR A 1 68  ? 0.58566   19.18619  33.66560 0.700 42.34632 ? 62  TYR A CE1 1 
ATOM   427  C CE2 . TYR A 1 68  ? -0.76853  20.18099  31.96389 0.700 42.76658 ? 62  TYR A CE2 1 
ATOM   428  C CZ  . TYR A 1 68  ? -0.01398  20.29711  33.10707 0.700 43.67453 ? 62  TYR A CZ  1 
ATOM   429  O OH  . TYR A 1 68  ? 0.13338   21.53517  33.68380 0.700 45.60512 ? 62  TYR A OH  1 
ATOM   430  N N   . CYS A 1 69  ? 0.49247   13.77801  30.00151 1.000 33.47520 ? 63  CYS A N   1 
ATOM   431  C CA  . CYS A 1 69  ? 0.28889   12.52056  29.28911 1.000 32.23130 ? 63  CYS A CA  1 
ATOM   432  C C   . CYS A 1 69  ? 0.66294   11.32799  30.14917 1.000 31.99935 ? 63  CYS A C   1 
ATOM   433  O O   . CYS A 1 69  ? -0.01587  10.29575  30.10836 1.000 30.71412 ? 63  CYS A O   1 
ATOM   434  C CB  . CYS A 1 69  ? 1.09891   12.50553  27.99537 1.000 31.35914 ? 63  CYS A CB  1 
ATOM   435  S SG  . CYS A 1 69  ? 0.49468   13.69246  26.79959 1.000 34.47343 ? 63  CYS A SG  1 
ATOM   436  N N   . GLN A 1 70  ? 1.74468   11.44836  30.92933 1.000 31.68392 ? 64  GLN A N   1 
ATOM   437  C CA  . GLN A 1 70  ? 2.13667   10.36433  31.81517 1.000 34.94271 ? 64  GLN A CA  1 
ATOM   438  C C   . GLN A 1 70  ? 1.05947   10.07237  32.84159 1.000 33.93645 ? 64  GLN A C   1 
ATOM   439  O O   . GLN A 1 70  ? 0.66902   8.92035   33.02603 1.000 33.87199 ? 64  GLN A O   1 
ATOM   440  C CB  . GLN A 1 70  ? 3.44245   10.68141  32.52826 0.800 36.91702 ? 64  GLN A CB  1 
ATOM   441  C CG  . GLN A 1 70  ? 4.58992   9.86045   32.02895 0.700 41.59216 ? 64  GLN A CG  1 
ATOM   442  C CD  . GLN A 1 70  ? 5.91511   10.45474  32.41079 0.600 44.15037 ? 64  GLN A CD  1 
ATOM   443  O OE1 . GLN A 1 70  ? 6.05826   10.97527  33.51692 0.600 45.96672 ? 64  GLN A OE1 1 
ATOM   444  N NE2 . GLN A 1 70  ? 6.92260   10.26567  31.56855 0.600 47.63344 ? 64  GLN A NE2 1 
ATOM   445  N N   . ARG A 1 71  ? 0.58688   11.10795  33.53482 1.000 32.53918 ? 65  ARG A N   1 
ATOM   446  C CA  . ARG A 1 71  ? -0.45063  10.92502  34.54895 1.000 30.91592 ? 65  ARG A CA  1 
ATOM   447  C C   . ARG A 1 71  ? -1.69847  10.28713  33.94277 1.000 29.00223 ? 65  ARG A C   1 
ATOM   448  O O   . ARG A 1 71  ? -2.29434  9.36504   34.52402 1.000 29.90445 ? 65  ARG A O   1 
ATOM   449  C CB  . ARG A 1 71  ? -0.76362  12.29007  35.16056 1.000 36.77568 ? 65  ARG A CB  1 
ATOM   450  C CG  . ARG A 1 71  ? -1.63027  12.26716  36.40140 1.000 40.63955 ? 65  ARG A CG  1 
ATOM   451  C CD  A ARG A 1 71  ? -1.32020  13.48807  37.26474 0.520 44.40733 ? 65  ARG A CD  1 
ATOM   452  C CD  B ARG A 1 71  ? -1.71925  13.60807  37.13827 0.480 40.27126 ? 65  ARG A CD  1 
ATOM   453  N NE  A ARG A 1 71  ? 0.11393   13.75543  37.31428 0.520 47.26781 ? 65  ARG A NE  1 
ATOM   454  N NE  B ARG A 1 71  ? -2.75940  13.56172  38.16201 0.480 38.03984 ? 65  ARG A NE  1 
ATOM   455  C CZ  A ARG A 1 71  ? 0.67773   14.68854  38.07184 0.520 48.38591 ? 65  ARG A CZ  1 
ATOM   456  C CZ  B ARG A 1 71  ? -2.89856  14.43276  39.15352 0.480 36.12051 ? 65  ARG A CZ  1 
ATOM   457  N NH1 A ARG A 1 71  ? -0.04119  15.43980  38.89158 0.520 49.15223 ? 65  ARG A NH1 1 
ATOM   458  N NH1 B ARG A 1 71  ? -2.06667  15.44934  39.30583 0.480 36.33947 ? 65  ARG A NH1 1 
ATOM   459  N NH2 A ARG A 1 71  ? 1.99700   14.86133  38.01690 0.520 47.70527 ? 65  ARG A NH2 1 
ATOM   460  N NH2 B ARG A 1 71  ? -3.90423  14.28063  40.01265 0.480 33.36014 ? 65  ARG A NH2 1 
ATOM   461  N N   . THR A 1 72  ? -2.08431  10.74531  32.74968 1.000 27.21659 ? 66  THR A N   1 
ATOM   462  C CA  . THR A 1 72  ? -3.28851  10.22031  32.10434 1.000 27.30646 ? 66  THR A CA  1 
ATOM   463  C C   . THR A 1 72  ? -3.11532  8.75429   31.70755 1.000 26.32556 ? 66  THR A C   1 
ATOM   464  O O   . THR A 1 72  ? -4.01539  7.92234   31.91507 1.000 25.38245 ? 66  THR A O   1 
ATOM   465  C CB  . THR A 1 72  ? -3.63132  11.07818  30.88077 1.000 28.89449 ? 66  THR A CB  1 
ATOM   466  O OG1 . THR A 1 72  ? -3.87085  12.42904  31.30088 1.000 30.56950 ? 66  THR A OG1 1 
ATOM   467  C CG2 . THR A 1 72  ? -4.87753  10.54578  30.11622 1.000 27.58029 ? 66  THR A CG2 1 
ATOM   468  N N   . LEU A 1 73  ? -1.97320  8.42185   31.10624 1.000 26.17779 ? 67  LEU A N   1 
ATOM   469  C CA  . LEU A 1 73  ? -1.74466  7.04443   30.70209 1.000 27.77853 ? 67  LEU A CA  1 
ATOM   470  C C   . LEU A 1 73  ? -1.68054  6.11591   31.91835 1.000 28.93216 ? 67  LEU A C   1 
ATOM   471  O O   . LEU A 1 73  ? -2.28679  5.03916   31.89621 1.000 28.37604 ? 67  LEU A O   1 
ATOM   472  C CB  . LEU A 1 73  ? -0.47772  6.94765   29.84015 1.000 28.24833 ? 67  LEU A CB  1 
ATOM   473  C CG  . LEU A 1 73  ? -0.11477  5.56598   29.31125 1.000 28.73543 ? 67  LEU A CG  1 
ATOM   474  C CD1 . LEU A 1 73  ? -1.24607  4.94686   28.49171 1.000 28.08320 ? 67  LEU A CD1 1 
ATOM   475  C CD2 . LEU A 1 73  ? 1.18082   5.64420   28.49635 1.000 31.24339 ? 67  LEU A CD2 1 
ATOM   476  N N   . ARG A 1 74  ? -0.98306  6.52578   32.99645 1.000 28.64843 ? 68  ARG A N   1 
ATOM   477  C CA  . ARG A 1 74  ? -0.89695  5.68295   34.19431 1.000 28.98070 ? 68  ARG A CA  1 
ATOM   478  C C   . ARG A 1 74  ? -2.28046  5.32185   34.69904 1.000 31.04503 ? 68  ARG A C   1 
ATOM   479  O O   . ARG A 1 74  ? -2.58530  4.14944   34.97636 1.000 31.12001 ? 68  ARG A O   1 
ATOM   480  C CB  . ARG A 1 74  ? -0.14665  6.39496   35.34115 0.900 31.20377 ? 68  ARG A CB  1 
ATOM   481  C CG  . ARG A 1 74  ? 1.27051   6.69534   35.10659 0.800 33.03691 ? 68  ARG A CG  1 
ATOM   482  C CD  . ARG A 1 74  ? 1.91746   7.32438   36.34153 0.700 33.11016 ? 68  ARG A CD  1 
ATOM   483  N NE  . ARG A 1 74  ? 3.29958   7.67160   36.04939 0.600 34.14451 ? 68  ARG A NE  1 
ATOM   484  C CZ  . ARG A 1 74  ? 4.31123   6.82151   36.09449 0.600 37.53431 ? 68  ARG A CZ  1 
ATOM   485  N NH1 . ARG A 1 74  ? 4.14680   5.57735   36.50751 0.600 39.68380 ? 68  ARG A NH1 1 
ATOM   486  N NH2 . ARG A 1 74  ? 5.51459   7.22482   35.69644 0.600 39.39921 ? 68  ARG A NH2 1 
ATOM   487  N N   . GLU A 1 75  ? -3.12355  6.33367   34.86844 1.000 29.42002 ? 69  GLU A N   1 
ATOM   488  C CA  . GLU A 1 75  ? -4.44332  6.09571   35.41868 1.000 29.47675 ? 69  GLU A CA  1 
ATOM   489  C C   . GLU A 1 75  ? -5.24522  5.15612   34.53647 1.000 28.29093 ? 69  GLU A C   1 
ATOM   490  O O   . GLU A 1 75  ? -5.85701  4.19569   35.02145 1.000 28.21988 ? 69  GLU A O   1 
ATOM   491  C CB  . GLU A 1 75  ? -5.16031  7.41300   35.58576 0.800 27.04409 ? 69  GLU A CB  1 
ATOM   492  C CG  . GLU A 1 75  ? -6.62936  7.21002   35.67753 0.700 29.57853 ? 69  GLU A CG  1 
ATOM   493  C CD  . GLU A 1 75  ? -7.26750  8.22285   36.52098 0.500 30.95390 ? 69  GLU A CD  1 
ATOM   494  O OE1 . GLU A 1 75  ? -7.71322  9.20744   35.89993 0.500 33.27461 ? 69  GLU A OE1 1 
ATOM   495  O OE2 . GLU A 1 75  ? -7.43973  7.99484   37.73903 0.500 30.49401 ? 69  GLU A OE2 1 
ATOM   496  N N   . ILE A 1 76  ? -5.27896  5.43195   33.22623 1.000 26.08836 ? 70  ILE A N   1 
ATOM   497  C CA  . ILE A 1 76  ? -6.09784  4.60340   32.34474 1.000 27.82373 ? 70  ILE A CA  1 
ATOM   498  C C   . ILE A 1 76  ? -5.60092  3.16427   32.34309 1.000 28.46822 ? 70  ILE A C   1 
ATOM   499  O O   . ILE A 1 76  ? -6.39438  2.22032   32.45417 1.000 28.59865 ? 70  ILE A O   1 
ATOM   500  C CB  . ILE A 1 76  ? -6.11518  5.20044   30.93119 1.000 25.69093 ? 70  ILE A CB  1 
ATOM   501  C CG1 . ILE A 1 76  ? -6.79816  6.57052   30.96595 1.000 26.59974 ? 70  ILE A CG1 1 
ATOM   502  C CG2 . ILE A 1 76  ? -6.86465  4.26753   29.99282 1.000 27.84859 ? 70  ILE A CG2 1 
ATOM   503  C CD1 . ILE A 1 76  ? -6.76030  7.32125   29.61850 1.000 29.04912 ? 70  ILE A CD1 1 
ATOM   504  N N   . LYS A 1 77  ? -4.28181  2.96890   32.24722 1.000 25.90265 ? 71  LYS A N   1 
ATOM   505  C CA  . LYS A 1 77  ? -3.74962  1.61258   32.19158 1.000 28.07981 ? 71  LYS A CA  1 
ATOM   506  C C   . LYS A 1 77  ? -4.10126  0.84756   33.45978 1.000 27.45893 ? 71  LYS A C   1 
ATOM   507  O O   . LYS A 1 77  ? -4.52020  -0.31201  33.40218 1.000 29.63393 ? 71  LYS A O   1 
ATOM   508  C CB  . LYS A 1 77  ? -2.23307  1.64347   32.00085 0.900 27.96065 ? 71  LYS A CB  1 
ATOM   509  C CG  . LYS A 1 77  ? -1.79826  1.75595   30.56095 0.800 31.47809 ? 71  LYS A CG  1 
ATOM   510  C CD  . LYS A 1 77  ? -0.29559  1.52629   30.42536 0.700 33.04753 ? 71  LYS A CD  1 
ATOM   511  C CE  . LYS A 1 77  ? 0.05763   0.08258   30.60401 0.600 34.71247 ? 71  LYS A CE  1 
ATOM   512  N NZ  . LYS A 1 77  ? -0.15674  -0.61201  29.29877 0.600 36.73555 ? 71  LYS A NZ  1 
ATOM   513  N N   . ILE A 1 78  ? -3.92161  1.47854   34.62071 1.000 25.13469 ? 72  ILE A N   1 
ATOM   514  C CA  . ILE A 1 78  ? -4.19958  0.80054   35.88010 1.000 25.03239 ? 72  ILE A CA  1 
ATOM   515  C C   . ILE A 1 78  ? -5.68547  0.49128   36.01548 1.000 26.99756 ? 72  ILE A C   1 
ATOM   516  O O   . ILE A 1 78  ? -6.07532  -0.64982  36.29502 1.000 28.51523 ? 72  ILE A O   1 
ATOM   517  C CB  . ILE A 1 78  ? -3.70384  1.65049   37.06091 1.000 25.07509 ? 72  ILE A CB  1 
ATOM   518  C CG1 . ILE A 1 78  ? -2.17639  1.69176   37.07493 1.000 25.93724 ? 72  ILE A CG1 1 
ATOM   519  C CG2 . ILE A 1 78  ? -4.30859  1.10606   38.35900 1.000 24.42351 ? 72  ILE A CG2 1 
ATOM   520  C CD1 . ILE A 1 78  ? -1.63183  2.82075   37.94866 1.000 26.97465 ? 72  ILE A CD1 1 
ATOM   521  N N   . LEU A 1 79  ? -6.53928  1.50717   35.83805 1.000 25.93042 ? 73  LEU A N   1 
ATOM   522  C CA  . LEU A 1 79  ? -7.95547  1.31838   36.13162 1.000 29.15410 ? 73  LEU A CA  1 
ATOM   523  C C   . LEU A 1 79  ? -8.61026  0.34232   35.17613 1.000 30.28554 ? 73  LEU A C   1 
ATOM   524  O O   . LEU A 1 79  ? -9.57635  -0.32487  35.54707 1.000 32.31637 ? 73  LEU A O   1 
ATOM   525  C CB  . LEU A 1 79  ? -8.68070  2.65070   36.10341 1.000 29.45565 ? 73  LEU A CB  1 
ATOM   526  C CG  . LEU A 1 79  ? -8.41717  3.46197   37.35155 1.000 30.59653 ? 73  LEU A CG  1 
ATOM   527  C CD1 . LEU A 1 79  ? -9.23213  4.72257   37.29001 1.000 32.57583 ? 73  LEU A CD1 1 
ATOM   528  C CD2 . LEU A 1 79  ? -8.74089  2.60687   38.61518 1.000 31.30991 ? 73  LEU A CD2 1 
ATOM   529  N N   . LEU A 1 80  ? -8.10874  0.23450   33.94731 1.000 29.77798 ? 74  LEU A N   1 
ATOM   530  C CA  . LEU A 1 80  ? -8.69464  -0.73849  33.04788 1.000 32.65994 ? 74  LEU A CA  1 
ATOM   531  C C   . LEU A 1 80  ? -8.31398  -2.16464  33.43835 1.000 30.96907 ? 74  LEU A C   1 
ATOM   532  O O   . LEU A 1 80  ? -8.99975  -3.11290  33.04373 1.000 35.01398 ? 74  LEU A O   1 
ATOM   533  C CB  . LEU A 1 80  ? -8.26425  -0.41214  31.62543 1.000 32.96908 ? 74  LEU A CB  1 
ATOM   534  C CG  . LEU A 1 80  ? -8.92906  0.84610   31.04002 1.000 32.89631 ? 74  LEU A CG  1 
ATOM   535  C CD1 . LEU A 1 80  ? -8.47709  0.97052   29.59946 1.000 33.68714 ? 74  LEU A CD1 1 
ATOM   536  C CD2 . LEU A 1 80  ? -10.47427 0.90013   31.12394 1.000 32.95635 ? 74  LEU A CD2 1 
ATOM   537  N N   . ARG A 1 81  ? -7.24396  -2.34603  34.20538 1.000 27.15635 ? 75  ARG A N   1 
ATOM   538  C CA  . ARG A 1 81  ? -6.92319  -3.67605  34.71645 1.000 26.46088 ? 75  ARG A CA  1 
ATOM   539  C C   . ARG A 1 81  ? -7.61983  -3.97898  36.03284 1.000 27.33233 ? 75  ARG A C   1 
ATOM   540  O O   . ARG A 1 81  ? -7.90970  -5.14275  36.31559 1.000 33.23352 ? 75  ARG A O   1 
ATOM   541  C CB  . ARG A 1 81  ? -5.41015  -3.83790  34.90235 0.900 28.69761 ? 75  ARG A CB  1 
ATOM   542  C CG  . ARG A 1 81  ? -4.60796  -3.71452  33.60877 0.700 33.05605 ? 75  ARG A CG  1 
ATOM   543  C CD  . ARG A 1 81  ? -3.97947  -5.04400  33.16610 0.600 34.97751 ? 75  ARG A CD  1 
ATOM   544  N NE  . ARG A 1 81  ? -3.02483  -5.58978  34.13227 0.500 34.17994 ? 75  ARG A NE  1 
ATOM   545  C CZ  . ARG A 1 81  ? -1.71026  -5.63913  33.94955 0.500 32.41294 ? 75  ARG A CZ  1 
ATOM   546  N NH1 . ARG A 1 81  ? -1.14231  -5.15721  32.85531 0.500 30.41477 ? 75  ARG A NH1 1 
ATOM   547  N NH2 . ARG A 1 81  ? -0.94445  -6.18536  34.88877 0.500 31.71412 ? 75  ARG A NH2 1 
ATOM   548  N N   . PHE A 1 82  ? -7.89890  -2.96897  36.83904 1.000 21.88558 ? 76  PHE A N   1 
ATOM   549  C CA  . PHE A 1 82  ? -8.46156  -3.22213  38.15821 1.000 21.18017 ? 76  PHE A CA  1 
ATOM   550  C C   . PHE A 1 82  ? -9.97013  -3.43395  38.09557 1.000 21.20743 ? 76  PHE A C   1 
ATOM   551  O O   . PHE A 1 82  ? -10.69051 -2.78752  37.31363 1.000 22.90742 ? 76  PHE A O   1 
ATOM   552  C CB  . PHE A 1 82  ? -8.19026  -2.04491  39.08559 1.000 19.93320 ? 76  PHE A CB  1 
ATOM   553  C CG  . PHE A 1 82  ? -6.77592  -1.96566  39.61336 1.000 20.96659 ? 76  PHE A CG  1 
ATOM   554  C CD1 . PHE A 1 82  ? -5.78958  -2.86497  39.22342 1.000 20.96586 ? 76  PHE A CD1 1 
ATOM   555  C CD2 . PHE A 1 82  ? -6.44226  -0.96089  40.50429 1.000 20.82095 ? 76  PHE A CD2 1 
ATOM   556  C CE1 . PHE A 1 82  ? -4.47489  -2.75032  39.73243 1.000 21.92841 ? 76  PHE A CE1 1 
ATOM   557  C CE2 . PHE A 1 82  ? -5.15237  -0.85573  41.00695 1.000 21.07250 ? 76  PHE A CE2 1 
ATOM   558  C CZ  . PHE A 1 82  ? -4.18309  -1.74890  40.63274 1.000 22.68707 ? 76  PHE A CZ  1 
ATOM   559  N N   . ARG A 1 83  ? -10.46033 -4.28743  38.99625 1.000 22.14193 ? 77  ARG A N   1 
ATOM   560  C CA  . ARG A 1 83  ? -11.89942 -4.45968  39.19277 1.000 22.30934 ? 77  ARG A CA  1 
ATOM   561  C C   . ARG A 1 83  ? -12.12042 -4.74504  40.67057 1.000 21.80366 ? 77  ARG A C   1 
ATOM   562  O O   . ARG A 1 83  ? -11.80502 -5.84469  41.12240 1.000 23.58911 ? 77  ARG A O   1 
ATOM   563  C CB  A ARG A 1 83  ? -12.46130 -5.58698  38.32457 0.500 22.49980 ? 77  ARG A CB  1 
ATOM   564  C CB  B ARG A 1 83  ? -12.43169 -5.59149  38.32100 0.500 28.25984 ? 77  ARG A CB  1 
ATOM   565  C CG  A ARG A 1 83  ? -13.98781 -5.70206  38.41014 0.500 23.83022 ? 77  ARG A CG  1 
ATOM   566  C CG  B ARG A 1 83  ? -13.86838 -5.41233  37.88417 0.500 34.91377 ? 77  ARG A CG  1 
ATOM   567  C CD  A ARG A 1 83  ? -14.55602 -6.85315  37.54342 0.500 27.62794 ? 77  ARG A CD  1 
ATOM   568  C CD  B ARG A 1 83  ? -13.96336 -5.43541  36.35925 0.500 40.13266 ? 77  ARG A CD  1 
ATOM   569  N NE  A ARG A 1 83  ? -14.69938 -8.09811  38.28821 0.500 34.17639 ? 77  ARG A NE  1 
ATOM   570  N NE  B ARG A 1 83  ? -13.06730 -4.46101  35.74745 0.500 42.21663 ? 77  ARG A NE  1 
ATOM   571  C CZ  A ARG A 1 83  ? -13.87212 -9.13084  38.20171 0.500 40.28621 ? 77  ARG A CZ  1 
ATOM   572  C CZ  B ARG A 1 83  ? -12.22437 -4.71721  34.75408 0.500 41.91776 ? 77  ARG A CZ  1 
ATOM   573  N NH1 A ARG A 1 83  ? -12.83566 -9.11831  37.38102 0.500 42.79576 ? 77  ARG A NH1 1 
ATOM   574  N NH1 B ARG A 1 83  ? -12.13915 -5.92017  34.20943 0.500 42.66328 ? 77  ARG A NH1 1 
ATOM   575  N NH2 A ARG A 1 83  ? -14.09376 -10.20501 38.95583 0.500 43.13978 ? 77  ARG A NH2 1 
ATOM   576  N NH2 B ARG A 1 83  ? -11.43859 -3.74267  34.30373 0.500 39.62791 ? 77  ARG A NH2 1 
ATOM   577  N N   . HIS A 1 84  ? -12.64729 -3.76831  41.40678 1.000 19.19906 ? 78  HIS A N   1 
ATOM   578  C CA  . HIS A 1 84  ? -12.83475 -3.93810  42.84066 1.000 17.60500 ? 78  HIS A CA  1 
ATOM   579  C C   . HIS A 1 84  ? -13.93453 -2.98618  43.31824 1.000 18.29801 ? 78  HIS A C   1 
ATOM   580  O O   . HIS A 1 84  ? -14.02102 -1.85357  42.84351 1.000 18.92389 ? 78  HIS A O   1 
ATOM   581  C CB  . HIS A 1 84  ? -11.50571 -3.67614  43.58317 1.000 17.66618 ? 78  HIS A CB  1 
ATOM   582  C CG  . HIS A 1 84  ? -11.55158 -4.02566  45.03571 1.000 16.93022 ? 78  HIS A CG  1 
ATOM   583  N ND1 . HIS A 1 84  ? -12.06097 -3.16905  45.99306 1.000 17.43778 ? 78  HIS A ND1 1 
ATOM   584  C CD2 . HIS A 1 84  ? -11.13634 -5.13661  45.69920 1.000 17.33930 ? 78  HIS A CD2 1 
ATOM   585  C CE1 . HIS A 1 84  ? -11.97167 -3.74945  47.18451 1.000 17.51294 ? 78  HIS A CE1 1 
ATOM   586  N NE2 . HIS A 1 84  ? -11.38143 -4.93023  47.03435 1.000 16.25597 ? 78  HIS A NE2 1 
ATOM   587  N N   . GLU A 1 85  ? -14.72977 -3.44159  44.29695 1.000 19.73311 ? 79  GLU A N   1 
ATOM   588  C CA  . GLU A 1 85  ? -15.86717 -2.65906  44.80081 1.000 19.62070 ? 79  GLU A CA  1 
ATOM   589  C C   . GLU A 1 85  ? -15.45116 -1.32445  45.39892 1.000 18.32081 ? 79  GLU A C   1 
ATOM   590  O O   . GLU A 1 85  ? -16.25740 -0.38670  45.42173 1.000 20.22041 ? 79  GLU A O   1 
ATOM   591  C CB  . GLU A 1 85  ? -16.64696 -3.44797  45.86372 0.900 21.82498 ? 79  GLU A CB  1 
ATOM   592  C CG  . GLU A 1 85  ? -17.45670 -4.58991  45.28459 0.800 26.52048 ? 79  GLU A CG  1 
ATOM   593  C CD  . GLU A 1 85  ? -18.20233 -5.37759  46.34261 0.700 31.17934 ? 79  GLU A CD  1 
ATOM   594  O OE1 . GLU A 1 85  ? -17.91338 -5.17482  47.54674 0.700 29.99264 ? 79  GLU A OE1 1 
ATOM   595  O OE2 . GLU A 1 85  ? -19.09578 -6.18178  45.96749 0.700 33.23711 ? 79  GLU A OE2 1 
ATOM   596  N N   . ASN A 1 86  ? -14.22039 -1.22135  45.94174 1.000 16.70217 ? 80  ASN A N   1 
ATOM   597  C CA  . ASN A 1 86  ? -13.79257 -0.00442  46.61829 1.000 17.13603 ? 80  ASN A CA  1 
ATOM   598  C C   . ASN A 1 86  ? -12.81696 0.81185   45.77660 1.000 16.07984 ? 80  ASN A C   1 
ATOM   599  O O   . ASN A 1 86  ? -12.06929 1.64399   46.31425 1.000 16.40831 ? 80  ASN A O   1 
ATOM   600  C CB  . ASN A 1 86  ? -13.17583 -0.34074  47.98799 1.000 15.89989 ? 80  ASN A CB  1 
ATOM   601  C CG  . ASN A 1 86  ? -14.15163 -1.05547  48.89562 1.000 17.08368 ? 80  ASN A CG  1 
ATOM   602  O OD1 . ASN A 1 86  ? -13.93547 -2.19872  49.25508 1.000 18.92518 ? 80  ASN A OD1 1 
ATOM   603  N ND2 . ASN A 1 86  ? -15.24209 -0.39301  49.24080 1.000 17.72623 ? 80  ASN A ND2 1 
ATOM   604  N N   . ILE A 1 87  ? -12.81799 0.59159   44.45883 1.000 16.91731 ? 81  ILE A N   1 
ATOM   605  C CA  . ILE A 1 87  ? -12.01425 1.35262   43.51596 1.000 17.07704 ? 81  ILE A CA  1 
ATOM   606  C C   . ILE A 1 87  ? -12.94323 1.80798   42.39898 1.000 17.26791 ? 81  ILE A C   1 
ATOM   607  O O   . ILE A 1 87  ? -13.62036 0.97868   41.78041 1.000 19.17618 ? 81  ILE A O   1 
ATOM   608  C CB  . ILE A 1 87  ? -10.85775 0.50938   42.93209 1.000 16.55207 ? 81  ILE A CB  1 
ATOM   609  C CG1 . ILE A 1 87  ? -9.94263  0.00869   44.06006 1.000 17.39527 ? 81  ILE A CG1 1 
ATOM   610  C CG2 . ILE A 1 87  ? -10.07159 1.33088   41.87131 1.000 19.40702 ? 81  ILE A CG2 1 
ATOM   611  C CD1 . ILE A 1 87  ? -8.84206  -0.94188  43.57087 1.000 19.05426 ? 81  ILE A CD1 1 
ATOM   612  N N   . ILE A 1 88  ? -12.96594 3.09834   42.10845 1.000 19.15485 ? 82  ILE A N   1 
ATOM   613  C CA  . ILE A 1 88  ? -13.94624 3.51816   41.12108 1.000 22.04041 ? 82  ILE A CA  1 
ATOM   614  C C   . ILE A 1 88  ? -13.43510 3.14165   39.72785 1.000 23.43933 ? 82  ILE A C   1 
ATOM   615  O O   . ILE A 1 88  ? -12.27350 3.37018   39.37726 1.000 28.04124 ? 82  ILE A O   1 
ATOM   616  C CB  . ILE A 1 88  ? -14.31133 5.00382   41.28483 1.000 26.07035 ? 82  ILE A CB  1 
ATOM   617  C CG1 . ILE A 1 88  ? -15.48036 5.34171   40.32182 1.000 28.82536 ? 82  ILE A CG1 1 
ATOM   618  C CG2 . ILE A 1 88  ? -13.11600 5.88545   41.15946 1.000 28.79817 ? 82  ILE A CG2 1 
ATOM   619  C CD1 . ILE A 1 88  ? -16.28621 6.58976   40.68765 1.000 32.75096 ? 82  ILE A CD1 1 
ATOM   620  N N   . GLY A 1 89  ? -14.27095 2.46560   38.96217 1.000 22.20611 ? 83  GLY A N   1 
ATOM   621  C CA  . GLY A 1 89  ? -13.84295 1.93342   37.68376 1.000 23.87817 ? 83  GLY A CA  1 
ATOM   622  C C   . GLY A 1 89  ? -14.15123 2.87936   36.54170 1.000 26.28399 ? 83  GLY A C   1 
ATOM   623  O O   . GLY A 1 89  ? -14.84109 3.87815   36.70751 1.000 31.85112 ? 83  GLY A O   1 
ATOM   624  N N   . ILE A 1 90  ? -13.64079 2.53721   35.36711 1.000 24.26200 ? 84  ILE A N   1 
ATOM   625  C CA  . ILE A 1 90  ? -13.89745 3.29395   34.14834 1.000 25.92776 ? 84  ILE A CA  1 
ATOM   626  C C   . ILE A 1 90  ? -15.00826 2.58391   33.38917 1.000 28.42863 ? 84  ILE A C   1 
ATOM   627  O O   . ILE A 1 90  ? -14.84128 1.43234   32.97888 1.000 30.58637 ? 84  ILE A O   1 
ATOM   628  C CB  . ILE A 1 90  ? -12.63846 3.41353   33.27153 1.000 25.97987 ? 84  ILE A CB  1 
ATOM   629  C CG1 . ILE A 1 90  ? -11.55974 4.28511   33.94661 1.000 25.87708 ? 84  ILE A CG1 1 
ATOM   630  C CG2 . ILE A 1 90  ? -13.02085 4.01677   31.90262 1.000 27.12281 ? 84  ILE A CG2 1 
ATOM   631  C CD1 . ILE A 1 90  ? -10.22590 4.40357   33.12654 1.000 28.00847 ? 84  ILE A CD1 1 
ATOM   632  N N   . ASN A 1 91  ? -16.14101 3.25772   33.20465 1.000 28.06896 ? 85  ASN A N   1 
ATOM   633  C CA  . ASN A 1 91  ? -17.26237 2.65172   32.49772 1.000 29.09721 ? 85  ASN A CA  1 
ATOM   634  C C   . ASN A 1 91  ? -17.21394 2.91832   31.00509 1.000 26.61552 ? 85  ASN A C   1 
ATOM   635  O O   . ASN A 1 91  ? -17.76371 2.13670   30.21268 1.000 29.49219 ? 85  ASN A O   1 
ATOM   636  C CB  . ASN A 1 91  ? -18.59753 3.18564   33.03013 0.800 30.22586 ? 85  ASN A CB  1 
ATOM   637  C CG  . ASN A 1 91  ? -18.79939 2.92743   34.49992 0.700 36.04549 ? 85  ASN A CG  1 
ATOM   638  O OD1 . ASN A 1 91  ? -18.17118 2.04908   35.09345 0.600 39.28078 ? 85  ASN A OD1 1 
ATOM   639  N ND2 . ASN A 1 91  ? -19.69212 3.69690   35.09791 0.600 35.23694 ? 85  ASN A ND2 1 
ATOM   640  N N   . ASP A 1 92  ? -16.58264 4.01325   30.60881 1.000 26.23493 ? 86  ASP A N   1 
ATOM   641  C CA  . ASP A 1 92  ? -16.58023 4.43498   29.21805 1.000 25.57024 ? 86  ASP A CA  1 
ATOM   642  C C   . ASP A 1 92  ? -15.46512 5.46464   29.09615 1.000 24.07436 ? 86  ASP A C   1 
ATOM   643  O O   . ASP A 1 92  ? -15.13849 6.14460   30.07295 1.000 24.81523 ? 86  ASP A O   1 
ATOM   644  C CB  . ASP A 1 92  ? -17.93254 5.04173   28.82108 1.000 27.50136 ? 86  ASP A CB  1 
ATOM   645  C CG  . ASP A 1 92  ? -18.13527 5.13103   27.30793 1.000 32.25341 ? 86  ASP A CG  1 
ATOM   646  O OD1 . ASP A 1 92  ? -17.27678 4.66658   26.52521 1.000 33.26627 ? 86  ASP A OD1 1 
ATOM   647  O OD2 . ASP A 1 92  ? -19.18370 5.69100   26.90269 1.000 34.37777 ? 86  ASP A OD2 1 
ATOM   648  N N   . ILE A 1 93  ? -14.87850 5.56433   27.90717 1.000 24.60182 ? 87  ILE A N   1 
ATOM   649  C CA  . ILE A 1 93  ? -13.94676 6.63450   27.60616 1.000 24.28150 ? 87  ILE A CA  1 
ATOM   650  C C   . ILE A 1 93  ? -14.36926 7.23437   26.27788 1.000 24.79375 ? 87  ILE A C   1 
ATOM   651  O O   . ILE A 1 93  ? -14.48019 6.51252   25.28011 1.000 27.24225 ? 87  ILE A O   1 
ATOM   652  C CB  . ILE A 1 93  ? -12.49022 6.15074   27.54230 1.000 24.61216 ? 87  ILE A CB  1 
ATOM   653  C CG1 . ILE A 1 93  ? -12.06824 5.56128   28.89365 1.000 24.70907 ? 87  ILE A CG1 1 
ATOM   654  C CG2 . ILE A 1 93  ? -11.57324 7.31419   27.17672 1.000 25.02450 ? 87  ILE A CG2 1 
ATOM   655  C CD1 . ILE A 1 93  ? -10.62545 5.11576   28.93743 1.000 25.29521 ? 87  ILE A CD1 1 
ATOM   656  N N   . ILE A 1 94  ? -14.57491 8.54870   26.26382 1.000 23.47266 ? 88  ILE A N   1 
ATOM   657  C CA  . ILE A 1 94  ? -14.97247 9.28435   25.06364 1.000 24.91107 ? 88  ILE A CA  1 
ATOM   658  C C   . ILE A 1 94  ? -13.77300 10.04260  24.51176 1.000 24.67061 ? 88  ILE A C   1 
ATOM   659  O O   . ILE A 1 94  ? -13.09928 10.78625  25.24448 1.000 26.84304 ? 88  ILE A O   1 
ATOM   660  C CB  . ILE A 1 94  ? -16.11874 10.26064  25.36482 1.000 31.31450 ? 88  ILE A CB  1 
ATOM   661  C CG1 . ILE A 1 94  ? -17.29406 9.50800   25.98685 1.000 32.80411 ? 88  ILE A CG1 1 
ATOM   662  C CG2 . ILE A 1 94  ? -16.47412 11.07917  24.11281 1.000 33.61153 ? 88  ILE A CG2 1 
ATOM   663  C CD1 . ILE A 1 94  ? -18.20186 10.39276  26.80933 1.000 34.63623 ? 88  ILE A CD1 1 
ATOM   664  N N   . ARG A 1 95  ? -13.52880 9.89145   23.21213 1.000 23.55070 ? 89  ARG A N   1 
ATOM   665  C CA  . ARG A 1 95  ? -12.51985 10.69017  22.52155 1.000 22.13471 ? 89  ARG A CA  1 
ATOM   666  C C   . ARG A 1 95  ? -12.75920 10.60109  21.01992 1.000 22.81268 ? 89  ARG A C   1 
ATOM   667  O O   . ARG A 1 95  ? -13.53665 9.76975   20.53855 1.000 24.26558 ? 89  ARG A O   1 
ATOM   668  C CB  . ARG A 1 95  ? -11.09184 10.24981  22.87108 1.000 23.71031 ? 89  ARG A CB  1 
ATOM   669  C CG  . ARG A 1 95  ? -10.83140 8.75746   22.79399 1.000 26.74350 ? 89  ARG A CG  1 
ATOM   670  C CD  . ARG A 1 95  ? -10.12933 8.42795   21.53954 1.000 25.57677 ? 89  ARG A CD  1 
ATOM   671  N NE  . ARG A 1 95  ? -9.58455  7.07463   21.49637 1.000 23.02614 ? 89  ARG A NE  1 
ATOM   672  C CZ  . ARG A 1 95  ? -9.68284  6.27472   20.44391 1.000 23.88522 ? 89  ARG A CZ  1 
ATOM   673  N NH1 . ARG A 1 95  ? -10.38676 6.63216   19.36134 1.000 23.53421 ? 89  ARG A NH1 1 
ATOM   674  N NH2 . ARG A 1 95  ? -9.06111  5.09427   20.47093 1.000 24.22166 ? 89  ARG A NH2 1 
ATOM   675  N N   . ALA A 1 96  ? -12.10161 11.49693  20.29271 1.000 22.86575 ? 90  ALA A N   1 
ATOM   676  C CA  . ALA A 1 96  ? -12.22651 11.55079  18.84507 1.000 23.56080 ? 90  ALA A CA  1 
ATOM   677  C C   . ALA A 1 96  ? -11.76833 10.23013  18.20415 1.000 23.84636 ? 90  ALA A C   1 
ATOM   678  O O   . ALA A 1 96  ? -11.01623 9.46049   18.80493 1.000 24.48596 ? 90  ALA A O   1 
ATOM   679  C CB  . ALA A 1 96  ? -11.41938 12.74158  18.31643 1.000 21.49224 ? 90  ALA A CB  1 
ATOM   680  N N   . PRO A 1 97  ? -12.21137 9.93639   16.97290 1.000 23.79523 ? 91  PRO A N   1 
ATOM   681  C CA  . PRO A 1 97  ? -11.89149 8.63073   16.36555 1.000 24.69078 ? 91  PRO A CA  1 
ATOM   682  C C   . PRO A 1 97  ? -10.47533 8.49330   15.86104 1.000 23.42102 ? 91  PRO A C   1 
ATOM   683  O O   . PRO A 1 97  ? -10.05549 7.36906   15.56302 1.000 24.50284 ? 91  PRO A O   1 
ATOM   684  C CB  . PRO A 1 97  ? -12.85856 8.53862   15.17571 1.000 24.62866 ? 91  PRO A CB  1 
ATOM   685  C CG  . PRO A 1 97  ? -13.20575 9.97157   14.84659 1.000 25.95358 ? 91  PRO A CG  1 
ATOM   686  C CD  . PRO A 1 97  ? -13.22291 10.68072  16.20268 1.000 23.96143 ? 91  PRO A CD  1 
ATOM   687  N N   . THR A 1 98  ? -9.74674  9.59056   15.71629 1.000 24.05262 ? 92  THR A N   1 
ATOM   688  C CA  . THR A 1 98  ? -8.38955  9.55321   15.19679 1.000 22.74056 ? 92  THR A CA  1 
ATOM   689  C C   . THR A 1 98  ? -7.46902  10.33200  16.11406 1.000 23.79957 ? 92  THR A C   1 
ATOM   690  O O   . THR A 1 98  ? -7.89941  11.23963  16.83767 1.000 24.60768 ? 92  THR A O   1 
ATOM   691  C CB  . THR A 1 98  ? -8.30446  10.15055  13.79531 1.000 25.77373 ? 92  THR A CB  1 
ATOM   692  O OG1 . THR A 1 98  ? -8.54541  11.57793  13.84901 1.000 26.65134 ? 92  THR A OG1 1 
ATOM   693  C CG2 . THR A 1 98  ? -9.33517  9.49522   12.91473 1.000 26.90385 ? 92  THR A CG2 1 
ATOM   694  N N   . ILE A 1 99  ? -6.17724  9.99544   16.04238 1.000 25.93741 ? 93  ILE A N   1 
ATOM   695  C CA  . ILE A 1 99  ? -5.19717  10.67295  16.88785 1.000 29.38352 ? 93  ILE A CA  1 
ATOM   696  C C   . ILE A 1 99  ? -5.12204  12.14472  16.52287 1.000 30.67045 ? 93  ILE A C   1 
ATOM   697  O O   . ILE A 1 99  ? -5.01870  13.01463  17.40426 1.000 31.57546 ? 93  ILE A O   1 
ATOM   698  C CB  A ILE A 1 99  ? -3.82908  9.96159   16.82041 0.350 30.22583 ? 93  ILE A CB  1 
ATOM   699  C CB  B ILE A 1 99  ? -3.80702  10.01043  16.76642 0.650 28.98064 ? 93  ILE A CB  1 
ATOM   700  C CG1 A ILE A 1 99  ? -2.95841  10.39277  18.00000 0.350 31.47591 ? 93  ILE A CG1 1 
ATOM   701  C CG1 B ILE A 1 99  ? -3.81289  8.58401   17.33249 0.650 29.14575 ? 93  ILE A CG1 1 
ATOM   702  C CG2 A ILE A 1 99  ? -3.11512  10.17655  15.47550 0.350 30.09895 ? 93  ILE A CG2 1 
ATOM   703  C CG2 B ILE A 1 99  ? -2.72616  10.89839  17.41094 0.650 28.63384 ? 93  ILE A CG2 1 
ATOM   704  C CD1 A ILE A 1 99  ? -1.79435  9.48013   18.23745 0.350 32.38680 ? 93  ILE A CD1 1 
ATOM   705  C CD1 B ILE A 1 99  ? -2.42819  7.91050   17.39952 0.650 33.58742 ? 93  ILE A CD1 1 
ATOM   706  N N   . GLU A 1 100 ? -5.20701  12.44209  15.21421 1.000 29.78550 ? 94  GLU A N   1 
ATOM   707  C CA  . GLU A 1 100 ? -5.15155  13.80885  14.71135 1.000 29.40581 ? 94  GLU A CA  1 
ATOM   708  C C   . GLU A 1 100 ? -6.22442  14.67725  15.33319 1.000 28.70833 ? 94  GLU A C   1 
ATOM   709  O O   . GLU A 1 100 ? -5.97874  15.85023  15.64184 1.000 32.35722 ? 94  GLU A O   1 
ATOM   710  C CB  . GLU A 1 100 ? -5.31045  13.80079  13.18442 0.800 28.64611 ? 94  GLU A CB  1 
ATOM   711  C CG  . GLU A 1 100 ? -4.06830  13.35277  12.46668 0.700 32.65338 ? 94  GLU A CG  1 
ATOM   712  C CD  . GLU A 1 100 ? -4.04129  11.86823  12.12917 0.700 34.46391 ? 94  GLU A CD  1 
ATOM   713  O OE1 . GLU A 1 100 ? -4.70201  11.04603  12.81587 0.700 34.71123 ? 94  GLU A OE1 1 
ATOM   714  O OE2 . GLU A 1 100 ? -3.33820  11.53031  11.15777 0.700 36.78384 ? 94  GLU A OE2 1 
ATOM   715  N N   . GLN A 1 101 ? -7.43694  14.12710  15.48884 1.000 25.36146 ? 95  GLN A N   1 
ATOM   716  C CA  . GLN A 1 101 ? -8.57411  14.88186  15.96770 1.000 23.80755 ? 95  GLN A CA  1 
ATOM   717  C C   . GLN A 1 101 ? -8.73059  14.83067  17.47165 1.000 23.27699 ? 95  GLN A C   1 
ATOM   718  O O   . GLN A 1 101 ? -9.58226  15.55377  17.99904 1.000 25.55254 ? 95  GLN A O   1 
ATOM   719  C CB  . GLN A 1 101 ? -9.85208  14.34309  15.34445 1.000 23.10077 ? 95  GLN A CB  1 
ATOM   720  C CG  . GLN A 1 101 ? -9.89985  14.53487  13.82767 1.000 24.10604 ? 95  GLN A CG  1 
ATOM   721  C CD  . GLN A 1 101 ? -11.02400 13.73857  13.22895 1.000 25.42778 ? 95  GLN A CD  1 
ATOM   722  O OE1 . GLN A 1 101 ? -10.97966 12.49255  13.19517 1.000 26.04469 ? 95  GLN A OE1 1 
ATOM   723  N NE2 . GLN A 1 101 ? -12.06293 14.43447  12.78070 1.000 26.17253 ? 95  GLN A NE2 1 
ATOM   724  N N   . MET A 1 102 ? -7.98492  13.95187  18.15309 1.000 24.84476 ? 96  MET A N   1 
ATOM   725  C CA  . MET A 1 102 ? -8.04100  13.80142  19.61464 1.000 24.72705 ? 96  MET A CA  1 
ATOM   726  C C   . MET A 1 102 ? -7.36889  14.97306  20.31265 1.000 26.70243 ? 96  MET A C   1 
ATOM   727  O O   . MET A 1 102 ? -6.13515  15.11950  20.27754 1.000 28.89441 ? 96  MET A O   1 
ATOM   728  C CB  . MET A 1 102 ? -7.36426  12.51561  20.06804 1.000 24.25748 ? 96  MET A CB  1 
ATOM   729  C CG  . MET A 1 102 ? -7.59738  12.25082  21.54781 1.000 23.74534 ? 96  MET A CG  1 
ATOM   730  S SD  . MET A 1 102 ? -7.16092  10.58673  22.09119 1.000 26.45420 ? 96  MET A SD  1 
ATOM   731  C CE  . MET A 1 102 ? -5.40375  10.57211  21.84699 1.000 25.40238 ? 96  MET A CE  1 
ATOM   732  N N   . LYS A 1 103 ? -8.16283  15.77767  21.00109 1.000 26.87526 ? 97  LYS A N   1 
ATOM   733  C CA  . LYS A 1 103 ? -7.62821  16.85717  21.80935 1.000 29.18372 ? 97  LYS A CA  1 
ATOM   734  C C   . LYS A 1 103 ? -7.91659  16.65874  23.28448 1.000 30.66007 ? 97  LYS A C   1 
ATOM   735  O O   . LYS A 1 103 ? -7.10338  17.05285  24.12023 1.000 34.76967 ? 97  LYS A O   1 
ATOM   736  C CB  . LYS A 1 103 ? -8.21493  18.21773  21.36429 0.800 31.12497 ? 97  LYS A CB  1 
ATOM   737  C CG  . LYS A 1 103 ? -7.99855  18.59017  19.90028 0.700 34.57557 ? 97  LYS A CG  1 
ATOM   738  C CD  . LYS A 1 103 ? -6.53464  18.62408  19.50410 0.600 37.45577 ? 97  LYS A CD  1 
ATOM   739  C CE  . LYS A 1 103 ? -6.36355  18.15234  18.06474 0.500 39.67533 ? 97  LYS A CE  1 
ATOM   740  N NZ  . LYS A 1 103 ? -5.07392  17.42656  17.82901 0.500 41.55094 ? 97  LYS A NZ  1 
ATOM   741  N N   . ASP A 1 104 ? -9.05320  16.06253  23.61978 1.000 32.90408 ? 98  ASP A N   1 
ATOM   742  C CA  . ASP A 1 104 ? -9.46325  15.83406  24.99851 1.000 32.89440 ? 98  ASP A CA  1 
ATOM   743  C C   . ASP A 1 104 ? -9.85268  14.36976  25.17217 1.000 30.30046 ? 98  ASP A C   1 
ATOM   744  O O   . ASP A 1 104 ? -10.11038 13.65218  24.21028 1.000 30.23623 ? 98  ASP A O   1 
ATOM   745  C CB  . ASP A 1 104 ? -10.66611 16.69372  25.38734 0.900 35.79863 ? 98  ASP A CB  1 
ATOM   746  C CG  . ASP A 1 104 ? -10.52606 18.13006  24.95880 0.600 37.22352 ? 98  ASP A CG  1 
ATOM   747  O OD1 . ASP A 1 104 ? -9.70661  18.86447  25.54553 0.600 36.65037 ? 98  ASP A OD1 1 
ATOM   748  O OD2 . ASP A 1 104 ? -11.29472 18.53728  24.06622 0.600 38.52106 ? 98  ASP A OD2 1 
ATOM   749  N N   . VAL A 1 105 ? -9.89436  13.92400  26.41371 1.000 28.19438 ? 99  VAL A N   1 
ATOM   750  C CA  . VAL A 1 105 ? -10.40202 12.60269  26.76623 1.000 28.29352 ? 99  VAL A CA  1 
ATOM   751  C C   . VAL A 1 105 ? -11.42662 12.78443  27.87888 1.000 27.05243 ? 99  VAL A C   1 
ATOM   752  O O   . VAL A 1 105 ? -11.21245 13.58271  28.79569 1.000 29.23168 ? 99  VAL A O   1 
ATOM   753  C CB  . VAL A 1 105 ? -9.25384  11.67660  27.21839 1.000 32.43118 ? 99  VAL A CB  1 
ATOM   754  C CG1 . VAL A 1 105 ? -9.76442  10.31445  27.59269 1.000 34.08189 ? 99  VAL A CG1 1 
ATOM   755  C CG2 . VAL A 1 105 ? -8.19745  11.58315  26.12584 1.000 33.33828 ? 99  VAL A CG2 1 
ATOM   756  N N   . TYR A 1 106 ? -12.54160 12.06592  27.79627 1.000 25.70802 ? 100 TYR A N   1 
ATOM   757  C CA  . TYR A 1 106 ? -13.55944 12.07926  28.85030 1.000 25.07188 ? 100 TYR A CA  1 
ATOM   758  C C   . TYR A 1 106 ? -13.63550 10.69835  29.46418 1.000 25.05767 ? 100 TYR A C   1 
ATOM   759  O O   . TYR A 1 106 ? -13.84903 9.71423   28.75221 1.000 26.41059 ? 100 TYR A O   1 
ATOM   760  C CB  . TYR A 1 106 ? -14.92301 12.45173  28.29303 1.000 26.37089 ? 100 TYR A CB  1 
ATOM   761  C CG  . TYR A 1 106 ? -14.94854 13.79803  27.61555 0.900 28.34998 ? 100 TYR A CG  1 
ATOM   762  C CD1 . TYR A 1 106 ? -15.20384 14.95115  28.33608 0.800 28.75481 ? 100 TYR A CD1 1 
ATOM   763  C CD2 . TYR A 1 106 ? -14.66976 13.92069  26.25670 0.800 29.73434 ? 100 TYR A CD2 1 
ATOM   764  C CE1 . TYR A 1 106 ? -15.23614 16.18366  27.72111 0.800 30.53936 ? 100 TYR A CE1 1 
ATOM   765  C CE2 . TYR A 1 106 ? -14.67861 15.15210  25.63820 0.800 31.52929 ? 100 TYR A CE2 1 
ATOM   766  C CZ  . TYR A 1 106 ? -14.95817 16.27948  26.37526 0.800 34.33397 ? 100 TYR A CZ  1 
ATOM   767  O OH  . TYR A 1 106 ? -14.97424 17.50248  25.76234 0.800 39.15014 ? 100 TYR A OH  1 
ATOM   768  N N   . ILE A 1 107 ? -13.45753 10.61912  30.77274 1.000 23.75558 ? 101 ILE A N   1 
ATOM   769  C CA  . ILE A 1 107 ? -13.57054 9.35389   31.48671 1.000 24.36899 ? 101 ILE A CA  1 
ATOM   770  C C   . ILE A 1 107 ? -14.89947 9.34107   32.22478 1.000 21.93681 ? 101 ILE A C   1 
ATOM   771  O O   . ILE A 1 107 ? -15.18803 10.25257  33.00976 1.000 24.26264 ? 101 ILE A O   1 
ATOM   772  C CB  . ILE A 1 107 ? -12.38559 9.13030   32.44775 1.000 27.56023 ? 101 ILE A CB  1 
ATOM   773  C CG1 . ILE A 1 107 ? -11.05210 9.20494   31.68563 1.000 30.02620 ? 101 ILE A CG1 1 
ATOM   774  C CG2 . ILE A 1 107 ? -12.51479 7.81116   33.18536 1.000 28.81458 ? 101 ILE A CG2 1 
ATOM   775  C CD1 . ILE A 1 107 ? -9.88441  9.15300   32.63699 1.000 34.87121 ? 101 ILE A CD1 1 
ATOM   776  N N   . VAL A 1 108 ? -15.70830 8.30972   31.96113 1.000 21.70422 ? 102 VAL A N   1 
ATOM   777  C CA  . VAL A 1 108 ? -17.04555 8.17076   32.53393 1.000 21.85529 ? 102 VAL A CA  1 
ATOM   778  C C   . VAL A 1 108 ? -16.96328 7.14881   33.65918 1.000 22.62970 ? 102 VAL A C   1 
ATOM   779  O O   . VAL A 1 108 ? -16.42117 6.05492   33.46815 1.000 24.91644 ? 102 VAL A O   1 
ATOM   780  C CB  . VAL A 1 108 ? -18.06703 7.72792   31.46664 1.000 23.31397 ? 102 VAL A CB  1 
ATOM   781  C CG1 . VAL A 1 108 ? -19.51495 7.72775   32.09318 1.000 23.55727 ? 102 VAL A CG1 1 
ATOM   782  C CG2 . VAL A 1 108 ? -17.99417 8.62113   30.20999 1.000 25.75821 ? 102 VAL A CG2 1 
ATOM   783  N N   . GLN A 1 109 ? -17.49083 7.49849   34.83240 1.000 23.07646 ? 103 GLN A N   1 
ATOM   784  C CA  A GLN A 1 109 ? -17.44402 6.63680   36.00898 0.700 21.72569 ? 103 GLN A CA  1 
ATOM   785  C CA  B GLN A 1 109 ? -17.47294 6.59812   35.98212 0.300 22.90419 ? 103 GLN A CA  1 
ATOM   786  C C   . GLN A 1 109 ? -18.80170 6.68717   36.71965 1.000 23.84446 ? 103 GLN A C   1 
ATOM   787  O O   . GLN A 1 109 ? -19.64652 7.52502   36.41233 1.000 24.64355 ? 103 GLN A O   1 
ATOM   788  C CB  A GLN A 1 109 ? -16.28355 7.06364   36.93418 0.700 22.69061 ? 103 GLN A CB  1 
ATOM   789  C CB  B GLN A 1 109 ? -16.31745 6.93221   36.92390 0.300 23.05658 ? 103 GLN A CB  1 
ATOM   790  C CG  A GLN A 1 109 ? -14.90790 7.18144   36.18451 0.700 22.48438 ? 103 GLN A CG  1 
ATOM   791  C CG  B GLN A 1 109 ? -16.32113 8.36790   37.36477 0.300 22.61779 ? 103 GLN A CG  1 
ATOM   792  C CD  A GLN A 1 109 ? -13.74330 7.56251   37.07859 0.700 25.55173 ? 103 GLN A CD  1 
ATOM   793  C CD  B GLN A 1 109 ? -15.16410 9.13999   36.76736 0.300 22.62215 ? 103 GLN A CD  1 
ATOM   794  O OE1 A GLN A 1 109 ? -13.49497 8.73207   37.31575 0.700 26.92586 ? 103 GLN A OE1 1 
ATOM   795  O OE1 B GLN A 1 109 ? -14.02241 8.66532   36.76365 0.300 23.78707 ? 103 GLN A OE1 1 
ATOM   796  N NE2 A GLN A 1 109 ? -13.02664 6.56580   37.57995 0.700 25.72117 ? 103 GLN A NE2 1 
ATOM   797  N NE2 B GLN A 1 109 ? -15.45365 10.33612  36.23914 0.300 19.90979 ? 103 GLN A NE2 1 
ATOM   798  N N   . ASP A 1 110 ? -18.99890 5.79425   37.70965 1.000 24.58453 ? 104 ASP A N   1 
ATOM   799  C CA  . ASP A 1 110 ? -20.22669 5.83787   38.50905 1.000 27.14463 ? 104 ASP A CA  1 
ATOM   800  C C   . ASP A 1 110 ? -20.38511 7.20511   39.17327 1.000 27.34824 ? 104 ASP A C   1 
ATOM   801  O O   . ASP A 1 110 ? -19.41140 7.80602   39.64363 1.000 26.81530 ? 104 ASP A O   1 
ATOM   802  C CB  . ASP A 1 110 ? -20.19915 4.77761   39.61070 1.000 29.85832 ? 104 ASP A CB  1 
ATOM   803  C CG  . ASP A 1 110 ? -20.18859 3.37003   39.06546 1.000 35.38805 ? 104 ASP A CG  1 
ATOM   804  O OD1 . ASP A 1 110 ? -20.64480 3.16811   37.90838 0.780 37.30435 ? 104 ASP A OD1 1 
ATOM   805  O OD2 . ASP A 1 110 ? -19.71245 2.47383   39.80278 0.680 35.78776 ? 104 ASP A OD2 1 
ATOM   806  N N   . LEU A 1 111 ? -21.62740 7.67032   39.29214 1.000 27.99019 ? 105 LEU A N   1 
ATOM   807  C CA  . LEU A 1 111 ? -21.86076 8.93305   39.97643 1.000 26.96447 ? 105 LEU A CA  1 
ATOM   808  C C   . LEU A 1 111 ? -21.92561 8.68391   41.47595 1.000 27.15140 ? 105 LEU A C   1 
ATOM   809  O O   . LEU A 1 111 ? -22.75057 7.89007   41.95288 1.000 28.39905 ? 105 LEU A O   1 
ATOM   810  C CB  . LEU A 1 111 ? -23.16183 9.56799   39.50088 1.000 28.43534 ? 105 LEU A CB  1 
ATOM   811  C CG  . LEU A 1 111 ? -23.53186 10.89772  40.15335 1.000 31.19840 ? 105 LEU A CG  1 
ATOM   812  C CD1 . LEU A 1 111 ? -22.52071 11.99075  39.91947 1.000 30.66143 ? 105 LEU A CD1 1 
ATOM   813  C CD2 . LEU A 1 111 ? -24.91215 11.33560  39.65477 1.000 32.82144 ? 105 LEU A CD2 1 
ATOM   814  N N   . MET A 1 112 ? -21.04693 9.34123   42.21835 1.000 24.70544 ? 106 MET A N   1 
ATOM   815  C CA  . MET A 1 112 ? -21.09056 9.23870   43.66003 1.000 22.52579 ? 106 MET A CA  1 
ATOM   816  C C   . MET A 1 112 ? -21.76024 10.48515  44.23439 1.000 25.46940 ? 106 MET A C   1 
ATOM   817  O O   . MET A 1 112 ? -22.08945 11.42140  43.51193 1.000 28.36971 ? 106 MET A O   1 
ATOM   818  C CB  . MET A 1 112 ? -19.67804 9.00337   44.20283 1.000 22.08445 ? 106 MET A CB  1 
ATOM   819  C CG  . MET A 1 112 ? -19.02082 7.88665   43.39787 1.000 22.93539 ? 106 MET A CG  1 
ATOM   820  S SD  . MET A 1 112 ? -19.54463 6.27038   44.00605 1.000 25.36551 ? 106 MET A SD  1 
ATOM   821  C CE  . MET A 1 112 ? -18.52088 5.96529   45.44773 1.000 25.44254 ? 106 MET A CE  1 
ATOM   822  N N   . GLU A 1 113 ? -22.05303 10.44444  45.53393 1.000 24.92655 ? 107 GLU A N   1 
ATOM   823  C CA  . GLU A 1 113 ? -22.73875 11.54905  46.20073 1.000 25.66799 ? 107 GLU A CA  1 
ATOM   824  C C   . GLU A 1 113 ? -21.79562 12.66188  46.63185 1.000 25.83951 ? 107 GLU A C   1 
ATOM   825  O O   . GLU A 1 113 ? -22.13778 13.84455  46.51970 1.000 27.09842 ? 107 GLU A O   1 
ATOM   826  C CB  . GLU A 1 113 ? -23.52134 11.03158  47.41288 0.800 25.30052 ? 107 GLU A CB  1 
ATOM   827  C CG  . GLU A 1 113 ? -24.27402 12.12642  48.15372 0.700 26.77969 ? 107 GLU A CG  1 
ATOM   828  C CD  . GLU A 1 113 ? -25.35007 11.61856  49.09080 0.500 30.90963 ? 107 GLU A CD  1 
ATOM   829  O OE1 . GLU A 1 113 ? -25.34539 12.05597  50.25086 0.500 34.32192 ? 107 GLU A OE1 1 
ATOM   830  O OE2 . GLU A 1 113 ? -26.32444 10.97765  48.61980 0.500 31.07224 ? 107 GLU A OE2 1 
ATOM   831  N N   . THR A 1 114 ? -20.62691 12.31292  47.15436 1.000 22.75496 ? 108 THR A N   1 
ATOM   832  C CA  . THR A 1 114 ? -19.72332 13.32669  47.67319 1.000 22.94414 ? 108 THR A CA  1 
ATOM   833  C C   . THR A 1 114 ? -18.32820 12.72333  47.72639 1.000 23.28127 ? 108 THR A C   1 
ATOM   834  O O   . THR A 1 114 ? -18.10930 11.56589  47.37528 1.000 23.85504 ? 108 THR A O   1 
ATOM   835  C CB  . THR A 1 114 ? -20.22046 13.81103  49.04783 1.000 25.35824 ? 108 THR A CB  1 
ATOM   836  O OG1 . THR A 1 114 ? -19.46878 14.94721  49.47874 1.000 30.10054 ? 108 THR A OG1 1 
ATOM   837  C CG2 . THR A 1 114 ? -20.10423 12.70269  50.08996 1.000 25.16973 ? 108 THR A CG2 1 
ATOM   838  N N   . ASP A 1 115 ? -17.37761 13.53217  48.12129 1.000 24.82341 ? 109 ASP A N   1 
ATOM   839  C CA  . ASP A 1 115 ? -16.06369 13.03011  48.47100 1.000 24.68962 ? 109 ASP A CA  1 
ATOM   840  C C   . ASP A 1 115 ? -15.82390 13.33753  49.94416 1.000 23.11493 ? 109 ASP A C   1 
ATOM   841  O O   . ASP A 1 115 ? -16.51503 14.17337  50.54983 1.000 22.80679 ? 109 ASP A O   1 
ATOM   842  C CB  . ASP A 1 115 ? -14.97881 13.62780  47.55537 1.000 28.10154 ? 109 ASP A CB  1 
ATOM   843  C CG  . ASP A 1 115 ? -14.88984 15.12939  47.67955 1.000 30.55383 ? 109 ASP A CG  1 
ATOM   844  O OD1 . ASP A 1 115 ? -14.22233 15.60475  48.60817 1.000 29.84930 ? 109 ASP A OD1 1 
ATOM   845  O OD2 . ASP A 1 115 ? -15.49972 15.85199  46.85445 1.000 35.49308 ? 109 ASP A OD2 1 
ATOM   846  N N   . LEU A 1 116 ? -14.86066 12.62242  50.53378 1.000 21.97011 ? 110 LEU A N   1 
ATOM   847  C CA  . LEU A 1 116 ? -14.61624 12.73994  51.96847 1.000 19.87293 ? 110 LEU A CA  1 
ATOM   848  C C   . LEU A 1 116 ? -14.08741 14.13452  52.33209 1.000 21.41871 ? 110 LEU A C   1 
ATOM   849  O O   . LEU A 1 116 ? -14.37862 14.65546  53.41305 1.000 22.44892 ? 110 LEU A O   1 
ATOM   850  C CB  . LEU A 1 116 ? -13.63154 11.64304  52.42249 1.000 20.75227 ? 110 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 116 ? -13.43971 11.52888  53.93337 1.000 20.85316 ? 110 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 116 ? -14.79074 11.18862  54.62284 1.000 23.38778 ? 110 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 116 ? -12.35931 10.51109  54.29191 1.000 21.71955 ? 110 LEU A CD2 1 
ATOM   854  N N   . TYR A 1 117 ? -13.33795 14.77828  51.43860 1.000 21.21416 ? 111 TYR A N   1 
ATOM   855  C CA  . TYR A 1 117 ? -12.92480 16.15814  51.69926 1.000 22.72182 ? 111 TYR A CA  1 
ATOM   856  C C   . TYR A 1 117 ? -14.13318 17.06233  51.93823 1.000 22.88822 ? 111 TYR A C   1 
ATOM   857  O O   . TYR A 1 117 ? -14.19157 17.79704  52.93631 1.000 23.22735 ? 111 TYR A O   1 
ATOM   858  C CB  . TYR A 1 117 ? -12.06176 16.67256  50.53276 1.000 24.27732 ? 111 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 117 ? -11.67469 18.11953  50.66646 1.000 26.32780 ? 111 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 117 ? -10.66020 18.47371  51.51860 1.000 29.20478 ? 111 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 117 ? -12.32429 19.13008  49.95060 1.000 31.51951 ? 111 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 117 ? -10.26888 19.79096  51.67267 1.000 32.83271 ? 111 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 117 ? -11.96459 20.46638  50.11233 1.000 34.80843 ? 111 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 117 ? -10.91633 20.78798  50.98031 1.000 35.60722 ? 111 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 117 ? -10.50390 22.08425  51.18156 0.490 36.08305 ? 111 TYR A OH  1 
ATOM   866  N N   . LYS A 1 118 ? -15.11551 17.02055  51.03382 1.000 23.80025 ? 112 LYS A N   1 
ATOM   867  C CA  . LYS A 1 118 ? -16.28387 17.88189  51.16914 1.000 24.92744 ? 112 LYS A CA  1 
ATOM   868  C C   . LYS A 1 118 ? -17.09324 17.48730  52.39242 1.000 25.89695 ? 112 LYS A C   1 
ATOM   869  O O   . LYS A 1 118 ? -17.58365 18.35170  53.13716 1.000 26.83092 ? 112 LYS A O   1 
ATOM   870  C CB  . LYS A 1 118 ? -17.14203 17.78482  49.90725 1.000 28.30470 ? 112 LYS A CB  1 
ATOM   871  C CG  . LYS A 1 118 ? -16.45910 18.30784  48.64396 0.800 34.53611 ? 112 LYS A CG  1 
ATOM   872  C CD  . LYS A 1 118 ? -16.53991 19.82784  48.51874 0.700 38.83374 ? 112 LYS A CD  1 
ATOM   873  C CE  . LYS A 1 118 ? -15.69444 20.35438  47.36434 0.600 41.51350 ? 112 LYS A CE  1 
ATOM   874  N NZ  . LYS A 1 118 ? -16.52986 20.71146  46.18040 0.600 43.86561 ? 112 LYS A NZ  1 
ATOM   875  N N   . LEU A 1 119 ? -17.24159 16.18537  52.61067 1.000 25.36694 ? 113 LEU A N   1 
ATOM   876  C CA  . LEU A 1 119 ? -17.98517 15.70425  53.77141 1.000 25.60047 ? 113 LEU A CA  1 
ATOM   877  C C   . LEU A 1 119 ? -17.37367 16.20700  55.07594 1.000 25.73929 ? 113 LEU A C   1 
ATOM   878  O O   . LEU A 1 119 ? -18.08037 16.68658  55.97189 1.000 28.81456 ? 113 LEU A O   1 
ATOM   879  C CB  . LEU A 1 119 ? -18.01887 14.18137  53.73663 1.000 26.91374 ? 113 LEU A CB  1 
ATOM   880  C CG  . LEU A 1 119 ? -19.01422 13.49804  54.64879 1.000 29.26800 ? 113 LEU A CG  1 
ATOM   881  C CD1 . LEU A 1 119 ? -20.43572 13.90124  54.27759 1.000 29.51118 ? 113 LEU A CD1 1 
ATOM   882  C CD2 . LEU A 1 119 ? -18.82893 11.98979  54.48574 1.000 32.02886 ? 113 LEU A CD2 1 
ATOM   883  N N   . LEU A 1 120 ? -16.05545 16.11494  55.20663 1.000 23.75297 ? 114 LEU A N   1 
ATOM   884  C CA  . LEU A 1 120 ? -15.43399 16.49421  56.47558 1.000 25.66788 ? 114 LEU A CA  1 
ATOM   885  C C   . LEU A 1 120 ? -15.46674 17.99293  56.75301 1.000 26.33959 ? 114 LEU A C   1 
ATOM   886  O O   . LEU A 1 120 ? -15.25949 18.39100  57.90315 1.000 27.44435 ? 114 LEU A O   1 
ATOM   887  C CB  . LEU A 1 120 ? -13.99719 15.99758  56.49916 1.000 26.80503 ? 114 LEU A CB  1 
ATOM   888  C CG  . LEU A 1 120 ? -13.90346 14.48015  56.59882 1.000 28.55898 ? 114 LEU A CG  1 
ATOM   889  C CD1 . LEU A 1 120 ? -12.44911 14.06610  56.43883 1.000 28.76152 ? 114 LEU A CD1 1 
ATOM   890  C CD2 . LEU A 1 120 ? -14.49364 14.01586  57.93887 1.000 31.48879 ? 114 LEU A CD2 1 
ATOM   891  N N   . LYS A 1 121 ? -15.71276 18.83396  55.74351 1.000 25.97876 ? 115 LYS A N   1 
ATOM   892  C CA  . LYS A 1 121 ? -15.84620 20.26566  55.99405 1.000 28.82779 ? 115 LYS A CA  1 
ATOM   893  C C   . LYS A 1 121 ? -17.04350 20.59147  56.87716 1.000 29.14817 ? 115 LYS A C   1 
ATOM   894  O O   . LYS A 1 121 ? -17.01112 21.58730  57.61098 1.000 31.27454 ? 115 LYS A O   1 
ATOM   895  C CB  . LYS A 1 121 ? -15.96714 21.05487  54.68804 0.800 30.29544 ? 115 LYS A CB  1 
ATOM   896  C CG  . LYS A 1 121 ? -14.83522 20.92873  53.72078 0.700 32.23453 ? 115 LYS A CG  1 
ATOM   897  C CD  . LYS A 1 121 ? -14.96945 22.01693  52.66866 0.600 36.16527 ? 115 LYS A CD  1 
ATOM   898  C CE  . LYS A 1 121 ? -15.65117 21.53214  51.40720 0.500 38.81289 ? 115 LYS A CE  1 
ATOM   899  N NZ  . LYS A 1 121 ? -14.97861 22.06143  50.17655 0.500 40.33275 ? 115 LYS A NZ  1 
ATOM   900  N N   . THR A 1 122 ? -18.12067 19.80680  56.80572 1.000 28.51945 ? 116 THR A N   1 
ATOM   901  C CA  . THR A 1 122 ? -19.32400 20.13881  57.56992 1.000 28.28776 ? 116 THR A CA  1 
ATOM   902  C C   . THR A 1 122 ? -19.89932 19.02766  58.43346 1.000 29.56821 ? 116 THR A C   1 
ATOM   903  O O   . THR A 1 122 ? -20.75670 19.32693  59.26876 1.000 33.55725 ? 116 THR A O   1 
ATOM   904  C CB  . THR A 1 122 ? -20.45377 20.62785  56.64596 0.800 27.56945 ? 116 THR A CB  1 
ATOM   905  O OG1 . THR A 1 122 ? -20.84771 19.58307  55.74190 0.800 27.98449 ? 116 THR A OG1 1 
ATOM   906  C CG2 . THR A 1 122 ? -20.05896 21.87328  55.89741 0.800 29.80183 ? 116 THR A CG2 1 
ATOM   907  N N   . GLN A 1 123 ? -19.48691 17.77676  58.27976 1.000 25.91634 ? 117 GLN A N   1 
ATOM   908  C CA  . GLN A 1 123 ? -20.16106 16.66432  58.94437 1.000 26.57285 ? 117 GLN A CA  1 
ATOM   909  C C   . GLN A 1 123 ? -19.25055 15.98925  59.96397 1.000 27.21419 ? 117 GLN A C   1 
ATOM   910  O O   . GLN A 1 123 ? -18.11357 15.61312  59.64780 1.000 27.87586 ? 117 GLN A O   1 
ATOM   911  C CB  . GLN A 1 123 ? -20.66278 15.63322  57.91065 1.000 24.80948 ? 117 GLN A CB  1 
ATOM   912  C CG  . GLN A 1 123 ? -21.54752 16.26992  56.80335 1.000 26.52006 ? 117 GLN A CG  1 
ATOM   913  C CD  . GLN A 1 123 ? -22.83548 16.85091  57.35388 1.000 28.84664 ? 117 GLN A CD  1 
ATOM   914  O OE1 . GLN A 1 123 ? -23.46383 16.25835  58.21288 1.000 28.72133 ? 117 GLN A OE1 1 
ATOM   915  N NE2 . GLN A 1 123 ? -23.20819 18.03878  56.88434 1.000 32.88434 ? 117 GLN A NE2 1 
ATOM   916  N N   . HIS A 1 124 ? -19.76410 15.81153  61.17492 1.000 29.02805 ? 118 HIS A N   1 
ATOM   917  C CA  . HIS A 1 124 ? -19.12751 14.95096  62.17239 1.000 29.51646 ? 118 HIS A CA  1 
ATOM   918  C C   . HIS A 1 124 ? -19.42891 13.48590  61.86346 1.000 28.84585 ? 118 HIS A C   1 
ATOM   919  O O   . HIS A 1 124 ? -20.56957 13.12793  61.55785 1.000 30.46523 ? 118 HIS A O   1 
ATOM   920  C CB  . HIS A 1 124 ? -19.62578 15.34376  63.56403 0.700 33.05036 ? 118 HIS A CB  1 
ATOM   921  C CG  . HIS A 1 124 ? -19.19494 14.42623  64.66304 0.600 37.86606 ? 118 HIS A CG  1 
ATOM   922  N ND1 . HIS A 1 124 ? -17.95967 14.51449  65.27143 0.600 40.29367 ? 118 HIS A ND1 1 
ATOM   923  C CD2 . HIS A 1 124 ? -19.87483 13.45824  65.32704 0.600 37.93407 ? 118 HIS A CD2 1 
ATOM   924  C CE1 . HIS A 1 124 ? -17.88199 13.60892  66.23380 0.600 40.46917 ? 118 HIS A CE1 1 
ATOM   925  N NE2 . HIS A 1 124 ? -19.03281 12.95797  66.29089 0.600 38.91329 ? 118 HIS A NE2 1 
ATOM   926  N N   . LEU A 1 125 ? -18.40842 12.63980  61.89695 1.000 27.61930 ? 119 LEU A N   1 
ATOM   927  C CA  . LEU A 1 125 ? -18.58968 11.21176  61.64243 1.000 27.52968 ? 119 LEU A CA  1 
ATOM   928  C C   . LEU A 1 125 ? -18.83055 10.46869  62.94499 1.000 30.29375 ? 119 LEU A C   1 
ATOM   929  O O   . LEU A 1 125 ? -18.07059 10.64768  63.90719 1.000 34.24894 ? 119 LEU A O   1 
ATOM   930  C CB  . LEU A 1 125 ? -17.36047 10.61427  60.94178 1.000 27.65942 ? 119 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 125 ? -17.36762 10.71604  59.41563 1.000 32.24871 ? 119 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 125 ? -17.63207 12.13616  58.96678 1.000 38.14841 ? 119 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 125 ? -16.03440 10.19715  58.83984 1.000 29.40474 ? 119 LEU A CD2 1 
ATOM   934  N N   . SER A 1 126 ? -19.86558 9.61596   62.96414 1.000 28.66223 ? 120 SER A N   1 
ATOM   935  C CA  . SER A 1 126 ? -20.04545 8.68031   64.07340 1.000 31.82657 ? 120 SER A CA  1 
ATOM   936  C C   . SER A 1 126 ? -18.89653 7.66685   64.08283 1.000 30.12416 ? 120 SER A C   1 
ATOM   937  O O   . SER A 1 126 ? -18.26482 7.42014   63.06163 1.000 27.38090 ? 120 SER A O   1 
ATOM   938  C CB  . SER A 1 126 ? -21.39630 7.96016   63.95821 1.000 34.49223 ? 120 SER A CB  1 
ATOM   939  O OG  . SER A 1 126 ? -21.35600 6.88112   63.00657 1.000 35.26127 ? 120 SER A OG  1 
ATOM   940  N N   . ASN A 1 127 ? -18.61685 7.07450   65.25123 1.000 28.67455 ? 121 ASN A N   1 
ATOM   941  C CA  . ASN A 1 127 ? -17.60392 6.02673   65.27302 1.000 26.15497 ? 121 ASN A CA  1 
ATOM   942  C C   . ASN A 1 127 ? -17.96937 4.88305   64.32864 1.000 25.82768 ? 121 ASN A C   1 
ATOM   943  O O   . ASN A 1 127 ? -17.07772 4.30870   63.68348 1.000 27.48822 ? 121 ASN A O   1 
ATOM   944  C CB  . ASN A 1 127 ? -17.36512 5.49975   66.69373 1.000 28.91063 ? 121 ASN A CB  1 
ATOM   945  C CG  . ASN A 1 127 ? -16.29332 4.37736   66.73318 0.800 28.82107 ? 121 ASN A CG  1 
ATOM   946  O OD1 . ASN A 1 127 ? -15.12588 4.56314   66.32054 0.800 25.69565 ? 121 ASN A OD1 1 
ATOM   947  N ND2 . ASN A 1 127 ? -16.69197 3.21307   67.21050 0.800 32.15015 ? 121 ASN A ND2 1 
ATOM   948  N N   . ASP A 1 128 ? -19.27538 4.57858   64.16774 1.000 27.29472 ? 122 ASP A N   1 
ATOM   949  C CA  . ASP A 1 128 ? -19.65321 3.52779   63.22451 1.000 27.63165 ? 122 ASP A CA  1 
ATOM   950  C C   . ASP A 1 128 ? -19.30216 3.91418   61.78653 1.000 25.90110 ? 122 ASP A C   1 
ATOM   951  O O   . ASP A 1 128 ? -18.89325 3.06146   60.98768 1.000 26.69579 ? 122 ASP A O   1 
ATOM   952  C CB  . ASP A 1 128 ? -21.14115 3.20336   63.34675 1.000 30.75940 ? 122 ASP A CB  1 
ATOM   953  C CG  . ASP A 1 128 ? -21.49075 2.48481   64.65882 0.700 31.86610 ? 122 ASP A CG  1 
ATOM   954  O OD1 . ASP A 1 128 ? -20.66508 1.69318   65.16890 0.500 33.95133 ? 122 ASP A OD1 1 
ATOM   955  O OD2 . ASP A 1 128 ? -22.59691 2.70892   65.17735 0.500 31.55620 ? 122 ASP A OD2 1 
ATOM   956  N N   . HIS A 1 129 ? -19.44014 5.18925   61.43309 1.000 23.78361 ? 123 HIS A N   1 
ATOM   957  C CA  . HIS A 1 129 ? -19.05342 5.58090   60.07599 1.000 22.10791 ? 123 HIS A CA  1 
ATOM   958  C C   . HIS A 1 129 ? -17.54084 5.55079   59.90200 1.000 22.78975 ? 123 HIS A C   1 
ATOM   959  O O   . HIS A 1 129 ? -17.04436 5.15567   58.84440 1.000 22.65410 ? 123 HIS A O   1 
ATOM   960  C CB  . HIS A 1 129 ? -19.57658 6.97432   59.75210 1.000 22.16481 ? 123 HIS A CB  1 
ATOM   961  C CG  . HIS A 1 129 ? -21.02165 6.98558   59.36528 1.000 23.94454 ? 123 HIS A CG  1 
ATOM   962  N ND1 . HIS A 1 129 ? -22.03128 7.16312   60.28428 1.000 27.63654 ? 123 HIS A ND1 1 
ATOM   963  C CD2 . HIS A 1 129 ? -21.62822 6.83520   58.16348 1.000 24.92014 ? 123 HIS A CD2 1 
ATOM   964  C CE1 . HIS A 1 129 ? -23.19665 7.12729   59.66613 1.000 28.02286 ? 123 HIS A CE1 1 
ATOM   965  N NE2 . HIS A 1 129 ? -22.97874 6.93762   58.37841 1.000 26.08377 ? 123 HIS A NE2 1 
ATOM   966  N N   . ILE A 1 130 ? -16.80006 6.01500   60.90874 1.000 22.28319 ? 124 ILE A N   1 
ATOM   967  C CA  . ILE A 1 130 ? -15.34311 6.00560   60.81203 1.000 19.88700 ? 124 ILE A CA  1 
ATOM   968  C C   . ILE A 1 130 ? -14.84266 4.58828   60.59516 1.000 19.33799 ? 124 ILE A C   1 
ATOM   969  O O   . ILE A 1 130 ? -13.96680 4.33932   59.75586 1.000 20.16706 ? 124 ILE A O   1 
ATOM   970  C CB  . ILE A 1 130 ? -14.72325 6.63287   62.06650 1.000 20.72300 ? 124 ILE A CB  1 
ATOM   971  C CG1 . ILE A 1 130 ? -15.10057 8.10130   62.15953 1.000 23.08689 ? 124 ILE A CG1 1 
ATOM   972  C CG2 . ILE A 1 130 ? -13.20241 6.49016   62.07468 1.000 21.35647 ? 124 ILE A CG2 1 
ATOM   973  C CD1 . ILE A 1 130 ? -14.68040 8.72061   63.46142 1.000 26.31039 ? 124 ILE A CD1 1 
ATOM   974  N N   . CYS A 1 131 ? -15.38016 3.64399   61.37339 1.000 19.80220 ? 125 CYS A N   1 
ATOM   975  C CA  . CYS A 1 131 ? -14.98137 2.24998   61.27476 1.000 19.85345 ? 125 CYS A CA  1 
ATOM   976  C C   . CYS A 1 131 ? -15.27658 1.70255   59.87604 1.000 18.54107 ? 125 CYS A C   1 
ATOM   977  O O   . CYS A 1 131 ? -14.41276 1.10794   59.22609 1.000 19.60513 ? 125 CYS A O   1 
ATOM   978  C CB  . CYS A 1 131 ? -15.70926 1.46876   62.37913 1.000 21.33528 ? 125 CYS A CB  1 
ATOM   979  S SG  . CYS A 1 131 ? -15.21216 -0.19902  62.58420 1.000 25.39975 ? 125 CYS A SG  1 
ATOM   980  N N   . TYR A 1 132 ? -16.47801 1.95181   59.36777 1.000 20.16117 ? 126 TYR A N   1 
ATOM   981  C CA  . TYR A 1 132 ? -16.84891 1.44803   58.05076 1.000 21.02405 ? 126 TYR A CA  1 
ATOM   982  C C   . TYR A 1 132 ? -16.02374 2.09173   56.94068 1.000 20.83439 ? 126 TYR A C   1 
ATOM   983  O O   . TYR A 1 132 ? -15.58939 1.40119   56.00015 1.000 20.86811 ? 126 TYR A O   1 
ATOM   984  C CB  . TYR A 1 132 ? -18.33613 1.70115   57.84303 1.000 23.05387 ? 126 TYR A CB  1 
ATOM   985  C CG  . TYR A 1 132 ? -18.91815 1.10822   56.58196 1.000 25.60443 ? 126 TYR A CG  1 
ATOM   986  C CD1 . TYR A 1 132 ? -18.61226 -0.20731  56.19582 1.000 30.07679 ? 126 TYR A CD1 1 
ATOM   987  C CD2 . TYR A 1 132 ? -19.78500 1.85669   55.77290 1.000 25.43147 ? 126 TYR A CD2 1 
ATOM   988  C CE1 . TYR A 1 132 ? -19.15110 -0.75275  55.02944 1.000 31.93660 ? 126 TYR A CE1 1 
ATOM   989  C CE2 . TYR A 1 132 ? -20.33390 1.30860   54.63687 1.000 28.31611 ? 126 TYR A CE2 1 
ATOM   990  C CZ  . TYR A 1 132 ? -20.00571 0.01745   54.26148 1.000 33.13876 ? 126 TYR A CZ  1 
ATOM   991  O OH  . TYR A 1 132 ? -20.54100 -0.51262  53.11143 1.000 39.01178 ? 126 TYR A OH  1 
ATOM   992  N N   . PHE A 1 133 ? -15.80020 3.40541   57.02504 1.000 18.19430 ? 127 PHE A N   1 
ATOM   993  C CA  . PHE A 1 133 ? -15.00766 4.07143   55.99366 1.000 18.59574 ? 127 PHE A CA  1 
ATOM   994  C C   . PHE A 1 133 ? -13.59074 3.52833   55.99376 1.000 16.88404 ? 127 PHE A C   1 
ATOM   995  O O   . PHE A 1 133 ? -13.04378 3.20940   54.93620 1.000 16.54665 ? 127 PHE A O   1 
ATOM   996  C CB  . PHE A 1 133 ? -14.95689 5.59918   56.19833 1.000 20.21207 ? 127 PHE A CB  1 
ATOM   997  C CG  . PHE A 1 133 ? -16.25498 6.31833   55.89111 1.000 20.47422 ? 127 PHE A CG  1 
ATOM   998  C CD1 . PHE A 1 133 ? -17.32435 5.67734   55.27301 1.000 24.04743 ? 127 PHE A CD1 1 
ATOM   999  C CD2 . PHE A 1 133 ? -16.40608 7.64210   56.25057 1.000 23.68193 ? 127 PHE A CD2 1 
ATOM   1000 C CE1 . PHE A 1 133 ? -18.51858 6.37419   55.01120 1.000 28.32207 ? 127 PHE A CE1 1 
ATOM   1001 C CE2 . PHE A 1 133 ? -17.61025 8.32882   56.01436 1.000 24.62647 ? 127 PHE A CE2 1 
ATOM   1002 C CZ  . PHE A 1 133 ? -18.64534 7.70184   55.38014 1.000 25.26063 ? 127 PHE A CZ  1 
ATOM   1003 N N   . LEU A 1 134 ? -12.99072 3.38587   57.18743 1.000 17.21081 ? 128 LEU A N   1 
ATOM   1004 C CA  . LEU A 1 134 ? -11.61851 2.89150   57.26995 1.000 15.73078 ? 128 LEU A CA  1 
ATOM   1005 C C   . LEU A 1 134 ? -11.51389 1.47269   56.72610 1.000 17.07303 ? 128 LEU A C   1 
ATOM   1006 O O   . LEU A 1 134 ? -10.55977 1.14434   55.99218 1.000 15.62546 ? 128 LEU A O   1 
ATOM   1007 C CB  . LEU A 1 134 ? -11.14592 2.91829   58.72197 1.000 16.07217 ? 128 LEU A CB  1 
ATOM   1008 C CG  . LEU A 1 134 ? -9.70928  2.42022   58.91505 1.000 17.73294 ? 128 LEU A CG  1 
ATOM   1009 C CD1 . LEU A 1 134 ? -8.72432  3.33116   58.18014 1.000 21.07748 ? 128 LEU A CD1 1 
ATOM   1010 C CD2 . LEU A 1 134 ? -9.38452  2.37189   60.38895 1.000 18.97933 ? 128 LEU A CD2 1 
ATOM   1011 N N   . TYR A 1 135 ? -12.48095 0.62218   57.08848 1.000 16.58158 ? 129 TYR A N   1 
ATOM   1012 C CA  . TYR A 1 135 ? -12.51444 -0.74407  56.57737 1.000 15.97046 ? 129 TYR A CA  1 
ATOM   1013 C C   . TYR A 1 135 ? -12.48351 -0.72623  55.05296 1.000 15.79993 ? 129 TYR A C   1 
ATOM   1014 O O   . TYR A 1 135 ? -11.68448 -1.43662  54.43034 1.000 15.22611 ? 129 TYR A O   1 
ATOM   1015 C CB  . TYR A 1 135 ? -13.76752 -1.49866  57.07742 1.000 17.62776 ? 129 TYR A CB  1 
ATOM   1016 C CG  . TYR A 1 135 ? -13.85054 -2.86587  56.44946 1.000 16.25655 ? 129 TYR A CG  1 
ATOM   1017 C CD1 . TYR A 1 135 ? -12.92596 -3.85379  56.77453 1.000 19.10497 ? 129 TYR A CD1 1 
ATOM   1018 C CD2 . TYR A 1 135 ? -14.81694 -3.15796  55.47448 1.000 19.09015 ? 129 TYR A CD2 1 
ATOM   1019 C CE1 . TYR A 1 135 ? -12.97519 -5.11246  56.18490 1.000 19.58725 ? 129 TYR A CE1 1 
ATOM   1020 C CE2 . TYR A 1 135 ? -14.88278 -4.40972  54.88625 1.000 21.10856 ? 129 TYR A CE2 1 
ATOM   1021 C CZ  . TYR A 1 135 ? -13.94807 -5.38313  55.23874 1.000 21.75991 ? 129 TYR A CZ  1 
ATOM   1022 O OH  . TYR A 1 135 ? -13.96742 -6.61290  54.63460 1.000 22.17732 ? 129 TYR A OH  1 
ATOM   1023 N N   . GLN A 1 136 ? -13.34488 0.10838   54.43573 1.000 14.87627 ? 130 GLN A N   1 
ATOM   1024 C CA  . GLN A 1 136 ? -13.41984 0.12144   52.97337 1.000 14.93903 ? 130 GLN A CA  1 
ATOM   1025 C C   . GLN A 1 136 ? -12.14725 0.67860   52.32603 1.000 15.50339 ? 130 GLN A C   1 
ATOM   1026 O O   . GLN A 1 136 ? -11.73577 0.19823   51.26487 1.000 15.86639 ? 130 GLN A O   1 
ATOM   1027 C CB  . GLN A 1 136 ? -14.63746 0.91543   52.53125 1.000 15.82676 ? 130 GLN A CB  1 
ATOM   1028 C CG  . GLN A 1 136 ? -15.93164 0.29004   52.95983 0.900 17.26375 ? 130 GLN A CG  1 
ATOM   1029 C CD  . GLN A 1 136 ? -17.07983 1.10719   52.45210 0.900 17.67780 ? 130 GLN A CD  1 
ATOM   1030 O OE1 . GLN A 1 136 ? -17.48579 0.95851   51.28197 0.800 18.03579 ? 130 GLN A OE1 1 
ATOM   1031 N NE2 . GLN A 1 136 ? -17.55852 2.04599   53.27693 0.800 16.86872 ? 130 GLN A NE2 1 
ATOM   1032 N N   . ILE A 1 137 ? -11.53644 1.70526   52.92097 1.000 14.29151 ? 131 ILE A N   1 
ATOM   1033 C CA  . ILE A 1 137 ? -10.26238 2.21494   52.40632 1.000 14.63916 ? 131 ILE A CA  1 
ATOM   1034 C C   . ILE A 1 137 ? -9.22284  1.09044   52.37929 1.000 14.99438 ? 131 ILE A C   1 
ATOM   1035 O O   . ILE A 1 137 ? -8.52841  0.86812   51.37139 1.000 15.10525 ? 131 ILE A O   1 
ATOM   1036 C CB  . ILE A 1 137 ? -9.76578  3.40007   53.26426 1.000 14.12711 ? 131 ILE A CB  1 
ATOM   1037 C CG1 . ILE A 1 137 ? -10.70636 4.60592   53.17066 1.000 15.83329 ? 131 ILE A CG1 1 
ATOM   1038 C CG2 . ILE A 1 137 ? -8.32644  3.78658   52.80653 1.000 14.34746 ? 131 ILE A CG2 1 
ATOM   1039 C CD1 . ILE A 1 137 ? -10.52651 5.61799   54.28890 1.000 16.67391 ? 131 ILE A CD1 1 
ATOM   1040 N N   . LEU A 1 138 ? -9.10884  0.35646   53.48783 1.000 15.16801 ? 132 LEU A N   1 
ATOM   1041 C CA  . LEU A 1 138 ? -8.08680  -0.69485  53.59358 1.000 15.01698 ? 132 LEU A CA  1 
ATOM   1042 C C   . LEU A 1 138 ? -8.40422  -1.86793  52.68110 1.000 14.01649 ? 132 LEU A C   1 
ATOM   1043 O O   . LEU A 1 138 ? -7.49849  -2.51126  52.14594 1.000 15.78156 ? 132 LEU A O   1 
ATOM   1044 C CB  . LEU A 1 138 ? -7.97160  -1.19023  55.04736 1.000 15.61674 ? 132 LEU A CB  1 
ATOM   1045 C CG  . LEU A 1 138 ? -7.37460  -0.12566  55.96139 1.000 14.85438 ? 132 LEU A CG  1 
ATOM   1046 C CD1 . LEU A 1 138 ? -7.56440  -0.50079  57.48152 1.000 17.05648 ? 132 LEU A CD1 1 
ATOM   1047 C CD2 . LEU A 1 138 ? -5.89808  0.12392   55.65609 1.000 16.19458 ? 132 LEU A CD2 1 
ATOM   1048 N N   . ARG A 1 139 ? -9.69938  -2.17584  52.49760 1.000 15.08138 ? 133 ARG A N   1 
ATOM   1049 C CA  . ARG A 1 139 ? -10.07251 -3.27432  51.61339 1.000 14.57684 ? 133 ARG A CA  1 
ATOM   1050 C C   . ARG A 1 139 ? -9.67206  -2.94393  50.18796 1.000 14.61563 ? 133 ARG A C   1 
ATOM   1051 O O   . ARG A 1 139 ? -9.09577  -3.78253  49.47777 1.000 15.81966 ? 133 ARG A O   1 
ATOM   1052 C CB  . ARG A 1 139 ? -11.58350 -3.51699  51.73776 1.000 14.12900 ? 133 ARG A CB  1 
ATOM   1053 C CG  . ARG A 1 139 ? -12.13584 -4.64498  50.92523 1.000 14.84785 ? 133 ARG A CG  1 
ATOM   1054 C CD  . ARG A 1 139 ? -13.65391 -4.84275  51.25504 1.000 16.47197 ? 133 ARG A CD  1 
ATOM   1055 N NE  . ARG A 1 139 ? -14.21817 -5.97409  50.54945 1.000 18.79025 ? 133 ARG A NE  1 
ATOM   1056 C CZ  . ARG A 1 139 ? -15.04008 -5.89195  49.51626 1.000 21.98445 ? 133 ARG A CZ  1 
ATOM   1057 N NH1 . ARG A 1 139 ? -15.34267 -4.71849  48.96363 1.000 23.56135 ? 133 ARG A NH1 1 
ATOM   1058 N NH2 . ARG A 1 139 ? -15.58575 -7.01665  49.03710 1.000 22.47919 ? 133 ARG A NH2 1 
ATOM   1059 N N   . GLY A 1 140 ? -9.94113  -1.71056  49.75457 1.000 14.64806 ? 134 GLY A N   1 
ATOM   1060 C CA  . GLY A 1 140 ? -9.48090  -1.29190  48.43161 1.000 14.21550 ? 134 GLY A CA  1 
ATOM   1061 C C   . GLY A 1 140 ? -7.96356  -1.25423  48.34928 1.000 13.81217 ? 134 GLY A C   1 
ATOM   1062 O O   . GLY A 1 140 ? -7.35684  -1.67099  47.34064 1.000 14.85220 ? 134 GLY A O   1 
ATOM   1063 N N   . LEU A 1 141 ? -7.32272  -0.74451  49.40513 1.000 14.43256 ? 135 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 141 ? -5.86280  -0.67899  49.39491 1.000 13.91015 ? 135 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 141 ? -5.22307  -2.07328  49.34969 1.000 15.84181 ? 135 LEU A C   1 
ATOM   1066 O O   . LEU A 1 141 ? -4.20100  -2.26548  48.66608 1.000 15.70515 ? 135 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 141 ? -5.37790  0.11514   50.59214 1.000 13.85961 ? 135 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 141 ? -3.89184  0.48207   50.51151 1.000 14.24979 ? 135 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 141 ? -3.56594  1.33351   49.27126 1.000 15.70413 ? 135 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 141 ? -3.53695  1.24131   51.81521 1.000 16.98719 ? 135 LEU A CD2 1 
ATOM   1071 N N   . LYS A 1 142 ? -5.82081  -3.06170  50.01490 1.000 14.34344 ? 136 LYS A N   1 
ATOM   1072 C CA  . LYS A 1 142 ? -5.30451  -4.42546  49.93497 1.000 13.94203 ? 136 LYS A CA  1 
ATOM   1073 C C   . LYS A 1 142 ? -5.24238  -4.89003  48.48049 1.000 13.95713 ? 136 LYS A C   1 
ATOM   1074 O O   . LYS A 1 142 ? -4.24899  -5.47953  48.03391 1.000 16.66682 ? 136 LYS A O   1 
ATOM   1075 C CB  . LYS A 1 142 ? -6.16698  -5.38329  50.76969 1.000 13.85824 ? 136 LYS A CB  1 
ATOM   1076 C CG  . LYS A 1 142 ? -5.75029  -6.83200  50.60401 1.000 15.29308 ? 136 LYS A CG  1 
ATOM   1077 C CD  . LYS A 1 142 ? -6.64333  -7.77040  51.34340 1.000 16.94895 ? 136 LYS A CD  1 
ATOM   1078 C CE  . LYS A 1 142 ? -6.20409  -9.24345  51.11946 1.000 18.94729 ? 136 LYS A CE  1 
ATOM   1079 N NZ  . LYS A 1 142 ? -7.13381  -10.25405 51.75670 1.000 19.49699 ? 136 LYS A NZ  1 
ATOM   1080 N N   . TYR A 1 143 ? -6.30216  -4.61761  47.71400 1.000 15.94887 ? 137 TYR A N   1 
ATOM   1081 C CA  . TYR A 1 143 ? -6.30422  -4.99242  46.30100 1.000 16.81009 ? 137 TYR A CA  1 
ATOM   1082 C C   . TYR A 1 143 ? -5.20988  -4.26921  45.52334 1.000 17.00803 ? 137 TYR A C   1 
ATOM   1083 O O   . TYR A 1 143 ? -4.49184  -4.88136  44.72041 1.000 17.08894 ? 137 TYR A O   1 
ATOM   1084 C CB  . TYR A 1 143 ? -7.68773  -4.69821  45.70606 1.000 16.67607 ? 137 TYR A CB  1 
ATOM   1085 C CG  . TYR A 1 143 ? -7.86929  -5.09425  44.26245 1.000 16.16140 ? 137 TYR A CG  1 
ATOM   1086 C CD1 . TYR A 1 143 ? -7.54448  -4.19383  43.22323 1.000 17.51459 ? 137 TYR A CD1 1 
ATOM   1087 C CD2 . TYR A 1 143 ? -8.35813  -6.35385  43.92423 1.000 18.34457 ? 137 TYR A CD2 1 
ATOM   1088 C CE1 . TYR A 1 143 ? -7.69064  -4.55000  41.90643 1.000 20.04579 ? 137 TYR A CE1 1 
ATOM   1089 C CE2 . TYR A 1 143 ? -8.52535  -6.71211  42.56609 1.000 18.57041 ? 137 TYR A CE2 1 
ATOM   1090 C CZ  . TYR A 1 143 ? -8.19908  -5.79047  41.58834 1.000 19.92240 ? 137 TYR A CZ  1 
ATOM   1091 O OH  . TYR A 1 143 ? -8.35806  -6.09508  40.25196 1.000 22.10741 ? 137 TYR A OH  1 
ATOM   1092 N N   . ILE A 1 144 ? -5.10583  -2.95659  45.70928 1.000 14.33945 ? 138 ILE A N   1 
ATOM   1093 C CA  . ILE A 1 144 ? -4.08846  -2.15915  45.01417 1.000 14.39285 ? 138 ILE A CA  1 
ATOM   1094 C C   . ILE A 1 144 ? -2.69592  -2.71774  45.28866 1.000 15.36362 ? 138 ILE A C   1 
ATOM   1095 O O   . ILE A 1 144 ? -1.90818  -2.97183  44.35970 1.000 17.00517 ? 138 ILE A O   1 
ATOM   1096 C CB  . ILE A 1 144 ? -4.18360  -0.68556  45.44925 1.000 14.33338 ? 138 ILE A CB  1 
ATOM   1097 C CG1 . ILE A 1 144 ? -5.57150  -0.09832  45.08469 1.000 15.51770 ? 138 ILE A CG1 1 
ATOM   1098 C CG2 . ILE A 1 144 ? -3.06713  0.13392   44.82292 1.000 16.23090 ? 138 ILE A CG2 1 
ATOM   1099 C CD1 . ILE A 1 144 ? -5.83567  1.28402   45.72733 1.000 17.39364 ? 138 ILE A CD1 1 
ATOM   1100 N N   . HIS A 1 145 ? -2.36189  -2.89699  46.58299 1.000 14.35159 ? 139 HIS A N   1 
ATOM   1101 C CA  . HIS A 1 145 ? -1.03434  -3.39980  46.94408 1.000 14.67605 ? 139 HIS A CA  1 
ATOM   1102 C C   . HIS A 1 145 ? -0.80933  -4.82628  46.47306 1.000 15.75929 ? 139 HIS A C   1 
ATOM   1103 O O   . HIS A 1 145 ? 0.33085   -5.18803  46.14219 1.000 18.04412 ? 139 HIS A O   1 
ATOM   1104 C CB  . HIS A 1 145 ? -0.86571  -3.30749  48.45611 1.000 14.95686 ? 139 HIS A CB  1 
ATOM   1105 C CG  . HIS A 1 145 ? -0.61904  -1.91420  48.92409 1.000 14.79827 ? 139 HIS A CG  1 
ATOM   1106 N ND1 . HIS A 1 145 ? -0.36756  -1.60420  50.25148 1.000 15.83514 ? 139 HIS A ND1 1 
ATOM   1107 C CD2 . HIS A 1 145 ? -0.54749  -0.74217  48.23946 1.000 14.44765 ? 139 HIS A CD2 1 
ATOM   1108 C CE1 . HIS A 1 145 ? -0.17228  -0.30327  50.36495 1.000 15.11245 ? 139 HIS A CE1 1 
ATOM   1109 N NE2 . HIS A 1 145 ? -0.26124  0.24352   49.15894 1.000 15.35453 ? 139 HIS A NE2 1 
ATOM   1110 N N   . SER A 1 146 ? -1.87074  -5.64102  46.39980 1.000 15.89619 ? 140 SER A N   1 
ATOM   1111 C CA  . SER A 1 146 ? -1.69846  -6.99348  45.89338 1.000 17.20319 ? 140 SER A CA  1 
ATOM   1112 C C   . SER A 1 146 ? -1.34093  -6.99820  44.39679 1.000 18.34697 ? 140 SER A C   1 
ATOM   1113 O O   . SER A 1 146 ? -0.79134  -7.98299  43.90679 1.000 20.83695 ? 140 SER A O   1 
ATOM   1114 C CB  . SER A 1 146 ? -2.95216  -7.82622  46.13094 1.000 16.50648 ? 140 SER A CB  1 
ATOM   1115 O OG  . SER A 1 146 ? -3.99528  -7.48011  45.22515 1.000 18.99417 ? 140 SER A OG  1 
ATOM   1116 N N   . ALA A 1 147 ? -1.62223  -5.91162  43.68225 1.000 18.37185 ? 141 ALA A N   1 
ATOM   1117 C CA  . ALA A 1 147 ? -1.25329  -5.75116  42.27599 1.000 19.07190 ? 141 ALA A CA  1 
ATOM   1118 C C   . ALA A 1 147 ? 0.15591   -5.17524  42.13958 1.000 20.89543 ? 141 ALA A C   1 
ATOM   1119 O O   . ALA A 1 147 ? 0.61644   -4.87662  41.01895 1.000 21.51085 ? 141 ALA A O   1 
ATOM   1120 C CB  . ALA A 1 147 ? -2.29191  -4.86956  41.55953 1.000 20.13289 ? 141 ALA A CB  1 
ATOM   1121 N N   . ASN A 1 148 ? 0.85946   -5.04037  43.26410 1.000 19.95172 ? 142 ASN A N   1 
ATOM   1122 C CA  . ASN A 1 148 ? 2.20609   -4.45486  43.30614 1.000 21.66126 ? 142 ASN A CA  1 
ATOM   1123 C C   . ASN A 1 148 ? 2.17222   -2.98075  42.89832 1.000 19.07120 ? 142 ASN A C   1 
ATOM   1124 O O   . ASN A 1 148 ? 3.15941   -2.43968  42.38879 1.000 19.92265 ? 142 ASN A O   1 
ATOM   1125 C CB  . ASN A 1 148 ? 3.20146   -5.22754  42.41528 1.000 26.10908 ? 142 ASN A CB  1 
ATOM   1126 C CG  . ASN A 1 148 ? 4.63638   -5.04632  42.86053 0.800 29.13365 ? 142 ASN A CG  1 
ATOM   1127 O OD1 . ASN A 1 148 ? 4.90386   -5.02594  44.05692 0.800 30.29058 ? 142 ASN A OD1 1 
ATOM   1128 N ND2 . ASN A 1 148 ? 5.57367   -4.95217  41.90730 0.800 30.92865 ? 142 ASN A ND2 1 
ATOM   1129 N N   . VAL A 1 149 ? 1.03427   -2.33344  43.10673 1.000 16.91068 ? 143 VAL A N   1 
ATOM   1130 C CA  . VAL A 1 149 ? 0.84771   -0.92949  42.77832 1.000 17.02877 ? 143 VAL A CA  1 
ATOM   1131 C C   . VAL A 1 149 ? 0.78587   -0.11527  44.06599 1.000 17.51503 ? 143 VAL A C   1 
ATOM   1132 O O   . VAL A 1 149 ? 0.23893   -0.57380  45.07529 1.000 17.69599 ? 143 VAL A O   1 
ATOM   1133 C CB  . VAL A 1 149 ? -0.42537  -0.73924  41.93193 1.000 19.00522 ? 143 VAL A CB  1 
ATOM   1134 C CG1 . VAL A 1 149 ? -0.75841  0.75144   41.78010 1.000 19.68691 ? 143 VAL A CG1 1 
ATOM   1135 C CG2 . VAL A 1 149 ? -0.21394  -1.41000  40.56438 1.000 20.67197 ? 143 VAL A CG2 1 
ATOM   1136 N N   . LEU A 1 150 ? 1.36083   1.08530   44.02212 1.000 16.91522 ? 144 LEU A N   1 
ATOM   1137 C CA  . LEU A 1 150 ? 1.26683   2.10230   45.06502 1.000 16.31466 ? 144 LEU A CA  1 
ATOM   1138 C C   . LEU A 1 150 ? 0.37040   3.22504   44.57254 1.000 15.81233 ? 144 LEU A C   1 
ATOM   1139 O O   . LEU A 1 150 ? 0.56374   3.71425   43.45916 1.000 17.81586 ? 144 LEU A O   1 
ATOM   1140 C CB  . LEU A 1 150 ? 2.65170   2.69045   45.38011 1.000 19.63971 ? 144 LEU A CB  1 
ATOM   1141 C CG  . LEU A 1 150 ? 3.67354   1.57636   45.52835 1.000 21.43875 ? 144 LEU A CG  1 
ATOM   1142 C CD1 . LEU A 1 150 ? 4.99461   2.22663   45.62914 1.000 22.10928 ? 144 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A 1 150 ? 3.33110   0.76345   46.77168 1.000 24.00954 ? 144 LEU A CD2 1 
ATOM   1144 N N   . HIS A 1 151 ? -0.59670  3.64831   45.39087 1.000 15.04602 ? 145 HIS A N   1 
ATOM   1145 C CA  . HIS A 1 151 ? -1.45674  4.75414   44.95792 1.000 15.61292 ? 145 HIS A CA  1 
ATOM   1146 C C   . HIS A 1 151 ? -0.70949  6.09207   44.98248 1.000 16.74556 ? 145 HIS A C   1 
ATOM   1147 O O   . HIS A 1 151 ? -0.71357  6.84794   43.98629 1.000 15.90778 ? 145 HIS A O   1 
ATOM   1148 C CB  . HIS A 1 151 ? -2.71796  4.80856   45.82781 1.000 14.75014 ? 145 HIS A CB  1 
ATOM   1149 C CG  . HIS A 1 151 ? -3.69406  5.85354   45.39747 1.000 15.68222 ? 145 HIS A CG  1 
ATOM   1150 N ND1 . HIS A 1 151 ? -3.50746  7.19920   45.64958 1.000 15.94161 ? 145 HIS A ND1 1 
ATOM   1151 C CD2 . HIS A 1 151 ? -4.89699  5.74537   44.77274 1.000 16.95028 ? 145 HIS A CD2 1 
ATOM   1152 C CE1 . HIS A 1 151 ? -4.54517  7.87715   45.18938 1.000 17.47149 ? 145 HIS A CE1 1 
ATOM   1153 N NE2 . HIS A 1 151 ? -5.39730  7.01825   44.64244 1.000 17.77807 ? 145 HIS A NE2 1 
ATOM   1154 N N   . ARG A 1 152 ? -0.06360  6.40323   46.11779 1.000 15.46534 ? 146 ARG A N   1 
ATOM   1155 C CA  . ARG A 1 152 ? 0.86842   7.52157   46.30422 1.000 16.13893 ? 146 ARG A CA  1 
ATOM   1156 C C   . ARG A 1 152 ? 0.19171   8.88415   46.38348 1.000 18.07073 ? 146 ARG A C   1 
ATOM   1157 O O   . ARG A 1 152 ? 0.88888   9.88005   46.44641 1.000 21.91973 ? 146 ARG A O   1 
ATOM   1158 C CB  . ARG A 1 152 ? 1.96933   7.55010   45.20726 1.000 17.85602 ? 146 ARG A CB  1 
ATOM   1159 C CG  . ARG A 1 152 ? 2.82451   6.26279   45.25074 1.000 20.45458 ? 146 ARG A CG  1 
ATOM   1160 C CD  . ARG A 1 152 ? 3.86860   6.10888   44.19260 0.800 23.05976 ? 146 ARG A CD  1 
ATOM   1161 N NE  . ARG A 1 152 ? 5.02087   6.95083   44.42542 0.700 30.57882 ? 146 ARG A NE  1 
ATOM   1162 C CZ  . ARG A 1 152 ? 5.34188   7.99229   43.68640 0.700 30.55058 ? 146 ARG A CZ  1 
ATOM   1163 N NH1 . ARG A 1 152 ? 4.52970   8.44827   42.76190 0.700 31.65897 ? 146 ARG A NH1 1 
ATOM   1164 N NH2 . ARG A 1 152 ? 6.51918   8.57304   43.86714 0.700 29.76492 ? 146 ARG A NH2 1 
ATOM   1165 N N   . ASP A 1 153 ? -1.15541  8.97243   46.37546 1.000 15.61365 ? 147 ASP A N   1 
ATOM   1166 C CA  . ASP A 1 153 ? -1.82299  10.24824  46.63372 1.000 19.52255 ? 147 ASP A CA  1 
ATOM   1167 C C   . ASP A 1 153 ? -3.13968  10.05074  47.36277 1.000 16.52436 ? 147 ASP A C   1 
ATOM   1168 O O   . ASP A 1 153 ? -4.15669  10.68566  47.03835 1.000 18.13046 ? 147 ASP A O   1 
ATOM   1169 C CB  . ASP A 1 153 ? -2.03404  11.05294  45.34953 1.000 20.44359 ? 147 ASP A CB  1 
ATOM   1170 C CG  . ASP A 1 153 ? -2.08097  12.56667  45.60365 1.000 22.57361 ? 147 ASP A CG  1 
ATOM   1171 O OD1 . ASP A 1 153 ? -1.72240  13.04336  46.71217 1.000 23.51846 ? 147 ASP A OD1 1 
ATOM   1172 O OD2 . ASP A 1 153 ? -2.56778  13.29093  44.70684 1.000 23.61364 ? 147 ASP A OD2 1 
ATOM   1173 N N   . LEU A 1 154 ? -3.13991  9.17871   48.36371 1.000 14.72585 ? 148 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 154 ? -4.35671  8.98643   49.13002 1.000 15.11843 ? 148 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 154 ? -4.60331  10.21473  50.00104 1.000 15.80390 ? 148 LEU A C   1 
ATOM   1176 O O   . LEU A 1 154 ? -3.70748  10.66410  50.71991 1.000 16.63284 ? 148 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 154 ? -4.26860  7.73188   49.98477 1.000 16.29492 ? 148 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 154 ? -4.21371  6.43882   49.19245 1.000 15.60849 ? 148 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 154 ? -3.85670  5.24638   50.09211 1.000 18.51215 ? 148 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 154 ? -5.51142  6.16290   48.41066 1.000 16.56375 ? 148 LEU A CD2 1 
ATOM   1181 N N   . LYS A 1 155 ? -5.83680  10.70619  49.97896 1.000 16.42478 ? 149 LYS A N   1 
ATOM   1182 C CA  . LYS A 1 155 ? -6.25609  11.87071  50.73405 1.000 16.34943 ? 149 LYS A CA  1 
ATOM   1183 C C   . LYS A 1 155 ? -7.77874  11.92909  50.65467 1.000 16.27742 ? 149 LYS A C   1 
ATOM   1184 O O   . LYS A 1 155 ? -8.36900  11.23913  49.81704 1.000 15.70594 ? 149 LYS A O   1 
ATOM   1185 C CB  . LYS A 1 155 ? -5.62416  13.16799  50.19326 1.000 16.92250 ? 149 LYS A CB  1 
ATOM   1186 C CG  . LYS A 1 155 ? -5.87782  13.45072  48.72346 1.000 19.12731 ? 149 LYS A CG  1 
ATOM   1187 C CD  . LYS A 1 155 ? -5.11257  14.68647  48.27933 1.000 23.19573 ? 149 LYS A CD  1 
ATOM   1188 C CE  . LYS A 1 155 ? -5.17981  14.84228  46.80054 1.000 24.75894 ? 149 LYS A CE  1 
ATOM   1189 N NZ  . LYS A 1 155 ? -4.59628  16.14760  46.38505 1.000 27.56298 ? 149 LYS A NZ  1 
ATOM   1190 N N   . PRO A 1 156 ? -8.43210  12.70739  51.53176 1.000 15.96722 ? 150 PRO A N   1 
ATOM   1191 C CA  . PRO A 1 156 ? -9.91841  12.70147  51.54798 1.000 17.44911 ? 150 PRO A CA  1 
ATOM   1192 C C   . PRO A 1 156 ? -10.53688 13.03483  50.20039 1.000 17.41787 ? 150 PRO A C   1 
ATOM   1193 O O   . PRO A 1 156 ? -11.57706 12.45866  49.84075 1.000 17.55370 ? 150 PRO A O   1 
ATOM   1194 C CB  . PRO A 1 156 ? -10.24971 13.73903  52.63302 1.000 18.87669 ? 150 PRO A CB  1 
ATOM   1195 C CG  . PRO A 1 156 ? -9.07494  13.66511  53.57447 1.000 18.02379 ? 150 PRO A CG  1 
ATOM   1196 C CD  . PRO A 1 156 ? -7.87700  13.51852  52.64532 1.000 16.73372 ? 150 PRO A CD  1 
ATOM   1197 N N   . SER A 1 157 ? -9.91913  13.91636  49.41156 1.000 18.99610 ? 151 SER A N   1 
ATOM   1198 C CA  . SER A 1 157 ? -10.58333 14.28683  48.17244 1.000 20.18984 ? 151 SER A CA  1 
ATOM   1199 C C   . SER A 1 157 ? -10.54970 13.16292  47.14800 1.000 17.88403 ? 151 SER A C   1 
ATOM   1200 O O   . SER A 1 157 ? -11.28310 13.23707  46.15162 1.000 20.91488 ? 151 SER A O   1 
ATOM   1201 C CB  . SER A 1 157 ? -9.97782  15.56297  47.60211 1.000 21.84950 ? 151 SER A CB  1 
ATOM   1202 O OG  . SER A 1 157 ? -8.62530  15.37718  47.18894 1.000 23.48817 ? 151 SER A OG  1 
ATOM   1203 N N   . ASN A 1 158 ? -9.71408  12.14399  47.34548 1.000 16.01664 ? 152 ASN A N   1 
ATOM   1204 C CA  . ASN A 1 158 ? -9.65843  10.99598  46.45303 1.000 16.37896 ? 152 ASN A CA  1 
ATOM   1205 C C   . ASN A 1 158 ? -10.46198 9.80884   46.97822 1.000 16.51828 ? 152 ASN A C   1 
ATOM   1206 O O   . ASN A 1 158 ? -10.30552 8.69702   46.48973 1.000 19.17930 ? 152 ASN A O   1 
ATOM   1207 C CB  . ASN A 1 158 ? -8.19572  10.61045  46.20939 1.000 17.35414 ? 152 ASN A CB  1 
ATOM   1208 C CG  . ASN A 1 158 ? -7.54664  11.53135  45.17218 1.000 19.73766 ? 152 ASN A CG  1 
ATOM   1209 O OD1 . ASN A 1 158 ? -8.25550  12.16709  44.36079 1.000 22.27350 ? 152 ASN A OD1 1 
ATOM   1210 N ND2 . ASN A 1 158 ? -6.21852  11.65086  45.21906 1.000 19.20718 ? 152 ASN A ND2 1 
ATOM   1211 N N   . LEU A 1 159 ? -11.32154 10.02789  47.97463 1.000 17.38506 ? 153 LEU A N   1 
ATOM   1212 C CA  . LEU A 1 159 ? -12.18992 8.99331   48.51828 1.000 16.21013 ? 153 LEU A CA  1 
ATOM   1213 C C   . LEU A 1 159 ? -13.63443 9.44782   48.26662 1.000 16.78932 ? 153 LEU A C   1 
ATOM   1214 O O   . LEU A 1 159 ? -14.09943 10.45097  48.84049 1.000 18.64912 ? 153 LEU A O   1 
ATOM   1215 C CB  . LEU A 1 159 ? -11.90921 8.79227   50.01621 1.000 16.14577 ? 153 LEU A CB  1 
ATOM   1216 C CG  . LEU A 1 159 ? -10.45310 8.41613   50.34866 1.000 17.00206 ? 153 LEU A CG  1 
ATOM   1217 C CD1 . LEU A 1 159 ? -10.28738 8.28716   51.85348 1.000 18.56059 ? 153 LEU A CD1 1 
ATOM   1218 C CD2 . LEU A 1 159 ? -10.05252 7.09651   49.63368 1.000 18.28637 ? 153 LEU A CD2 1 
ATOM   1219 N N   . LEU A 1 160 ? -14.34062 8.72801   47.41773 1.000 15.92795 ? 154 LEU A N   1 
ATOM   1220 C CA  . LEU A 1 160 ? -15.71178 9.07809   47.03257 1.000 17.02303 ? 154 LEU A CA  1 
ATOM   1221 C C   . LEU A 1 160 ? -16.70426 8.21806   47.79721 1.000 17.88103 ? 154 LEU A C   1 
ATOM   1222 O O   . LEU A 1 160 ? -16.43956 7.04161   48.06645 1.000 19.01024 ? 154 LEU A O   1 
ATOM   1223 C CB  . LEU A 1 160 ? -15.91555 8.85290   45.53349 1.000 18.85162 ? 154 LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 160 ? -14.85277 9.47759   44.62179 1.000 19.79876 ? 154 LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 160 ? -15.10922 9.18259   43.13918 1.000 21.86437 ? 154 LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 160 ? -14.75056 10.96766  44.86656 1.000 22.71606 ? 154 LEU A CD2 1 
ATOM   1227 N N   . LEU A 1 161 ? -17.88196 8.78587   48.07921 1.000 20.27709 ? 155 LEU A N   1 
ATOM   1228 C CA  . LEU A 1 161 ? -18.91507 8.08917   48.83562 1.000 21.03700 ? 155 LEU A CA  1 
ATOM   1229 C C   . LEU A 1 161 ? -20.21633 8.17389   48.05318 1.000 23.30806 ? 155 LEU A C   1 
ATOM   1230 O O   . LEU A 1 161 ? -20.55326 9.24287   47.55011 1.000 22.62665 ? 155 LEU A O   1 
ATOM   1231 C CB  . LEU A 1 161 ? -19.10427 8.73305   50.22409 1.000 21.93335 ? 155 LEU A CB  1 
ATOM   1232 C CG  . LEU A 1 161 ? -17.80661 8.65894   51.02815 1.000 26.33560 ? 155 LEU A CG  1 
ATOM   1233 C CD1 . LEU A 1 161 ? -17.70464 9.80460   51.96616 1.000 33.56153 ? 155 LEU A CD1 1 
ATOM   1234 C CD2 . LEU A 1 161 ? -17.68833 7.29598   51.70734 1.000 27.10762 ? 155 LEU A CD2 1 
ATOM   1235 N N   . ASN A 1 162 ? -20.95129 7.05878   47.96047 1.000 23.60592 ? 156 ASN A N   1 
ATOM   1236 C CA  . ASN A 1 162 ? -22.28125 7.13276   47.37000 1.000 22.76997 ? 156 ASN A CA  1 
ATOM   1237 C C   . ASN A 1 162 ? -23.30613 7.38542   48.47927 1.000 22.90030 ? 156 ASN A C   1 
ATOM   1238 O O   . ASN A 1 162 ? -22.95347 7.64681   49.63430 1.000 23.67806 ? 156 ASN A O   1 
ATOM   1239 C CB  . ASN A 1 162 ? -22.59019 5.88332   46.54192 1.000 24.74727 ? 156 ASN A CB  1 
ATOM   1240 C CG  . ASN A 1 162 ? -22.75729 4.63670   47.36771 1.000 27.48526 ? 156 ASN A CG  1 
ATOM   1241 O OD1 . ASN A 1 162 ? -22.81998 4.68344   48.57901 1.000 25.85146 ? 156 ASN A OD1 1 
ATOM   1242 N ND2 . ASN A 1 162 ? -22.91589 3.50534   46.68641 1.000 32.50926 ? 156 ASN A ND2 1 
ATOM   1243 N N   . THR A 1 163 ? -24.59797 7.31885   48.12909 1.000 25.30755 ? 157 THR A N   1 
ATOM   1244 C CA  . THR A 1 163 ? -25.62954 7.74211   49.06286 1.000 26.57639 ? 157 THR A CA  1 
ATOM   1245 C C   . THR A 1 163 ? -25.80801 6.79613   50.24689 1.000 28.33954 ? 157 THR A C   1 
ATOM   1246 O O   . THR A 1 163 ? -26.38475 7.20003   51.26923 1.000 27.04165 ? 157 THR A O   1 
ATOM   1247 C CB  A THR A 1 163 ? -26.97442 7.87455   48.35346 0.460 30.26429 ? 157 THR A CB  1 
ATOM   1248 C CB  B THR A 1 163 ? -26.95691 7.92666   48.31759 0.540 28.18658 ? 157 THR A CB  1 
ATOM   1249 O OG1 A THR A 1 163 ? -26.84284 8.67757   47.17704 0.460 30.56937 ? 157 THR A OG1 1 
ATOM   1250 O OG1 B THR A 1 163 ? -27.75022 8.88235   49.01978 0.540 31.75279 ? 157 THR A OG1 1 
ATOM   1251 C CG2 A THR A 1 163 ? -27.89933 8.49909   49.25523 0.460 32.65214 ? 157 THR A CG2 1 
ATOM   1252 C CG2 B THR A 1 163 ? -27.69430 6.62876   48.22108 0.540 24.85859 ? 157 THR A CG2 1 
ATOM   1253 N N   . THR A 1 164 ? -25.32837 5.56803   50.13760 1.000 27.81848 ? 158 THR A N   1 
ATOM   1254 C CA  . THR A 1 164 ? -25.37851 4.62677   51.22577 1.000 28.59382 ? 158 THR A CA  1 
ATOM   1255 C C   . THR A 1 164 ? -23.98959 4.43678   51.82546 1.000 27.09955 ? 158 THR A C   1 
ATOM   1256 O O   . THR A 1 164 ? -23.72960 3.42931   52.46662 1.000 29.53639 ? 158 THR A O   1 
ATOM   1257 C CB  . THR A 1 164 ? -25.95766 3.28873   50.74397 1.000 31.26404 ? 158 THR A CB  1 
ATOM   1258 O OG1 . THR A 1 164 ? -25.29293 2.90090   49.53423 1.000 31.62585 ? 158 THR A OG1 1 
ATOM   1259 C CG2 . THR A 1 164 ? -27.45172 3.46303   50.46885 1.000 33.94751 ? 158 THR A CG2 1 
HETATM 1260 N N   . CME A 1 165 ? -23.10724 5.40808   51.58249 1.000 25.12525 ? 159 CME A N   1 
HETATM 1261 C CA  . CME A 1 165 ? -21.78758 5.45774   52.20487 1.000 25.29126 ? 159 CME A CA  1 
HETATM 1262 C CB  . CME A 1 165 ? -21.90420 5.49522   53.74724 1.000 30.36933 ? 159 CME A CB  1 
HETATM 1263 S SG  . CME A 1 165 ? -22.66827 6.95158   54.44326 0.800 32.79431 ? 159 CME A SG  1 
HETATM 1264 S SD  . CME A 1 165 ? -21.59329 8.68172   53.83097 0.700 35.90826 ? 159 CME A SD  1 
HETATM 1265 C CE  . CME A 1 165 ? -22.30474 9.29963   52.34275 0.700 34.96992 ? 159 CME A CE  1 
HETATM 1266 C CZ  . CME A 1 165 ? -23.71637 9.78326   52.53389 0.700 34.92678 ? 159 CME A CZ  1 
HETATM 1267 O OH  . CME A 1 165 ? -23.65409 10.74942  53.57804 0.700 34.18289 ? 159 CME A OH  1 
HETATM 1268 C C   . CME A 1 165 ? -20.84454 4.31241   51.80409 1.000 22.62786 ? 159 CME A C   1 
HETATM 1269 O O   . CME A 1 165 ? -19.87418 3.94759   52.52661 1.000 22.67709 ? 159 CME A O   1 
ATOM   1270 N N   . ASP A 1 166 ? -21.09318 3.74494   50.61756 1.000 23.56817 ? 160 ASP A N   1 
ATOM   1271 C CA  . ASP A 1 166 ? -20.08448 2.89261   49.97191 1.000 24.29827 ? 160 ASP A CA  1 
ATOM   1272 C C   . ASP A 1 166 ? -18.95980 3.79120   49.48376 1.000 20.43191 ? 160 ASP A C   1 
ATOM   1273 O O   . ASP A 1 166 ? -19.22304 4.86623   48.92018 1.000 20.81944 ? 160 ASP A O   1 
ATOM   1274 C CB  . ASP A 1 166 ? -20.70137 2.08946   48.81543 0.700 26.71173 ? 160 ASP A CB  1 
ATOM   1275 C CG  . ASP A 1 166 ? -21.82334 1.21233   49.28297 0.700 29.79560 ? 160 ASP A CG  1 
ATOM   1276 O OD1 . ASP A 1 166 ? -21.56364 0.28354   50.05405 0.700 32.32352 ? 160 ASP A OD1 1 
ATOM   1277 O OD2 . ASP A 1 166 ? -22.97101 1.43192   48.87164 0.700 33.28538 ? 160 ASP A OD2 1 
ATOM   1278 N N   . LEU A 1 167 ? -17.71060 3.36091   49.72860 1.000 16.98937 ? 161 LEU A N   1 
ATOM   1279 C CA  . LEU A 1 167 ? -16.52259 4.17290   49.50757 1.000 16.58414 ? 161 LEU A CA  1 
ATOM   1280 C C   . LEU A 1 167 ? -15.70960 3.62913   48.33732 1.000 17.55756 ? 161 LEU A C   1 
ATOM   1281 O O   . LEU A 1 167 ? -15.50768 2.41099   48.21436 1.000 19.23070 ? 161 LEU A O   1 
ATOM   1282 C CB  . LEU A 1 167 ? -15.66797 4.20752   50.78545 1.000 17.76792 ? 161 LEU A CB  1 
ATOM   1283 C CG  . LEU A 1 167 ? -14.38660 5.04984   50.78159 1.000 18.39981 ? 161 LEU A CG  1 
ATOM   1284 C CD1 . LEU A 1 167 ? -14.10608 5.57790   52.22028 1.000 19.09668 ? 161 LEU A CD1 1 
ATOM   1285 C CD2 . LEU A 1 167 ? -13.15947 4.27780   50.23193 1.000 19.89496 ? 161 LEU A CD2 1 
ATOM   1286 N N   . LYS A 1 168 ? -15.24583 4.52920   47.47132 1.000 15.64182 ? 162 LYS A N   1 
ATOM   1287 C CA  . LYS A 1 168 ? -14.37986 4.13913   46.35578 1.000 15.56137 ? 162 LYS A CA  1 
ATOM   1288 C C   . LYS A 1 168 ? -13.17431 5.06429   46.25454 1.000 16.07655 ? 162 LYS A C   1 
ATOM   1289 O O   . LYS A 1 168 ? -13.29425 6.29043   46.39662 1.000 18.10841 ? 162 LYS A O   1 
ATOM   1290 C CB  . LYS A 1 168 ? -15.12477 4.15577   45.00693 1.000 18.06687 ? 162 LYS A CB  1 
ATOM   1291 C CG  . LYS A 1 168 ? -16.27529 3.11859   44.94869 1.000 21.38821 ? 162 LYS A CG  1 
ATOM   1292 C CD  . LYS A 1 168 ? -16.97846 3.18328   43.59798 1.000 23.69382 ? 162 LYS A CD  1 
ATOM   1293 C CE  . LYS A 1 168 ? -18.28172 2.44185   43.60842 1.000 28.12975 ? 162 LYS A CE  1 
ATOM   1294 N NZ  . LYS A 1 168 ? -18.11599 0.98259   43.58975 1.000 30.45413 ? 162 LYS A NZ  1 
ATOM   1295 N N   . ILE A 1 169 ? -12.01633 4.46333   45.97398 1.000 15.07304 ? 163 ILE A N   1 
ATOM   1296 C CA  . ILE A 1 169 ? -10.75633 5.19146   45.82844 1.000 16.76751 ? 163 ILE A CA  1 
ATOM   1297 C C   . ILE A 1 169 ? -10.64001 5.68981   44.39313 1.000 16.64031 ? 163 ILE A C   1 
ATOM   1298 O O   . ILE A 1 169 ? -10.82740 4.92320   43.43332 1.000 17.88504 ? 163 ILE A O   1 
ATOM   1299 C CB  . ILE A 1 169 ? -9.57281  4.28510   46.19119 1.000 15.16152 ? 163 ILE A CB  1 
ATOM   1300 C CG1 . ILE A 1 169 ? -9.66501  3.83600   47.67072 1.000 15.44335 ? 163 ILE A CG1 1 
ATOM   1301 C CG2 . ILE A 1 169 ? -8.22294  4.99523   45.90468 1.000 15.27955 ? 163 ILE A CG2 1 
ATOM   1302 C CD1 . ILE A 1 169 ? -8.76705  2.68465   48.00290 1.000 17.45499 ? 163 ILE A CD1 1 
ATOM   1303 N N   . CYS A 1 170 ? -10.28616 6.94929   44.24219 1.000 16.62062 ? 164 CYS A N   1 
ATOM   1304 C CA  A CYS A 1 170 ? -10.17004 7.62147   42.95474 0.900 17.83407 ? 164 CYS A CA  1 
ATOM   1305 C CA  B CYS A 1 170 ? -10.12285 7.49526   42.91908 0.100 17.50598 ? 164 CYS A CA  1 
ATOM   1306 C C   . CYS A 1 170 ? -8.72945  8.08638   42.72197 1.000 17.16692 ? 164 CYS A C   1 
ATOM   1307 O O   . CYS A 1 170 ? -7.93197  8.20543   43.64951 1.000 17.73660 ? 164 CYS A O   1 
ATOM   1308 C CB  A CYS A 1 170 ? -11.14978 8.81980   42.88677 0.900 19.61943 ? 164 CYS A CB  1 
ATOM   1309 C CB  B CYS A 1 170 ? -11.23224 8.49744   42.69412 0.100 18.57376 ? 164 CYS A CB  1 
ATOM   1310 S SG  A CYS A 1 170 ? -11.57636 9.34780   41.20406 0.900 21.94609 ? 164 CYS A SG  1 
ATOM   1311 S SG  B CYS A 1 170 ? -10.94736 9.89613   43.71430 0.100 19.23685 ? 164 CYS A SG  1 
ATOM   1312 N N   . ASP A 1 171 ? -8.42782  8.35877   41.44953 1.000 19.05495 ? 165 ASP A N   1 
ATOM   1313 C CA  . ASP A 1 171 ? -7.23851  9.02025   40.90787 1.000 21.66168 ? 165 ASP A CA  1 
ATOM   1314 C C   . ASP A 1 171 ? -5.95037  8.22035   41.05131 1.000 23.85934 ? 165 ASP A C   1 
ATOM   1315 O O   . ASP A 1 171 ? -5.24434  8.29494   42.06542 1.000 26.01788 ? 165 ASP A O   1 
ATOM   1316 C CB  . ASP A 1 171 ? -7.04306  10.40585  41.50643 1.000 23.63262 ? 165 ASP A CB  1 
ATOM   1317 C CG  . ASP A 1 171 ? -5.94776  11.19883  40.76213 0.800 25.82903 ? 165 ASP A CG  1 
ATOM   1318 O OD1 . ASP A 1 171 ? -5.33818  10.68147  39.77649 0.600 24.37898 ? 165 ASP A OD1 1 
ATOM   1319 O OD2 . ASP A 1 171 ? -5.77261  12.38002  41.09223 0.600 27.56981 ? 165 ASP A OD2 1 
ATOM   1320 N N   . PHE A 1 172 ? -5.60192  7.49848   40.00426 1.000 22.52926 ? 166 PHE A N   1 
ATOM   1321 C CA  . PHE A 1 172 ? -4.33993  6.77381   39.98814 1.000 23.11789 ? 166 PHE A CA  1 
ATOM   1322 C C   . PHE A 1 172 ? -3.27979  7.46745   39.13892 1.000 24.08578 ? 166 PHE A C   1 
ATOM   1323 O O   . PHE A 1 172 ? -2.33440  6.81695   38.69270 1.000 25.02959 ? 166 PHE A O   1 
ATOM   1324 C CB  . PHE A 1 172 ? -4.58854  5.32861   39.54805 1.000 22.98906 ? 166 PHE A CB  1 
ATOM   1325 C CG  . PHE A 1 172 ? -5.26451  4.48906   40.62740 1.000 20.37042 ? 166 PHE A CG  1 
ATOM   1326 C CD1 . PHE A 1 172 ? -6.62356  4.62511   40.89074 1.000 21.78163 ? 166 PHE A CD1 1 
ATOM   1327 C CD2 . PHE A 1 172 ? -4.52764  3.59411   41.39814 1.000 21.31162 ? 166 PHE A CD2 1 
ATOM   1328 C CE1 . PHE A 1 172 ? -7.23128  3.90201   41.93748 1.000 23.08329 ? 166 PHE A CE1 1 
ATOM   1329 C CE2 . PHE A 1 172 ? -5.12514  2.85397   42.41322 1.000 20.88706 ? 166 PHE A CE2 1 
ATOM   1330 C CZ  . PHE A 1 172 ? -6.48805  2.98282   42.67305 1.000 21.30695 ? 166 PHE A CZ  1 
ATOM   1331 N N   . GLY A 1 173 ? -3.40849  8.77714   38.90883 1.000 23.20754 ? 167 GLY A N   1 
ATOM   1332 C CA  . GLY A 1 173 ? -2.43941  9.43419   38.05181 1.000 23.38780 ? 167 GLY A CA  1 
ATOM   1333 C C   . GLY A 1 173 ? -1.04387  9.54201   38.64472 1.000 23.15561 ? 167 GLY A C   1 
ATOM   1334 O O   . GLY A 1 173 ? -0.09259  9.82706   37.90976 1.000 25.21093 ? 167 GLY A O   1 
ATOM   1335 N N   . LEU A 1 174 ? -0.90357  9.34750   39.95379 1.000 22.55378 ? 168 LEU A N   1 
ATOM   1336 C CA  . LEU A 1 174 ? 0.39596   9.41148   40.60379 1.000 24.28570 ? 168 LEU A CA  1 
ATOM   1337 C C   . LEU A 1 174 ? 0.89467   8.02156   40.98585 1.000 22.62665 ? 168 LEU A C   1 
ATOM   1338 O O   . LEU A 1 174 ? 1.95561   7.89207   41.60978 1.000 23.46738 ? 168 LEU A O   1 
ATOM   1339 C CB  . LEU A 1 174 ? 0.30410   10.29685  41.85140 1.000 30.92500 ? 168 LEU A CB  1 
ATOM   1340 C CG  . LEU A 1 174 ? 0.60492   11.79320  41.69906 1.000 38.48119 ? 168 LEU A CG  1 
ATOM   1341 C CD1 . LEU A 1 174 ? 0.95383   12.39235  43.05527 1.000 41.67117 ? 168 LEU A CD1 1 
ATOM   1342 C CD2 . LEU A 1 174 ? 1.66148   12.13166  40.65113 1.000 41.33862 ? 168 LEU A CD2 1 
ATOM   1343 N N   . ALA A 1 175 ? 0.17106   6.97754   40.60195 1.000 18.99239 ? 169 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 175 ? 0.49841   5.62687   41.01497 1.000 18.85388 ? 169 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 175 ? 1.77657   5.13900   40.33570 1.000 21.39584 ? 169 ALA A C   1 
ATOM   1346 O O   . ALA A 1 175 ? 2.14028   5.59497   39.24691 1.000 25.21063 ? 169 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 175 ? -0.66145  4.68527   40.69394 1.000 20.72091 ? 169 ALA A CB  1 
ATOM   1348 N N   . ARG A 1 176 ? 2.44870   4.19330   40.98878 1.000 19.72053 ? 170 ARG A N   1 
ATOM   1349 C CA  . ARG A 1 176 ? 3.63717   3.54973   40.45850 1.000 19.77741 ? 170 ARG A CA  1 
ATOM   1350 C C   . ARG A 1 176 ? 3.62762   2.07930   40.84241 1.000 19.01734 ? 170 ARG A C   1 
ATOM   1351 O O   . ARG A 1 176 ? 2.95660   1.66503   41.79527 1.000 19.85144 ? 170 ARG A O   1 
ATOM   1352 C CB  . ARG A 1 176 ? 4.94295   4.15637   41.01621 1.000 22.48554 ? 170 ARG A CB  1 
ATOM   1353 C CG  . ARG A 1 176 ? 5.17971   5.63631   40.71273 0.900 25.94956 ? 170 ARG A CG  1 
ATOM   1354 C CD  . ARG A 1 176 ? 5.57086   5.90107   39.27121 0.800 29.05911 ? 170 ARG A CD  1 
ATOM   1355 N NE  . ARG A 1 176 ? 6.12430   7.24465   39.10054 0.800 31.06672 ? 170 ARG A NE  1 
ATOM   1356 C CZ  . ARG A 1 176 ? 5.39856   8.35556   39.06065 0.700 28.92922 ? 170 ARG A CZ  1 
ATOM   1357 N NH1 . ARG A 1 176 ? 4.07362   8.32195   39.13067 0.600 26.19601 ? 170 ARG A NH1 1 
ATOM   1358 N NH2 . ARG A 1 176 ? 6.01372   9.52683   38.94029 0.500 29.46844 ? 170 ARG A NH2 1 
ATOM   1359 N N   . VAL A 1 177 ? 4.43582   1.29924   40.12693 1.000 20.85944 ? 171 VAL A N   1 
ATOM   1360 C CA  . VAL A 1 177 ? 4.71796   -0.07297  40.53745 1.000 21.28693 ? 171 VAL A CA  1 
ATOM   1361 C C   . VAL A 1 177 ? 5.72561   -0.04500  41.68874 1.000 22.59796 ? 171 VAL A C   1 
ATOM   1362 O O   . VAL A 1 177 ? 6.72656   0.68226   41.63501 1.000 24.45347 ? 171 VAL A O   1 
ATOM   1363 C CB  . VAL A 1 177 ? 5.23781   -0.90315  39.35332 1.000 23.87685 ? 171 VAL A CB  1 
ATOM   1364 C CG1 . VAL A 1 177 ? 5.62626   -2.29818  39.83902 1.000 26.25882 ? 171 VAL A CG1 1 
ATOM   1365 C CG2 . VAL A 1 177 ? 4.14623   -1.02522  38.27178 1.000 26.37406 ? 171 VAL A CG2 1 
ATOM   1366 N N   . ALA A 1 178 ? 5.46001   -0.82227  42.73953 1.000 21.52476 ? 172 ALA A N   1 
ATOM   1367 C CA  . ALA A 1 178 ? 6.33498   -0.82210  43.90846 1.000 22.92401 ? 172 ALA A CA  1 
ATOM   1368 C C   . ALA A 1 178 ? 7.74960   -1.24330  43.52021 1.000 23.36886 ? 172 ALA A C   1 
ATOM   1369 O O   . ALA A 1 178 ? 7.93949   -2.12495  42.68037 1.000 25.14202 ? 172 ALA A O   1 
ATOM   1370 C CB  . ALA A 1 178 ? 5.78355   -1.77371  44.96539 1.000 24.99149 ? 172 ALA A CB  1 
ATOM   1371 N N   . ASP A 1 179 ? 8.75224   -0.61948  44.14570 1.000 25.05673 ? 173 ASP A N   1 
ATOM   1372 C CA  . ASP A 1 179 ? 10.15571  -0.87104  43.81344 1.000 26.04833 ? 173 ASP A CA  1 
ATOM   1373 C C   . ASP A 1 179 ? 11.00536  -0.63720  45.05676 1.000 28.09914 ? 173 ASP A C   1 
ATOM   1374 O O   . ASP A 1 179 ? 11.78755  0.31670   45.12850 1.000 28.01816 ? 173 ASP A O   1 
ATOM   1375 C CB  . ASP A 1 179 ? 10.58856  0.02436   42.65245 1.000 31.18866 ? 173 ASP A CB  1 
ATOM   1376 C CG  . ASP A 1 179 ? 11.98715  -0.30384  42.12513 1.000 36.99733 ? 173 ASP A CG  1 
ATOM   1377 O OD1 . ASP A 1 179 ? 12.61548  -1.30476  42.56154 1.000 38.30618 ? 173 ASP A OD1 1 
ATOM   1378 O OD2 . ASP A 1 179 ? 12.44946  0.45960   41.25208 1.000 39.29474 ? 173 ASP A OD2 1 
ATOM   1379 N N   . PRO A 1 180 ? 10.89281  -1.51941  46.05628 1.000 29.44969 ? 174 PRO A N   1 
ATOM   1380 C CA  . PRO A 1 180 ? 11.57382  -1.25987  47.33607 1.000 31.65474 ? 174 PRO A CA  1 
ATOM   1381 C C   . PRO A 1 180 ? 13.08762  -1.26064  47.24241 1.000 34.41885 ? 174 PRO A C   1 
ATOM   1382 O O   . PRO A 1 180 ? 13.73240  -0.54774  48.02892 1.000 34.32755 ? 174 PRO A O   1 
ATOM   1383 C CB  . PRO A 1 180 ? 11.06061  -2.39004  48.24584 1.000 32.23412 ? 174 PRO A CB  1 
ATOM   1384 C CG  . PRO A 1 180 ? 10.49872  -3.43431  47.32043 1.000 32.49090 ? 174 PRO A CG  1 
ATOM   1385 C CD  . PRO A 1 180 ? 9.98769   -2.68682  46.12631 1.000 31.59614 ? 174 PRO A CD  1 
ATOM   1386 N N   . ASP A 1 181 ? 13.66972  -2.01531  46.29880 1.000 36.15266 ? 175 ASP A N   1 
ATOM   1387 C CA  . ASP A 1 181 ? 15.12754  -2.05939  46.13855 1.000 36.02969 ? 175 ASP A CA  1 
ATOM   1388 C C   . ASP A 1 181 ? 15.70415  -0.74844  45.62207 1.000 35.94434 ? 175 ASP A C   1 
ATOM   1389 O O   . ASP A 1 181 ? 16.92304  -0.53894  45.68842 1.000 38.19940 ? 175 ASP A O   1 
ATOM   1390 C CB  . ASP A 1 181 ? 15.54250  -3.18077  45.17430 0.800 38.88835 ? 175 ASP A CB  1 
ATOM   1391 C CG  . ASP A 1 181 ? 15.22224  -4.55991  45.70135 0.800 42.49259 ? 175 ASP A CG  1 
ATOM   1392 O OD1 . ASP A 1 181 ? 15.16124  -4.74401  46.93455 0.700 43.01203 ? 175 ASP A OD1 1 
ATOM   1393 O OD2 . ASP A 1 181 ? 15.08278  -5.48058  44.87168 0.700 45.85869 ? 175 ASP A OD2 1 
ATOM   1394 N N   . HIS A 1 182 ? 14.87605  0.12933   45.07772 1.000 33.09001 ? 176 HIS A N   1 
ATOM   1395 C CA  . HIS A 1 182 ? 15.35812  1.38788   44.52962 1.000 31.98924 ? 176 HIS A CA  1 
ATOM   1396 C C   . HIS A 1 182 ? 14.77394  2.57819   45.28999 1.000 31.23813 ? 176 HIS A C   1 
ATOM   1397 O O   . HIS A 1 182 ? 14.70630  3.68871   44.74595 1.000 33.10801 ? 176 HIS A O   1 
ATOM   1398 C CB  . HIS A 1 182 ? 14.99665  1.46609   43.05184 0.800 33.14719 ? 176 HIS A CB  1 
ATOM   1399 C CG  . HIS A 1 182 ? 15.84502  0.61028   42.17386 0.600 36.30802 ? 176 HIS A CG  1 
ATOM   1400 N ND1 . HIS A 1 182 ? 15.32180  -0.07677  41.10070 0.600 38.93401 ? 176 HIS A ND1 1 
ATOM   1401 C CD2 . HIS A 1 182 ? 17.17350  0.34823   42.18067 0.600 38.80138 ? 176 HIS A CD2 1 
ATOM   1402 C CE1 . HIS A 1 182 ? 16.28943  -0.74005  40.49403 0.600 40.01989 ? 176 HIS A CE1 1 
ATOM   1403 N NE2 . HIS A 1 182 ? 17.42125  -0.50134  41.13051 0.600 40.24733 ? 176 HIS A NE2 1 
ATOM   1404 N N   . ASP A 1 183 ? 14.33719  2.37351   46.54111 1.000 27.25203 ? 177 ASP A N   1 
ATOM   1405 C CA  . ASP A 1 183 ? 13.59216  3.41125   47.25869 1.000 26.21591 ? 177 ASP A CA  1 
ATOM   1406 C C   . ASP A 1 183 ? 14.48682  4.47773   47.90260 1.000 25.95244 ? 177 ASP A C   1 
ATOM   1407 O O   . ASP A 1 183 ? 14.01760  5.58774   48.18692 1.000 25.78874 ? 177 ASP A O   1 
ATOM   1408 C CB  . ASP A 1 183 ? 12.72167  2.76070   48.34586 1.000 25.89584 ? 177 ASP A CB  1 
ATOM   1409 C CG  . ASP A 1 183 ? 11.81650  3.75269   49.02292 1.000 28.51663 ? 177 ASP A CG  1 
ATOM   1410 O OD1 . ASP A 1 183 ? 10.97058  4.32821   48.31506 1.000 29.43886 ? 177 ASP A OD1 1 
ATOM   1411 O OD2 . ASP A 1 183 ? 11.97661  4.00389   50.23978 1.000 29.89131 ? 177 ASP A OD2 1 
ATOM   1412 N N   . HIS A 1 184 ? 15.76124  4.17984   48.13910 1.000 25.83764 ? 178 HIS A N   1 
ATOM   1413 C CA  A HIS A 1 184 ? 16.59159  5.10199   48.90808 0.500 25.32177 ? 178 HIS A CA  1 
ATOM   1414 C CA  B HIS A 1 184 ? 16.63427  5.07186   48.89051 0.500 25.39104 ? 178 HIS A CA  1 
ATOM   1415 C C   . HIS A 1 184 ? 17.05997  6.28723   48.07594 1.000 24.88650 ? 178 HIS A C   1 
ATOM   1416 O O   . HIS A 1 184 ? 17.48309  6.14811   46.91244 1.000 29.09725 ? 178 HIS A O   1 
ATOM   1417 C CB  A HIS A 1 184 ? 17.82334  4.40566   49.49874 0.500 28.74968 ? 178 HIS A CB  1 
ATOM   1418 C CB  B HIS A 1 184 ? 17.87234  4.28958   49.27567 0.500 28.87512 ? 178 HIS A CB  1 
ATOM   1419 C CG  A HIS A 1 184 ? 17.51955  3.30410   50.47253 0.500 34.06938 ? 178 HIS A CG  1 
ATOM   1420 C CG  B HIS A 1 184 ? 18.41656  3.48065   48.13475 0.500 34.28952 ? 178 HIS A CG  1 
ATOM   1421 N ND1 A HIS A 1 184 ? 16.99984  3.54274   51.72827 0.500 36.87212 ? 178 HIS A ND1 1 
ATOM   1422 N ND1 B HIS A 1 184 ? 17.80506  2.32860   47.67770 0.500 36.60315 ? 178 HIS A ND1 1 
ATOM   1423 C CD2 A HIS A 1 184 ? 17.65595  1.96055   50.37281 0.500 36.82390 ? 178 HIS A CD2 1 
ATOM   1424 C CD2 B HIS A 1 184 ? 19.49213  3.67704   47.33496 0.500 37.17692 ? 178 HIS A CD2 1 
ATOM   1425 C CE1 A HIS A 1 184 ? 16.85123  2.39647   52.36656 0.500 38.18588 ? 178 HIS A CE1 1 
ATOM   1426 C CE1 B HIS A 1 184 ? 18.49186  1.84346   46.66066 0.500 38.41111 ? 178 HIS A CE1 1 
ATOM   1427 N NE2 A HIS A 1 184 ? 17.23390  1.42055   51.56328 0.500 38.36396 ? 178 HIS A NE2 1 
ATOM   1428 N NE2 B HIS A 1 184 ? 19.52545  2.63763   46.43542 0.500 38.36939 ? 178 HIS A NE2 1 
ATOM   1429 N N   . THR A 1 185 ? 17.06239  7.45169   48.72136 1.000 24.26815 ? 179 THR A N   1 
ATOM   1430 C CA  . THR A 1 185 ? 17.47796  8.69822   48.10392 1.000 22.49967 ? 179 THR A CA  1 
ATOM   1431 C C   . THR A 1 185 ? 18.00475  9.61640   49.20261 1.000 22.48329 ? 179 THR A C   1 
ATOM   1432 O O   . THR A 1 185 ? 18.04998  9.25183   50.39397 1.000 22.84246 ? 179 THR A O   1 
ATOM   1433 C CB  . THR A 1 185 ? 16.31981  9.34778   47.30394 1.000 24.08501 ? 179 THR A CB  1 
ATOM   1434 O OG1 . THR A 1 185 ? 16.83016  10.45499  46.53582 1.000 28.17141 ? 179 THR A OG1 1 
ATOM   1435 C CG2 . THR A 1 185 ? 15.16435  9.85065   48.25368 1.000 24.57121 ? 179 THR A CG2 1 
ATOM   1436 N N   . GLY A 1 186 ? 18.43053  10.80273  48.78798 1.000 24.12745 ? 180 GLY A N   1 
ATOM   1437 C CA  . GLY A 1 186 ? 19.04179  11.75408  49.67799 1.000 25.09032 ? 180 GLY A CA  1 
ATOM   1438 C C   . GLY A 1 186 ? 18.01850  12.57916  50.43530 1.000 24.96446 ? 180 GLY A C   1 
ATOM   1439 O O   . GLY A 1 186 ? 16.80572  12.52114  50.22377 1.000 26.55213 ? 180 GLY A O   1 
ATOM   1440 N N   . PHE A 1 187 ? 18.55128  13.37984  51.32788 1.000 24.12466 ? 181 PHE A N   1 
ATOM   1441 C CA  . PHE A 1 187 ? 17.76631  14.20906  52.23392 1.000 23.10724 ? 181 PHE A CA  1 
ATOM   1442 C C   . PHE A 1 187 ? 17.17240  15.41430  51.49988 1.000 22.44115 ? 181 PHE A C   1 
ATOM   1443 O O   . PHE A 1 187 ? 17.87614  16.09992  50.75124 1.000 27.59002 ? 181 PHE A O   1 
ATOM   1444 C CB  . PHE A 1 187 ? 18.72928  14.63532  53.34596 1.000 21.38348 ? 181 PHE A CB  1 
ATOM   1445 C CG  . PHE A 1 187 ? 18.17246  15.58538  54.39194 1.000 21.27950 ? 181 PHE A CG  1 
ATOM   1446 C CD1 . PHE A 1 187 ? 16.98898  15.34003  55.07443 1.000 20.60964 ? 181 PHE A CD1 1 
ATOM   1447 C CD2 . PHE A 1 187 ? 18.90495  16.73006  54.72075 1.000 23.74777 ? 181 PHE A CD2 1 
ATOM   1448 C CE1 . PHE A 1 187 ? 16.55117  16.23111  56.07714 1.000 22.76078 ? 181 PHE A CE1 1 
ATOM   1449 C CE2 . PHE A 1 187 ? 18.45732  17.62849  55.68499 1.000 22.89868 ? 181 PHE A CE2 1 
ATOM   1450 C CZ  . PHE A 1 187 ? 17.27997  17.37546  56.37107 1.000 22.11387 ? 181 PHE A CZ  1 
ATOM   1451 N N   . LEU A 1 188 ? 15.87159  15.66219  51.71888 1.000 22.83385 ? 182 LEU A N   1 
ATOM   1452 C CA  . LEU A 1 188 ? 15.15171  16.83569  51.21110 1.000 26.67526 ? 182 LEU A CA  1 
ATOM   1453 C C   . LEU A 1 188 ? 15.04546  16.82490  49.68257 1.000 30.00879 ? 182 LEU A C   1 
ATOM   1454 O O   . LEU A 1 188 ? 15.13805  17.87437  49.02670 1.000 31.95841 ? 182 LEU A O   1 
ATOM   1455 C CB  . LEU A 1 188 ? 15.77997  18.14795  51.72037 1.000 30.39531 ? 182 LEU A CB  1 
ATOM   1456 C CG  . LEU A 1 188 ? 15.67351  18.37723  53.24947 1.000 32.45621 ? 182 LEU A CG  1 
ATOM   1457 C CD1 . LEU A 1 188 ? 16.10606  19.77108  53.70869 1.000 35.06493 ? 182 LEU A CD1 1 
ATOM   1458 C CD2 . LEU A 1 188 ? 14.28240  18.03539  53.79257 1.000 36.49607 ? 182 LEU A CD2 1 
ATOM   1459 N N   A THR A 1 189 ? 14.85734  15.62797  49.12085 0.400 27.48770 ? 183 THR A N   1 
ATOM   1460 N N   B THR A 1 189 ? 14.82581  15.65924  49.08098 0.600 29.38562 ? 183 THR A N   1 
ATOM   1461 C CA  A THR A 1 189 ? 14.64916  15.48592  47.68468 0.400 25.20849 ? 183 THR A CA  1 
ATOM   1462 C CA  B THR A 1 189 ? 14.75934  15.66618  47.62176 0.600 29.40546 ? 183 THR A CA  1 
ATOM   1463 C C   A THR A 1 189 ? 13.19748  15.77840  47.35512 0.400 21.84844 ? 183 THR A C   1 
ATOM   1464 C C   B THR A 1 189 ? 13.40328  15.27613  47.05290 0.600 31.16396 ? 183 THR A C   1 
ATOM   1465 O O   A THR A 1 189 ? 12.29082  15.39182  48.10036 0.400 21.40494 ? 183 THR A O   1 
ATOM   1466 O O   B THR A 1 189 ? 13.09598  15.67201  45.92152 0.600 31.82877 ? 183 THR A O   1 
ATOM   1467 C CB  A THR A 1 189 ? 15.00398  14.07856  47.20167 0.400 29.02556 ? 183 THR A CB  1 
ATOM   1468 C CB  B THR A 1 189 ? 15.86394  14.76877  47.02679 0.600 29.62822 ? 183 THR A CB  1 
ATOM   1469 O OG1 A THR A 1 189 ? 14.26255  13.11371  47.94628 0.400 32.88900 ? 183 THR A OG1 1 
ATOM   1470 O OG1 B THR A 1 189 ? 15.78999  13.44352  47.58030 0.600 29.67860 ? 183 THR A OG1 1 
ATOM   1471 C CG2 A THR A 1 189 ? 16.48602  13.80808  47.38901 0.400 27.94713 ? 183 THR A CG2 1 
ATOM   1472 C CG2 B THR A 1 189 ? 17.25824  15.36826  47.35596 0.600 31.56918 ? 183 THR A CG2 1 
ATOM   1473 N N   A GLU A 1 190 ? 12.98882  16.45656  46.22771 0.400 20.90673 ? 184 GLU A N   1 
ATOM   1474 N N   B GLU A 1 190 ? 12.56804  14.56791  47.80871 0.600 32.71549 ? 184 GLU A N   1 
ATOM   1475 C CA  A GLU A 1 190 ? 11.66166  16.89125  45.82335 0.400 23.60676 ? 184 GLU A CA  1 
ATOM   1476 C CA  B GLU A 1 190 ? 11.36805  13.93531  47.27209 0.600 34.99156 ? 184 GLU A CA  1 
ATOM   1477 C C   A GLU A 1 190 ? 10.68975  15.72148  45.68657 0.400 20.91968 ? 184 GLU A C   1 
ATOM   1478 C C   B GLU A 1 190 ? 10.10045  14.68979  47.65363 0.600 37.20042 ? 184 GLU A C   1 
ATOM   1479 O O   A GLU A 1 190 ? 11.05802  14.60924  45.30220 0.400 21.71505 ? 184 GLU A O   1 
ATOM   1480 O O   B GLU A 1 190 ? 10.02834  15.30062  48.71870 0.600 35.93056 ? 184 GLU A O   1 
ATOM   1481 C CB  A GLU A 1 190 ? 11.72474  17.63387  44.48605 0.400 28.53673 ? 184 GLU A CB  1 
ATOM   1482 C CB  B GLU A 1 190 ? 11.27556  12.48330  47.75610 0.600 37.99314 ? 184 GLU A CB  1 
ATOM   1483 C CG  A GLU A 1 190 ? 12.30071  16.80273  43.34034 0.400 34.52258 ? 184 GLU A CG  1 
ATOM   1484 C CG  B GLU A 1 190 ? 12.35626  11.62897  47.19920 0.600 44.01024 ? 184 GLU A CG  1 
ATOM   1485 C CD  A GLU A 1 190 ? 12.92993  17.65139  42.24745 0.400 39.21175 ? 184 GLU A CD  1 
ATOM   1486 C CD  B GLU A 1 190 ? 12.32583  11.64093  45.68752 0.600 47.39309 ? 184 GLU A CD  1 
ATOM   1487 O OE1 A GLU A 1 190 ? 12.25817  18.59290  41.76950 0.400 40.94532 ? 184 GLU A OE1 1 
ATOM   1488 O OE1 B GLU A 1 190 ? 11.20964  11.61373  45.13240 0.600 45.08385 ? 184 GLU A OE1 1 
ATOM   1489 O OE2 A GLU A 1 190 ? 14.08856  17.37791  41.85827 0.400 41.11488 ? 184 GLU A OE2 1 
ATOM   1490 O OE2 B GLU A 1 190 ? 13.40310  11.68115  45.06503 0.600 51.30453 ? 184 GLU A OE2 1 
ATOM   1491 N N   A TYR A 1 191 ? 9.41887   16.01066  45.95175 0.400 19.07668 ? 185 TYR A N   1 
ATOM   1492 N N   B TYR A 1 191 ? 9.08030   14.61030  46.77396 0.600 39.24587 ? 185 TYR A N   1 
ATOM   1493 C CA  A TYR A 1 191 ? 8.34279   15.02651  45.91611 0.400 20.04890 ? 185 TYR A CA  1 
ATOM   1494 C CA  B TYR A 1 191 ? 7.83126   15.35466  46.93656 0.600 43.16046 ? 185 TYR A CA  1 
ATOM   1495 C C   A TYR A 1 191 ? 7.07306   15.66069  45.35088 0.400 23.66196 ? 185 TYR A C   1 
ATOM   1496 C C   B TYR A 1 191 ? 6.58934   14.48033  46.75276 0.600 41.32410 ? 185 TYR A C   1 
ATOM   1497 O O   A TYR A 1 191 ? 6.84195   16.85903  45.53216 0.400 27.62180 ? 185 TYR A O   1 
ATOM   1498 O O   B TYR A 1 191 ? 5.50815   15.00562  46.46354 0.600 45.79105 ? 185 TYR A O   1 
ATOM   1499 C CB  A TYR A 1 191 ? 8.06382   14.47953  47.31642 0.400 18.31803 ? 185 TYR A CB  1 
ATOM   1500 C CB  B TYR A 1 191 ? 7.77293   16.53432  45.95261 0.600 48.11562 ? 185 TYR A CB  1 
ATOM   1501 C CG  A TYR A 1 191 ? 7.39294   13.11678  47.30320 0.400 19.12186 ? 185 TYR A CG  1 
ATOM   1502 C CG  B TYR A 1 191 ? 8.93731   17.49716  46.06795 0.600 52.26709 ? 185 TYR A CG  1 
ATOM   1503 C CD1 A TYR A 1 191 ? 8.05248   11.99808  46.80674 0.400 19.25899 ? 185 TYR A CD1 1 
ATOM   1504 C CD1 B TYR A 1 191 ? 10.11777  17.28269  45.37323 0.600 54.78581 ? 185 TYR A CD1 1 
ATOM   1505 C CD2 A TYR A 1 191 ? 6.10523   12.94376  47.81219 0.400 18.42044 ? 185 TYR A CD2 1 
ATOM   1506 C CD2 B TYR A 1 191 ? 8.85604   18.61326  46.88425 0.600 53.17796 ? 185 TYR A CD2 1 
ATOM   1507 C CE1 A TYR A 1 191 ? 7.45601   10.76041  46.80092 0.400 18.98474 ? 185 TYR A CE1 1 
ATOM   1508 C CE1 B TYR A 1 191 ? 11.18572  18.16976  45.49082 0.600 55.82576 ? 185 TYR A CE1 1 
ATOM   1509 C CE2 A TYR A 1 191 ? 5.49429   11.68410  47.80789 0.400 19.68288 ? 185 TYR A CE2 1 
ATOM   1510 C CE2 B TYR A 1 191 ? 9.90275   19.49908  47.00962 0.600 54.93472 ? 185 TYR A CE2 1 
ATOM   1511 C CZ  A TYR A 1 191 ? 6.18164   10.59864  47.30234 0.400 20.03207 ? 185 TYR A CZ  1 
ATOM   1512 C CZ  B TYR A 1 191 ? 11.06803  19.27734  46.31805 0.600 56.43519 ? 185 TYR A CZ  1 
ATOM   1513 O OH  A TYR A 1 191 ? 5.59880   9.34952   47.30097 0.400 22.63530 ? 185 TYR A OH  1 
ATOM   1514 O OH  B TYR A 1 191 ? 12.10667  20.16950  46.45782 0.600 57.36866 ? 185 TYR A OH  1 
ATOM   1515 N N   A VAL A 1 192 ? 6.23270   14.85302  44.70158 0.400 22.40659 ? 186 VAL A N   1 
ATOM   1516 N N   B VAL A 1 192 ? 6.71874   13.16370  46.92330 0.600 34.17079 ? 186 VAL A N   1 
ATOM   1517 C CA  A VAL A 1 192 ? 5.06428   15.36726  43.98204 0.400 21.82271 ? 186 VAL A CA  1 
ATOM   1518 C CA  B VAL A 1 192 ? 5.61197   12.24095  46.70383 0.600 27.56699 ? 186 VAL A CA  1 
ATOM   1519 C C   A VAL A 1 192 ? 3.76961   15.31441  44.80819 0.400 19.58488 ? 186 VAL A C   1 
ATOM   1520 C C   B VAL A 1 192 ? 4.40126   12.63332  47.56656 0.600 25.16069 ? 186 VAL A C   1 
ATOM   1521 O O   A VAL A 1 192 ? 2.97604   16.25154  44.75474 0.400 23.37728 ? 186 VAL A O   1 
ATOM   1522 O O   B VAL A 1 192 ? 4.55334   13.21146  48.64828 0.600 26.66448 ? 186 VAL A O   1 
ATOM   1523 C CB  A VAL A 1 192 ? 4.90213   14.62208  42.63747 0.400 22.91831 ? 186 VAL A CB  1 
ATOM   1524 C CB  B VAL A 1 192 ? 6.12478   10.82489  47.02604 0.600 28.70249 ? 186 VAL A CB  1 
ATOM   1525 C CG1 A VAL A 1 192 ? 3.65758   15.12319  41.89142 0.400 23.58617 ? 186 VAL A CG1 1 
ATOM   1526 C CG1 B VAL A 1 192 ? 5.08689   9.75512   46.73068 0.600 29.44969 ? 186 VAL A CG1 1 
ATOM   1527 C CG2 A VAL A 1 192 ? 6.15714   14.77817  41.78414 0.400 27.40257 ? 186 VAL A CG2 1 
ATOM   1528 C CG2 B VAL A 1 192 ? 7.44949   10.58676  46.32495 0.600 29.51120 ? 186 VAL A CG2 1 
ATOM   1529 N N   A ALA A 1 193 ? 3.53139   14.25837  45.58616 0.400 16.67452 ? 187 ALA A N   1 
ATOM   1530 N N   B ALA A 1 193 ? 3.19076   12.34837  47.06759 0.600 22.78874 ? 187 ALA A N   1 
ATOM   1531 C CA  A ALA A 1 193 ? 2.21203   13.95235  46.15807 0.400 16.37459 ? 187 ALA A CA  1 
ATOM   1532 C CA  B ALA A 1 193 ? 1.93418   12.76557  47.71450 0.600 23.30514 ? 187 ALA A CA  1 
ATOM   1533 C C   A ALA A 1 193 ? 1.81169   14.93392  47.27238 0.400 19.95259 ? 187 ALA A C   1 
ATOM   1534 C C   B ALA A 1 193 ? 1.81758   14.29018  47.86563 0.600 23.64940 ? 187 ALA A C   1 
ATOM   1535 O O   A ALA A 1 193 ? 2.58163   15.80302  47.66275 0.400 21.94922 ? 187 ALA A O   1 
ATOM   1536 O O   B ALA A 1 193 ? 2.80872   15.01747  47.87895 0.600 28.03989 ? 187 ALA A O   1 
ATOM   1537 C CB  A ALA A 1 193 ? 2.19893   12.52525  46.68855 0.400 18.31065 ? 187 ALA A CB  1 
ATOM   1538 C CB  B ALA A 1 193 ? 1.76516   12.09359  49.10589 0.600 25.05754 ? 187 ALA A CB  1 
ATOM   1539 N N   . THR A 1 194 ? 0.58410   14.78914  47.83577 1.000 26.87249 ? 188 THR A N   1 
ATOM   1540 C CA  . THR A 1 194 ? 0.07087   15.89245  48.66075 1.000 23.61707 ? 188 THR A CA  1 
ATOM   1541 C C   . THR A 1 194 ? 0.69953   16.02548  50.06532 1.000 25.69662 ? 188 THR A C   1 
ATOM   1542 O O   . THR A 1 194 ? 0.71905   15.06512  50.85465 1.000 26.24985 ? 188 THR A O   1 
ATOM   1543 C CB  . THR A 1 194 ? -1.45595  15.74812  48.74849 1.000 21.65638 ? 188 THR A CB  1 
ATOM   1544 O OG1 . THR A 1 194 ? -1.94395  15.60898  47.41144 1.000 22.02687 ? 188 THR A OG1 1 
ATOM   1545 C CG2 . THR A 1 194 ? -2.08536  16.97034  49.35658 1.000 24.31523 ? 188 THR A CG2 1 
ATOM   1546 N N   . ARG A 1 195 ? 1.11201   17.26193  50.41065 1.000 22.71159 ? 189 ARG A N   1 
ATOM   1547 C CA  . ARG A 1 195 ? 1.99711   17.49920  51.55345 1.000 21.86619 ? 189 ARG A CA  1 
ATOM   1548 C C   . ARG A 1 195 ? 1.47476   16.91455  52.85787 1.000 21.85121 ? 189 ARG A C   1 
ATOM   1549 O O   . ARG A 1 195 ? 2.21136   16.21597  53.56805 1.000 22.46554 ? 189 ARG A O   1 
ATOM   1550 C CB  . ARG A 1 195 ? 2.24193   19.00426  51.72869 0.900 22.81812 ? 189 ARG A CB  1 
ATOM   1551 C CG  . ARG A 1 195 ? 3.23583   19.31409  52.87124 0.900 24.62451 ? 189 ARG A CG  1 
ATOM   1552 C CD  . ARG A 1 195 ? 3.24828   20.79205  53.23002 0.800 29.23156 ? 189 ARG A CD  1 
ATOM   1553 N NE  . ARG A 1 195 ? 3.20060   21.61815  52.02622 0.800 33.96603 ? 189 ARG A NE  1 
ATOM   1554 C CZ  . ARG A 1 195 ? 2.34596   22.60526  51.78921 0.800 38.46307 ? 189 ARG A CZ  1 
ATOM   1555 N NH1 . ARG A 1 195 ? 1.47781   23.01265  52.69989 0.800 38.85510 ? 189 ARG A NH1 1 
ATOM   1556 N NH2 . ARG A 1 195 ? 2.36597   23.20312  50.60106 0.800 42.76415 ? 189 ARG A NH2 1 
ATOM   1557 N N   . TRP A 1 196 ? 0.21227   17.20599  53.20908 1.000 21.92123 ? 190 TRP A N   1 
ATOM   1558 C CA  . TRP A 1 196 ? -0.28903  16.83373  54.53373 1.000 21.52564 ? 190 TRP A CA  1 
ATOM   1559 C C   . TRP A 1 196 ? -0.35089  15.32470  54.75308 1.000 20.18917 ? 190 TRP A C   1 
ATOM   1560 O O   . TRP A 1 196 ? -0.41530  14.88096  55.90943 1.000 20.74579 ? 190 TRP A O   1 
ATOM   1561 C CB  . TRP A 1 196 ? -1.68276  17.43940  54.77168 0.900 20.71333 ? 190 TRP A CB  1 
ATOM   1562 C CG  . TRP A 1 196 ? -1.70274  18.91841  54.84152 0.800 21.40746 ? 190 TRP A CG  1 
ATOM   1563 C CD1 . TRP A 1 196 ? -0.64628  19.76031  55.00519 0.700 22.07005 ? 190 TRP A CD1 1 
ATOM   1564 C CD2 . TRP A 1 196 ? -2.86787  19.73519  54.76595 0.700 22.24401 ? 190 TRP A CD2 1 
ATOM   1565 N NE1 . TRP A 1 196 ? -1.08305  21.07000  55.03052 0.700 21.59456 ? 190 TRP A NE1 1 
ATOM   1566 C CE2 . TRP A 1 196 ? -2.45167  21.07674  54.88203 0.700 23.32903 ? 190 TRP A CE2 1 
ATOM   1567 C CE3 . TRP A 1 196 ? -4.22760  19.45902  54.59937 0.700 24.04966 ? 190 TRP A CE3 1 
ATOM   1568 C CZ2 . TRP A 1 196 ? -3.34990  22.14193  54.83387 0.700 26.09428 ? 190 TRP A CZ2 1 
ATOM   1569 C CZ3 . TRP A 1 196 ? -5.10714  20.51189  54.55609 0.700 25.59725 ? 190 TRP A CZ3 1 
ATOM   1570 C CH2 . TRP A 1 196 ? -4.66972  21.83082  54.67306 0.700 26.69343 ? 190 TRP A CH2 1 
ATOM   1571 N N   . TYR A 1 197 ? -0.32367  14.52231  53.68878 1.000 18.28457 ? 191 TYR A N   1 
ATOM   1572 C CA  . TYR A 1 197 ? -0.48652  13.07706  53.76017 1.000 17.37198 ? 191 TYR A CA  1 
ATOM   1573 C C   . TYR A 1 197 ? 0.82360   12.34735  53.48050 1.000 16.33656 ? 191 TYR A C   1 
ATOM   1574 O O   . TYR A 1 197 ? 0.83986   11.13135  53.33836 1.000 17.91019 ? 191 TYR A O   1 
ATOM   1575 C CB  . TYR A 1 197 ? -1.61322  12.64104  52.81389 1.000 18.04731 ? 191 TYR A CB  1 
ATOM   1576 C CG  . TYR A 1 197 ? -2.85725  13.42484  53.15232 1.000 17.92196 ? 191 TYR A CG  1 
ATOM   1577 C CD1 . TYR A 1 197 ? -3.13060  14.66451  52.53805 1.000 19.32796 ? 191 TYR A CD1 1 
ATOM   1578 C CD2 . TYR A 1 197 ? -3.70412  13.00011  54.20413 1.000 19.18453 ? 191 TYR A CD2 1 
ATOM   1579 C CE1 . TYR A 1 197 ? -4.22692  15.42869  52.92060 1.000 21.10332 ? 191 TYR A CE1 1 
ATOM   1580 C CE2 . TYR A 1 197 ? -4.80758  13.78645  54.58720 1.000 20.60828 ? 191 TYR A CE2 1 
ATOM   1581 C CZ  . TYR A 1 197 ? -5.04693  14.99576  53.94161 1.000 21.47968 ? 191 TYR A CZ  1 
ATOM   1582 O OH  . TYR A 1 197 ? -6.10595  15.77731  54.30801 1.000 22.93765 ? 191 TYR A OH  1 
ATOM   1583 N N   . ARG A 1 198 ? 1.92930   13.07259  53.51635 1.000 19.37362 ? 192 ARG A N   1 
ATOM   1584 C CA  . ARG A 1 198 ? 3.22883   12.57826  53.09945 1.000 18.23478 ? 192 ARG A CA  1 
ATOM   1585 C C   . ARG A 1 198 ? 3.98552   11.99412  54.30872 1.000 15.65390 ? 192 ARG A C   1 
ATOM   1586 O O   . ARG A 1 198 ? 4.12158   12.65048  55.35043 1.000 17.06432 ? 192 ARG A O   1 
ATOM   1587 C CB  . ARG A 1 198 ? 3.90906   13.77379  52.41358 0.900 22.95417 ? 192 ARG A CB  1 
ATOM   1588 C CG  . ARG A 1 198 ? 5.22979   13.69657  51.82261 0.800 25.05088 ? 192 ARG A CG  1 
ATOM   1589 C CD  . ARG A 1 198 ? 5.60471   15.11486  51.23952 0.800 19.25961 ? 192 ARG A CD  1 
ATOM   1590 N NE  . ARG A 1 198 ? 4.90755   15.66980  50.05774 0.800 19.15333 ? 192 ARG A NE  1 
ATOM   1591 C CZ  . ARG A 1 198 ? 5.10033   16.90599  49.61106 0.700 20.10145 ? 192 ARG A CZ  1 
ATOM   1592 N NH1 . ARG A 1 198 ? 5.80012   17.78793  50.30345 0.700 24.55065 ? 192 ARG A NH1 1 
ATOM   1593 N NH2 . ARG A 1 198 ? 4.57351   17.28178  48.44330 0.700 24.03801 ? 192 ARG A NH2 1 
ATOM   1594 N N   . ALA A 1 199 ? 4.45502   10.75729  54.16678 1.000 15.55762 ? 193 ALA A N   1 
ATOM   1595 C CA  . ALA A 1 199 ? 5.17581   10.04764  55.24182 1.000 15.77051 ? 193 ALA A CA  1 
ATOM   1596 C C   . ALA A 1 199 ? 6.50567   10.73224  55.57855 1.000 17.94451 ? 193 ALA A C   1 
ATOM   1597 O O   . ALA A 1 199 ? 7.13892   11.34250  54.71183 1.000 16.03318 ? 193 ALA A O   1 
ATOM   1598 C CB  . ALA A 1 199 ? 5.43398   8.58407   54.84497 1.000 16.44954 ? 193 ALA A CB  1 
ATOM   1599 N N   . PRO A 1 200 ? 6.94551   10.63496  56.84110 1.000 16.36767 ? 194 PRO A N   1 
ATOM   1600 C CA  . PRO A 1 200 ? 8.16886   11.33687  57.23722 1.000 17.56587 ? 194 PRO A CA  1 
ATOM   1601 C C   . PRO A 1 200 ? 9.35844   10.94536  56.38616 1.000 16.48830 ? 194 PRO A C   1 
ATOM   1602 O O   . PRO A 1 200 ? 10.20066  11.81453  56.08693 1.000 17.02700 ? 194 PRO A O   1 
ATOM   1603 C CB  . PRO A 1 200 ? 8.34017   10.94013  58.71967 1.000 18.87572 ? 194 PRO A CB  1 
ATOM   1604 C CG  . PRO A 1 200 ? 7.49266   9.73225   58.93922 1.000 17.00902 ? 194 PRO A CG  1 
ATOM   1605 C CD  . PRO A 1 200 ? 6.33542   9.86679   57.95665 1.000 15.93379 ? 194 PRO A CD  1 
ATOM   1606 N N   . GLU A 1 201 ? 9.43634   9.67749   55.94626 1.000 16.91888 ? 195 GLU A N   1 
ATOM   1607 C CA  . GLU A 1 201 ? 10.64031  9.26464   55.22104 1.000 17.23977 ? 195 GLU A CA  1 
ATOM   1608 C C   . GLU A 1 201 ? 10.76030  9.93734   53.85070 1.000 17.36699 ? 195 GLU A C   1 
ATOM   1609 O O   . GLU A 1 201 ? 11.86454  9.99046   53.30160 1.000 18.58679 ? 195 GLU A O   1 
ATOM   1610 C CB  . GLU A 1 201 ? 10.69713  7.73057   55.06118 1.000 17.58379 ? 195 GLU A CB  1 
ATOM   1611 C CG  . GLU A 1 201 ? 9.47910   7.10705   54.37395 1.000 16.59028 ? 195 GLU A CG  1 
ATOM   1612 C CD  . GLU A 1 201 ? 8.33218   6.72911   55.29500 1.000 19.74073 ? 195 GLU A CD  1 
ATOM   1613 O OE1 . GLU A 1 201 ? 8.21762   7.26167   56.43682 1.000 19.48034 ? 195 GLU A OE1 1 
ATOM   1614 O OE2 . GLU A 1 201 ? 7.51177   5.91277   54.80664 1.000 19.04063 ? 195 GLU A OE2 1 
ATOM   1615 N N   . ILE A 1 202 ? 9.66594   10.45105  53.27722 1.000 16.67676 ? 196 ILE A N   1 
ATOM   1616 C CA  . ILE A 1 202 ? 9.76520   11.17197  51.99813 1.000 17.00147 ? 196 ILE A CA  1 
ATOM   1617 C C   . ILE A 1 202 ? 10.75001  12.33190  52.09671 1.000 17.61384 ? 196 ILE A C   1 
ATOM   1618 O O   . ILE A 1 202 ? 11.53236  12.58958  51.16629 1.000 20.52023 ? 196 ILE A O   1 
ATOM   1619 C CB  . ILE A 1 202 ? 8.36093   11.65761  51.56552 1.000 17.85298 ? 196 ILE A CB  1 
ATOM   1620 C CG1 . ILE A 1 202 ? 7.48213   10.45415  51.22668 1.000 19.42777 ? 196 ILE A CG1 1 
ATOM   1621 C CG2 . ILE A 1 202 ? 8.45071   12.66153  50.38323 1.000 19.11446 ? 196 ILE A CG2 1 
ATOM   1622 C CD1 . ILE A 1 202 ? 8.00888   9.65805   50.10459 1.000 20.80606 ? 196 ILE A CD1 1 
ATOM   1623 N N   . MET A 1 203 ? 10.73397  13.04712  53.22149 1.000 18.48697 ? 197 MET A N   1 
ATOM   1624 C CA  . MET A 1 203 ? 11.62485  14.17998  53.44414 1.000 21.34312 ? 197 MET A CA  1 
ATOM   1625 C C   . MET A 1 203 ? 13.02556  13.74876  53.86512 1.000 21.74754 ? 197 MET A C   1 
ATOM   1626 O O   . MET A 1 203 ? 13.94073  14.57040  53.85687 1.000 25.13129 ? 197 MET A O   1 
ATOM   1627 C CB  . MET A 1 203 ? 11.03700  15.09916  54.51592 1.000 20.75313 ? 197 MET A CB  1 
ATOM   1628 C CG  . MET A 1 203 ? 9.79737   15.86735  54.10415 1.000 20.25829 ? 197 MET A CG  1 
ATOM   1629 S SD  . MET A 1 203 ? 8.23459   14.91646  53.92338 1.000 23.31419 ? 197 MET A SD  1 
ATOM   1630 C CE  . MET A 1 203 ? 7.65033   14.84471  55.63641 1.000 24.82701 ? 197 MET A CE  1 
ATOM   1631 N N   . LEU A 1 204 ? 13.20122  12.49183  54.26148 1.000 18.84161 ? 198 LEU A N   1 
ATOM   1632 C CA  . LEU A 1 204 ? 14.45918  12.04286  54.84463 1.000 19.31675 ? 198 LEU A CA  1 
ATOM   1633 C C   . LEU A 1 204 ? 15.29010  11.23239  53.85236 1.000 20.20406 ? 198 LEU A C   1 
ATOM   1634 O O   . LEU A 1 204 ? 16.46807  11.56274  53.59096 1.000 21.72061 ? 198 LEU A O   1 
ATOM   1635 C CB  . LEU A 1 204 ? 14.14312  11.22244  56.09809 1.000 20.15534 ? 198 LEU A CB  1 
ATOM   1636 C CG  . LEU A 1 204 ? 13.58804  12.04479  57.26247 1.000 18.49079 ? 198 LEU A CG  1 
ATOM   1637 C CD1 . LEU A 1 204 ? 13.02033  11.06316  58.32569 1.000 19.95392 ? 198 LEU A CD1 1 
ATOM   1638 C CD2 . LEU A 1 204 ? 14.69611  12.96871  57.83901 1.000 20.26356 ? 198 LEU A CD2 1 
ATOM   1639 N N   . ASN A 1 205 ? 14.71528  10.14133  53.31892 1.000 19.22355 ? 199 ASN A N   1 
ATOM   1640 C CA  . ASN A 1 205 ? 15.54782  9.22206   52.53071 1.000 20.35151 ? 199 ASN A CA  1 
ATOM   1641 C C   . ASN A 1 205 ? 14.74268  8.33050   51.59150 1.000 20.72495 ? 199 ASN A C   1 
ATOM   1642 O O   . ASN A 1 205 ? 15.29827  7.32418   51.14390 1.000 21.83048 ? 199 ASN A O   1 
ATOM   1643 C CB  . ASN A 1 205 ? 16.39265  8.31426   53.46207 1.000 20.41895 ? 199 ASN A CB  1 
ATOM   1644 C CG  . ASN A 1 205 ? 15.52987  7.38193   54.32204 0.800 19.02659 ? 199 ASN A CG  1 
ATOM   1645 O OD1 . ASN A 1 205 ? 14.31914  7.53204   54.38130 0.800 20.82167 ? 199 ASN A OD1 1 
ATOM   1646 N ND2 . ASN A 1 205 ? 16.15883  6.39703   54.96216 0.800 19.65564 ? 199 ASN A ND2 1 
ATOM   1647 N N   . SER A 1 206 ? 13.47042  8.61746   51.28223 1.000 18.50981 ? 200 SER A N   1 
ATOM   1648 C CA  . SER A 1 206 ? 12.65563  7.68020   50.52048 1.000 19.46971 ? 200 SER A CA  1 
ATOM   1649 C C   . SER A 1 206 ? 12.07397  8.36405   49.28592 1.000 20.76680 ? 200 SER A C   1 
ATOM   1650 O O   . SER A 1 206 ? 11.61512  9.51114   49.35675 1.000 20.14466 ? 200 SER A O   1 
ATOM   1651 C CB  . SER A 1 206 ? 11.51525  7.10739   51.39309 1.000 21.23587 ? 200 SER A CB  1 
ATOM   1652 O OG  . SER A 1 206 ? 10.60697  6.34913   50.60365 1.000 20.83541 ? 200 SER A OG  1 
ATOM   1653 N N   . LYS A 1 207 ? 12.07486  7.63445   48.16962 1.000 19.52437 ? 201 LYS A N   1 
ATOM   1654 C CA  . LYS A 1 207 ? 11.41800  8.01646   46.91640 1.000 21.40218 ? 201 LYS A CA  1 
ATOM   1655 C C   . LYS A 1 207 ? 9.92318   7.68448   46.90143 1.000 22.46332 ? 201 LYS A C   1 
ATOM   1656 O O   . LYS A 1 207 ? 9.24364   8.00970   45.91752 1.000 24.98449 ? 201 LYS A O   1 
ATOM   1657 C CB  . LYS A 1 207 ? 12.09274  7.29965   45.74857 1.000 24.19778 ? 201 LYS A CB  1 
ATOM   1658 C CG  . LYS A 1 207 ? 13.55620  7.65755   45.58283 1.000 25.60390 ? 201 LYS A CG  1 
ATOM   1659 C CD  . LYS A 1 207 ? 14.01500  7.35973   44.14089 1.000 33.12536 ? 201 LYS A CD  1 
ATOM   1660 C CE  . LYS A 1 207 ? 15.36509  6.63908   44.12878 0.600 35.62013 ? 201 LYS A CE  1 
ATOM   1661 N NZ  . LYS A 1 207 ? 16.02760  6.51817   42.79432 0.400 34.85221 ? 201 LYS A NZ  1 
ATOM   1662 N N   . GLY A 1 208 ? 9.39003   7.03986   47.94173 1.000 21.11500 ? 202 GLY A N   1 
ATOM   1663 C CA  . GLY A 1 208 ? 7.96931   6.71532   47.92195 1.000 19.42114 ? 202 GLY A CA  1 
ATOM   1664 C C   . GLY A 1 208 ? 7.65009   5.52422   47.05481 1.000 19.23911 ? 202 GLY A C   1 
ATOM   1665 O O   . GLY A 1 208 ? 6.56562   5.46494   46.45698 1.000 20.13555 ? 202 GLY A O   1 
ATOM   1666 N N   . TYR A 1 209 ? 8.54665   4.54788   46.98710 1.000 20.85435 ? 203 TYR A N   1 
ATOM   1667 C CA  A TYR A 1 209 ? 8.40079   3.36252   46.15393 0.700 19.13718 ? 203 TYR A CA  1 
ATOM   1668 C CA  B TYR A 1 209 ? 8.31228   3.38277   46.14206 0.300 20.25170 ? 203 TYR A CA  1 
ATOM   1669 C C   . TYR A 1 209 ? 8.06220   2.11373   46.95445 1.000 21.27543 ? 203 TYR A C   1 
ATOM   1670 O O   . TYR A 1 209 ? 8.22143   1.00038   46.43350 1.000 23.76626 ? 203 TYR A O   1 
ATOM   1671 C CB  A TYR A 1 209 ? 9.69023   3.10056   45.36237 0.700 20.92529 ? 203 TYR A CB  1 
ATOM   1672 C CB  B TYR A 1 209 ? 9.47466   3.18490   45.16234 0.300 20.24027 ? 203 TYR A CB  1 
ATOM   1673 C CG  A TYR A 1 209 ? 10.05350  4.09079   44.27620 0.700 25.77727 ? 203 TYR A CG  1 
ATOM   1674 C CG  B TYR A 1 209 ? 9.32391   3.94868   43.85191 0.300 21.56376 ? 203 TYR A CG  1 
ATOM   1675 C CD1 A TYR A 1 209 ? 9.23168   5.17025   43.95803 0.700 27.85998 ? 203 TYR A CD1 1 
ATOM   1676 C CD1 B TYR A 1 209 ? 9.66644   5.29547   43.77039 0.300 23.27622 ? 203 TYR A CD1 1 
ATOM   1677 C CD2 A TYR A 1 209 ? 11.25287  3.94822   43.57797 0.700 27.15864 ? 203 TYR A CD2 1 
ATOM   1678 C CD2 B TYR A 1 209 ? 8.81294   3.33126   42.70449 0.300 21.24311 ? 203 TYR A CD2 1 
ATOM   1679 C CE1 A TYR A 1 209 ? 9.59878   6.08752   42.96388 0.700 30.59148 ? 203 TYR A CE1 1 
ATOM   1680 C CE1 B TYR A 1 209 ? 9.54046   6.00365   42.58017 0.300 23.80834 ? 203 TYR A CE1 1 
ATOM   1681 C CE2 A TYR A 1 209 ? 11.62533  4.84222   42.57408 0.700 29.63792 ? 203 TYR A CE2 1 
ATOM   1682 C CE2 B TYR A 1 209 ? 8.68789   4.02881   41.51187 0.300 22.89733 ? 203 TYR A CE2 1 
ATOM   1683 C CZ  A TYR A 1 209 ? 10.79166  5.91202   42.27369 0.700 32.98539 ? 203 TYR A CZ  1 
ATOM   1684 C CZ  B TYR A 1 209 ? 9.04714   5.36615   41.45823 0.300 25.02012 ? 203 TYR A CZ  1 
ATOM   1685 O OH  A TYR A 1 209 ? 11.13896  6.80160   41.28201 0.700 35.50994 ? 203 TYR A OH  1 
ATOM   1686 O OH  B TYR A 1 209 ? 8.91807   6.07267   40.28770 0.300 27.18954 ? 203 TYR A OH  1 
ATOM   1687 N N   . THR A 1 210 ? 7.63062   2.25224   48.22393 1.000 19.31057 ? 204 THR A N   1 
ATOM   1688 C CA  . THR A 1 210 ? 7.22962   1.07674   48.99705 1.000 21.68822 ? 204 THR A CA  1 
ATOM   1689 C C   . THR A 1 210 ? 5.81266   1.28546   49.52664 1.000 20.10763 ? 204 THR A C   1 
ATOM   1690 O O   . THR A 1 210 ? 5.34285   2.41282   49.68709 1.000 21.21570 ? 204 THR A O   1 
ATOM   1691 C CB  . THR A 1 210 ? 8.13249   0.75981   50.19180 1.000 26.35597 ? 204 THR A CB  1 
ATOM   1692 O OG1 . THR A 1 210 ? 7.96708   1.78234   51.15826 1.000 31.25597 ? 204 THR A OG1 1 
ATOM   1693 C CG2 . THR A 1 210 ? 9.62265   0.71463   49.78309 1.000 26.86947 ? 204 THR A CG2 1 
ATOM   1694 N N   . LYS A 1 211 ? 5.16130   0.16716   49.83401 1.000 17.94434 ? 205 LYS A N   1 
ATOM   1695 C CA  . LYS A 1 211 ? 3.74505   0.18523   50.20847 1.000 17.09982 ? 205 LYS A CA  1 
ATOM   1696 C C   . LYS A 1 211 ? 3.48767   0.96226   51.49579 1.000 15.94682 ? 205 LYS A C   1 
ATOM   1697 O O   . LYS A 1 211 ? 2.38423   1.49573   51.70145 1.000 16.18202 ? 205 LYS A O   1 
ATOM   1698 C CB  . LYS A 1 211 ? 3.25057   -1.24279  50.33832 1.000 20.11715 ? 205 LYS A CB  1 
ATOM   1699 C CG  . LYS A 1 211 ? 3.16977   -1.97171  48.99945 1.000 19.00591 ? 205 LYS A CG  1 
ATOM   1700 C CD  . LYS A 1 211 ? 2.94982   -3.43695  49.19985 1.000 19.00198 ? 205 LYS A CD  1 
ATOM   1701 C CE  . LYS A 1 211 ? 2.93793   -4.16128  47.84848 1.000 20.44457 ? 205 LYS A CE  1 
ATOM   1702 N NZ  . LYS A 1 211 ? 2.72562   -5.61043  47.97446 1.000 22.13080 ? 205 LYS A NZ  1 
ATOM   1703 N N   . SER A 1 212 ? 4.47626   1.02676   52.38724 1.000 15.21710 ? 206 SER A N   1 
ATOM   1704 C CA  . SER A 1 212 ? 4.30284   1.79524   53.61822 1.000 15.56573 ? 206 SER A CA  1 
ATOM   1705 C C   . SER A 1 212 ? 3.95860   3.28071   53.39882 1.000 15.53819 ? 206 SER A C   1 
ATOM   1706 O O   . SER A 1 212 ? 3.43029   3.90978   54.32745 1.000 15.82474 ? 206 SER A O   1 
ATOM   1707 C CB  . SER A 1 212 ? 5.57867   1.65857   54.47400 1.000 19.23151 ? 206 SER A CB  1 
ATOM   1708 O OG  . SER A 1 212 ? 6.75855   2.01080   53.74220 1.000 21.60253 ? 206 SER A OG  1 
ATOM   1709 N N   . ILE A 1 213 ? 4.28198   3.86701   52.23244 1.000 16.30184 ? 207 ILE A N   1 
ATOM   1710 C CA  . ILE A 1 213 ? 3.87302   5.23457   51.91349 1.000 17.57690 ? 207 ILE A CA  1 
ATOM   1711 C C   . ILE A 1 213 ? 2.35033   5.39369   51.97892 1.000 16.15358 ? 207 ILE A C   1 
ATOM   1712 O O   . ILE A 1 213 ? 1.81548   6.40420   52.47638 1.000 17.32447 ? 207 ILE A O   1 
ATOM   1713 C CB  . ILE A 1 213 ? 4.45596   5.66512   50.53973 1.000 19.37729 ? 207 ILE A CB  1 
ATOM   1714 C CG1 . ILE A 1 213 ? 4.38963   7.16689   50.45501 1.000 22.94630 ? 207 ILE A CG1 1 
ATOM   1715 C CG2 . ILE A 1 213 ? 3.73190   5.04852   49.33098 1.000 21.76522 ? 207 ILE A CG2 1 
ATOM   1716 C CD1 . ILE A 1 213 ? 5.52413   7.76765   51.12372 1.000 26.45821 ? 207 ILE A CD1 1 
ATOM   1717 N N   . ASP A 1 214 ? 1.64003   4.39152   51.52370 1.000 14.99526 ? 208 ASP A N   1 
ATOM   1718 C CA  . ASP A 1 214 ? 0.18464   4.50796   51.46218 1.000 15.02447 ? 208 ASP A CA  1 
ATOM   1719 C C   . ASP A 1 214 ? -0.42157  4.33050   52.84089 1.000 16.11166 ? 208 ASP A C   1 
ATOM   1720 O O   . ASP A 1 214 ? -1.41282  4.98674   53.16578 1.000 15.39477 ? 208 ASP A O   1 
ATOM   1721 C CB  . ASP A 1 214 ? -0.40091  3.46955   50.48653 1.000 14.35262 ? 208 ASP A CB  1 
ATOM   1722 C CG  . ASP A 1 214 ? -0.25506  3.86491   48.99115 1.000 14.47930 ? 208 ASP A CG  1 
ATOM   1723 O OD1 . ASP A 1 214 ? -0.16069  5.07413   48.64090 1.000 16.36804 ? 208 ASP A OD1 1 
ATOM   1724 O OD2 . ASP A 1 214 ? -0.23944  2.91815   48.16654 1.000 16.87710 ? 208 ASP A OD2 1 
ATOM   1725 N N   . ILE A 1 215 ? 0.15840   3.44826   53.66321 1.000 13.36498 ? 209 ILE A N   1 
ATOM   1726 C CA  . ILE A 1 215 ? -0.38842  3.23074   55.00138 1.000 14.27654 ? 209 ILE A CA  1 
ATOM   1727 C C   . ILE A 1 215 ? -0.28880  4.51199   55.82686 1.000 14.94080 ? 209 ILE A C   1 
ATOM   1728 O O   . ILE A 1 215 ? -1.19825  4.84239   56.60439 1.000 14.24032 ? 209 ILE A O   1 
ATOM   1729 C CB  . ILE A 1 215 ? 0.30244   2.03170   55.68084 1.000 14.79901 ? 209 ILE A CB  1 
ATOM   1730 C CG1 . ILE A 1 215 ? 0.00677   0.71956   54.92375 1.000 16.27670 ? 209 ILE A CG1 1 
ATOM   1731 C CG2 . ILE A 1 215 ? -0.12323  1.95373   57.16162 1.000 16.04993 ? 209 ILE A CG2 1 
ATOM   1732 C CD1 . ILE A 1 215 ? -1.47359  0.30302   55.03822 1.000 19.34283 ? 209 ILE A CD1 1 
ATOM   1733 N N   . TRP A 1 216 ? 0.82768   5.24732   55.69600 1.000 14.54641 ? 210 TRP A N   1 
ATOM   1734 C CA  . TRP A 1 216 ? 0.92968   6.54417   56.36387 1.000 13.20359 ? 210 TRP A CA  1 
ATOM   1735 C C   . TRP A 1 216 ? -0.23579  7.46591   55.97259 1.000 14.10399 ? 210 TRP A C   1 
ATOM   1736 O O   . TRP A 1 216 ? -0.89506  8.06761   56.83738 1.000 14.37536 ? 210 TRP A O   1 
ATOM   1737 C CB  . TRP A 1 216 ? 2.28603   7.20019   56.06441 1.000 13.51525 ? 210 TRP A CB  1 
ATOM   1738 C CG  . TRP A 1 216 ? 2.39590   8.51199   56.79861 1.000 12.77586 ? 210 TRP A CG  1 
ATOM   1739 C CD1 . TRP A 1 216 ? 1.96824   9.74016   56.36927 1.000 12.74644 ? 210 TRP A CD1 1 
ATOM   1740 C CD2 . TRP A 1 216 ? 2.91237   8.71564   58.13275 1.000 13.15752 ? 210 TRP A CD2 1 
ATOM   1741 N NE1 . TRP A 1 216 ? 2.22369   10.68951  57.32994 1.000 14.81202 ? 210 TRP A NE1 1 
ATOM   1742 C CE2 . TRP A 1 216 ? 2.79485   10.08632  58.42142 1.000 14.52789 ? 210 TRP A CE2 1 
ATOM   1743 C CE3 . TRP A 1 216 ? 3.48635   7.86432   59.10295 1.000 14.86440 ? 210 TRP A CE3 1 
ATOM   1744 C CZ2 . TRP A 1 216 ? 3.24021   10.64659  59.64649 1.000 15.95645 ? 210 TRP A CZ2 1 
ATOM   1745 C CZ3 . TRP A 1 216 ? 3.92055   8.43400   60.33998 1.000 16.51032 ? 210 TRP A CZ3 1 
ATOM   1746 C CH2 . TRP A 1 216 ? 3.79833   9.80162   60.57356 1.000 16.21971 ? 210 TRP A CH2 1 
ATOM   1747 N N   . SER A 1 217 ? -0.50731  7.58200   54.67137 1.000 14.21279 ? 211 SER A N   1 
ATOM   1748 C CA  . SER A 1 217 ? -1.60626  8.43328   54.24273 1.000 14.23874 ? 211 SER A CA  1 
ATOM   1749 C C   . SER A 1 217 ? -2.92664  7.99651   54.86735 1.000 15.38493 ? 211 SER A C   1 
ATOM   1750 O O   . SER A 1 217 ? -3.72478  8.84186   55.29611 1.000 15.24843 ? 211 SER A O   1 
ATOM   1751 C CB  . SER A 1 217 ? -1.70433  8.43396   52.70988 1.000 13.96722 ? 211 SER A CB  1 
ATOM   1752 O OG  . SER A 1 217 ? -0.47301  8.89583   52.14566 1.000 16.20404 ? 211 SER A OG  1 
ATOM   1753 N N   . VAL A 1 218 ? -3.16607  6.68816   54.93624 1.000 13.29334 ? 212 VAL A N   1 
ATOM   1754 C CA  . VAL A 1 218 ? -4.41688  6.20295   55.53092 1.000 14.78853 ? 212 VAL A CA  1 
ATOM   1755 C C   . VAL A 1 218 ? -4.49375  6.60582   56.99759 1.000 14.21290 ? 212 VAL A C   1 
ATOM   1756 O O   . VAL A 1 218 ? -5.55292  7.00721   57.48542 1.000 15.94991 ? 212 VAL A O   1 
ATOM   1757 C CB  . VAL A 1 218 ? -4.56886  4.68004   55.34493 1.000 14.46658 ? 212 VAL A CB  1 
ATOM   1758 C CG1 . VAL A 1 218 ? -5.82343  4.17222   56.09621 1.000 18.44379 ? 212 VAL A CG1 1 
ATOM   1759 C CG2 . VAL A 1 218 ? -4.68950  4.36215   53.85740 1.000 17.38784 ? 212 VAL A CG2 1 
ATOM   1760 N N   . GLY A 1 219 ? -3.37504  6.50340   57.71649 1.000 13.45034 ? 213 GLY A N   1 
ATOM   1761 C CA  . GLY A 1 219 ? -3.37008  6.94019   59.10443 1.000 14.46751 ? 213 GLY A CA  1 
ATOM   1762 C C   . GLY A 1 219 ? -3.69385  8.41823   59.24955 1.000 16.68955 ? 213 GLY A C   1 
ATOM   1763 O O   . GLY A 1 219 ? -4.45535  8.80724   60.14816 1.000 16.52781 ? 213 GLY A O   1 
ATOM   1764 N N   . CYS A 1 220 ? -3.16619  9.26562   58.33447 1.000 14.88507 ? 214 CYS A N   1 
ATOM   1765 C CA  . CYS A 1 220 ? -3.55107  10.67971  58.34120 1.000 15.82642 ? 214 CYS A CA  1 
ATOM   1766 C C   . CYS A 1 220 ? -5.05034  10.86975  58.08999 1.000 17.22402 ? 214 CYS A C   1 
ATOM   1767 O O   . CYS A 1 220 ? -5.68694  11.75253  58.69670 1.000 18.47060 ? 214 CYS A O   1 
ATOM   1768 C CB  . CYS A 1 220 ? -2.78423  11.45460  57.28173 1.000 14.52873 ? 214 CYS A CB  1 
ATOM   1769 S SG  . CYS A 1 220 ? -0.97224  11.51080  57.59996 1.000 18.23656 ? 214 CYS A SG  1 
ATOM   1770 N N   . ILE A 1 221 ? -5.62522  10.07054  57.19593 1.000 16.02728 ? 215 ILE A N   1 
ATOM   1771 C CA  . ILE A 1 221 ? -7.05804  10.16071  56.90894 1.000 14.92675 ? 215 ILE A CA  1 
ATOM   1772 C C   . ILE A 1 221 ? -7.87986  9.75435   58.12854 1.000 16.34122 ? 215 ILE A C   1 
ATOM   1773 O O   . ILE A 1 221 ? -8.89573  10.38692  58.45122 1.000 17.40669 ? 215 ILE A O   1 
ATOM   1774 C CB  . ILE A 1 221 ? -7.39282  9.32131   55.65805 1.000 15.70091 ? 215 ILE A CB  1 
ATOM   1775 C CG1 . ILE A 1 221 ? -6.75363  9.95460   54.41193 1.000 16.87032 ? 215 ILE A CG1 1 
ATOM   1776 C CG2 . ILE A 1 221 ? -8.93541  9.27243   55.47364 1.000 17.68842 ? 215 ILE A CG2 1 
ATOM   1777 C CD1 . ILE A 1 221 ? -6.63148  9.01312   53.23040 1.000 17.44292 ? 215 ILE A CD1 1 
ATOM   1778 N N   . LEU A 1 222 ? -7.49731  8.66279   58.78241 1.000 15.67258 ? 216 LEU A N   1 
ATOM   1779 C CA  . LEU A 1 222 ? -8.16825  8.24370   60.01299 1.000 16.54686 ? 216 LEU A CA  1 
ATOM   1780 C C   . LEU A 1 222 ? -8.16343  9.36299   61.05525 1.000 17.50893 ? 216 LEU A C   1 
ATOM   1781 O O   . LEU A 1 222 ? -9.20055  9.67787   61.66408 1.000 17.48676 ? 216 LEU A O   1 
ATOM   1782 C CB  . LEU A 1 222 ? -7.50362  6.97347   60.55623 1.000 16.30759 ? 216 LEU A CB  1 
ATOM   1783 C CG  . LEU A 1 222 ? -8.07713  6.52352   61.91986 1.000 16.30805 ? 216 LEU A CG  1 
ATOM   1784 C CD1 . LEU A 1 222 ? -9.61824  6.35128   61.87288 1.000 16.68911 ? 216 LEU A CD1 1 
ATOM   1785 C CD2 . LEU A 1 222 ? -7.39819  5.24428   62.40634 1.000 19.92935 ? 216 LEU A CD2 1 
ATOM   1786 N N   . ALA A 1 223 ? -6.99238  9.97553   61.29460 1.000 16.41887 ? 217 ALA A N   1 
ATOM   1787 C CA  . ALA A 1 223 ? -6.94942  11.06227  62.27023 1.000 18.72232 ? 217 ALA A CA  1 
ATOM   1788 C C   . ALA A 1 223 ? -7.89338  12.18928  61.88421 1.000 19.82226 ? 217 ALA A C   1 
ATOM   1789 O O   . ALA A 1 223 ? -8.59043  12.75770  62.74381 1.000 20.34621 ? 217 ALA A O   1 
ATOM   1790 C CB  . ALA A 1 223 ? -5.52643  11.58763  62.39629 1.000 19.60444 ? 217 ALA A CB  1 
ATOM   1791 N N   . GLU A 1 224 ? -7.95064  12.50624  60.58691 1.000 20.16658 ? 218 GLU A N   1 
ATOM   1792 C CA  . GLU A 1 224 ? -8.81554  13.57906  60.12496 1.000 20.14772 ? 218 GLU A CA  1 
ATOM   1793 C C   . GLU A 1 224 ? -10.30092 13.21599  60.29749 1.000 21.37821 ? 218 GLU A C   1 
ATOM   1794 O O   . GLU A 1 224 ? -11.12530 14.07766  60.65138 1.000 23.51566 ? 218 GLU A O   1 
ATOM   1795 C CB  . GLU A 1 224 ? -8.46752  13.89447  58.66969 1.000 21.68546 ? 218 GLU A CB  1 
ATOM   1796 C CG  . GLU A 1 224 ? -9.01472  15.17955  58.16816 1.000 23.75128 ? 218 GLU A CG  1 
ATOM   1797 C CD  . GLU A 1 224 ? -8.27953  15.71785  56.94799 1.000 25.86410 ? 218 GLU A CD  1 
ATOM   1798 O OE1 . GLU A 1 224 ? -7.12159  15.27353  56.65960 1.000 24.47038 ? 218 GLU A OE1 1 
ATOM   1799 O OE2 . GLU A 1 224 ? -8.87091  16.58571  56.27408 1.000 26.95242 ? 218 GLU A OE2 1 
ATOM   1800 N N   . MET A 1 225 ? -10.65845 11.94442  60.09458 1.000 19.13955 ? 219 MET A N   1 
ATOM   1801 C CA  . MET A 1 225 ? -12.04870 11.51641  60.33772 1.000 20.33018 ? 219 MET A CA  1 
ATOM   1802 C C   . MET A 1 225 ? -12.41931 11.62905  61.81707 1.000 21.77079 ? 219 MET A C   1 
ATOM   1803 O O   . MET A 1 225 ? -13.58954 11.87258  62.14517 1.000 24.14039 ? 219 MET A O   1 
ATOM   1804 C CB  . MET A 1 225 ? -12.20942 10.06524  59.88346 1.000 20.52924 ? 219 MET A CB  1 
ATOM   1805 C CG  . MET A 1 225 ? -12.07368 9.85177   58.42580 1.000 21.71645 ? 219 MET A CG  1 
ATOM   1806 S SD  . MET A 1 225 ? -12.89900 8.34430   57.85209 1.000 22.55230 ? 219 MET A SD  1 
ATOM   1807 C CE  . MET A 1 225 ? -11.49582 7.24186   58.18056 1.000 20.93159 ? 219 MET A CE  1 
ATOM   1808 N N   . LEU A 1 226 ? -11.44659 11.44479  62.71477 1.000 21.46501 ? 220 LEU A N   1 
ATOM   1809 C CA  . LEU A 1 226 ? -11.71468 11.51763  64.14468 1.000 24.75930 ? 220 LEU A CA  1 
ATOM   1810 C C   . LEU A 1 226 ? -11.94288 12.94241  64.63911 1.000 28.69786 ? 220 LEU A C   1 
ATOM   1811 O O   . LEU A 1 226 ? -12.56060 13.12383  65.69285 1.000 34.49248 ? 220 LEU A O   1 
ATOM   1812 C CB  . LEU A 1 226 ? -10.54221 10.89189  64.92531 1.000 23.16515 ? 220 LEU A CB  1 
ATOM   1813 C CG  . LEU A 1 226 ? -10.35915 9.36636   64.80630 1.000 23.20125 ? 220 LEU A CG  1 
ATOM   1814 C CD1 . LEU A 1 226 ? -8.97913  8.95238   65.34921 1.000 24.59139 ? 220 LEU A CD1 1 
ATOM   1815 C CD2 . LEU A 1 226 ? -11.48895 8.64158   65.54273 1.000 24.60371 ? 220 LEU A CD2 1 
ATOM   1816 N N   . SER A 1 227 ? -11.43549 13.95734  63.93705 1.000 29.36514 ? 221 SER A N   1 
ATOM   1817 C CA  . SER A 1 227 ? -11.48234 15.31790  64.44756 1.000 31.95714 ? 221 SER A CA  1 
ATOM   1818 C C   . SER A 1 227 ? -11.94474 16.36544  63.45118 1.000 30.16555 ? 221 SER A C   1 
ATOM   1819 O O   . SER A 1 227 ? -12.05104 17.53575  63.83368 1.000 31.71613 ? 221 SER A O   1 
ATOM   1820 C CB  . SER A 1 227 ? -10.09161 15.73666  64.94482 1.000 34.87322 ? 221 SER A CB  1 
ATOM   1821 O OG  . SER A 1 227 ? -9.20786  15.79170  63.82905 1.000 35.38835 ? 221 SER A OG  1 
ATOM   1822 N N   . ASN A 1 228 ? -12.15755 16.00181  62.18347 1.000 29.44818 ? 222 ASN A N   1 
ATOM   1823 C CA  . ASN A 1 228 ? -12.46980 16.95442  61.11467 1.000 30.42980 ? 222 ASN A CA  1 
ATOM   1824 C C   . ASN A 1 228 ? -11.40509 18.03557  60.93074 1.000 31.61474 ? 222 ASN A C   1 
ATOM   1825 O O   . ASN A 1 228 ? -11.73158 19.16503  60.54783 1.000 35.43861 ? 222 ASN A O   1 
ATOM   1826 C CB  . ASN A 1 228 ? -13.81837 17.62703  61.35323 1.000 29.66902 ? 222 ASN A CB  1 
ATOM   1827 C CG  . ASN A 1 228 ? -14.96689 16.65198  61.29399 1.000 32.35611 ? 222 ASN A CG  1 
ATOM   1828 O OD1 . ASN A 1 228 ? -15.24989 15.93755  62.27067 1.000 35.84557 ? 222 ASN A OD1 1 
ATOM   1829 N ND2 . ASN A 1 228 ? -15.63836 16.60859  60.15218 1.000 32.06630 ? 222 ASN A ND2 1 
ATOM   1830 N N   . ARG A 1 229 ? -10.13451 17.73626  61.21789 1.000 28.96210 ? 223 ARG A N   1 
ATOM   1831 C CA  . ARG A 1 229 ? -9.06466  18.64122  60.87691 1.000 30.90115 ? 223 ARG A CA  1 
ATOM   1832 C C   . ARG A 1 229 ? -7.83374  17.81509  60.54541 1.000 25.73932 ? 223 ARG A C   1 
ATOM   1833 O O   . ARG A 1 229 ? -7.66298  16.72485  61.10505 1.000 24.57378 ? 223 ARG A O   1 
ATOM   1834 C CB  . ARG A 1 229 ? -8.78928  19.64050  62.01506 1.000 35.67219 ? 223 ARG A CB  1 
ATOM   1835 C CG  . ARG A 1 229 ? -8.14726  19.06892  63.26788 1.000 42.67516 ? 223 ARG A CG  1 
ATOM   1836 C CD  . ARG A 1 229 ? -7.35224  20.13791  63.98780 0.700 48.19907 ? 223 ARG A CD  1 
ATOM   1837 N NE  . ARG A 1 229 ? -6.76162  21.02576  63.00105 0.600 52.63162 ? 223 ARG A NE  1 
ATOM   1838 C CZ  . ARG A 1 229 ? -5.50249  20.94916  62.59067 0.600 53.65404 ? 223 ARG A CZ  1 
ATOM   1839 N NH1 . ARG A 1 229 ? -4.61909  20.18579  63.21093 0.600 53.78016 ? 223 ARG A NH1 1 
ATOM   1840 N NH2 . ARG A 1 229 ? -5.12143  21.65850  61.53435 0.600 55.11267 ? 223 ARG A NH2 1 
ATOM   1841 N N   . PRO A 1 230 ? -7.02308  18.25008  59.59118 1.000 24.68087 ? 224 PRO A N   1 
ATOM   1842 C CA  . PRO A 1 230 ? -5.79242  17.50301  59.28309 1.000 25.65952 ? 224 PRO A CA  1 
ATOM   1843 C C   . PRO A 1 230 ? -4.87852  17.40867  60.50367 1.000 24.67192 ? 224 PRO A C   1 
ATOM   1844 O O   . PRO A 1 230 ? -4.72465  18.36533  61.26535 1.000 24.99466 ? 224 PRO A O   1 
ATOM   1845 C CB  . PRO A 1 230 ? -5.15376  18.31031  58.14669 1.000 28.77556 ? 224 PRO A CB  1 
ATOM   1846 C CG  . PRO A 1 230 ? -5.79280  19.65503  58.20922 1.000 28.61058 ? 224 PRO A CG  1 
ATOM   1847 C CD  . PRO A 1 230 ? -7.19380  19.43433  58.72609 1.000 26.59813 ? 224 PRO A CD  1 
ATOM   1848 N N   . ILE A 1 231 ? -4.29781  16.22434  60.70323 1.000 23.18734 ? 225 ILE A N   1 
ATOM   1849 C CA  . ILE A 1 231 ? -3.45273  16.02951  61.87610 1.000 23.48059 ? 225 ILE A CA  1 
ATOM   1850 C C   . ILE A 1 231 ? -2.07983  16.69494  61.70092 1.000 23.51447 ? 225 ILE A C   1 
ATOM   1851 O O   . ILE A 1 231 ? -1.52559  17.22867  62.67398 1.000 22.94532 ? 225 ILE A O   1 
ATOM   1852 C CB  A ILE A 1 231 ? -3.32817  14.53457  62.22260 0.440 22.82911 ? 225 ILE A CB  1 
ATOM   1853 C CB  B ILE A 1 231 ? -3.33460  14.52479  62.21211 0.560 23.81624 ? 225 ILE A CB  1 
ATOM   1854 C CG1 A ILE A 1 231 ? -2.41556  14.35371  63.44134 0.440 21.54434 ? 225 ILE A CG1 1 
ATOM   1855 C CG1 B ILE A 1 231 ? -2.50767  14.30153  63.48666 0.560 25.67042 ? 225 ILE A CG1 1 
ATOM   1856 C CG2 A ILE A 1 231 ? -2.83521  13.70137  61.01788 0.440 22.76785 ? 225 ILE A CG2 1 
ATOM   1857 C CG2 B ILE A 1 231 ? -2.70504  13.68964  61.05116 0.560 21.62692 ? 225 ILE A CG2 1 
ATOM   1858 C CD1 A ILE A 1 231 ? -2.33422  12.95637  63.91468 0.440 19.90814 ? 225 ILE A CD1 1 
ATOM   1859 C CD1 B ILE A 1 231 ? -3.16543  14.82191  64.74476 0.560 26.15903 ? 225 ILE A CD1 1 
ATOM   1860 N N   . PHE A 1 232 ? -1.53672  16.74406  60.48308 1.000 23.69267 ? 226 PHE A N   1 
ATOM   1861 C CA  . PHE A 1 232 ? -0.20133  17.29638  60.22699 1.000 22.18733 ? 226 PHE A CA  1 
ATOM   1862 C C   . PHE A 1 232 ? -0.26873  18.38228  59.15341 1.000 23.92211 ? 226 PHE A C   1 
ATOM   1863 O O   . PHE A 1 232 ? 0.16273   18.16976  58.01426 1.000 22.50364 ? 226 PHE A O   1 
ATOM   1864 C CB  . PHE A 1 232 ? 0.77181   16.19926  59.79100 1.000 20.08592 ? 226 PHE A CB  1 
ATOM   1865 C CG  . PHE A 1 232 ? 0.85601   15.04354  60.71771 1.000 19.23757 ? 226 PHE A CG  1 
ATOM   1866 C CD1 . PHE A 1 232 ? 1.21290   15.23308  62.06795 1.000 19.95246 ? 226 PHE A CD1 1 
ATOM   1867 C CD2 . PHE A 1 232 ? 0.70389   13.74498  60.22955 1.000 18.30208 ? 226 PHE A CD2 1 
ATOM   1868 C CE1 . PHE A 1 232 ? 1.34937   14.14364  62.92715 1.000 20.14601 ? 226 PHE A CE1 1 
ATOM   1869 C CE2 . PHE A 1 232 ? 0.83860   12.63144  61.09040 1.000 18.15180 ? 226 PHE A CE2 1 
ATOM   1870 C CZ  . PHE A 1 232 ? 1.16668   12.83498  62.45359 1.000 20.27838 ? 226 PHE A CZ  1 
ATOM   1871 N N   . PRO A 1 233 ? -0.78813  19.57235  59.48442 1.000 26.42441 ? 227 PRO A N   1 
ATOM   1872 C CA  . PRO A 1 233 ? -1.03287  20.57305  58.41374 1.000 28.96128 ? 227 PRO A CA  1 
ATOM   1873 C C   . PRO A 1 233 ? 0.17590   21.46176  58.14238 1.000 28.96333 ? 227 PRO A C   1 
ATOM   1874 O O   . PRO A 1 233 ? 0.17764   22.67077  58.40921 1.000 31.18103 ? 227 PRO A O   1 
ATOM   1875 C CB  . PRO A 1 233 ? -2.22104  21.35545  58.96893 1.000 31.21701 ? 227 PRO A CB  1 
ATOM   1876 C CG  . PRO A 1 233 ? -1.99664  21.33780  60.45298 1.000 32.74094 ? 227 PRO A CG  1 
ATOM   1877 C CD  . PRO A 1 233 ? -1.41737  19.97256  60.76132 1.000 31.25587 ? 227 PRO A CD  1 
ATOM   1878 N N   . GLY A 1 234 ? 1.22875   20.86054  57.59657 1.000 28.58167 ? 228 GLY A N   1 
ATOM   1879 C CA  . GLY A 1 234 ? 2.44188   21.62419  57.33742 1.000 26.53218 ? 228 GLY A CA  1 
ATOM   1880 C C   . GLY A 1 234 ? 2.16871   22.73573  56.34005 1.000 31.60824 ? 228 GLY A C   1 
ATOM   1881 O O   . GLY A 1 234 ? 1.36006   22.58142  55.41929 1.000 33.38432 ? 228 GLY A O   1 
ATOM   1882 N N   . LYS A 1 235 ? 2.80764   23.89162  56.56318 1.000 33.05261 ? 229 LYS A N   1 
ATOM   1883 C CA  . LYS A 1 235 ? 2.55354   25.04319  55.71473 1.000 35.57015 ? 229 LYS A CA  1 
ATOM   1884 C C   . LYS A 1 235 ? 3.44952   25.06630  54.48629 1.000 36.23599 ? 229 LYS A C   1 
ATOM   1885 O O   . LYS A 1 235 ? 3.21670   25.88178  53.58417 1.000 40.00948 ? 229 LYS A O   1 
ATOM   1886 C CB  . LYS A 1 235 ? 2.71987   26.35232  56.50603 1.000 36.86822 ? 229 LYS A CB  1 
ATOM   1887 C CG  . LYS A 1 235 ? 1.91266   26.43440  57.79379 0.700 38.67470 ? 229 LYS A CG  1 
ATOM   1888 C CD  . LYS A 1 235 ? 1.14143   27.74093  57.87678 0.700 40.23987 ? 229 LYS A CD  1 
ATOM   1889 C CE  . LYS A 1 235 ? 0.88221   28.15848  59.31657 0.600 42.35522 ? 229 LYS A CE  1 
ATOM   1890 N NZ  . LYS A 1 235 ? 0.18205   27.10954  60.08963 0.600 43.29754 ? 229 LYS A NZ  1 
ATOM   1891 N N   . HIS A 1 236 ? 4.44996   24.19616  54.42799 1.000 35.87063 ? 230 HIS A N   1 
ATOM   1892 C CA  . HIS A 1 236 ? 5.38458   24.09512  53.30895 1.000 37.33880 ? 230 HIS A CA  1 
ATOM   1893 C C   . HIS A 1 236 ? 6.18608   22.81437  53.51311 1.000 36.75975 ? 230 HIS A C   1 
ATOM   1894 O O   . HIS A 1 236 ? 6.02566   22.14561  54.52842 1.000 34.16736 ? 230 HIS A O   1 
ATOM   1895 C CB  . HIS A 1 236 ? 6.28778   25.32794  53.18697 1.000 39.25865 ? 230 HIS A CB  1 
ATOM   1896 C CG  . HIS A 1 236 ? 6.97892   25.70384  54.46087 1.000 38.74292 ? 230 HIS A CG  1 
ATOM   1897 N ND1 . HIS A 1 236 ? 8.12019   25.06859  54.90085 1.000 39.04619 ? 230 HIS A ND1 1 
ATOM   1898 C CD2 . HIS A 1 236 ? 6.71165   26.67593  55.37044 1.000 35.91940 ? 230 HIS A CD2 1 
ATOM   1899 C CE1 . HIS A 1 236 ? 8.50421   25.60736  56.04668 1.000 38.59903 ? 230 HIS A CE1 1 
ATOM   1900 N NE2 . HIS A 1 236 ? 7.68033   26.60007  56.34162 1.000 37.67671 ? 230 HIS A NE2 1 
ATOM   1901 N N   A TYR A 1 237 ? 7.19752   22.56305  52.65641 0.500 38.20423 ? 231 TYR A N   1 
ATOM   1902 N N   B TYR A 1 237 ? 6.89467   22.42701  52.44197 0.500 36.96511 ? 231 TYR A N   1 
ATOM   1903 C CA  A TYR A 1 237 ? 7.89632   21.25224  52.59279 0.500 36.74971 ? 231 TYR A CA  1 
ATOM   1904 C CA  B TYR A 1 237 ? 7.60574   21.15080  52.39918 0.500 35.64262 ? 231 TYR A CA  1 
ATOM   1905 C C   A TYR A 1 237 ? 8.50426   20.65713  53.88465 0.500 30.76565 ? 231 TYR A C   1 
ATOM   1906 C C   B TYR A 1 237 ? 8.41270   20.95269  53.65205 0.500 32.47593 ? 231 TYR A C   1 
ATOM   1907 O O   A TYR A 1 237 ? 8.03721   19.60873  54.35017 0.500 27.63335 ? 231 TYR A O   1 
ATOM   1908 O O   B TYR A 1 237 ? 8.46519   19.84918  54.21144 0.500 31.29423 ? 231 TYR A O   1 
ATOM   1909 C CB  A TYR A 1 237 ? 9.02498   21.30696  51.54927 0.500 38.62071 ? 231 TYR A CB  1 
ATOM   1910 C CB  B TYR A 1 237 ? 8.54522   21.10775  51.19512 0.500 37.27535 ? 231 TYR A CB  1 
ATOM   1911 C CG  A TYR A 1 237 ? 9.70813   19.96668  51.27397 0.500 38.60660 ? 231 TYR A CG  1 
ATOM   1912 C CG  B TYR A 1 237 ? 9.35964   19.84499  51.07337 0.500 38.51039 ? 231 TYR A CG  1 
ATOM   1913 C CD1 A TYR A 1 237 ? 9.21401   19.09109  50.30579 0.500 39.28252 ? 231 TYR A CD1 1 
ATOM   1914 C CD1 B TYR A 1 237 ? 8.83891   18.72556  50.43807 0.500 38.36474 ? 231 TYR A CD1 1 
ATOM   1915 C CD2 A TYR A 1 237 ? 10.81919  19.55656  52.01290 0.500 38.10229 ? 231 TYR A CD2 1 
ATOM   1916 C CD2 B TYR A 1 237 ? 10.66034  19.77959  51.56288 0.500 39.96633 ? 231 TYR A CD2 1 
ATOM   1917 C CE1 A TYR A 1 237 ? 9.83846   17.86416  50.04623 0.500 38.60390 ? 231 TYR A CE1 1 
ATOM   1918 C CE1 B TYR A 1 237 ? 9.58284   17.56846  50.30902 0.500 39.35302 ? 231 TYR A CE1 1 
ATOM   1919 C CE2 A TYR A 1 237 ? 11.43730  18.32994  51.77673 0.500 38.06347 ? 231 TYR A CE2 1 
ATOM   1920 C CE2 B TYR A 1 237 ? 11.41791  18.62348  51.44108 0.500 40.78811 ? 231 TYR A CE2 1 
ATOM   1921 C CZ  A TYR A 1 237 ? 10.94975  17.49092  50.78333 0.500 38.39540 ? 231 TYR A CZ  1 
ATOM   1922 C CZ  B TYR A 1 237 ? 10.88072  17.51998  50.80299 0.500 40.25810 ? 231 TYR A CZ  1 
ATOM   1923 O OH  A TYR A 1 237 ? 11.56116  16.27320  50.55178 0.500 37.85120 ? 231 TYR A OH  1 
ATOM   1924 O OH  B TYR A 1 237 ? 11.63099  16.36487  50.68238 0.500 39.94758 ? 231 TYR A OH  1 
ATOM   1925 N N   A LEU A 1 238 ? 9.61261   21.23137  54.41576 0.500 28.91288 ? 232 LEU A N   1 
ATOM   1926 N N   B LEU A 1 238 ? 9.05637   22.02459  54.10175 0.500 30.54061 ? 232 LEU A N   1 
ATOM   1927 C CA  A LEU A 1 238 ? 10.25774  20.70310  55.62643 0.500 28.56313 ? 232 LEU A CA  1 
ATOM   1928 C CA  B LEU A 1 238 ? 9.95267   21.91077  55.22374 0.500 26.75534 ? 232 LEU A CA  1 
ATOM   1929 C C   A LEU A 1 238 ? 9.39447   20.91561  56.86443 0.500 25.93088 ? 232 LEU A C   1 
ATOM   1930 C C   B LEU A 1 238 ? 9.22684   22.01443  56.55559 0.500 26.17330 ? 232 LEU A C   1 
ATOM   1931 O O   A LEU A 1 238 ? 9.52151   20.16321  57.84152 0.500 23.19767 ? 232 LEU A O   1 
ATOM   1932 O O   B LEU A 1 238 ? 9.82213   21.68292  57.58246 0.500 28.70156 ? 232 LEU A O   1 
ATOM   1933 C CB  A LEU A 1 238 ? 11.63481  21.35632  55.85999 0.500 30.06584 ? 232 LEU A CB  1 
ATOM   1934 C CB  B LEU A 1 238 ? 11.08519  22.94216  55.09187 0.500 25.85553 ? 232 LEU A CB  1 
ATOM   1935 C CG  A LEU A 1 238 ? 12.59024  20.72939  56.89546 0.500 29.50561 ? 232 LEU A CG  1 
ATOM   1936 C CG  B LEU A 1 238 ? 11.74267  23.02454  53.70274 0.500 24.61710 ? 232 LEU A CG  1 
ATOM   1937 C CD1 A LEU A 1 238 ? 12.62469  19.19840  56.76408 0.500 31.44973 ? 232 LEU A CD1 1 
ATOM   1938 C CD1 B LEU A 1 238 ? 12.22642  24.42208  53.35850 0.500 25.17655 ? 232 LEU A CD1 1 
ATOM   1939 C CD2 A LEU A 1 238 ? 14.02473  21.33263  56.92631 0.500 30.75437 ? 232 LEU A CD2 1 
ATOM   1940 C CD2 B LEU A 1 238 ? 12.88000  22.03066  53.63317 0.500 22.81740 ? 232 LEU A CD2 1 
ATOM   1941 N N   A ASP A 1 239 ? 8.51930   21.92560  56.83398 0.500 28.00540 ? 233 ASP A N   1 
ATOM   1942 N N   B ASP A 1 239 ? 7.94418   22.40451  56.56396 0.500 26.71853 ? 233 ASP A N   1 
ATOM   1943 C CA  A ASP A 1 239 ? 7.56608   22.14686  57.91742 0.500 26.97619 ? 233 ASP A CA  1 
ATOM   1944 C CA  B ASP A 1 239 ? 7.16699   22.39402  57.79703 0.500 25.39605 ? 233 ASP A CA  1 
ATOM   1945 C C   A ASP A 1 239 ? 6.69509   20.92294  58.15575 0.500 23.34044 ? 233 ASP A C   1 
ATOM   1946 C C   B ASP A 1 239 ? 6.55891   21.02857  58.10576 0.500 24.57262 ? 233 ASP A C   1 
ATOM   1947 O O   A ASP A 1 239 ? 6.22180   20.70202  59.26794 0.500 22.39839 ? 233 ASP A O   1 
ATOM   1948 O O   B ASP A 1 239 ? 6.21679   20.77126  59.25719 0.500 27.18196 ? 233 ASP A O   1 
ATOM   1949 C CB  A ASP A 1 239 ? 6.67377   23.34599  57.59718 0.500 29.42939 ? 233 ASP A CB  1 
ATOM   1950 C CB  B ASP A 1 239 ? 6.04461   23.44399  57.73185 0.500 24.61370 ? 233 ASP A CB  1 
ATOM   1951 C CG  A ASP A 1 239 ? 5.86567   23.81029  58.79072 0.500 30.69792 ? 233 ASP A CG  1 
ATOM   1952 C CG  B ASP A 1 239 ? 5.48740   23.79697  59.10498 0.500 25.63196 ? 233 ASP A CG  1 
ATOM   1953 O OD1 A ASP A 1 239 ? 6.44136   23.92898  59.89607 0.500 31.70745 ? 233 ASP A OD1 1 
ATOM   1954 O OD1 B ASP A 1 239 ? 6.28898   23.90242  60.05713 0.500 25.38062 ? 233 ASP A OD1 1 
ATOM   1955 O OD2 A ASP A 1 239 ? 4.64401   24.02580  58.63176 0.500 29.64536 ? 233 ASP A OD2 1 
ATOM   1956 O OD2 B ASP A 1 239 ? 4.25818   24.00803  59.22969 0.500 25.92536 ? 233 ASP A OD2 1 
ATOM   1957 N N   . GLN A 1 240 ? 6.44043   20.14150  57.11714 1.000 21.13428 ? 234 GLN A N   1 
ATOM   1958 C CA  . GLN A 1 240 ? 5.64259   18.93046  57.30287 1.000 20.10016 ? 234 GLN A CA  1 
ATOM   1959 C C   . GLN A 1 240 ? 6.26823   17.99903  58.32707 1.000 21.35977 ? 234 GLN A C   1 
ATOM   1960 O O   . GLN A 1 240 ? 5.57284   17.47967  59.21491 1.000 22.45608 ? 234 GLN A O   1 
ATOM   1961 C CB  . GLN A 1 240 ? 5.46658   18.23930  55.95640 1.000 19.84887 ? 234 GLN A CB  1 
ATOM   1962 C CG  . GLN A 1 240 ? 4.49368   17.08654  56.00174 1.000 20.71262 ? 234 GLN A CG  1 
ATOM   1963 C CD  . GLN A 1 240 ? 3.08717   17.53921  56.40340 1.000 21.89533 ? 234 GLN A CD  1 
ATOM   1964 O OE1 . GLN A 1 240 ? 2.68888   18.68837  56.15937 1.000 23.42307 ? 234 GLN A OE1 1 
ATOM   1965 N NE2 . GLN A 1 240 ? 2.36512   16.66206  57.06115 1.000 20.47006 ? 234 GLN A NE2 1 
ATOM   1966 N N   . LEU A 1 241 ? 7.59718   17.84005  58.27031 1.000 22.70682 ? 235 LEU A N   1 
ATOM   1967 C CA  . LEU A 1 241 ? 8.27145   16.99195  59.25869 0.850 23.44746 ? 235 LEU A CA  1 
ATOM   1968 C C   . LEU A 1 241 ? 8.18619   17.57201  60.67503 1.000 24.63841 ? 235 LEU A C   1 
ATOM   1969 O O   . LEU A 1 241 ? 8.09041   16.79432  61.64405 1.000 24.65573 ? 235 LEU A O   1 
ATOM   1970 C CB  . LEU A 1 241 ? 9.73498   16.76713  58.84328 1.000 25.92955 ? 235 LEU A CB  1 
ATOM   1971 C CG  . LEU A 1 241 ? 10.58894  15.75650  59.59746 1.000 28.96274 ? 235 LEU A CG  1 
ATOM   1972 C CD1 . LEU A 1 241 ? 10.04181  14.34187  59.54315 1.000 29.79632 ? 235 LEU A CD1 1 
ATOM   1973 C CD2 . LEU A 1 241 ? 11.98357  15.80565  58.98499 1.000 28.24491 ? 235 LEU A CD2 1 
ATOM   1974 N N   . ASN A 1 242 ? 8.21109   18.91119  60.81178 1.000 26.42904 ? 236 ASN A N   1 
ATOM   1975 C CA  . ASN A 1 242 ? 8.02124   19.57746  62.11266 1.000 27.63210 ? 236 ASN A CA  1 
ATOM   1976 C C   . ASN A 1 242 ? 6.71477   19.12926  62.75671 1.000 25.31135 ? 236 ASN A C   1 
ATOM   1977 O O   . ASN A 1 242 ? 6.64822   18.84465  63.96299 1.000 25.75866 ? 236 ASN A O   1 
ATOM   1978 C CB  . ASN A 1 242 ? 7.93001   21.11682  61.96541 0.700 25.43482 ? 236 ASN A CB  1 
ATOM   1979 C CG  . ASN A 1 242 ? 9.21960   21.81067  61.51074 0.700 26.40288 ? 236 ASN A CG  1 
ATOM   1980 O OD1 . ASN A 1 242 ? 10.33682  21.29639  61.64559 0.700 28.63557 ? 236 ASN A OD1 1 
ATOM   1981 N ND2 . ASN A 1 242 ? 9.04452   23.03121  60.94510 0.700 25.05669 ? 236 ASN A ND2 1 
ATOM   1982 N N   . HIS A 1 243 ? 5.63345   19.13808  61.97618 1.000 23.02101 ? 237 HIS A N   1 
ATOM   1983 C CA  . HIS A 1 243 ? 4.33437   18.73719  62.51100 1.000 23.38493 ? 237 HIS A CA  1 
ATOM   1984 C C   . HIS A 1 243 ? 4.32055   17.26802  62.90558 1.000 21.59649 ? 237 HIS A C   1 
ATOM   1985 O O   . HIS A 1 243 ? 3.79412   16.91145  63.96773 1.000 22.06042 ? 237 HIS A O   1 
ATOM   1986 C CB  . HIS A 1 243 ? 3.22678   19.02073  61.48472 1.000 23.42876 ? 237 HIS A CB  1 
ATOM   1987 C CG  . HIS A 1 243 ? 2.84252   20.46296  61.38421 1.000 26.44796 ? 237 HIS A CG  1 
ATOM   1988 N ND1 . HIS A 1 243 ? 1.78005   20.99817  62.08301 1.000 30.51260 ? 237 HIS A ND1 1 
ATOM   1989 C CD2 . HIS A 1 243 ? 3.42216   21.49719  60.72839 1.000 28.93644 ? 237 HIS A CD2 1 
ATOM   1990 C CE1 . HIS A 1 243 ? 1.70004   22.29433  61.83152 1.000 31.80259 ? 237 HIS A CE1 1 
ATOM   1991 N NE2 . HIS A 1 243 ? 2.68014   22.61957  61.00594 1.000 30.43882 ? 237 HIS A NE2 1 
ATOM   1992 N N   . ILE A 1 244 ? 4.89323   16.39658  62.07377 1.000 19.51988 ? 238 ILE A N   1 
ATOM   1993 C CA  . ILE A 1 244 ? 4.92288   14.96795  62.39283 1.000 17.54479 ? 238 ILE A CA  1 
ATOM   1994 C C   . ILE A 1 244 ? 5.68377   14.73062  63.69025 1.000 20.58271 ? 238 ILE A C   1 
ATOM   1995 O O   . ILE A 1 244 ? 5.19775   14.05052  64.61481 1.000 20.80655 ? 238 ILE A O   1 
ATOM   1996 C CB  . ILE A 1 244 ? 5.53075   14.17839  61.21849 1.000 17.06201 ? 238 ILE A CB  1 
ATOM   1997 C CG1 . ILE A 1 244 ? 4.58377   14.29229  60.00024 1.000 17.65876 ? 238 ILE A CG1 1 
ATOM   1998 C CG2 . ILE A 1 244 ? 5.75122   12.73258  61.61568 1.000 18.29113 ? 238 ILE A CG2 1 
ATOM   1999 C CD1 . ILE A 1 244 ? 5.20937   13.71468  58.69957 1.000 18.84912 ? 238 ILE A CD1 1 
ATOM   2000 N N   . LEU A 1 245 ? 6.89467   15.28159  63.77682 1.000 20.95092 ? 239 LEU A N   1 
ATOM   2001 C CA  . LEU A 1 245 ? 7.70298   15.07950  64.98175 1.000 21.36728 ? 239 LEU A CA  1 
ATOM   2002 C C   . LEU A 1 245 ? 7.10577   15.76652  66.20838 1.000 23.32921 ? 239 LEU A C   1 
ATOM   2003 O O   . LEU A 1 245 ? 7.34232   15.31773  67.34231 1.000 23.21884 ? 239 LEU A O   1 
ATOM   2004 C CB  . LEU A 1 245 ? 9.13660   15.56163  64.72544 1.000 22.12024 ? 239 LEU A CB  1 
ATOM   2005 C CG  . LEU A 1 245 ? 9.88677   14.77159  63.63972 1.000 24.45657 ? 239 LEU A CG  1 
ATOM   2006 C CD1 . LEU A 1 245 ? 11.30622  15.32464  63.37620 1.000 27.63022 ? 239 LEU A CD1 1 
ATOM   2007 C CD2 . LEU A 1 245 ? 9.95528   13.28215  63.97654 1.000 28.60099 ? 239 LEU A CD2 1 
ATOM   2008 N N   . GLY A 1 246 ? 6.32435   16.83714  66.01272 1.000 23.23720 ? 240 GLY A N   1 
ATOM   2009 C CA  . GLY A 1 246 ? 5.69030   17.50175  67.13694 1.000 23.80546 ? 240 GLY A CA  1 
ATOM   2010 C C   . GLY A 1 246 ? 4.69024   16.62946  67.86323 1.000 24.44020 ? 240 GLY A C   1 
ATOM   2011 O O   . GLY A 1 246 ? 4.40581   16.87022  69.04075 1.000 26.53314 ? 240 GLY A O   1 
ATOM   2012 N N   . ILE A 1 247 ? 4.13501   15.62826  67.18861 1.000 22.46712 ? 241 ILE A N   1 
ATOM   2013 C CA  . ILE A 1 247 ? 3.17836   14.71043  67.80395 1.000 22.62418 ? 241 ILE A CA  1 
ATOM   2014 C C   . ILE A 1 247 ? 3.82060   13.36786  68.14827 1.000 20.92867 ? 241 ILE A C   1 
ATOM   2015 O O   . ILE A 1 247 ? 3.62105   12.82789  69.24813 1.000 21.03599 ? 241 ILE A O   1 
ATOM   2016 C CB  . ILE A 1 247 ? 1.95925   14.55350  66.86623 1.000 23.34713 ? 241 ILE A CB  1 
ATOM   2017 C CG1 . ILE A 1 247 ? 1.14228   15.85144  66.95803 1.000 29.48338 ? 241 ILE A CG1 1 
ATOM   2018 C CG2 . ILE A 1 247 ? 1.11309   13.31775  67.21577 1.000 23.97546 ? 241 ILE A CG2 1 
ATOM   2019 C CD1 . ILE A 1 247 ? 0.01310   15.95503  65.96382 1.000 33.41546 ? 241 ILE A CD1 1 
ATOM   2020 N N   . LEU A 1 248 ? 4.57522   12.78787  67.20625 1.000 20.77194 ? 242 LEU A N   1 
ATOM   2021 C CA  . LEU A 1 248 ? 5.21591   11.50002  67.45528 1.000 19.86837 ? 242 LEU A CA  1 
ATOM   2022 C C   . LEU A 1 248 ? 6.35121   11.60602  68.46412 1.000 21.02614 ? 242 LEU A C   1 
ATOM   2023 O O   . LEU A 1 248 ? 6.70356   10.59906  69.08164 1.000 23.90977 ? 242 LEU A O   1 
ATOM   2024 C CB  A LEU A 1 248 ? 5.75213   10.90557  66.14251 0.500 18.61486 ? 242 LEU A CB  1 
ATOM   2025 C CB  B LEU A 1 248 ? 5.78263   10.90346  66.15864 0.500 18.27748 ? 242 LEU A CB  1 
ATOM   2026 C CG  A LEU A 1 248 ? 4.77628   9.97427   65.41008 0.500 18.11527 ? 242 LEU A CG  1 
ATOM   2027 C CG  B LEU A 1 248 ? 4.75406   10.46508  65.12235 0.500 17.70102 ? 242 LEU A CG  1 
ATOM   2028 C CD1 A LEU A 1 248 ? 3.49856   10.71916  64.98257 0.500 18.32602 ? 242 LEU A CD1 1 
ATOM   2029 C CD1 B LEU A 1 248 ? 5.45253   9.68621   64.01269 0.500 18.46204 ? 242 LEU A CD1 1 
ATOM   2030 C CD2 A LEU A 1 248 ? 5.46208   9.29521   64.23679 0.500 18.65864 ? 242 LEU A CD2 1 
ATOM   2031 C CD2 B LEU A 1 248 ? 3.65446   9.65388   65.77990 0.500 18.64415 ? 242 LEU A CD2 1 
ATOM   2032 N N   . GLY A 1 249 ? 6.94218   12.77886  68.61374 1.000 20.32560 ? 243 GLY A N   1 
ATOM   2033 C CA  . GLY A 1 249 ? 8.13293   12.91531  69.43163 1.000 21.76437 ? 243 GLY A CA  1 
ATOM   2034 C C   . GLY A 1 249 ? 9.36043   12.44471  68.67234 1.000 22.50337 ? 243 GLY A C   1 
ATOM   2035 O O   . GLY A 1 249 ? 9.30285   12.00944  67.50736 1.000 23.36895 ? 243 GLY A O   1 
ATOM   2036 N N   . SER A 1 250 ? 10.50070  12.53955  69.35951 1.000 21.29364 ? 244 SER A N   1 
ATOM   2037 C CA  . SER A 1 250 ? 11.78140  12.20891  68.75438 1.000 21.03324 ? 244 SER A CA  1 
ATOM   2038 C C   . SER A 1 250 ? 11.85418  10.72700  68.39024 1.000 21.75028 ? 244 SER A C   1 
ATOM   2039 O O   . SER A 1 250 ? 11.46918  9.86823   69.19373 1.000 22.83479 ? 244 SER A O   1 
ATOM   2040 C CB  . SER A 1 250 ? 12.91885  12.52178  69.72869 1.000 21.37958 ? 244 SER A CB  1 
ATOM   2041 O OG  . SER A 1 250 ? 12.93002  13.88255  70.07170 1.000 23.26317 ? 244 SER A OG  1 
ATOM   2042 N N   . PRO A 1 251 ? 12.41562  10.39087  67.22733 1.000 20.50905 ? 245 PRO A N   1 
ATOM   2043 C CA  . PRO A 1 251 ? 12.64048  8.97522   66.90265 1.000 19.67480 ? 245 PRO A CA  1 
ATOM   2044 C C   . PRO A 1 251 ? 13.63919  8.32811   67.85605 1.000 21.23985 ? 245 PRO A C   1 
ATOM   2045 O O   . PRO A 1 251 ? 14.60197  8.95927   68.31871 1.000 21.72165 ? 245 PRO A O   1 
ATOM   2046 C CB  . PRO A 1 251 ? 13.20478  9.02291   65.47604 1.000 22.19855 ? 245 PRO A CB  1 
ATOM   2047 C CG  . PRO A 1 251 ? 12.88404  10.33036  64.98156 1.000 25.66866 ? 245 PRO A CG  1 
ATOM   2048 C CD  . PRO A 1 251 ? 12.79829  11.26963  66.10188 1.000 22.32475 ? 245 PRO A CD  1 
ATOM   2049 N N   . SER A 1 252 ? 13.41041  7.04070   68.10480 1.000 21.46474 ? 246 SER A N   1 
ATOM   2050 C CA  . SER A 1 252 ? 14.26790  6.20790   68.92943 1.000 21.11772 ? 246 SER A CA  1 
ATOM   2051 C C   . SER A 1 252 ? 15.63670  6.01471   68.26520 1.000 22.23024 ? 246 SER A C   1 
ATOM   2052 O O   . SER A 1 252 ? 15.82019  6.23332   67.05881 1.000 24.30653 ? 246 SER A O   1 
ATOM   2053 C CB  . SER A 1 252 ? 13.60124  4.85071   69.17485 1.000 23.44617 ? 246 SER A CB  1 
ATOM   2054 O OG  . SER A 1 252 ? 13.56171  4.09268   67.97579 1.000 23.29770 ? 246 SER A OG  1 
ATOM   2055 N N   . GLN A 1 253 ? 16.62398  5.63899   69.08291 1.000 24.35823 ? 247 GLN A N   1 
ATOM   2056 C CA  . GLN A 1 253 ? 17.93102  5.30610   68.52150 1.000 26.95132 ? 247 GLN A CA  1 
ATOM   2057 C C   . GLN A 1 253 ? 17.81274  4.23147   67.45316 1.000 27.39569 ? 247 GLN A C   1 
ATOM   2058 O O   . GLN A 1 253 ? 18.45423  4.31646   66.40308 1.000 25.79451 ? 247 GLN A O   1 
ATOM   2059 C CB  . GLN A 1 253 ? 18.87181  4.83060   69.63186 1.000 29.51412 ? 247 GLN A CB  1 
ATOM   2060 C CG  . GLN A 1 253 ? 20.29939  4.56151   69.17664 1.000 31.62169 ? 247 GLN A CG  1 
ATOM   2061 C CD  A GLN A 1 253 ? 21.23277  4.22704   70.33475 0.600 33.81201 ? 247 GLN A CD  1 
ATOM   2062 C CD  B GLN A 1 253 ? 21.04009  5.84051   68.76774 0.400 32.48985 ? 247 GLN A CD  1 
ATOM   2063 O OE1 A GLN A 1 253 ? 20.88673  3.45748   71.23054 0.600 35.74135 ? 247 GLN A OE1 1 
ATOM   2064 O OE1 B GLN A 1 253 ? 21.35500  6.68044   69.60950 0.400 33.71269 ? 247 GLN A OE1 1 
ATOM   2065 N NE2 A GLN A 1 253 ? 22.42291  4.81184   70.31701 0.600 34.35993 ? 247 GLN A NE2 1 
ATOM   2066 N NE2 B GLN A 1 253 ? 21.35500  5.96708   67.48078 0.400 32.18873 ? 247 GLN A NE2 1 
ATOM   2067 N N   . GLU A 1 254 ? 16.99677  3.20713   67.70812 1.000 27.38166 ? 248 GLU A N   1 
ATOM   2068 C CA  . GLU A 1 254 ? 16.84924  2.13318   66.73978 1.000 29.96542 ? 248 GLU A CA  1 
ATOM   2069 C C   . GLU A 1 254 ? 16.30861  2.65065   65.41299 1.000 28.36941 ? 248 GLU A C   1 
ATOM   2070 O O   . GLU A 1 254 ? 16.76500  2.23584   64.33993 1.000 28.12610 ? 248 GLU A O   1 
ATOM   2071 C CB  . GLU A 1 254 ? 15.89651  1.07808   67.26929 1.000 33.31796 ? 248 GLU A CB  1 
ATOM   2072 C CG  . GLU A 1 254 ? 15.85622  -0.11774  66.38107 0.800 35.45251 ? 248 GLU A CG  1 
ATOM   2073 C CD  . GLU A 1 254 ? 15.37179  -1.34777  67.09156 0.600 36.60207 ? 248 GLU A CD  1 
ATOM   2074 O OE1 . GLU A 1 254 ? 14.24366  -1.76120  66.76030 0.600 34.98309 ? 248 GLU A OE1 1 
ATOM   2075 O OE2 . GLU A 1 254 ? 16.07293  -1.88331  67.98547 0.600 39.59681 ? 248 GLU A OE2 1 
ATOM   2076 N N   . ASP A 1 255 ? 15.29796  3.51612   65.46671 1.000 25.32501 ? 249 ASP A N   1 
ATOM   2077 C CA  . ASP A 1 255 ? 14.74637  4.05891   64.23777 1.000 24.75087 ? 249 ASP A CA  1 
ATOM   2078 C C   . ASP A 1 255 ? 15.74191  4.95231   63.52796 1.000 23.11041 ? 249 ASP A C   1 
ATOM   2079 O O   . ASP A 1 255 ? 15.76026  4.98078   62.28507 1.000 23.38905 ? 249 ASP A O   1 
ATOM   2080 C CB  . ASP A 1 255 ? 13.45105  4.79108   64.54854 1.000 25.77192 ? 249 ASP A CB  1 
ATOM   2081 C CG  . ASP A 1 255 ? 12.34427  3.83333   64.95481 0.800 27.76167 ? 249 ASP A CG  1 
ATOM   2082 O OD1 . ASP A 1 255 ? 12.52615  2.58631   64.83317 0.800 27.07286 ? 249 ASP A OD1 1 
ATOM   2083 O OD2 . ASP A 1 255 ? 11.29615  4.32852   65.38926 0.800 29.14844 ? 249 ASP A OD2 1 
ATOM   2084 N N   . LEU A 1 256 ? 16.60335  5.65947   64.27775 1.000 23.02184 ? 250 LEU A N   1 
ATOM   2085 C CA  . LEU A 1 256 ? 17.63331  6.46114   63.62326 1.000 24.93462 ? 250 LEU A CA  1 
ATOM   2086 C C   . LEU A 1 256 ? 18.68832  5.58231   62.97639 1.000 26.09368 ? 250 LEU A C   1 
ATOM   2087 O O   . LEU A 1 256 ? 19.17781  5.89552   61.88806 1.000 27.97975 ? 250 LEU A O   1 
ATOM   2088 C CB  . LEU A 1 256 ? 18.30288  7.39565   64.61718 1.000 28.31050 ? 250 LEU A CB  1 
ATOM   2089 C CG  . LEU A 1 256 ? 17.47478  8.55047   65.14980 1.000 32.22658 ? 250 LEU A CG  1 
ATOM   2090 C CD1 . LEU A 1 256 ? 18.32963  9.34193   66.08458 1.000 33.04928 ? 250 LEU A CD1 1 
ATOM   2091 C CD2 . LEU A 1 256 ? 16.96339  9.41707   64.02327 1.000 35.33341 ? 250 LEU A CD2 1 
ATOM   2092 N N   . ASN A 1 257 ? 19.05376  4.47873   63.61861 1.000 29.43227 ? 251 ASN A N   1 
ATOM   2093 C CA  . ASN A 1 257 ? 20.04975  3.58470   63.02185 1.000 34.40678 ? 251 ASN A CA  1 
ATOM   2094 C C   . ASN A 1 257 ? 19.54614  2.99087   61.69421 1.000 34.94838 ? 251 ASN A C   1 
ATOM   2095 O O   . ASN A 1 257 ? 20.35334  2.60184   60.83287 1.000 37.42593 ? 251 ASN A O   1 
ATOM   2096 C CB  . ASN A 1 257 ? 20.45531  2.48228   64.01248 1.000 37.92188 ? 251 ASN A CB  1 
ATOM   2097 C CG  . ASN A 1 257 ? 21.19440  3.03456   65.23413 0.900 41.02637 ? 251 ASN A CG  1 
ATOM   2098 O OD1 . ASN A 1 257 ? 21.81120  4.11077   65.17267 0.900 40.59718 ? 251 ASN A OD1 1 
ATOM   2099 N ND2 . ASN A 1 257 ? 21.12432  2.30773   66.35316 0.900 43.15151 ? 251 ASN A ND2 1 
HETATM 2100 N N   . CME A 1 258 ? 18.22304  2.95892   61.52139 1.000 33.12387 ? 252 CME A N   1 
HETATM 2101 C CA  . CME A 1 258 ? 17.57936  2.61079   60.26808 1.000 35.13733 ? 252 CME A CA  1 
HETATM 2102 C CB  . CME A 1 258 ? 16.06077  2.68455   60.33174 0.700 40.56123 ? 252 CME A CB  1 
HETATM 2103 S SG  . CME A 1 258 ? 15.31026  1.21588   59.83026 0.700 47.76995 ? 252 CME A SG  1 
HETATM 2104 S SD  . CME A 1 258 ? 16.01770  0.43328   61.60863 0.700 38.79201 ? 252 CME A SD  1 
HETATM 2105 C CE  . CME A 1 258 ? 16.52275  -1.15905  61.02785 0.700 38.10012 ? 252 CME A CE  1 
HETATM 2106 C CZ  . CME A 1 258 ? 15.33747  -2.10167  60.84755 0.500 38.85407 ? 252 CME A CZ  1 
HETATM 2107 O OH  . CME A 1 258 ? 14.14060  -1.32883  60.74737 0.500 40.22904 ? 252 CME A OH  1 
HETATM 2108 C C   . CME A 1 258 ? 17.84426  3.52110   59.08209 1.000 33.05833 ? 252 CME A C   1 
HETATM 2109 O O   . CME A 1 258 ? 17.66319  3.18431   57.91172 1.000 36.64140 ? 252 CME A O   1 
ATOM   2110 N N   . ILE A 1 259 ? 18.16844  4.76115   59.41888 1.000 27.80841 ? 253 ILE A N   1 
ATOM   2111 C CA  . ILE A 1 259 ? 18.42340  5.80173   58.43799 1.000 27.40848 ? 253 ILE A CA  1 
ATOM   2112 C C   . ILE A 1 259 ? 19.92871  5.89647   58.23616 1.000 29.09338 ? 253 ILE A C   1 
ATOM   2113 O O   . ILE A 1 259 ? 20.62473  6.55407   59.01424 1.000 30.54927 ? 253 ILE A O   1 
ATOM   2114 C CB  . ILE A 1 259 ? 17.84353  7.13576   58.89236 1.000 25.03433 ? 253 ILE A CB  1 
ATOM   2115 C CG1 . ILE A 1 259 ? 16.33357  7.00400   59.15003 1.000 25.22494 ? 253 ILE A CG1 1 
ATOM   2116 C CG2 . ILE A 1 259 ? 18.09526  8.22694   57.87164 1.000 25.20799 ? 253 ILE A CG2 1 
ATOM   2117 C CD1 . ILE A 1 259 ? 15.74985  8.23435   59.73798 1.000 29.32793 ? 253 ILE A CD1 1 
ATOM   2118 N N   . ILE A 1 260 ? 20.44018  5.25649   57.19239 1.000 30.94718 ? 254 ILE A N   1 
ATOM   2119 C CA  . ILE A 1 260 ? 21.90095  5.27381   57.06607 1.000 31.66212 ? 254 ILE A CA  1 
ATOM   2120 C C   . ILE A 1 260 ? 22.36007  6.60071   56.45868 1.000 30.94278 ? 254 ILE A C   1 
ATOM   2121 O O   . ILE A 1 260 ? 23.48755  7.04814   56.71901 1.000 34.20462 ? 254 ILE A O   1 
ATOM   2122 C CB  . ILE A 1 260 ? 22.42671  4.05614   56.28079 1.000 37.55987 ? 254 ILE A CB  1 
ATOM   2123 C CG1 . ILE A 1 260 ? 23.96295  4.02122   56.33241 1.000 41.45847 ? 254 ILE A CG1 1 
ATOM   2124 C CG2 . ILE A 1 260 ? 22.01678  4.10480   54.80805 1.000 40.67291 ? 254 ILE A CG2 1 
ATOM   2125 C CD1 . ILE A 1 260 ? 24.58221  2.70488   55.86571 1.000 44.01000 ? 254 ILE A CD1 1 
ATOM   2126 N N   . ASN A 1 261 ? 21.51212  7.27796   55.68105 1.000 27.90084 ? 255 ASN A N   1 
ATOM   2127 C CA  . ASN A 1 261 ? 21.94924  8.51478   55.03812 1.000 23.99975 ? 255 ASN A CA  1 
ATOM   2128 C C   . ASN A 1 261 ? 22.35714  9.53102   56.09281 1.000 24.52314 ? 255 ASN A C   1 
ATOM   2129 O O   . ASN A 1 261 ? 21.56719  9.86577   56.98247 1.000 25.34567 ? 255 ASN A O   1 
ATOM   2130 C CB  . ASN A 1 261 ? 20.83089  9.07392   54.16235 1.000 24.42498 ? 255 ASN A CB  1 
ATOM   2131 C CG  . ASN A 1 261 ? 21.26603  10.30657  53.40661 1.000 27.08653 ? 255 ASN A CG  1 
ATOM   2132 O OD1 . ASN A 1 261 ? 21.18802  11.39758  53.93735 1.000 27.10754 ? 255 ASN A OD1 1 
ATOM   2133 N ND2 . ASN A 1 261 ? 21.74465  10.13485  52.15461 1.000 26.93779 ? 255 ASN A ND2 1 
ATOM   2134 N N   . LEU A 1 262 ? 23.60593  9.99024   56.01109 1.000 26.76161 ? 256 LEU A N   1 
ATOM   2135 C CA  . LEU A 1 262 ? 24.18412  10.81575  57.06335 1.000 28.57027 ? 256 LEU A CA  1 
ATOM   2136 C C   . LEU A 1 262 ? 23.48240  12.16166  57.18739 1.000 27.59046 ? 256 LEU A C   1 
ATOM   2137 O O   . LEU A 1 262 ? 23.23507  12.63068  58.31000 1.000 28.37640 ? 256 LEU A O   1 
ATOM   2138 C CB  A LEU A 1 262 ? 25.67877  11.01924  56.78257 0.500 29.86096 ? 256 LEU A CB  1 
ATOM   2139 C CB  B LEU A 1 262 ? 25.68277  10.98969  56.81176 0.500 30.52896 ? 256 LEU A CB  1 
ATOM   2140 C CG  A LEU A 1 262 ? 26.52555  10.17000  57.70530 0.500 28.78266 ? 256 LEU A CG  1 
ATOM   2141 C CG  B LEU A 1 262 ? 26.39935  11.64197  57.98210 0.500 29.94210 ? 256 LEU A CG  1 
ATOM   2142 C CD1 A LEU A 1 262 ? 28.02565  10.22559  57.31707 0.500 26.98688 ? 256 LEU A CD1 1 
ATOM   2143 C CD1 B LEU A 1 262 ? 26.10288  10.89183  59.28982 0.500 28.57996 ? 256 LEU A CD1 1 
ATOM   2144 C CD2 A LEU A 1 262 ? 26.28910  10.59786  59.16441 0.500 30.14068 ? 256 LEU A CD2 1 
ATOM   2145 C CD2 B LEU A 1 262 ? 27.86341  11.66117  57.68446 0.500 30.98254 ? 256 LEU A CD2 1 
ATOM   2146 N N   . LYS A 1 263 ? 23.15003  12.80185  56.05729 1.000 26.56513 ? 257 LYS A N   1 
ATOM   2147 C CA  . LYS A 1 263 ? 22.49416  14.10943  56.13225 1.000 25.17355 ? 257 LYS A CA  1 
ATOM   2148 C C   . LYS A 1 263 ? 21.12420  14.01584  56.80741 1.000 22.77052 ? 257 LYS A C   1 
ATOM   2149 O O   . LYS A 1 263 ? 20.79181  14.83586  57.67626 1.000 21.20927 ? 257 LYS A O   1 
ATOM   2150 C CB  . LYS A 1 263 ? 22.37173  14.73798  54.73630 1.000 27.18921 ? 257 LYS A CB  1 
ATOM   2151 C CG  . LYS A 1 263 ? 23.69753  15.27304  54.18338 0.900 31.74344 ? 257 LYS A CG  1 
ATOM   2152 C CD  . LYS A 1 263 ? 23.43618  16.35646  53.12177 0.900 34.42790 ? 257 LYS A CD  1 
ATOM   2153 C CE  . LYS A 1 263 ? 24.45728  17.48891  53.18080 0.600 38.63061 ? 257 LYS A CE  1 
ATOM   2154 N NZ  . LYS A 1 263 ? 24.33560  18.39744  52.00446 0.600 39.73754 ? 257 LYS A NZ  1 
ATOM   2155 N N   . ALA A 1 264 ? 20.32884  13.00532  56.45746 1.000 21.14137 ? 258 ALA A N   1 
ATOM   2156 C CA  . ALA A 1 264 ? 19.02889  12.84129  57.09940 1.000 20.98366 ? 258 ALA A CA  1 
ATOM   2157 C C   . ALA A 1 264 ? 19.17361  12.49930  58.57843 1.000 19.49016 ? 258 ALA A C   1 
ATOM   2158 O O   . ALA A 1 264 ? 18.49285  13.08883  59.42695 1.000 18.60860 ? 258 ALA A O   1 
ATOM   2159 C CB  . ALA A 1 264 ? 18.21970  11.76795  56.38024 1.000 21.67836 ? 258 ALA A CB  1 
ATOM   2160 N N   . ARG A 1 265 ? 20.07337  11.57382  58.91595 1.000 18.86650 ? 259 ARG A N   1 
ATOM   2161 C CA  . ARG A 1 265 ? 20.22200  11.20213  60.31887 1.000 19.65804 ? 259 ARG A CA  1 
ATOM   2162 C C   . ARG A 1 265 ? 20.71800  12.38657  61.15610 1.000 19.59261 ? 259 ARG A C   1 
ATOM   2163 O O   . ARG A 1 265 ? 20.20751  12.63255  62.26191 1.000 20.46795 ? 259 ARG A O   1 
ATOM   2164 C CB  . ARG A 1 265 ? 21.15401  9.99557   60.45621 0.900 22.00713 ? 259 ARG A CB  1 
ATOM   2165 C CG  . ARG A 1 265 ? 21.06190  9.38109   61.87982 0.800 23.89685 ? 259 ARG A CG  1 
ATOM   2166 C CD  . ARG A 1 265 ? 22.18370  8.41314   62.18407 0.800 25.68173 ? 259 ARG A CD  1 
ATOM   2167 N NE  . ARG A 1 265 ? 22.07692  7.17216   61.41995 0.800 26.42971 ? 259 ARG A NE  1 
ATOM   2168 C CZ  . ARG A 1 265 ? 22.82487  6.10618   61.65834 0.700 29.01176 ? 259 ARG A CZ  1 
ATOM   2169 N NH1 . ARG A 1 265 ? 23.73766  6.10746   62.62114 0.700 29.19554 ? 259 ARG A NH1 1 
ATOM   2170 N NH2 . ARG A 1 265 ? 22.66837  5.02153   60.90587 0.700 29.83871 ? 259 ARG A NH2 1 
ATOM   2171 N N   . ASN A 1 266 ? 21.69640  13.14801  60.63578 1.000 20.93274 ? 260 ASN A N   1 
ATOM   2172 C CA  . ASN A 1 266 ? 22.21855  14.28963  61.38387 1.000 20.53523 ? 260 ASN A CA  1 
ATOM   2173 C C   . ASN A 1 266 ? 21.22139  15.40813  61.54533 1.000 19.55319 ? 260 ASN A C   1 
ATOM   2174 O O   . ASN A 1 266 ? 21.25841  16.10981  62.55783 1.000 21.50661 ? 260 ASN A O   1 
ATOM   2175 C CB  . ASN A 1 266 ? 23.49741  14.83635  60.77744 1.000 21.47818 ? 260 ASN A CB  1 
ATOM   2176 C CG  . ASN A 1 266 ? 24.67667  13.97884  61.12054 1.000 25.97508 ? 260 ASN A CG  1 
ATOM   2177 O OD1 . ASN A 1 266 ? 24.59008  13.16591  62.04276 1.000 28.48034 ? 260 ASN A OD1 1 
ATOM   2178 N ND2 . ASN A 1 266 ? 25.77842  14.18721  60.45850 1.000 25.95929 ? 260 ASN A ND2 1 
ATOM   2179 N N   . TYR A 1 267 ? 20.30786  15.58149  60.60043 1.000 19.03878 ? 261 TYR A N   1 
ATOM   2180 C CA  . TYR A 1 267 ? 19.25101  16.55442  60.82090 1.000 20.00383 ? 261 TYR A CA  1 
ATOM   2181 C C   . TYR A 1 267 ? 18.42191  16.15282  62.03661 1.000 19.65900 ? 261 TYR A C   1 
ATOM   2182 O O   . TYR A 1 267 ? 18.19116  16.96123  62.95267 1.000 20.10651 ? 261 TYR A O   1 
ATOM   2183 C CB  . TYR A 1 267 ? 18.36363  16.66756  59.57912 1.000 19.41304 ? 261 TYR A CB  1 
ATOM   2184 C CG  . TYR A 1 267 ? 17.20474  17.56002  59.88463 1.000 22.09365 ? 261 TYR A CG  1 
ATOM   2185 C CD1 . TYR A 1 267 ? 17.40212  18.92736  60.08181 1.000 22.09505 ? 261 TYR A CD1 1 
ATOM   2186 C CD2 . TYR A 1 267 ? 15.93452  17.03648  60.04896 1.000 21.16934 ? 261 TYR A CD2 1 
ATOM   2187 C CE1 . TYR A 1 267 ? 16.36955  19.74468  60.41541 1.000 22.80668 ? 261 TYR A CE1 1 
ATOM   2188 C CE2 . TYR A 1 267 ? 14.85032  17.87561  60.38123 1.000 23.06252 ? 261 TYR A CE2 1 
ATOM   2189 C CZ  . TYR A 1 267 ? 15.09372  19.22404  60.56355 1.000 22.73541 ? 261 TYR A CZ  1 
ATOM   2190 O OH  . TYR A 1 267 ? 14.10243  20.10723  60.88769 1.000 25.11207 ? 261 TYR A OH  1 
ATOM   2191 N N   . LEU A 1 268 ? 17.97972  14.89032  62.07618 1.000 18.34665 ? 262 LEU A N   1 
ATOM   2192 C CA  . LEU A 1 268 ? 17.18237  14.42821  63.21942 1.000 17.22276 ? 262 LEU A CA  1 
ATOM   2193 C C   . LEU A 1 268 ? 17.96716  14.52969  64.53167 1.000 18.48228 ? 262 LEU A C   1 
ATOM   2194 O O   . LEU A 1 268 ? 17.40362  14.91462  65.56847 1.000 18.68144 ? 262 LEU A O   1 
ATOM   2195 C CB  . LEU A 1 268 ? 16.72050  12.99428  62.97675 1.000 18.99551 ? 262 LEU A CB  1 
ATOM   2196 C CG  . LEU A 1 268 ? 15.73932  12.88831  61.80699 1.000 19.40346 ? 262 LEU A CG  1 
ATOM   2197 C CD1 . LEU A 1 268 ? 15.53466  11.43228  61.49161 1.000 24.12803 ? 262 LEU A CD1 1 
ATOM   2198 C CD2 . LEU A 1 268 ? 14.39148  13.60475  62.12756 1.000 20.18251 ? 262 LEU A CD2 1 
ATOM   2199 N N   . LEU A 1 269 ? 19.27285  14.20825  64.50528 1.000 18.61665 ? 263 LEU A N   1 
ATOM   2200 C CA  . LEU A 1 269 ? 20.07012  14.28692  65.72736 1.000 20.47320 ? 263 LEU A CA  1 
ATOM   2201 C C   . LEU A 1 269 ? 20.26043  15.71263  66.20313 1.000 21.99878 ? 263 LEU A C   1 
ATOM   2202 O O   . LEU A 1 269 ? 20.49329  15.92258  67.40464 1.000 23.80150 ? 263 LEU A O   1 
ATOM   2203 C CB  . LEU A 1 269 ? 21.44826  13.64096  65.51199 1.000 21.05119 ? 263 LEU A CB  1 
ATOM   2204 C CG  . LEU A 1 269 ? 21.41398  12.12009  65.37295 1.000 24.07201 ? 263 LEU A CG  1 
ATOM   2205 C CD1 . LEU A 1 269 ? 22.74879  11.56396  64.91842 1.000 26.78929 ? 263 LEU A CD1 1 
ATOM   2206 C CD2 . LEU A 1 269 ? 21.04920  11.48621  66.70577 1.000 25.22428 ? 263 LEU A CD2 1 
ATOM   2207 N N   . SER A 1 270 ? 20.17734  16.69049  65.29282 1.000 21.10445 ? 264 SER A N   1 
ATOM   2208 C CA  . SER A 1 270 ? 20.36218  18.08771  65.64358 1.000 23.19786 ? 264 SER A CA  1 
ATOM   2209 C C   . SER A 1 270 ? 19.15361  18.67146  66.36284 1.000 23.54412 ? 264 SER A C   1 
ATOM   2210 O O   . SER A 1 270 ? 19.25717  19.76774  66.93028 1.000 25.19493 ? 264 SER A O   1 
ATOM   2211 C CB  . SER A 1 270 ? 20.65798  18.91407  64.38121 1.000 25.26057 ? 264 SER A CB  1 
ATOM   2212 O OG  . SER A 1 270 ? 19.46293  19.22003  63.64188 1.000 25.28324 ? 264 SER A OG  1 
ATOM   2213 N N   . LEU A 1 271 ? 18.01826  17.97029  66.36273 1.000 20.67569 ? 265 LEU A N   1 
ATOM   2214 C CA  . LEU A 1 271 ? 16.81593  18.52348  66.95976 1.000 21.25816 ? 265 LEU A CA  1 
ATOM   2215 C C   . LEU A 1 271 ? 16.82233  18.29184  68.47205 1.000 21.77098 ? 265 LEU A C   1 
ATOM   2216 O O   . LEU A 1 271 ? 17.34334  17.27689  68.94377 1.000 23.44953 ? 265 LEU A O   1 
ATOM   2217 C CB  . LEU A 1 271 ? 15.57379  17.87069  66.34315 1.000 20.38370 ? 265 LEU A CB  1 
ATOM   2218 C CG  . LEU A 1 271 ? 15.42659  18.05497  64.84457 1.000 20.98573 ? 265 LEU A CG  1 
ATOM   2219 C CD1 . LEU A 1 271 ? 14.24644  17.21833  64.31794 1.000 21.22633 ? 265 LEU A CD1 1 
ATOM   2220 C CD2 . LEU A 1 271 ? 15.23091  19.55222  64.54165 1.000 24.45911 ? 265 LEU A CD2 1 
ATOM   2221 N N   . PRO A 1 272 ? 16.24136  19.21519  69.25109 1.000 22.33272 ? 266 PRO A N   1 
ATOM   2222 C CA  . PRO A 1 272 ? 16.03338  18.95328  70.68833 1.000 22.54404 ? 266 PRO A CA  1 
ATOM   2223 C C   . PRO A 1 272 ? 15.07264  17.78980  70.89926 1.000 22.42764 ? 266 PRO A C   1 
ATOM   2224 O O   . PRO A 1 272 ? 14.21518  17.51148  70.06086 1.000 23.69307 ? 266 PRO A O   1 
ATOM   2225 C CB  . PRO A 1 272 ? 15.41674  20.26267  71.20825 1.000 25.57974 ? 266 PRO A CB  1 
ATOM   2226 C CG  . PRO A 1 272 ? 15.71498  21.31165  70.15055 1.000 29.19724 ? 266 PRO A CG  1 
ATOM   2227 C CD  . PRO A 1 272 ? 15.75982  20.55161  68.83981 1.000 26.71933 ? 266 PRO A CD  1 
ATOM   2228 N N   . HIS A 1 273 ? 15.21613  17.10882  72.04874 1.000 23.45807 ? 267 HIS A N   1 
ATOM   2229 C CA  . HIS A 1 273 ? 14.30926  16.02410  72.42666 1.000 25.18908 ? 267 HIS A CA  1 
ATOM   2230 C C   . HIS A 1 273 ? 12.87210  16.53631  72.50360 1.000 26.54264 ? 267 HIS A C   1 
ATOM   2231 O O   . HIS A 1 273 ? 12.62504  17.55202  73.16449 1.000 31.28236 ? 267 HIS A O   1 
ATOM   2232 C CB  . HIS A 1 273 ? 14.78341  15.48373  73.79593 0.900 26.34967 ? 267 HIS A CB  1 
ATOM   2233 C CG  . HIS A 1 273 ? 14.01530  14.31985  74.33294 0.800 28.33704 ? 267 HIS A CG  1 
ATOM   2234 N ND1 . HIS A 1 273 ? 13.22395  13.49571  73.56391 0.800 30.33349 ? 267 HIS A ND1 1 
ATOM   2235 C CD2 . HIS A 1 273 ? 13.92624  13.84731  75.59967 0.800 30.02306 ? 267 HIS A CD2 1 
ATOM   2236 C CE1 . HIS A 1 273 ? 12.67541  12.57074  74.33047 0.800 30.63689 ? 267 HIS A CE1 1 
ATOM   2237 N NE2 . HIS A 1 273 ? 13.08615  12.76040  75.57061 0.800 32.95767 ? 267 HIS A NE2 1 
ATOM   2238 N N   . LYS A 1 274 ? 11.93061  15.84911  71.81089 1.000 25.88771 ? 268 LYS A N   1 
ATOM   2239 C CA  . LYS A 1 274 ? 10.49319  16.14286  71.84272 1.000 28.36131 ? 268 LYS A CA  1 
ATOM   2240 C C   . LYS A 1 274 ? 9.75691   14.91600  72.37867 1.000 28.53287 ? 268 LYS A C   1 
ATOM   2241 O O   . LYS A 1 274 ? 9.98008   13.80389  71.89051 1.000 27.52604 ? 268 LYS A O   1 
ATOM   2242 C CB  . LYS A 1 274 ? 9.92033   16.46180  70.43883 0.900 30.05971 ? 268 LYS A CB  1 
ATOM   2243 C CG  . LYS A 1 274 ? 10.64234  17.52304  69.57866 0.800 30.55189 ? 268 LYS A CG  1 
ATOM   2244 C CD  . LYS A 1 274 ? 10.11374  17.51687  68.09237 0.700 30.88639 ? 268 LYS A CD  1 
ATOM   2245 C CE  . LYS A 1 274 ? 11.11229  18.14706  67.10480 0.600 31.38599 ? 268 LYS A CE  1 
ATOM   2246 N NZ  . LYS A 1 274 ? 11.02689  19.63500  67.02418 0.500 33.07897 ? 268 LYS A NZ  1 
ATOM   2247 N N   . ASN A 1 275 ? 8.84337   15.11307  73.34040 1.000 31.09658 ? 269 ASN A N   1 
ATOM   2248 C CA  . ASN A 1 275 ? 8.03331   14.00302  73.82547 1.000 30.11934 ? 269 ASN A CA  1 
ATOM   2249 C C   . ASN A 1 275 ? 6.83474   13.74061  72.92020 1.000 28.38969 ? 269 ASN A C   1 
ATOM   2250 O O   . ASN A 1 275 ? 6.31277   14.64140  72.25956 1.000 30.76929 ? 269 ASN A O   1 
ATOM   2251 C CB  . ASN A 1 275 ? 7.48312   14.26614  75.23396 0.800 33.09177 ? 269 ASN A CB  1 
ATOM   2252 C CG  . ASN A 1 275 ? 8.52748   14.78007  76.18386 0.600 38.28438 ? 269 ASN A CG  1 
ATOM   2253 O OD1 . ASN A 1 275 ? 9.54028   14.12421  76.42948 0.600 38.97721 ? 269 ASN A OD1 1 
ATOM   2254 N ND2 . ASN A 1 275 ? 8.27079   15.95252  76.75724 0.600 41.55682 ? 269 ASN A ND2 1 
ATOM   2255 N N   . LYS A 1 276 ? 6.39971   12.48688  72.91461 1.000 26.50716 ? 270 LYS A N   1 
ATOM   2256 C CA  . LYS A 1 276 ? 5.17778   12.07780  72.23825 1.000 26.38729 ? 270 LYS A CA  1 
ATOM   2257 C C   . LYS A 1 276 ? 3.94209   12.71268  72.87691 1.000 28.02386 ? 270 LYS A C   1 
ATOM   2258 O O   . LYS A 1 276 ? 3.82177   12.79189  74.10768 1.000 29.77308 ? 270 LYS A O   1 
ATOM   2259 C CB  . LYS A 1 276 ? 5.08080   10.54806  72.27737 1.000 28.28330 ? 270 LYS A CB  1 
ATOM   2260 C CG  . LYS A 1 276 ? 3.84830   9.92742   71.59653 1.000 31.36582 ? 270 LYS A CG  1 
ATOM   2261 C CD  . LYS A 1 276 ? 3.91575   8.40140   71.71261 1.000 35.75573 ? 270 LYS A CD  1 
ATOM   2262 C CE  . LYS A 1 276 ? 2.69288   7.70358   71.12255 1.000 40.66074 ? 270 LYS A CE  1 
ATOM   2263 N NZ  . LYS A 1 276 ? 2.67212   7.79553   69.60647 1.000 41.63443 ? 270 LYS A NZ  1 
ATOM   2264 N N   . VAL A 1 277 ? 3.02391   13.18136  72.03544 1.000 26.50749 ? 271 VAL A N   1 
ATOM   2265 C CA  . VAL A 1 277 ? 1.70198   13.61389  72.47918 1.000 25.88005 ? 271 VAL A CA  1 
ATOM   2266 C C   . VAL A 1 277 ? 0.78966   12.39406  72.42996 1.000 25.57909 ? 271 VAL A C   1 
ATOM   2267 O O   . VAL A 1 277 ? 0.62072   11.81773  71.35295 1.000 27.26030 ? 271 VAL A O   1 
ATOM   2268 C CB  . VAL A 1 277 ? 1.13997   14.72963  71.58773 1.000 28.39641 ? 271 VAL A CB  1 
ATOM   2269 C CG1 . VAL A 1 277 ? -0.26966  15.15862  72.05745 1.000 31.66541 ? 271 VAL A CG1 1 
ATOM   2270 C CG2 . VAL A 1 277 ? 2.10566   15.90925  71.47206 1.000 30.18657 ? 271 VAL A CG2 1 
ATOM   2271 N N   . PRO A 1 278 ? 0.15865   12.00213  73.53076 1.000 26.27930 ? 272 PRO A N   1 
ATOM   2272 C CA  . PRO A 1 278 ? -0.68513  10.80051  73.49873 1.000 26.92938 ? 272 PRO A CA  1 
ATOM   2273 C C   . PRO A 1 278 ? -1.89731  10.99326  72.61469 1.000 25.63395 ? 272 PRO A C   1 
ATOM   2274 O O   . PRO A 1 278 ? -2.52821  12.05514  72.63028 1.000 26.04393 ? 272 PRO A O   1 
ATOM   2275 C CB  . PRO A 1 278 ? -1.10989  10.61243  74.95899 1.000 29.84773 ? 272 PRO A CB  1 
ATOM   2276 C CG  . PRO A 1 278 ? -0.25615  11.50881  75.74476 1.000 30.48089 ? 272 PRO A CG  1 
ATOM   2277 C CD  . PRO A 1 278 ? 0.20306   12.62077  74.86594 1.000 26.93289 ? 272 PRO A CD  1 
ATOM   2278 N N   . TRP A 1 279 ? -2.22852  9.94239   71.84993 1.000 23.40601 ? 273 TRP A N   1 
ATOM   2279 C CA  . TRP A 1 279 ? -3.37296  10.03422  70.94901 1.000 23.59801 ? 273 TRP A CA  1 
ATOM   2280 C C   . TRP A 1 279 ? -4.65057  10.33255  71.71386 1.000 24.44524 ? 273 TRP A C   1 
ATOM   2281 O O   . TRP A 1 279 ? -5.52371  11.04546  71.20514 1.000 26.17256 ? 273 TRP A O   1 
ATOM   2282 C CB  . TRP A 1 279 ? -3.53908  8.74345   70.15374 1.000 24.90075 ? 273 TRP A CB  1 
ATOM   2283 C CG  . TRP A 1 279 ? -2.34568  8.42851   69.27571 1.000 26.58933 ? 273 TRP A CG  1 
ATOM   2284 C CD1 . TRP A 1 279 ? -1.48667  7.37233   69.39121 1.000 27.01924 ? 273 TRP A CD1 1 
ATOM   2285 C CD2 . TRP A 1 279 ? -1.90214  9.18686   68.14623 1.000 27.05430 ? 273 TRP A CD2 1 
ATOM   2286 N NE1 . TRP A 1 279 ? -0.51462  7.43430   68.40522 1.000 26.14497 ? 273 TRP A NE1 1 
ATOM   2287 C CE2 . TRP A 1 279 ? -0.74614  8.53783   67.62779 1.000 26.80341 ? 273 TRP A CE2 1 
ATOM   2288 C CE3 . TRP A 1 279 ? -2.33349  10.37124  67.54695 1.000 26.26542 ? 273 TRP A CE3 1 
ATOM   2289 C CZ2 . TRP A 1 279 ? -0.04746  9.02100   66.51731 1.000 29.79576 ? 273 TRP A CZ2 1 
ATOM   2290 C CZ3 . TRP A 1 279 ? -1.64265  10.83932  66.41036 1.000 28.16525 ? 273 TRP A CZ3 1 
ATOM   2291 C CH2 . TRP A 1 279 ? -0.51487  10.16979  65.92234 1.000 28.66668 ? 273 TRP A CH2 1 
ATOM   2292 N N   . ASN A 1 280 ? -4.80431  9.77748   72.93105 1.000 25.82399 ? 274 ASN A N   1 
ATOM   2293 C CA  . ASN A 1 280 ? -6.07576  9.99689   73.60929 1.000 29.22497 ? 274 ASN A CA  1 
ATOM   2294 C C   . ASN A 1 280 ? -6.19039  11.41039  74.17788 1.000 30.98530 ? 274 ASN A C   1 
ATOM   2295 O O   . ASN A 1 280 ? -7.29253  11.83319  74.57038 1.000 32.13660 ? 274 ASN A O   1 
ATOM   2296 C CB  . ASN A 1 280 ? -6.27778  8.92352   74.69139 1.000 33.25284 ? 274 ASN A CB  1 
ATOM   2297 C CG  . ASN A 1 280 ? -5.45946  9.17082   75.94538 1.000 38.99144 ? 274 ASN A CG  1 
ATOM   2298 O OD1 . ASN A 1 280 ? -4.40679  9.81824   75.91787 1.000 40.82113 ? 274 ASN A OD1 1 
ATOM   2299 N ND2 . ASN A 1 280 ? -5.91543  8.58902   77.05348 1.000 42.95798 ? 274 ASN A ND2 1 
ATOM   2300 N N   . ARG A 1 281 ? -5.09060  12.16480  74.19135 1.000 30.79345 ? 275 ARG A N   1 
ATOM   2301 C CA  . ARG A 1 281 ? -5.17684  13.58407  74.52621 1.000 32.61173 ? 275 ARG A CA  1 
ATOM   2302 C C   . ARG A 1 281 ? -5.57376  14.41289  73.30261 1.000 33.04715 ? 275 ARG A C   1 
ATOM   2303 O O   . ARG A 1 281 ? -6.37223  15.35105  73.42323 1.000 33.49914 ? 275 ARG A O   1 
ATOM   2304 C CB  . ARG A 1 281 ? -3.85561  14.05806  75.13226 1.000 34.61510 ? 275 ARG A CB  1 
ATOM   2305 C CG  . ARG A 1 281 ? -3.55121  13.48338  76.53720 0.800 38.38676 ? 275 ARG A CG  1 
ATOM   2306 C CD  . ARG A 1 281 ? -2.86253  14.52475  77.42895 0.700 43.20251 ? 275 ARG A CD  1 
ATOM   2307 N NE  . ARG A 1 281 ? -1.81792  15.26254  76.71888 0.600 44.78435 ? 275 ARG A NE  1 
ATOM   2308 C CZ  . ARG A 1 281 ? -0.53441  15.27914  77.05933 0.600 47.04441 ? 275 ARG A CZ  1 
ATOM   2309 N NH1 . ARG A 1 281 ? -0.09480  14.65352  78.14393 0.600 47.08749 ? 275 ARG A NH1 1 
ATOM   2310 N NH2 . ARG A 1 281 ? 0.32887   15.95185  76.30051 0.600 46.80177 ? 275 ARG A NH2 1 
ATOM   2311 N N   . LEU A 1 282 ? -5.05702  14.05301  72.11458 1.000 29.44444 ? 276 LEU A N   1 
ATOM   2312 C CA  . LEU A 1 282 ? -5.50308  14.66613  70.86971 1.000 29.17484 ? 276 LEU A CA  1 
ATOM   2313 C C   . LEU A 1 282 ? -6.94227  14.31419  70.54040 1.000 30.22226 ? 276 LEU A C   1 
ATOM   2314 O O   . LEU A 1 282 ? -7.65517  15.13531  69.95963 1.000 32.85646 ? 276 LEU A O   1 
ATOM   2315 C CB  . LEU A 1 282 ? -4.61790  14.22086  69.70669 1.000 31.52891 ? 276 LEU A CB  1 
ATOM   2316 C CG  . LEU A 1 282 ? -3.18557  14.73050  69.74342 1.000 34.29141 ? 276 LEU A CG  1 
ATOM   2317 C CD1 . LEU A 1 282 ? -2.42033  14.16099  68.56032 1.000 37.20594 ? 276 LEU A CD1 1 
ATOM   2318 C CD2 . LEU A 1 282 ? -3.22791  16.22742  69.65726 1.000 36.59243 ? 276 LEU A CD2 1 
ATOM   2319 N N   . PHE A 1 283 ? -7.36915  13.09399  70.85592 1.000 28.06256 ? 277 PHE A N   1 
ATOM   2320 C CA  . PHE A 1 283 ? -8.66458  12.56423  70.41869 1.000 27.88514 ? 277 PHE A CA  1 
ATOM   2321 C C   . PHE A 1 283 ? -9.40628  11.96010  71.60890 1.000 29.62316 ? 277 PHE A C   1 
ATOM   2322 O O   . PHE A 1 283 ? -9.56730  10.73733  71.69766 1.000 29.89220 ? 277 PHE A O   1 
ATOM   2323 C CB  . PHE A 1 283 ? -8.47645  11.52280  69.31079 1.000 26.35477 ? 277 PHE A CB  1 
ATOM   2324 C CG  . PHE A 1 283 ? -7.70607  12.02555  68.10927 1.000 27.33542 ? 277 PHE A CG  1 
ATOM   2325 C CD1 . PHE A 1 283 ? -8.26374  12.95207  67.23952 1.000 29.01820 ? 277 PHE A CD1 1 
ATOM   2326 C CD2 . PHE A 1 283 ? -6.43751  11.53026  67.82165 1.000 28.39744 ? 277 PHE A CD2 1 
ATOM   2327 C CE1 . PHE A 1 283 ? -7.55532  13.38342  66.10396 1.000 29.70295 ? 277 PHE A CE1 1 
ATOM   2328 C CE2 . PHE A 1 283 ? -5.73878  11.96165  66.69725 1.000 27.95482 ? 277 PHE A CE2 1 
ATOM   2329 C CZ  . PHE A 1 283 ? -6.29281  12.90416  65.85575 1.000 27.46407 ? 277 PHE A CZ  1 
ATOM   2330 N N   . PRO A 1 284 ? -9.89588  12.79757  72.53255 1.000 31.27074 ? 278 PRO A N   1 
ATOM   2331 C CA  . PRO A 1 284 ? -10.47124 12.26162  73.78606 1.000 33.04544 ? 278 PRO A CA  1 
ATOM   2332 C C   . PRO A 1 284 ? -11.78762 11.50858  73.62037 1.000 35.00489 ? 278 PRO A C   1 
ATOM   2333 O O   . PRO A 1 284 ? -12.15027 10.73341  74.51567 1.000 37.05216 ? 278 PRO A O   1 
ATOM   2334 C CB  . PRO A 1 284 ? -10.67675 13.51654  74.65159 1.000 32.99305 ? 278 PRO A CB  1 
ATOM   2335 C CG  . PRO A 1 284 ? -10.73552 14.64960  73.67252 1.000 33.89378 ? 278 PRO A CG  1 
ATOM   2336 C CD  . PRO A 1 284 ? -9.81987  14.26939  72.53840 1.000 31.21236 ? 278 PRO A CD  1 
ATOM   2337 N N   . ASN A 1 285 ? -12.53893 11.70141  72.54505 1.000 33.23241 ? 279 ASN A N   1 
ATOM   2338 C CA  A ASN A 1 285 ? -13.78367 10.96957  72.34771 0.500 34.44645 ? 279 ASN A CA  1 
ATOM   2339 C CA  B ASN A 1 285 ? -13.76966 10.93639  72.39069 0.500 35.43625 ? 279 ASN A CA  1 
ATOM   2340 C C   . ASN A 1 285 ? -13.60891 9.76853   71.43487 1.000 35.06926 ? 279 ASN A C   1 
ATOM   2341 O O   . ASN A 1 285 ? -14.60062 9.09880   71.11202 1.000 37.67774 ? 279 ASN A O   1 
ATOM   2342 C CB  A ASN A 1 285 ? -14.87284 11.88357  71.77994 0.500 35.64486 ? 279 ASN A CB  1 
ATOM   2343 C CB  B ASN A 1 285 ? -14.93644 11.83519  71.95996 0.500 38.63904 ? 279 ASN A CB  1 
ATOM   2344 C CG  A ASN A 1 285 ? -16.28013 11.32973  72.01163 0.500 36.76605 ? 279 ASN A CG  1 
ATOM   2345 C CG  B ASN A 1 285 ? -14.51436 12.97246  71.05691 0.500 41.33062 ? 279 ASN A CG  1 
ATOM   2346 O OD1 A ASN A 1 285 ? -16.55859 10.73483  73.05523 0.500 36.86910 ? 279 ASN A OD1 1 
ATOM   2347 O OD1 B ASN A 1 285 ? -14.33002 12.78552  69.85476 0.500 42.93605 ? 279 ASN A OD1 1 
ATOM   2348 N ND2 A ASN A 1 285 ? -17.15661 11.48850  71.02010 0.500 38.36345 ? 279 ASN A ND2 1 
ATOM   2349 N ND2 B ASN A 1 285 ? -14.41173 14.17979  71.62647 0.500 41.79921 ? 279 ASN A ND2 1 
ATOM   2350 N N   . ALA A 1 286 ? -12.38220 9.47944   71.01099 1.000 30.82796 ? 280 ALA A N   1 
ATOM   2351 C CA  . ALA A 1 286 ? -12.17639 8.39323   70.06210 1.000 28.81380 ? 280 ALA A CA  1 
ATOM   2352 C C   . ALA A 1 286 ? -12.22539 7.04486   70.76960 1.000 26.97678 ? 280 ALA A C   1 
ATOM   2353 O O   . ALA A 1 286 ? -11.85776 6.92253   71.94029 1.000 28.44672 ? 280 ALA A O   1 
ATOM   2354 C CB  . ALA A 1 286 ? -10.82287 8.53955   69.34590 1.000 27.39703 ? 280 ALA A CB  1 
ATOM   2355 N N   . ASP A 1 287 ? -12.66388 6.03303   70.02122 1.000 26.48424 ? 281 ASP A N   1 
ATOM   2356 C CA  . ASP A 1 287 ? -12.60342 4.63048   70.41799 1.000 27.61449 ? 281 ASP A CA  1 
ATOM   2357 C C   . ASP A 1 287 ? -11.14593 4.22602   70.66448 1.000 28.25150 ? 281 ASP A C   1 
ATOM   2358 O O   . ASP A 1 287 ? -10.25955 4.53742   69.85931 1.000 27.38938 ? 281 ASP A O   1 
ATOM   2359 C CB  . ASP A 1 287 ? -13.22185 3.81211   69.27960 0.800 26.81561 ? 281 ASP A CB  1 
ATOM   2360 C CG  . ASP A 1 287 ? -13.25337 2.32384   69.53127 0.700 30.36282 ? 281 ASP A CG  1 
ATOM   2361 O OD1 . ASP A 1 287 ? -12.20321 1.70996   69.77329 0.700 34.00313 ? 281 ASP A OD1 1 
ATOM   2362 O OD2 . ASP A 1 287 ? -14.34361 1.74447   69.36868 0.700 33.35127 ? 281 ASP A OD2 1 
ATOM   2363 N N   . SER A 1 288 ? -10.88523 3.54879   71.78892 1.000 27.31156 ? 282 SER A N   1 
ATOM   2364 C CA  . SER A 1 288 ? -9.49995  3.21978   72.11947 1.000 25.63295 ? 282 SER A CA  1 
ATOM   2365 C C   . SER A 1 288 ? -8.88939  2.26349   71.10121 1.000 24.69277 ? 282 SER A C   1 
ATOM   2366 O O   . SER A 1 288 ? -7.68122  2.33326   70.84170 1.000 24.28862 ? 282 SER A O   1 
ATOM   2367 C CB  . SER A 1 288 ? -9.39894  2.62202   73.53013 1.000 31.66676 ? 282 SER A CB  1 
ATOM   2368 O OG  . SER A 1 288 ? -10.03124 1.34701   73.58882 1.000 35.88657 ? 282 SER A OG  1 
ATOM   2369 N N   . LYS A 1 289 ? -9.70182  1.37112   70.51588 1.000 23.82691 ? 283 LYS A N   1 
ATOM   2370 C CA  . LYS A 1 289 ? -9.19119  0.47182   69.48306 1.000 23.79253 ? 283 LYS A CA  1 
ATOM   2371 C C   . LYS A 1 289 ? -8.80983  1.24401   68.23392 1.000 23.52561 ? 283 LYS A C   1 
ATOM   2372 O O   . LYS A 1 289 ? -7.81698  0.90042   67.57235 1.000 21.44285 ? 283 LYS A O   1 
ATOM   2373 C CB  . LYS A 1 289 ? -10.22681 -0.60529  69.13110 1.000 24.11504 ? 283 LYS A CB  1 
ATOM   2374 C CG  . LYS A 1 289 ? -10.62645 -1.44515  70.34743 1.000 28.86547 ? 283 LYS A CG  1 
ATOM   2375 C CD  . LYS A 1 289 ? -11.50651 -2.65480  69.99629 1.000 32.97096 ? 283 LYS A CD  1 
ATOM   2376 C CE  . LYS A 1 289 ? -11.70143 -3.52595  71.21875 0.800 36.50221 ? 283 LYS A CE  1 
ATOM   2377 N NZ  . LYS A 1 289 ? -12.54386 -4.71944  70.95310 0.700 38.05923 ? 283 LYS A NZ  1 
ATOM   2378 N N   . ALA A 1 290 ? -9.59799  2.27625   67.88293 1.000 21.59392 ? 284 ALA A N   1 
ATOM   2379 C CA  . ALA A 1 290 ? -9.24165  3.15035   66.76052 1.000 20.44297 ? 284 ALA A CA  1 
ATOM   2380 C C   . ALA A 1 290 ? -7.89128  3.81262   66.99541 1.000 19.33136 ? 284 ALA A C   1 
ATOM   2381 O O   . ALA A 1 290 ? -7.06286  3.89314   66.07348 1.000 19.33896 ? 284 ALA A O   1 
ATOM   2382 C CB  . ALA A 1 290 ? -10.31951 4.21417   66.54662 1.000 22.31722 ? 284 ALA A CB  1 
ATOM   2383 N N   . LEU A 1 291 ? -7.63911  4.27095   68.23318 1.000 19.51143 ? 285 LEU A N   1 
ATOM   2384 C CA  . LEU A 1 291 ? -6.36746  4.94505   68.50512 1.000 21.01633 ? 285 LEU A CA  1 
ATOM   2385 C C   . LEU A 1 291 ? -5.18118  3.97932   68.48087 1.000 23.12179 ? 285 LEU A C   1 
ATOM   2386 O O   . LEU A 1 291 ? -4.06464  4.37304   68.10856 1.000 22.16380 ? 285 LEU A O   1 
ATOM   2387 C CB  . LEU A 1 291 ? -6.44241  5.69405   69.84969 1.000 22.55874 ? 285 LEU A CB  1 
ATOM   2388 C CG  . LEU A 1 291 ? -7.45087  6.84745   69.85839 1.000 23.43993 ? 285 LEU A CG  1 
ATOM   2389 C CD1 . LEU A 1 291 ? -7.41748  7.64878   71.20649 1.000 23.36799 ? 285 LEU A CD1 1 
ATOM   2390 C CD2 . LEU A 1 291 ? -7.26915  7.78273   68.62923 1.000 23.39943 ? 285 LEU A CD2 1 
ATOM   2391 N N   . ASP A 1 292 ? -5.39629  2.72972   68.86826 1.000 21.76298 ? 286 ASP A N   1 
ATOM   2392 C CA  . ASP A 1 292 ? -4.33622  1.73832   68.78642 1.000 21.10441 ? 286 ASP A CA  1 
ATOM   2393 C C   . ASP A 1 292 ? -3.95990  1.46076   67.33845 1.000 19.14287 ? 286 ASP A C   1 
ATOM   2394 O O   . ASP A 1 292 ? -2.77120  1.38551   66.99414 1.000 19.88613 ? 286 ASP A O   1 
ATOM   2395 C CB  . ASP A 1 292 ? -4.77290  0.45325   69.46343 1.000 20.96677 ? 286 ASP A CB  1 
ATOM   2396 C CG  . ASP A 1 292 ? -3.65444  -0.56052  69.55113 0.700 21.80668 ? 286 ASP A CG  1 
ATOM   2397 O OD1 . ASP A 1 292 ? -2.82992  -0.44489  70.48660 0.700 25.44892 ? 286 ASP A OD1 1 
ATOM   2398 O OD2 . ASP A 1 292 ? -3.59703  -1.47165  68.70503 0.700 21.94179 ? 286 ASP A OD2 1 
ATOM   2399 N N   . LEU A 1 293 ? -4.96102  1.33958   66.47159 1.000 18.02855 ? 287 LEU A N   1 
ATOM   2400 C CA  . LEU A 1 293 ? -4.67054  1.17045   65.05776 1.000 16.55200 ? 287 LEU A CA  1 
ATOM   2401 C C   . LEU A 1 293 ? -4.03889  2.43163   64.45643 1.000 18.02931 ? 287 LEU A C   1 
ATOM   2402 O O   . LEU A 1 293 ? -3.11208  2.32498   63.64552 1.000 17.44466 ? 287 LEU A O   1 
ATOM   2403 C CB  . LEU A 1 293 ? -5.95742  0.79817   64.31909 1.000 17.49640 ? 287 LEU A CB  1 
ATOM   2404 C CG  . LEU A 1 293 ? -5.81655  0.57771   62.80099 1.000 17.20200 ? 287 LEU A CG  1 
ATOM   2405 C CD1 . LEU A 1 293 ? -4.69703  -0.35067  62.43147 1.000 21.64838 ? 287 LEU A CD1 1 
ATOM   2406 C CD2 . LEU A 1 293 ? -7.16336  0.01469   62.27682 1.000 17.54117 ? 287 LEU A CD2 1 
ATOM   2407 N N   . LEU A 1 294 ? -4.54437  3.62426   64.81462 1.000 17.64308 ? 288 LEU A N   1 
ATOM   2408 C CA  . LEU A 1 294 ? -3.95258  4.88028   64.35182 1.000 17.19806 ? 288 LEU A CA  1 
ATOM   2409 C C   . LEU A 1 294 ? -2.44992  4.92913   64.64544 1.000 16.64802 ? 288 LEU A C   1 
ATOM   2410 O O   . LEU A 1 294 ? -1.62944  5.26542   63.76570 1.000 17.83197 ? 288 LEU A O   1 
ATOM   2411 C CB  . LEU A 1 294 ? -4.66765  6.05202   65.01514 1.000 16.16046 ? 288 LEU A CB  1 
ATOM   2412 C CG  . LEU A 1 294 ? -4.13227  7.42019   64.63402 1.000 17.92090 ? 288 LEU A CG  1 
ATOM   2413 C CD1 . LEU A 1 294 ? -4.30232  7.72848   63.16156 1.000 17.64352 ? 288 LEU A CD1 1 
ATOM   2414 C CD2 . LEU A 1 294 ? -4.79644  8.49407   65.48510 1.000 19.69235 ? 288 LEU A CD2 1 
ATOM   2415 N N   . ASP A 1 295 ? -2.07392  4.54889   65.87876 1.000 17.63958 ? 289 ASP A N   1 
ATOM   2416 C CA  . ASP A 1 295 ? -0.66944  4.55647   66.28593 1.000 17.52833 ? 289 ASP A CA  1 
ATOM   2417 C C   . ASP A 1 295 ? 0.17879   3.65142   65.39850 1.000 18.73015 ? 289 ASP A C   1 
ATOM   2418 O O   . ASP A 1 295 ? 1.33503   3.98902   65.04083 1.000 18.98730 ? 289 ASP A O   1 
ATOM   2419 C CB  . ASP A 1 295 ? -0.56269  4.09987   67.72970 1.000 20.70529 ? 289 ASP A CB  1 
ATOM   2420 C CG  . ASP A 1 295 ? 0.87087   4.19838   68.22794 1.000 25.68895 ? 289 ASP A CG  1 
ATOM   2421 O OD1 . ASP A 1 295 ? 1.36185   5.33127   68.35804 1.000 29.43122 ? 289 ASP A OD1 1 
ATOM   2422 O OD2 . ASP A 1 295 ? 1.52829   3.16613   68.41481 1.000 31.37249 ? 289 ASP A OD2 1 
ATOM   2423 N N   . LYS A 1 296 ? -0.36960  2.49270   65.03859 1.000 17.30008 ? 290 LYS A N   1 
ATOM   2424 C CA  . LYS A 1 296 ? 0.37331   1.54536   64.21614 1.000 18.01671 ? 290 LYS A CA  1 
ATOM   2425 C C   . LYS A 1 296 ? 0.50673   2.01310   62.76957 1.000 17.55241 ? 290 LYS A C   1 
ATOM   2426 O O   . LYS A 1 296 ? 1.50207   1.69844   62.11377 1.000 18.34230 ? 290 LYS A O   1 
ATOM   2427 C CB  . LYS A 1 296 ? -0.31117  0.17814   64.29517 1.000 18.43064 ? 290 LYS A CB  1 
ATOM   2428 C CG  . LYS A 1 296 ? -0.18574  -0.40603  65.71821 1.000 22.16990 ? 290 LYS A CG  1 
ATOM   2429 C CD  A LYS A 1 296 ? -0.96944  -1.69761  65.83617 0.500 24.69401 ? 290 LYS A CD  1 
ATOM   2430 C CD  B LYS A 1 296 ? -1.03329  -1.64171  65.86641 0.500 25.77889 ? 290 LYS A CD  1 
ATOM   2431 C CE  A LYS A 1 296 ? -0.53597  -2.55339  67.04018 0.500 24.98742 ? 290 LYS A CE  1 
ATOM   2432 C CE  B LYS A 1 296 ? -0.90991  -2.24513  67.25978 0.500 28.06593 ? 290 LYS A CE  1 
ATOM   2433 N NZ  A LYS A 1 296 ? -0.74963  -1.91600  68.37770 0.500 24.29812 ? 290 LYS A NZ  1 
ATOM   2434 N NZ  B LYS A 1 296 ? -1.41560  -3.64146  67.30325 0.500 30.95327 ? 290 LYS A NZ  1 
ATOM   2435 N N   . MET A 1 297 ? -0.47795  2.73655   62.25446 1.000 16.85647 ? 291 MET A N   1 
ATOM   2436 C CA  . MET A 1 297 ? -0.34806  3.31281   60.91059 1.000 16.86591 ? 291 MET A CA  1 
ATOM   2437 C C   . MET A 1 297 ? 0.60685   4.50364   60.87890 1.000 15.75875 ? 291 MET A C   1 
ATOM   2438 O O   . MET A 1 297 ? 1.27369   4.75431   59.85418 1.000 17.51654 ? 291 MET A O   1 
ATOM   2439 C CB  A MET A 1 297 ? -1.73709  3.69366   60.38859 0.550 17.62662 ? 291 MET A CB  1 
ATOM   2440 C CB  B MET A 1 297 ? -1.71166  3.75208   60.38886 0.450 17.65039 ? 291 MET A CB  1 
ATOM   2441 C CG  A MET A 1 297 ? -2.60549  2.44721   60.21138 0.550 18.09274 ? 291 MET A CG  1 
ATOM   2442 C CG  B MET A 1 297 ? -2.60780  2.59996   60.09410 0.450 18.29605 ? 291 MET A CG  1 
ATOM   2443 S SD  A MET A 1 297 ? -4.14230  2.69514   59.28780 0.550 21.34742 ? 291 MET A SD  1 
ATOM   2444 S SD  B MET A 1 297 ? -4.24728  3.20958   59.68635 0.450 21.02142 ? 291 MET A SD  1 
ATOM   2445 C CE  A MET A 1 297 ? -5.02136  3.79287   60.37899 0.550 20.55622 ? 291 MET A CE  1 
ATOM   2446 C CE  B MET A 1 297 ? -4.93633  1.72064   58.98192 0.450 22.49616 ? 291 MET A CE  1 
ATOM   2447 N N   . LEU A 1 298 ? 0.60192   5.30551   61.93316 1.000 16.74181 ? 292 LEU A N   1 
ATOM   2448 C CA  . LEU A 1 298 ? 1.42411   6.50940   62.00643 1.000 16.92723 ? 292 LEU A CA  1 
ATOM   2449 C C   . LEU A 1 298 ? 2.69757   6.22961   62.80152 1.000 19.36558 ? 292 LEU A C   1 
ATOM   2450 O O   . LEU A 1 298 ? 3.08629   6.95890   63.70935 1.000 23.79860 ? 292 LEU A O   1 
ATOM   2451 C CB  . LEU A 1 298 ? 0.63271   7.67096   62.59945 1.000 15.35352 ? 292 LEU A CB  1 
ATOM   2452 C CG  . LEU A 1 298 ? -0.54336  8.14400   61.73752 1.000 15.58845 ? 292 LEU A CG  1 
ATOM   2453 C CD1 . LEU A 1 298 ? -1.22376  9.35502   62.34354 1.000 18.75321 ? 292 LEU A CD1 1 
ATOM   2454 C CD2 . LEU A 1 298 ? -0.07469  8.42757   60.28817 1.000 16.10892 ? 292 LEU A CD2 1 
ATOM   2455 N N   . THR A 1 299 ? 3.32677   5.11699   62.47563 1.000 18.37635 ? 293 THR A N   1 
ATOM   2456 C CA  . THR A 1 299 ? 4.59372   4.72114   63.08171 1.000 19.63445 ? 293 THR A CA  1 
ATOM   2457 C C   . THR A 1 299 ? 5.70620   5.33016   62.26045 1.000 17.14234 ? 293 THR A C   1 
ATOM   2458 O O   . THR A 1 299 ? 5.67862   5.24939   61.02227 1.000 17.31117 ? 293 THR A O   1 
ATOM   2459 C CB  . THR A 1 299 ? 4.67109   3.19667   63.11180 1.000 21.72194 ? 293 THR A CB  1 
ATOM   2460 O OG1 . THR A 1 299 ? 3.76479   2.72923   64.10889 1.000 24.14011 ? 293 THR A OG1 1 
ATOM   2461 C CG2 . THR A 1 299 ? 6.05079   2.67477   63.41440 1.000 22.25863 ? 293 THR A CG2 1 
ATOM   2462 N N   . PHE A 1 300 ? 6.70582   5.92338   62.93863 1.000 17.23538 ? 294 PHE A N   1 
ATOM   2463 C CA  . PHE A 1 300 ? 7.75349   6.66777   62.22452 1.000 16.93028 ? 294 PHE A CA  1 
ATOM   2464 C C   . PHE A 1 300 ? 8.56332   5.74634   61.30523 1.000 18.79897 ? 294 PHE A C   1 
ATOM   2465 O O   . PHE A 1 300 ? 8.83554   6.08296   60.15035 1.000 19.13219 ? 294 PHE A O   1 
ATOM   2466 C CB  . PHE A 1 300 ? 8.66988   7.35823   63.23798 1.000 18.50531 ? 294 PHE A CB  1 
ATOM   2467 C CG  . PHE A 1 300 ? 9.86325   8.05699   62.62395 1.000 21.39934 ? 294 PHE A CG  1 
ATOM   2468 C CD1 . PHE A 1 300 ? 9.76373   9.35598   62.15773 1.000 23.67816 ? 294 PHE A CD1 1 
ATOM   2469 C CD2 . PHE A 1 300 ? 11.10216  7.40757   62.53111 1.000 24.57474 ? 294 PHE A CD2 1 
ATOM   2470 C CE1 . PHE A 1 300 ? 10.87654  10.01366  61.58824 1.000 24.56871 ? 294 PHE A CE1 1 
ATOM   2471 C CE2 . PHE A 1 300 ? 12.20423  8.04485   61.93798 1.000 25.82873 ? 294 PHE A CE2 1 
ATOM   2472 C CZ  . PHE A 1 300 ? 12.08801  9.35688   61.48268 1.000 24.49910 ? 294 PHE A CZ  1 
ATOM   2473 N N   . ASN A 1 301 ? 8.99371   4.60920   61.81970 1.000 18.26726 ? 295 ASN A N   1 
ATOM   2474 C CA  . ASN A 1 301 ? 9.85111   3.69294   61.07259 1.000 19.37549 ? 295 ASN A CA  1 
ATOM   2475 C C   . ASN A 1 301 ? 9.01617   2.96441   60.03911 1.000 19.09511 ? 295 ASN A C   1 
ATOM   2476 O O   . ASN A 1 301 ? 8.12058   2.20323   60.41999 1.000 20.26370 ? 295 ASN A O   1 
ATOM   2477 C CB  . ASN A 1 301 ? 10.48086  2.67641   62.02661 1.000 23.38280 ? 295 ASN A CB  1 
ATOM   2478 C CG  . ASN A 1 301 ? 11.50570  1.76245   61.35399 1.000 26.74371 ? 295 ASN A CG  1 
ATOM   2479 O OD1 . ASN A 1 301 ? 11.37937  1.40741   60.19244 1.000 29.73726 ? 295 ASN A OD1 1 
ATOM   2480 N ND2 . ASN A 1 301 ? 12.53294  1.35755   62.11435 1.000 28.24450 ? 295 ASN A ND2 1 
ATOM   2481 N N   . PRO A 1 302 ? 9.27918   3.13082   58.73757 1.000 17.91264 ? 296 PRO A N   1 
ATOM   2482 C CA  . PRO A 1 302 ? 8.38489   2.49789   57.74821 1.000 19.30091 ? 296 PRO A CA  1 
ATOM   2483 C C   . PRO A 1 302 ? 8.42622   0.98725   57.77475 1.000 19.72735 ? 296 PRO A C   1 
ATOM   2484 O O   . PRO A 1 302 ? 7.45249   0.34702   57.35848 1.000 21.28416 ? 296 PRO A O   1 
ATOM   2485 C CB  . PRO A 1 302 ? 8.87532   3.05314   56.39594 1.000 20.52300 ? 296 PRO A CB  1 
ATOM   2486 C CG  . PRO A 1 302 ? 10.30668  3.52540   56.64466 1.000 20.48237 ? 296 PRO A CG  1 
ATOM   2487 C CD  . PRO A 1 302 ? 10.33949  3.95237   58.13139 1.000 18.63649 ? 296 PRO A CD  1 
ATOM   2488 N N   . HIS A 1 303 ? 9.52588   0.38828   58.24052 1.000 21.49687 ? 297 HIS A N   1 
ATOM   2489 C CA  . HIS A 1 303 ? 9.61189   -1.06422  58.32143 1.000 22.90595 ? 297 HIS A CA  1 
ATOM   2490 C C   . HIS A 1 303 ? 8.77928   -1.61567  59.47583 1.000 24.63119 ? 297 HIS A C   1 
ATOM   2491 O O   . HIS A 1 303 ? 8.34949   -2.77051  59.43208 1.000 29.96136 ? 297 HIS A O   1 
ATOM   2492 C CB  . HIS A 1 303 ? 11.07894  -1.46682  58.49389 0.800 25.16445 ? 297 HIS A CB  1 
ATOM   2493 C CG  . HIS A 1 303 ? 11.95854  -0.98591  57.38538 0.600 30.19340 ? 297 HIS A CG  1 
ATOM   2494 N ND1 . HIS A 1 303 ? 11.87396  -1.48157  56.10337 0.600 34.52778 ? 297 HIS A ND1 1 
ATOM   2495 C CD2 . HIS A 1 303 ? 12.89135  -0.00545  57.34893 0.600 33.60723 ? 297 HIS A CD2 1 
ATOM   2496 C CE1 . HIS A 1 303 ? 12.75261  -0.86268  55.33439 0.600 36.57857 ? 297 HIS A CE1 1 
ATOM   2497 N NE2 . HIS A 1 303 ? 13.38010  0.04218   56.06453 0.600 36.46398 ? 297 HIS A NE2 1 
ATOM   2498 N N   . LYS A 1 304 ? 8.56763   -0.82602  60.52898 1.000 22.79101 ? 298 LYS A N   1 
ATOM   2499 C CA  . LYS A 1 304 ? 7.74414   -1.26106  61.65886 1.000 21.01903 ? 298 LYS A CA  1 
ATOM   2500 C C   . LYS A 1 304 ? 6.27822   -0.90734  61.47603 1.000 20.27323 ? 298 LYS A C   1 
ATOM   2501 O O   . LYS A 1 304 ? 5.43770   -1.41005  62.22492 1.000 22.30328 ? 298 LYS A O   1 
ATOM   2502 C CB  . LYS A 1 304 ? 8.24305   -0.63906  62.96745 1.000 22.80623 ? 298 LYS A CB  1 
ATOM   2503 C CG  . LYS A 1 304 ? 9.65126   -1.03919  63.37367 1.000 26.83387 ? 298 LYS A CG  1 
ATOM   2504 C CD  . LYS A 1 304 ? 10.06148  -0.37600  64.67899 0.800 28.52622 ? 298 LYS A CD  1 
ATOM   2505 C CE  . LYS A 1 304 ? 11.43498  -0.89652  65.08111 0.700 30.64995 ? 298 LYS A CE  1 
ATOM   2506 N NZ  . LYS A 1 304 ? 12.09453  -0.04264  66.08395 0.700 34.52946 ? 298 LYS A NZ  1 
ATOM   2507 N N   . ARG A 1 305 ? 5.97821   -0.05303  60.51178 1.000 17.98055 ? 299 ARG A N   1 
ATOM   2508 C CA  . ARG A 1 305 ? 4.61769   0.39981   60.26004 1.000 16.15058 ? 299 ARG A CA  1 
ATOM   2509 C C   . ARG A 1 305 ? 3.73649   -0.78321  59.84527 1.000 16.27890 ? 299 ARG A C   1 
ATOM   2510 O O   . ARG A 1 305 ? 4.15763   -1.66484  59.08167 1.000 18.76068 ? 299 ARG A O   1 
ATOM   2511 C CB  . ARG A 1 305 ? 4.64913   1.48364   59.15825 1.000 16.09298 ? 299 ARG A CB  1 
ATOM   2512 C CG  . ARG A 1 305 ? 3.32912   2.31439   59.00339 1.000 16.05121 ? 299 ARG A CG  1 
ATOM   2513 C CD  . ARG A 1 305 ? 3.51979   3.46166   57.98282 1.000 15.11244 ? 299 ARG A CD  1 
ATOM   2514 N NE  . ARG A 1 305 ? 4.61769   4.34139   58.40808 1.000 16.78681 ? 299 ARG A NE  1 
ATOM   2515 C CZ  . ARG A 1 305 ? 5.45628   4.99804   57.61265 1.000 16.49164 ? 299 ARG A CZ  1 
ATOM   2516 N NH1 . ARG A 1 305 ? 5.34510   4.95096   56.28358 1.000 14.97982 ? 299 ARG A NH1 1 
ATOM   2517 N NH2 . ARG A 1 305 ? 6.46776   5.68752   58.16382 1.000 16.30341 ? 299 ARG A NH2 1 
ATOM   2518 N N   . ILE A 1 306 ? 2.49938   -0.80345  60.35038 1.000 15.94296 ? 300 ILE A N   1 
ATOM   2519 C CA  . ILE A 1 306 ? 1.56712   -1.88513  60.01352 1.000 16.06764 ? 300 ILE A CA  1 
ATOM   2520 C C   . ILE A 1 306 ? 1.32467   -1.94982  58.50218 1.000 16.05424 ? 300 ILE A C   1 
ATOM   2521 O O   . ILE A 1 306 ? 1.26319   -0.91309  57.80795 1.000 16.41981 ? 300 ILE A O   1 
ATOM   2522 C CB  . ILE A 1 306 ? 0.25613   -1.67638  60.80130 1.000 17.05473 ? 300 ILE A CB  1 
ATOM   2523 C CG1 . ILE A 1 306 ? -0.57057  -2.94762  60.86231 1.000 17.97267 ? 300 ILE A CG1 1 
ATOM   2524 C CG2 . ILE A 1 306 ? -0.57295  -0.52543  60.22548 1.000 18.86276 ? 300 ILE A CG2 1 
ATOM   2525 C CD1 . ILE A 1 306 ? -1.67274  -2.90222  61.90453 1.000 18.52468 ? 300 ILE A CD1 1 
ATOM   2526 N N   . GLU A 1 307 ? 1.18859   -3.17872  57.98165 1.000 15.69720 ? 301 GLU A N   1 
ATOM   2527 C CA  . GLU A 1 307 ? 0.83048   -3.40314  56.57846 1.000 16.68676 ? 301 GLU A CA  1 
ATOM   2528 C C   . GLU A 1 307 ? -0.68245  -3.55652  56.43004 1.000 17.27185 ? 301 GLU A C   1 
ATOM   2529 O O   . GLU A 1 307 ? -1.40267  -3.74971  57.40915 1.000 17.23738 ? 301 GLU A O   1 
ATOM   2530 C CB  . GLU A 1 307 ? 1.54485   -4.61691  55.98645 1.000 18.42954 ? 301 GLU A CB  1 
ATOM   2531 C CG  . GLU A 1 307 ? 3.07698   -4.45590  55.96940 1.000 22.73858 ? 301 GLU A CG  1 
ATOM   2532 C CD  . GLU A 1 307 ? 3.77968   -5.48994  55.09044 0.900 27.10270 ? 301 GLU A CD  1 
ATOM   2533 O OE1 . GLU A 1 307 ? 5.01173   -5.35197  54.89598 0.700 28.19171 ? 301 GLU A OE1 1 
ATOM   2534 O OE2 . GLU A 1 307 ? 3.12769   -6.45490  54.62189 0.700 29.43862 ? 301 GLU A OE2 1 
ATOM   2535 N N   . VAL A 1 308 ? -1.15808  -3.45901  55.18190 1.000 16.61166 ? 302 VAL A N   1 
ATOM   2536 C CA  . VAL A 1 308 ? -2.60833  -3.38167  54.95283 1.000 15.70683 ? 302 VAL A CA  1 
ATOM   2537 C C   . VAL A 1 308 ? -3.34382  -4.61662  55.48654 1.000 15.31099 ? 302 VAL A C   1 
ATOM   2538 O O   . VAL A 1 308 ? -4.44084  -4.48720  56.06630 1.000 17.94313 ? 302 VAL A O   1 
ATOM   2539 C CB  . VAL A 1 308 ? -2.90828  -3.09378  53.46479 1.000 15.67958 ? 302 VAL A CB  1 
ATOM   2540 C CG1 . VAL A 1 308 ? -2.47945  -4.26474  52.52869 1.000 17.46809 ? 302 VAL A CG1 1 
ATOM   2541 C CG2 . VAL A 1 308 ? -4.42376  -2.75305  53.27889 1.000 17.65264 ? 302 VAL A CG2 1 
ATOM   2542 N N   . GLU A 1 309 ? -2.79891  -5.83351  55.28577 1.000 17.47439 ? 303 GLU A N   1 
ATOM   2543 C CA  . GLU A 1 309 ? -3.51141  -7.02215  55.74447 1.000 19.32358 ? 303 GLU A CA  1 
ATOM   2544 C C   . GLU A 1 309 ? -3.54384  -7.12093  57.26449 1.000 19.66923 ? 303 GLU A C   1 
ATOM   2545 O O   . GLU A 1 309 ? -4.53810  -7.61512  57.83439 1.000 19.40014 ? 303 GLU A O   1 
ATOM   2546 C CB  . GLU A 1 309 ? -2.92989  -8.28859  55.10617 0.900 20.30005 ? 303 GLU A CB  1 
ATOM   2547 C CG  . GLU A 1 309 ? -3.28437  -8.35483  53.60585 0.800 23.23222 ? 303 GLU A CG  1 
ATOM   2548 C CD  . GLU A 1 309 ? -2.51554  -9.43011  52.85973 0.600 28.63668 ? 303 GLU A CD  1 
ATOM   2549 O OE1 . GLU A 1 309 ? -1.36985  -9.70616  53.24196 0.600 32.51519 ? 303 GLU A OE1 1 
ATOM   2550 O OE2 . GLU A 1 309 ? -3.02676  -9.95419  51.85047 0.600 31.02223 ? 303 GLU A OE2 1 
ATOM   2551 N N   . GLN A 1 310 ? -2.48834  -6.65472  57.93479 1.000 18.24629 ? 304 GLN A N   1 
ATOM   2552 C CA  A GLN A 1 310 ? -2.50544  -6.58291  59.40136 0.700 17.52743 ? 304 GLN A CA  1 
ATOM   2553 C CA  B GLN A 1 310 ? -2.51592  -6.60673  59.39658 0.300 19.90582 ? 304 GLN A CA  1 
ATOM   2554 C C   . GLN A 1 310 ? -3.51854  -5.57697  59.89418 1.000 18.56420 ? 304 GLN A C   1 
ATOM   2555 O O   . GLN A 1 310 ? -4.19527  -5.80726  60.91210 1.000 20.41850 ? 304 GLN A O   1 
ATOM   2556 C CB  A GLN A 1 310 ? -1.15422  -6.15587  59.95728 0.700 20.79555 ? 304 GLN A CB  1 
ATOM   2557 C CB  B GLN A 1 310 ? -1.11813  -6.30587  59.95039 0.300 24.00514 ? 304 GLN A CB  1 
ATOM   2558 C CG  A GLN A 1 310 ? -0.02743  -7.00090  59.63724 0.700 20.57738 ? 304 GLN A CG  1 
ATOM   2559 C CG  B GLN A 1 310 ? -0.48742  -7.41134  60.80772 0.300 26.76815 ? 304 GLN A CG  1 
ATOM   2560 C CD  A GLN A 1 310 ? 1.26373   -6.39044  60.20147 0.700 20.50397 ? 304 GLN A CD  1 
ATOM   2561 C CD  B GLN A 1 310 ? -1.12301  -7.58334  62.20282 0.300 29.19779 ? 304 GLN A CD  1 
ATOM   2562 O OE1 A GLN A 1 310 ? 1.85396   -5.51351  59.57151 0.700 19.13421 ? 304 GLN A OE1 1 
ATOM   2563 O OE1 B GLN A 1 310 ? -2.34521  -7.61481  62.35076 0.300 32.22470 ? 304 GLN A OE1 1 
ATOM   2564 N NE2 A GLN A 1 310 ? 1.68906   -6.84903  61.37463 0.700 22.84570 ? 304 GLN A NE2 1 
ATOM   2565 N NE2 B GLN A 1 310 ? -0.27457  -7.70915  63.23134 0.300 28.85489 ? 304 GLN A NE2 1 
ATOM   2566 N N   . ALA A 1 311 ? -3.59800  -4.43334  59.21528 1.000 18.65936 ? 305 ALA A N   1 
ATOM   2567 C CA  . ALA A 1 311 ? -4.56103  -3.41113  59.60856 1.000 18.26759 ? 305 ALA A CA  1 
ATOM   2568 C C   . ALA A 1 311 ? -5.98329  -3.94426  59.49890 1.000 18.34720 ? 305 ALA A C   1 
ATOM   2569 O O   . ALA A 1 311 ? -6.79523  -3.72094  60.40479 1.000 17.87688 ? 305 ALA A O   1 
ATOM   2570 C CB  . ALA A 1 311 ? -4.37428  -2.13918  58.76815 1.000 16.65095 ? 305 ALA A CB  1 
ATOM   2571 N N   . LEU A 1 312 ? -6.29074  -4.68084  58.41873 1.000 15.94918 ? 306 LEU A N   1 
ATOM   2572 C CA  . LEU A 1 312 ? -7.63699  -5.25039  58.27273 1.000 16.33755 ? 306 LEU A CA  1 
ATOM   2573 C C   . LEU A 1 312 ? -7.97887  -6.19604  59.42775 1.000 17.77518 ? 306 LEU A C   1 
ATOM   2574 O O   . LEU A 1 312 ? -9.13940  -6.27025  59.85136 1.000 18.52372 ? 306 LEU A O   1 
ATOM   2575 C CB  . LEU A 1 312 ? -7.75639  -5.97789  56.91139 1.000 17.83187 ? 306 LEU A CB  1 
ATOM   2576 C CG  . LEU A 1 312 ? -8.01112  -5.04185  55.72030 1.000 15.20032 ? 306 LEU A CG  1 
ATOM   2577 C CD1 . LEU A 1 312 ? -7.66089  -5.77221  54.41600 1.000 17.64719 ? 306 LEU A CD1 1 
ATOM   2578 C CD2 . LEU A 1 312 ? -9.47874  -4.47606  55.68533 1.000 16.28835 ? 306 LEU A CD2 1 
ATOM   2579 N N   . ALA A 1 313 ? -6.99019  -6.88134  59.97506 1.000 18.69991 ? 307 ALA A N   1 
ATOM   2580 C CA  . ALA A 1 313 ? -7.17971  -7.85476  61.04337 1.000 18.79220 ? 307 ALA A CA  1 
ATOM   2581 C C   . ALA A 1 313 ? -7.12915  -7.23174  62.44231 1.000 19.49917 ? 307 ALA A C   1 
ATOM   2582 O O   . ALA A 1 313 ? -7.20463  -7.96692  63.44324 1.000 22.26810 ? 307 ALA A O   1 
ATOM   2583 C CB  . ALA A 1 313 ? -6.10937  -8.95901  60.94174 1.000 20.64629 ? 307 ALA A CB  1 
ATOM   2584 N N   . HIS A 1 314 ? -7.02668  -5.92038  62.53679 1.000 18.39651 ? 308 HIS A N   1 
ATOM   2585 C CA  . HIS A 1 314 ? -6.95993  -5.26301  63.82678 1.000 20.04631 ? 308 HIS A CA  1 
ATOM   2586 C C   . HIS A 1 314 ? -8.32335  -5.30749  64.52627 1.000 20.29662 ? 308 HIS A C   1 
ATOM   2587 O O   . HIS A 1 314 ? -9.36965  -5.18662  63.86603 1.000 20.77275 ? 308 HIS A O   1 
ATOM   2588 C CB  . HIS A 1 314 ? -6.50101  -3.81487  63.61490 1.000 19.89770 ? 308 HIS A CB  1 
ATOM   2589 C CG  . HIS A 1 314 ? -6.19567  -3.09459  64.88447 1.000 19.92033 ? 308 HIS A CG  1 
ATOM   2590 N ND1 . HIS A 1 314 ? -7.18129  -2.53018  65.66543 1.000 18.88026 ? 308 HIS A ND1 1 
ATOM   2591 C CD2 . HIS A 1 314 ? -5.01956  -2.83194  65.50420 1.000 21.71066 ? 308 HIS A CD2 1 
ATOM   2592 C CE1 . HIS A 1 314 ? -6.62431  -1.98685  66.74228 1.000 20.96888 ? 308 HIS A CE1 1 
ATOM   2593 N NE2 . HIS A 1 314 ? -5.31133  -2.15064  66.66099 1.000 22.19479 ? 308 HIS A NE2 1 
ATOM   2594 N N   . PRO A 1 315 ? -8.34290  -5.42535  65.85315 1.000 22.33722 ? 309 PRO A N   1 
ATOM   2595 C CA  . PRO A 1 315 ? -9.61839  -5.49617  66.58845 1.000 21.90569 ? 309 PRO A CA  1 
ATOM   2596 C C   . PRO A 1 315 ? -10.58608 -4.36510  66.28189 1.000 20.62532 ? 309 PRO A C   1 
ATOM   2597 O O   . PRO A 1 315 ? -11.80813 -4.56236  66.37229 1.000 22.22649 ? 309 PRO A O   1 
ATOM   2598 C CB  . PRO A 1 315 ? -9.16240  -5.45665  68.05556 1.000 23.95421 ? 309 PRO A CB  1 
ATOM   2599 C CG  . PRO A 1 315 ? -7.84637  -6.14397  68.02444 1.000 24.60664 ? 309 PRO A CG  1 
ATOM   2600 C CD  . PRO A 1 315 ? -7.19030  -5.69701  66.72551 1.000 23.95001 ? 309 PRO A CD  1 
ATOM   2601 N N   . TYR A 1 316 ? -10.09126 -3.17828  65.93668 1.000 21.22217 ? 310 TYR A N   1 
ATOM   2602 C CA  . TYR A 1 316 ? -11.01126 -2.08406  65.63416 1.000 20.39849 ? 310 TYR A CA  1 
ATOM   2603 C C   . TYR A 1 316 ? -11.97360 -2.45602  64.50080 1.000 20.15609 ? 310 TYR A C   1 
ATOM   2604 O O   . TYR A 1 316 ? -13.12373 -1.99469  64.49316 1.000 21.47143 ? 310 TYR A O   1 
ATOM   2605 C CB  . TYR A 1 316 ? -10.22794 -0.80614  65.29483 1.000 20.57774 ? 310 TYR A CB  1 
ATOM   2606 C CG  . TYR A 1 316 ? -11.11013 0.38497   64.98708 1.000 22.28263 ? 310 TYR A CG  1 
ATOM   2607 C CD1 . TYR A 1 316 ? -12.09661 0.79856   65.89940 1.000 23.07532 ? 310 TYR A CD1 1 
ATOM   2608 C CD2 . TYR A 1 316 ? -10.99691 1.07354   63.77763 1.000 21.72706 ? 310 TYR A CD2 1 
ATOM   2609 C CE1 . TYR A 1 316 ? -12.92848 1.89434   65.63194 1.000 23.62418 ? 310 TYR A CE1 1 
ATOM   2610 C CE2 . TYR A 1 316 ? -11.81784 2.17013   63.50777 1.000 23.44395 ? 310 TYR A CE2 1 
ATOM   2611 C CZ  . TYR A 1 316 ? -12.78902 2.56634   64.43484 1.000 26.42333 ? 310 TYR A CZ  1 
ATOM   2612 O OH  . TYR A 1 316 ? -13.61792 3.64529   64.15387 1.000 28.34596 ? 310 TYR A OH  1 
ATOM   2613 N N   . LEU A 1 317 ? -11.53260 -3.30507  63.55779 1.000 20.33186 ? 311 LEU A N   1 
ATOM   2614 C CA  . LEU A 1 317 ? -12.31892 -3.63832  62.37213 1.000 20.38298 ? 311 LEU A CA  1 
ATOM   2615 C C   . LEU A 1 317 ? -12.98772 -5.01592  62.47811 1.000 21.34118 ? 311 LEU A C   1 
ATOM   2616 O O   . LEU A 1 317 ? -13.47802 -5.53910  61.46345 1.000 21.11123 ? 311 LEU A O   1 
ATOM   2617 C CB  . LEU A 1 317 ? -11.41685 -3.54788  61.11460 1.000 20.04612 ? 311 LEU A CB  1 
ATOM   2618 C CG  . LEU A 1 317 ? -10.80640 -2.13186  60.92813 1.000 19.57040 ? 311 LEU A CG  1 
ATOM   2619 C CD1 . LEU A 1 317 ? -9.81360  -2.11038  59.75532 1.000 21.21528 ? 311 LEU A CD1 1 
ATOM   2620 C CD2 . LEU A 1 317 ? -11.91781 -1.04204  60.74145 1.000 20.64232 ? 311 LEU A CD2 1 
ATOM   2621 N N   . GLU A 1 318 ? -13.03149 -5.61377  63.68344 1.000 22.43874 ? 312 GLU A N   1 
ATOM   2622 C CA  . GLU A 1 318 ? -13.51411 -6.99539  63.82246 1.000 24.46954 ? 312 GLU A CA  1 
ATOM   2623 C C   . GLU A 1 318 ? -14.93855 -7.19405  63.28579 1.000 24.37985 ? 312 GLU A C   1 
ATOM   2624 O O   . GLU A 1 318 ? -15.25377 -8.27974  62.80665 1.000 27.09660 ? 312 GLU A O   1 
ATOM   2625 C CB  A GLU A 1 318 ? -13.42186 -7.44557  65.28456 0.500 27.40441 ? 312 GLU A CB  1 
ATOM   2626 C CB  B GLU A 1 318 ? -13.41289 -7.46094  65.29418 0.500 27.44288 ? 312 GLU A CB  1 
ATOM   2627 C CG  A GLU A 1 318 ? -13.87138 -8.89796  65.51954 0.500 31.53555 ? 312 GLU A CG  1 
ATOM   2628 C CG  B GLU A 1 318 ? -14.05676 -6.55420  66.36764 0.500 30.86882 ? 312 GLU A CG  1 
ATOM   2629 C CD  A GLU A 1 318 ? -13.52220 -9.41815  66.90712 0.500 37.98178 ? 312 GLU A CD  1 
ATOM   2630 C CD  B GLU A 1 318 ? -13.46638 -6.74390  67.81377 0.500 35.81993 ? 312 GLU A CD  1 
ATOM   2631 O OE1 A GLU A 1 318 ? -12.81487 -8.70830  67.64748 0.500 41.21660 ? 312 GLU A OE1 1 
ATOM   2632 O OE1 B GLU A 1 318 ? -13.22543 -7.89620  68.23196 0.500 39.37202 ? 312 GLU A OE1 1 
ATOM   2633 O OE2 A GLU A 1 318 ? -13.96906 -10.52894 67.26632 0.500 40.33241 ? 312 GLU A OE2 1 
ATOM   2634 O OE2 B GLU A 1 318 ? -13.17843 -5.73870  68.50686 0.500 33.40481 ? 312 GLU A OE2 1 
ATOM   2635 N N   . GLN A 1 319 ? -15.79074 -6.16518  63.30979 1.000 23.35067 ? 313 GLN A N   1 
ATOM   2636 C CA  . GLN A 1 319 ? -17.16990 -6.31097  62.81806 1.000 25.02713 ? 313 GLN A CA  1 
ATOM   2637 C C   . GLN A 1 319 ? -17.22490 -6.58642  61.31769 1.000 24.24624 ? 313 GLN A C   1 
ATOM   2638 O O   . GLN A 1 319 ? -18.20580 -7.17733  60.83768 1.000 27.89628 ? 313 GLN A O   1 
ATOM   2639 C CB  . GLN A 1 319 ? -17.92842 -5.02055  63.11382 1.000 25.95143 ? 313 GLN A CB  1 
ATOM   2640 C CG  . GLN A 1 319 ? -18.35722 -4.88405  64.50791 0.700 28.97588 ? 313 GLN A CG  1 
ATOM   2641 C CD  . GLN A 1 319 ? -18.65573 -3.43778  64.80472 0.600 33.73645 ? 313 GLN A CD  1 
ATOM   2642 O OE1 . GLN A 1 319 ? -18.15219 -2.53426  64.09810 0.600 34.44196 ? 313 GLN A OE1 1 
ATOM   2643 N NE2 . GLN A 1 319 ? -19.58205 -3.20443  65.72908 0.600 35.98338 ? 313 GLN A NE2 1 
ATOM   2644 N N   . TYR A 1 320 ? -16.19562 -6.17476  60.57774 1.000 23.93434 ? 314 TYR A N   1 
ATOM   2645 C CA  . TYR A 1 320 ? -16.16596 -6.24427  59.12409 1.000 22.42166 ? 314 TYR A CA  1 
ATOM   2646 C C   . TYR A 1 320 ? -15.17697 -7.26110  58.57663 1.000 23.17129 ? 314 TYR A C   1 
ATOM   2647 O O   . TYR A 1 320 ? -15.37554 -7.77384  57.45976 1.000 23.18564 ? 314 TYR A O   1 
ATOM   2648 C CB  . TYR A 1 320 ? -15.81855 -4.85429  58.53849 1.000 23.56200 ? 314 TYR A CB  1 
ATOM   2649 C CG  . TYR A 1 320 ? -16.86839 -3.81747  58.87649 1.000 25.20951 ? 314 TYR A CG  1 
ATOM   2650 C CD1 . TYR A 1 320 ? -18.15062 -3.91698  58.34552 1.000 27.81040 ? 314 TYR A CD1 1 
ATOM   2651 C CD2 . TYR A 1 320 ? -16.60988 -2.78713  59.76074 1.000 26.35536 ? 314 TYR A CD2 1 
ATOM   2652 C CE1 . TYR A 1 320 ? -19.11516 -3.00294  58.65512 1.000 31.21852 ? 314 TYR A CE1 1 
ATOM   2653 C CE2 . TYR A 1 320 ? -17.58495 -1.85340  60.09334 1.000 27.34260 ? 314 TYR A CE2 1 
ATOM   2654 C CZ  . TYR A 1 320 ? -18.83507 -1.97276  59.53153 1.000 30.58694 ? 314 TYR A CZ  1 
ATOM   2655 O OH  . TYR A 1 320 ? -19.82741 -1.06568  59.84074 1.000 33.51929 ? 314 TYR A OH  1 
ATOM   2656 N N   . TYR A 1 321 ? -14.11889 -7.56537  59.33343 1.000 21.75947 ? 315 TYR A N   1 
ATOM   2657 C CA  . TYR A 1 321 ? -13.00546 -8.34987  58.80407 1.000 22.16716 ? 315 TYR A CA  1 
ATOM   2658 C C   . TYR A 1 321 ? -13.43890 -9.73379  58.32880 1.000 22.69423 ? 315 TYR A C   1 
ATOM   2659 O O   . TYR A 1 321 ? -14.01353 -10.52922 59.08636 1.000 26.60126 ? 315 TYR A O   1 
ATOM   2660 C CB  . TYR A 1 321 ? -11.94145 -8.49127  59.87612 1.000 22.42474 ? 315 TYR A CB  1 
ATOM   2661 C CG  . TYR A 1 321 ? -10.72017 -9.27578  59.46802 1.000 22.40562 ? 315 TYR A CG  1 
ATOM   2662 C CD1 . TYR A 1 321 ? -9.97065  -8.92893  58.33084 1.000 23.17328 ? 315 TYR A CD1 1 
ATOM   2663 C CD2 . TYR A 1 321 ? -10.27515 -10.33155 60.25816 1.000 24.63137 ? 315 TYR A CD2 1 
ATOM   2664 C CE1 . TYR A 1 321 ? -8.82154  -9.63165  57.99903 1.000 23.63766 ? 315 TYR A CE1 1 
ATOM   2665 C CE2 . TYR A 1 321 ? -9.13784  -11.03387 59.94780 1.000 23.20891 ? 315 TYR A CE2 1 
ATOM   2666 C CZ  . TYR A 1 321 ? -8.40410  -10.67602 58.82437 1.000 24.90375 ? 315 TYR A CZ  1 
ATOM   2667 O OH  . TYR A 1 321 ? -7.28522  -11.39248 58.52987 1.000 26.26548 ? 315 TYR A OH  1 
ATOM   2668 N N   . ASP A 1 322 ? -13.10885 -10.02580 57.06625 1.000 21.02823 ? 316 ASP A N   1 
ATOM   2669 C CA  . ASP A 1 322 ? -13.41683 -11.30065 56.46493 1.000 23.01566 ? 316 ASP A CA  1 
ATOM   2670 C C   . ASP A 1 322 ? -12.46761 -11.51968 55.28834 1.000 22.81255 ? 316 ASP A C   1 
ATOM   2671 O O   . ASP A 1 322 ? -12.74420 -11.03197 54.17908 1.000 22.74907 ? 316 ASP A O   1 
ATOM   2672 C CB  . ASP A 1 322 ? -14.87839 -11.31544 56.02406 1.000 25.33806 ? 316 ASP A CB  1 
ATOM   2673 C CG  . ASP A 1 322 ? -15.24964 -12.57281 55.26861 0.800 26.42570 ? 316 ASP A CG  1 
ATOM   2674 O OD1 . ASP A 1 322 ? -14.45405 -13.54127 55.26485 0.700 28.73571 ? 316 ASP A OD1 1 
ATOM   2675 O OD2 . ASP A 1 322 ? -16.33778 -12.58208 54.65362 0.700 27.23071 ? 316 ASP A OD2 1 
ATOM   2676 N N   . PRO A 1 323 ? -11.32903 -12.20528 55.49939 1.000 23.30743 ? 317 PRO A N   1 
ATOM   2677 C CA  . PRO A 1 323 ? -10.30478 -12.27757 54.43342 1.000 22.88889 ? 317 PRO A CA  1 
ATOM   2678 C C   . PRO A 1 323 ? -10.80449 -12.87172 53.12296 1.000 23.60022 ? 317 PRO A C   1 
ATOM   2679 O O   . PRO A 1 323 ? -10.33724 -12.45911 52.05019 1.000 23.81146 ? 317 PRO A O   1 
ATOM   2680 C CB  . PRO A 1 323 ? -9.20407  -13.15904 55.06026 1.000 24.97659 ? 317 PRO A CB  1 
ATOM   2681 C CG  . PRO A 1 323 ? -9.39350  -13.02667 56.55707 1.000 25.62497 ? 317 PRO A CG  1 
ATOM   2682 C CD  . PRO A 1 323 ? -10.87180 -12.81625 56.77264 1.000 24.09541 ? 317 PRO A CD  1 
ATOM   2683 N N   . SER A 1 324 ? -11.75440 -13.80716 53.17290 1.000 24.07388 ? 318 SER A N   1 
ATOM   2684 C CA  . SER A 1 324 ? -12.31205 -14.39926 51.95688 1.000 24.32799 ? 318 SER A CA  1 
ATOM   2685 C C   . SER A 1 324 ? -13.21750 -13.43507 51.19128 1.000 23.27902 ? 318 SER A C   1 
ATOM   2686 O O   . SER A 1 324 ? -13.56117 -13.72591 50.03714 1.000 25.41373 ? 318 SER A O   1 
ATOM   2687 C CB  . SER A 1 324 ? -13.09387 -15.66620 52.28927 1.000 26.15555 ? 318 SER A CB  1 
ATOM   2688 O OG  . SER A 1 324 ? -14.33688 -15.34458 52.94937 1.000 31.19460 ? 318 SER A OG  1 
ATOM   2689 N N   . ASP A 1 325 ? -13.60931 -12.29997 51.78800 1.000 20.55345 ? 319 ASP A N   1 
ATOM   2690 C CA  . ASP A 1 325 ? -14.37056 -11.26125 51.10477 1.000 21.45323 ? 319 ASP A CA  1 
ATOM   2691 C C   . ASP A 1 325 ? -13.54145 -9.99812  50.91785 1.000 20.29777 ? 319 ASP A C   1 
ATOM   2692 O O   . ASP A 1 325 ? -14.08556 -8.89049  50.80730 1.000 19.75588 ? 319 ASP A O   1 
ATOM   2693 C CB  . ASP A 1 325 ? -15.65412 -10.96346 51.88375 1.000 24.64009 ? 319 ASP A CB  1 
ATOM   2694 C CG  . ASP A 1 325 ? -16.64657 -10.09108 51.10832 1.000 29.87635 ? 319 ASP A CG  1 
ATOM   2695 O OD1 . ASP A 1 325 ? -16.80793 -10.26720 49.87918 1.000 30.61818 ? 319 ASP A OD1 1 
ATOM   2696 O OD2 . ASP A 1 325 ? -17.24740 -9.19565  51.74347 1.000 33.15304 ? 319 ASP A OD2 1 
ATOM   2697 N N   . GLU A 1 326 ? -12.21404 -10.15697 50.87678 1.000 20.67825 ? 320 GLU A N   1 
ATOM   2698 C CA  . GLU A 1 326 ? -11.29200 -9.03901  50.73258 1.000 19.67385 ? 320 GLU A CA  1 
ATOM   2699 C C   . GLU A 1 326 ? -10.36771 -9.42108  49.57437 1.000 19.90771 ? 320 GLU A C   1 
ATOM   2700 O O   . GLU A 1 326 ? -9.22845  -9.88038  49.78248 1.000 20.41975 ? 320 GLU A O   1 
ATOM   2701 C CB  . GLU A 1 326 ? -10.52655 -8.80281  52.03803 1.000 20.92954 ? 320 GLU A CB  1 
ATOM   2702 C CG  . GLU A 1 326 ? -11.28578 -7.91250  53.06481 1.000 23.16878 ? 320 GLU A CG  1 
ATOM   2703 C CD  . GLU A 1 326 ? -11.04852 -8.27355  54.52709 1.000 25.36811 ? 320 GLU A CD  1 
ATOM   2704 O OE1 . GLU A 1 326 ? -11.96326 -8.08053  55.38029 1.000 25.31977 ? 320 GLU A OE1 1 
ATOM   2705 O OE2 . GLU A 1 326 ? -9.93982  -8.79589  54.82961 1.000 22.94763 ? 320 GLU A OE2 1 
ATOM   2706 N N   . PRO A 1 327 ? -10.82553 -9.26979  48.33598 1.000 18.33898 ? 321 PRO A N   1 
ATOM   2707 C CA  . PRO A 1 327 ? -10.12258 -9.91922  47.21237 1.000 20.28911 ? 321 PRO A CA  1 
ATOM   2708 C C   . PRO A 1 327 ? -8.80629  -9.24073  46.82814 1.000 19.51551 ? 321 PRO A C   1 
ATOM   2709 O O   . PRO A 1 327 ? -8.55350  -8.07113  47.11785 1.000 20.27078 ? 321 PRO A O   1 
ATOM   2710 C CB  . PRO A 1 327 ? -11.13402 -9.84942  46.06260 1.000 23.14524 ? 321 PRO A CB  1 
ATOM   2711 C CG  . PRO A 1 327 ? -12.11762 -8.79842  46.42444 1.000 22.29052 ? 321 PRO A CG  1 
ATOM   2712 C CD  . PRO A 1 327 ? -12.14555 -8.73967  47.95953 1.000 18.68550 ? 321 PRO A CD  1 
ATOM   2713 N N   . ILE A 1 328 ? -7.97680  -10.00107 46.11037 1.000 17.92245 ? 322 ILE A N   1 
ATOM   2714 C CA  . ILE A 1 328 ? -6.72020  -9.49969  45.58291 1.000 18.59718 ? 322 ILE A CA  1 
ATOM   2715 C C   . ILE A 1 328 ? -6.75659  -9.56951  44.06010 1.000 18.94865 ? 322 ILE A C   1 
ATOM   2716 O O   . ILE A 1 328 ? -7.66037  -10.16031 43.43480 1.000 20.70048 ? 322 ILE A O   1 
ATOM   2717 C CB  . ILE A 1 328 ? -5.50604  -10.24157 46.17038 1.000 19.95344 ? 322 ILE A CB  1 
ATOM   2718 C CG1 . ILE A 1 328 ? -5.55805  -11.74464 45.85926 1.000 21.24277 ? 322 ILE A CG1 1 
ATOM   2719 C CG2 . ILE A 1 328 ? -5.47928  -10.05731 47.71353 1.000 21.04182 ? 322 ILE A CG2 1 
ATOM   2720 C CD1 . ILE A 1 328 ? -4.24748  -12.46250 46.20293 1.000 25.18030 ? 322 ILE A CD1 1 
ATOM   2721 N N   . ALA A 1 329 ? -5.77773  -8.91342  43.47795 1.000 18.52533 ? 323 ALA A N   1 
ATOM   2722 C CA  . ALA A 1 329 ? -5.69507  -8.75765  42.03680 1.000 20.80901 ? 323 ALA A CA  1 
ATOM   2723 C C   . ALA A 1 329 ? -5.31983  -10.07415 41.36207 1.000 25.48560 ? 323 ALA A C   1 
ATOM   2724 O O   . ALA A 1 329 ? -4.48566  -10.83932 41.85822 1.000 26.63158 ? 323 ALA A O   1 
ATOM   2725 C CB  . ALA A 1 329 ? -4.68652  -7.66212  41.70687 1.000 23.40631 ? 323 ALA A CB  1 
ATOM   2726 N N   . GLU A 1 330 ? -5.95840  -10.33350 40.21648 1.000 29.19636 ? 324 GLU A N   1 
ATOM   2727 C CA  . GLU A 1 330 ? -5.66035  -11.52997 39.44031 1.000 36.11379 ? 324 GLU A CA  1 
ATOM   2728 C C   . GLU A 1 330 ? -4.29916  -11.41949 38.78476 1.000 41.75738 ? 324 GLU A C   1 
ATOM   2729 O O   . GLU A 1 330 ? -3.55409  -12.40550 38.70795 1.000 44.99041 ? 324 GLU A O   1 
ATOM   2730 C CB  . GLU A 1 330 ? -6.74550  -11.76071 38.36922 1.000 39.30741 ? 324 GLU A CB  1 
ATOM   2731 C CG  . GLU A 1 330 ? -8.05416  -12.35493 38.90974 0.700 43.22235 ? 324 GLU A CG  1 
ATOM   2732 C CD  . GLU A 1 330 ? -9.24117  -12.22129 37.95706 0.600 46.95761 ? 324 GLU A CD  1 
ATOM   2733 O OE1 . GLU A 1 330 ? -9.02851  -12.01174 36.73895 0.600 48.90248 ? 324 GLU A OE1 1 
ATOM   2734 O OE2 . GLU A 1 330 ? -10.39393 -12.36305 38.42950 0.600 48.28977 ? 324 GLU A OE2 1 
ATOM   2735 N N   . ALA A 1 331 ? -3.95683  -10.21456 38.33301 1.000 42.26718 ? 325 ALA A N   1 
ATOM   2736 C CA  . ALA A 1 331 ? -2.84520  -9.96399  37.41951 1.000 42.66435 ? 325 ALA A CA  1 
ATOM   2737 C C   . ALA A 1 331 ? -2.04540  -8.75943  37.90501 1.000 42.56215 ? 325 ALA A C   1 
ATOM   2738 O O   . ALA A 1 331 ? -2.25143  -7.63248  37.42867 1.000 43.31385 ? 325 ALA A O   1 
ATOM   2739 C CB  . ALA A 1 331 ? -3.36971  -9.73707  36.00407 1.000 42.65771 ? 325 ALA A CB  1 
ATOM   2740 N N   . PRO A 1 332 ? -1.13334  -8.95717  38.86475 1.000 40.27084 ? 326 PRO A N   1 
ATOM   2741 C CA  . PRO A 1 332 ? -0.24264  -7.86581  39.29508 1.000 38.91566 ? 326 PRO A CA  1 
ATOM   2742 C C   . PRO A 1 332 ? 0.56836   -7.24125  38.15532 1.000 34.59694 ? 326 PRO A C   1 
ATOM   2743 O O   . PRO A 1 332 ? 0.88933   -7.88542  37.14643 1.000 35.82078 ? 326 PRO A O   1 
ATOM   2744 C CB  . PRO A 1 332 ? 0.68650   -8.55045  40.30555 1.000 40.64207 ? 326 PRO A CB  1 
ATOM   2745 C CG  . PRO A 1 332 ? -0.09539  -9.75507  40.78481 1.000 41.19368 ? 326 PRO A CG  1 
ATOM   2746 C CD  . PRO A 1 332 ? -0.85915  -10.22037 39.56338 1.000 40.04534 ? 326 PRO A CD  1 
ATOM   2747 N N   . PHE A 1 333 ? 0.89582   -5.95790  38.31830 1.000 32.18299 ? 327 PHE A N   1 
ATOM   2748 C CA  . PHE A 1 333 ? 1.80373   -5.28337  37.38891 1.000 36.57533 ? 327 PHE A CA  1 
ATOM   2749 C C   . PHE A 1 333 ? 3.22699   -5.73391  37.69209 1.000 42.98305 ? 327 PHE A C   1 
ATOM   2750 O O   . PHE A 1 333 ? 3.64588   -5.74239  38.85880 1.000 45.02338 ? 327 PHE A O   1 
ATOM   2751 C CB  . PHE A 1 333 ? 1.71838   -3.75731  37.50511 1.000 38.78747 ? 327 PHE A CB  1 
ATOM   2752 C CG  . PHE A 1 333 ? 0.50500   -3.14838  36.83986 1.000 39.41659 ? 327 PHE A CG  1 
ATOM   2753 C CD1 . PHE A 1 333 ? -0.71610  -3.12612  37.48733 1.000 37.74834 ? 327 PHE A CD1 1 
ATOM   2754 C CD2 . PHE A 1 333 ? 0.58679   -2.62777  35.54031 1.000 41.64300 ? 327 PHE A CD2 1 
ATOM   2755 C CE1 . PHE A 1 333 ? -1.83499  -2.57794  36.87077 1.000 39.10605 ? 327 PHE A CE1 1 
ATOM   2756 C CE2 . PHE A 1 333 ? -0.54389  -2.07482  34.90018 1.000 41.80778 ? 327 PHE A CE2 1 
ATOM   2757 C CZ  . PHE A 1 333 ? -1.74872  -2.05640  35.56839 1.000 40.17984 ? 327 PHE A CZ  1 
ATOM   2758 N N   . LYS A 1 334 ? 3.97119   -6.10158  36.64173 0.700 46.16295 ? 328 LYS A N   1 
ATOM   2759 C CA  . LYS A 1 334 ? 5.29576   -6.69453  36.82268 0.700 50.97413 ? 328 LYS A CA  1 
ATOM   2760 C C   . LYS A 1 334 ? 6.36464   -5.64023  37.10636 0.700 52.76134 ? 328 LYS A C   1 
ATOM   2761 O O   . LYS A 1 334 ? 7.13261   -5.77133  38.06679 0.700 54.19997 ? 328 LYS A O   1 
ATOM   2762 C CB  . LYS A 1 334 ? 5.68135   -7.51031  35.58967 0.700 52.98865 ? 328 LYS A CB  1 
ATOM   2763 C CG  . LYS A 1 334 ? 4.85603   -8.76964  35.36382 0.700 55.18261 ? 328 LYS A CG  1 
ATOM   2764 C CD  . LYS A 1 334 ? 5.37289   -9.54527  34.14389 0.700 56.55779 ? 328 LYS A CD  1 
ATOM   2765 C CE  . LYS A 1 334 ? 5.13685   -8.80450  32.82442 0.700 57.68062 ? 328 LYS A CE  1 
ATOM   2766 N NZ  . LYS A 1 334 ? 3.70117   -8.59028  32.48834 0.700 58.96476 ? 328 LYS A NZ  1 
ATOM   2767 N N   . PHE A 1 335 ? 6.44553   -4.60229  36.27679 0.700 52.18296 ? 329 PHE A N   1 
ATOM   2768 C CA  . PHE A 1 335 ? 7.46662   -3.56485  36.44746 0.700 51.67739 ? 329 PHE A CA  1 
ATOM   2769 C C   . PHE A 1 335 ? 6.96474   -2.18120  36.03986 0.700 50.92015 ? 329 PHE A C   1 
ATOM   2770 O O   . PHE A 1 335 ? 5.86076   -2.03995  35.52505 0.700 51.97518 ? 329 PHE A O   1 
ATOM   2771 C CB  . PHE A 1 335 ? 8.72664   -3.91059  35.64231 0.700 52.81579 ? 329 PHE A CB  1 
ATOM   2772 N N   . ASP A 1 341 ? 10.72571  8.97648   29.85799 0.700 51.40414 ? 335 ASP A N   1 
ATOM   2773 C CA  . ASP A 1 341 ? 11.54477  9.49313   28.76838 0.700 53.74754 ? 335 ASP A CA  1 
ATOM   2774 C C   . ASP A 1 341 ? 10.77492  9.52519   27.45090 0.700 54.77602 ? 335 ASP A C   1 
ATOM   2775 O O   . ASP A 1 341 ? 11.24151  10.08872  26.45646 0.700 55.16378 ? 335 ASP A O   1 
ATOM   2776 C CB  . ASP A 1 341 ? 12.81768  8.65204   28.61336 0.700 54.79627 ? 335 ASP A CB  1 
ATOM   2777 N N   . LEU A 1 342 ? 9.58937   8.92726   27.45592 1.000 54.50457 ? 336 LEU A N   1 
ATOM   2778 C CA  . LEU A 1 342 ? 8.77497   8.86474   26.24813 1.000 53.69092 ? 336 LEU A CA  1 
ATOM   2779 C C   . LEU A 1 342 ? 8.28364   10.25891  25.88111 1.000 50.68094 ? 336 LEU A C   1 
ATOM   2780 O O   . LEU A 1 342 ? 7.69764   10.94813  26.72687 1.000 48.43399 ? 336 LEU A O   1 
ATOM   2781 C CB  . LEU A 1 342 ? 7.58151   7.92444   26.44409 1.000 54.09389 ? 336 LEU A CB  1 
ATOM   2782 C CG  . LEU A 1 342 ? 7.83119   6.48035   26.88182 1.000 55.07868 ? 336 LEU A CG  1 
ATOM   2783 C CD1 . LEU A 1 342 ? 6.74736   5.57370   26.32450 1.000 55.89440 ? 336 LEU A CD1 1 
ATOM   2784 C CD2 . LEU A 1 342 ? 9.20499   5.99634   26.40550 1.000 55.17580 ? 336 LEU A CD2 1 
ATOM   2785 N N   . PRO A 1 343 ? 8.48980   10.70603  24.64686 1.000 48.96435 ? 337 PRO A N   1 
ATOM   2786 C CA  . PRO A 1 343 ? 7.94306   12.00001  24.24284 1.000 46.44400 ? 337 PRO A CA  1 
ATOM   2787 C C   . PRO A 1 343 ? 6.42822   11.94798  24.27120 1.000 43.61608 ? 337 PRO A C   1 
ATOM   2788 O O   . PRO A 1 343 ? 5.81275   10.87791  24.24133 1.000 43.23485 ? 337 PRO A O   1 
ATOM   2789 C CB  . PRO A 1 343 ? 8.46040   12.20020  22.81492 1.000 49.19027 ? 337 PRO A CB  1 
ATOM   2790 C CG  . PRO A 1 343 ? 9.10108   10.90812  22.41008 1.000 51.55601 ? 337 PRO A CG  1 
ATOM   2791 C CD  . PRO A 1 343 ? 8.98870   9.91516   23.51005 1.000 50.51110 ? 337 PRO A CD  1 
ATOM   2792 N N   . LYS A 1 344 ? 5.83190   13.13599  24.34933 1.000 40.48899 ? 338 LYS A N   1 
ATOM   2793 C CA  . LYS A 1 344 ? 4.37935   13.21563  24.45275 1.000 38.40121 ? 338 LYS A CA  1 
ATOM   2794 C C   . LYS A 1 344 ? 3.69028   12.64887  23.21852 1.000 38.79605 ? 338 LYS A C   1 
ATOM   2795 O O   . LYS A 1 344 ? 2.56337   12.16134  23.31929 1.000 39.12511 ? 338 LYS A O   1 
ATOM   2796 C CB  . LYS A 1 344 ? 3.96083   14.66131  24.69795 0.900 38.54467 ? 338 LYS A CB  1 
ATOM   2797 C CG  . LYS A 1 344 ? 4.29270   15.60472  23.55325 0.800 39.44333 ? 338 LYS A CG  1 
ATOM   2798 C CD  . LYS A 1 344 ? 4.08204   17.05681  23.96945 0.700 38.73930 ? 338 LYS A CD  1 
ATOM   2799 C CE  . LYS A 1 344 ? 4.16636   17.98300  22.76762 0.600 39.14489 ? 338 LYS A CE  1 
ATOM   2800 N NZ  . LYS A 1 344 ? 5.53039   18.01255  22.20156 0.600 39.97731 ? 338 LYS A NZ  1 
ATOM   2801 N N   . GLU A 1 345 ? 4.34263   12.71441  22.04998 1.000 36.54032 ? 339 GLU A N   1 
ATOM   2802 C CA  . GLU A 1 345 ? 3.76140   12.15446  20.83192 1.000 38.60976 ? 339 GLU A CA  1 
ATOM   2803 C C   . GLU A 1 345 ? 3.52557   10.65594  20.97770 1.000 38.18154 ? 339 GLU A C   1 
ATOM   2804 O O   . GLU A 1 345 ? 2.46642   10.13659  20.59204 1.000 37.91645 ? 339 GLU A O   1 
ATOM   2805 C CB  . GLU A 1 345 ? 4.69848   12.43100  19.64793 1.000 38.65720 ? 339 GLU A CB  1 
ATOM   2806 C CG  . GLU A 1 345 ? 4.78200   13.89277  19.21110 0.800 39.73653 ? 339 GLU A CG  1 
ATOM   2807 C CD  . GLU A 1 345 ? 5.68818   14.71743  20.11773 0.700 41.12801 ? 339 GLU A CD  1 
ATOM   2808 O OE1 . GLU A 1 345 ? 6.53651   14.12119  20.81584 0.700 39.20002 ? 339 GLU A OE1 1 
ATOM   2809 O OE2 . GLU A 1 345 ? 5.56544   15.96531  20.11368 0.700 43.70170 ? 339 GLU A OE2 1 
ATOM   2810 N N   . LYS A 1 346 ? 4.50774   9.94288   21.52856 1.000 37.67870 ? 340 LYS A N   1 
ATOM   2811 C CA  . LYS A 1 346 ? 4.35700   8.50748   21.73992 1.000 36.52254 ? 340 LYS A CA  1 
ATOM   2812 C C   . LYS A 1 346 ? 3.34783   8.21933   22.84585 1.000 36.47443 ? 340 LYS A C   1 
ATOM   2813 O O   . LYS A 1 346 ? 2.60370   7.23250   22.77358 1.000 37.24426 ? 340 LYS A O   1 
ATOM   2814 C CB  . LYS A 1 346 ? 5.71340   7.88662   22.08004 0.800 33.54004 ? 340 LYS A CB  1 
ATOM   2815 C CG  . LYS A 1 346 ? 6.64344   7.65758   20.86170 0.700 36.90556 ? 340 LYS A CG  1 
ATOM   2816 C CD  . LYS A 1 346 ? 6.05525   6.61745   19.91152 0.600 39.40783 ? 340 LYS A CD  1 
ATOM   2817 C CE  . LYS A 1 346 ? 6.84065   6.50735   18.63026 0.600 41.81596 ? 340 LYS A CE  1 
ATOM   2818 N NZ  . LYS A 1 346 ? 6.69556   7.76660   17.86033 0.600 43.97820 ? 340 LYS A NZ  1 
ATOM   2819 N N   . LEU A 1 347 ? 3.30641   9.06921   23.87858 1.000 34.24600 ? 341 LEU A N   1 
ATOM   2820 C CA  . LEU A 1 347 ? 2.33151   8.87507   24.95069 1.000 33.86391 ? 341 LEU A CA  1 
ATOM   2821 C C   . LEU A 1 347 ? 0.92388   9.07410   24.43217 1.000 31.71210 ? 341 LEU A C   1 
ATOM   2822 O O   . LEU A 1 347 ? -0.00253  8.37942   24.86958 1.000 30.26165 ? 341 LEU A O   1 
ATOM   2823 C CB  . LEU A 1 347 ? 2.60000   9.84036   26.10101 1.000 35.65255 ? 341 LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 347 ? 3.88275   9.52935   26.88042 1.000 38.36605 ? 341 LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 347 ? 4.11757   10.56437  27.96954 1.000 39.06999 ? 341 LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 347 ? 3.81503   8.12163   27.47709 1.000 38.19647 ? 341 LEU A CD2 1 
ATOM   2827 N N   . LYS A 1 348 ? 0.73955   10.04687  23.52790 1.000 29.63164 ? 342 LYS A N   1 
ATOM   2828 C CA  . LYS A 1 348 ? -0.58446  10.25814  22.94694 1.000 28.60976 ? 342 LYS A CA  1 
ATOM   2829 C C   . LYS A 1 348 ? -1.01886  9.04124   22.16665 1.000 29.25108 ? 342 LYS A C   1 
ATOM   2830 O O   . LYS A 1 348 ? -2.19082  8.62262   22.23908 1.000 28.61949 ? 342 LYS A O   1 
ATOM   2831 C CB  . LYS A 1 348 ? -0.59783  11.49711  22.05384 1.000 28.84462 ? 342 LYS A CB  1 
ATOM   2832 C CG  . LYS A 1 348 ? -1.97874  11.79405  21.48104 1.000 27.92250 ? 342 LYS A CG  1 
ATOM   2833 C CD  . LYS A 1 348 ? -2.01058  13.07510  20.64271 1.000 29.56205 ? 342 LYS A CD  1 
ATOM   2834 C CE  . LYS A 1 348 ? -3.45131  13.40568  20.24653 1.000 30.56789 ? 342 LYS A CE  1 
ATOM   2835 N NZ  . LYS A 1 348 ? -3.55159  14.51798  19.27783 1.000 31.79384 ? 342 LYS A NZ  1 
ATOM   2836 N N   . GLU A 1 349 ? -0.09750  8.47696   21.38743 1.000 32.58001 ? 343 GLU A N   1 
ATOM   2837 C CA  . GLU A 1 349 ? -0.39035  7.24172   20.68164 1.000 36.10199 ? 343 GLU A CA  1 
ATOM   2838 C C   . GLU A 1 349 ? -0.75055  6.13412   21.65382 1.000 35.50472 ? 343 GLU A C   1 
ATOM   2839 O O   . GLU A 1 349 ? -1.69235  5.36829   21.40432 1.000 35.02343 ? 343 GLU A O   1 
ATOM   2840 C CB  . GLU A 1 349 ? 0.81325   6.82627   19.83869 1.000 39.73872 ? 343 GLU A CB  1 
ATOM   2841 C CG  . GLU A 1 349 ? 0.55351   5.60106   18.98870 1.000 46.59021 ? 343 GLU A CG  1 
ATOM   2842 C CD  . GLU A 1 349 ? 1.33533   5.62312   17.69951 0.800 54.18688 ? 343 GLU A CD  1 
ATOM   2843 O OE1 . GLU A 1 349 ? 2.57257   5.80280   17.76869 0.800 53.47585 ? 343 GLU A OE1 1 
ATOM   2844 O OE2 . GLU A 1 349 ? 0.71248   5.49382   16.61926 0.800 60.86065 ? 343 GLU A OE2 1 
ATOM   2845 N N   . LEU A 1 350 ? -0.01463  6.04221   22.77648 1.000 32.99168 ? 344 LEU A N   1 
ATOM   2846 C CA  . LEU A 1 350 ? -0.31093  5.02351   23.78675 1.000 33.39063 ? 344 LEU A CA  1 
ATOM   2847 C C   . LEU A 1 350 ? -1.69568  5.22241   24.39567 1.000 32.10995 ? 344 LEU A C   1 
ATOM   2848 O O   . LEU A 1 350 ? -2.43791  4.25410   24.59297 1.000 33.20322 ? 344 LEU A O   1 
ATOM   2849 C CB  . LEU A 1 350 ? 0.77660   5.01824   24.86651 1.000 34.03699 ? 344 LEU A CB  1 
ATOM   2850 C CG  . LEU A 1 350 ? 2.11314   4.49622   24.33077 1.000 38.53693 ? 344 LEU A CG  1 
ATOM   2851 C CD1 . LEU A 1 350 ? 3.16099   4.66466   25.39306 1.000 40.41365 ? 344 LEU A CD1 1 
ATOM   2852 C CD2 . LEU A 1 350 ? 1.96200   3.04576   23.94657 1.000 40.01510 ? 344 LEU A CD2 1 
ATOM   2853 N N   . ILE A 1 351 ? -2.05630  6.46725   24.70241 1.000 28.01737 ? 345 ILE A N   1 
ATOM   2854 C CA  . ILE A 1 351 ? -3.38539  6.76535   25.24402 1.000 25.61267 ? 345 ILE A CA  1 
ATOM   2855 C C   . ILE A 1 351 ? -4.46276  6.42088   24.22751 1.000 25.59157 ? 345 ILE A C   1 
ATOM   2856 O O   . ILE A 1 351 ? -5.51846  5.86810   24.57950 1.000 25.91201 ? 345 ILE A O   1 
ATOM   2857 C CB  . ILE A 1 351 ? -3.43889  8.24402   25.67196 1.000 24.57711 ? 345 ILE A CB  1 
ATOM   2858 C CG1 . ILE A 1 351 ? -2.49290  8.46273   26.87310 1.000 27.35339 ? 345 ILE A CG1 1 
ATOM   2859 C CG2 . ILE A 1 351 ? -4.85641  8.68940   25.99610 1.000 25.83872 ? 345 ILE A CG2 1 
ATOM   2860 C CD1 . ILE A 1 351 ? -2.26125  9.91188   27.20984 1.000 27.16657 ? 345 ILE A CD1 1 
ATOM   2861 N N   . PHE A 1 352 ? -4.23765  6.77353   22.95915 1.000 25.33371 ? 346 PHE A N   1 
ATOM   2862 C CA  . PHE A 1 352 ? -5.19556  6.42852   21.91015 1.000 25.70321 ? 346 PHE A CA  1 
ATOM   2863 C C   . PHE A 1 352 ? -5.41259  4.91575   21.82396 1.000 27.53265 ? 346 PHE A C   1 
ATOM   2864 O O   . PHE A 1 352 ? -6.55804  4.43671   21.75425 1.000 26.79217 ? 346 PHE A O   1 
ATOM   2865 C CB  . PHE A 1 352 ? -4.68911  6.98249   20.57501 1.000 27.89661 ? 346 PHE A CB  1 
ATOM   2866 C CG  . PHE A 1 352 ? -5.62776  6.78848   19.43373 1.000 28.46414 ? 346 PHE A CG  1 
ATOM   2867 C CD1 . PHE A 1 352 ? -6.65579  7.70331   19.20234 1.000 26.80118 ? 346 PHE A CD1 1 
ATOM   2868 C CD2 . PHE A 1 352 ? -5.46554  5.71432   18.55971 1.000 28.97933 ? 346 PHE A CD2 1 
ATOM   2869 C CE1 . PHE A 1 352 ? -7.51641  7.55153   18.10572 1.000 27.03032 ? 346 PHE A CE1 1 
ATOM   2870 C CE2 . PHE A 1 352 ? -6.32184  5.55415   17.45125 1.000 29.61734 ? 346 PHE A CE2 1 
ATOM   2871 C CZ  . PHE A 1 352 ? -7.35346  6.47093   17.23613 1.000 29.24230 ? 346 PHE A CZ  1 
ATOM   2872 N N   . GLU A 1 353 ? -4.31752  4.14924   21.82948 1.000 28.81055 ? 347 GLU A N   1 
ATOM   2873 C CA  . GLU A 1 353 ? -4.40177  2.69395   21.80958 1.000 34.01701 ? 347 GLU A CA  1 
ATOM   2874 C C   . GLU A 1 353 ? -5.11763  2.13945   23.03555 1.000 33.10559 ? 347 GLU A C   1 
ATOM   2875 O O   . GLU A 1 353 ? -5.96890  1.25260   22.91477 1.000 35.38245 ? 347 GLU A O   1 
ATOM   2876 C CB  . GLU A 1 353 ? -2.99671  2.09399   21.68395 1.000 39.36295 ? 347 GLU A CB  1 
ATOM   2877 C CG  . GLU A 1 353 ? -2.93428  0.55578   21.62998 1.000 47.62826 ? 347 GLU A CG  1 
ATOM   2878 C CD  . GLU A 1 353 ? -3.66134  -0.10047  20.44084 0.800 53.32749 ? 347 GLU A CD  1 
ATOM   2879 O OE1 . GLU A 1 353 ? -3.10372  -1.07394  19.87817 0.700 56.41427 ? 347 GLU A OE1 1 
ATOM   2880 O OE2 . GLU A 1 353 ? -4.81276  0.28693   20.11655 0.700 53.88353 ? 347 GLU A OE2 1 
ATOM   2881 N N   . GLU A 1 354 ? -4.78542  2.64452   24.22654 1.000 31.76559 ? 348 GLU A N   1 
ATOM   2882 C CA  . GLU A 1 354 ? -5.38960  2.12473   25.45773 1.000 31.26272 ? 348 GLU A CA  1 
ATOM   2883 C C   . GLU A 1 354 ? -6.88731  2.38907   25.54052 1.000 30.25548 ? 348 GLU A C   1 
ATOM   2884 O O   . GLU A 1 354 ? -7.58318  1.68844   26.27844 1.000 34.11700 ? 348 GLU A O   1 
ATOM   2885 C CB  . GLU A 1 354 ? -4.73037  2.73686   26.69468 1.000 33.50590 ? 348 GLU A CB  1 
ATOM   2886 C CG  . GLU A 1 354 ? -3.37721  2.17829   27.06029 0.800 38.56726 ? 348 GLU A CG  1 
ATOM   2887 C CD  . GLU A 1 354 ? -3.45674  0.75508   27.56190 0.750 41.28766 ? 348 GLU A CD  1 
ATOM   2888 O OE1 . GLU A 1 354 ? -4.27023  0.46847   28.47254 0.750 42.45126 ? 348 GLU A OE1 1 
ATOM   2889 O OE2 . GLU A 1 354 ? -2.72072  -0.08178  27.02480 0.750 42.71144 ? 348 GLU A OE2 1 
ATOM   2890 N N   . THR A 1 355 ? -7.39453  3.39050   24.83128 1.000 26.34746 ? 349 THR A N   1 
ATOM   2891 C CA  . THR A 1 355 ? -8.80079  3.76414   24.90649 1.000 25.29378 ? 349 THR A CA  1 
ATOM   2892 C C   . THR A 1 355 ? -9.60788  3.21547   23.72930 1.000 25.29338 ? 349 THR A C   1 
ATOM   2893 O O   . THR A 1 355 ? -10.81658 3.45319   23.65000 1.000 25.11990 ? 349 THR A O   1 
ATOM   2894 C CB  . THR A 1 355 ? -8.93198  5.30241   24.98695 1.000 24.65282 ? 349 THR A CB  1 
ATOM   2895 O OG1 . THR A 1 355 ? -8.28781  5.91245   23.85953 1.000 24.45953 ? 349 THR A OG1 1 
ATOM   2896 C CG2 . THR A 1 355 ? -8.28518  5.85201   26.27911 1.000 26.04445 ? 349 THR A CG2 1 
ATOM   2897 N N   . ALA A 1 356 ? -8.97058  2.45856   22.83546 1.000 27.54308 ? 350 ALA A N   1 
ATOM   2898 C CA  . ALA A 1 356 ? -9.64397  1.97939   21.63348 1.000 28.55365 ? 350 ALA A CA  1 
ATOM   2899 C C   . ALA A 1 356 ? -10.82712 1.06390   21.93937 1.000 32.11554 ? 350 ALA A C   1 
ATOM   2900 O O   . ALA A 1 356 ? -11.76040 0.97907   21.12906 1.000 33.21564 ? 350 ALA A O   1 
ATOM   2901 C CB  . ALA A 1 356 ? -8.64382  1.26444   20.72619 1.000 29.06852 ? 350 ALA A CB  1 
ATOM   2902 N N   . ARG A 1 357 ? -10.81838 0.37673   23.08804 1.000 31.84524 ? 351 ARG A N   1 
ATOM   2903 C CA  . ARG A 1 357 ? -11.85485 -0.61031  23.36683 1.000 33.23356 ? 351 ARG A CA  1 
ATOM   2904 C C   . ARG A 1 357 ? -13.24081 0.01315   23.49561 1.000 33.36739 ? 351 ARG A C   1 
ATOM   2905 O O   . ARG A 1 357 ? -14.24591 -0.69724  23.35492 1.000 35.72507 ? 351 ARG A O   1 
ATOM   2906 C CB  . ARG A 1 357 ? -11.49682 -1.40017  24.63900 0.800 33.19678 ? 351 ARG A CB  1 
ATOM   2907 C CG  . ARG A 1 357 ? -11.75290 -0.67635  25.96354 0.700 34.57562 ? 351 ARG A CG  1 
ATOM   2908 C CD  . ARG A 1 357 ? -11.44024 -1.56194  27.17225 0.700 34.75272 ? 351 ARG A CD  1 
ATOM   2909 N NE  . ARG A 1 357 ? -10.02937 -1.91923  27.27419 0.600 35.25734 ? 351 ARG A NE  1 
ATOM   2910 C CZ  . ARG A 1 357 ? -9.48738  -2.52435  28.32586 0.600 39.73183 ? 351 ARG A CZ  1 
ATOM   2911 N NH1 . ARG A 1 357 ? -10.20732 -2.83084  29.39679 0.600 42.25493 ? 351 ARG A NH1 1 
ATOM   2912 N NH2 . ARG A 1 357 ? -8.19330  -2.83935  28.30042 0.600 39.24791 ? 351 ARG A NH2 1 
ATOM   2913 N N   . PHE A 1 358 ? -13.31696 1.31477   23.75275 1.000 31.34218 ? 352 PHE A N   1 
ATOM   2914 C CA  . PHE A 1 358 ? -14.58818 1.97813   23.98033 1.000 29.13619 ? 352 PHE A CA  1 
ATOM   2915 C C   . PHE A 1 358 ? -15.14464 2.60626   22.73020 1.000 31.57027 ? 352 PHE A C   1 
ATOM   2916 O O   . PHE A 1 358 ? -16.22716 3.19868   22.78821 1.000 32.60244 ? 352 PHE A O   1 
ATOM   2917 C CB  . PHE A 1 358 ? -14.42941 3.03319   25.08068 1.000 28.35365 ? 352 PHE A CB  1 
ATOM   2918 C CG  . PHE A 1 358 ? -14.05257 2.44423   26.39076 1.000 30.95189 ? 352 PHE A CG  1 
ATOM   2919 C CD1 . PHE A 1 358 ? -14.99299 1.79718   27.17645 1.000 30.59660 ? 352 PHE A CD1 1 
ATOM   2920 C CD2 . PHE A 1 358 ? -12.74780 2.51096   26.82946 1.000 33.08784 ? 352 PHE A CD2 1 
ATOM   2921 C CE1 . PHE A 1 358 ? -14.64405 1.24758   28.40309 1.000 31.34542 ? 352 PHE A CE1 1 
ATOM   2922 C CE2 . PHE A 1 358 ? -12.38150 1.95510   28.05486 1.000 33.74210 ? 352 PHE A CE2 1 
ATOM   2923 C CZ  . PHE A 1 358 ? -13.33453 1.31176   28.83494 1.000 32.63930 ? 352 PHE A CZ  1 
ATOM   2924 N N   . GLN A 1 359 ? -14.43681 2.48522   21.61070 1.000 32.14239 ? 353 GLN A N   1 
ATOM   2925 C CA  . GLN A 1 359 ? -14.95173 2.97348   20.34865 1.000 37.19875 ? 353 GLN A CA  1 
ATOM   2926 C C   . GLN A 1 359 ? -15.91550 1.95480   19.74366 1.000 43.64671 ? 353 GLN A C   1 
ATOM   2927 O O   . GLN A 1 359 ? -15.81344 0.75666   20.01534 1.000 47.68184 ? 353 GLN A O   1 
ATOM   2928 C CB  . GLN A 1 359 ? -13.80737 3.23115   19.37805 1.000 34.41083 ? 353 GLN A CB  1 
ATOM   2929 C CG  . GLN A 1 359 ? -12.91090 4.35660   19.83032 1.000 33.60591 ? 353 GLN A CG  1 
ATOM   2930 C CD  . GLN A 1 359 ? -13.66039 5.67543   19.83679 1.000 34.25287 ? 353 GLN A CD  1 
ATOM   2931 O OE1 . GLN A 1 359 ? -14.17612 6.11173   18.79361 1.000 36.65427 ? 353 GLN A OE1 1 
ATOM   2932 N NE2 . GLN A 1 359 ? -13.74583 6.31349   21.01114 1.000 29.78233 ? 353 GLN A NE2 1 
ATOM   2933 N N   . PRO A 1 360 ? -16.87378 2.41767   18.93275 0.700 46.21266 ? 354 PRO A N   1 
ATOM   2934 C CA  . PRO A 1 360 ? -17.73729 1.63967   18.04016 0.700 47.95135 ? 354 PRO A CA  1 
ATOM   2935 C C   . PRO A 1 360 ? -17.11231 0.36456   17.49073 0.700 49.87313 ? 354 PRO A C   1 
ATOM   2936 O O   . PRO A 1 360 ? -17.32737 0.11581   16.30397 0.700 52.15427 ? 354 PRO A O   1 
ATOM   2937 C CB  . PRO A 1 360 ? -17.98342 2.61652   16.90684 0.700 46.47577 ? 354 PRO A CB  1 
ATOM   2938 C CG  . PRO A 1 360 ? -17.99582 3.96023   17.58338 0.700 45.49289 ? 354 PRO A CG  1 
ATOM   2939 C CD  . PRO A 1 360 ? -17.26817 3.83731   18.91683 0.700 45.82720 ? 354 PRO A CD  1 
HETATM 2940 S S   A SO4 B 2 .   ? 4.31514   20.99036  48.89712 0.500 26.71357 ? 401 SO4 A S   1 
HETATM 2941 S S   B SO4 B 2 .   ? 6.37372   21.08359  48.53573 0.500 28.71474 ? 401 SO4 A S   1 
HETATM 2942 O O1  A SO4 B 2 .   ? 5.11715   22.15460  48.54365 0.500 29.57339 ? 401 SO4 A O1  1 
HETATM 2943 O O1  B SO4 B 2 .   ? 7.59302   21.88746  48.45098 0.500 29.33434 ? 401 SO4 A O1  1 
HETATM 2944 O O2  A SO4 B 2 .   ? 4.62749   19.83579  48.04672 0.500 27.83971 ? 401 SO4 A O2  1 
HETATM 2945 O O2  B SO4 B 2 .   ? 6.52517   19.84030  47.77503 0.500 27.05184 ? 401 SO4 A O2  1 
HETATM 2946 O O3  A SO4 B 2 .   ? 2.90706   21.31645  48.68217 0.500 27.28637 ? 401 SO4 A O3  1 
HETATM 2947 O O3  B SO4 B 2 .   ? 5.27214   21.83212  47.93741 0.500 30.19875 ? 401 SO4 A O3  1 
HETATM 2948 O O4  A SO4 B 2 .   ? 4.50086   20.66057  50.31516 0.500 26.20127 ? 401 SO4 A O4  1 
HETATM 2949 O O4  B SO4 B 2 .   ? 6.03056   20.70783  49.90457 0.500 29.01537 ? 401 SO4 A O4  1 
HETATM 2950 S S   . SO4 C 2 .   ? 5.30433   -5.23651  60.87996 0.600 58.48650 ? 402 SO4 A S   1 
HETATM 2951 O O1  . SO4 C 2 .   ? 4.86514   -5.54463  59.51448 0.600 56.91526 ? 402 SO4 A O1  1 
HETATM 2952 O O2  . SO4 C 2 .   ? 6.76740   -5.30622  60.98338 0.600 57.68730 ? 402 SO4 A O2  1 
HETATM 2953 O O3  . SO4 C 2 .   ? 4.71095   -6.18670  61.81947 0.600 57.50410 ? 402 SO4 A O3  1 
HETATM 2954 O O4  . SO4 C 2 .   ? 4.85294   -3.89185  61.21557 0.600 58.50542 ? 402 SO4 A O4  1 
HETATM 2955 C C15 . WM6 D 3 .   ? -10.92219 14.24390  42.74221 0.900 30.20064 ? 403 WM6 A C15 1 
HETATM 2956 C C1  . WM6 D 3 .   ? -13.26662 15.20153  42.28089 0.900 29.03850 ? 403 WM6 A C1  1 
HETATM 2957 C C2  . WM6 D 3 .   ? -14.71175 15.02183  42.68342 0.900 26.67325 ? 403 WM6 A C2  1 
HETATM 2958 C C3  . WM6 D 3 .   ? -16.38312 13.34886  42.40490 0.900 25.65727 ? 403 WM6 A C3  1 
HETATM 2959 C C8  . WM6 D 3 .   ? -16.87501 12.26040  41.67758 0.900 24.39388 ? 403 WM6 A C8  1 
HETATM 2960 C C4  . WM6 D 3 .   ? -17.19705 14.03433  43.28852 0.900 28.12806 ? 403 WM6 A C4  1 
HETATM 2961 C C5  . WM6 D 3 .   ? -18.51299 13.63760  43.47068 0.900 28.13341 ? 403 WM6 A C5  1 
HETATM 2962 C C6  . WM6 D 3 .   ? -19.03581 12.56496  42.76790 0.900 26.42148 ? 403 WM6 A C6  1 
HETATM 2963 C C7  . WM6 D 3 .   ? -18.22199 11.89074  41.87525 0.900 24.36017 ? 403 WM6 A C7  1 
HETATM 2964 C C9  . WM6 D 3 .   ? -16.07298 11.45720  40.70659 0.900 24.32016 ? 403 WM6 A C9  1 
HETATM 2965 C C10 . WM6 D 3 .   ? -13.99312 11.02740  39.70032 0.900 22.55182 ? 403 WM6 A C10 1 
HETATM 2966 C C11 . WM6 D 3 .   ? -12.55029 11.47358  39.80125 0.900 22.31441 ? 403 WM6 A C11 1 
HETATM 2967 C C12 . WM6 D 3 .   ? -11.89093 11.26725  41.16043 0.900 23.56730 ? 403 WM6 A C12 1 
HETATM 2968 C C13 . WM6 D 3 .   ? -10.58619 12.00152  41.41291 0.900 25.56925 ? 403 WM6 A C13 1 
HETATM 2969 C C14 . WM6 D 3 .   ? -10.74381 13.49733  41.42436 0.900 29.65042 ? 403 WM6 A C14 1 
HETATM 2970 C C16 . WM6 D 3 .   ? -12.37329 14.35827  43.20114 0.900 29.02951 ? 403 WM6 A C16 1 
HETATM 2971 O O1  . WM6 D 3 .   ? -12.91718 16.58596  42.36830 0.900 32.71814 ? 403 WM6 A O1  1 
HETATM 2972 O O2  . WM6 D 3 .   ? -15.09555 13.72905  42.20903 0.900 25.47936 ? 403 WM6 A O2  1 
HETATM 2973 O O3  . WM6 D 3 .   ? -19.29581 14.32692  44.35318 0.900 30.05476 ? 403 WM6 A O3  1 
HETATM 2974 O O4  . WM6 D 3 .   ? -18.72702 10.83171  41.20605 0.900 25.53453 ? 403 WM6 A O4  1 
HETATM 2975 O O5  . WM6 D 3 .   ? -16.53109 10.55169  40.06101 0.900 24.08842 ? 403 WM6 A O5  1 
HETATM 2976 O O6  . WM6 D 3 .   ? -14.77970 11.77455  40.66352 0.900 24.10582 ? 403 WM6 A O6  1 
HETATM 2977 O O7  . WM6 D 3 .   ? -10.72459 14.13361  40.39121 0.900 33.03939 ? 403 WM6 A O7  1 
HETATM 2978 O O8  . WM6 D 3 .   ? -10.42591 15.55984  42.62191 0.900 31.70145 ? 403 WM6 A O8  1 
HETATM 2979 O O9  . WM6 D 3 .   ? -12.41312 14.93254  44.51244 0.900 29.67680 ? 403 WM6 A O9  1 
HETATM 2980 O O   . HOH E 4 .   ? 6.62295   -4.08224  56.00370 1.000 37.95059 ? 501 HOH A O   1 
HETATM 2981 O O   . HOH E 4 .   ? 10.79310  5.88298   67.13309 1.000 29.62307 ? 502 HOH A O   1 
HETATM 2982 O O   . HOH E 4 .   ? 11.53513  19.22140  61.31403 1.000 44.84302 ? 503 HOH A O   1 
HETATM 2983 O O   . HOH E 4 .   ? -11.91375 12.98296  69.78412 1.000 37.51714 ? 504 HOH A O   1 
HETATM 2984 O O   . HOH E 4 .   ? -4.93776  13.15449  43.24842 1.000 46.46848 ? 505 HOH A O   1 
HETATM 2985 O O   . HOH E 4 .   ? -14.68186 8.50166   18.46001 1.000 41.48829 ? 506 HOH A O   1 
HETATM 2986 O O   . HOH E 4 .   ? 8.19629   15.75805  21.66179 1.000 46.85723 ? 507 HOH A O   1 
HETATM 2987 O O   . HOH E 4 .   ? -18.01803 -10.70769 54.72245 1.000 49.87220 ? 508 HOH A O   1 
HETATM 2988 O O   . HOH E 4 .   ? -15.71493 13.45781  62.31358 1.000 41.29203 ? 509 HOH A O   1 
HETATM 2989 O O   . HOH E 4 .   ? 12.45858  -3.41798  43.94869 1.000 48.68651 ? 510 HOH A O   1 
HETATM 2990 O O   . HOH E 4 .   ? -7.65127  13.69337  42.42691 1.000 43.21458 ? 511 HOH A O   1 
HETATM 2991 O O   . HOH E 4 .   ? -19.87634 -0.01437  40.32310 1.000 67.59136 ? 512 HOH A O   1 
HETATM 2992 O O   . HOH E 4 .   ? 3.55945   -6.65492  45.49959 1.000 38.54124 ? 513 HOH A O   1 
HETATM 2993 O O   . HOH E 4 .   ? -10.50532 5.24949   16.92670 1.000 32.76811 ? 514 HOH A O   1 
HETATM 2994 O O   . HOH E 4 .   ? -4.91040  11.92108  37.57700 1.000 57.06323 ? 515 HOH A O   1 
HETATM 2995 O O   . HOH E 4 .   ? -22.61434 4.06000   36.53252 1.000 53.51888 ? 516 HOH A O   1 
HETATM 2996 O O   . HOH E 4 .   ? 8.12213   4.28546   52.91640 1.000 27.40730 ? 517 HOH A O   1 
HETATM 2997 O O   . HOH E 4 .   ? -17.19932 3.59664   37.68417 1.000 30.31359 ? 518 HOH A O   1 
HETATM 2998 O O   . HOH E 4 .   ? -16.34191 -7.20560  53.09769 1.000 30.85713 ? 519 HOH A O   1 
HETATM 2999 O O   . HOH E 4 .   ? 8.51498   17.61361  74.79816 1.000 54.76378 ? 520 HOH A O   1 
HETATM 3000 O O   . HOH E 4 .   ? -19.38002 0.54173   61.81112 1.000 36.55179 ? 521 HOH A O   1 
HETATM 3001 O O   . HOH E 4 .   ? 8.43815   -4.88747  57.94610 1.000 44.91979 ? 522 HOH A O   1 
HETATM 3002 O O   . HOH E 4 .   ? -4.91930  18.03147  25.11278 1.000 37.98015 ? 523 HOH A O   1 
HETATM 3003 O O   . HOH E 4 .   ? -22.78565 20.46725  60.41093 1.000 47.04327 ? 524 HOH A O   1 
HETATM 3004 O O   . HOH E 4 .   ? -3.27142  -11.73584 49.97353 1.000 43.23711 ? 525 HOH A O   1 
HETATM 3005 O O   . HOH E 4 .   ? 2.30599   10.46916  37.12510 1.000 59.43041 ? 526 HOH A O   1 
HETATM 3006 O O   . HOH E 4 .   ? -7.48302  -9.56352  54.41213 1.000 26.97873 ? 527 HOH A O   1 
HETATM 3007 O O   . HOH E 4 .   ? -13.62795 17.61774  23.34580 1.000 58.86974 ? 528 HOH A O   1 
HETATM 3008 O O   . HOH E 4 .   ? -19.77343 19.76190  53.29955 1.000 49.26255 ? 529 HOH A O   1 
HETATM 3009 O O   . HOH E 4 .   ? -8.76957  -0.15468  24.84325 1.000 54.47805 ? 530 HOH A O   1 
HETATM 3010 O O   . HOH E 4 .   ? 3.04868   6.42977   66.27610 1.000 35.76740 ? 531 HOH A O   1 
HETATM 3011 O O   . HOH E 4 .   ? 8.81848   3.88112   64.65715 1.000 22.95023 ? 532 HOH A O   1 
HETATM 3012 O O   . HOH E 4 .   ? 13.24807  15.37512  67.93789 1.000 32.24329 ? 533 HOH A O   1 
HETATM 3013 O O   . HOH E 4 .   ? 14.11127  13.31675  50.56288 1.000 28.49352 ? 534 HOH A O   1 
HETATM 3014 O O   . HOH E 4 .   ? 0.32713   0.40008   69.01652 1.000 54.86117 ? 535 HOH A O   1 
HETATM 3015 O O   . HOH E 4 .   ? -15.40141 -10.40385 47.65355 1.000 38.83407 ? 536 HOH A O   1 
HETATM 3016 O O   . HOH E 4 .   ? -22.86961 0.80698   52.28635 1.000 45.18537 ? 537 HOH A O   1 
HETATM 3017 O O   . HOH E 4 .   ? -17.95299 16.17616  45.92247 1.000 36.52124 ? 538 HOH A O   1 
HETATM 3018 O O   . HOH E 4 .   ? 1.13952   19.37463  48.36532 1.000 29.61526 ? 539 HOH A O   1 
HETATM 3019 O O   . HOH E 4 .   ? -1.30030  15.42794  43.79205 1.000 51.92919 ? 540 HOH A O   1 
HETATM 3020 O O   . HOH E 4 .   ? 16.95004  19.58838  48.12475 1.000 49.99085 ? 541 HOH A O   1 
HETATM 3021 O O   . HOH E 4 .   ? -19.47663 6.59895   24.42337 1.000 56.00662 ? 542 HOH A O   1 
HETATM 3022 O O   . HOH E 4 .   ? -27.25810 13.33251  51.58123 1.000 44.10159 ? 543 HOH A O   1 
HETATM 3023 O O   . HOH E 4 .   ? 9.66183   9.66223   43.87329 1.000 40.93370 ? 544 HOH A O   1 
HETATM 3024 O O   . HOH E 4 .   ? 13.06803  -0.10855  50.57062 1.000 55.24741 ? 545 HOH A O   1 
HETATM 3025 O O   . HOH E 4 .   ? -13.12797 -1.83721  36.81261 1.000 60.83667 ? 546 HOH A O   1 
HETATM 3026 O O   . HOH E 4 .   ? -13.65798 6.49529   67.42383 1.000 32.04657 ? 547 HOH A O   1 
HETATM 3027 O O   . HOH E 4 .   ? 5.68195   -1.58298  56.85836 1.000 24.13581 ? 548 HOH A O   1 
HETATM 3028 O O   . HOH E 4 .   ? -8.28627  12.12527  77.03151 1.000 54.37420 ? 549 HOH A O   1 
HETATM 3029 O O   . HOH E 4 .   ? -8.71606  -8.62666  39.47880 1.000 45.89219 ? 550 HOH A O   1 
HETATM 3030 O O   . HOH E 4 .   ? -7.41534  17.40238  52.63879 1.000 31.18799 ? 551 HOH A O   1 
HETATM 3031 O O   . HOH E 4 .   ? -10.34904 -7.07326  62.24605 1.000 22.03012 ? 552 HOH A O   1 
HETATM 3032 O O   . HOH E 4 .   ? 8.37778   4.26691   50.25030 1.000 28.03399 ? 553 HOH A O   1 
HETATM 3033 O O   . HOH E 4 .   ? -23.80162 6.09668   38.07113 1.000 29.35966 ? 554 HOH A O   1 
HETATM 3034 O O   . HOH E 4 .   ? 12.30437  1.83241   68.67602 1.000 59.18696 ? 555 HOH A O   1 
HETATM 3035 O O   . HOH E 4 .   ? -26.27981 2.96450   47.03479 1.000 53.05354 ? 556 HOH A O   1 
HETATM 3036 O O   . HOH E 4 .   ? -13.95547 -10.49714 62.00882 1.000 49.38149 ? 557 HOH A O   1 
HETATM 3037 O O   . HOH E 4 .   ? -10.33636 -8.82417  66.60640 1.000 46.53586 ? 558 HOH A O   1 
HETATM 3038 O O   . HOH E 4 .   ? 15.13973  17.04533  44.70636 1.000 49.28239 ? 559 HOH A O   1 
HETATM 3039 O O   . HOH E 4 .   ? 8.84101   9.37429   70.18943 1.000 45.61731 ? 560 HOH A O   1 
HETATM 3040 O O   . HOH E 4 .   ? -2.28963  19.77633  27.63311 1.000 38.26375 ? 561 HOH A O   1 
HETATM 3041 O O   . HOH E 4 .   ? 1.38013   10.21461  69.31015 1.000 40.32245 ? 562 HOH A O   1 
HETATM 3042 O O   . HOH E 4 .   ? 10.42740  7.68913   58.65991 1.000 25.38950 ? 563 HOH A O   1 
HETATM 3043 O O   . HOH E 4 .   ? -10.99326 17.83816  57.39956 1.000 38.50173 ? 564 HOH A O   1 
HETATM 3044 O O   . HOH E 4 .   ? -12.25289 0.00235   35.23302 1.000 30.63408 ? 565 HOH A O   1 
HETATM 3045 O O   . HOH E 4 .   ? -10.95108 13.79076  21.63138 1.000 30.98728 ? 566 HOH A O   1 
HETATM 3046 O O   . HOH E 4 .   ? -6.55377  15.23057  63.08658 1.000 31.71680 ? 567 HOH A O   1 
HETATM 3047 O O   . HOH E 4 .   ? -8.29714  15.31305  44.49066 1.000 46.71370 ? 568 HOH A O   1 
HETATM 3048 O O   . HOH E 4 .   ? 3.85747   2.18983   66.77380 1.000 46.75672 ? 569 HOH A O   1 
HETATM 3049 O O   . HOH E 4 .   ? 5.83803   17.24477  71.32399 1.000 34.30918 ? 570 HOH A O   1 
HETATM 3050 O O   . HOH E 4 .   ? 6.84435   17.63139  52.90809 1.000 23.77213 ? 571 HOH A O   1 
HETATM 3051 O O   . HOH E 4 .   ? -7.93656  -10.56148 63.82692 1.000 34.09224 ? 572 HOH A O   1 
HETATM 3052 O O   . HOH E 4 .   ? -4.57396  -1.66409  31.03722 1.000 48.35921 ? 573 HOH A O   1 
HETATM 3053 O O   . HOH E 4 .   ? -17.99928 0.69143   47.24354 1.000 41.99963 ? 574 HOH A O   1 
HETATM 3054 O O   . HOH E 4 .   ? -20.38758 -8.06087  62.25310 1.000 57.28871 ? 575 HOH A O   1 
HETATM 3055 O O   . HOH E 4 .   ? -10.26855 9.42378   76.02926 1.000 57.03290 ? 576 HOH A O   1 
HETATM 3056 O O   . HOH E 4 .   ? 22.41818  17.03803  57.92628 1.000 26.48050 ? 577 HOH A O   1 
HETATM 3057 O O   . HOH E 4 .   ? 9.31620   9.94368   65.69273 1.000 26.99509 ? 578 HOH A O   1 
HETATM 3058 O O   . HOH E 4 .   ? -12.45105 5.67156   23.35680 1.000 27.86506 ? 579 HOH A O   1 
HETATM 3059 O O   . HOH E 4 .   ? 7.71301   15.05662  24.95849 1.000 49.44141 ? 580 HOH A O   1 
HETATM 3060 O O   . HOH E 4 .   ? 0.83061   14.51591  23.10953 1.000 39.38588 ? 581 HOH A O   1 
HETATM 3061 O O   . HOH E 4 .   ? -15.47173 -3.44833  64.29510 1.000 32.70517 ? 582 HOH A O   1 
HETATM 3062 O O   . HOH E 4 .   ? 20.80912  17.58902  69.59505 1.000 52.21208 ? 583 HOH A O   1 
HETATM 3063 O O   . HOH E 4 .   ? 15.07697  13.76089  66.53922 1.000 20.49243 ? 584 HOH A O   1 
HETATM 3064 O O   . HOH E 4 .   ? -7.71950  16.14457  75.71355 1.000 52.33631 ? 585 HOH A O   1 
HETATM 3065 O O   . HOH E 4 .   ? 23.67321  16.64987  63.81311 1.000 46.52307 ? 586 HOH A O   1 
HETATM 3066 O O   . HOH E 4 .   ? 0.77903   11.12566  18.62285 1.000 41.05626 ? 587 HOH A O   1 
HETATM 3067 O O   . HOH E 4 .   ? 11.77317  20.05626  72.32195 1.000 50.70929 ? 588 HOH A O   1 
HETATM 3068 O O   . HOH E 4 .   ? -16.41269 -0.34406  41.84371 1.000 32.63494 ? 589 HOH A O   1 
HETATM 3069 O O   . HOH E 4 .   ? -2.31109  -4.97461  65.03580 1.000 34.80960 ? 590 HOH A O   1 
HETATM 3070 O O   . HOH E 4 .   ? 14.43758  4.61687   51.66026 1.000 38.93937 ? 591 HOH A O   1 
HETATM 3071 O O   . HOH E 4 .   ? -9.86022  -6.41374  49.00743 1.000 18.65168 ? 592 HOH A O   1 
HETATM 3072 O O   . HOH E 4 .   ? -0.79332  7.65490   49.46264 1.000 18.01147 ? 593 HOH A O   1 
HETATM 3073 O O   . HOH E 4 .   ? 15.02731  22.33808  62.27430 1.000 28.20877 ? 594 HOH A O   1 
HETATM 3074 O O   . HOH E 4 .   ? 5.92112   -3.13719  64.35618 1.000 53.50766 ? 595 HOH A O   1 
HETATM 3075 O O   . HOH E 4 .   ? -13.22438 -12.25753 47.69379 1.000 41.60291 ? 596 HOH A O   1 
HETATM 3076 O O   . HOH E 4 .   ? 2.66392   18.81826  65.65691 1.000 35.73470 ? 597 HOH A O   1 
HETATM 3077 O O   . HOH E 4 .   ? 1.96917   -8.36521  43.89575 1.000 56.15051 ? 598 HOH A O   1 
HETATM 3078 O O   . HOH E 4 .   ? -15.15259 5.33763   16.30065 1.000 40.48016 ? 599 HOH A O   1 
HETATM 3079 O O   . HOH E 4 .   ? -5.63295  3.08807   72.57994 1.000 35.23488 ? 600 HOH A O   1 
HETATM 3080 O O   . HOH E 4 .   ? 5.22528   -8.71844  62.87638 1.000 41.73995 ? 601 HOH A O   1 
HETATM 3081 O O   . HOH E 4 .   ? -22.09415 17.21392  61.80942 1.000 37.86282 ? 602 HOH A O   1 
HETATM 3082 O O   . HOH E 4 .   ? -11.12957 17.71369  17.13614 1.000 35.74189 ? 603 HOH A O   1 
HETATM 3083 O O   . HOH E 4 .   ? -12.08560 18.71386  54.52692 1.000 31.63195 ? 604 HOH A O   1 
HETATM 3084 O O   . HOH E 4 .   ? -3.40802  -5.59300  67.48374 1.000 37.98057 ? 605 HOH A O   1 
HETATM 3085 O O   . HOH E 4 .   ? 12.27652  7.97705   71.09013 1.000 42.25034 ? 606 HOH A O   1 
HETATM 3086 O O   . HOH E 4 .   ? 5.43176   24.14460  62.70925 1.000 53.34932 ? 607 HOH A O   1 
HETATM 3087 O O   . HOH E 4 .   ? 0.34083   19.17884  63.65559 1.000 42.35470 ? 608 HOH A O   1 
HETATM 3088 O O   . HOH E 4 .   ? 1.99549   13.62047  56.89910 1.000 16.88394 ? 609 HOH A O   1 
HETATM 3089 O O   . HOH E 4 .   ? -16.74129 1.59643   39.96373 1.000 46.48736 ? 610 HOH A O   1 
HETATM 3090 O O   . HOH E 4 .   ? -24.48356 16.43069  25.88290 1.000 57.32372 ? 611 HOH A O   1 
HETATM 3091 O O   . HOH E 4 .   ? -2.38646  8.24713   42.21823 1.000 28.76013 ? 612 HOH A O   1 
HETATM 3092 O O   . HOH E 4 .   ? 4.97361   -6.41735  49.45761 1.000 42.23157 ? 613 HOH A O   1 
HETATM 3093 O O   . HOH E 4 .   ? -14.54412 -1.51458  66.87489 1.000 47.05498 ? 614 HOH A O   1 
HETATM 3094 O O   . HOH E 4 .   ? -30.89903 13.39509  34.58207 1.000 47.94046 ? 615 HOH A O   1 
HETATM 3095 O O   . HOH E 4 .   ? -4.91306  14.41487  58.19800 1.000 20.84317 ? 616 HOH A O   1 
HETATM 3096 O O   . HOH E 4 .   ? -5.84706  -9.91172  56.60186 1.000 26.11583 ? 617 HOH A O   1 
HETATM 3097 O O   . HOH E 4 .   ? 18.27982  -0.14349  64.17745 1.000 61.69603 ? 618 HOH A O   1 
HETATM 3098 O O   . HOH E 4 .   ? -10.17993 4.78096   40.64578 1.000 36.22914 ? 619 HOH A O   1 
HETATM 3099 O O   . HOH E 4 .   ? -2.33353  15.60117  58.02497 1.000 24.03474 ? 620 HOH A O   1 
HETATM 3100 O O   . HOH E 4 .   ? -2.32220  -10.61137 43.66145 1.000 54.28405 ? 621 HOH A O   1 
HETATM 3101 O O   . HOH E 4 .   ? 3.36290   -0.16410  56.06632 1.000 20.41879 ? 622 HOH A O   1 
HETATM 3102 O O   . HOH E 4 .   ? 3.04764   -0.82503  63.64693 1.000 29.37637 ? 623 HOH A O   1 
HETATM 3103 O O   . HOH E 4 .   ? -12.99743 11.46501  11.47712 1.000 22.09379 ? 624 HOH A O   1 
HETATM 3104 O O   . HOH E 4 .   ? -12.12234 -7.42627  43.46315 1.000 25.42644 ? 625 HOH A O   1 
HETATM 3105 O O   . HOH E 4 .   ? -1.74170  12.32147  49.46271 1.000 19.85183 ? 626 HOH A O   1 
HETATM 3106 O O   . HOH E 4 .   ? -12.96230 -1.18562  40.05686 1.000 22.18516 ? 627 HOH A O   1 
HETATM 3107 O O   . HOH E 4 .   ? -13.14631 -0.78052  32.39666 1.000 52.38654 ? 628 HOH A O   1 
HETATM 3108 O O   . HOH E 4 .   ? -29.21846 12.24653  23.10670 1.000 53.04977 ? 629 HOH A O   1 
HETATM 3109 O O   . HOH E 4 .   ? -2.04687  18.86025  64.95407 1.000 60.92149 ? 630 HOH A O   1 
HETATM 3110 O O   . HOH E 4 .   ? 2.71118   9.11313   52.47448 1.000 18.67252 ? 631 HOH A O   1 
HETATM 3111 O O   . HOH E 4 .   ? -20.01588 7.80547   67.63029 1.000 50.68864 ? 632 HOH A O   1 
HETATM 3112 O O   . HOH E 4 .   ? 16.18000  2.35472   70.31320 1.000 42.86254 ? 633 HOH A O   1 
HETATM 3113 O O   . HOH E 4 .   ? -15.74230 8.13979   21.93887 1.000 27.42962 ? 634 HOH A O   1 
HETATM 3114 O O   . HOH E 4 .   ? -17.49794 -7.31329  55.59023 1.000 48.28663 ? 635 HOH A O   1 
HETATM 3115 O O   . HOH E 4 .   ? 21.58594  21.41003  67.25357 1.000 34.32449 ? 636 HOH A O   1 
HETATM 3116 O O   A HOH E 4 .   ? 11.01524  23.61583  53.65917 0.500 30.10996 ? 637 HOH A O   1 
HETATM 3117 O O   B HOH E 4 .   ? 13.00352  20.13753  57.15429 0.500 40.62020 ? 637 HOH A O   1 
HETATM 3118 O O   . HOH E 4 .   ? 5.59272   7.98193   68.69498 1.000 44.20636 ? 638 HOH A O   1 
HETATM 3119 O O   . HOH E 4 .   ? -3.47356  7.39906   73.83751 1.000 42.77784 ? 639 HOH A O   1 
HETATM 3120 O O   . HOH E 4 .   ? 19.95150  -0.31723  66.36389 1.000 54.99167 ? 640 HOH A O   1 
HETATM 3121 O O   . HOH E 4 .   ? -25.32634 6.97441   45.36873 1.000 59.16398 ? 641 HOH A O   1 
HETATM 3122 O O   . HOH E 4 .   ? -19.28628 1.72988   27.80379 1.000 47.85531 ? 642 HOH A O   1 
HETATM 3123 O O   . HOH E 4 .   ? -9.28506  3.41841   18.14031 1.000 35.98701 ? 643 HOH A O   1 
HETATM 3124 O O   . HOH E 4 .   ? -1.61938  14.39890  17.14546 1.000 42.37503 ? 644 HOH A O   1 
HETATM 3125 O O   . HOH E 4 .   ? 6.80422   5.91337   65.83093 1.000 27.96417 ? 645 HOH A O   1 
HETATM 3126 O O   . HOH E 4 .   ? 13.36648  4.76147   60.67107 1.000 27.40236 ? 646 HOH A O   1 
HETATM 3127 O O   . HOH E 4 .   ? 18.75393  3.46073   55.24322 1.000 46.26069 ? 647 HOH A O   1 
HETATM 3128 O O   . HOH E 4 .   ? -9.88794  7.24779   39.09883 1.000 35.43165 ? 648 HOH A O   1 
HETATM 3129 O O   . HOH E 4 .   ? 0.49583   -2.77207  52.76044 1.000 17.19430 ? 649 HOH A O   1 
HETATM 3130 O O   . HOH E 4 .   ? 16.03901  4.89790   71.83263 1.000 33.51162 ? 650 HOH A O   1 
HETATM 3131 O O   . HOH E 4 .   ? -14.43551 -6.26668  44.92461 1.000 32.44185 ? 651 HOH A O   1 
HETATM 3132 O O   . HOH E 4 .   ? 3.02503   15.44960  75.32032 1.000 52.09098 ? 652 HOH A O   1 
HETATM 3133 O O   . HOH E 4 .   ? -10.71190 17.87833  44.36305 1.000 55.81147 ? 653 HOH A O   1 
HETATM 3134 O O   . HOH E 4 .   ? -9.84125  8.47244   73.51859 1.000 39.42632 ? 654 HOH A O   1 
HETATM 3135 O O   . HOH E 4 .   ? -5.65629  15.98468  43.66744 1.000 47.39230 ? 655 HOH A O   1 
HETATM 3136 O O   . HOH E 4 .   ? -11.30851 1.38177   18.26949 1.000 40.86977 ? 656 HOH A O   1 
HETATM 3137 O O   . HOH E 4 .   ? -18.21473 2.37434   24.96946 1.000 56.44468 ? 657 HOH A O   1 
HETATM 3138 O O   . HOH E 4 .   ? -12.37625 -15.56421 55.65380 1.000 44.90045 ? 658 HOH A O   1 
HETATM 3139 O O   . HOH E 4 .   ? -21.90368 15.37652  43.52828 1.000 59.18713 ? 659 HOH A O   1 
HETATM 3140 O O   . HOH E 4 .   ? 13.37497  5.62209   56.39724 1.000 44.78742 ? 660 HOH A O   1 
HETATM 3141 O O   . HOH E 4 .   ? -13.10980 3.25309   73.67889 1.000 42.37426 ? 661 HOH A O   1 
HETATM 3142 O O   . HOH E 4 .   ? -8.87023  -12.79533 46.26942 1.000 41.78773 ? 662 HOH A O   1 
HETATM 3143 O O   . HOH E 4 .   ? -26.79651 14.61364  39.45271 1.000 53.74782 ? 663 HOH A O   1 
HETATM 3144 O O   . HOH E 4 .   ? -2.18577  -6.70941  49.74070 1.000 26.23410 ? 664 HOH A O   1 
HETATM 3145 O O   . HOH E 4 .   ? -5.51426  7.83365   14.14756 1.000 39.76181 ? 665 HOH A O   1 
HETATM 3146 O O   . HOH E 4 .   ? -0.34609  -6.78952  53.94371 1.000 24.85987 ? 666 HOH A O   1 
HETATM 3147 O O   . HOH E 4 .   ? -16.84365 6.11247   23.53021 1.000 37.64499 ? 667 HOH A O   1 
HETATM 3148 O O   . HOH E 4 .   ? -7.98748  15.98817  50.29862 1.000 21.01986 ? 668 HOH A O   1 
HETATM 3149 O O   . HOH E 4 .   ? -24.44007 13.22373  43.20634 1.000 58.88964 ? 669 HOH A O   1 
HETATM 3150 O O   . HOH E 4 .   ? -21.18728 4.20743   24.00805 1.000 52.02261 ? 670 HOH A O   1 
HETATM 3151 O O   . HOH E 4 .   ? 6.28793   18.41682  27.60753 1.000 52.46940 ? 671 HOH A O   1 
HETATM 3152 O O   . HOH E 4 .   ? 19.11329  6.11858   54.33039 1.000 34.31025 ? 672 HOH A O   1 
HETATM 3153 O O   . HOH E 4 .   ? -21.22496 5.34408   66.29829 1.000 48.70600 ? 673 HOH A O   1 
HETATM 3154 O O   . HOH E 4 .   ? 19.43230  6.85607   51.52766 1.000 29.00755 ? 674 HOH A O   1 
HETATM 3155 O O   . HOH E 4 .   ? 10.85196  3.47969   52.96420 1.000 32.73019 ? 675 HOH A O   1 
HETATM 3156 O O   . HOH E 4 .   ? -11.06971 -0.04778  38.47849 1.000 31.67430 ? 676 HOH A O   1 
HETATM 3157 O O   . HOH E 4 .   ? -8.06491  22.27629  52.92389 1.000 52.56048 ? 677 HOH A O   1 
HETATM 3158 O O   . HOH E 4 .   ? 2.34518   -6.16691  33.64853 1.000 52.65885 ? 678 HOH A O   1 
HETATM 3159 O O   . HOH E 4 .   ? -4.00800  0.80905   72.96416 1.000 58.88538 ? 679 HOH A O   1 
HETATM 3160 O O   . HOH E 4 .   ? -11.07179 16.55113  20.77351 1.000 43.31112 ? 680 HOH A O   1 
HETATM 3161 O O   . HOH E 4 .   ? -21.13824 4.34071   31.09139 1.000 57.46988 ? 681 HOH A O   1 
HETATM 3162 O O   . HOH E 4 .   ? -20.49210 9.53462   23.82320 1.000 54.08152 ? 682 HOH A O   1 
HETATM 3163 O O   . HOH E 4 .   ? 0.29250   -6.59148  49.48334 1.000 30.56514 ? 683 HOH A O   1 
HETATM 3164 O O   . HOH E 4 .   ? -12.99044 -13.28079 59.82779 1.000 60.30954 ? 684 HOH A O   1 
HETATM 3165 O O   . HOH E 4 .   ? 0.24588   -5.11253  64.75872 1.000 37.96043 ? 685 HOH A O   1 
HETATM 3166 O O   . HOH E 4 .   ? 6.86515   -2.22330  48.97902 1.000 26.93374 ? 686 HOH A O   1 
HETATM 3167 O O   . HOH E 4 .   ? -26.93718 7.79003   39.61552 1.000 51.16435 ? 687 HOH A O   1 
HETATM 3168 O O   . HOH E 4 .   ? 5.94934   2.49503   37.73192 1.000 39.06817 ? 688 HOH A O   1 
HETATM 3169 O O   . HOH E 4 .   ? -0.63019  7.46492   72.76988 1.000 36.25703 ? 689 HOH A O   1 
HETATM 3170 O O   . HOH E 4 .   ? -29.51854 8.29266   38.52745 1.000 56.45969 ? 690 HOH A O   1 
HETATM 3171 O O   . HOH E 4 .   ? -17.54922 -2.05800  50.53958 1.000 42.06375 ? 691 HOH A O   1 
HETATM 3172 O O   . HOH E 4 .   ? -8.76971  -12.92281 49.32617 1.000 48.73799 ? 692 HOH A O   1 
HETATM 3173 O O   . HOH E 4 .   ? 6.99570   4.49068   35.36369 1.000 55.35139 ? 693 HOH A O   1 
HETATM 3174 O O   . HOH E 4 .   ? 8.86179   -0.29520  54.21665 1.000 58.83235 ? 694 HOH A O   1 
HETATM 3175 O O   . HOH E 4 .   ? 12.79647  4.76319   54.22054 1.000 47.29860 ? 695 HOH A O   1 
HETATM 3176 O O   . HOH E 4 .   ? -4.53452  -4.40903  69.45014 1.000 53.69708 ? 696 HOH A O   1 
HETATM 3177 O O   . HOH E 4 .   ? -17.37790 -13.38995 49.80990 1.000 44.21433 ? 697 HOH A O   1 
HETATM 3178 O O   . HOH E 4 .   ? -15.86796 -4.33644  67.56642 1.000 60.66926 ? 698 HOH A O   1 
HETATM 3179 O O   . HOH E 4 .   ? -4.43167  -8.69765  64.83588 1.000 57.85798 ? 699 HOH A O   1 
HETATM 3180 O O   . HOH E 4 .   ? -16.27471 6.61329   69.97331 1.000 52.95917 ? 700 HOH A O   1 
HETATM 3181 O O   . HOH E 4 .   ? 18.77995  1.13140   70.55173 1.000 54.83155 ? 701 HOH A O   1 
HETATM 3182 O O   . HOH E 4 .   ? -16.04817 -8.02703  46.01852 1.000 38.88525 ? 702 HOH A O   1 
HETATM 3183 O O   . HOH E 4 .   ? 23.57702  16.97310  67.26113 1.000 49.23660 ? 703 HOH A O   1 
HETATM 3184 O O   . HOH E 4 .   ? -22.91347 4.71804   42.84085 1.000 58.10064 ? 704 HOH A O   1 
HETATM 3185 O O   . HOH E 4 .   ? 1.19236   -5.32618  52.19788 1.000 21.93484 ? 705 HOH A O   1 
HETATM 3186 O O   . HOH E 4 .   ? -6.65100  -11.95669 34.42117 1.000 63.51805 ? 706 HOH A O   1 
HETATM 3187 O O   . HOH E 4 .   ? -5.83001  -7.46663  38.24265 1.000 56.32316 ? 707 HOH A O   1 
HETATM 3188 O O   . HOH E 4 .   ? 13.76149  2.98293   58.44721 1.000 57.34538 ? 708 HOH A O   1 
HETATM 3189 O O   . HOH E 4 .   ? 5.42213   -2.45580  53.21366 1.000 49.76564 ? 709 HOH A O   1 
HETATM 3190 O O   . HOH E 4 .   ? -1.68661  19.66034  51.87219 1.000 39.96049 ? 710 HOH A O   1 
HETATM 3191 O O   . HOH E 4 .   ? -22.45197 8.39779   21.92832 1.000 66.92575 ? 711 HOH A O   1 
HETATM 3192 O O   . HOH E 4 .   ? 2.72698   -1.57306  53.75504 1.000 21.12116 ? 712 HOH A O   1 
HETATM 3193 O O   . HOH E 4 .   ? 3.86041   -0.15340  66.06510 1.000 37.80903 ? 713 HOH A O   1 
HETATM 3194 O O   . HOH E 4 .   ? -11.59687 21.46771  54.44072 1.000 50.69439 ? 714 HOH A O   1 
HETATM 3195 O O   . HOH E 4 .   ? 6.57706   -4.62610  47.21675 1.000 45.78712 ? 715 HOH A O   1 
HETATM 3196 O O   . HOH E 4 .   ? -1.21006  17.01155  20.39724 1.000 57.44767 ? 716 HOH A O   1 
HETATM 3197 O O   . HOH E 4 .   ? -10.70723 -2.24417  19.84241 1.000 53.61372 ? 717 HOH A O   1 
HETATM 3198 O O   . HOH E 4 .   ? -17.42469 -4.98891  51.94298 1.000 45.55530 ? 718 HOH A O   1 
HETATM 3199 O O   . HOH E 4 .   ? -13.18474 -2.54574  20.40138 1.000 57.10121 ? 719 HOH A O   1 
HETATM 3200 O O   . HOH E 4 .   ? -25.49079 10.17747  43.94720 1.000 56.75450 ? 720 HOH A O   1 
HETATM 3201 O O   . HOH E 4 .   ? -10.58247 -9.33295  63.71899 1.000 32.64881 ? 721 HOH A O   1 
HETATM 3202 O O   . HOH E 4 .   ? -16.99178 -3.23592  41.21450 1.000 58.19021 ? 722 HOH A O   1 
HETATM 3203 O O   . HOH E 4 .   ? -14.99824 -2.09667  26.69781 1.000 60.39222 ? 723 HOH A O   1 
HETATM 3204 O O   . HOH E 4 .   ? 1.98182   -3.35938  63.49544 1.000 46.56039 ? 724 HOH A O   1 
HETATM 3205 O O   . HOH E 4 .   ? 4.39929   21.67277  65.22883 1.000 54.22734 ? 725 HOH A O   1 
HETATM 3206 O O   . HOH E 4 .   ? -8.82710  6.13032   74.18133 1.000 47.57287 ? 726 HOH A O   1 
HETATM 3207 O O   . HOH E 4 .   ? -6.97825  -2.82785  70.09543 1.000 38.13691 ? 727 HOH A O   1 
HETATM 3208 O O   . HOH E 4 .   ? -15.09861 9.13013   67.26690 1.000 44.56987 ? 728 HOH A O   1 
HETATM 3209 O O   . HOH E 4 .   ? -15.68139 -6.47240  41.94794 1.000 46.88348 ? 729 HOH A O   1 
HETATM 3210 O O   . HOH E 4 .   ? -13.62544 14.95922  21.60576 1.000 54.67581 ? 730 HOH A O   1 
HETATM 3211 O O   . HOH E 4 .   ? -5.32626  20.79553  25.22732 1.000 54.37845 ? 731 HOH A O   1 
HETATM 3212 O O   . HOH E 4 .   ? 19.65305  19.08685  71.70936 1.000 55.41752 ? 732 HOH A O   1 
HETATM 3213 O O   . HOH E 4 .   ? -7.00041  2.23485   17.30331 1.000 63.42357 ? 733 HOH A O   1 
HETATM 3214 O O   . HOH E 4 .   ? -15.18829 -2.01561  38.69012 1.000 49.78494 ? 734 HOH A O   1 
HETATM 3215 O O   . HOH E 4 .   ? -8.47109  -4.76670  71.58611 1.000 52.57839 ? 735 HOH A O   1 
HETATM 3216 O O   . HOH E 4 .   ? 8.61086   7.68645   66.86298 1.000 31.40319 ? 736 HOH A O   1 
HETATM 3217 O O   . HOH E 4 .   ? 12.71558  6.39569   58.74630 1.000 32.96498 ? 737 HOH A O   1 
HETATM 3218 O O   . HOH E 4 .   ? 1.30307   15.29189  20.47358 1.000 46.71677 ? 738 HOH A O   1 
HETATM 3219 O O   . HOH E 4 .   ? -24.58697 8.17556   65.42801 1.000 46.17890 ? 739 HOH A O   1 
HETATM 3220 O O   . HOH E 4 .   ? 6.53693   -0.54867  66.29635 1.000 41.42832 ? 740 HOH A O   1 
HETATM 3221 O O   . HOH E 4 .   ? 7.81333   1.83035   66.29137 1.000 47.64919 ? 741 HOH A O   1 
HETATM 3222 O O   . HOH E 4 .   ? -6.04737  5.43058   73.99982 1.000 47.42511 ? 742 HOH A O   1 
HETATM 3223 O O   . HOH E 4 .   ? 16.61295  21.95897  49.71564 1.000 53.15106 ? 743 HOH A O   1 
HETATM 3224 O O   . HOH E 4 .   ? 1.33377   7.88071   74.55478 1.000 49.04210 ? 744 HOH A O   1 
HETATM 3225 O O   . HOH E 4 .   ? -28.00153 12.62724  40.97444 1.000 59.93795 ? 745 HOH A O   1 
HETATM 3226 O O   . HOH E 4 .   ? 23.77259  19.41029  66.83136 1.000 50.17964 ? 746 HOH A O   1 
HETATM 3227 O O   . HOH E 4 .   ? 0.95606   13.65678  18.13595 1.000 45.26962 ? 747 HOH A O   1 
HETATM 3228 O O   . HOH E 4 .   ? -8.71361  21.03039  55.25978 1.000 40.82445 ? 748 HOH A O   1 
HETATM 3229 O O   . HOH E 4 .   ? -5.03754  -8.13601  67.66940 1.000 59.40509 ? 749 HOH A O   1 
HETATM 3230 O O   . HOH E 4 .   ? -4.61706  18.81447  50.95391 1.000 49.75031 ? 750 HOH A O   1 
HETATM 3231 O O   . HOH E 4 .   ? 28.10027  19.39851  48.92825 1.000 63.48846 ? 751 HOH A O   1 
HETATM 3232 O O   . HOH E 4 .   ? 5.78526   -9.08013  49.93421 1.000 57.49231 ? 752 HOH A O   1 
HETATM 3233 O O   . HOH E 4 .   ? 0.26796   7.61639   76.93522 1.000 51.39253 ? 753 HOH A O   1 
HETATM 3234 O O   . HOH E 4 .   ? -10.65965 -13.40992 62.55186 1.000 49.06980 ? 754 HOH A O   1 
HETATM 3235 O O   . HOH E 4 .   ? -4.19266  25.40640  52.88030 1.000 59.54884 ? 755 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 15  ? 1.03396 0.86958 0.83598 0.05954  0.07655  0.00798  9   PRO A N   
2    C CA  . PRO A 15  ? 1.01731 0.87453 0.81654 0.06224  0.04049  0.02458  9   PRO A CA  
3    C C   . PRO A 15  ? 1.00461 0.89262 0.82809 0.07143  0.01251  0.06223  9   PRO A C   
4    O O   . PRO A 15  ? 1.00721 0.89903 0.82916 0.06436  -0.01337 0.07643  9   PRO A O   
5    C CB  . PRO A 15  ? 1.00741 0.86394 0.79680 0.04927  0.03309  0.00906  9   PRO A CB  
6    C CG  . PRO A 15  ? 1.01716 0.85987 0.80961 0.04214  0.05997  -0.00488 9   PRO A CG  
7    C CD  . PRO A 15  ? 1.03030 0.86263 0.82317 0.05360  0.07234  -0.00021 9   PRO A CD  
8    N N   . GLU A 16  ? 0.97657 0.89837 0.83500 0.09486  0.00835  0.08118  10  GLU A N   
9    C CA  . GLU A 16  ? 0.94244 0.90253 0.83791 0.10683  -0.00843 0.09280  10  GLU A CA  
10   C C   . GLU A 16  ? 0.95253 0.91191 0.86149 0.12037  -0.01794 0.08189  10  GLU A C   
11   O O   . GLU A 16  ? 0.94780 0.91487 0.84002 0.13029  -0.03952 0.07991  10  GLU A O   
12   C CB  . GLU A 16  ? 0.88756 0.89278 0.81287 0.10419  -0.02922 0.11487  10  GLU A CB  
13   C CG  . GLU A 16  ? 0.82997 0.87854 0.77875 0.10268  -0.05773 0.13702  10  GLU A CG  
14   C CD  . GLU A 16  ? 0.77493 0.86324 0.74811 0.10417  -0.08208 0.16770  10  GLU A CD  
15   O OE1 . GLU A 16  ? 0.75849 0.85723 0.75252 0.09318  -0.06989 0.18618  10  GLU A OE1 
16   O OE2 . GLU A 16  ? 0.75520 0.85813 0.71852 0.11592  -0.09986 0.17651  10  GLU A OE2 
17   N N   . MET A 17  ? 0.95977 0.91494 0.90858 0.12258  -0.00240 0.08362  11  MET A N   
18   C CA  . MET A 17  ? 0.96250 0.90941 0.93715 0.11589  0.00712  0.08840  11  MET A CA  
19   C C   . MET A 17  ? 0.94058 0.89173 0.89514 0.09937  -0.03718 0.07651  11  MET A C   
20   O O   . MET A 17  ? 0.94221 0.88389 0.87497 0.11426  -0.06184 0.08696  11  MET A O   
21   C CB  . MET A 17  ? 0.99763 0.92506 0.99664 0.12172  0.05476  0.09901  11  MET A CB  
22   C CG  . MET A 17  ? 1.03612 0.94000 1.03004 0.13052  0.07878  0.11815  11  MET A CG  
23   S SD  . MET A 17  ? 1.07868 0.94946 1.07285 0.13372  0.09868  0.13749  11  MET A SD  
24   C CE  . MET A 17  ? 1.10502 0.94962 1.08867 0.13254  0.10572  0.14560  11  MET A CE  
25   N N   . VAL A 18  ? 0.92095 0.89069 0.88477 0.05860  -0.04488 0.05592  12  VAL A N   
26   C CA  . VAL A 18  ? 0.90221 0.89278 0.86471 0.02394  -0.07326 0.04628  12  VAL A CA  
27   C C   . VAL A 18  ? 0.90543 0.89034 0.87190 0.01311  -0.05910 0.03660  12  VAL A C   
28   O O   . VAL A 18  ? 0.90891 0.90227 0.87516 0.00322  -0.05369 0.03579  12  VAL A O   
29   C CB  . VAL A 18  ? 0.87550 0.89059 0.82448 0.00400  -0.12177 0.05227  12  VAL A CB  
30   C CG1 . VAL A 18  ? 0.87095 0.89025 0.82445 -0.00815 -0.11363 0.04660  12  VAL A CG1 
31   C CG2 . VAL A 18  ? 0.86231 0.88695 0.79705 -0.00556 -0.15248 0.05063  12  VAL A CG2 
32   N N   . ARG A 19  ? 0.90609 0.87095 0.88111 0.01947  -0.03401 0.02171  13  ARG A N   
33   C CA  . ARG A 19  ? 0.91914 0.84938 0.89621 0.02060  0.00675  -0.00434 13  ARG A CA  
34   C C   . ARG A 19  ? 0.95325 0.86730 0.91926 0.00400  0.04430  -0.00829 13  ARG A C   
35   O O   . ARG A 19  ? 0.96009 0.86457 0.91683 -0.00104 0.05589  -0.00936 13  ARG A O   
36   C CB  . ARG A 19  ? 0.90097 0.81394 0.88635 0.03754  0.00427  -0.02945 13  ARG A CB  
37   C CG  . ARG A 19  ? 0.88114 0.77901 0.86925 0.06232  -0.01421 -0.03858 13  ARG A CG  
38   C CD  . ARG A 19  ? 0.86315 0.74539 0.84889 0.08888  -0.03518 -0.04026 13  ARG A CD  
39   N NE  . ARG A 19  ? 0.85131 0.71622 0.82800 0.12320  -0.04438 -0.04297 13  ARG A NE  
40   C CZ  . ARG A 19  ? 0.83780 0.69137 0.81267 0.15903  -0.05662 -0.04892 13  ARG A CZ  
41   N NH1 . ARG A 19  ? 0.83937 0.68989 0.81708 0.17894  -0.05089 -0.04196 13  ARG A NH1 
42   N NH2 . ARG A 19  ? 0.82577 0.67477 0.79496 0.16675  -0.07602 -0.05502 13  ARG A NH2 
43   N N   . GLY A 20  ? 0.97529 0.88705 0.93696 0.00182  0.05326  -0.00571 14  GLY A N   
44   C CA  . GLY A 20  ? 1.00201 0.90671 0.95454 -0.01100 0.06561  0.00189  14  GLY A CA  
45   C C   . GLY A 20  ? 1.03537 0.92571 0.96738 -0.03078 0.07059  0.00734  14  GLY A C   
46   O O   . GLY A 20  ? 1.05262 0.94218 0.98990 -0.04315 0.07747  0.01427  14  GLY A O   
47   N N   . GLN A 21  ? 1.03015 0.91869 0.94361 -0.02739 0.05445  0.01164  15  GLN A N   
48   C CA  . GLN A 21  ? 1.00287 0.91054 0.92134 -0.01681 0.04514  0.03266  15  GLN A CA  
49   C C   . GLN A 21  ? 0.98550 0.90206 0.88925 0.00254  0.05885  0.06119  15  GLN A C   
50   O O   . GLN A 21  ? 0.99452 0.91926 0.89970 -0.02056 0.06612  0.04391  15  GLN A O   
51   C CB  . GLN A 21  ? 0.97951 0.91171 0.91915 -0.02536 0.02580  0.03277  15  GLN A CB  
52   C CG  . GLN A 21  ? 0.95278 0.91074 0.90403 -0.04210 0.00119  0.03153  15  GLN A CG  
53   C CD  . GLN A 21  ? 0.92750 0.90771 0.88315 -0.06728 -0.02152 0.01707  15  GLN A CD  
54   O OE1 . GLN A 21  ? 0.91566 0.90296 0.87466 -0.08062 -0.03742 0.01400  15  GLN A OE1 
55   N NE2 . GLN A 21  ? 0.92342 0.90925 0.87938 -0.07504 -0.01128 0.00862  15  GLN A NE2 
56   N N   . VAL A 22  ? 0.94534 0.86769 0.83052 0.04473  0.06147  0.12527  16  VAL A N   
57   C CA  . VAL A 22  ? 0.90699 0.82662 0.77016 0.07589  0.05881  0.19146  16  VAL A CA  
58   C C   . VAL A 22  ? 0.84795 0.78516 0.74425 0.10064  0.03514  0.22635  16  VAL A C   
59   O O   . VAL A 22  ? 0.86811 0.76524 0.74333 0.12528  0.03609  0.25605  16  VAL A O   
60   C CB  . VAL A 22  ? 0.92312 0.81672 0.73143 0.07239  0.09859  0.22089  16  VAL A CB  
61   C CG1 . VAL A 22  ? 0.92625 0.80332 0.71336 0.06206  0.10361  0.24626  16  VAL A CG1 
62   C CG2 . VAL A 22  ? 0.93654 0.81967 0.74298 0.07488  0.12735  0.20317  16  VAL A CG2 
63   N N   . PHE A 23  ? 0.78331 0.78034 0.72792 0.10985  0.03593  0.22429  17  PHE A N   
64   C CA  . PHE A 23  ? 0.71460 0.77113 0.69821 0.10741  0.03256  0.24599  17  PHE A CA  
65   C C   . PHE A 23  ? 0.68431 0.76001 0.70352 0.09801  0.04537  0.29310  17  PHE A C   
66   O O   . PHE A 23  ? 0.70922 0.75462 0.73895 0.10115  0.03524  0.31253  17  PHE A O   
67   C CB  . PHE A 23  ? 0.69663 0.77939 0.69203 0.11338  0.01547  0.19256  17  PHE A CB  
68   C CG  . PHE A 23  ? 0.66883 0.75796 0.65578 0.10363  -0.00289 0.14969  17  PHE A CG  
69   C CD1 . PHE A 23  ? 0.65223 0.75019 0.65467 0.10291  -0.00035 0.12938  17  PHE A CD1 
70   C CD2 . PHE A 23  ? 0.65663 0.74264 0.64136 0.07874  -0.00836 0.11460  17  PHE A CD2 
71   C CE1 . PHE A 23  ? 0.63380 0.74625 0.64306 0.08983  0.00861  0.11916  17  PHE A CE1 
72   C CE2 . PHE A 23  ? 0.63494 0.72576 0.63043 0.08363  -0.00542 0.12297  17  PHE A CE2 
73   C CZ  . PHE A 23  ? 0.62338 0.73437 0.62727 0.09024  -0.00349 0.12422  17  PHE A CZ  
74   N N   . ASP A 24  ? 0.65162 0.76641 0.67182 0.07542  0.06431  0.29111  18  ASP A N   
75   C CA  . ASP A 24  ? 0.62827 0.76901 0.64459 0.06348  0.10157  0.28713  18  ASP A CA  
76   C C   . ASP A 24  ? 0.55171 0.73883 0.52756 0.06724  0.10027  0.32911  18  ASP A C   
77   O O   . ASP A 24  ? 0.55084 0.75655 0.55219 0.02111  0.12279  0.31574  18  ASP A O   
78   C CB  . ASP A 24  ? 0.68897 0.77458 0.68216 0.04804  0.12128  0.28025  18  ASP A CB  
79   C CG  . ASP A 24  ? 0.72835 0.77515 0.72929 0.03642  0.12735  0.25029  18  ASP A CG  
80   O OD1 . ASP A 24  ? 0.72796 0.76938 0.75428 0.04140  0.10101  0.24127  18  ASP A OD1 
81   O OD2 . ASP A 24  ? 0.74621 0.78035 0.76229 0.01142  0.16664  0.22708  18  ASP A OD2 
82   N N   . VAL A 25  ? 0.50480 0.72656 0.44922 0.08123  0.04320  0.29328  19  VAL A N   
83   C CA  . VAL A 25  ? 0.47600 0.72853 0.37444 0.05927  0.02968  0.25710  19  VAL A CA  
84   C C   . VAL A 25  ? 0.53573 0.75046 0.33602 0.06351  0.01479  0.23210  19  VAL A C   
85   O O   . VAL A 25  ? 0.56503 0.72956 0.28555 0.07520  -0.02685 0.19441  19  VAL A O   
86   C CB  . VAL A 25  ? 0.41124 0.70725 0.37809 0.05179  -0.01519 0.24043  19  VAL A CB  
87   C CG1 . VAL A 25  ? 0.34508 0.69807 0.40063 0.00422  -0.02949 0.21502  19  VAL A CG1 
88   C CG2 . VAL A 25  ? 0.48388 0.70383 0.41931 0.05071  0.02945  0.21770  19  VAL A CG2 
89   N N   . GLY A 26  ? 0.50298 0.78416 0.40009 0.04951  -0.00114 0.21931  20  GLY A N   
90   C CA  . GLY A 26  ? 0.49636 0.81250 0.44993 0.04161  -0.00858 0.18495  20  GLY A CA  
91   C C   . GLY A 26  ? 0.46429 0.84441 0.46107 0.02433  -0.05224 0.17560  20  GLY A C   
92   O O   . GLY A 26  ? 0.44888 0.83795 0.47115 0.06337  -0.04675 0.20302  20  GLY A O   
93   N N   . PRO A 27  ? 0.43797 0.87802 0.43471 -0.00745 -0.08096 0.16818  21  PRO A N   
94   C CA  . PRO A 27  ? 0.41556 0.88121 0.40351 0.00397  -0.12941 0.20186  21  PRO A CA  
95   C C   . PRO A 27  ? 0.38572 0.87622 0.40099 -0.00602 -0.09510 0.23254  21  PRO A C   
96   O O   . PRO A 27  ? 0.34463 0.89294 0.42197 0.01582  -0.09321 0.22277  21  PRO A O   
97   C CB  . PRO A 27  ? 0.42998 0.89673 0.41766 0.00848  -0.12726 0.17120  21  PRO A CB  
98   C CG  . PRO A 27  ? 0.44631 0.89586 0.41666 -0.00713 -0.09532 0.14384  21  PRO A CG  
99   C CD  . PRO A 27  ? 0.44767 0.89310 0.40686 -0.02433 -0.10659 0.13171  21  PRO A CD  
100  N N   . ARG A 28  ? 0.37272 0.84108 0.36378 -0.04642 -0.10443 0.21006  22  ARG A N   
101  C CA  . ARG A 28  ? 0.39218 0.78613 0.31525 -0.04396 -0.09036 0.18912  22  ARG A CA  
102  C C   . ARG A 28  ? 0.36517 0.77280 0.33790 -0.04551 -0.10565 0.19345  22  ARG A C   
103  O O   . ARG A 28  ? 0.35740 0.80830 0.39345 -0.04469 -0.07468 0.21236  22  ARG A O   
104  C CB  . ARG A 28  ? 0.42316 0.75810 0.27430 -0.02590 -0.08383 0.15442  22  ARG A CB  
105  C CG  . ARG A 28  ? 0.39352 0.73266 0.30270 -0.01978 -0.07059 0.12487  22  ARG A CG  
106  C CD  . ARG A 28  ? 0.38507 0.71310 0.31434 -0.03848 -0.07164 0.10359  22  ARG A CD  
107  N NE  . ARG A 28  ? 0.35279 0.69015 0.35735 -0.07002 -0.11107 0.06120  22  ARG A NE  
108  C CZ  . ARG A 28  ? 0.38509 0.66586 0.42051 -0.08132 -0.04070 0.02218  22  ARG A CZ  
109  N NH1 . ARG A 28  ? 0.39846 0.64788 0.44096 -0.07864 -0.02881 -0.01529 22  ARG A NH1 
110  N NH2 . ARG A 28  ? 0.38170 0.68103 0.45042 -0.07138 -0.01632 0.02634  22  ARG A NH2 
111  N N   . TYR A 29  ? 0.35953 0.72351 0.32063 -0.04989 -0.11123 0.17682  23  TYR A N   
112  C CA  . TYR A 29  ? 0.35875 0.70034 0.35694 -0.00629 -0.12643 0.18050  23  TYR A CA  
113  C C   . TYR A 29  ? 0.39851 0.72138 0.42574 0.02436  -0.10598 0.24552  23  TYR A C   
114  O O   . TYR A 29  ? 0.45341 0.73247 0.43196 0.01822  -0.05696 0.30133  23  TYR A O   
115  C CB  . TYR A 29  ? 0.33299 0.66368 0.32685 0.03564  -0.10216 0.16305  23  TYR A CB  
116  C CG  . TYR A 29  ? 0.32075 0.65681 0.31682 0.03091  -0.06223 0.13809  23  TYR A CG  
117  C CD1 . TYR A 29  ? 0.28094 0.64472 0.28374 0.03884  -0.05875 0.13663  23  TYR A CD1 
118  C CD2 . TYR A 29  ? 0.26706 0.63219 0.28882 0.01991  -0.08798 0.12154  23  TYR A CD2 
119  C CE1 . TYR A 29  ? 0.25819 0.62610 0.29110 -0.00130 -0.05872 0.11051  23  TYR A CE1 
120  C CE2 . TYR A 29  ? 0.29146 0.63950 0.30250 0.00903  -0.06913 0.11443  23  TYR A CE2 
121  C CZ  . TYR A 29  ? 0.25271 0.61448 0.31517 -0.01051 -0.07829 0.09374  23  TYR A CZ  
122  O OH  . TYR A 29  ? 0.25651 0.59478 0.30534 -0.03973 -0.11125 0.04616  23  TYR A OH  
123  N N   . THR A 30  ? 0.43185 0.72809 0.46170 0.07076  -0.10112 0.24355  24  THR A N   
124  C CA  . THR A 30  ? 0.44145 0.73952 0.50135 0.10564  -0.11863 0.23744  24  THR A CA  
125  C C   . THR A 30  ? 0.47824 0.71797 0.52064 0.13511  -0.10164 0.21306  24  THR A C   
126  O O   . THR A 30  ? 0.49457 0.69561 0.51040 0.17723  -0.07571 0.25442  24  THR A O   
127  C CB  . THR A 30  ? 0.44996 0.76583 0.54565 0.09132  -0.09266 0.23984  24  THR A CB  
128  O OG1 . THR A 30  ? 0.42009 0.78541 0.56618 0.11312  -0.06822 0.26972  24  THR A OG1 
129  C CG2 . THR A 30  ? 0.49974 0.76613 0.56522 0.06145  -0.04179 0.22784  24  THR A CG2 
130  N N   . ASN A 31  ? 0.53804 0.70824 0.57267 0.14725  -0.06792 0.19394  25  ASN A N   
131  C CA  . ASN A 31  ? 0.55730 0.69239 0.58977 0.16293  -0.07754 0.19678  25  ASN A CA  
132  C C   . ASN A 31  ? 0.55847 0.67684 0.57437 0.15601  -0.08437 0.18664  25  ASN A C   
133  O O   . ASN A 31  ? 0.53782 0.67110 0.56403 0.16502  -0.08527 0.20727  25  ASN A O   
134  C CB  . ASN A 31  ? 0.57988 0.68693 0.63328 0.16848  -0.03610 0.20219  25  ASN A CB  
135  C CG  . ASN A 31  ? 0.60718 0.68496 0.66946 0.17957  0.00470  0.19708  25  ASN A CG  
136  O OD1 . ASN A 31  ? 0.61660 0.68379 0.70144 0.19711  0.02720  0.17845  25  ASN A OD1 
137  N ND2 . ASN A 31  ? 0.61461 0.68646 0.69402 0.17334  0.03121  0.19264  25  ASN A ND2 
138  N N   . LEU A 32  ? 0.57128 0.66875 0.56107 0.14154  -0.07555 0.15713  26  LEU A N   
139  C CA  . LEU A 32  ? 0.58803 0.65541 0.57544 0.15679  -0.06293 0.14139  26  LEU A CA  
140  C C   . LEU A 32  ? 0.59998 0.63690 0.61960 0.21350  -0.03894 0.13015  26  LEU A C   
141  O O   . LEU A 32  ? 0.61657 0.63692 0.69044 0.25299  -0.00129 0.13261  26  LEU A O   
142  C CB  . LEU A 32  ? 0.60281 0.67607 0.57534 0.09661  -0.06861 0.12657  26  LEU A CB  
143  C CG  . LEU A 32  ? 0.62184 0.69815 0.58707 0.04958  -0.05160 0.11483  26  LEU A CG  
144  C CD1 . LEU A 32  ? 0.58637 0.70046 0.56081 0.03994  -0.10910 0.10591  26  LEU A CD1 
145  C CD2 . LEU A 32  ? 0.66075 0.71177 0.60339 0.02954  -0.02634 0.10631  26  LEU A CD2 
146  N N   . SER A 33  ? 0.57495 0.62370 0.58475 0.19519  -0.04130 0.10761  27  SER A N   
147  C CA  . SER A 33  ? 0.57818 0.61956 0.55102 0.15929  -0.06301 0.08946  27  SER A CA  
148  C C   . SER A 33  ? 0.64134 0.59006 0.54143 0.14899  -0.00519 0.08356  27  SER A C   
149  O O   . SER A 33  ? 0.64520 0.55796 0.53574 0.17010  -0.00364 0.04524  27  SER A O   
150  C CB  . SER A 33  ? 0.58090 0.64382 0.56750 0.13346  -0.07934 0.07710  27  SER A CB  
151  O OG  . SER A 33  ? 0.62131 0.66056 0.58131 0.12107  -0.07633 0.05433  27  SER A OG  
152  N N   . TYR A 34  ? 0.67780 0.58137 0.52134 0.11905  0.02214  0.10963  28  TYR A N   
153  C CA  . TYR A 34  ? 0.70951 0.58983 0.51168 0.10310  0.04003  0.12262  28  TYR A CA  
154  C C   . TYR A 34  ? 0.74626 0.63829 0.50173 0.10961  0.03807  0.13482  28  TYR A C   
155  O O   . TYR A 34  ? 0.79522 0.64097 0.49002 0.10159  0.08637  0.13212  28  TYR A O   
156  C CB  . TYR A 34  ? 0.70378 0.55864 0.53498 0.10242  0.03186  0.09490  28  TYR A CB  
157  C CG  . TYR A 34  ? 0.69382 0.53555 0.55521 0.10615  0.00840  0.08520  28  TYR A CG  
158  C CD1 . TYR A 34  ? 0.73269 0.53701 0.58976 0.08971  -0.01480 0.07166  28  TYR A CD1 
159  C CD2 . TYR A 34  ? 0.65855 0.53189 0.53642 0.12317  0.01948  0.08969  28  TYR A CD2 
160  C CE1 . TYR A 34  ? 0.74474 0.55060 0.58580 0.09207  -0.03245 0.06614  28  TYR A CE1 
161  C CE2 . TYR A 34  ? 0.67706 0.54566 0.55493 0.12630  0.03939  0.08272  28  TYR A CE2 
162  C CZ  . TYR A 34  ? 0.72157 0.56370 0.57611 0.11403  -0.00997 0.07135  28  TYR A CZ  
163  O OH  . TYR A 34  ? 0.73764 0.58580 0.57785 0.10690  -0.04335 0.05096  28  TYR A OH  
164  N N   . ILE A 35  ? 0.72134 0.67274 0.50774 0.12761  -0.00720 0.13489  29  ILE A N   
165  C CA  . ILE A 35  ? 0.74550 0.71841 0.52742 0.10137  -0.00989 0.11221  29  ILE A CA  
166  C C   . ILE A 35  ? 0.79858 0.77704 0.59053 0.07195  -0.00453 0.04859  29  ILE A C   
167  O O   . ILE A 35  ? 0.83811 0.80153 0.59230 0.05448  -0.00323 0.02516  29  ILE A O   
168  C CB  . ILE A 35  ? 0.72670 0.70820 0.48196 0.08537  -0.01897 0.14884  29  ILE A CB  
169  C CG1 . ILE A 35  ? 0.71263 0.70264 0.47243 0.07192  -0.00889 0.14365  29  ILE A CG1 
170  C CG2 . ILE A 35  ? 0.73252 0.70672 0.47043 0.07945  -0.01203 0.17766  29  ILE A CG2 
171  C CD1 . ILE A 35  ? 0.69605 0.70368 0.43995 0.06309  -0.02124 0.16034  29  ILE A CD1 
172  N N   . GLY A 36  ? 0.80507 0.80500 0.63630 0.05592  0.00376  0.03915  30  GLY A N   
173  C CA  . GLY A 36  ? 0.82820 0.82332 0.69857 0.04358  0.01270  0.02946  30  GLY A CA  
174  C C   . GLY A 36  ? 0.84317 0.83403 0.75131 0.03674  -0.00970 0.02825  30  GLY A C   
175  O O   . GLY A 36  ? 0.84663 0.82892 0.75802 0.05735  -0.02430 0.05142  30  GLY A O   
176  N N   . GLU A 37  ? 0.85568 0.84571 0.78418 0.01276  -0.02285 -0.00079 31  GLU A N   
177  C CA  . GLU A 37  ? 0.89674 0.85737 0.84206 -0.00349 0.01700  -0.01919 31  GLU A CA  
178  C C   . GLU A 37  ? 0.91621 0.87753 0.90320 -0.03518 0.07151  -0.03976 31  GLU A C   
179  O O   . GLU A 37  ? 0.90634 0.87645 0.89220 -0.05442 0.07331  -0.02706 31  GLU A O   
180  C CB  . GLU A 37  ? 0.93722 0.84921 0.84577 -0.00290 0.02772  -0.01643 31  GLU A CB  
181  C CG  . GLU A 37  ? 0.97044 0.84956 0.86356 -0.01174 0.04250  -0.01493 31  GLU A CG  
182  C CD  . GLU A 37  ? 1.00028 0.85082 0.89299 -0.02354 0.05830  -0.01643 31  GLU A CD  
183  O OE1 . GLU A 37  ? 1.00019 0.83703 0.88515 -0.04102 0.05594  -0.03020 31  GLU A OE1 
184  O OE2 . GLU A 37  ? 1.01971 0.86422 0.91763 -0.01739 0.07272  -0.00585 31  GLU A OE2 
185  N N   . GLY A 38  ? 0.93256 0.89446 0.95960 -0.03858 0.09179  -0.06650 32  GLY A N   
186  C CA  . GLY A 38  ? 0.93593 0.90065 0.98525 -0.03103 0.08574  -0.08781 32  GLY A CA  
187  C C   . GLY A 38  ? 0.95399 0.91056 1.00521 -0.02022 0.08496  -0.10614 32  GLY A C   
188  O O   . GLY A 38  ? 0.95619 0.91033 1.02534 -0.02492 0.09659  -0.11432 32  GLY A O   
189  N N   . ALA A 39  ? 0.97318 0.91475 1.00259 -0.01881 0.07944  -0.10647 33  ALA A N   
190  C CA  . ALA A 39  ? 1.00863 0.90649 0.99302 -0.01096 0.06618  -0.10007 33  ALA A CA  
191  C C   . ALA A 39  ? 1.01449 0.89048 0.97991 -0.02717 0.02092  -0.11903 33  ALA A C   
192  O O   . ALA A 39  ? 1.02785 0.88476 0.96774 -0.03916 0.00350  -0.15588 33  ALA A O   
193  C CB  . ALA A 39  ? 1.02317 0.90574 0.99291 0.01630  0.07665  -0.08447 33  ALA A CB  
194  N N   . TYR A 40  ? 0.97379 0.87228 0.95640 -0.03135 -0.04181 -0.10375 34  TYR A N   
195  C CA  . TYR A 40  ? 0.91717 0.83849 0.93446 -0.02439 -0.08996 -0.09399 34  TYR A CA  
196  C C   . TYR A 40  ? 0.88500 0.77475 0.88707 -0.06702 -0.07202 -0.09420 34  TYR A C   
197  O O   . TYR A 40  ? 0.89339 0.76123 0.87662 -0.08910 -0.06660 -0.10716 34  TYR A O   
198  C CB  . TYR A 40  ? 0.88827 0.86301 0.96545 0.02056  -0.11258 -0.10034 34  TYR A CB  
199  C CG  . TYR A 40  ? 0.88215 0.88865 1.01609 0.05361  -0.10702 -0.11213 34  TYR A CG  
200  C CD1 . TYR A 40  ? 0.88512 0.89680 1.05413 0.06617  -0.08934 -0.11067 34  TYR A CD1 
201  C CD2 . TYR A 40  ? 0.87733 0.89753 1.02973 0.06537  -0.11497 -0.12804 34  TYR A CD2 
202  C CE1 . TYR A 40  ? 0.88258 0.90693 1.06794 0.07512  -0.09380 -0.11446 34  TYR A CE1 
203  C CE2 . TYR A 40  ? 0.87744 0.90548 1.05083 0.08690  -0.11425 -0.11746 34  TYR A CE2 
204  C CZ  . TYR A 40  ? 0.88019 0.91406 1.06084 0.09742  -0.11514 -0.10200 34  TYR A CZ  
205  O OH  . TYR A 40  ? 0.89006 0.92576 1.04858 0.10540  -0.13180 -0.09176 34  TYR A OH  
206  N N   . GLY A 41  ? 0.85020 0.72523 0.83070 -0.07829 -0.04297 -0.08047 35  GLY A N   
207  C CA  . GLY A 41  ? 0.81886 0.67745 0.75557 -0.08099 -0.02181 -0.05313 35  GLY A CA  
208  C C   . GLY A 41  ? 0.79047 0.62875 0.65964 -0.08985 -0.02052 -0.02868 35  GLY A C   
209  O O   . GLY A 41  ? 0.80993 0.61693 0.61448 -0.08121 -0.03027 0.00709  35  GLY A O   
210  N N   . MET A 42  ? 0.76146 0.58184 0.60370 -0.10209 -0.00597 -0.03158 36  MET A N   
211  C CA  . MET A 42  ? 0.73150 0.53505 0.55550 -0.09001 -0.02096 -0.01091 36  MET A CA  
212  C C   . MET A 42  ? 0.64301 0.48016 0.45351 -0.10561 -0.04043 0.02887  36  MET A C   
213  O O   . MET A 42  ? 0.63665 0.46891 0.44966 -0.10275 -0.01047 0.09159  36  MET A O   
214  C CB  . MET A 42  ? 0.79301 0.54653 0.58780 -0.08060 -0.02807 -0.03637 36  MET A CB  
215  C CG  . MET A 42  ? 0.81762 0.54868 0.60123 -0.07447 -0.04148 -0.07549 36  MET A CG  
216  S SD  . MET A 42  ? 0.86086 0.55556 0.61872 -0.05504 -0.01907 -0.09097 36  MET A SD  
217  C CE  . MET A 42  ? 0.85944 0.54932 0.62952 -0.04900 -0.02554 -0.10538 36  MET A CE  
218  N N   . VAL A 43  ? 0.60949 0.45101 0.36999 -0.11503 -0.04100 0.02763  37  VAL A N   
219  C CA  . VAL A 43  ? 0.56702 0.48197 0.36122 -0.06340 -0.02868 0.05346  37  VAL A CA  
220  C C   . VAL A 43  ? 0.54938 0.48671 0.40270 0.00406  0.01722  0.05804  37  VAL A C   
221  O O   . VAL A 43  ? 0.55531 0.51738 0.40793 0.00070  0.04032  0.05410  37  VAL A O   
222  C CB  . VAL A 43  ? 0.57900 0.49510 0.35905 -0.08142 -0.03001 0.07076  37  VAL A CB  
223  C CG1 . VAL A 43  ? 0.55327 0.51043 0.35498 -0.11632 -0.01662 0.07124  37  VAL A CG1 
224  C CG2 . VAL A 43  ? 0.58051 0.50435 0.37629 -0.09271 -0.04485 0.06438  37  VAL A CG2 
225  N N   . CYS A 44  ? 0.51733 0.46048 0.40086 0.04980  0.02513  0.07532  38  CYS A N   
226  C CA  . CYS A 44  ? 0.51861 0.45083 0.40275 0.06704  0.01634  0.05657  38  CYS A CA  
227  C C   . CYS A 44  ? 0.45732 0.48419 0.38826 0.09691  -0.02149 0.04015  38  CYS A C   
228  O O   . CYS A 44  ? 0.41610 0.46584 0.38827 0.09783  -0.04376 0.00208  38  CYS A O   
229  C CB  . CYS A 44  ? 0.58581 0.41141 0.42728 0.06408  0.01297  0.06679  38  CYS A CB  
230  S SG  . CYS A 44  ? 0.63119 0.38991 0.45115 0.04603  0.07303  0.05317  38  CYS A SG  
231  N N   . SER A 45  ? 0.43654 0.52334 0.39793 0.11007  -0.00974 0.05722  39  SER A N   
232  C CA  . SER A 45  ? 0.45685 0.55073 0.40706 0.15584  0.01650  0.08009  39  SER A CA  
233  C C   . SER A 45  ? 0.42703 0.56611 0.39510 0.17171  -0.00274 0.11574  39  SER A C   
234  O O   . SER A 45  ? 0.46408 0.58100 0.43306 0.18576  0.05295  0.12899  39  SER A O   
235  C CB  . SER A 45  ? 0.47829 0.54940 0.42558 0.21343  0.04158  0.09912  39  SER A CB  
236  O OG  . SER A 45  ? 0.49398 0.54548 0.45177 0.27676  0.07071  0.09282  39  SER A OG  
237  N N   . ALA A 46  ? 0.39246 0.57446 0.34932 0.14336  -0.02793 0.10014  40  ALA A N   
238  C CA  . ALA A 46  ? 0.34142 0.58702 0.32624 0.13258  -0.02940 0.11389  40  ALA A CA  
239  C C   . ALA A 46  ? 0.31143 0.60721 0.36021 0.11393  -0.04148 0.12941  40  ALA A C   
240  O O   . ALA A 46  ? 0.34896 0.58954 0.33222 0.10612  -0.03782 0.14595  40  ALA A O   
241  C CB  . ALA A 46  ? 0.41322 0.58700 0.27173 0.11811  0.04079  0.10020  40  ALA A CB  
242  N N   . TYR A 47  ? 0.23969 0.64262 0.38822 0.08340  -0.05179 0.13772  41  TYR A N   
243  C CA  . TYR A 47  ? 0.26255 0.65530 0.41184 0.04156  -0.05226 0.13304  41  TYR A CA  
244  C C   . TYR A 47  ? 0.27334 0.66974 0.42275 -0.00290 -0.01662 0.14946  41  TYR A C   
245  O O   . TYR A 47  ? 0.30188 0.67171 0.43100 0.02647  -0.00616 0.14926  41  TYR A O   
246  C CB  . TYR A 47  ? 0.25158 0.65086 0.41430 0.04822  -0.04855 0.12295  41  TYR A CB  
247  C CG  . TYR A 47  ? 0.21623 0.63408 0.37702 0.02749  -0.07658 0.12203  41  TYR A CG  
248  C CD1 . TYR A 47  ? 0.24757 0.64047 0.38469 0.01541  -0.05197 0.11267  41  TYR A CD1 
249  C CD2 . TYR A 47  ? 0.26431 0.62526 0.35803 0.03955  -0.04303 0.13381  41  TYR A CD2 
250  C CE1 . TYR A 47  ? 0.26518 0.64925 0.42345 0.00371  -0.00004 0.09183  41  TYR A CE1 
251  C CE2 . TYR A 47  ? 0.25477 0.63502 0.36713 0.02398  -0.01796 0.11265  41  TYR A CE2 
252  C CZ  . TYR A 47  ? 0.26421 0.65744 0.42572 -0.00127 -0.00578 0.08074  41  TYR A CZ  
253  O OH  . TYR A 47  ? 0.29032 0.68494 0.45416 -0.00969 0.01111  0.05057  41  TYR A OH  
254  N N   . ASP A 48  ? 0.27253 0.68847 0.42506 -0.06019 -0.01609 0.15838  42  ASP A N   
255  C CA  . ASP A 48  ? 0.25699 0.71314 0.42214 -0.05650 -0.05402 0.15879  42  ASP A CA  
256  C C   . ASP A 48  ? 0.28840 0.75681 0.44659 -0.06374 -0.07242 0.16974  42  ASP A C   
257  O O   . ASP A 48  ? 0.27724 0.78476 0.47351 -0.06727 -0.06206 0.13167  42  ASP A O   
258  C CB  . ASP A 48  ? 0.29640 0.71757 0.41827 -0.02881 -0.03708 0.13982  42  ASP A CB  
259  C CG  . ASP A 48  ? 0.34920 0.73312 0.39931 0.00773  -0.03043 0.15500  42  ASP A CG  
260  O OD1 . ASP A 48  ? 0.36399 0.72713 0.41518 0.00694  0.02198  0.16201  42  ASP A OD1 
261  O OD2 . ASP A 48  ? 0.41139 0.74319 0.38234 0.01423  -0.04056 0.15914  42  ASP A OD2 
262  N N   . ASN A 49  ? 0.28145 0.77713 0.46492 -0.07819 -0.10351 0.19060  43  ASN A N   
263  C CA  . ASN A 49  ? 0.30304 0.78035 0.48088 -0.10551 -0.13541 0.18756  43  ASN A CA  
264  C C   . ASN A 49  ? 0.29347 0.75753 0.53567 -0.13995 -0.13706 0.12818  43  ASN A C   
265  O O   . ASN A 49  ? 0.30878 0.77167 0.58701 -0.14231 -0.13801 0.10105  43  ASN A O   
266  C CB  . ASN A 49  ? 0.36038 0.80898 0.44766 -0.06741 -0.12971 0.23455  43  ASN A CB  
267  C CG  . ASN A 49  ? 0.33828 0.81872 0.50207 -0.04016 -0.13632 0.24073  43  ASN A CG  
268  O OD1 . ASN A 49  ? 0.37246 0.84415 0.53726 -0.04169 -0.11815 0.24982  43  ASN A OD1 
269  N ND2 . ASN A 49  ? 0.31680 0.81764 0.54415 -0.02426 -0.12630 0.25098  43  ASN A ND2 
270  N N   . LEU A 50  ? 0.35237 0.77146 0.53353 -0.10992 -0.12039 0.16396  44  LEU A N   
271  C CA  . LEU A 50  ? 0.41858 0.77442 0.53414 -0.16230 -0.11467 0.11814  44  LEU A CA  
272  C C   . LEU A 50  ? 0.47972 0.78653 0.52925 -0.16488 -0.15125 0.12962  44  LEU A C   
273  O O   . LEU A 50  ? 0.50297 0.78833 0.53363 -0.18579 -0.13344 0.16317  44  LEU A O   
274  C CB  . LEU A 50  ? 0.49632 0.77939 0.56556 -0.16493 -0.06359 0.09200  44  LEU A CB  
275  C CG  . LEU A 50  ? 0.58114 0.78696 0.60979 -0.16854 0.00902  0.08444  44  LEU A CG  
276  C CD1 . LEU A 50  ? 0.58153 0.79227 0.61663 -0.16518 0.00878  0.07953  44  LEU A CD1 
277  C CD2 . LEU A 50  ? 0.62942 0.79359 0.64630 -0.17150 0.03584  0.07728  44  LEU A CD2 
278  N N   . ASN A 51  ? 0.49732 0.79177 0.50973 -0.14846 -0.16122 0.11494  45  ASN A N   
279  C CA  . ASN A 51  ? 0.53026 0.78941 0.51578 -0.12581 -0.11918 0.12284  45  ASN A CA  
280  C C   . ASN A 51  ? 0.52655 0.79007 0.54525 -0.12748 -0.03936 0.13227  45  ASN A C   
281  O O   . ASN A 51  ? 0.56448 0.78958 0.55511 -0.12553 -0.01300 0.14231  45  ASN A O   
282  C CB  . ASN A 51  ? 0.61138 0.79677 0.55281 -0.11757 -0.07341 0.10845  45  ASN A CB  
283  C CG  . ASN A 51  ? 0.69742 0.81419 0.59126 -0.11544 -0.02211 0.09006  45  ASN A CG  
284  O OD1 . ASN A 51  ? 0.74644 0.82244 0.62986 -0.11349 0.00803  0.08272  45  ASN A OD1 
285  N ND2 . ASN A 51  ? 0.73823 0.82812 0.59870 -0.10597 0.00342  0.07824  45  ASN A ND2 
286  N N   . LYS A 52  ? 0.48753 0.79995 0.54552 -0.12401 -0.01214 0.10771  46  LYS A N   
287  C CA  . LYS A 52  ? 0.40613 0.79721 0.53664 -0.16718 -0.00441 0.07452  46  LYS A CA  
288  C C   . LYS A 52  ? 0.40414 0.80545 0.51373 -0.16526 0.02542  0.05314  46  LYS A C   
289  O O   . LYS A 52  ? 0.43798 0.82763 0.53407 -0.15061 0.02114  0.05440  46  LYS A O   
290  C CB  . LYS A 52  ? 0.35020 0.77999 0.53738 -0.19579 -0.04769 0.03376  46  LYS A CB  
291  C CG  . LYS A 52  ? 0.40293 0.77770 0.58111 -0.17616 -0.03503 0.02062  46  LYS A CG  
292  C CD  . LYS A 52  ? 0.47401 0.77610 0.62048 -0.15010 -0.00555 0.01544  46  LYS A CD  
293  C CE  . LYS A 52  ? 0.51604 0.77671 0.64802 -0.13145 0.02637  0.02770  46  LYS A CE  
294  N NZ  . LYS A 52  ? 0.51733 0.77542 0.66195 -0.12932 0.02564  0.03003  46  LYS A NZ  
295  N N   . VAL A 53  ? 0.39448 0.78361 0.46905 -0.15188 0.03114  0.05996  47  VAL A N   
296  C CA  . VAL A 53  ? 0.39154 0.75155 0.43539 -0.10638 -0.00604 0.07629  47  VAL A CA  
297  C C   . VAL A 53  ? 0.35215 0.72544 0.38225 -0.02292 -0.03810 0.08466  47  VAL A C   
298  O O   . VAL A 53  ? 0.30626 0.72602 0.36519 0.02286  -0.02230 0.06979  47  VAL A O   
299  C CB  . VAL A 53  ? 0.45357 0.74097 0.45641 -0.09961 0.00078  0.07875  47  VAL A CB  
300  C CG1 . VAL A 53  ? 0.43560 0.72899 0.42515 -0.08777 0.00968  0.07459  47  VAL A CG1 
301  C CG2 . VAL A 53  ? 0.51466 0.74574 0.49393 -0.11040 0.00061  0.05961  47  VAL A CG2 
302  N N   . ARG A 54  ? 0.34170 0.69058 0.36226 0.02335  -0.00578 0.09725  48  ARG A N   
303  C CA  . ARG A 54  ? 0.31789 0.66954 0.35132 0.07117  -0.05145 0.11398  48  ARG A CA  
304  C C   . ARG A 54  ? 0.29579 0.63356 0.30675 0.04369  -0.05288 0.12655  48  ARG A C   
305  O O   . ARG A 54  ? 0.32771 0.62915 0.31152 0.01486  -0.05001 0.08682  48  ARG A O   
306  C CB  . ARG A 54  ? 0.31029 0.68351 0.33938 0.12505  -0.07465 0.11771  48  ARG A CB  
307  C CG  . ARG A 54  ? 0.30634 0.69752 0.40309 0.14128  -0.05619 0.10302  48  ARG A CG  
308  C CD  . ARG A 54  ? 0.39248 0.70312 0.47218 0.18539  0.01206  0.11799  48  ARG A CD  
309  N NE  . ARG A 54  ? 0.45025 0.69855 0.49369 0.22461  0.05661  0.12625  48  ARG A NE  
310  C CZ  . ARG A 54  ? 0.48326 0.69839 0.49819 0.26153  0.04203  0.14627  48  ARG A CZ  
311  N NH1 . ARG A 54  ? 0.49031 0.70268 0.47357 0.28759  0.02786  0.17405  48  ARG A NH1 
312  N NH2 . ARG A 54  ? 0.51237 0.69401 0.51274 0.27028  0.02743  0.14679  48  ARG A NH2 
313  N N   . VAL A 55  ? 0.27758 0.61969 0.32752 0.06501  -0.01101 0.12914  49  VAL A N   
314  C CA  . VAL A 55  ? 0.22763 0.58230 0.26755 0.04422  -0.02953 0.11562  49  VAL A CA  
315  C C   . VAL A 55  ? 0.24021 0.54762 0.27886 0.04661  0.00694  0.10913  49  VAL A C   
316  O O   . VAL A 55  ? 0.25153 0.54051 0.30650 0.03892  0.00247  0.13822  49  VAL A O   
317  C CB  . VAL A 55  ? 0.23307 0.58131 0.24925 0.02065  -0.05262 0.11123  49  VAL A CB  
318  C CG1 . VAL A 55  ? 0.29646 0.56856 0.26875 0.00030  -0.03861 0.11861  49  VAL A CG1 
319  C CG2 . VAL A 55  ? 0.21667 0.55756 0.26424 0.00799  -0.07332 0.11069  49  VAL A CG2 
320  N N   . ALA A 56  ? 0.24194 0.53326 0.22764 0.03645  0.00247  0.08107  50  ALA A N   
321  C CA  . ALA A 56  ? 0.22843 0.51089 0.18530 0.00544  -0.04019 0.09874  50  ALA A CA  
322  C C   . ALA A 56  ? 0.32560 0.48985 0.24258 0.02734  0.00084  0.11283  50  ALA A C   
323  O O   . ALA A 56  ? 0.34356 0.48453 0.32726 0.03665  0.02685  0.14979  50  ALA A O   
324  C CB  . ALA A 56  ? 0.24157 0.51139 0.22669 -0.00035 -0.01482 0.09914  50  ALA A CB  
325  N N   . ILE A 57  ? 0.34683 0.44455 0.21945 0.01473  -0.01529 0.10914  51  ILE A N   
326  C CA  . ILE A 57  ? 0.35688 0.44207 0.21539 0.02732  -0.00672 0.06071  51  ILE A CA  
327  C C   . ILE A 57  ? 0.35659 0.46788 0.25479 0.01875  0.00620  0.05867  51  ILE A C   
328  O O   . ILE A 57  ? 0.37039 0.47544 0.27804 0.01919  0.00969  0.04772  51  ILE A O   
329  C CB  . ILE A 57  ? 0.37701 0.43219 0.21975 0.03288  -0.01633 0.07435  51  ILE A CB  
330  C CG1 . ILE A 57  ? 0.37202 0.42782 0.23861 0.02643  -0.02303 0.08831  51  ILE A CG1 
331  C CG2 . ILE A 57  ? 0.40360 0.42537 0.19550 0.04100  -0.00239 0.06929  51  ILE A CG2 
332  C CD1 . ILE A 57  ? 0.37407 0.42768 0.26011 0.02417  -0.03846 0.12094  51  ILE A CD1 
333  N N   . LYS A 58  ? 0.32303 0.48318 0.25143 0.01782  0.01960  0.04445  52  LYS A N   
334  C CA  . LYS A 58  ? 0.32988 0.49558 0.24211 -0.00850 -0.00781 0.05278  52  LYS A CA  
335  C C   . LYS A 58  ? 0.37759 0.48688 0.24192 -0.01802 -0.00328 0.04011  52  LYS A C   
336  O O   . LYS A 58  ? 0.38981 0.49977 0.25943 -0.03317 0.00504  0.02039  52  LYS A O   
337  C CB  . LYS A 58  ? 0.33384 0.53121 0.28702 -0.04467 -0.06333 0.00305  52  LYS A CB  
338  C CG  . LYS A 58  ? 0.39647 0.54527 0.34732 0.00127  -0.05550 0.02468  52  LYS A CG  
339  C CD  . LYS A 58  ? 0.39685 0.53995 0.36359 0.07501  -0.11085 0.04523  52  LYS A CD  
340  C CE  . LYS A 58  ? 0.41107 0.54735 0.34523 0.11597  -0.14876 0.08463  52  LYS A CE  
341  N NZ  . LYS A 58  ? 0.44839 0.54087 0.39197 0.12111  -0.09781 0.07820  52  LYS A NZ  
342  N N   . LYS A 59  ? 0.46243 0.44889 0.24839 0.00291  0.02535  0.06552  53  LYS A N   
343  C CA  . LYS A 59  ? 0.45701 0.45300 0.28728 -0.01730 -0.00455 0.05032  53  LYS A CA  
344  C C   . LYS A 59  ? 0.40669 0.47333 0.27708 -0.03449 -0.03246 -0.02722 53  LYS A C   
345  O O   . LYS A 59  ? 0.43145 0.49513 0.32549 -0.01526 0.01559  -0.09355 53  LYS A O   
346  C CB  . LYS A 59  ? 0.52869 0.42884 0.34015 -0.02427 0.03825  0.10084  53  LYS A CB  
347  C CG  . LYS A 59  ? 0.56650 0.43325 0.38227 -0.03279 0.03113  0.13613  53  LYS A CG  
348  C CD  . LYS A 59  ? 0.63759 0.44175 0.39337 -0.01792 0.02824  0.19750  53  LYS A CD  
349  C CE  . LYS A 59  ? 0.70548 0.44491 0.44335 -0.02299 0.06579  0.22696  53  LYS A CE  
350  N NZ  . LYS A 59  ? 0.76945 0.47874 0.44961 -0.04906 0.11893  0.23428  53  LYS A NZ  
351  N N   . ILE A 60  ? 0.38468 0.46304 0.27542 -0.08656 0.02829  -0.01915 54  ILE A N   
352  C CA  . ILE A 60  ? 0.36467 0.47383 0.30618 -0.10733 0.04042  0.01668  54  ILE A CA  
353  C C   . ILE A 60  ? 0.43949 0.45388 0.30654 -0.14119 0.02642  0.02048  54  ILE A C   
354  O O   . ILE A 60  ? 0.46388 0.45952 0.26765 -0.13701 0.00629  0.01656  54  ILE A O   
355  C CB  . ILE A 60  ? 0.32606 0.51849 0.35445 -0.10320 0.02107  0.03246  54  ILE A CB  
356  C CG1 . ILE A 60  ? 0.42109 0.51067 0.42813 -0.04698 0.04045  0.04619  54  ILE A CG1 
357  C CG2 . ILE A 60  ? 0.33430 0.56381 0.36383 -0.07873 0.05400  0.01253  54  ILE A CG2 
358  C CD1 . ILE A 60  ? 0.47020 0.51864 0.47654 -0.04480 0.02636  0.04009  54  ILE A CD1 
359  N N   . SER A 61  ? 0.46370 0.44426 0.36864 -0.17416 0.00158  0.01487  55  SER A N   
360  C CA  . SER A 61  ? 0.48978 0.44060 0.40636 -0.12982 0.02061  0.02578  55  SER A CA  
361  C C   . SER A 61  ? 0.49449 0.41436 0.38418 -0.19640 -0.03319 0.00239  55  SER A C   
362  O O   . SER A 61  ? 0.55634 0.38785 0.46968 -0.19932 0.02629  -0.01328 55  SER A O   
363  C CB  . SER A 61  ? 0.51829 0.46369 0.46663 -0.05784 0.09153  0.05235  55  SER A CB  
364  O OG  . SER A 61  ? 0.53807 0.47492 0.49553 -0.01902 0.14207  0.06864  55  SER A OG  
365  N N   . PRO A 62  ? 0.49248 0.44735 0.34178 -0.21123 -0.01984 0.03530  56  PRO A N   
366  C CA  . PRO A 62  ? 0.48639 0.47580 0.35999 -0.20913 -0.01756 0.04733  56  PRO A CA  
367  C C   . PRO A 62  ? 0.45898 0.50471 0.34644 -0.22606 -0.00702 0.03619  56  PRO A C   
368  O O   . PRO A 62  ? 0.46459 0.52459 0.30461 -0.24174 -0.00046 0.05340  56  PRO A O   
369  C CB  . PRO A 62  ? 0.50186 0.46864 0.36074 -0.22455 -0.03126 0.05642  56  PRO A CB  
370  C CG  . PRO A 62  ? 0.53951 0.46599 0.36496 -0.20707 -0.00644 0.05916  56  PRO A CG  
371  C CD  . PRO A 62  ? 0.52689 0.44238 0.33341 -0.20817 -0.01800 0.05237  56  PRO A CD  
372  N N   . PHE A 63  ? 0.42632 0.50630 0.33144 -0.20880 -0.02088 0.03815  57  PHE A N   
373  C CA  . PHE A 63  ? 0.40912 0.51416 0.34905 -0.19909 -0.03498 0.05558  57  PHE A CA  
374  C C   . PHE A 63  ? 0.43918 0.55097 0.40478 -0.17018 0.02368  0.10180  57  PHE A C   
375  O O   . PHE A 63  ? 0.48052 0.58450 0.42476 -0.12905 0.09599  0.09450  57  PHE A O   
376  C CB  . PHE A 63  ? 0.41009 0.50504 0.32347 -0.15659 -0.01898 0.08987  57  PHE A CB  
377  C CG  . PHE A 63  ? 0.32524 0.48456 0.29797 -0.14950 -0.06765 0.07923  57  PHE A CG  
378  C CD1 . PHE A 63  ? 0.36123 0.47689 0.29784 -0.12146 -0.01740 0.07093  57  PHE A CD1 
379  C CD2 . PHE A 63  ? 0.33898 0.47299 0.31706 -0.13869 -0.02074 0.06232  57  PHE A CD2 
380  C CE1 . PHE A 63  ? 0.32452 0.45988 0.24213 -0.10715 -0.05168 0.07674  57  PHE A CE1 
381  C CE2 . PHE A 63  ? 0.36738 0.45256 0.26186 -0.11883 -0.03770 0.02309  57  PHE A CE2 
382  C CZ  . PHE A 63  ? 0.34510 0.46171 0.24587 -0.10914 -0.03732 0.04358  57  PHE A CZ  
383  N N   . GLU A 64  ? 0.45889 0.52192 0.44339 -0.22253 0.01752  0.11906  58  GLU A N   
384  C CA  . GLU A 64  ? 0.49682 0.53836 0.51674 -0.21639 0.02893  0.12455  58  GLU A CA  
385  C C   . GLU A 64  ? 0.49392 0.54815 0.53922 -0.20603 0.01848  0.13049  58  GLU A C   
386  O O   . GLU A 64  ? 0.50643 0.55749 0.56395 -0.21347 0.01029  0.10713  58  GLU A O   
387  C CB  . GLU A 64  ? 0.50145 0.52946 0.56639 -0.22685 0.01377  0.11257  58  GLU A CB  
388  C CG  . GLU A 64  ? 0.53124 0.54494 0.62367 -0.21813 0.00972  0.09391  58  GLU A CG  
389  C CD  . GLU A 64  ? 0.56984 0.56834 0.65866 -0.19654 0.01736  0.09104  58  GLU A CD  
390  O OE1 . GLU A 64  ? 0.57262 0.58218 0.67922 -0.16455 0.00302  0.07756  58  GLU A OE1 
391  O OE2 . GLU A 64  ? 0.62262 0.58767 0.67658 -0.17784 0.05768  0.11305  58  GLU A OE2 
392  N N   . HIS A 65  ? 0.50545 0.54180 0.56847 -0.17868 0.02020  0.13741  59  HIS A N   
393  C CA  . HIS A 65  ? 0.50347 0.54066 0.57694 -0.17092 -0.00490 0.12040  59  HIS A CA  
394  C C   . HIS A 65  ? 0.43187 0.55145 0.55817 -0.19385 -0.07334 0.12668  59  HIS A C   
395  O O   . HIS A 65  ? 0.43394 0.54584 0.53957 -0.22233 -0.03817 0.13075  59  HIS A O   
396  C CB  . HIS A 65  ? 0.55333 0.53678 0.57406 -0.14617 0.01183  0.07669  59  HIS A CB  
397  C CG  . HIS A 65  ? 0.58823 0.55048 0.60518 -0.09723 0.02420  0.05345  59  HIS A CG  
398  N ND1 . HIS A 65  ? 0.59530 0.55168 0.62842 -0.08845 0.00813  0.04304  59  HIS A ND1 
399  C CD2 . HIS A 65  ? 0.59687 0.56063 0.62572 -0.07491 0.01895  0.05030  59  HIS A CD2 
400  C CE1 . HIS A 65  ? 0.60452 0.56120 0.65114 -0.07876 0.01925  0.04193  59  HIS A CE1 
401  N NE2 . HIS A 65  ? 0.59702 0.56413 0.65035 -0.07569 0.01759  0.04228  59  HIS A NE2 
402  N N   . GLN A 66  ? 0.36827 0.57483 0.55640 -0.18649 -0.12899 0.14680  60  GLN A N   
403  C CA  . GLN A 66  ? 0.37052 0.59827 0.57091 -0.18734 -0.10862 0.14922  60  GLN A CA  
404  C C   . GLN A 66  ? 0.45101 0.59426 0.49961 -0.20450 -0.07249 0.13759  60  GLN A C   
405  O O   . GLN A 66  ? 0.43536 0.61086 0.46949 -0.19215 -0.09512 0.13159  60  GLN A O   
406  C CB  . GLN A 66  ? 0.34998 0.62077 0.67160 -0.16575 -0.08967 0.14807  60  GLN A CB  
407  C CG  . GLN A 66  ? 0.38210 0.65459 0.72002 -0.10446 -0.07716 0.13711  60  GLN A CG  
408  C CD  . GLN A 66  ? 0.44494 0.67901 0.77487 -0.06134 -0.02250 0.10623  60  GLN A CD  
409  O OE1 . GLN A 66  ? 0.46828 0.68873 0.79662 -0.04670 0.00940  0.09056  60  GLN A OE1 
410  N NE2 . GLN A 66  ? 0.46283 0.68217 0.78987 -0.05521 -0.02625 0.08423  60  GLN A NE2 
411  N N   . THR A 67  ? 0.50623 0.57746 0.49293 -0.22787 -0.03320 0.10317  61  THR A N   
412  C CA  . THR A 67  ? 0.51947 0.56145 0.50715 -0.21039 -0.02836 0.06006  61  THR A CA  
413  C C   . THR A 67  ? 0.51445 0.55110 0.46286 -0.22798 -0.03160 0.05047  61  THR A C   
414  O O   . THR A 67  ? 0.51539 0.56088 0.46215 -0.26591 -0.03325 0.04625  61  THR A O   
415  C CB  . THR A 67  ? 0.50699 0.54330 0.52119 -0.17762 -0.08308 0.02481  61  THR A CB  
416  O OG1 . THR A 67  ? 0.50527 0.54491 0.55643 -0.16425 -0.09263 0.01000  61  THR A OG1 
417  C CG2 . THR A 67  ? 0.49480 0.53603 0.50880 -0.16037 -0.11091 0.01679  61  THR A CG2 
418  N N   . TYR A 68  ? 0.48495 0.52107 0.38693 -0.20316 -0.07769 0.04245  62  TYR A N   
419  C CA  . TYR A 68  ? 0.48498 0.50489 0.35215 -0.18118 -0.05353 0.02306  62  TYR A CA  
420  C C   . TYR A 68  ? 0.45942 0.51749 0.34388 -0.16947 -0.02598 0.06039  62  TYR A C   
421  O O   . TYR A 68  ? 0.46107 0.52882 0.33212 -0.17936 -0.01754 0.08297  62  TYR A O   
422  C CB  . TYR A 68  ? 0.53379 0.49236 0.37507 -0.16520 -0.05797 -0.03696 62  TYR A CB  
423  C CG  . TYR A 68  ? 0.60285 0.48689 0.40536 -0.12940 -0.05551 -0.07640 62  TYR A CG  
424  C CD1 . TYR A 68  ? 0.63258 0.48911 0.41883 -0.11737 -0.05336 -0.09058 62  TYR A CD1 
425  C CD2 . TYR A 68  ? 0.63670 0.48367 0.42014 -0.09021 -0.07830 -0.08575 62  TYR A CD2 
426  C CE1 . TYR A 68  ? 0.66950 0.49275 0.44672 -0.09285 -0.01967 -0.10780 62  TYR A CE1 
427  C CE2 . TYR A 68  ? 0.67649 0.49387 0.45458 -0.06630 -0.05062 -0.09141 62  TYR A CE2 
428  C CZ  . TYR A 68  ? 0.70222 0.50015 0.45707 -0.07541 -0.03135 -0.11403 62  TYR A CZ  
429  O OH  . TYR A 68  ? 0.75253 0.51214 0.46812 -0.07942 -0.02420 -0.13233 62  TYR A OH  
430  N N   . CYS A 69  ? 0.44916 0.51777 0.30497 -0.12163 -0.02965 0.07838  63  CYS A N   
431  C CA  . CYS A 69  ? 0.41198 0.52069 0.29196 -0.08462 -0.02432 0.11072  63  CYS A CA  
432  C C   . CYS A 69  ? 0.37662 0.54851 0.29070 -0.07358 -0.01333 0.10943  63  CYS A C   
433  O O   . CYS A 69  ? 0.33196 0.55706 0.27798 -0.05926 -0.04441 0.12187  63  CYS A O   
434  C CB  . CYS A 69  ? 0.36768 0.51138 0.31245 -0.09216 -0.07188 0.13129  63  CYS A CB  
435  S SG  . CYS A 69  ? 0.43239 0.54192 0.33552 -0.11996 -0.01485 0.11033  63  CYS A SG  
436  N N   . GLN A 70  ? 0.33771 0.57579 0.29034 -0.09642 -0.09982 0.10680  64  GLN A N   
437  C CA  . GLN A 70  ? 0.36863 0.59579 0.36324 -0.09195 -0.10296 0.10634  64  GLN A CA  
438  C C   . GLN A 70  ? 0.36799 0.58540 0.33604 -0.11535 -0.08683 0.11451  64  GLN A C   
439  O O   . GLN A 70  ? 0.34762 0.57990 0.35946 -0.13474 -0.11078 0.15611  64  GLN A O   
440  C CB  . GLN A 70  ? 0.36370 0.62527 0.41371 -0.05436 -0.18928 0.12194  64  GLN A CB  
441  C CG  . GLN A 70  ? 0.39315 0.67737 0.50979 -0.06372 -0.22312 0.06161  64  GLN A CG  
442  C CD  . GLN A 70  ? 0.39471 0.71960 0.56320 -0.06868 -0.21642 0.00949  64  GLN A CD  
443  O OE1 . GLN A 70  ? 0.40968 0.74479 0.59206 -0.06279 -0.18453 -0.00710 64  GLN A OE1 
444  N NE2 . GLN A 70  ? 0.46436 0.72839 0.61711 -0.06410 -0.14712 -0.00120 64  GLN A NE2 
445  N N   . ARG A 71  ? 0.36090 0.56974 0.30570 -0.13240 -0.08701 0.05808  65  ARG A N   
446  C CA  . ARG A 71  ? 0.36361 0.53652 0.27453 -0.12690 -0.06475 0.05051  65  ARG A CA  
447  C C   . ARG A 71  ? 0.36556 0.51628 0.22012 -0.14252 -0.04374 0.08235  65  ARG A C   
448  O O   . ARG A 71  ? 0.38821 0.53507 0.21295 -0.13503 -0.04575 0.07922  65  ARG A O   
449  C CB  . ARG A 71  ? 0.49922 0.53439 0.36370 -0.10314 0.02838  0.01637  65  ARG A CB  
450  C CG  . ARG A 71  ? 0.57454 0.51595 0.45363 -0.08388 0.06682  -0.00334 65  ARG A CG  
451  C CD  A ARG A 71  ? 0.64161 0.52307 0.52260 -0.07311 0.06124  0.00966  65  ARG A CD  
452  C CD  B ARG A 71  ? 0.56933 0.48796 0.47284 -0.06189 0.09461  -0.01248 65  ARG A CD  
453  N NE  A ARG A 71  ? 0.69327 0.53321 0.56948 -0.05607 0.07609  0.03142  65  ARG A NE  
454  N NE  B ARG A 71  ? 0.52707 0.45568 0.46260 -0.04563 0.09248  -0.02123 65  ARG A NE  
455  C CZ  A ARG A 71  ? 0.71892 0.54448 0.57505 -0.03714 0.10595  0.04208  65  ARG A CZ  
456  C CZ  B ARG A 71  ? 0.49021 0.42134 0.46086 -0.06406 0.06437  -0.06079 65  ARG A CZ  
457  N NH1 A ARG A 71  ? 0.74117 0.54687 0.57952 -0.02238 0.11255  0.04426  65  ARG A NH1 
458  N NH1 B ARG A 71  ? 0.48440 0.41855 0.47779 -0.08242 0.07947  -0.08973 65  ARG A NH1 
459  N NH2 A ARG A 71  ? 0.69827 0.54889 0.56542 -0.04364 0.14303  0.05576  65  ARG A NH2 
460  N NH2 B ARG A 71  ? 0.44925 0.39279 0.42549 -0.08239 0.01920  -0.07024 65  ARG A NH2 
461  N N   . THR A 72  ? 0.34727 0.48559 0.20125 -0.09485 -0.06365 0.10603  66  THR A N   
462  C CA  . THR A 72  ? 0.30326 0.47371 0.26055 -0.08841 -0.10030 0.06719  66  THR A CA  
463  C C   . THR A 72  ? 0.25931 0.48084 0.26010 -0.06061 -0.07732 0.07252  66  THR A C   
464  O O   . THR A 72  ? 0.28751 0.47100 0.20591 -0.05796 -0.04839 0.05324  66  THR A O   
465  C CB  . THR A 72  ? 0.34036 0.44962 0.30788 -0.06626 -0.06174 0.11433  66  THR A CB  
466  O OG1 . THR A 72  ? 0.38111 0.45048 0.32991 -0.07217 -0.04642 0.13180  66  THR A OG1 
467  C CG2 . THR A 72  ? 0.34265 0.42960 0.27567 -0.08614 -0.06881 0.11428  66  THR A CG2 
468  N N   . LEU A 73  ? 0.24229 0.50615 0.24621 -0.05855 -0.09673 0.09340  67  LEU A N   
469  C CA  . LEU A 73  ? 0.26400 0.52218 0.26929 -0.05488 -0.02838 0.11511  67  LEU A CA  
470  C C   . LEU A 73  ? 0.28463 0.55070 0.26396 -0.05908 -0.05137 0.13706  67  LEU A C   
471  O O   . LEU A 73  ? 0.27576 0.53494 0.26746 -0.06491 -0.06006 0.11744  67  LEU A O   
472  C CB  . LEU A 73  ? 0.25554 0.52149 0.29628 -0.02482 -0.01643 0.08157  67  LEU A CB  
473  C CG  . LEU A 73  ? 0.22536 0.52502 0.34143 -0.00725 -0.00156 0.09227  67  LEU A CG  
474  C CD1 . LEU A 73  ? 0.25161 0.50707 0.30836 0.01224  0.01492  0.08218  67  LEU A CD1 
475  C CD2 . LEU A 73  ? 0.22790 0.54867 0.41053 -0.01673 0.03948  0.08181  67  LEU A CD2 
476  N N   . ARG A 74  ? 0.26698 0.56723 0.25430 -0.06043 -0.08427 0.14503  68  ARG A N   
477  C CA  . ARG A 74  ? 0.32253 0.54206 0.23655 -0.10887 -0.10802 0.10966  68  ARG A CA  
478  C C   . ARG A 74  ? 0.37529 0.55113 0.25315 -0.12319 -0.08243 0.11343  68  ARG A C   
479  O O   . ARG A 74  ? 0.37219 0.56139 0.24884 -0.14117 -0.10312 0.13004  68  ARG A O   
480  C CB  . ARG A 74  ? 0.35047 0.55807 0.27706 -0.14278 -0.12051 0.07466  68  ARG A CB  
481  C CG  . ARG A 74  ? 0.37469 0.56432 0.31625 -0.10295 -0.13355 0.02691  68  ARG A CG  
482  C CD  . ARG A 74  ? 0.39213 0.55974 0.30617 -0.05191 -0.17748 0.00337  68  ARG A CD  
483  N NE  . ARG A 74  ? 0.42463 0.56143 0.31128 -0.03396 -0.19564 0.00000  68  ARG A NE  
484  C CZ  . ARG A 74  ? 0.47834 0.57536 0.37243 -0.06155 -0.14683 -0.00893 68  ARG A CZ  
485  N NH1 . ARG A 74  ? 0.49869 0.57107 0.43804 -0.08678 -0.11117 -0.02081 68  ARG A NH1 
486  N NH2 . ARG A 74  ? 0.53459 0.59742 0.36497 -0.06501 -0.06528 -0.00079 68  ARG A NH2 
487  N N   . GLU A 75  ? 0.34110 0.53816 0.23857 -0.13501 -0.11074 0.10759  69  GLU A N   
488  C CA  . GLU A 75  ? 0.33871 0.52822 0.25305 -0.10727 -0.05673 0.08835  69  GLU A CA  
489  C C   . GLU A 75  ? 0.35033 0.49713 0.22747 -0.08357 -0.08294 0.09126  69  GLU A C   
490  O O   . GLU A 75  ? 0.34751 0.47532 0.24940 -0.06645 -0.02315 0.07480  69  GLU A O   
491  C CB  . GLU A 75  ? 0.28087 0.49242 0.25426 -0.08584 -0.02497 0.06203  69  GLU A CB  
492  C CG  . GLU A 75  ? 0.32044 0.51336 0.29005 -0.06869 -0.03006 0.04090  69  GLU A CG  
493  C CD  . GLU A 75  ? 0.36202 0.52473 0.28936 -0.06228 -0.02672 0.00901  69  GLU A CD  
494  O OE1 . GLU A 75  ? 0.42160 0.52784 0.31485 -0.07522 0.00521  0.02551  69  GLU A OE1 
495  O OE2 . GLU A 75  ? 0.37263 0.53577 0.25023 -0.05635 -0.02409 -0.01834 69  GLU A OE2 
496  N N   . ILE A 76  ? 0.34484 0.45415 0.19225 -0.09533 -0.08898 0.10194  70  ILE A N   
497  C CA  . ILE A 76  ? 0.34839 0.47469 0.23409 -0.10682 -0.09331 0.10225  70  ILE A CA  
498  C C   . ILE A 76  ? 0.36865 0.46495 0.24806 -0.10313 -0.08595 0.08905  70  ILE A C   
499  O O   . ILE A 76  ? 0.37402 0.44068 0.27192 -0.08015 -0.12706 0.09762  70  ILE A O   
500  C CB  . ILE A 76  ? 0.29593 0.44785 0.23236 -0.08934 -0.11189 0.11643  70  ILE A CB  
501  C CG1 . ILE A 76  ? 0.35527 0.43485 0.22055 -0.07148 -0.07931 0.14446  70  ILE A CG1 
502  C CG2 . ILE A 76  ? 0.38132 0.47918 0.19762 -0.08709 -0.07585 0.11859  70  ILE A CG2 
503  C CD1 . ILE A 76  ? 0.42626 0.45159 0.22589 -0.08461 -0.09709 0.11668  70  ILE A CD1 
504  N N   . LYS A 77  ? 0.33457 0.45637 0.19324 -0.08415 -0.08538 0.04941  71  LYS A N   
505  C CA  . LYS A 77  ? 0.36123 0.47033 0.23535 -0.04755 -0.02132 0.06704  71  LYS A CA  
506  C C   . LYS A 77  ? 0.35807 0.46909 0.21616 -0.02136 -0.06540 0.05740  71  LYS A C   
507  O O   . LYS A 77  ? 0.39207 0.50024 0.23364 -0.01246 -0.07313 0.04842  71  LYS A O   
508  C CB  . LYS A 77  ? 0.31820 0.48869 0.25549 -0.05966 0.03148  0.05637  71  LYS A CB  
509  C CG  . LYS A 77  ? 0.32856 0.52139 0.34608 -0.02693 0.05322  0.05220  71  LYS A CG  
510  C CD  . LYS A 77  ? 0.32524 0.53042 0.39999 0.00647  0.05894  0.04799  71  LYS A CD  
511  C CE  . LYS A 77  ? 0.38249 0.53361 0.40282 0.06867  0.07278  0.06886  71  LYS A CE  
512  N NZ  . LYS A 77  ? 0.43340 0.53701 0.42537 0.10787  0.09406  0.05858  71  LYS A NZ  
513  N N   . ILE A 78  ? 0.34882 0.43531 0.17087 -0.02036 -0.08768 0.03730  72  ILE A N   
514  C CA  . ILE A 78  ? 0.34778 0.41753 0.18581 -0.03357 -0.10565 0.02367  72  ILE A CA  
515  C C   . ILE A 78  ? 0.36379 0.43223 0.22977 -0.04404 -0.06724 0.07410  72  ILE A C   
516  O O   . ILE A 78  ? 0.40035 0.41796 0.26514 -0.04031 -0.04977 0.08722  72  ILE A O   
517  C CB  . ILE A 78  ? 0.37924 0.38673 0.18677 -0.02506 -0.07977 0.01385  72  ILE A CB  
518  C CG1 . ILE A 78  ? 0.40245 0.35864 0.22440 -0.03285 -0.07035 -0.02335 72  ILE A CG1 
519  C CG2 . ILE A 78  ? 0.40804 0.38691 0.13303 -0.00176 -0.05817 0.04753  72  ILE A CG2 
520  C CD1 . ILE A 78  ? 0.43572 0.36422 0.22497 -0.06731 -0.05586 -0.03637 72  ILE A CD1 
521  N N   . LEU A 79  ? 0.28009 0.45087 0.25428 -0.07329 -0.09095 0.10811  73  LEU A N   
522  C CA  . LEU A 79  ? 0.31127 0.47748 0.31897 -0.05046 -0.06014 0.13177  73  LEU A CA  
523  C C   . LEU A 79  ? 0.35220 0.47384 0.32467 -0.06564 -0.03161 0.12311  73  LEU A C   
524  O O   . LEU A 79  ? 0.36335 0.48856 0.37597 -0.09552 -0.03161 0.10709  73  LEU A O   
525  C CB  . LEU A 79  ? 0.30379 0.46391 0.35148 -0.03775 -0.04245 0.12893  73  LEU A CB  
526  C CG  . LEU A 79  ? 0.34266 0.47616 0.34371 -0.01546 -0.06823 0.15373  73  LEU A CG  
527  C CD1 . LEU A 79  ? 0.35337 0.50185 0.38251 0.01515  -0.04329 0.10212  73  LEU A CD1 
528  C CD2 . LEU A 79  ? 0.35555 0.48370 0.35038 0.01500  -0.04645 0.15890  73  LEU A CD2 
529  N N   . LEU A 80  ? 0.38965 0.45689 0.28489 -0.05151 -0.09118 0.11656  74  LEU A N   
530  C CA  . LEU A 80  ? 0.44894 0.44652 0.34547 -0.08476 -0.08597 0.08805  74  LEU A CA  
531  C C   . LEU A 80  ? 0.42796 0.41425 0.33447 -0.08001 -0.13042 0.05890  74  LEU A C   
532  O O   . LEU A 80  ? 0.51727 0.41274 0.40036 -0.10644 -0.14610 0.03906  74  LEU A O   
533  C CB  . LEU A 80  ? 0.44815 0.47104 0.33349 -0.10887 -0.06748 0.07010  74  LEU A CB  
534  C CG  . LEU A 80  ? 0.42617 0.49981 0.32392 -0.11649 -0.09777 0.08039  74  LEU A CG  
535  C CD1 . LEU A 80  ? 0.45992 0.49505 0.32499 -0.10064 -0.11146 0.10928  74  LEU A CD1 
536  C CD2 . LEU A 80  ? 0.44032 0.52737 0.28450 -0.10624 -0.11044 0.03922  74  LEU A CD2 
537  N N   . ARG A 81  ? 0.36874 0.39919 0.26388 -0.04080 -0.05056 0.02276  75  ARG A N   
538  C CA  . ARG A 81  ? 0.36856 0.39613 0.24070 -0.00889 -0.02622 0.01137  75  ARG A CA  
539  C C   . ARG A 81  ? 0.45265 0.35258 0.23327 -0.04348 0.03410  -0.00123 75  ARG A C   
540  O O   . ARG A 81  ? 0.64638 0.34692 0.26942 -0.01313 0.10380  -0.02099 75  ARG A O   
541  C CB  . ARG A 81  ? 0.36304 0.45296 0.27438 0.02230  -0.03010 -0.01329 75  ARG A CB  
542  C CG  . ARG A 81  ? 0.45401 0.48405 0.31792 0.06902  0.01412  -0.01117 75  ARG A CG  
543  C CD  . ARG A 81  ? 0.48505 0.50709 0.33684 0.09945  0.02707  -0.02175 75  ARG A CD  
544  N NE  . ARG A 81  ? 0.47256 0.50131 0.32480 0.11307  -0.00097 -0.04377 75  ARG A NE  
545  C CZ  . ARG A 81  ? 0.46077 0.47320 0.29758 0.14009  -0.01103 -0.04962 75  ARG A CZ  
546  N NH1 . ARG A 81  ? 0.42494 0.44806 0.28263 0.16064  0.00460  -0.03829 75  ARG A NH1 
547  N NH2 . ARG A 81  ? 0.45767 0.47110 0.27623 0.14002  -0.01931 -0.04091 75  ARG A NH2 
548  N N   . PHE A 82  ? 0.31186 0.32700 0.19269 -0.03617 -0.06268 0.02633  76  PHE A N   
549  C CA  . PHE A 82  ? 0.28741 0.30764 0.20969 -0.02064 -0.02625 -0.00927 76  PHE A CA  
550  C C   . PHE A 82  ? 0.30293 0.29846 0.20439 -0.01788 -0.05928 -0.00766 76  PHE A C   
551  O O   . PHE A 82  ? 0.32756 0.30945 0.23336 0.00910  -0.06283 -0.01447 76  PHE A O   
552  C CB  . PHE A 82  ? 0.29926 0.26085 0.19726 -0.02422 -0.05000 -0.00487 76  PHE A CB  
553  C CG  . PHE A 82  ? 0.28837 0.29203 0.21624 -0.02127 -0.03033 0.02896  76  PHE A CG  
554  C CD1 . PHE A 82  ? 0.24720 0.31374 0.23566 0.00157  -0.04109 0.03064  76  PHE A CD1 
555  C CD2 . PHE A 82  ? 0.29319 0.28933 0.20859 -0.03167 -0.01419 0.01992  76  PHE A CD2 
556  C CE1 . PHE A 82  ? 0.30351 0.30550 0.22417 -0.01696 0.01525  -0.00682 76  PHE A CE1 
557  C CE2 . PHE A 82  ? 0.30669 0.30661 0.18736 -0.01182 -0.01146 0.02353  76  PHE A CE2 
558  C CZ  . PHE A 82  ? 0.32467 0.31144 0.22589 0.00532  0.02167  -0.00312 76  PHE A CZ  
559  N N   . ARG A 83  ? 0.30895 0.29919 0.23315 -0.03534 -0.03282 0.00828  77  ARG A N   
560  C CA  . ARG A 83  ? 0.30772 0.31509 0.22485 -0.06723 -0.05948 0.00127  77  ARG A CA  
561  C C   . ARG A 83  ? 0.34856 0.28690 0.19299 -0.04394 -0.02181 0.01284  77  ARG A C   
562  O O   . ARG A 83  ? 0.40655 0.26410 0.22563 -0.04444 -0.01242 0.02357  77  ARG A O   
563  C CB  A ARG A 83  ? 0.31439 0.31770 0.22280 -0.07207 -0.13205 -0.00320 77  ARG A CB  
564  C CB  B ARG A 83  ? 0.39545 0.36383 0.31447 -0.07292 -0.02235 0.00903  77  ARG A CB  
565  C CG  A ARG A 83  ? 0.31599 0.33649 0.25295 -0.07690 -0.14220 -0.03717 77  ARG A CG  
566  C CG  B ARG A 83  ? 0.51062 0.41571 0.40024 -0.06669 0.04258  0.00861  77  ARG A CG  
567  C CD  A ARG A 83  ? 0.37920 0.35759 0.31295 -0.11265 -0.13737 -0.05175 77  ARG A CD  
568  C CD  B ARG A 83  ? 0.59542 0.44712 0.48231 -0.04971 0.10991  0.00881  77  ARG A CD  
569  N NE  A ARG A 83  ? 0.45592 0.39992 0.44271 -0.08754 -0.06208 -0.03290 77  ARG A NE  
570  N NE  B ARG A 83  ? 0.62887 0.44952 0.52566 -0.04145 0.14208  0.00310  77  ARG A NE  
571  C CZ  A ARG A 83  ? 0.55508 0.42279 0.55283 -0.08717 0.04094  -0.01706 77  ARG A CZ  
572  C CZ  B ARG A 83  ? 0.64633 0.44510 0.50125 -0.01967 0.15235  -0.00423 77  ARG A CZ  
573  N NH1 A ARG A 83  ? 0.59706 0.42964 0.59935 -0.07830 0.09249  -0.01632 77  ARG A NH1 
574  N NH1 B ARG A 83  ? 0.66527 0.43855 0.51720 0.00816  0.15939  -0.01639 77  ARG A NH1 
575  N NH2 A ARG A 83  ? 0.60443 0.43710 0.59758 -0.09163 0.07100  -0.00330 77  ARG A NH2 
576  N NH2 B ARG A 83  ? 0.61441 0.43723 0.45405 -0.02679 0.12161  0.01315  77  ARG A NH2 
577  N N   . HIS A 84  ? 0.26646 0.28158 0.18144 -0.05062 -0.04352 -0.00417 78  HIS A N   
578  C CA  . HIS A 84  ? 0.21319 0.27540 0.18032 -0.02418 -0.03986 0.00112  78  HIS A CA  
579  C C   . HIS A 84  ? 0.21626 0.26361 0.21538 -0.00079 -0.04770 0.02477  78  HIS A C   
580  O O   . HIS A 84  ? 0.25725 0.21307 0.24870 -0.01409 -0.04881 0.01656  78  HIS A O   
581  C CB  . HIS A 84  ? 0.20583 0.29000 0.17540 -0.05646 -0.05437 0.01834  78  HIS A CB  
582  C CG  . HIS A 84  ? 0.20961 0.26977 0.16389 -0.01279 -0.04582 0.00578  78  HIS A CG  
583  N ND1 . HIS A 84  ? 0.21463 0.25978 0.18815 -0.01847 -0.00084 0.00913  78  HIS A ND1 
584  C CD2 . HIS A 84  ? 0.21265 0.26252 0.18365 -0.00648 -0.01984 0.02828  78  HIS A CD2 
585  C CE1 . HIS A 84  ? 0.22441 0.24500 0.19600 0.00006  0.00621  0.01111  78  HIS A CE1 
586  N NE2 . HIS A 84  ? 0.19065 0.22413 0.20287 0.01231  -0.01465 0.00907  78  HIS A NE2 
587  N N   . GLU A 85  ? 0.22559 0.29306 0.23112 -0.02205 -0.00937 -0.00891 79  GLU A N   
588  C CA  . GLU A 85  ? 0.20268 0.29651 0.24630 -0.04541 -0.02344 0.02180  79  GLU A CA  
589  C C   . GLU A 85  ? 0.19599 0.26688 0.23323 -0.01281 -0.04415 0.03756  79  GLU A C   
590  O O   . GLU A 85  ? 0.19966 0.27950 0.28913 -0.03915 -0.05782 0.02400  79  GLU A O   
591  C CB  . GLU A 85  ? 0.21190 0.32072 0.29663 -0.09637 -0.04012 0.04853  79  GLU A CB  
592  C CG  . GLU A 85  ? 0.22386 0.41287 0.37092 -0.10348 -0.02428 0.09654  79  GLU A CG  
593  C CD  . GLU A 85  ? 0.27876 0.50701 0.39889 -0.14439 -0.03905 0.10572  79  GLU A CD  
594  O OE1 . GLU A 85  ? 0.23974 0.54103 0.35881 -0.12686 -0.10653 0.14068  79  GLU A OE1 
595  O OE2 . GLU A 85  ? 0.31232 0.53853 0.41201 -0.16946 -0.05177 0.08585  79  GLU A OE2 
596  N N   . ASN A 86  ? 0.14637 0.26942 0.21881 -0.02396 -0.04601 0.02403  80  ASN A N   
597  C CA  . ASN A 86  ? 0.20403 0.26655 0.18051 -0.01825 -0.01989 0.05204  80  ASN A CA  
598  C C   . ASN A 86  ? 0.15705 0.27077 0.18314 0.00809  -0.01443 0.03813  80  ASN A C   
599  O O   . ASN A 86  ? 0.15885 0.26429 0.20029 -0.01357 -0.02593 0.03441  80  ASN A O   
600  C CB  . ASN A 86  ? 0.17770 0.24653 0.17990 -0.00550 0.00763  0.07970  80  ASN A CB  
601  C CG  . ASN A 86  ? 0.19724 0.24822 0.20364 0.01305  0.00953  0.02391  80  ASN A CG  
602  O OD1 . ASN A 86  ? 0.20510 0.24233 0.27164 -0.00484 0.00404  0.02727  80  ASN A OD1 
603  N ND2 . ASN A 86  ? 0.16546 0.29244 0.21562 0.02846  0.01001  0.01130  80  ASN A ND2 
604  N N   . ILE A 87  ? 0.19971 0.27911 0.16396 0.02057  -0.02213 0.04842  81  ILE A N   
605  C CA  . ILE A 87  ? 0.21203 0.25658 0.18024 0.02678  0.00088  0.06193  81  ILE A CA  
606  C C   . ILE A 87  ? 0.22466 0.24752 0.18393 0.02374  -0.04893 0.03828  81  ILE A C   
607  O O   . ILE A 87  ? 0.25046 0.30232 0.17583 -0.02995 -0.08082 0.02886  81  ILE A O   
608  C CB  . ILE A 87  ? 0.20976 0.24688 0.17226 0.04068  -0.02909 0.07040  81  ILE A CB  
609  C CG1 . ILE A 87  ? 0.23334 0.23012 0.19748 0.05561  -0.05867 0.00411  81  ILE A CG1 
610  C CG2 . ILE A 87  ? 0.24544 0.27873 0.21321 -0.00135 0.03348  0.06740  81  ILE A CG2 
611  C CD1 . ILE A 87  ? 0.24444 0.22569 0.25384 0.07200  -0.03049 -0.05022 81  ILE A CD1 
612  N N   . ILE A 88  ? 0.27143 0.26322 0.19314 0.05704  -0.03094 0.06154  82  ILE A N   
613  C CA  . ILE A 88  ? 0.31517 0.30629 0.21597 0.04167  -0.08039 0.07849  82  ILE A CA  
614  C C   . ILE A 88  ? 0.31772 0.37333 0.19954 0.01068  -0.07390 0.09213  82  ILE A C   
615  O O   . ILE A 88  ? 0.34246 0.50604 0.21694 0.00128  -0.03225 0.04616  82  ILE A O   
616  C CB  . ILE A 88  ? 0.34737 0.34208 0.30110 0.00708  -0.13746 0.09756  82  ILE A CB  
617  C CG1 . ILE A 88  ? 0.38907 0.35547 0.35069 0.05717  -0.12476 0.10937  82  ILE A CG1 
618  C CG2 . ILE A 88  ? 0.36641 0.36974 0.35805 -0.04981 -0.17176 0.08903  82  ILE A CG2 
619  C CD1 . ILE A 88  ? 0.41327 0.40824 0.42287 0.04486  -0.09649 0.08350  82  ILE A CD1 
620  N N   . GLY A 89  ? 0.33236 0.33220 0.17917 0.01389  -0.05755 0.06059  83  GLY A N   
621  C CA  . GLY A 89  ? 0.41441 0.34917 0.14367 0.04434  -0.03185 0.06042  83  GLY A CA  
622  C C   . GLY A 89  ? 0.43532 0.38365 0.17970 0.04254  -0.02953 0.06492  83  GLY A C   
623  O O   . GLY A 89  ? 0.58353 0.41824 0.20842 0.09927  -0.00246 0.09886  83  GLY A O   
624  N N   . ILE A 90  ? 0.33103 0.40142 0.18940 -0.00839 -0.05799 0.05031  84  ILE A N   
625  C CA  . ILE A 90  ? 0.35723 0.42159 0.20632 -0.04869 -0.05815 0.05489  84  ILE A CA  
626  C C   . ILE A 90  ? 0.37947 0.45656 0.24413 -0.08468 -0.05205 0.02556  84  ILE A C   
627  O O   . ILE A 90  ? 0.41685 0.47481 0.27049 -0.05469 -0.07100 -0.02286 84  ILE A O   
628  C CB  . ILE A 90  ? 0.37380 0.41741 0.19591 -0.03295 -0.04524 0.06285  84  ILE A CB  
629  C CG1 . ILE A 90  ? 0.33747 0.44167 0.20407 -0.06420 -0.05627 0.07150  84  ILE A CG1 
630  C CG2 . ILE A 90  ? 0.41262 0.39604 0.22188 0.01661  -0.04828 0.08974  84  ILE A CG2 
631  C CD1 . ILE A 90  ? 0.38094 0.45224 0.23102 -0.07307 -0.02032 0.06187  84  ILE A CD1 
632  N N   . ASN A 91  ? 0.36230 0.48068 0.22351 -0.12248 -0.05306 0.04669  85  ASN A N   
633  C CA  . ASN A 91  ? 0.36644 0.51661 0.22251 -0.14970 -0.02714 0.03846  85  ASN A CA  
634  C C   . ASN A 91  ? 0.30386 0.48013 0.22727 -0.14278 -0.04775 0.05572  85  ASN A C   
635  O O   . ASN A 91  ? 0.37056 0.48357 0.26644 -0.14343 -0.01420 -0.01129 85  ASN A O   
636  C CB  . ASN A 91  ? 0.35552 0.55831 0.23462 -0.18777 0.06495  0.00897  85  ASN A CB  
637  C CG  . ASN A 91  ? 0.46722 0.59563 0.30671 -0.18627 0.13117  -0.02057 85  ASN A CG  
638  O OD1 . ASN A 91  ? 0.51930 0.62070 0.35249 -0.16944 0.14968  0.02127  85  ASN A OD1 
639  N ND2 . ASN A 91  ? 0.45251 0.58465 0.30168 -0.22133 0.15265  -0.10556 85  ASN A ND2 
640  N N   . ASP A 92  ? 0.29355 0.46330 0.23995 -0.11005 -0.00056 0.09300  86  ASP A N   
641  C CA  . ASP A 92  ? 0.24626 0.48703 0.23826 -0.10673 -0.04182 0.05090  86  ASP A CA  
642  C C   . ASP A 92  ? 0.21957 0.44472 0.25042 -0.08432 -0.05232 0.02542  86  ASP A C   
643  O O   . ASP A 92  ? 0.26734 0.41697 0.25855 -0.04806 -0.07058 0.01230  86  ASP A O   
644  C CB  . ASP A 92  ? 0.24297 0.57005 0.23190 -0.06879 -0.06401 0.05099  86  ASP A CB  
645  C CG  . ASP A 92  ? 0.29170 0.64533 0.28845 -0.02885 -0.03856 0.05986  86  ASP A CG  
646  O OD1 . ASP A 92  ? 0.31005 0.66081 0.29311 -0.03831 -0.03111 0.01520  86  ASP A OD1 
647  O OD2 . ASP A 92  ? 0.32776 0.66910 0.30934 -0.01002 -0.03222 0.09343  86  ASP A OD2 
648  N N   . ILE A 93  ? 0.23428 0.44342 0.25705 -0.03463 -0.00956 0.04858  87  ILE A N   
649  C CA  . ILE A 93  ? 0.26560 0.43993 0.21706 -0.02155 -0.03550 0.07137  87  ILE A CA  
650  C C   . ILE A 93  ? 0.28184 0.45370 0.20651 -0.03708 -0.02475 0.04875  87  ILE A C   
651  O O   . ILE A 93  ? 0.35467 0.45695 0.22346 -0.03125 0.00400  0.01463  87  ILE A O   
652  C CB  . ILE A 93  ? 0.24961 0.43064 0.25490 -0.05279 0.00003  0.04151  87  ILE A CB  
653  C CG1 . ILE A 93  ? 0.23832 0.43638 0.26413 -0.01444 -0.05224 0.05650  87  ILE A CG1 
654  C CG2 . ILE A 93  ? 0.25251 0.41525 0.28306 -0.06063 0.02616  0.02081  87  ILE A CG2 
655  C CD1 . ILE A 93  ? 0.23730 0.45021 0.27359 -0.00975 -0.02913 0.03438  87  ILE A CD1 
656  N N   . ILE A 94  ? 0.22338 0.45359 0.21488 -0.01996 -0.03956 0.05044  88  ILE A N   
657  C CA  . ILE A 94  ? 0.24174 0.46204 0.24273 -0.01994 -0.03746 0.04607  88  ILE A CA  
658  C C   . ILE A 94  ? 0.28487 0.45887 0.19363 -0.03525 -0.02572 0.01870  88  ILE A C   
659  O O   . ILE A 94  ? 0.32981 0.48250 0.20760 -0.03728 -0.00204 0.03160  88  ILE A O   
660  C CB  . ILE A 94  ? 0.28092 0.49673 0.41216 -0.02781 0.01118  0.05739  88  ILE A CB  
661  C CG1 . ILE A 94  ? 0.23290 0.52396 0.48955 0.03166  0.06346  0.11003  88  ILE A CG1 
662  C CG2 . ILE A 94  ? 0.34219 0.48257 0.45232 -0.03031 0.00423  0.05319  88  ILE A CG2 
663  C CD1 . ILE A 94  ? 0.23507 0.56557 0.51538 0.02767  0.11395  0.11159  88  ILE A CD1 
664  N N   . ARG A 95  ? 0.27694 0.41700 0.20088 -0.02347 -0.01434 0.04006  89  ARG A N   
665  C CA  . ARG A 95  ? 0.27127 0.36442 0.20534 -0.02296 -0.02030 0.03305  89  ARG A CA  
666  C C   . ARG A 95  ? 0.30973 0.35860 0.19846 -0.01306 -0.03621 0.04816  89  ARG A C   
667  O O   . ARG A 95  ? 0.34882 0.35855 0.21461 -0.00474 -0.04479 0.03561  89  ARG A O   
668  C CB  . ARG A 95  ? 0.32998 0.30188 0.26902 0.02542  0.01653  0.03135  89  ARG A CB  
669  C CG  . ARG A 95  ? 0.40468 0.29984 0.31161 -0.02759 0.07163  0.01054  89  ARG A CG  
670  C CD  . ARG A 95  ? 0.41170 0.28236 0.27774 -0.02049 0.03802  -0.00904 89  ARG A CD  
671  N NE  . ARG A 95  ? 0.34801 0.28626 0.24061 -0.02100 -0.01993 -0.03015 89  ARG A NE  
672  C CZ  . ARG A 95  ? 0.34011 0.32833 0.23909 -0.00241 -0.03066 0.01455  89  ARG A CZ  
673  N NH1 . ARG A 95  ? 0.31400 0.35712 0.22308 0.00661  -0.08597 0.05193  89  ARG A NH1 
674  N NH2 . ARG A 95  ? 0.32488 0.35502 0.24042 -0.00151 -0.05818 0.01013  89  ARG A NH2 
675  N N   . ALA A 96  ? 0.33078 0.35692 0.18109 -0.03898 -0.02344 0.06083  90  ALA A N   
676  C CA  . ALA A 96  ? 0.35479 0.34212 0.19829 -0.07888 -0.01530 0.05918  90  ALA A CA  
677  C C   . ALA A 96  ? 0.33597 0.35211 0.21797 -0.01315 -0.07872 0.05403  90  ALA A C   
678  O O   . ALA A 96  ? 0.33882 0.36036 0.23117 -0.01377 -0.08499 0.06300  90  ALA A O   
679  C CB  . ALA A 96  ? 0.35148 0.28870 0.17644 -0.13873 -0.00519 0.05694  90  ALA A CB  
680  N N   . PRO A 97  ? 0.33634 0.34780 0.21998 0.00373  -0.06969 0.02254  91  PRO A N   
681  C CA  . PRO A 97  ? 0.31466 0.35484 0.26864 -0.01359 -0.07754 0.02624  91  PRO A CA  
682  C C   . PRO A 97  ? 0.30185 0.34082 0.24723 0.03231  -0.07161 0.01899  91  PRO A C   
683  O O   . PRO A 97  ? 0.31292 0.32579 0.29228 0.06848  -0.03497 0.01340  91  PRO A O   
684  C CB  . PRO A 97  ? 0.31609 0.36355 0.25614 -0.00746 -0.11454 0.05542  91  PRO A CB  
685  C CG  . PRO A 97  ? 0.38869 0.35140 0.24603 -0.02541 -0.08008 0.03178  91  PRO A CG  
686  C CD  . PRO A 97  ? 0.35358 0.34567 0.21118 0.00586  -0.08036 -0.00090 91  PRO A CD  
687  N N   . THR A 98  ? 0.29219 0.37359 0.24812 0.01672  -0.05876 0.02866  92  THR A N   
688  C CA  . THR A 98  ? 0.29764 0.36319 0.20321 -0.01486 -0.03932 0.01102  92  THR A CA  
689  C C   . THR A 98  ? 0.30882 0.36717 0.22828 0.00716  -0.01034 0.01630  92  THR A C   
690  O O   . THR A 98  ? 0.33691 0.35451 0.24356 0.01596  0.02963  -0.00688 92  THR A O   
691  C CB  . THR A 98  ? 0.46061 0.32329 0.19539 -0.06226 -0.02340 0.03900  92  THR A CB  
692  O OG1 . THR A 98  ? 0.51309 0.28872 0.21081 -0.08549 -0.04765 0.02756  92  THR A OG1 
693  C CG2 . THR A 98  ? 0.48961 0.34643 0.18619 -0.05658 -0.04927 0.04958  92  THR A CG2 
694  N N   . ILE A 99  ? 0.32315 0.39864 0.26371 0.02339  0.01046  0.07307  93  ILE A N   
695  C CA  . ILE A 99  ? 0.34793 0.45984 0.30867 -0.01013 -0.00248 0.04963  93  ILE A CA  
696  C C   . ILE A 99  ? 0.34736 0.51060 0.30737 -0.03964 -0.01702 0.05878  93  ILE A C   
697  O O   . ILE A 99  ? 0.33150 0.54303 0.32519 -0.07999 -0.06475 0.06153  93  ILE A O   
698  C CB  A ILE A 99  ? 0.38438 0.44740 0.31667 0.01093  0.01710  -0.00798 93  ILE A CB  
699  C CB  B ILE A 99  ? 0.31459 0.46270 0.32384 -0.02600 -0.01711 0.06965  93  ILE A CB  
700  C CG1 A ILE A 99  ? 0.41048 0.44227 0.34319 0.02905  -0.00130 -0.04031 93  ILE A CG1 
701  C CG1 B ILE A 99  ? 0.31023 0.47101 0.32616 -0.01027 -0.07364 0.11755  93  ILE A CG1 
702  C CG2 A ILE A 99  ? 0.40468 0.44518 0.29376 0.00607  0.04964  -0.01783 93  ILE A CG2 
703  C CG2 B ILE A 99  ? 0.30698 0.46337 0.31760 -0.05071 0.01020  0.06789  93  ILE A CG2 
704  C CD1 A ILE A 99  ? 0.43194 0.43570 0.36291 0.03283  -0.00820 -0.06441 93  ILE A CD1 
705  C CD1 B ILE A 99  ? 0.38796 0.48335 0.40486 -0.02401 -0.02251 0.10352  93  ILE A CD1 
706  N N   . GLU A 100 ? 0.33433 0.52358 0.27380 -0.02956 -0.02315 0.08312  94  GLU A N   
707  C CA  . GLU A 100 ? 0.33637 0.51028 0.27063 -0.03824 -0.00527 0.05992  94  GLU A CA  
708  C C   . GLU A 100 ? 0.32380 0.46050 0.30649 -0.06954 -0.03527 0.06263  94  GLU A C   
709  O O   . GLU A 100 ? 0.38994 0.46838 0.37111 -0.11072 0.00220  0.07277  94  GLU A O   
710  C CB  . GLU A 100 ? 0.31616 0.53860 0.23366 -0.02173 0.04064  0.02681  94  GLU A CB  
711  C CG  . GLU A 100 ? 0.38730 0.57109 0.28230 0.00235  0.07913  -0.00417 94  GLU A CG  
712  C CD  . GLU A 100 ? 0.41166 0.59781 0.30000 0.03079  0.06594  -0.06006 94  GLU A CD  
713  O OE1 . GLU A 100 ? 0.45672 0.59141 0.27074 0.03555  0.06903  -0.06509 94  GLU A OE1 
714  O OE2 . GLU A 100 ? 0.40194 0.64128 0.35439 0.04810  0.05907  -0.04503 94  GLU A OE2 
715  N N   . GLN A 101 ? 0.27548 0.41826 0.26988 -0.02347 -0.04207 0.08953  95  GLN A N   
716  C CA  . GLN A 101 ? 0.29556 0.36409 0.24493 -0.01718 -0.08941 0.07213  95  GLN A CA  
717  C C   . GLN A 101 ? 0.31297 0.35095 0.22050 -0.02774 -0.05423 0.06174  95  GLN A C   
718  O O   . GLN A 101 ? 0.39036 0.32662 0.25390 -0.03081 -0.04475 0.06142  95  GLN A O   
719  C CB  . GLN A 101 ? 0.32948 0.33402 0.21423 -0.01532 -0.10841 0.05923  95  GLN A CB  
720  C CG  . GLN A 101 ? 0.36419 0.33701 0.21472 -0.02244 -0.11133 0.04365  95  GLN A CG  
721  C CD  . GLN A 101 ? 0.40031 0.32112 0.24471 -0.03411 -0.10150 -0.01020 95  GLN A CD  
722  O OE1 . GLN A 101 ? 0.39819 0.31563 0.27575 -0.03498 -0.09706 -0.02657 95  GLN A OE1 
723  N NE2 . GLN A 101 ? 0.43629 0.32210 0.23604 -0.01287 -0.09335 0.00512  95  GLN A NE2 
724  N N   . MET A 102 ? 0.32975 0.36885 0.24540 -0.01822 -0.03342 0.05246  96  MET A N   
725  C CA  . MET A 102 ? 0.34429 0.39064 0.20458 -0.03235 -0.02200 0.04692  96  MET A CA  
726  C C   . MET A 102 ? 0.35084 0.41053 0.25321 -0.11954 -0.04163 0.02191  96  MET A C   
727  O O   . MET A 102 ? 0.32817 0.45314 0.31654 -0.14955 -0.03574 -0.00792 96  MET A O   
728  C CB  . MET A 102 ? 0.33945 0.39231 0.18992 -0.01398 -0.02456 0.05876  96  MET A CB  
729  C CG  . MET A 102 ? 0.34875 0.37403 0.17943 -0.04627 -0.04361 0.08174  96  MET A CG  
730  S SD  . MET A 102 ? 0.34177 0.42172 0.24165 -0.05564 -0.03286 0.06056  96  MET A SD  
731  C CE  . MET A 102 ? 0.28215 0.42247 0.26055 -0.01372 0.01255  0.00431  96  MET A CE  
732  N N   . LYS A 103 ? 0.39810 0.39917 0.22386 -0.13346 -0.03833 0.04962  97  LYS A N   
733  C CA  . LYS A 103 ? 0.48766 0.38956 0.23163 -0.10853 0.00478  0.04537  97  LYS A CA  
734  C C   . LYS A 103 ? 0.47227 0.43570 0.25698 -0.11347 0.01702  -0.01522 97  LYS A C   
735  O O   . LYS A 103 ? 0.51027 0.47281 0.33801 -0.06906 0.04315  -0.04806 97  LYS A O   
736  C CB  . LYS A 103 ? 0.55306 0.36102 0.26852 -0.07593 0.03236  0.07852  97  LYS A CB  
737  C CG  . LYS A 103 ? 0.59301 0.37332 0.34739 -0.06629 0.05949  0.06835  97  LYS A CG  
738  C CD  . LYS A 103 ? 0.62656 0.39691 0.39967 -0.05568 0.10351  0.07387  97  LYS A CD  
739  C CE  . LYS A 103 ? 0.64481 0.42805 0.43462 -0.06843 0.13712  0.07162  97  LYS A CE  
740  N NZ  . LYS A 103 ? 0.66766 0.45045 0.46063 -0.07851 0.15139  0.07282  97  LYS A NZ  
741  N N   . ASP A 104 ? 0.52252 0.44018 0.28751 -0.15554 0.07043  -0.00049 98  ASP A N   
742  C CA  . ASP A 104 ? 0.50643 0.45275 0.29066 -0.15239 0.10867  0.02497  98  ASP A CA  
743  C C   . ASP A 104 ? 0.45405 0.44942 0.24781 -0.14513 0.01583  0.03303  98  ASP A C   
744  O O   . ASP A 104 ? 0.49107 0.45122 0.20656 -0.13015 -0.04775 0.03866  98  ASP A O   
745  C CB  . ASP A 104 ? 0.51572 0.47373 0.37073 -0.12560 0.15918  0.03165  98  ASP A CB  
746  C CG  . ASP A 104 ? 0.53657 0.48098 0.39677 -0.08397 0.11569  0.03097  98  ASP A CG  
747  O OD1 . ASP A 104 ? 0.52245 0.47342 0.39668 -0.07645 0.07229  0.02170  98  ASP A OD1 
748  O OD2 . ASP A 104 ? 0.53531 0.49896 0.42935 -0.06969 0.09615  0.02923  98  ASP A OD2 
749  N N   . VAL A 105 ? 0.37986 0.45280 0.23860 -0.13438 -0.02784 0.04406  99  VAL A N   
750  C CA  . VAL A 105 ? 0.36036 0.44370 0.27097 -0.08361 0.00534  0.04755  99  VAL A CA  
751  C C   . VAL A 105 ? 0.32859 0.45177 0.24751 -0.09365 0.00523  0.03325  99  VAL A C   
752  O O   . VAL A 105 ? 0.36904 0.47952 0.26211 -0.10962 -0.03060 0.00995  99  VAL A O   
753  C CB  . VAL A 105 ? 0.38981 0.45929 0.38314 -0.04706 0.05852  0.03246  99  VAL A CB  
754  C CG1 . VAL A 105 ? 0.40953 0.47521 0.41022 -0.00966 0.03759  0.01639  99  VAL A CG1 
755  C CG2 . VAL A 105 ? 0.38042 0.46505 0.42123 -0.03229 0.10295  0.03612  99  VAL A CG2 
756  N N   . TYR A 106 ? 0.31994 0.43445 0.22239 -0.06251 0.03985  0.01324  100 TYR A N   
757  C CA  . TYR A 106 ? 0.33463 0.41117 0.20682 -0.02696 0.03163  0.02385  100 TYR A CA  
758  C C   . TYR A 106 ? 0.31621 0.40855 0.22733 -0.03925 0.03002  0.00108  100 TYR A C   
759  O O   . TYR A 106 ? 0.37070 0.39492 0.23786 -0.07756 0.00160  -0.02341 100 TYR A O   
760  C CB  . TYR A 106 ? 0.33730 0.40544 0.25923 -0.02081 -0.03893 0.06098  100 TYR A CB  
761  C CG  . TYR A 106 ? 0.38750 0.41040 0.27927 -0.04599 -0.01476 0.10689  100 TYR A CG  
762  C CD1 . TYR A 106 ? 0.39453 0.42140 0.27662 -0.04138 -0.03917 0.11888  100 TYR A CD1 
763  C CD2 . TYR A 106 ? 0.40627 0.42117 0.30233 -0.05863 -0.03414 0.12020  100 TYR A CD2 
764  C CE1 . TYR A 106 ? 0.42795 0.43481 0.29760 -0.05667 -0.02416 0.14162  100 TYR A CE1 
765  C CE2 . TYR A 106 ? 0.42910 0.44389 0.32498 -0.06860 -0.02272 0.13205  100 TYR A CE2 
766  C CZ  . TYR A 106 ? 0.48467 0.45875 0.36111 -0.04040 0.02496  0.16463  100 TYR A CZ  
767  O OH  . TYR A 106 ? 0.56128 0.49717 0.42908 -0.01689 0.07566  0.19677  100 TYR A OH  
768  N N   . ILE A 107 ? 0.24425 0.42824 0.23011 -0.04307 0.01832  0.01038  101 ILE A N   
769  C CA  . ILE A 107 ? 0.20117 0.44917 0.27557 -0.02646 -0.00332 0.04375  101 ILE A CA  
770  C C   . ILE A 107 ? 0.17687 0.43731 0.21932 -0.02708 -0.04941 0.00025  101 ILE A C   
771  O O   . ILE A 107 ? 0.23508 0.43860 0.24819 -0.04587 0.02419  -0.02066 101 ILE A O   
772  C CB  . ILE A 107 ? 0.17871 0.49859 0.36986 -0.01777 -0.00961 0.07753  101 ILE A CB  
773  C CG1 . ILE A 107 ? 0.17623 0.54529 0.41934 -0.01261 -0.09043 0.06914  101 ILE A CG1 
774  C CG2 . ILE A 107 ? 0.26882 0.48938 0.33662 -0.04612 -0.01056 0.09265  101 ILE A CG2 
775  C CD1 . ILE A 107 ? 0.23735 0.59419 0.49341 -0.01506 -0.02945 0.03925  101 ILE A CD1 
776  N N   . VAL A 108 ? 0.17117 0.44362 0.20987 -0.00202 -0.02291 0.03114  102 VAL A N   
777  C CA  . VAL A 108 ? 0.20375 0.44432 0.18233 -0.03493 -0.02761 0.04685  102 VAL A CA  
778  C C   . VAL A 108 ? 0.24886 0.43095 0.18002 -0.01661 -0.03354 0.06267  102 VAL A C   
779  O O   . VAL A 108 ? 0.28111 0.44239 0.22321 -0.03702 -0.07800 0.05331  102 VAL A O   
780  C CB  . VAL A 108 ? 0.23854 0.46892 0.17836 -0.05446 0.01387  0.06408  102 VAL A CB  
781  C CG1 . VAL A 108 ? 0.19946 0.47633 0.21928 -0.02404 -0.03486 0.06407  102 VAL A CG1 
782  C CG2 . VAL A 108 ? 0.28100 0.49083 0.20687 -0.01390 -0.01618 0.12131  102 VAL A CG2 
783  N N   . GLN A 109 ? 0.27183 0.42880 0.17617 0.00742  -0.01033 0.05811  103 GLN A N   
784  C CA  A GLN A 109 ? 0.22690 0.43072 0.16786 0.00419  -0.04609 0.08768  103 GLN A CA  
785  C CA  B GLN A 109 ? 0.24634 0.42744 0.19647 0.01110  -0.01385 0.07260  103 GLN A CA  
786  C C   . GLN A 109 ? 0.26203 0.44205 0.20190 0.01108  -0.00060 0.07503  103 GLN A C   
787  O O   . GLN A 109 ? 0.25409 0.46057 0.22169 0.02382  0.00844  0.05941  103 GLN A O   
788  C CB  A GLN A 109 ? 0.20623 0.43253 0.22338 0.02955  -0.05111 0.09057  103 GLN A CB  
789  C CB  B GLN A 109 ? 0.22125 0.41272 0.24207 0.02868  -0.01301 0.07740  103 GLN A CB  
790  C CG  A GLN A 109 ? 0.22075 0.41723 0.21632 0.04248  -0.08132 0.07067  103 GLN A CG  
791  C CG  B GLN A 109 ? 0.20638 0.38922 0.26378 0.03988  -0.02738 0.07391  103 GLN A CG  
792  C CD  A GLN A 109 ? 0.28476 0.39821 0.28787 0.06644  -0.04287 0.02921  103 GLN A CD  
793  C CD  B GLN A 109 ? 0.19873 0.37288 0.28794 0.05448  -0.03698 0.09753  103 GLN A CD  
794  O OE1 A GLN A 109 ? 0.31784 0.38070 0.32452 0.04845  -0.10048 0.02532  103 GLN A OE1 
795  O OE1 B GLN A 109 ? 0.23249 0.37974 0.29156 0.06576  -0.04716 0.10529  103 GLN A OE1 
796  N NE2 A GLN A 109 ? 0.28266 0.40012 0.29450 0.08844  0.00997  -0.01767 103 GLN A NE2 
797  N NE2 B GLN A 109 ? 0.16834 0.33025 0.25789 0.05387  -0.04972 0.10658  103 GLN A NE2 
798  N N   . ASP A 110 ? 0.26273 0.44520 0.22617 0.01106  0.07623  0.06813  104 ASP A N   
799  C CA  . ASP A 110 ? 0.33138 0.45555 0.24444 0.00133  0.06385  0.09751  104 ASP A CA  
800  C C   . ASP A 110 ? 0.27554 0.48802 0.27556 0.01443  0.04074  0.07567  104 ASP A C   
801  O O   . ASP A 110 ? 0.27482 0.48766 0.25638 -0.00657 -0.04533 0.04398  104 ASP A O   
802  C CB  . ASP A 110 ? 0.43424 0.45456 0.24569 -0.02960 0.07540  0.09392  104 ASP A CB  
803  C CG  . ASP A 110 ? 0.56598 0.48528 0.29332 -0.01612 0.05848  0.11013  104 ASP A CG  
804  O OD1 . ASP A 110 ? 0.60044 0.51310 0.30385 -0.00032 0.10321  0.08757  104 ASP A OD1 
805  O OD2 . ASP A 110 ? 0.56508 0.47533 0.31937 -0.02541 0.00458  0.12565  104 ASP A OD2 
806  N N   . LEU A 111 ? 0.27183 0.51798 0.27369 0.04440  -0.00176 0.07533  105 LEU A N   
807  C CA  . LEU A 111 ? 0.21397 0.53590 0.27466 0.05905  -0.04262 0.07002  105 LEU A CA  
808  C C   . LEU A 111 ? 0.23367 0.51844 0.27952 -0.01198 -0.05891 0.03176  105 LEU A C   
809  O O   . LEU A 111 ? 0.26084 0.52428 0.29391 -0.05328 -0.00978 0.03481  105 LEU A O   
810  C CB  . LEU A 111 ? 0.24312 0.55325 0.28404 0.11788  -0.04697 0.09874  105 LEU A CB  
811  C CG  . LEU A 111 ? 0.23359 0.59683 0.35498 0.14725  0.02073  0.09913  105 LEU A CG  
812  C CD1 . LEU A 111 ? 0.23400 0.59493 0.33606 0.12885  0.05137  0.10592  105 LEU A CD1 
813  C CD2 . LEU A 111 ? 0.23882 0.62475 0.38349 0.16074  0.02880  0.08556  105 LEU A CD2 
814  N N   . MET A 112 ? 0.24020 0.47358 0.22491 0.01783  -0.06282 0.02221  106 MET A N   
815  C CA  . MET A 112 ? 0.18604 0.42782 0.24202 0.05518  -0.06145 0.04995  106 MET A CA  
816  C C   . MET A 112 ? 0.24979 0.42384 0.29409 0.05833  0.02235  0.04802  106 MET A C   
817  O O   . MET A 112 ? 0.32711 0.43544 0.31536 0.09611  0.03857  0.06534  106 MET A O   
818  C CB  . MET A 112 ? 0.16064 0.41547 0.26299 0.06943  -0.00077 0.05494  106 MET A CB  
819  C CG  . MET A 112 ? 0.16790 0.40429 0.29924 0.04022  0.01198  0.03754  106 MET A CG  
820  S SD  . MET A 112 ? 0.23664 0.40153 0.32560 0.03145  -0.00320 0.02159  106 MET A SD  
821  C CE  . MET A 112 ? 0.23552 0.39256 0.33862 0.04573  -0.08720 0.00722  106 MET A CE  
822  N N   . GLU A 113 ? 0.25464 0.43673 0.25572 0.06116  -0.01381 0.01372  107 GLU A N   
823  C CA  . GLU A 113 ? 0.23874 0.44271 0.29382 0.09345  0.01295  0.01243  107 GLU A CA  
824  C C   . GLU A 113 ? 0.23021 0.42424 0.32734 0.09197  -0.00416 0.00671  107 GLU A C   
825  O O   . GLU A 113 ? 0.24522 0.43147 0.35292 0.08725  -0.00684 -0.02322 107 GLU A O   
826  C CB  . GLU A 113 ? 0.22294 0.47906 0.25931 0.10548  0.07053  0.02380  107 GLU A CB  
827  C CG  . GLU A 113 ? 0.17564 0.53804 0.30382 0.05205  0.02413  0.03285  107 GLU A CG  
828  C CD  . GLU A 113 ? 0.24849 0.57470 0.35124 -0.01386 0.04935  0.03815  107 GLU A CD  
829  O OE1 . GLU A 113 ? 0.29933 0.58221 0.42253 0.00424  0.12295  0.05760  107 GLU A OE1 
830  O OE2 . GLU A 113 ? 0.26354 0.60001 0.31705 -0.04110 0.00988  0.07851  107 GLU A OE2 
831  N N   . THR A 114 ? 0.18214 0.39875 0.28369 0.07973  -0.03158 -0.02003 108 THR A N   
832  C CA  . THR A 114 ? 0.17457 0.38256 0.31464 0.04869  -0.01922 -0.01573 108 THR A CA  
833  C C   . THR A 114 ? 0.19914 0.35142 0.33403 0.02270  -0.03976 0.00759  108 THR A C   
834  O O   . THR A 114 ? 0.19630 0.34344 0.36664 0.04569  0.01301  0.01017  108 THR A O   
835  C CB  . THR A 114 ? 0.24608 0.38841 0.32901 0.05301  -0.03059 -0.02759 108 THR A CB  
836  O OG1 . THR A 114 ? 0.32120 0.41183 0.41065 0.04202  -0.01385 -0.02939 108 THR A OG1 
837  C CG2 . THR A 114 ? 0.23946 0.40600 0.31087 0.06520  -0.02098 0.00222  108 THR A CG2 
838  N N   . ASP A 115 ? 0.22008 0.36012 0.36298 0.06861  -0.09466 0.01372  109 ASP A N   
839  C CA  . ASP A 115 ? 0.21461 0.35202 0.37147 0.05325  -0.05620 -0.01859 109 ASP A CA  
840  C C   . ASP A 115 ? 0.20644 0.31959 0.35224 0.06552  -0.01197 -0.03931 109 ASP A C   
841  O O   . ASP A 115 ? 0.20344 0.32584 0.33728 0.08672  0.00511  -0.02916 109 ASP A O   
842  C CB  . ASP A 115 ? 0.32737 0.38449 0.35586 0.04435  -0.02128 -0.05507 109 ASP A CB  
843  C CG  . ASP A 115 ? 0.37779 0.40855 0.37456 0.06033  -0.06553 -0.00621 109 ASP A CG  
844  O OD1 . ASP A 115 ? 0.33219 0.41036 0.39159 0.05653  -0.04952 -0.00219 109 ASP A OD1 
845  O OD2 . ASP A 115 ? 0.52649 0.43716 0.38492 0.06319  -0.02984 -0.01970 109 ASP A OD2 
846  N N   . LEU A 116 ? 0.17477 0.29881 0.36118 0.03307  -0.03896 -0.03302 110 LEU A N   
847  C CA  . LEU A 116 ? 0.16693 0.26074 0.32741 0.05125  -0.05838 0.00115  110 LEU A CA  
848  C C   . LEU A 116 ? 0.21837 0.24683 0.34861 0.03829  -0.01446 -0.01668 110 LEU A C   
849  O O   . LEU A 116 ? 0.24202 0.27652 0.33441 0.00205  0.06629  -0.01504 110 LEU A O   
850  C CB  . LEU A 116 ? 0.23099 0.26339 0.29411 0.03852  -0.00573 0.02646  110 LEU A CB  
851  C CG  . LEU A 116 ? 0.19411 0.31973 0.27849 0.05534  0.01578  0.01275  110 LEU A CG  
852  C CD1 . LEU A 116 ? 0.22051 0.35967 0.30844 0.01724  0.05334  0.00409  110 LEU A CD1 
853  C CD2 . LEU A 116 ? 0.22974 0.33633 0.25918 0.05036  0.01245  0.01013  110 LEU A CD2 
854  N N   . TYR A 117 ? 0.21498 0.22524 0.36581 0.05249  -0.00473 -0.02660 111 TYR A N   
855  C CA  . TYR A 117 ? 0.22818 0.24281 0.39233 0.06306  0.00734  -0.04597 111 TYR A CA  
856  C C   . TYR A 117 ? 0.23541 0.26725 0.36698 0.05714  -0.02046 -0.08500 111 TYR A C   
857  O O   . TYR A 117 ? 0.25770 0.27515 0.34968 0.08232  0.00837  -0.03884 111 TYR A O   
858  C CB  . TYR A 117 ? 0.23139 0.26444 0.42660 0.03198  0.00927  -0.03899 111 TYR A CB  
859  C CG  . TYR A 117 ? 0.25087 0.28796 0.46151 0.02592  -0.00026 -0.05403 111 TYR A CG  
860  C CD1 . TYR A 117 ? 0.29478 0.30952 0.50535 -0.03250 -0.00847 -0.09914 111 TYR A CD1 
861  C CD2 . TYR A 117 ? 0.34388 0.32970 0.52402 -0.04074 0.04248  -0.05085 111 TYR A CD2 
862  C CE1 . TYR A 117 ? 0.38003 0.31232 0.55514 -0.03365 0.04130  -0.06015 111 TYR A CE1 
863  C CE2 . TYR A 117 ? 0.39136 0.35917 0.57203 -0.07162 0.01503  -0.01918 111 TYR A CE2 
864  C CZ  . TYR A 117 ? 0.40669 0.35416 0.59206 -0.03925 0.03147  -0.01881 111 TYR A CZ  
865  O OH  . TYR A 117 ? 0.40393 0.35451 0.61255 0.00578  0.03849  0.01817  111 TYR A OH  
866  N N   . LYS A 118 ? 0.21061 0.31186 0.38183 0.10281  -0.03038 -0.07830 112 LYS A N   
867  C CA  . LYS A 118 ? 0.22494 0.33120 0.39098 0.10547  -0.02254 -0.09821 112 LYS A CA  
868  C C   . LYS A 118 ? 0.24944 0.32695 0.40758 0.04625  -0.01493 -0.06803 112 LYS A C   
869  O O   . LYS A 118 ? 0.28141 0.30731 0.43073 0.04303  -0.01720 -0.05062 112 LYS A O   
870  C CB  . LYS A 118 ? 0.28916 0.36346 0.42283 0.09084  -0.01464 -0.07204 112 LYS A CB  
871  C CG  . LYS A 118 ? 0.41728 0.40041 0.49452 0.10448  0.07459  -0.02256 112 LYS A CG  
872  C CD  . LYS A 118 ? 0.51583 0.42951 0.53017 0.12173  0.16379  0.01543  112 LYS A CD  
873  C CE  . LYS A 118 ? 0.58455 0.43970 0.55307 0.12331  0.19393  0.03660  112 LYS A CE  
874  N NZ  . LYS A 118 ? 0.63172 0.45236 0.58261 0.11802  0.22918  0.03328  112 LYS A NZ  
875  N N   . LEU A 119 ? 0.24153 0.34726 0.37504 0.03552  -0.02920 -0.06401 113 LEU A N   
876  C CA  . LEU A 119 ? 0.22599 0.34659 0.40012 0.02580  0.02636  -0.04908 113 LEU A CA  
877  C C   . LEU A 119 ? 0.23255 0.35271 0.39272 0.01928  0.05608  -0.06212 113 LEU A C   
878  O O   . LEU A 119 ? 0.26682 0.39348 0.43453 -0.01696 0.12029  -0.08999 113 LEU A O   
879  C CB  . LEU A 119 ? 0.23237 0.33453 0.45571 -0.01341 0.07819  -0.07783 113 LEU A CB  
880  C CG  . LEU A 119 ? 0.21275 0.35579 0.54351 0.04034  0.08552  -0.07407 113 LEU A CG  
881  C CD1 . LEU A 119 ? 0.18660 0.39943 0.53526 0.01927  0.04528  -0.09410 113 LEU A CD1 
882  C CD2 . LEU A 119 ? 0.26294 0.36562 0.58839 0.02642  0.09294  -0.07012 113 LEU A CD2 
883  N N   . LEU A 120 ? 0.21297 0.33844 0.35110 0.03252  -0.01587 -0.02354 114 LEU A N   
884  C CA  . LEU A 120 ? 0.28004 0.34426 0.35096 0.02904  0.03144  -0.04275 114 LEU A CA  
885  C C   . LEU A 120 ? 0.31036 0.34743 0.34299 0.02614  0.00370  -0.07883 114 LEU A C   
886  O O   . LEU A 120 ? 0.36502 0.33226 0.34548 0.03337  0.00445  -0.12348 114 LEU A O   
887  C CB  . LEU A 120 ? 0.29325 0.36220 0.36303 0.02886  0.00399  -0.04154 114 LEU A CB  
888  C CG  . LEU A 120 ? 0.31825 0.38655 0.38030 0.04446  0.01839  -0.03538 114 LEU A CG  
889  C CD1 . LEU A 120 ? 0.27726 0.40335 0.41220 0.06107  -0.05908 -0.06368 114 LEU A CD1 
890  C CD2 . LEU A 120 ? 0.39175 0.40234 0.40234 0.04896  0.08073  -0.02849 114 LEU A CD2 
891  N N   . LYS A 121 ? 0.30265 0.33139 0.35304 0.00889  0.02071  -0.05025 115 LYS A N   
892  C CA  . LYS A 121 ? 0.37318 0.34142 0.38073 0.01128  0.04706  -0.04396 115 LYS A CA  
893  C C   . LYS A 121 ? 0.37114 0.34784 0.38852 0.03806  0.03871  -0.03921 115 LYS A C   
894  O O   . LYS A 121 ? 0.41132 0.34244 0.43453 0.03336  0.02781  -0.05075 115 LYS A O   
895  C CB  . LYS A 121 ? 0.40097 0.33489 0.41523 0.02214  0.02337  -0.00932 115 LYS A CB  
896  C CG  . LYS A 121 ? 0.44449 0.33231 0.44796 0.05701  0.05755  0.03405  115 LYS A CG  
897  C CD  . LYS A 121 ? 0.52273 0.36657 0.48482 0.07416  0.08160  0.04831  115 LYS A CD  
898  C CE  . LYS A 121 ? 0.55810 0.39343 0.52318 0.08508  0.10516  0.07044  115 LYS A CE  
899  N NZ  . LYS A 121 ? 0.57071 0.41723 0.54452 0.11298  0.12577  0.09269  115 LYS A NZ  
900  N N   . THR A 122 ? 0.36358 0.36378 0.35625 0.04888  0.05766  -0.00060 116 THR A N   
901  C CA  . THR A 122 ? 0.30585 0.38478 0.38418 0.11436  0.02461  0.02699  116 THR A CA  
902  C C   . THR A 122 ? 0.29997 0.41980 0.40369 0.13303  0.04857  0.01337  116 THR A C   
903  O O   . THR A 122 ? 0.34807 0.46274 0.46422 0.11508  0.09053  0.00310  116 THR A O   
904  C CB  . THR A 122 ? 0.33112 0.35461 0.36179 0.16633  0.03813  0.08195  116 THR A CB  
905  O OG1 . THR A 122 ? 0.33858 0.36634 0.35836 0.13864  0.04763  0.04346  116 THR A OG1 
906  C CG2 . THR A 122 ? 0.39848 0.35473 0.37912 0.14406  0.04467  0.12536  116 THR A CG2 
907  N N   . GLN A 123 ? 0.22370 0.39743 0.36357 0.13838  0.02108  -0.00858 117 GLN A N   
908  C CA  . GLN A 123 ? 0.26600 0.39812 0.34552 0.08457  0.01026  -0.01726 117 GLN A CA  
909  C C   . GLN A 123 ? 0.29013 0.41358 0.33030 0.09478  -0.01003 -0.00294 117 GLN A C   
910  O O   . GLN A 123 ? 0.26235 0.43770 0.35911 0.08953  -0.00494 -0.00240 117 GLN A O   
911  C CB  . GLN A 123 ? 0.21760 0.38682 0.33823 0.04140  -0.06470 -0.02364 117 GLN A CB  
912  C CG  . GLN A 123 ? 0.23215 0.37351 0.40198 0.06296  -0.01333 0.00329  117 GLN A CG  
913  C CD  . GLN A 123 ? 0.25670 0.38596 0.45338 0.02806  0.00115  0.04637  117 GLN A CD  
914  O OE1 . GLN A 123 ? 0.29629 0.36961 0.42538 -0.00231 0.04445  0.03784  117 GLN A OE1 
915  N NE2 . GLN A 123 ? 0.27051 0.42715 0.55180 0.07025  0.00986  0.09638  117 GLN A NE2 
916  N N   . HIS A 124 ? 0.34347 0.40535 0.35411 0.10123  0.01393  -0.00816 118 HIS A N   
917  C CA  . HIS A 124 ? 0.32414 0.42402 0.37333 0.13643  -0.01394 0.00566  118 HIS A CA  
918  C C   . HIS A 124 ? 0.29533 0.43090 0.36978 0.13309  -0.02201 0.01996  118 HIS A C   
919  O O   . HIS A 124 ? 0.29989 0.43197 0.42568 0.11701  -0.02493 0.01779  118 HIS A O   
920  C CB  . HIS A 124 ? 0.42091 0.44982 0.38504 0.16008  -0.00769 0.03659  118 HIS A CB  
921  C CG  . HIS A 124 ? 0.51333 0.45434 0.47107 0.14445  0.09103  0.02865  118 HIS A CG  
922  N ND1 . HIS A 124 ? 0.56582 0.45176 0.51340 0.13071  0.14874  0.02336  118 HIS A ND1 
923  C CD2 . HIS A 124 ? 0.50193 0.44626 0.49313 0.14899  0.11615  0.02140  118 HIS A CD2 
924  C CE1 . HIS A 124 ? 0.57300 0.45758 0.50707 0.13236  0.14445  0.01665  118 HIS A CE1 
925  N NE2 . HIS A 124 ? 0.52887 0.45119 0.49847 0.14579  0.15030  0.01985  118 HIS A NE2 
926  N N   . LEU A 125 ? 0.26386 0.44637 0.33918 0.14311  0.01456  -0.00849 119 LEU A N   
927  C CA  . LEU A 125 ? 0.23180 0.47538 0.33882 0.11322  0.05350  -0.00384 119 LEU A CA  
928  C C   . LEU A 125 ? 0.29097 0.50947 0.35058 0.10050  0.08069  -0.00042 119 LEU A C   
929  O O   . LEU A 125 ? 0.41473 0.51879 0.36779 0.11373  0.11459  0.00730  119 LEU A O   
930  C CB  . LEU A 125 ? 0.21483 0.48846 0.34764 0.11380  0.08395  -0.03570 119 LEU A CB  
931  C CG  . LEU A 125 ? 0.30603 0.52297 0.39630 0.11679  0.12810  -0.04329 119 LEU A CG  
932  C CD1 . LEU A 125 ? 0.44161 0.54319 0.46467 0.12395  0.16381  -0.02473 119 LEU A CD1 
933  C CD2 . LEU A 125 ? 0.23399 0.53649 0.34677 0.10489  0.07779  -0.08208 119 LEU A CD2 
934  N N   . SER A 126 ? 0.20306 0.52569 0.36029 0.06723  0.06987  -0.00493 120 SER A N   
935  C CA  . SER A 126 ? 0.26792 0.54694 0.39440 0.03939  0.06414  -0.04932 120 SER A CA  
936  C C   . SER A 126 ? 0.27642 0.51085 0.35731 0.03705  0.08626  -0.03999 120 SER A C   
937  O O   . SER A 126 ? 0.24467 0.48516 0.31052 0.02705  0.09284  -0.07293 120 SER A O   
938  C CB  . SER A 126 ? 0.26959 0.59169 0.44926 0.03846  0.08630  -0.09942 120 SER A CB  
939  O OG  . SER A 126 ? 0.23061 0.61243 0.49673 0.01638  0.05785  -0.12285 120 SER A OG  
940  N N   . ASN A 127 ? 0.27262 0.48453 0.33236 0.05576  0.09098  -0.01947 121 ASN A N   
941  C CA  . ASN A 127 ? 0.24842 0.46626 0.27909 0.04602  0.02028  -0.01040 121 ASN A CA  
942  C C   . ASN A 127 ? 0.20611 0.47716 0.29807 -0.01497 0.02634  0.01247  121 ASN A C   
943  O O   . ASN A 127 ? 0.25797 0.46767 0.31879 -0.01108 0.05874  0.05210  121 ASN A O   
944  C CB  . ASN A 127 ? 0.33372 0.43719 0.32756 0.07036  0.04581  -0.01647 121 ASN A CB  
945  C CG  . ASN A 127 ? 0.30654 0.43926 0.34927 0.04307  0.01286  -0.00783 121 ASN A CG  
946  O OD1 . ASN A 127 ? 0.22038 0.44005 0.31588 0.02842  -0.01400 -0.02275 121 ASN A OD1 
947  N ND2 . ASN A 127 ? 0.36042 0.44517 0.41597 0.01135  0.07075  0.01010  121 ASN A ND2 
948  N N   . ASP A 128 ? 0.23908 0.50054 0.29746 -0.05711 0.05827  0.01288  122 ASP A N   
949  C CA  . ASP A 128 ? 0.23486 0.49787 0.31714 -0.09024 0.05589  0.04304  122 ASP A CA  
950  C C   . ASP A 128 ? 0.22387 0.46154 0.29871 -0.06625 0.02738  0.02748  122 ASP A C   
951  O O   . ASP A 128 ? 0.24419 0.43478 0.33535 -0.03443 0.03703  0.03538  122 ASP A O   
952  C CB  . ASP A 128 ? 0.26431 0.52622 0.37819 -0.06724 0.08650  0.07030  122 ASP A CB  
953  C CG  . ASP A 128 ? 0.29358 0.52144 0.39574 -0.06195 0.06269  0.11105  122 ASP A CG  
954  O OD1 . ASP A 128 ? 0.34736 0.51575 0.42688 -0.05187 0.07451  0.13723  122 ASP A OD1 
955  O OD2 . ASP A 128 ? 0.29700 0.51193 0.39006 -0.06085 0.10095  0.12764  122 ASP A OD2 
956  N N   . HIS A 129 ? 0.17785 0.44237 0.28345 -0.02218 0.02046  0.02721  123 HIS A N   
957  C CA  . HIS A 129 ? 0.14657 0.39757 0.29585 0.01377  0.02343  0.02224  123 HIS A CA  
958  C C   . HIS A 129 ? 0.17076 0.39104 0.30410 0.00982  0.01123  0.00566  123 HIS A C   
959  O O   . HIS A 129 ? 0.17967 0.40022 0.28086 0.01803  -0.00352 0.02145  123 HIS A O   
960  C CB  . HIS A 129 ? 0.15238 0.37947 0.31031 0.04585  -0.00646 0.00275  123 HIS A CB  
961  C CG  . HIS A 129 ? 0.18925 0.37160 0.34893 0.05905  0.00428  -0.00419 123 HIS A CG  
962  N ND1 . HIS A 129 ? 0.24858 0.39256 0.40893 0.06187  0.06186  -0.03594 123 HIS A ND1 
963  C CD2 . HIS A 129 ? 0.20706 0.35090 0.38888 0.03513  0.00718  -0.00896 123 HIS A CD2 
964  C CE1 . HIS A 129 ? 0.26168 0.40331 0.39975 0.05600  0.04047  -0.02379 123 HIS A CE1 
965  N NE2 . HIS A 129 ? 0.22864 0.36832 0.39411 0.04541  0.02086  -0.01733 123 HIS A NE2 
966  N N   . ILE A 130 ? 0.19339 0.38501 0.26827 0.02298  0.02836  0.00312  124 ILE A N   
967  C CA  . ILE A 130 ? 0.15325 0.34779 0.25458 0.00639  -0.01290 -0.03342 124 ILE A CA  
968  C C   . ILE A 130 ? 0.16632 0.33299 0.23545 0.00378  0.01790  0.00443  124 ILE A C   
969  O O   . ILE A 130 ? 0.19563 0.34555 0.22508 0.01528  0.03596  -0.02804 124 ILE A O   
970  C CB  . ILE A 130 ? 0.14183 0.34896 0.29659 0.02369  -0.01772 -0.03801 124 ILE A CB  
971  C CG1 . ILE A 130 ? 0.21005 0.34079 0.32636 0.02124  -0.01690 -0.02326 124 ILE A CG1 
972  C CG2 . ILE A 130 ? 0.12335 0.35067 0.33743 0.03865  -0.00012 -0.05489 124 ILE A CG2 
973  C CD1 . ILE A 130 ? 0.26711 0.37636 0.35620 -0.00850 -0.03137 -0.04365 124 ILE A CD1 
974  N N   . CYS A 131 ? 0.22877 0.30520 0.21843 -0.02394 0.04318  0.01125  125 CYS A N   
975  C CA  . CYS A 131 ? 0.20587 0.32465 0.22382 -0.02754 0.06661  0.00638  125 CYS A CA  
976  C C   . CYS A 131 ? 0.16473 0.34173 0.19801 -0.01524 -0.00251 0.01650  125 CYS A C   
977  O O   . CYS A 131 ? 0.19427 0.34359 0.20705 0.01204  0.04351  -0.00498 125 CYS A O   
978  C CB  . CYS A 131 ? 0.25884 0.32992 0.22189 -0.02479 0.04059  0.02178  125 CYS A CB  
979  S SG  . CYS A 131 ? 0.29697 0.37731 0.29079 -0.00961 0.06702  0.02023  125 CYS A SG  
980  N N   . TYR A 132 ? 0.17393 0.39032 0.20179 -0.05190 -0.01899 0.01401  126 TYR A N   
981  C CA  . TYR A 132 ? 0.15365 0.39988 0.24529 -0.04157 -0.00722 0.03695  126 TYR A CA  
982  C C   . TYR A 132 ? 0.17817 0.35236 0.26108 0.00816  0.02137  0.04697  126 TYR A C   
983  O O   . TYR A 132 ? 0.18111 0.32522 0.28656 -0.01459 0.04701  0.00548  126 TYR A O   
984  C CB  . TYR A 132 ? 0.14428 0.45288 0.27878 -0.04424 0.03051  0.02712  126 TYR A CB  
985  C CG  . TYR A 132 ? 0.22277 0.46944 0.28063 -0.05562 -0.00482 0.02054  126 TYR A CG  
986  C CD1 . TYR A 132 ? 0.32941 0.49641 0.31697 -0.08805 -0.02544 -0.00228 126 TYR A CD1 
987  C CD2 . TYR A 132 ? 0.20820 0.47145 0.28662 -0.07485 -0.03768 0.05795  126 TYR A CD2 
988  C CE1 . TYR A 132 ? 0.37245 0.49997 0.34103 -0.10270 -0.07608 0.01426  126 TYR A CE1 
989  C CE2 . TYR A 132 ? 0.28837 0.47277 0.31474 -0.12745 -0.05350 0.08201  126 TYR A CE2 
990  C CZ  . TYR A 132 ? 0.38964 0.50504 0.36444 -0.13696 -0.09097 0.03714  126 TYR A CZ  
991  O OH  . TYR A 132 ? 0.49068 0.53632 0.45526 -0.15263 -0.10235 0.04685  126 TYR A OH  
992  N N   . PHE A 133 ? 0.15550 0.30702 0.22878 -0.00084 -0.00467 0.03928  127 PHE A N   
993  C CA  . PHE A 133 ? 0.17687 0.27277 0.25690 -0.00931 0.00823  0.02689  127 PHE A CA  
994  C C   . PHE A 133 ? 0.16478 0.25801 0.21872 -0.00875 -0.02790 0.01080  127 PHE A C   
995  O O   . PHE A 133 ? 0.17778 0.23477 0.21615 -0.00154 0.02648  0.01199  127 PHE A O   
996  C CB  . PHE A 133 ? 0.21268 0.27450 0.28079 0.03530  0.03730  0.01491  127 PHE A CB  
997  C CG  . PHE A 133 ? 0.14754 0.32757 0.30281 0.04612  0.02935  0.01050  127 PHE A CG  
998  C CD1 . PHE A 133 ? 0.15839 0.37353 0.38177 0.06044  -0.02016 0.02010  127 PHE A CD1 
999  C CD2 . PHE A 133 ? 0.19830 0.33510 0.36641 0.02239  0.05387  -0.00153 127 PHE A CD2 
1000 C CE1 . PHE A 133 ? 0.26966 0.38332 0.42313 0.07320  0.02867  0.02828  127 PHE A CE1 
1001 C CE2 . PHE A 133 ? 0.22602 0.34695 0.36272 0.05984  0.01102  0.00949  127 PHE A CE2 
1002 C CZ  . PHE A 133 ? 0.21847 0.36756 0.37376 0.07374  0.02328  0.01308  127 PHE A CZ  
1003 N N   . LEU A 134 ? 0.18593 0.26106 0.20695 0.00593  -0.00536 0.02024  128 LEU A N   
1004 C CA  . LEU A 134 ? 0.16481 0.24769 0.18520 -0.00064 -0.02587 -0.01267 128 LEU A CA  
1005 C C   . LEU A 134 ? 0.19848 0.23421 0.21601 0.01706  0.00071  0.00869  128 LEU A C   
1006 O O   . LEU A 134 ? 0.17118 0.23593 0.18659 -0.01448 0.00755  0.00126  128 LEU A O   
1007 C CB  . LEU A 134 ? 0.13443 0.28990 0.18633 -0.00183 -0.01485 -0.02049 128 LEU A CB  
1008 C CG  . LEU A 134 ? 0.13407 0.32703 0.21267 -0.02329 -0.00738 0.01239  128 LEU A CG  
1009 C CD1 . LEU A 134 ? 0.19511 0.34057 0.26517 -0.03825 0.01237  0.00484  128 LEU A CD1 
1010 C CD2 . LEU A 134 ? 0.20559 0.31112 0.20442 -0.04135 0.00887  -0.03559 128 LEU A CD2 
1011 N N   . TYR A 135 ? 0.18788 0.23410 0.20804 -0.02229 -0.00059 -0.02447 129 TYR A N   
1012 C CA  . TYR A 135 ? 0.17712 0.21565 0.21403 -0.06903 0.00834  -0.03856 129 TYR A CA  
1013 C C   . TYR A 135 ? 0.22917 0.20475 0.16640 -0.00118 0.01086  -0.00039 129 TYR A C   
1014 O O   . TYR A 135 ? 0.21661 0.18787 0.17404 -0.01988 0.01081  0.01366  129 TYR A O   
1015 C CB  . TYR A 135 ? 0.17330 0.22248 0.27400 -0.07927 0.03614  -0.02471 129 TYR A CB  
1016 C CG  . TYR A 135 ? 0.14563 0.23879 0.23326 -0.07071 0.01491  0.01980  129 TYR A CG  
1017 C CD1 . TYR A 135 ? 0.24957 0.28984 0.18649 -0.03074 0.04414  0.02037  129 TYR A CD1 
1018 C CD2 . TYR A 135 ? 0.19444 0.26597 0.26492 -0.07254 0.02831  0.02088  129 TYR A CD2 
1019 C CE1 . TYR A 135 ? 0.21796 0.29207 0.23420 -0.02320 -0.00169 -0.00501 129 TYR A CE1 
1020 C CE2 . TYR A 135 ? 0.22578 0.27716 0.29909 -0.07822 0.04116  0.02192  129 TYR A CE2 
1021 C CZ  . TYR A 135 ? 0.26619 0.28018 0.28041 -0.06413 0.02330  0.00200  129 TYR A CZ  
1022 O OH  . TYR A 135 ? 0.25890 0.29275 0.29099 -0.06820 0.02988  -0.01520 129 TYR A OH  
1023 N N   . GLN A 136 ? 0.18433 0.20328 0.17762 0.00432  -0.02576 0.02073  130 GLN A N   
1024 C CA  . GLN A 136 ? 0.09829 0.23547 0.23386 -0.02100 -0.02687 0.00673  130 GLN A CA  
1025 C C   . GLN A 136 ? 0.12213 0.22747 0.23946 -0.02695 0.00527  0.00980  130 GLN A C   
1026 O O   . GLN A 136 ? 0.14963 0.24157 0.21165 0.02416  0.01530  0.00854  130 GLN A O   
1027 C CB  . GLN A 136 ? 0.09008 0.25697 0.25430 0.00055  -0.01132 -0.03191 130 GLN A CB  
1028 C CG  . GLN A 136 ? 0.08968 0.30263 0.26364 0.00712  -0.04031 -0.00005 130 GLN A CG  
1029 C CD  . GLN A 136 ? 0.11926 0.29988 0.25253 0.01755  0.00641  -0.01004 130 GLN A CD  
1030 O OE1 . GLN A 136 ? 0.12140 0.31550 0.24838 0.00721  0.01365  -0.01765 130 GLN A OE1 
1031 N NE2 . GLN A 136 ? 0.14649 0.27254 0.22190 0.01185  0.05334  -0.02274 130 GLN A NE2 
1032 N N   . ILE A 137 ? 0.12173 0.20909 0.21219 -0.03046 -0.02012 0.03649  131 ILE A N   
1033 C CA  . ILE A 137 ? 0.12790 0.19973 0.22859 -0.00491 0.00624  -0.00142 131 ILE A CA  
1034 C C   . ILE A 137 ? 0.14726 0.21032 0.21214 0.01866  -0.00985 0.00709  131 ILE A C   
1035 O O   . ILE A 137 ? 0.17278 0.19267 0.20848 0.02403  0.02392  0.00154  131 ILE A O   
1036 C CB  . ILE A 137 ? 0.13372 0.16754 0.23550 0.02244  0.01101  -0.00568 131 ILE A CB  
1037 C CG1 . ILE A 137 ? 0.22677 0.17517 0.19965 0.01898  0.01651  -0.02771 131 ILE A CG1 
1038 C CG2 . ILE A 137 ? 0.12828 0.20368 0.21318 0.01303  0.01736  -0.01677 131 ILE A CG2 
1039 C CD1 . ILE A 137 ? 0.25788 0.18927 0.18638 0.00681  0.03643  0.01692  131 ILE A CD1 
1040 N N   . LEU A 138 ? 0.19875 0.19417 0.18340 0.00630  -0.03670 0.05950  132 LEU A N   
1041 C CA  . LEU A 138 ? 0.20992 0.20140 0.15926 0.01115  -0.03193 0.03746  132 LEU A CA  
1042 C C   . LEU A 138 ? 0.15040 0.20363 0.17854 -0.01189 -0.04574 -0.00592 132 LEU A C   
1043 O O   . LEU A 138 ? 0.17848 0.22300 0.19815 0.01070  -0.01379 -0.00924 132 LEU A O   
1044 C CB  . LEU A 138 ? 0.22449 0.23252 0.13635 0.00334  -0.04444 0.02398  132 LEU A CB  
1045 C CG  . LEU A 138 ? 0.19679 0.23153 0.13607 -0.00496 -0.02074 0.00783  132 LEU A CG  
1046 C CD1 . LEU A 138 ? 0.21824 0.28947 0.14036 -0.01092 -0.01566 0.02717  132 LEU A CD1 
1047 C CD2 . LEU A 138 ? 0.16774 0.22237 0.22521 -0.00742 -0.05015 -0.00742 132 LEU A CD2 
1048 N N   . ARG A 139 ? 0.16494 0.22663 0.18145 -0.01510 -0.03158 0.02210  133 ARG A N   
1049 C CA  . ARG A 139 ? 0.13747 0.22623 0.19015 -0.03892 -0.05088 0.03368  133 ARG A CA  
1050 C C   . ARG A 139 ? 0.14302 0.23784 0.17447 0.01525  -0.03196 0.00469  133 ARG A C   
1051 O O   . ARG A 139 ? 0.16148 0.24447 0.19513 0.01440  0.00752  -0.02048 133 ARG A O   
1052 C CB  . ARG A 139 ? 0.13113 0.20348 0.20224 -0.03162 -0.03509 0.00514  133 ARG A CB  
1053 C CG  . ARG A 139 ? 0.12868 0.19585 0.23962 -0.06934 -0.02895 0.01291  133 ARG A CG  
1054 C CD  . ARG A 139 ? 0.14859 0.24063 0.23663 -0.09760 -0.03523 -0.00683 133 ARG A CD  
1055 N NE  . ARG A 139 ? 0.19633 0.26386 0.25375 -0.05145 -0.03706 0.00687  133 ARG A NE  
1056 C CZ  . ARG A 139 ? 0.26388 0.26337 0.30806 -0.04941 -0.04635 0.02537  133 ARG A CZ  
1057 N NH1 . ARG A 139 ? 0.30231 0.26282 0.33009 -0.03546 -0.09512 0.02154  133 ARG A NH1 
1058 N NH2 . ARG A 139 ? 0.28356 0.24477 0.32578 -0.06539 -0.05911 0.02483  133 ARG A NH2 
1059 N N   . GLY A 140 ? 0.15491 0.23040 0.17125 0.00184  -0.00384 0.03690  134 GLY A N   
1060 C CA  . GLY A 140 ? 0.15594 0.23783 0.14635 -0.00442 0.00823  0.01118  134 GLY A CA  
1061 C C   . GLY A 140 ? 0.14369 0.21019 0.17091 0.01728  0.02455  -0.01243 134 GLY A C   
1062 O O   . GLY A 140 ? 0.17335 0.20181 0.18916 0.00974  -0.00021 0.02745  134 GLY A O   
1063 N N   . LEU A 141 ? 0.15551 0.18755 0.20532 -0.00090 0.03360  0.00822  135 LEU A N   
1064 C CA  . LEU A 141 ? 0.16452 0.16120 0.20280 -0.03644 0.01585  -0.00601 135 LEU A CA  
1065 C C   . LEU A 141 ? 0.20956 0.20656 0.18580 -0.00801 0.01966  0.02385  135 LEU A C   
1066 O O   . LEU A 141 ? 0.19973 0.22404 0.17295 -0.01156 0.00915  -0.00610 135 LEU A O   
1067 C CB  . LEU A 141 ? 0.17412 0.17608 0.17640 -0.01825 -0.03056 -0.01954 135 LEU A CB  
1068 C CG  . LEU A 141 ? 0.15578 0.19617 0.18948 -0.02833 -0.02401 0.00893  135 LEU A CG  
1069 C CD1 . LEU A 141 ? 0.19308 0.21995 0.18366 -0.03981 0.01863  0.00425  135 LEU A CD1 
1070 C CD2 . LEU A 141 ? 0.22372 0.25468 0.16704 -0.03464 -0.03168 -0.00999 135 LEU A CD2 
1071 N N   . LYS A 142 ? 0.14227 0.21340 0.18932 0.00377  -0.02021 -0.01037 136 LYS A N   
1072 C CA  . LYS A 142 ? 0.17510 0.17541 0.17923 -0.00126 0.00650  -0.00464 136 LYS A CA  
1073 C C   . LYS A 142 ? 0.16566 0.20806 0.15659 0.04981  0.01062  -0.01320 136 LYS A C   
1074 O O   . LYS A 142 ? 0.20124 0.23118 0.20084 0.03019  0.00851  -0.01778 136 LYS A O   
1075 C CB  . LYS A 142 ? 0.19449 0.12764 0.20441 0.00239  -0.00965 0.01344  136 LYS A CB  
1076 C CG  . LYS A 142 ? 0.22808 0.13735 0.21564 0.02031  -0.00593 0.03094  136 LYS A CG  
1077 C CD  . LYS A 142 ? 0.20509 0.19221 0.24668 -0.00820 -0.00942 0.01682  136 LYS A CD  
1078 C CE  . LYS A 142 ? 0.24486 0.19865 0.27639 -0.04792 0.02271  0.00418  136 LYS A CE  
1079 N NZ  . LYS A 142 ? 0.26487 0.21070 0.26522 -0.03918 -0.02465 0.02801  136 LYS A NZ  
1080 N N   . TYR A 143 ? 0.18226 0.24892 0.17481 0.02187  -0.05318 -0.00173 137 TYR A N   
1081 C CA  . TYR A 143 ? 0.18844 0.27133 0.17893 -0.02222 -0.05221 0.00868  137 TYR A CA  
1082 C C   . TYR A 143 ? 0.19693 0.24591 0.20338 -0.00348 -0.02834 0.01269  137 TYR A C   
1083 O O   . TYR A 143 ? 0.20171 0.24912 0.19847 -0.00170 -0.00075 -0.00722 137 TYR A O   
1084 C CB  . TYR A 143 ? 0.15275 0.27631 0.20455 -0.03584 -0.04661 -0.00296 137 TYR A CB  
1085 C CG  . TYR A 143 ? 0.16064 0.25514 0.19828 -0.01608 -0.04477 -0.00730 137 TYR A CG  
1086 C CD1 . TYR A 143 ? 0.20201 0.24852 0.21494 0.00985  -0.00967 -0.02190 137 TYR A CD1 
1087 C CD2 . TYR A 143 ? 0.19498 0.27925 0.22278 0.00974  -0.02483 -0.00833 137 TYR A CD2 
1088 C CE1 . TYR A 143 ? 0.28605 0.24348 0.23212 -0.02534 -0.00269 -0.02424 137 TYR A CE1 
1089 C CE2 . TYR A 143 ? 0.19891 0.28988 0.21680 0.01054  0.02245  -0.02640 137 TYR A CE2 
1090 C CZ  . TYR A 143 ? 0.26760 0.26986 0.21951 0.00337  0.00844  -0.04005 137 TYR A CZ  
1091 O OH  . TYR A 143 ? 0.34343 0.29306 0.20350 -0.00137 0.00995  -0.02621 137 TYR A OH  
1092 N N   . ILE A 144 ? 0.15566 0.20086 0.18831 -0.01959 -0.00731 0.01132  138 ILE A N   
1093 C CA  . ILE A 144 ? 0.14647 0.19306 0.20733 -0.01615 -0.03004 0.02047  138 ILE A CA  
1094 C C   . ILE A 144 ? 0.17349 0.22344 0.18682 0.03037  -0.00430 0.00920  138 ILE A C   
1095 O O   . ILE A 144 ? 0.19993 0.24462 0.20157 -0.01007 0.02419  -0.01138 138 ILE A O   
1096 C CB  . ILE A 144 ? 0.13219 0.19891 0.21350 -0.02467 -0.03888 0.00442  138 ILE A CB  
1097 C CG1 . ILE A 144 ? 0.18727 0.21015 0.19219 0.01835  -0.04279 -0.00184 138 ILE A CG1 
1098 C CG2 . ILE A 144 ? 0.17233 0.25830 0.18607 -0.04196 -0.01259 0.01232  138 ILE A CG2 
1099 C CD1 . ILE A 144 ? 0.22124 0.24765 0.19199 0.03561  -0.01765 0.00599  138 ILE A CD1 
1100 N N   . HIS A 145 ? 0.19038 0.19698 0.15793 0.03244  -0.02422 0.00234  139 HIS A N   
1101 C CA  . HIS A 145 ? 0.18500 0.19859 0.17403 0.05617  0.00364  -0.03018 139 HIS A CA  
1102 C C   . HIS A 145 ? 0.18429 0.20631 0.20818 0.04803  0.00459  -0.01715 139 HIS A C   
1103 O O   . HIS A 145 ? 0.19973 0.22121 0.26466 0.04382  0.02602  -0.05011 139 HIS A O   
1104 C CB  . HIS A 145 ? 0.18107 0.22109 0.16613 0.01977  -0.00471 -0.03286 139 HIS A CB  
1105 C CG  . HIS A 145 ? 0.16552 0.20654 0.19021 0.02898  -0.00669 -0.01786 139 HIS A CG  
1106 N ND1 . HIS A 145 ? 0.20093 0.21665 0.18409 0.01500  -0.00932 -0.02503 139 HIS A ND1 
1107 C CD2 . HIS A 145 ? 0.14506 0.20945 0.19444 0.01889  -0.01178 -0.01490 139 HIS A CD2 
1108 C CE1 . HIS A 145 ? 0.19872 0.22364 0.15185 -0.00493 -0.06754 0.00490  139 HIS A CE1 
1109 N NE2 . HIS A 145 ? 0.19259 0.23647 0.15434 0.01340  -0.03483 -0.03765 139 HIS A NE2 
1110 N N   . SER A 146 ? 0.20545 0.21953 0.17900 0.00707  -0.04031 -0.00393 140 SER A N   
1111 C CA  . SER A 146 ? 0.22608 0.22323 0.20434 -0.02956 0.00442  -0.03692 140 SER A CA  
1112 C C   . SER A 146 ? 0.26368 0.25500 0.17843 0.00744  0.01625  -0.02320 140 SER A C   
1113 O O   . SER A 146 ? 0.27570 0.28826 0.22775 0.00447  -0.00879 -0.04558 140 SER A O   
1114 C CB  . SER A 146 ? 0.17914 0.22904 0.21899 -0.02617 -0.04026 -0.02085 140 SER A CB  
1115 O OG  . SER A 146 ? 0.22330 0.25158 0.24681 -0.01752 -0.01252 -0.04914 140 SER A OG  
1116 N N   . ALA A 147 ? 0.24097 0.27871 0.17837 -0.00052 -0.00699 0.00422  141 ALA A N   
1117 C CA  . ALA A 147 ? 0.22342 0.29922 0.20200 -0.01298 -0.02176 -0.00833 141 ALA A CA  
1118 C C   . ALA A 147 ? 0.26465 0.29719 0.23210 -0.01223 0.06440  -0.01977 141 ALA A C   
1119 O O   . ALA A 147 ? 0.27514 0.31908 0.22309 -0.03864 0.05898  -0.03872 141 ALA A O   
1120 C CB  . ALA A 147 ? 0.23007 0.31013 0.22475 -0.03278 -0.03781 -0.00316 141 ALA A CB  
1121 N N   . ASN A 148 ? 0.26129 0.26398 0.23280 0.01964  0.02580  -0.04505 142 ASN A N   
1122 C CA  . ASN A 148 ? 0.25518 0.27409 0.29375 0.02977  0.05586  -0.01527 142 ASN A CA  
1123 C C   . ASN A 148 ? 0.24548 0.24441 0.23473 0.03067  0.05997  -0.00539 142 ASN A C   
1124 O O   . ASN A 148 ? 0.22576 0.28316 0.24805 0.02298  0.04623  -0.00868 142 ASN A O   
1125 C CB  . ASN A 148 ? 0.28365 0.33814 0.37023 0.04881  0.06800  -0.01476 142 ASN A CB  
1126 C CG  . ASN A 148 ? 0.32922 0.35153 0.42619 0.04402  0.09385  0.00086  142 ASN A CG  
1127 O OD1 . ASN A 148 ? 0.35271 0.34646 0.45174 0.03126  0.04972  0.02745  142 ASN A OD1 
1128 N ND2 . ASN A 148 ? 0.37570 0.36855 0.43089 0.06850  0.13458  -0.00478 142 ASN A ND2 
1129 N N   . VAL A 149 ? 0.21475 0.23244 0.19534 0.00392  -0.01981 -0.00615 143 VAL A N   
1130 C CA  . VAL A 149 ? 0.18951 0.25085 0.20666 0.01919  -0.01946 -0.00036 143 VAL A CA  
1131 C C   . VAL A 149 ? 0.20506 0.26763 0.19280 0.00537  0.00623  -0.01560 143 VAL A C   
1132 O O   . VAL A 149 ? 0.19781 0.28882 0.18573 0.00153  -0.02437 -0.00911 143 VAL A O   
1133 C CB  . VAL A 149 ? 0.24998 0.26966 0.20248 0.02354  0.02104  -0.00112 143 VAL A CB  
1134 C CG1 . VAL A 149 ? 0.30615 0.22579 0.21608 0.02111  0.05203  -0.01408 143 VAL A CG1 
1135 C CG2 . VAL A 149 ? 0.26131 0.33025 0.19388 0.02622  0.03073  -0.01591 143 VAL A CG2 
1136 N N   . LEU A 150 ? 0.20897 0.25133 0.18241 -0.00005 -0.01009 -0.00541 144 LEU A N   
1137 C CA  . LEU A 150 ? 0.16604 0.25539 0.19846 -0.00689 -0.04036 -0.03256 144 LEU A CA  
1138 C C   . LEU A 150 ? 0.17482 0.24613 0.17984 0.02982  -0.00449 0.01282  144 LEU A C   
1139 O O   . LEU A 150 ? 0.22206 0.26783 0.18703 0.03314  0.01235  0.02201  144 LEU A O   
1140 C CB  . LEU A 150 ? 0.19850 0.29720 0.25052 0.02397  -0.03926 0.00129  144 LEU A CB  
1141 C CG  . LEU A 150 ? 0.19647 0.33729 0.28082 0.03327  -0.03154 0.02297  144 LEU A CG  
1142 C CD1 . LEU A 150 ? 0.18198 0.33063 0.32744 0.02925  -0.05374 -0.00379 144 LEU A CD1 
1143 C CD2 . LEU A 150 ? 0.27139 0.35982 0.28105 0.05765  -0.04272 0.04818  144 LEU A CD2 
1144 N N   . HIS A 151 ? 0.15441 0.23249 0.18478 0.03859  -0.01633 -0.02236 145 HIS A N   
1145 C CA  . HIS A 151 ? 0.10530 0.24745 0.24048 0.02645  0.01446  -0.02478 145 HIS A CA  
1146 C C   . HIS A 151 ? 0.18922 0.23532 0.21172 -0.00802 0.04226  -0.00860 145 HIS A C   
1147 O O   . HIS A 151 ? 0.19561 0.23872 0.17009 -0.03644 0.04440  0.00247  145 HIS A O   
1148 C CB  . HIS A 151 ? 0.08691 0.27367 0.19986 0.03982  -0.00723 0.01831  145 HIS A CB  
1149 C CG  . HIS A 151 ? 0.12354 0.27222 0.20010 0.01481  -0.01952 -0.01748 145 HIS A CG  
1150 N ND1 . HIS A 151 ? 0.11532 0.26986 0.22053 -0.00842 -0.00573 -0.01121 145 HIS A ND1 
1151 C CD2 . HIS A 151 ? 0.14414 0.27983 0.22007 0.05180  -0.01245 -0.00281 145 HIS A CD2 
1152 C CE1 . HIS A 151 ? 0.16741 0.27987 0.21656 0.02766  -0.01741 -0.00981 145 HIS A CE1 
1153 N NE2 . HIS A 151 ? 0.18418 0.26627 0.22504 0.03149  -0.00245 -0.01211 145 HIS A NE2 
1154 N N   . ARG A 152 ? 0.16414 0.23145 0.19202 -0.00940 -0.00123 -0.01189 146 ARG A N   
1155 C CA  . ARG A 152 ? 0.16103 0.25679 0.19539 -0.00986 0.05832  -0.00324 146 ARG A CA  
1156 C C   . ARG A 152 ? 0.19693 0.24828 0.24140 0.01468  0.04331  0.03028  146 ARG A C   
1157 O O   . ARG A 152 ? 0.25044 0.24549 0.33691 -0.00169 0.07035  -0.01153 146 ARG A O   
1158 C CB  . ARG A 152 ? 0.18241 0.27601 0.22003 0.00898  0.04266  -0.01890 146 ARG A CB  
1159 C CG  . ARG A 152 ? 0.19560 0.35070 0.23087 0.05225  0.05781  -0.01993 146 ARG A CG  
1160 C CD  . ARG A 152 ? 0.24257 0.37753 0.25607 0.02635  -0.02635 -0.07222 146 ARG A CD  
1161 N NE  . ARG A 152 ? 0.44620 0.38450 0.33115 0.02917  0.04678  -0.09595 146 ARG A NE  
1162 C CZ  . ARG A 152 ? 0.50082 0.36177 0.29820 0.04383  0.00632  -0.10556 146 ARG A CZ  
1163 N NH1 . ARG A 152 ? 0.52692 0.35081 0.32516 0.09097  -0.03074 -0.14497 146 ARG A NH1 
1164 N NH2 . ARG A 152 ? 0.46072 0.37943 0.29078 0.01877  -0.02313 -0.08373 146 ARG A NH2 
1165 N N   . ASP A 153 ? 0.18667 0.22482 0.18176 0.01870  0.00633  0.01093  147 ASP A N   
1166 C CA  . ASP A 153 ? 0.24656 0.24207 0.25314 0.02789  -0.00234 0.03095  147 ASP A CA  
1167 C C   . ASP A 153 ? 0.22135 0.20077 0.20573 0.01928  -0.03527 0.02366  147 ASP A C   
1168 O O   . ASP A 153 ? 0.23553 0.23165 0.22170 0.05214  0.00561  0.02781  147 ASP A O   
1169 C CB  . ASP A 153 ? 0.28003 0.25729 0.23945 -0.00146 0.00946  0.03892  147 ASP A CB  
1170 C CG  . ASP A 153 ? 0.30453 0.29749 0.25567 0.00046  0.00716  0.04748  147 ASP A CG  
1171 O OD1 . ASP A 153 ? 0.31931 0.32791 0.24637 -0.00144 -0.02061 0.03995  147 ASP A OD1 
1172 O OD2 . ASP A 153 ? 0.31394 0.32718 0.25609 -0.00067 -0.02322 0.03527  147 ASP A OD2 
1173 N N   . LEU A 154 ? 0.20592 0.16707 0.18653 0.02032  0.00238  0.02011  148 LEU A N   
1174 C CA  . LEU A 154 ? 0.19252 0.18890 0.19301 0.00901  0.04169  -0.00111 148 LEU A CA  
1175 C C   . LEU A 154 ? 0.19554 0.20645 0.19849 0.02542  0.02321  -0.00032 148 LEU A C   
1176 O O   . LEU A 154 ? 0.19600 0.23059 0.20538 -0.00167 -0.01875 0.01904  148 LEU A O   
1177 C CB  . LEU A 154 ? 0.21559 0.19345 0.21009 -0.02634 0.00169  -0.00755 148 LEU A CB  
1178 C CG  . LEU A 154 ? 0.20749 0.19216 0.19340 -0.00879 -0.05298 -0.02728 148 LEU A CG  
1179 C CD1 . LEU A 154 ? 0.23798 0.19533 0.27007 -0.00216 -0.05262 0.02457  148 LEU A CD1 
1180 C CD2 . LEU A 154 ? 0.18876 0.23752 0.20307 0.02584  -0.03646 0.01119  148 LEU A CD2 
1181 N N   . LYS A 155 ? 0.20065 0.22953 0.19389 0.02955  0.01773  -0.00304 149 LYS A N   
1182 C CA  . LYS A 155 ? 0.17880 0.25627 0.18613 0.02362  0.04576  0.01501  149 LYS A CA  
1183 C C   . LYS A 155 ? 0.17036 0.24295 0.20516 0.03230  -0.00066 -0.00700 149 LYS A C   
1184 O O   . LYS A 155 ? 0.17970 0.20906 0.20799 0.01142  0.00529  -0.00527 149 LYS A O   
1185 C CB  . LYS A 155 ? 0.16523 0.27559 0.20216 0.02054  0.00703  0.07013  149 LYS A CB  
1186 C CG  . LYS A 155 ? 0.15566 0.30057 0.27052 0.02053  0.03191  0.12698  149 LYS A CG  
1187 C CD  . LYS A 155 ? 0.24277 0.33823 0.30033 -0.00302 0.00621  0.12436  149 LYS A CD  
1188 C CE  . LYS A 155 ? 0.26556 0.35129 0.32387 -0.01342 0.00991  0.10215  149 LYS A CE  
1189 N NZ  . LYS A 155 ? 0.27211 0.37787 0.39728 0.00080  -0.00883 0.13347  149 LYS A NZ  
1190 N N   . PRO A 156 ? 0.15867 0.24358 0.20443 0.02982  -0.02531 -0.02973 150 PRO A N   
1191 C CA  . PRO A 156 ? 0.17913 0.24731 0.23654 0.05973  -0.00931 -0.02196 150 PRO A CA  
1192 C C   . PRO A 156 ? 0.17052 0.25150 0.23978 0.00796  -0.00708 -0.02832 150 PRO A C   
1193 O O   . PRO A 156 ? 0.16243 0.28204 0.22249 0.01940  0.00711  -0.00558 150 PRO A O   
1194 C CB  . PRO A 156 ? 0.18986 0.24649 0.28088 0.01066  -0.05270 -0.04328 150 PRO A CB  
1195 C CG  . PRO A 156 ? 0.13407 0.27723 0.27352 0.01895  -0.01028 -0.03999 150 PRO A CG  
1196 C CD  . PRO A 156 ? 0.15053 0.25501 0.23027 0.04839  -0.00350 -0.05346 150 PRO A CD  
1197 N N   . SER A 157 ? 0.19320 0.28304 0.24553 0.02135  -0.01427 0.00734  151 SER A N   
1198 C CA  . SER A 157 ? 0.21828 0.29953 0.24931 0.01309  0.00941  0.02498  151 SER A CA  
1199 C C   . SER A 157 ? 0.20180 0.26833 0.20939 0.03874  -0.01423 0.01760  151 SER A C   
1200 O O   . SER A 157 ? 0.26337 0.28222 0.24907 0.04393  -0.03378 0.02238  151 SER A O   
1201 C CB  . SER A 157 ? 0.21818 0.32340 0.28861 0.00922  0.02516  0.07149  151 SER A CB  
1202 O OG  . SER A 157 ? 0.23690 0.32301 0.33254 0.02526  0.01416  0.10372  151 SER A OG  
1203 N N   . ASN A 158 ? 0.16135 0.22276 0.22445 0.05970  0.02421  0.00016  152 ASN A N   
1204 C CA  . ASN A 158 ? 0.14184 0.25648 0.22400 0.03098  0.02515  0.01061  152 ASN A CA  
1205 C C   . ASN A 158 ? 0.15730 0.25981 0.21051 0.03009  -0.01608 0.00396  152 ASN A C   
1206 O O   . ASN A 158 ? 0.22589 0.25783 0.24500 0.00192  0.01903  -0.01736 152 ASN A O   
1207 C CB  . ASN A 158 ? 0.16114 0.27475 0.22349 -0.01235 0.00499  0.00718  152 ASN A CB  
1208 C CG  . ASN A 158 ? 0.20383 0.31880 0.22731 0.02762  -0.02130 0.04668  152 ASN A CG  
1209 O OD1 . ASN A 158 ? 0.22621 0.39070 0.22938 0.03826  -0.04519 0.06409  152 ASN A OD1 
1210 N ND2 . ASN A 158 ? 0.16036 0.32070 0.24873 0.01091  -0.04959 0.03968  152 ASN A ND2 
1211 N N   . LEU A 159 ? 0.14191 0.28508 0.23357 0.01847  -0.02061 -0.00541 153 LEU A N   
1212 C CA  . LEU A 159 ? 0.14877 0.26991 0.19724 0.00585  -0.03906 0.00000  153 LEU A CA  
1213 C C   . LEU A 159 ? 0.14439 0.26276 0.23076 0.03697  -0.05351 -0.01370 153 LEU A C   
1214 O O   . LEU A 159 ? 0.16803 0.27397 0.26658 0.04936  -0.02598 -0.05234 153 LEU A O   
1215 C CB  . LEU A 159 ? 0.16742 0.26119 0.18486 0.04451  -0.06100 0.03304  153 LEU A CB  
1216 C CG  . LEU A 159 ? 0.19021 0.26554 0.19025 0.03820  -0.03670 -0.02590 153 LEU A CG  
1217 C CD1 . LEU A 159 ? 0.23241 0.27263 0.20017 0.01072  -0.03268 -0.01447 153 LEU A CD1 
1218 C CD2 . LEU A 159 ? 0.19833 0.26809 0.22838 0.06999  -0.00869 -0.01513 153 LEU A CD2 
1219 N N   . LEU A 160 ? 0.12675 0.25781 0.22063 0.00051  -0.03952 0.01091  154 LEU A N   
1220 C CA  . LEU A 160 ? 0.13489 0.27338 0.23853 0.01524  -0.04488 0.01760  154 LEU A CA  
1221 C C   . LEU A 160 ? 0.12342 0.31132 0.24465 0.03204  -0.02380 -0.00566 154 LEU A C   
1222 O O   . LEU A 160 ? 0.18924 0.29473 0.23833 0.01940  0.00503  0.00328  154 LEU A O   
1223 C CB  . LEU A 160 ? 0.17744 0.27361 0.26522 0.00897  -0.02934 0.01511  154 LEU A CB  
1224 C CG  . LEU A 160 ? 0.20017 0.27905 0.27304 -0.01038 -0.05241 0.00994  154 LEU A CG  
1225 C CD1 . LEU A 160 ? 0.24303 0.31704 0.27067 -0.00284 -0.05341 0.03902  154 LEU A CD1 
1226 C CD2 . LEU A 160 ? 0.28148 0.28347 0.29816 0.00607  -0.01330 0.04289  154 LEU A CD2 
1227 N N   . LEU A 161 ? 0.14438 0.34258 0.28348 0.04592  0.00628  -0.01769 155 LEU A N   
1228 C CA  . LEU A 161 ? 0.14863 0.38997 0.26071 0.03317  -0.02197 -0.03586 155 LEU A CA  
1229 C C   . LEU A 161 ? 0.17502 0.41956 0.29103 0.04353  0.00020  -0.01762 155 LEU A C   
1230 O O   . LEU A 161 ? 0.19262 0.39554 0.27155 0.06030  -0.03154 -0.02426 155 LEU A O   
1231 C CB  . LEU A 161 ? 0.18049 0.40863 0.24425 0.04548  -0.05609 0.00616  155 LEU A CB  
1232 C CG  . LEU A 161 ? 0.31593 0.43297 0.25173 0.14207  -0.11150 -0.00268 155 LEU A CG  
1233 C CD1 . LEU A 161 ? 0.45139 0.46830 0.35549 0.15255  -0.07438 -0.02038 155 LEU A CD1 
1234 C CD2 . LEU A 161 ? 0.31427 0.43028 0.28542 0.10430  -0.14590 -0.01009 155 LEU A CD2 
1235 N N   . ASN A 162 ? 0.15661 0.45448 0.28583 0.04280  -0.01427 -0.00824 156 ASN A N   
1236 C CA  . ASN A 162 ? 0.12616 0.44175 0.29724 0.04211  -0.00270 -0.00918 156 ASN A CA  
1237 C C   . ASN A 162 ? 0.11837 0.43001 0.32173 0.00673  -0.00050 -0.00466 156 ASN A C   
1238 O O   . ASN A 162 ? 0.15760 0.40523 0.33682 -0.00247 0.00304  -0.00160 156 ASN A O   
1239 C CB  . ASN A 162 ? 0.17163 0.43509 0.33356 0.02054  -0.03828 -0.02127 156 ASN A CB  
1240 C CG  . ASN A 162 ? 0.19800 0.44982 0.39650 0.00876  -0.02400 -0.08246 156 ASN A CG  
1241 O OD1 . ASN A 162 ? 0.16629 0.42690 0.38905 -0.00258 0.00423  -0.03614 156 ASN A OD1 
1242 N ND2 . ASN A 162 ? 0.28756 0.46600 0.48165 -0.00264 -0.01985 -0.13891 156 ASN A ND2 
1243 N N   . THR A 163 ? 0.15092 0.44482 0.36583 0.04163  0.03421  0.02250  157 THR A N   
1244 C CA  . THR A 163 ? 0.15289 0.47806 0.37883 0.06018  0.00588  0.06246  157 THR A CA  
1245 C C   . THR A 163 ? 0.19990 0.44310 0.43377 0.05297  0.07377  0.03550  157 THR A C   
1246 O O   . THR A 163 ? 0.19807 0.42162 0.40777 0.05251  0.04564  0.01550  157 THR A O   
1247 C CB  A THR A 163 ? 0.20205 0.54173 0.40613 0.05742  0.01146  0.10028  157 THR A CB  
1248 C CB  B THR A 163 ? 0.16624 0.48595 0.41878 0.08068  0.00550  0.04583  157 THR A CB  
1249 O OG1 A THR A 163 ? 0.19123 0.58513 0.38514 0.04442  -0.04813 0.10789  157 THR A OG1 
1250 O OG1 B THR A 163 ? 0.25059 0.49899 0.45688 0.08143  0.00725  0.05007  157 THR A OG1 
1251 C CG2 A THR A 163 ? 0.25568 0.54499 0.43996 0.03842  0.05050  0.11188  157 THR A CG2 
1252 C CG2 B THR A 163 ? 0.12375 0.43953 0.38123 0.05040  -0.03053 0.00374  157 THR A CG2 
1253 N N   . THR A 164 ? 0.17242 0.43846 0.44610 0.05447  0.03315  0.02245  158 THR A N   
1254 C CA  . THR A 164 ? 0.17539 0.45078 0.46027 0.03599  0.02128  -0.01226 158 THR A CA  
1255 C C   . THR A 164 ? 0.16277 0.45466 0.41223 0.01881  0.04980  -0.00606 158 THR A C   
1256 O O   . THR A 164 ? 0.21959 0.46334 0.43932 0.01051  0.07864  0.04759  158 THR A O   
1257 C CB  . THR A 164 ? 0.19070 0.46939 0.52779 0.02662  -0.02036 -0.01788 158 THR A CB  
1258 O OG1 . THR A 164 ? 0.22319 0.46579 0.51266 -0.02679 0.03081  -0.02906 158 THR A OG1 
1259 C CG2 . THR A 164 ? 0.21463 0.48898 0.58624 -0.00142 -0.04841 -0.01549 158 THR A CG2 
1260 N N   . CME A 165 ? 0.15059 0.45806 0.34600 0.03599  0.02635  -0.03686 159 CME A N   
1261 C CA  . CME A 165 ? 0.19906 0.46377 0.29813 0.08211  0.01343  -0.02637 159 CME A CA  
1262 C CB  . CME A 165 ? 0.26939 0.55662 0.32789 0.09446  0.05122  -0.05731 159 CME A CB  
1263 S SG  . CME A 165 ? 0.26740 0.62430 0.35434 0.13110  0.00642  -0.07880 159 CME A SG  
1264 S SD  . CME A 165 ? 0.33850 0.63237 0.39349 0.12890  -0.06788 -0.14043 159 CME A SD  
1265 C CE  . CME A 165 ? 0.36152 0.61982 0.34736 0.09880  -0.00325 -0.14446 159 CME A CE  
1266 C CZ  . CME A 165 ? 0.36815 0.60088 0.35802 0.08264  0.00032  -0.16558 159 CME A CZ  
1267 O OH  . CME A 165 ? 0.36056 0.57074 0.36749 0.10699  0.05476  -0.19142 159 CME A OH  
1268 C C   . CME A 165 ? 0.18464 0.39281 0.28231 0.04884  -0.01546 0.00882  159 CME A C   
1269 O O   . CME A 165 ? 0.20336 0.37070 0.28756 0.02216  -0.00015 0.01759  159 CME A O   
1270 N N   . ASP A 166 ? 0.17586 0.33748 0.38215 0.01248  0.05491  -0.04620 160 ASP A N   
1271 C CA  . ASP A 166 ? 0.18587 0.33941 0.39794 -0.00907 0.04283  -0.05585 160 ASP A CA  
1272 C C   . ASP A 166 ? 0.12564 0.32761 0.32307 0.03861  -0.00523 -0.02701 160 ASP A C   
1273 O O   . ASP A 166 ? 0.14201 0.32961 0.31943 0.02126  -0.01178 0.00595  160 ASP A O   
1274 C CB  . ASP A 166 ? 0.18038 0.35543 0.47911 -0.02380 -0.03166 -0.07362 160 ASP A CB  
1275 C CG  . ASP A 166 ? 0.20283 0.37794 0.55133 -0.03352 -0.09943 -0.02679 160 ASP A CG  
1276 O OD1 . ASP A 166 ? 0.25138 0.35884 0.61792 -0.07596 -0.02744 -0.01043 160 ASP A OD1 
1277 O OD2 . ASP A 166 ? 0.22636 0.42994 0.60840 -0.03941 -0.12065 -0.01383 160 ASP A OD2 
1278 N N   . LEU A 167 ? 0.09013 0.30452 0.25086 0.01085  0.01057  -0.02337 161 LEU A N   
1279 C CA  . LEU A 167 ? 0.15105 0.25771 0.22136 -0.03568 -0.00811 -0.02156 161 LEU A CA  
1280 C C   . LEU A 167 ? 0.18148 0.26140 0.22423 -0.01456 0.01159  0.00871  161 LEU A C   
1281 O O   . LEU A 167 ? 0.19760 0.29944 0.23364 -0.00302 0.01504  0.02488  161 LEU A O   
1282 C CB  . LEU A 167 ? 0.16110 0.29223 0.22177 -0.00927 -0.04083 -0.01236 161 LEU A CB  
1283 C CG  . LEU A 167 ? 0.17412 0.31566 0.20933 -0.01317 0.01530  -0.00517 161 LEU A CG  
1284 C CD1 . LEU A 167 ? 0.23252 0.31753 0.17554 -0.02381 -0.01171 -0.01428 161 LEU A CD1 
1285 C CD2 . LEU A 167 ? 0.20949 0.32673 0.21970 0.01942  0.06885  0.01174  161 LEU A CD2 
1286 N N   . LYS A 168 ? 0.17188 0.24103 0.18142 -0.01653 0.03209  0.01022  162 LYS A N   
1287 C CA  . LYS A 168 ? 0.14441 0.24415 0.20270 -0.00464 -0.02014 0.01944  162 LYS A CA  
1288 C C   . LYS A 168 ? 0.12101 0.22773 0.26210 0.00062  -0.04398 0.00179  162 LYS A C   
1289 O O   . LYS A 168 ? 0.15626 0.23649 0.29528 0.01457  0.02342  0.01293  162 LYS A O   
1290 C CB  . LYS A 168 ? 0.16020 0.29387 0.23239 -0.00905 -0.03827 0.01641  162 LYS A CB  
1291 C CG  . LYS A 168 ? 0.20940 0.31627 0.28698 -0.05981 -0.06924 -0.00022 162 LYS A CG  
1292 C CD  . LYS A 168 ? 0.21234 0.34424 0.34368 -0.04237 -0.10041 0.02235  162 LYS A CD  
1293 C CE  . LYS A 168 ? 0.29321 0.35223 0.42336 -0.01784 -0.05047 0.03578  162 LYS A CE  
1294 N NZ  . LYS A 168 ? 0.30601 0.37748 0.47363 -0.00145 -0.06055 0.01996  162 LYS A NZ  
1295 N N   . ILE A 169 ? 0.12713 0.22667 0.21890 0.03128  -0.05479 -0.00739 163 ILE A N   
1296 C CA  . ILE A 169 ? 0.15366 0.23844 0.24499 0.02998  -0.01741 0.00973  163 ILE A CA  
1297 C C   . ILE A 169 ? 0.14324 0.23507 0.25394 0.00415  -0.03031 0.01517  163 ILE A C   
1298 O O   . ILE A 169 ? 0.20854 0.22105 0.24996 0.01505  -0.00637 0.00739  163 ILE A O   
1299 C CB  . ILE A 169 ? 0.15327 0.21260 0.21019 0.00773  0.01276  0.03475  163 ILE A CB  
1300 C CG1 . ILE A 169 ? 0.15942 0.24080 0.18656 0.02564  0.00896  0.06931  163 ILE A CG1 
1301 C CG2 . ILE A 169 ? 0.11006 0.23889 0.23161 0.00078  -0.00370 0.00827  163 ILE A CG2 
1302 C CD1 . ILE A 169 ? 0.17980 0.25370 0.22971 0.05427  -0.00060 0.05854  163 ILE A CD1 
1303 N N   . CYS A 170 ? 0.16840 0.25294 0.21017 0.00709  0.00225  0.04608  164 CYS A N   
1304 C CA  A CYS A 170 ? 0.17190 0.29558 0.21013 0.02450  -0.02804 0.03219  164 CYS A CA  
1305 C CA  B CYS A 170 ? 0.18072 0.27293 0.21150 0.01542  -0.01290 0.05303  164 CYS A CA  
1306 C C   . CYS A 170 ? 0.16807 0.30590 0.17829 0.00906  -0.01905 0.03360  164 CYS A C   
1307 O O   . CYS A 170 ? 0.15038 0.30627 0.21727 -0.00442 -0.01363 0.02466  164 CYS A O   
1308 C CB  A CYS A 170 ? 0.21015 0.34712 0.18817 0.02700  -0.03076 0.04483  164 CYS A CB  
1309 C CB  B CYS A 170 ? 0.20400 0.26315 0.23856 0.02395  -0.00698 0.08332  164 CYS A CB  
1310 S SG  A CYS A 170 ? 0.22425 0.36656 0.24304 0.01662  -0.02269 0.03851  164 CYS A SG  
1311 S SG  B CYS A 170 ? 0.22363 0.24334 0.26394 0.02788  0.00722  0.10467  164 CYS A SG  
1312 N N   . ASP A 171 ? 0.18237 0.33329 0.20833 0.03501  0.04749  0.08272  165 ASP A N   
1313 C CA  . ASP A 171 ? 0.20272 0.34493 0.27539 0.03250  0.03849  0.08272  165 ASP A CA  
1314 C C   . ASP A 171 ? 0.24409 0.39375 0.26871 0.03400  0.04929  0.05840  165 ASP A C   
1315 O O   . ASP A 171 ? 0.28456 0.42492 0.27908 0.03567  0.01122  0.03213  165 ASP A O   
1316 C CB  . ASP A 171 ? 0.23249 0.34137 0.32408 -0.04147 0.05836  0.08250  165 ASP A CB  
1317 C CG  . ASP A 171 ? 0.25926 0.35270 0.36943 -0.02308 0.06843  0.06928  165 ASP A CG  
1318 O OD1 . ASP A 171 ? 0.23401 0.35672 0.33556 0.02633  0.04815  0.10608  165 ASP A OD1 
1319 O OD2 . ASP A 171 ? 0.31946 0.32440 0.40367 -0.06282 0.07380  0.05462  165 ASP A OD2 
1320 N N   . PHE A 172 ? 0.21251 0.38159 0.26191 0.02460  0.09712  0.09057  166 PHE A N   
1321 C CA  . PHE A 172 ? 0.24894 0.36665 0.26279 0.05774  0.02988  0.10478  166 PHE A CA  
1322 C C   . PHE A 172 ? 0.27813 0.38959 0.24743 0.06118  0.00131  0.10623  166 PHE A C   
1323 O O   . PHE A 172 ? 0.27296 0.43299 0.24506 0.06454  0.02259  0.05325  166 PHE A O   
1324 C CB  . PHE A 172 ? 0.28717 0.33344 0.25287 0.01680  0.05102  0.08717  166 PHE A CB  
1325 C CG  . PHE A 172 ? 0.25624 0.29043 0.22731 -0.01878 0.02303  0.06293  166 PHE A CG  
1326 C CD1 . PHE A 172 ? 0.25718 0.30551 0.26492 -0.04296 0.01328  0.07111  166 PHE A CD1 
1327 C CD2 . PHE A 172 ? 0.28718 0.29260 0.22996 -0.01602 0.00359  0.01850  166 PHE A CD2 
1328 C CE1 . PHE A 172 ? 0.28411 0.31388 0.27907 -0.06367 -0.00452 0.02530  166 PHE A CE1 
1329 C CE2 . PHE A 172 ? 0.26165 0.29007 0.24189 -0.03423 0.00384  0.00467  166 PHE A CE2 
1330 C CZ  . PHE A 172 ? 0.26558 0.30251 0.24148 -0.02788 -0.02779 0.01840  166 PHE A CZ  
1331 N N   . GLY A 173 ? 0.24393 0.35814 0.27971 0.02419  0.04882  0.12991  167 GLY A N   
1332 C CA  . GLY A 173 ? 0.27053 0.36123 0.25687 -0.00996 -0.01359 0.13206  167 GLY A CA  
1333 C C   . GLY A 173 ? 0.29225 0.35576 0.23180 0.00046  -0.01058 0.12804  167 GLY A C   
1334 O O   . GLY A 173 ? 0.30127 0.40653 0.25009 0.00286  0.02514  0.09050  167 GLY A O   
1335 N N   . LEU A 174 ? 0.30713 0.32851 0.22130 0.01572  -0.00999 0.08365  168 LEU A N   
1336 C CA  . LEU A 174 ? 0.38848 0.33223 0.20203 -0.01053 0.01370  0.00780  168 LEU A CA  
1337 C C   . LEU A 174 ? 0.31541 0.34619 0.19811 -0.01766 0.01361  0.01321  168 LEU A C   
1338 O O   . LEU A 174 ? 0.30064 0.36921 0.22180 -0.05961 0.01366  -0.00364 168 LEU A O   
1339 C CB  . LEU A 174 ? 0.53395 0.37238 0.26868 0.00797  0.04840  -0.09317 168 LEU A CB  
1340 C CG  . LEU A 174 ? 0.67001 0.45332 0.33878 -0.01239 0.13524  -0.10839 168 LEU A CG  
1341 C CD1 . LEU A 174 ? 0.71670 0.47523 0.39138 -0.02671 0.11616  -0.12857 168 LEU A CD1 
1342 C CD2 . LEU A 174 ? 0.74897 0.47625 0.34546 -0.01190 0.15403  -0.09551 168 LEU A CD2 
1343 N N   . ALA A 175 ? 0.21766 0.31855 0.18542 -0.00862 -0.00086 0.00725  169 ALA A N   
1344 C CA  . ALA A 175 ? 0.20380 0.30739 0.20517 0.00347  -0.02513 0.03543  169 ALA A CA  
1345 C C   . ALA A 175 ? 0.26238 0.33286 0.21770 0.06394  0.04276  0.03806  169 ALA A C   
1346 O O   . ALA A 175 ? 0.33546 0.38649 0.23593 0.07134  0.08315  0.08636  169 ALA A O   
1347 C CB  . ALA A 175 ? 0.27512 0.31548 0.19670 -0.00540 -0.03126 0.03100  169 ALA A CB  
1348 N N   . ARG A 176 ? 0.22110 0.31070 0.21749 0.03706  0.02029  0.01877  170 ARG A N   
1349 C CA  . ARG A 176 ? 0.22090 0.28454 0.24601 0.02813  0.01834  0.00174  170 ARG A CA  
1350 C C   . ARG A 176 ? 0.20350 0.28351 0.23556 0.01606  0.05530  0.00089  170 ARG A C   
1351 O O   . ARG A 176 ? 0.23471 0.28976 0.22979 -0.00460 0.07547  -0.01119 170 ARG A O   
1352 C CB  . ARG A 176 ? 0.23829 0.28224 0.33381 -0.00639 0.00725  0.02819  170 ARG A CB  
1353 C CG  . ARG A 176 ? 0.35231 0.27577 0.35789 -0.00276 0.06473  0.09899  170 ARG A CG  
1354 C CD  . ARG A 176 ? 0.40274 0.31910 0.38227 -0.01247 0.02980  0.08291  170 ARG A CD  
1355 N NE  . ARG A 176 ? 0.46756 0.33454 0.37830 0.01624  0.06243  0.07316  170 ARG A NE  
1356 C CZ  . ARG A 176 ? 0.42691 0.33714 0.33513 0.03243  0.07822  0.04974  170 ARG A CZ  
1357 N NH1 . ARG A 176 ? 0.37381 0.34761 0.27390 0.05100  0.08098  0.03388  170 ARG A NH1 
1358 N NH2 . ARG A 176 ? 0.44174 0.33683 0.34109 0.01929  0.09127  0.03730  170 ARG A NH2 
1359 N N   . VAL A 177 ? 0.21789 0.30123 0.27344 0.05328  0.06624  -0.01140 171 VAL A N   
1360 C CA  . VAL A 177 ? 0.19798 0.32154 0.28928 0.03510  0.06363  -0.03191 171 VAL A CA  
1361 C C   . VAL A 177 ? 0.21913 0.33158 0.30791 -0.00194 0.07760  -0.02307 171 VAL A C   
1362 O O   . VAL A 177 ? 0.20208 0.34034 0.38671 -0.02723 0.07473  -0.01863 171 VAL A O   
1363 C CB  . VAL A 177 ? 0.28645 0.35230 0.26846 0.03808  0.04403  -0.03468 171 VAL A CB  
1364 C CG1 . VAL A 177 ? 0.33706 0.34066 0.32000 0.08653  0.06018  -0.03014 171 VAL A CG1 
1365 C CG2 . VAL A 177 ? 0.35280 0.38183 0.26746 0.00986  0.05922  -0.05928 171 VAL A CG2 
1366 N N   . ALA A 178 ? 0.21373 0.33362 0.27050 0.03298  0.04682  -0.02956 172 ALA A N   
1367 C CA  . ALA A 178 ? 0.21477 0.37484 0.28140 0.05380  -0.00669 -0.01173 172 ALA A CA  
1368 C C   . ALA A 178 ? 0.18849 0.37985 0.31958 0.00545  -0.04029 -0.06261 172 ALA A C   
1369 O O   . ALA A 178 ? 0.20559 0.38180 0.36790 -0.01941 0.00397  -0.11578 172 ALA A O   
1370 C CB  . ALA A 178 ? 0.26161 0.40881 0.27914 0.07378  0.02857  0.01555  172 ALA A CB  
1371 N N   . ASP A 179 ? 0.17547 0.38417 0.39241 -0.00559 -0.00128 -0.09183 173 ASP A N   
1372 C CA  . ASP A 179 ? 0.16418 0.41297 0.41257 -0.01860 -0.02168 -0.11998 173 ASP A CA  
1373 C C   . ASP A 179 ? 0.21913 0.40163 0.44688 0.01532  0.02570  -0.08690 173 ASP A C   
1374 O O   . ASP A 179 ? 0.21323 0.41020 0.44113 0.03043  0.01048  -0.08644 173 ASP A O   
1375 C CB  . ASP A 179 ? 0.22807 0.45817 0.49879 -0.05169 0.07227  -0.13754 173 ASP A CB  
1376 C CG  . ASP A 179 ? 0.31799 0.51910 0.56864 -0.06643 0.08500  -0.13380 173 ASP A CG  
1377 O OD1 . ASP A 179 ? 0.31235 0.51640 0.62672 -0.02126 0.08758  -0.12490 173 ASP A OD1 
1378 O OD2 . ASP A 179 ? 0.35571 0.57597 0.56134 -0.10702 0.10334  -0.14080 173 ASP A OD2 
1379 N N   . PRO A 180 ? 0.26508 0.39119 0.46269 0.00447  -0.01022 -0.03086 174 PRO A N   
1380 C CA  . PRO A 180 ? 0.28465 0.41047 0.50762 0.00577  -0.06017 -0.03384 174 PRO A CA  
1381 C C   . PRO A 180 ? 0.28721 0.43421 0.58633 0.04564  -0.10902 -0.12398 174 PRO A C   
1382 O O   . PRO A 180 ? 0.28323 0.43126 0.58980 0.06415  -0.18879 -0.14509 174 PRO A O   
1383 C CB  . PRO A 180 ? 0.35684 0.39736 0.47054 -0.02043 -0.01129 0.02114  174 PRO A CB  
1384 C CG  . PRO A 180 ? 0.41011 0.38581 0.43858 -0.03726 0.03474  0.02391  174 PRO A CG  
1385 C CD  . PRO A 180 ? 0.36042 0.37324 0.46685 -0.02045 0.03286  0.01892  174 PRO A CD  
1386 N N   . ASP A 181 ? 0.27900 0.42507 0.66957 0.08321  -0.08802 -0.16216 175 ASP A N   
1387 C CA  . ASP A 181 ? 0.24039 0.46239 0.66618 0.07553  -0.11517 -0.18360 175 ASP A CA  
1388 C C   . ASP A 181 ? 0.24121 0.49167 0.63284 0.04579  -0.06218 -0.19049 175 ASP A C   
1389 O O   . ASP A 181 ? 0.21798 0.55619 0.67724 0.02787  -0.02856 -0.16441 175 ASP A O   
1390 C CB  . ASP A 181 ? 0.28791 0.48435 0.70531 0.05799  -0.11828 -0.20296 175 ASP A CB  
1391 C CG  . ASP A 181 ? 0.38259 0.51271 0.71922 0.05851  -0.07922 -0.20788 175 ASP A CG  
1392 O OD1 . ASP A 181 ? 0.38227 0.53268 0.71931 0.08157  -0.04777 -0.19588 175 ASP A OD1 
1393 O OD2 . ASP A 181 ? 0.46739 0.52475 0.75029 0.04816  -0.05152 -0.18967 175 ASP A OD2 
1394 N N   . HIS A 182 ? 0.25890 0.44709 0.55128 0.01980  -0.01959 -0.20962 176 HIS A N   
1395 C CA  . HIS A 182 ? 0.26979 0.44471 0.50095 -0.04608 0.01487  -0.20894 176 HIS A CA  
1396 C C   . HIS A 182 ? 0.28636 0.40992 0.49062 -0.01784 0.09641  -0.15528 176 HIS A C   
1397 O O   . HIS A 182 ? 0.27616 0.45484 0.52695 -0.00887 0.13852  -0.11080 176 HIS A O   
1398 C CB  . HIS A 182 ? 0.29880 0.48212 0.47852 -0.07029 0.00571  -0.25825 176 HIS A CB  
1399 C CG  . HIS A 182 ? 0.34627 0.51206 0.52120 -0.02762 0.05105  -0.27457 176 HIS A CG  
1400 N ND1 . HIS A 182 ? 0.38511 0.52715 0.56705 0.01396  0.10610  -0.28413 176 HIS A ND1 
1401 C CD2 . HIS A 182 ? 0.40082 0.52954 0.54392 0.00130  0.09741  -0.27010 176 HIS A CD2 
1402 C CE1 . HIS A 182 ? 0.40543 0.54747 0.56767 0.02446  0.13477  -0.27452 176 HIS A CE1 
1403 N NE2 . HIS A 182 ? 0.40897 0.55799 0.56225 -0.00236 0.11429  -0.26884 176 HIS A NE2 
1404 N N   . ASP A 183 ? 0.25295 0.36212 0.42038 -0.02210 0.07731  -0.13093 177 ASP A N   
1405 C CA  . ASP A 183 ? 0.22830 0.36587 0.40191 0.00539  0.05687  -0.09559 177 ASP A CA  
1406 C C   . ASP A 183 ? 0.21568 0.37543 0.39496 0.00234  0.00072  -0.07183 177 ASP A C   
1407 O O   . ASP A 183 ? 0.20225 0.38612 0.39148 -0.01058 0.02586  -0.07192 177 ASP A O   
1408 C CB  . ASP A 183 ? 0.19487 0.34713 0.44193 0.01752  0.02000  -0.09072 177 ASP A CB  
1409 C CG  . ASP A 183 ? 0.24292 0.36090 0.47969 0.00796  0.01676  -0.09410 177 ASP A CG  
1410 O OD1 . ASP A 183 ? 0.24099 0.36920 0.50835 0.04045  -0.07256 -0.12967 177 ASP A OD1 
1411 O OD2 . ASP A 183 ? 0.29788 0.34586 0.49200 -0.00027 0.08225  -0.08919 177 ASP A OD2 
1412 N N   . HIS A 184 ? 0.20759 0.37928 0.39484 0.02712  -0.03959 -0.06045 178 HIS A N   
1413 C CA  A HIS A 184 ? 0.19635 0.35674 0.40903 0.01740  -0.03130 -0.08806 178 HIS A CA  
1414 C CA  B HIS A 184 ? 0.19788 0.35731 0.40955 0.01685  -0.03111 -0.08732 178 HIS A CA  
1415 C C   . HIS A 184 ? 0.21146 0.32505 0.40906 0.00727  0.09411  -0.11654 178 HIS A C   
1416 O O   . HIS A 184 ? 0.31809 0.34723 0.44025 -0.00017 0.14345  -0.14230 178 HIS A O   
1417 C CB  A HIS A 184 ? 0.25943 0.39937 0.43356 0.03906  -0.07473 -0.02729 178 HIS A CB  
1418 C CB  B HIS A 184 ? 0.26081 0.40119 0.43513 0.03959  -0.07375 -0.02572 178 HIS A CB  
1419 C CG  A HIS A 184 ? 0.38177 0.44772 0.46500 0.06312  -0.01095 0.02851  178 HIS A CG  
1420 C CG  B HIS A 184 ? 0.38697 0.44860 0.46728 0.06136  -0.00408 0.02492  178 HIS A CG  
1421 N ND1 A HIS A 184 ? 0.45251 0.46487 0.48360 0.06308  0.03165  0.04557  178 HIS A ND1 
1422 N ND1 B HIS A 184 ? 0.44654 0.46099 0.48322 0.06797  0.03263  0.04348  178 HIS A ND1 
1423 C CD2 A HIS A 184 ? 0.45638 0.46015 0.48261 0.07709  0.06162  0.05526  178 HIS A CD2 
1424 C CD2 B HIS A 184 ? 0.46155 0.46408 0.48693 0.07398  0.06383  0.05038  178 HIS A CD2 
1425 C CE1 A HIS A 184 ? 0.48597 0.47059 0.49433 0.06330  0.09313  0.04478  178 HIS A CE1 
1426 C CE1 B HIS A 184 ? 0.48962 0.47307 0.49675 0.05661  0.09234  0.04070  178 HIS A CE1 
1427 N NE2 A HIS A 184 ? 0.49842 0.47072 0.48851 0.06624  0.10650  0.04388  178 HIS A NE2 
1428 N NE2 B HIS A 184 ? 0.50112 0.47009 0.48665 0.06487  0.10732  0.03441  178 HIS A NE2 
1429 N N   . THR A 185 ? 0.22816 0.31454 0.37938 -0.03877 0.06544  -0.06937 179 THR A N   
1430 C CA  . THR A 185 ? 0.21972 0.31499 0.32018 -0.04796 0.01038  -0.07406 179 THR A CA  
1431 C C   . THR A 185 ? 0.21139 0.33398 0.30890 -0.02172 0.01321  -0.05450 179 THR A C   
1432 O O   . THR A 185 ? 0.17969 0.35247 0.33575 -0.03096 0.05809  -0.09910 179 THR A O   
1433 C CB  . THR A 185 ? 0.23951 0.34631 0.32930 -0.02101 0.01367  -0.01843 179 THR A CB  
1434 O OG1 . THR A 185 ? 0.36290 0.39071 0.31677 -0.02811 0.04909  -0.01062 179 THR A OG1 
1435 C CG2 . THR A 185 ? 0.19254 0.36478 0.37627 -0.00352 -0.01248 0.00200  179 THR A CG2 
1436 N N   . GLY A 186 ? 0.21952 0.34809 0.34912 -0.01533 0.03149  -0.09527 180 GLY A N   
1437 C CA  . GLY A 186 ? 0.24209 0.34872 0.36250 -0.00165 -0.01343 -0.08386 180 GLY A CA  
1438 C C   . GLY A 186 ? 0.28156 0.33475 0.33223 0.00428  -0.01565 -0.06206 180 GLY A C   
1439 O O   . GLY A 186 ? 0.30081 0.35315 0.35490 0.02532  -0.04307 -0.05725 180 GLY A O   
1440 N N   . PHE A 187 ? 0.31027 0.30525 0.30111 -0.00384 -0.02084 -0.03591 181 PHE A N   
1441 C CA  . PHE A 187 ? 0.27713 0.30310 0.29774 -0.01558 -0.02356 -0.02671 181 PHE A CA  
1442 C C   . PHE A 187 ? 0.25382 0.29264 0.30620 -0.06226 -0.10411 0.00599  181 PHE A C   
1443 O O   . PHE A 187 ? 0.38892 0.31322 0.34616 -0.08642 0.00674  0.03856  181 PHE A O   
1444 C CB  . PHE A 187 ? 0.22130 0.31305 0.27813 -0.00438 -0.08018 -0.06093 181 PHE A CB  
1445 C CG  . PHE A 187 ? 0.24108 0.29549 0.27195 -0.00242 -0.02777 -0.02131 181 PHE A CG  
1446 C CD1 . PHE A 187 ? 0.25157 0.29187 0.23963 0.01794  -0.04607 0.04647  181 PHE A CD1 
1447 C CD2 . PHE A 187 ? 0.31063 0.31107 0.28061 -0.01099 0.00995  -0.04185 181 PHE A CD2 
1448 C CE1 . PHE A 187 ? 0.29092 0.29237 0.28151 -0.02473 -0.04028 0.04573  181 PHE A CE1 
1449 C CE2 . PHE A 187 ? 0.29248 0.31921 0.25836 -0.03095 0.01962  -0.03126 181 PHE A CE2 
1450 C CZ  . PHE A 187 ? 0.28238 0.31774 0.24011 -0.03506 -0.02651 0.02362  181 PHE A CZ  
1451 N N   . LEU A 188 ? 0.27006 0.27689 0.32064 -0.00690 -0.09565 0.02030  182 LEU A N   
1452 C CA  . LEU A 188 ? 0.35156 0.32936 0.33262 -0.05067 -0.09174 0.01242  182 LEU A CA  
1453 C C   . LEU A 188 ? 0.37649 0.39248 0.37124 -0.06671 -0.06809 0.00492  182 LEU A C   
1454 O O   . LEU A 188 ? 0.43154 0.40369 0.37904 -0.09053 -0.10301 0.06596  182 LEU A O   
1455 C CB  . LEU A 188 ? 0.46040 0.32861 0.36587 -0.05545 -0.09012 0.04877  182 LEU A CB  
1456 C CG  . LEU A 188 ? 0.53089 0.33488 0.36742 -0.03941 -0.11651 0.00713  182 LEU A CG  
1457 C CD1 . LEU A 188 ? 0.56315 0.38746 0.38170 -0.02074 -0.13060 0.00796  182 LEU A CD1 
1458 C CD2 . LEU A 188 ? 0.63348 0.34345 0.40976 0.01482  -0.01312 -0.00624 182 LEU A CD2 
1459 N N   A THR A 189 ? 0.32869 0.37600 0.33972 -0.05101 -0.04939 -0.01889 183 THR A N   
1460 N N   B THR A 189 ? 0.35176 0.43368 0.33107 -0.07775 -0.04205 -0.05020 183 THR A N   
1461 C CA  A THR A 189 ? 0.28635 0.35865 0.31281 -0.01109 -0.06238 0.00212  183 THR A CA  
1462 C CA  B THR A 189 ? 0.30952 0.47150 0.33625 -0.06803 -0.06627 -0.05120 183 THR A CA  
1463 C C   A THR A 189 ? 0.25317 0.31943 0.25755 0.00250  -0.08495 0.02373  183 THR A C   
1464 C C   B THR A 189 ? 0.31487 0.50425 0.36497 -0.05397 -0.07022 -0.00679 183 THR A C   
1465 O O   A THR A 189 ? 0.19530 0.31951 0.29849 0.03151  -0.09942 0.04899  183 THR A O   
1466 O O   B THR A 189 ? 0.30360 0.52227 0.38347 -0.03117 -0.07903 0.07226  183 THR A O   
1467 C CB  A THR A 189 ? 0.32673 0.38010 0.39601 -0.00758 -0.00661 0.04143  183 THR A CB  
1468 C CB  B THR A 189 ? 0.29363 0.47264 0.35946 -0.11481 -0.04776 -0.06930 183 THR A CB  
1469 O OG1 A THR A 189 ? 0.39619 0.41271 0.44074 -0.01082 0.04414  0.03374  183 THR A OG1 
1470 O OG1 B THR A 189 ? 0.32022 0.45528 0.35214 -0.09159 0.00862  -0.01637 183 THR A OG1 
1471 C CG2 A THR A 189 ? 0.26504 0.36769 0.42913 0.00018  -0.01527 0.05977  183 THR A CG2 
1472 C CG2 B THR A 189 ? 0.33601 0.47954 0.38393 -0.14325 -0.01741 -0.08694 183 THR A CG2 
1473 N N   A GLU A 190 ? 0.27623 0.29250 0.22563 -0.00921 -0.09454 0.04708  184 GLU A N   
1474 N N   B GLU A 190 ? 0.32097 0.51880 0.40327 -0.06996 -0.08926 -0.02862 184 GLU A N   
1475 C CA  A GLU A 190 ? 0.30831 0.31752 0.27112 -0.04885 -0.07049 0.03996  184 GLU A CA  
1476 C CA  B GLU A 190 ? 0.31596 0.54299 0.47057 -0.04945 -0.08803 -0.01623 184 GLU A CA  
1477 C C   A GLU A 190 ? 0.25007 0.30868 0.23611 -0.04096 -0.04972 0.06085  184 GLU A C   
1478 C C   B GLU A 190 ? 0.37368 0.53897 0.50079 -0.00891 -0.08934 0.01281  184 GLU A C   
1479 O O   A GLU A 190 ? 0.29092 0.30878 0.22538 -0.03863 -0.00944 0.05108  184 GLU A O   
1480 O O   B GLU A 190 ? 0.35123 0.53521 0.47876 0.01800  -0.10313 0.04388  184 GLU A O   
1481 C CB  A GLU A 190 ? 0.36525 0.35312 0.36589 -0.08349 -0.06994 0.04918  184 GLU A CB  
1482 C CB  B GLU A 190 ? 0.34500 0.57616 0.52241 -0.05079 -0.00994 -0.01740 184 GLU A CB  
1483 C CG  A GLU A 190 ? 0.45329 0.40129 0.45712 -0.09584 -0.02300 0.05565  184 GLU A CG  
1484 C CG  B GLU A 190 ? 0.49787 0.62109 0.55323 -0.03072 0.03936  0.02153  184 GLU A CG  
1485 C CD  A GLU A 190 ? 0.52523 0.44609 0.51855 -0.08444 -0.01570 0.07474  184 GLU A CD  
1486 C CD  B GLU A 190 ? 0.57142 0.66075 0.56855 -0.00518 0.08194  0.05559  184 GLU A CD  
1487 O OE1 A GLU A 190 ? 0.54637 0.45963 0.54974 -0.07237 -0.01180 0.08407  184 GLU A OE1 
1488 O OE1 B GLU A 190 ? 0.53806 0.65794 0.51699 0.02418  0.02254  0.07628  184 GLU A OE1 
1489 O OE2 A GLU A 190 ? 0.55459 0.46920 0.53838 -0.08461 -0.01464 0.07296  184 GLU A OE2 
1490 O OE2 B GLU A 190 ? 0.59463 0.69152 0.66319 0.00368  0.13273  0.06441  184 GLU A OE2 
1491 N N   A TYR A 191 ? 0.16624 0.31879 0.23980 -0.03128 -0.02002 0.07164  185 TYR A N   
1492 N N   B TYR A 191 ? 0.41884 0.54789 0.52444 0.00430  -0.09483 0.00716  185 TYR A N   
1493 C CA  A TYR A 191 ? 0.18788 0.32538 0.24851 -0.07540 -0.03973 0.02554  185 TYR A CA  
1494 C CA  B TYR A 191 ? 0.49428 0.56687 0.57875 0.00191  -0.00062 -0.00995 185 TYR A CA  
1495 C C   A TYR A 191 ? 0.26926 0.36821 0.26158 -0.06292 -0.00831 0.03232  185 TYR A C   
1496 C C   B TYR A 191 ? 0.51644 0.52733 0.52637 0.01534  0.08926  -0.01600 185 TYR A C   
1497 O O   A TYR A 191 ? 0.34469 0.37450 0.33031 -0.04265 0.02163  0.02125  185 TYR A O   
1498 O O   B TYR A 191 ? 0.60981 0.54782 0.58222 0.01601  0.11451  -0.01203 185 TYR A O   
1499 C CB  A TYR A 191 ? 0.15336 0.28870 0.25394 -0.07893 -0.07995 0.01363  185 TYR A CB  
1500 C CB  B TYR A 191 ? 0.56039 0.63249 0.63530 0.00889  -0.01621 -0.03728 185 TYR A CB  
1501 C CG  A TYR A 191 ? 0.20736 0.25408 0.26510 -0.09123 -0.07040 -0.02388 185 TYR A CG  
1502 C CG  B TYR A 191 ? 0.61025 0.68421 0.69145 0.00493  0.00701  -0.08288 185 TYR A CG  
1503 C CD1 A TYR A 191 ? 0.24148 0.24352 0.24675 -0.05873 -0.07872 0.00608  185 TYR A CD1 
1504 C CD1 B TYR A 191 ? 0.65450 0.70647 0.72064 0.00632  0.04690  -0.11015 185 TYR A CD1 
1505 C CD2 A TYR A 191 ? 0.19224 0.24262 0.26504 -0.07942 -0.09806 -0.01709 185 TYR A CD2 
1506 C CD2 B TYR A 191 ? 0.61390 0.69894 0.70768 0.01069  0.02397  -0.10583 185 TYR A CD2 
1507 C CE1 A TYR A 191 ? 0.25567 0.23620 0.22946 -0.06264 -0.07247 -0.00465 185 TYR A CE1 
1508 C CE1 B TYR A 191 ? 0.67598 0.71605 0.72910 0.00799  0.05145  -0.12782 185 TYR A CE1 
1509 C CE2 A TYR A 191 ? 0.22798 0.24389 0.27599 -0.07384 -0.06219 -0.01148 185 TYR A CE2 
1510 C CE2 B TYR A 191 ? 0.64943 0.71631 0.72153 0.01328  0.03579  -0.11979 185 TYR A CE2 
1511 C CZ  A TYR A 191 ? 0.26118 0.23554 0.26440 -0.07596 -0.06849 -0.00616 185 TYR A CZ  
1512 C CZ  B TYR A 191 ? 0.68776 0.72300 0.73353 0.01015  0.03953  -0.13063 185 TYR A CZ  
1513 O OH  A TYR A 191 ? 0.28407 0.26583 0.31014 -0.07495 -0.07371 0.01195  185 TYR A OH  
1514 O OH  B TYR A 191 ? 0.71017 0.72702 0.74256 0.01529  0.02391  -0.13072 185 TYR A OH  
1515 N N   A VAL A 192 ? 0.27738 0.39606 0.17791 -0.07089 0.02971  0.00574  186 VAL A N   
1516 N N   B VAL A 192 ? 0.43325 0.46947 0.39561 0.01444  0.11068  -0.03977 186 VAL A N   
1517 C CA  A VAL A 192 ? 0.23750 0.43047 0.16120 -0.05561 0.01269  0.01217  186 VAL A CA  
1518 C CA  B VAL A 192 ? 0.30366 0.41744 0.32632 0.00767  0.05476  -0.05738 186 VAL A CA  
1519 C C   A VAL A 192 ? 0.17200 0.40267 0.16946 -0.01965 -0.00205 0.01526  186 VAL A C   
1520 C C   B VAL A 192 ? 0.24281 0.38987 0.32332 0.03203  -0.00856 -0.05445 186 VAL A C   
1521 O O   A VAL A 192 ? 0.24975 0.43405 0.20443 -0.02458 0.03553  0.05656  186 VAL A O   
1522 O O   B VAL A 192 ? 0.25022 0.42095 0.34195 0.00538  0.00973  -0.07673 186 VAL A O   
1523 C CB  A VAL A 192 ? 0.24578 0.48056 0.14445 -0.04900 -0.01766 0.05650  186 VAL A CB  
1524 C CB  B VAL A 192 ? 0.30806 0.41858 0.36392 -0.01216 0.06736  -0.02460 186 VAL A CB  
1525 C CG1 A VAL A 192 ? 0.24378 0.48553 0.16685 -0.04681 -0.03019 0.07100  186 VAL A CG1 
1526 C CG1 B VAL A 192 ? 0.30738 0.42793 0.38364 -0.00282 0.07343  -0.00801 186 VAL A CG1 
1527 C CG2 A VAL A 192 ? 0.34514 0.50378 0.19225 -0.02374 0.04199  0.07123  186 VAL A CG2 
1528 C CG2 B VAL A 192 ? 0.32089 0.42808 0.37232 -0.03675 0.07656  0.00002  186 VAL A CG2 
1529 N N   A ALA A 193 ? 0.11178 0.34408 0.17770 0.00118  0.01587  0.01060  187 ALA A N   
1530 N N   B ALA A 193 ? 0.19344 0.33477 0.33766 0.08130  -0.03398 -0.04016 187 ALA A N   
1531 C CA  A ALA A 193 ? 0.13080 0.30727 0.18409 0.04148  -0.00678 0.02851  187 ALA A CA  
1532 C CA  B ALA A 193 ? 0.23474 0.29859 0.35215 0.07254  -0.10460 -0.00035 187 ALA A CA  
1533 C C   A ALA A 193 ? 0.18595 0.31938 0.25278 0.04595  0.00511  -0.00937 187 ALA A C   
1534 C C   B ALA A 193 ? 0.22601 0.31338 0.35918 0.11008  -0.12244 -0.05382 187 ALA A C   
1535 O O   A ALA A 193 ? 0.28497 0.32442 0.22458 0.10639  0.07669  0.05831  187 ALA A O   
1536 O O   B ALA A 193 ? 0.30320 0.31093 0.45125 0.11258  -0.00116 -0.02802 187 ALA A O   
1537 C CB  A ALA A 193 ? 0.18950 0.28822 0.21800 0.02380  -0.01210 -0.02682 187 ALA A CB  
1538 C CB  B ALA A 193 ? 0.26475 0.26703 0.42029 0.02837  -0.17021 0.01216  187 ALA A CB  
1539 N N   . THR A 194 ? 0.25159 0.35487 0.41456 0.04999  -0.05211 -0.09177 188 THR A N   
1540 C CA  . THR A 194 ? 0.19838 0.31954 0.37942 0.02611  -0.10151 -0.09315 188 THR A CA  
1541 C C   . THR A 194 ? 0.27418 0.26679 0.43538 0.01697  -0.11083 -0.08147 188 THR A C   
1542 O O   . THR A 194 ? 0.30714 0.24654 0.44369 0.03900  -0.16030 -0.06082 188 THR A O   
1543 C CB  . THR A 194 ? 0.20396 0.31951 0.29937 0.00167  -0.06355 -0.03242 188 THR A CB  
1544 O OG1 . THR A 194 ? 0.25159 0.33867 0.24666 -0.02753 -0.01341 -0.00858 188 THR A OG1 
1545 C CG2 . THR A 194 ? 0.23431 0.33450 0.35506 0.01234  -0.01335 -0.00778 188 THR A CG2 
1546 N N   . ARG A 195 ? 0.24063 0.21660 0.40571 0.00421  -0.10435 -0.05793 189 ARG A N   
1547 C CA  . ARG A 195 ? 0.29440 0.17505 0.36137 -0.05325 -0.12830 -0.02736 189 ARG A CA  
1548 C C   . ARG A 195 ? 0.29111 0.16521 0.37393 -0.03571 -0.10222 -0.01462 189 ARG A C   
1549 O O   . ARG A 195 ? 0.30722 0.19723 0.34914 -0.03007 -0.11492 0.00193  189 ARG A O   
1550 C CB  . ARG A 195 ? 0.37995 0.18294 0.30409 -0.08523 -0.15912 0.01515  189 ARG A CB  
1551 C CG  . ARG A 195 ? 0.44426 0.19554 0.29581 -0.08158 -0.19177 0.02974  189 ARG A CG  
1552 C CD  . ARG A 195 ? 0.60210 0.20547 0.30310 -0.10270 -0.14589 0.00582  189 ARG A CD  
1553 N NE  . ARG A 195 ? 0.72899 0.25021 0.31135 -0.12950 -0.11947 -0.01359 189 ARG A NE  
1554 C CZ  . ARG A 195 ? 0.79385 0.31029 0.35728 -0.11790 -0.13125 0.01839  189 ARG A CZ  
1555 N NH1 . ARG A 195 ? 0.76419 0.33357 0.37856 -0.14608 -0.18329 -0.01755 189 ARG A NH1 
1556 N NH2 . ARG A 195 ? 0.85277 0.34092 0.43116 -0.09272 -0.12276 0.03450  189 ARG A NH2 
1557 N N   . TRP A 196 ? 0.28216 0.17322 0.37753 -0.04168 -0.06746 -0.01244 190 TRP A N   
1558 C CA  . TRP A 196 ? 0.25513 0.18378 0.37896 0.01818  -0.06498 -0.00382 190 TRP A CA  
1559 C C   . TRP A 196 ? 0.26463 0.18194 0.32053 -0.00007 -0.05762 -0.00925 190 TRP A C   
1560 O O   . TRP A 196 ? 0.30670 0.18330 0.29824 0.02993  -0.05443 -0.02960 190 TRP A O   
1561 C CB  . TRP A 196 ? 0.24497 0.15655 0.38549 0.04891  -0.08694 -0.01938 190 TRP A CB  
1562 C CG  . TRP A 196 ? 0.27875 0.15632 0.37832 0.04707  -0.09635 -0.04227 190 TRP A CG  
1563 C CD1 . TRP A 196 ? 0.29162 0.15138 0.39556 0.05046  -0.14627 -0.02924 190 TRP A CD1 
1564 C CD2 . TRP A 196 ? 0.27299 0.15823 0.41396 0.07570  -0.08824 -0.00397 190 TRP A CD2 
1565 N NE1 . TRP A 196 ? 0.24037 0.15447 0.42565 0.03759  -0.14409 -0.00614 190 TRP A NE1 
1566 C CE2 . TRP A 196 ? 0.26368 0.17896 0.44376 0.07399  -0.10189 0.01026  190 TRP A CE2 
1567 C CE3 . TRP A 196 ? 0.30278 0.16131 0.44969 0.06046  -0.06828 -0.02724 190 TRP A CE3 
1568 C CZ2 . TRP A 196 ? 0.27506 0.20134 0.51506 0.06912  -0.05634 0.01280  190 TRP A CZ2 
1569 C CZ3 . TRP A 196 ? 0.27437 0.19266 0.50555 0.08451  -0.05245 -0.03948 190 TRP A CZ3 
1570 C CH2 . TRP A 196 ? 0.28833 0.20075 0.52515 0.09383  -0.03134 -0.01267 190 TRP A CH2 
1571 N N   . TYR A 197 ? 0.22344 0.19218 0.27912 -0.00069 -0.07334 -0.00758 191 TYR A N   
1572 C CA  . TYR A 197 ? 0.17071 0.20710 0.28224 0.01312  -0.06112 0.02276  191 TYR A CA  
1573 C C   . TYR A 197 ? 0.15989 0.21991 0.24091 -0.01934 -0.04394 -0.00067 191 TYR A C   
1574 O O   . TYR A 197 ? 0.22852 0.23126 0.22073 -0.00942 0.01338  -0.01311 191 TYR A O   
1575 C CB  . TYR A 197 ? 0.17438 0.22332 0.28801 0.00945  -0.08581 0.01135  191 TYR A CB  
1576 C CG  . TYR A 197 ? 0.19377 0.22042 0.26676 0.00657  -0.03657 -0.00810 191 TYR A CG  
1577 C CD1 . TYR A 197 ? 0.21709 0.23654 0.28074 0.01403  -0.09666 0.02531  191 TYR A CD1 
1578 C CD2 . TYR A 197 ? 0.17514 0.28190 0.27189 0.01285  -0.02852 -0.03135 191 TYR A CD2 
1579 C CE1 . TYR A 197 ? 0.22074 0.25782 0.32328 -0.03865 -0.06788 0.02532  191 TYR A CE1 
1580 C CE2 . TYR A 197 ? 0.20369 0.31914 0.26019 0.02978  -0.05282 -0.01254 191 TYR A CE2 
1581 C CZ  . TYR A 197 ? 0.20008 0.30843 0.30762 0.02130  -0.05959 -0.00355 191 TYR A CZ  
1582 O OH  . TYR A 197 ? 0.23234 0.33574 0.30345 0.05683  -0.05038 -0.00372 191 TYR A OH  
1583 N N   . ARG A 198 ? 0.22923 0.23686 0.27002 -0.02908 -0.03870 -0.00164 192 ARG A N   
1584 C CA  . ARG A 198 ? 0.18475 0.21492 0.29317 -0.05813 0.02497  -0.02204 192 ARG A CA  
1585 C C   . ARG A 198 ? 0.14329 0.20722 0.24426 -0.01180 0.02262  -0.02943 192 ARG A C   
1586 O O   . ARG A 198 ? 0.16027 0.24479 0.24331 0.01370  0.00530  -0.03546 192 ARG A O   
1587 C CB  . ARG A 198 ? 0.26581 0.22494 0.38140 -0.09908 0.04514  -0.04097 192 ARG A CB  
1588 C CG  . ARG A 198 ? 0.33602 0.23210 0.38371 -0.06790 0.05836  -0.04475 192 ARG A CG  
1589 C CD  . ARG A 198 ? 0.28209 0.18963 0.26006 -0.05007 0.06647  0.03782  192 ARG A CD  
1590 N NE  . ARG A 198 ? 0.22742 0.20460 0.29572 -0.04598 0.04813  -0.02583 192 ARG A NE  
1591 C CZ  . ARG A 198 ? 0.32518 0.21879 0.21980 0.04764  -0.08827 0.00638  192 ARG A CZ  
1592 N NH1 . ARG A 198 ? 0.45184 0.21784 0.26313 0.01575  -0.05829 0.01778  192 ARG A NH1 
1593 N NH2 . ARG A 198 ? 0.42351 0.23694 0.25289 0.05330  -0.11570 -0.05435 192 ARG A NH2 
1594 N N   . ALA A 199 ? 0.15868 0.18348 0.24896 0.00375  -0.02277 0.00965  193 ALA A N   
1595 C CA  . ALA A 199 ? 0.14129 0.19650 0.26142 -0.00221 0.00653  -0.02959 193 ALA A CA  
1596 C C   . ALA A 199 ? 0.18268 0.24173 0.25739 -0.01625 0.02791  -0.01463 193 ALA A C   
1597 O O   . ALA A 199 ? 0.14285 0.22999 0.23634 0.01296  0.00610  -0.03633 193 ALA A O   
1598 C CB  . ALA A 199 ? 0.18586 0.20524 0.23391 -0.02026 -0.01549 -0.03802 193 ALA A CB  
1599 N N   . PRO A 200 ? 0.13509 0.24379 0.24301 -0.05007 0.01425  -0.00133 194 PRO A N   
1600 C CA  . PRO A 200 ? 0.19125 0.26353 0.21265 -0.01146 0.02299  -0.02212 194 PRO A CA  
1601 C C   . PRO A 200 ? 0.16153 0.26328 0.20167 -0.01033 0.01343  0.00029  194 PRO A C   
1602 O O   . PRO A 200 ? 0.14629 0.25740 0.24326 -0.03766 -0.00527 0.01502  194 PRO A O   
1603 C CB  . PRO A 200 ? 0.23925 0.24899 0.22895 -0.02224 0.01760  -0.02843 194 PRO A CB  
1604 C CG  . PRO A 200 ? 0.14191 0.25451 0.24985 -0.03833 -0.03280 -0.02970 194 PRO A CG  
1605 C CD  . PRO A 200 ? 0.13847 0.25247 0.21448 -0.08420 -0.00911 0.00263  194 PRO A CD  
1606 N N   . GLU A 201 ? 0.18418 0.25636 0.20230 0.02464  0.03411  0.01373  195 GLU A N   
1607 C CA  . GLU A 201 ? 0.17457 0.27141 0.20906 -0.00589 0.00885  0.01070  195 GLU A CA  
1608 C C   . GLU A 201 ? 0.20499 0.26133 0.19354 -0.02309 -0.02370 -0.01120 195 GLU A C   
1609 O O   . GLU A 201 ? 0.20616 0.28118 0.21887 -0.00637 0.03706  -0.00500 195 GLU A O   
1610 C CB  . GLU A 201 ? 0.13200 0.27459 0.26151 0.01127  0.00332  0.03328  195 GLU A CB  
1611 C CG  . GLU A 201 ? 0.10797 0.28452 0.23786 -0.00671 -0.01121 0.02968  195 GLU A CG  
1612 C CD  . GLU A 201 ? 0.19920 0.27694 0.27392 -0.02442 0.04917  -0.00593 195 GLU A CD  
1613 O OE1 . GLU A 201 ? 0.20530 0.27701 0.25786 -0.03400 0.05251  0.00498  195 GLU A OE1 
1614 O OE2 . GLU A 201 ? 0.18370 0.27513 0.26462 -0.00264 0.03933  -0.00753 195 GLU A OE2 
1615 N N   . ILE A 202 ? 0.19478 0.25226 0.18660 0.01278  0.00460  0.00574  196 ILE A N   
1616 C CA  . ILE A 202 ? 0.17384 0.27563 0.19651 -0.00663 -0.03583 0.01121  196 ILE A CA  
1617 C C   . ILE A 202 ? 0.14352 0.31697 0.20876 0.01045  -0.00751 -0.00332 196 ILE A C   
1618 O O   . ILE A 202 ? 0.19779 0.34683 0.23506 -0.04069 0.03907  -0.00166 196 ILE A O   
1619 C CB  . ILE A 202 ? 0.21031 0.25505 0.21297 -0.02346 -0.00478 0.03236  196 ILE A CB  
1620 C CG1 . ILE A 202 ? 0.24602 0.27972 0.21242 0.00514  0.03618  0.01091  196 ILE A CG1 
1621 C CG2 . ILE A 202 ? 0.22644 0.24985 0.24997 0.00567  0.02624  0.07390  196 ILE A CG2 
1622 C CD1 . ILE A 202 ? 0.21248 0.31841 0.25965 0.03820  0.03588  -0.05337 196 ILE A CD1 
1623 N N   . MET A 203 ? 0.17530 0.30090 0.22623 -0.01467 -0.03849 -0.04235 197 MET A N   
1624 C CA  . MET A 203 ? 0.22832 0.30143 0.28119 -0.00843 -0.02469 -0.02436 197 MET A CA  
1625 C C   . MET A 203 ? 0.24101 0.28050 0.30480 -0.02580 -0.02954 -0.00643 197 MET A C   
1626 O O   . MET A 203 ? 0.26348 0.30560 0.38580 -0.05338 -0.00260 0.03910  197 MET A O   
1627 C CB  . MET A 203 ? 0.21412 0.30079 0.27362 0.01895  -0.03321 0.00711  197 MET A CB  
1628 C CG  . MET A 203 ? 0.17775 0.32664 0.26533 -0.00794 -0.05751 0.01310  197 MET A CG  
1629 S SD  . MET A 203 ? 0.26542 0.35265 0.26776 0.00309  -0.03751 -0.01273 197 MET A SD  
1630 C CE  . MET A 203 ? 0.34052 0.34445 0.25834 0.03315  0.01758  -0.03778 197 MET A CE  
1631 N N   . LEU A 204 ? 0.20965 0.25461 0.25163 0.01185  -0.03302 0.00431  198 LEU A N   
1632 C CA  . LEU A 204 ? 0.19619 0.29731 0.24045 -0.01266 -0.01526 0.00426  198 LEU A CA  
1633 C C   . LEU A 204 ? 0.17252 0.33364 0.26150 -0.02152 -0.01735 -0.00693 198 LEU A C   
1634 O O   . LEU A 204 ? 0.19907 0.36768 0.25853 -0.05133 -0.02674 -0.01794 198 LEU A O   
1635 C CB  . LEU A 204 ? 0.22825 0.32060 0.21696 -0.01317 -0.00368 -0.00386 198 LEU A CB  
1636 C CG  . LEU A 204 ? 0.17394 0.29319 0.23544 -0.03472 -0.02881 0.01187  198 LEU A CG  
1637 C CD1 . LEU A 204 ? 0.18658 0.32006 0.25151 -0.04870 -0.01976 0.03232  198 LEU A CD1 
1638 C CD2 . LEU A 204 ? 0.22160 0.28394 0.26438 -0.04039 -0.00324 -0.02635 198 LEU A CD2 
1639 N N   . ASN A 205 ? 0.19034 0.33196 0.20811 -0.01988 -0.02863 -0.03391 199 ASN A N   
1640 C CA  . ASN A 205 ? 0.22314 0.32520 0.22492 0.00675  0.02296  -0.04148 199 ASN A CA  
1641 C C   . ASN A 205 ? 0.17421 0.34286 0.27038 -0.02301 0.00588  -0.05753 199 ASN A C   
1642 O O   . ASN A 205 ? 0.17993 0.36653 0.28300 0.01721  0.01754  -0.04610 199 ASN A O   
1643 C CB  . ASN A 205 ? 0.20690 0.30717 0.26176 0.03612  0.02833  0.00503  199 ASN A CB  
1644 C CG  . ASN A 205 ? 0.15202 0.28672 0.28418 0.03892  -0.00711 0.00382  199 ASN A CG  
1645 O OD1 . ASN A 205 ? 0.15294 0.31663 0.32156 0.00768  0.02157  0.01523  199 ASN A OD1 
1646 N ND2 . ASN A 205 ? 0.15567 0.29437 0.29679 0.04193  -0.00941 0.02201  199 ASN A ND2 
1647 N N   . SER A 206 ? 0.15241 0.31632 0.23456 -0.03156 -0.01212 -0.05038 200 SER A N   
1648 C CA  . SER A 206 ? 0.20104 0.28344 0.25528 -0.02044 -0.00579 -0.03314 200 SER A CA  
1649 C C   . SER A 206 ? 0.23205 0.30790 0.24910 -0.03614 0.00254  -0.02608 200 SER A C   
1650 O O   . SER A 206 ? 0.19964 0.29499 0.27077 -0.00441 0.00129  -0.04379 200 SER A O   
1651 C CB  . SER A 206 ? 0.25404 0.26054 0.29229 -0.05579 0.03494  -0.06970 200 SER A CB  
1652 O OG  . SER A 206 ? 0.23495 0.28110 0.27560 -0.02931 0.00287  -0.01828 200 SER A OG  
1653 N N   . LYS A 207 ? 0.19756 0.33304 0.21124 -0.00306 -0.00293 -0.03091 201 LYS A N   
1654 C CA  . LYS A 207 ? 0.17344 0.39803 0.24171 0.02097  0.01703  -0.03537 201 LYS A CA  
1655 C C   . LYS A 207 ? 0.20210 0.37437 0.27703 0.03349  -0.00879 -0.02688 201 LYS A C   
1656 O O   . LYS A 207 ? 0.25400 0.37641 0.31889 0.05013  -0.01584 -0.02522 201 LYS A O   
1657 C CB  . LYS A 207 ? 0.20887 0.47293 0.23760 -0.03694 0.06680  -0.08624 201 LYS A CB  
1658 C CG  . LYS A 207 ? 0.18444 0.51495 0.27345 -0.02722 0.07215  -0.10834 201 LYS A CG  
1659 C CD  . LYS A 207 ? 0.30477 0.56362 0.39023 0.00834  0.17876  -0.08592 201 LYS A CD  
1660 C CE  . LYS A 207 ? 0.32154 0.61173 0.42012 -0.00110 0.16514  -0.10847 201 LYS A CE  
1661 N NZ  . LYS A 207 ? 0.27851 0.62579 0.41993 -0.01722 0.12163  -0.13657 201 LYS A NZ  
1662 N N   . GLY A 208 ? 0.17924 0.34649 0.27655 0.01058  -0.01656 -0.03717 202 GLY A N   
1663 C CA  . GLY A 208 ? 0.19261 0.30525 0.24005 -0.00726 0.00166  -0.07686 202 GLY A CA  
1664 C C   . GLY A 208 ? 0.16678 0.33408 0.23014 -0.00457 -0.01568 -0.05666 202 GLY A C   
1665 O O   . GLY A 208 ? 0.16555 0.34002 0.25949 0.02179  -0.04816 -0.04453 202 GLY A O   
1666 N N   . TYR A 209 ? 0.20433 0.35423 0.23381 0.00612  0.05529  -0.01347 203 TYR A N   
1667 C CA  A TYR A 209 ? 0.18101 0.33951 0.20660 -0.03992 0.03511  -0.04277 203 TYR A CA  
1668 C CA  B TYR A 209 ? 0.17810 0.35442 0.23695 0.00088  0.06686  -0.00633 203 TYR A CA  
1669 C C   . TYR A 209 ? 0.20531 0.35931 0.24375 0.01339  0.05177  -0.02500 203 TYR A C   
1670 O O   . TYR A 209 ? 0.24549 0.36684 0.29069 -0.00892 0.05457  -0.03942 203 TYR A O   
1671 C CB  A TYR A 209 ? 0.21875 0.36124 0.21508 -0.08477 0.01747  -0.04997 203 TYR A CB  
1672 C CB  B TYR A 209 ? 0.15654 0.36421 0.24828 -0.00124 0.07375  0.02034  203 TYR A CB  
1673 C CG  A TYR A 209 ? 0.31255 0.39357 0.27330 -0.10864 0.02837  -0.04739 203 TYR A CG  
1674 C CG  B TYR A 209 ? 0.16366 0.37969 0.27598 -0.00032 0.06809  0.05438  203 TYR A CG  
1675 C CD1 A TYR A 209 ? 0.35072 0.41271 0.29513 -0.10816 0.06898  -0.04885 203 TYR A CD1 
1676 C CD1 B TYR A 209 ? 0.20146 0.38947 0.29345 0.02241  0.08266  0.07829  203 TYR A CD1 
1677 C CD2 A TYR A 209 ? 0.32786 0.41427 0.28978 -0.12524 -0.00792 -0.02643 203 TYR A CD2 
1678 C CD2 B TYR A 209 ? 0.15858 0.38252 0.26604 0.01362  0.03282  0.09016  203 TYR A CD2 
1679 C CE1 A TYR A 209 ? 0.40112 0.43658 0.32463 -0.11757 0.08276  -0.05516 203 TYR A CE1 
1680 C CE1 B TYR A 209 ? 0.19049 0.40123 0.31289 0.01662  0.04814  0.09929  203 TYR A CE1 
1681 C CE2 A TYR A 209 ? 0.38235 0.44233 0.30142 -0.12970 -0.00188 -0.02054 203 TYR A CE2 
1682 C CE2 B TYR A 209 ? 0.16408 0.39336 0.31256 0.00859  0.00147  0.10532  203 TYR A CE2 
1683 C CZ  A TYR A 209 ? 0.45313 0.45458 0.34559 -0.12983 0.09587  -0.04062 203 TYR A CZ  
1684 C CZ  B TYR A 209 ? 0.20035 0.41127 0.33904 -0.00033 0.03893  0.10685  203 TYR A CZ  
1685 O OH  A TYR A 209 ? 0.50658 0.46773 0.37491 -0.15099 0.14865  -0.06128 203 TYR A OH  
1686 O OH  B TYR A 209 ? 0.21730 0.42750 0.38828 -0.03492 0.05984  0.11005  203 TYR A OH  
1687 N N   . THR A 210 ? 0.16275 0.35323 0.21774 0.02589  0.01782  -0.03500 204 THR A N   
1688 C CA  . THR A 210 ? 0.18505 0.37702 0.26198 -0.00561 -0.01291 -0.00444 204 THR A CA  
1689 C C   . THR A 210 ? 0.18021 0.33377 0.25002 0.01780  -0.00807 0.00206  204 THR A C   
1690 O O   . THR A 210 ? 0.21648 0.34747 0.24215 0.02464  0.03155  0.02820  204 THR A O   
1691 C CB  . THR A 210 ? 0.21506 0.43483 0.35151 -0.02594 -0.03482 -0.00330 204 THR A CB  
1692 O OG1 . THR A 210 ? 0.36696 0.46754 0.35308 -0.04452 -0.05846 -0.02236 204 THR A OG1 
1693 C CG2 . THR A 210 ? 0.14153 0.45573 0.42366 -0.00295 -0.02105 0.08183  204 THR A CG2 
1694 N N   . LYS A 211 ? 0.16153 0.29793 0.22234 -0.00115 -0.02668 -0.00926 205 LYS A N   
1695 C CA  . LYS A 211 ? 0.16007 0.24324 0.24640 -0.01394 -0.00575 -0.04877 205 LYS A CA  
1696 C C   . LYS A 211 ? 0.16598 0.22595 0.21398 -0.00332 0.01053  -0.02184 205 LYS A C   
1697 O O   . LYS A 211 ? 0.16811 0.23189 0.21484 -0.00754 0.01677  -0.03940 205 LYS A O   
1698 C CB  . LYS A 211 ? 0.23501 0.25464 0.27471 -0.01526 0.00506  -0.04465 205 LYS A CB  
1699 C CG  . LYS A 211 ? 0.23086 0.23553 0.25574 -0.00542 0.00380  -0.06734 205 LYS A CG  
1700 C CD  . LYS A 211 ? 0.24893 0.21216 0.26089 0.01283  -0.03618 -0.05850 205 LYS A CD  
1701 C CE  . LYS A 211 ? 0.30093 0.19512 0.28075 0.00724  -0.01429 -0.05676 205 LYS A CE  
1702 N NZ  . LYS A 211 ? 0.31366 0.20766 0.31955 0.02105  0.04205  -0.00820 205 LYS A NZ  
1703 N N   . SER A 212 ? 0.16269 0.22572 0.18977 -0.01639 -0.03095 -0.02024 206 SER A N   
1704 C CA  . SER A 212 ? 0.15293 0.22285 0.21565 0.01270  -0.04668 -0.02192 206 SER A CA  
1705 C C   . SER A 212 ? 0.16914 0.22650 0.19474 -0.01226 -0.04157 -0.00474 206 SER A C   
1706 O O   . SER A 212 ? 0.16508 0.24004 0.19615 -0.00423 -0.03230 -0.02148 206 SER A O   
1707 C CB  . SER A 212 ? 0.14187 0.30327 0.28557 -0.00956 -0.03472 -0.00319 206 SER A CB  
1708 O OG  . SER A 212 ? 0.16922 0.36443 0.28715 -0.01895 -0.03569 -0.03008 206 SER A OG  
1709 N N   . ILE A 213 ? 0.20174 0.21805 0.19960 -0.03507 -0.04275 0.01413  207 ILE A N   
1710 C CA  . ILE A 213 ? 0.19057 0.23662 0.24066 -0.03208 0.00843  0.08277  207 ILE A CA  
1711 C C   . ILE A 213 ? 0.15089 0.23825 0.22462 0.02879  0.04337  0.03957  207 ILE A C   
1712 O O   . ILE A 213 ? 0.17547 0.25721 0.22557 -0.00856 -0.03203 0.00968  207 ILE A O   
1713 C CB  . ILE A 213 ? 0.19063 0.25165 0.29397 -0.01980 -0.06005 0.10046  207 ILE A CB  
1714 C CG1 . ILE A 213 ? 0.18729 0.30359 0.38097 -0.01486 -0.04203 0.05740  207 ILE A CG1 
1715 C CG2 . ILE A 213 ? 0.22130 0.28844 0.31723 -0.01908 -0.04095 0.08501  207 ILE A CG2 
1716 C CD1 . ILE A 213 ? 0.25070 0.33780 0.41679 -0.04522 -0.02790 -0.00541 207 ILE A CD1 
1717 N N   . ASP A 214 ? 0.16135 0.22227 0.18613 0.02541  0.05215  0.00071  208 ASP A N   
1718 C CA  . ASP A 214 ? 0.18783 0.21357 0.16946 0.03098  0.01415  -0.01525 208 ASP A CA  
1719 C C   . ASP A 214 ? 0.23303 0.19343 0.18571 0.00471  0.01282  -0.01735 208 ASP A C   
1720 O O   . ASP A 214 ? 0.21669 0.18835 0.17989 0.00585  0.00775  0.00090  208 ASP A O   
1721 C CB  . ASP A 214 ? 0.22365 0.20686 0.11482 0.00637  -0.00356 -0.02143 208 ASP A CB  
1722 C CG  . ASP A 214 ? 0.17543 0.21177 0.16295 0.04031  -0.02452 -0.03076 208 ASP A CG  
1723 O OD1 . ASP A 214 ? 0.18522 0.26052 0.17617 0.03425  0.00905  0.00371  208 ASP A OD1 
1724 O OD2 . ASP A 214 ? 0.22937 0.22825 0.18363 -0.01487 0.01159  -0.01128 208 ASP A OD2 
1725 N N   . ILE A 215 ? 0.17824 0.18122 0.14835 0.01041  -0.01111 -0.00170 209 ILE A N   
1726 C CA  . ILE A 215 ? 0.22005 0.15995 0.16243 -0.01376 -0.00349 0.00367  209 ILE A CA  
1727 C C   . ILE A 215 ? 0.19626 0.15624 0.21518 -0.00635 -0.03281 -0.02060 209 ILE A C   
1728 O O   . ILE A 215 ? 0.15691 0.16105 0.22311 0.01518  -0.00166 -0.00937 209 ILE A O   
1729 C CB  . ILE A 215 ? 0.20521 0.17826 0.17882 -0.00520 -0.00882 0.01393  209 ILE A CB  
1730 C CG1 . ILE A 215 ? 0.18992 0.21304 0.21548 -0.00327 -0.03294 0.03866  209 ILE A CG1 
1731 C CG2 . ILE A 215 ? 0.22729 0.22262 0.15991 0.01106  -0.00392 0.01956  209 ILE A CG2 
1732 C CD1 . ILE A 215 ? 0.24273 0.22683 0.26538 -0.01021 -0.04464 0.00754  209 ILE A CD1 
1733 N N   . TRP A 216 ? 0.18560 0.14400 0.22310 -0.02382 -0.04751 -0.01256 210 TRP A N   
1734 C CA  . TRP A 216 ? 0.12174 0.17153 0.20840 -0.01539 -0.01552 -0.00286 210 TRP A CA  
1735 C C   . TRP A 216 ? 0.16167 0.19248 0.18174 0.02215  0.00058  0.03266  210 TRP A C   
1736 O O   . TRP A 216 ? 0.14391 0.18196 0.22033 -0.00100 0.00541  0.03737  210 TRP A O   
1737 C CB  . TRP A 216 ? 0.12754 0.18159 0.20439 -0.05322 -0.00461 -0.02221 210 TRP A CB  
1738 C CG  . TRP A 216 ? 0.13058 0.16858 0.18626 -0.03485 -0.00010 -0.00578 210 TRP A CG  
1739 C CD1 . TRP A 216 ? 0.12203 0.15888 0.20340 -0.03944 0.00643  -0.02049 210 TRP A CD1 
1740 C CD2 . TRP A 216 ? 0.16661 0.19792 0.13540 -0.02244 0.00005  -0.02326 210 TRP A CD2 
1741 N NE1 . TRP A 216 ? 0.16114 0.19625 0.20540 -0.00974 -0.00418 0.00368  210 TRP A NE1 
1742 C CE2 . TRP A 216 ? 0.15679 0.22314 0.17206 -0.00485 0.00980  0.00917  210 TRP A CE2 
1743 C CE3 . TRP A 216 ? 0.16191 0.25290 0.14996 -0.01131 0.03182  -0.00977 210 TRP A CE3 
1744 C CZ2 . TRP A 216 ? 0.16584 0.27461 0.16582 -0.02595 0.00415  0.00029  210 TRP A CZ2 
1745 C CZ3 . TRP A 216 ? 0.18990 0.25824 0.17918 -0.02820 0.01869  -0.03667 210 TRP A CZ3 
1746 C CH2 . TRP A 216 ? 0.16149 0.27238 0.18240 -0.03156 -0.01048 -0.02419 210 TRP A CH2 
1747 N N   . SER A 217 ? 0.14497 0.21844 0.17661 0.00158  -0.03515 0.02756  211 SER A N   
1748 C CA  . SER A 217 ? 0.15282 0.23365 0.15454 0.00930  -0.02769 0.02116  211 SER A CA  
1749 C C   . SER A 217 ? 0.16999 0.22656 0.18801 0.00019  0.03924  0.00937  211 SER A C   
1750 O O   . SER A 217 ? 0.14525 0.24907 0.18504 -0.01115 0.00915  0.00132  211 SER A O   
1751 C CB  . SER A 217 ? 0.13657 0.25948 0.13465 -0.00895 0.02439  0.03172  211 SER A CB  
1752 O OG  . SER A 217 ? 0.17768 0.26375 0.17425 0.01267  0.01933  0.03455  211 SER A OG  
1753 N N   . VAL A 218 ? 0.14518 0.18991 0.17000 -0.02493 0.00199  0.02031  212 VAL A N   
1754 C CA  . VAL A 218 ? 0.17505 0.20091 0.18594 -0.03757 0.02585  -0.01625 212 VAL A CA  
1755 C C   . VAL A 218 ? 0.16828 0.20941 0.16233 0.00775  -0.01164 -0.02016 212 VAL A C   
1756 O O   . VAL A 218 ? 0.17581 0.21479 0.21543 0.01962  0.01951  -0.00704 212 VAL A O   
1757 C CB  . VAL A 218 ? 0.13064 0.22101 0.19801 -0.02068 0.00562  -0.06271 212 VAL A CB  
1758 C CG1 . VAL A 218 ? 0.18367 0.27114 0.24597 -0.02614 0.04754  -0.04906 212 VAL A CG1 
1759 C CG2 . VAL A 218 ? 0.23794 0.23141 0.19131 -0.01770 -0.00581 -0.05223 212 VAL A CG2 
1760 N N   . GLY A 219 ? 0.16791 0.21984 0.12330 -0.04082 -0.00657 -0.03403 213 GLY A N   
1761 C CA  . GLY A 219 ? 0.18474 0.22183 0.14313 -0.01529 -0.01015 -0.00343 213 GLY A CA  
1762 C C   . GLY A 219 ? 0.19367 0.23292 0.20754 -0.01590 0.00602  0.00411  213 GLY A C   
1763 O O   . GLY A 219 ? 0.18519 0.24949 0.19331 0.01394  0.00425  0.00317  213 GLY A O   
1764 N N   . CYS A 220 ? 0.14233 0.23704 0.18619 -0.00250 -0.01648 0.02892  214 CYS A N   
1765 C CA  . CYS A 220 ? 0.15669 0.22838 0.21626 -0.00574 -0.00295 0.01153  214 CYS A CA  
1766 C C   . CYS A 220 ? 0.14177 0.26456 0.24811 -0.00550 0.01954  0.00088  214 CYS A C   
1767 O O   . CYS A 220 ? 0.15365 0.29979 0.24835 0.01829  -0.01624 -0.02007 214 CYS A O   
1768 C CB  . CYS A 220 ? 0.11711 0.21159 0.22332 -0.01241 0.00239  -0.01489 214 CYS A CB  
1769 S SG  . CYS A 220 ? 0.20198 0.24165 0.24927 -0.00642 0.01003  -0.01194 214 CYS A SG  
1770 N N   . ILE A 221 ? 0.12107 0.26939 0.21851 0.01497  -0.02547 -0.00155 215 ILE A N   
1771 C CA  . ILE A 221 ? 0.08736 0.24546 0.23433 -0.00475 -0.02238 -0.02132 215 ILE A CA  
1772 C C   . ILE A 221 ? 0.14265 0.25438 0.22386 0.01845  -0.01117 -0.00663 215 ILE A C   
1773 O O   . ILE A 221 ? 0.14922 0.26822 0.24393 0.02287  0.00525  0.00510  215 ILE A O   
1774 C CB  . ILE A 221 ? 0.13321 0.28058 0.18278 -0.01705 -0.00550 -0.00424 215 ILE A CB  
1775 C CG1 . ILE A 221 ? 0.17136 0.27334 0.19629 -0.01019 0.00201  -0.01456 215 ILE A CG1 
1776 C CG2 . ILE A 221 ? 0.15500 0.29199 0.22509 0.01088  -0.00408 -0.05164 215 ILE A CG2 
1777 C CD1 . ILE A 221 ? 0.16903 0.30007 0.19365 -0.02172 -0.00400 -0.04347 215 ILE A CD1 
1778 N N   . LEU A 222 ? 0.17269 0.23129 0.19150 -0.00471 -0.00084 -0.00616 216 LEU A N   
1779 C CA  . LEU A 222 ? 0.22149 0.22290 0.18431 -0.00419 0.01966  0.00856  216 LEU A CA  
1780 C C   . LEU A 222 ? 0.21435 0.22808 0.22283 -0.01372 0.03622  -0.04590 216 LEU A C   
1781 O O   . LEU A 222 ? 0.21184 0.22774 0.22484 0.00750  0.02107  -0.02688 216 LEU A O   
1782 C CB  . LEU A 222 ? 0.21568 0.25136 0.15257 0.03024  0.00913  0.02761  216 LEU A CB  
1783 C CG  . LEU A 222 ? 0.16292 0.27907 0.17764 0.00206  -0.04562 0.05226  216 LEU A CG  
1784 C CD1 . LEU A 222 ? 0.16011 0.27239 0.20161 -0.05095 -0.03591 0.00776  216 LEU A CD1 
1785 C CD2 . LEU A 222 ? 0.24262 0.30764 0.20697 -0.01160 -0.00687 0.06427  216 LEU A CD2 
1786 N N   . ALA A 223 ? 0.19431 0.23808 0.19145 -0.02843 0.01436  -0.02865 217 ALA A N   
1787 C CA  . ALA A 223 ? 0.21029 0.26535 0.23572 -0.02280 0.00878  -0.06472 217 ALA A CA  
1788 C C   . ALA A 223 ? 0.21855 0.27817 0.25644 0.01936  0.04894  -0.05512 217 ALA A C   
1789 O O   . ALA A 223 ? 0.21533 0.28561 0.27213 0.05699  0.03315  -0.05547 217 ALA A O   
1790 C CB  . ALA A 223 ? 0.18243 0.30409 0.25836 -0.01478 0.03787  -0.08809 217 ALA A CB  
1791 N N   . GLU A 224 ? 0.24082 0.26744 0.25798 -0.00327 0.04007  -0.03565 218 GLU A N   
1792 C CA  . GLU A 224 ? 0.24830 0.26188 0.25534 0.00055  0.01420  0.00805  218 GLU A CA  
1793 C C   . GLU A 224 ? 0.23969 0.27142 0.30117 0.01372  0.01838  -0.00626 218 GLU A C   
1794 O O   . GLU A 224 ? 0.27864 0.25051 0.36434 0.01638  0.01632  -0.02849 218 GLU A O   
1795 C CB  . GLU A 224 ? 0.26502 0.27413 0.28480 0.00577  0.00427  0.00908  218 GLU A CB  
1796 C CG  . GLU A 224 ? 0.25673 0.31523 0.33048 0.03502  0.00896  0.02206  218 GLU A CG  
1797 C CD  . GLU A 224 ? 0.27554 0.35836 0.34882 0.04238  0.00424  0.03178  218 GLU A CD  
1798 O OE1 . GLU A 224 ? 0.22674 0.35023 0.35280 0.03129  -0.01885 0.02815  218 GLU A OE1 
1799 O OE2 . GLU A 224 ? 0.27341 0.40305 0.34761 0.02329  -0.03805 0.02868  218 GLU A OE2 
1800 N N   . MET A 225 ? 0.17240 0.30756 0.24725 0.01798  0.01909  0.00184  219 MET A N   
1801 C CA  . MET A 225 ? 0.17789 0.35604 0.23852 0.03480  -0.00056 -0.02552 219 MET A CA  
1802 C C   . MET A 225 ? 0.19061 0.39329 0.24329 0.04815  0.00592  -0.02240 219 MET A C   
1803 O O   . MET A 225 ? 0.20412 0.43104 0.28207 0.07275  0.02790  -0.04097 219 MET A O   
1804 C CB  . MET A 225 ? 0.19768 0.33012 0.25222 -0.00778 0.00455  -0.04083 219 MET A CB  
1805 C CG  . MET A 225 ? 0.22309 0.34709 0.25495 -0.01682 -0.00207 -0.03152 219 MET A CG  
1806 S SD  . MET A 225 ? 0.19421 0.39054 0.27214 -0.00228 -0.00067 -0.01450 219 MET A SD  
1807 C CE  . MET A 225 ? 0.15731 0.38329 0.25470 0.01140  -0.01240 -0.04641 219 MET A CE  
1808 N N   . LEU A 226 ? 0.21771 0.38136 0.21651 0.04335  0.01699  -0.05944 220 LEU A N   
1809 C CA  . LEU A 226 ? 0.30127 0.38197 0.25749 0.05453  0.03604  -0.05140 220 LEU A CA  
1810 C C   . LEU A 226 ? 0.37423 0.41702 0.29914 0.08483  0.10082  -0.06088 220 LEU A C   
1811 O O   . LEU A 226 ? 0.50076 0.43927 0.37052 0.09364  0.19987  -0.04449 220 LEU A O   
1812 C CB  . LEU A 226 ? 0.24268 0.36380 0.27369 0.07701  0.03189  -0.01749 220 LEU A CB  
1813 C CG  . LEU A 226 ? 0.22281 0.36288 0.29586 0.06220  0.06661  -0.01283 220 LEU A CG  
1814 C CD1 . LEU A 226 ? 0.23692 0.39383 0.30362 0.05284  0.02251  -0.00977 220 LEU A CD1 
1815 C CD2 . LEU A 226 ? 0.25736 0.35157 0.32590 -0.00599 0.07414  -0.01933 220 LEU A CD2 
1816 N N   . SER A 227 ? 0.35355 0.44041 0.32179 0.05862  -0.01141 -0.08051 221 SER A N   
1817 C CA  . SER A 227 ? 0.35487 0.47969 0.37966 0.03807  -0.04021 -0.08393 221 SER A CA  
1818 C C   . SER A 227 ? 0.29727 0.46050 0.38838 0.08942  -0.03935 -0.09529 221 SER A C   
1819 O O   . SER A 227 ? 0.33184 0.46844 0.40479 0.07348  -0.01430 -0.12328 221 SER A O   
1820 C CB  . SER A 227 ? 0.35872 0.52610 0.44020 -0.01071 -0.02249 -0.08232 221 SER A CB  
1821 O OG  . SER A 227 ? 0.33362 0.54542 0.46556 -0.00673 -0.02623 -0.08319 221 SER A OG  
1822 N N   . ASN A 228 ? 0.28054 0.45284 0.38551 0.09939  -0.03028 -0.08842 222 ASN A N   
1823 C CA  . ASN A 228 ? 0.26698 0.44937 0.43984 0.08587  -0.01106 -0.07802 222 ASN A CA  
1824 C C   . ASN A 228 ? 0.24645 0.45437 0.50040 0.04594  -0.00650 -0.05349 222 ASN A C   
1825 O O   . ASN A 228 ? 0.28912 0.50357 0.55382 0.00017  -0.02373 -0.01767 222 ASN A O   
1826 C CB  . ASN A 228 ? 0.20033 0.46702 0.45994 0.08334  0.00324  -0.08118 222 ASN A CB  
1827 C CG  . ASN A 228 ? 0.24296 0.48382 0.50260 0.07231  0.00698  -0.08267 222 ASN A CG  
1828 O OD1 . ASN A 228 ? 0.29565 0.49776 0.56856 0.11500  0.00175  -0.08552 222 ASN A OD1 
1829 N ND2 . ASN A 228 ? 0.25616 0.48231 0.47990 0.07618  0.02988  -0.06864 222 ASN A ND2 
1830 N N   . ARG A 229 ? 0.22044 0.41353 0.46646 0.02723  -0.03288 -0.08852 223 ARG A N   
1831 C CA  . ARG A 229 ? 0.27488 0.38836 0.51087 0.06296  -0.02853 -0.09757 223 ARG A CA  
1832 C C   . ARG A 229 ? 0.21507 0.31529 0.44761 0.04781  -0.02545 -0.06179 223 ARG A C   
1833 O O   . ARG A 229 ? 0.21334 0.31542 0.40493 0.02638  -0.00032 -0.06135 223 ARG A O   
1834 C CB  . ARG A 229 ? 0.34358 0.42566 0.58615 0.05903  -0.03598 -0.12226 223 ARG A CB  
1835 C CG  . ARG A 229 ? 0.46470 0.47662 0.68014 0.03728  0.04434  -0.11550 223 ARG A CG  
1836 C CD  . ARG A 229 ? 0.56417 0.51734 0.74984 -0.00218 0.13848  -0.09613 223 ARG A CD  
1837 N NE  . ARG A 229 ? 0.65116 0.55167 0.79693 -0.01907 0.19786  -0.06386 223 ARG A NE  
1838 C CZ  . ARG A 229 ? 0.63928 0.57338 0.82595 -0.00953 0.23289  -0.04054 223 ARG A CZ  
1839 N NH1 . ARG A 229 ? 0.63154 0.58247 0.82940 -0.01012 0.24600  -0.03926 223 ARG A NH1 
1840 N NH2 . ARG A 229 ? 0.66275 0.59020 0.84108 -0.00247 0.24253  -0.02928 223 ARG A NH2 
1841 N N   . PRO A 230 ? 0.22028 0.30107 0.41641 0.07568  -0.00431 -0.00899 224 PRO A N   
1842 C CA  . PRO A 230 ? 0.24628 0.30052 0.42814 0.07702  0.00407  -0.00421 224 PRO A CA  
1843 C C   . PRO A 230 ? 0.24643 0.27450 0.41649 0.04472  0.02306  -0.03252 224 PRO A C   
1844 O O   . PRO A 230 ? 0.27434 0.25997 0.41537 0.03477  -0.00543 -0.05766 224 PRO A O   
1845 C CB  . PRO A 230 ? 0.33607 0.31547 0.44181 0.07718  0.02864  0.01524  224 PRO A CB  
1846 C CG  . PRO A 230 ? 0.26266 0.34874 0.47567 0.08962  0.02896  0.05755  224 PRO A CG  
1847 C CD  . PRO A 230 ? 0.21475 0.34175 0.45411 0.05326  -0.00469 0.03265  224 PRO A CD  
1848 N N   . ILE A 231 ? 0.20936 0.25472 0.41693 0.01616  -0.01075 -0.02674 225 ILE A N   
1849 C CA  . ILE A 231 ? 0.25395 0.25117 0.38703 -0.00390 -0.02105 -0.04647 225 ILE A CA  
1850 C C   . ILE A 231 ? 0.24716 0.24562 0.40066 -0.01656 0.00482  -0.07645 225 ILE A C   
1851 O O   . ILE A 231 ? 0.24847 0.26240 0.36094 0.02132  -0.01709 -0.06413 225 ILE A O   
1852 C CB  A ILE A 231 ? 0.28533 0.25610 0.32597 0.01986  -0.04065 -0.03180 225 ILE A CB  
1853 C CB  B ILE A 231 ? 0.24906 0.26126 0.39459 0.04969  -0.01279 -0.05170 225 ILE A CB  
1854 C CG1 A ILE A 231 ? 0.29747 0.26153 0.25959 0.03085  -0.06827 0.01545  225 ILE A CG1 
1855 C CG1 B ILE A 231 ? 0.29961 0.29631 0.37944 0.02803  -0.00403 -0.02758 225 ILE A CG1 
1856 C CG2 A ILE A 231 ? 0.28376 0.26495 0.31637 0.02318  -0.00742 -0.04301 225 ILE A CG2 
1857 C CG2 B ILE A 231 ? 0.18500 0.24872 0.38800 0.09902  0.01609  -0.06193 225 ILE A CG2 
1858 C CD1 A ILE A 231 ? 0.29134 0.25261 0.21247 0.00973  -0.08186 0.02620  225 ILE A CD1 
1859 C CD1 B ILE A 231 ? 0.31349 0.30980 0.37063 0.00514  0.00156  -0.01766 225 ILE A CD1 
1860 N N   . PHE A 232 ? 0.24848 0.23629 0.41545 -0.03328 -0.02648 -0.05569 226 PHE A N   
1861 C CA  . PHE A 232 ? 0.21825 0.22591 0.39886 0.01506  -0.03835 -0.03542 226 PHE A CA  
1862 C C   . PHE A 232 ? 0.24990 0.22677 0.43226 0.01245  -0.05699 -0.02000 226 PHE A C   
1863 O O   . PHE A 232 ? 0.28449 0.21199 0.35856 0.00987  -0.02613 0.01402  226 PHE A O   
1864 C CB  . PHE A 232 ? 0.24149 0.20681 0.31487 0.01945  -0.05232 -0.03639 226 PHE A CB  
1865 C CG  . PHE A 232 ? 0.22767 0.23666 0.26661 0.02276  -0.00552 -0.02730 226 PHE A CG  
1866 C CD1 . PHE A 232 ? 0.22867 0.28793 0.24150 0.00450  -0.01094 0.00337  226 PHE A CD1 
1867 C CD2 . PHE A 232 ? 0.18921 0.25157 0.25461 -0.00507 -0.00171 -0.03508 226 PHE A CD2 
1868 C CE1 . PHE A 232 ? 0.22851 0.30540 0.23155 0.00095  -0.01476 -0.01417 226 PHE A CE1 
1869 C CE2 . PHE A 232 ? 0.17496 0.29905 0.21568 0.01078  0.00877  -0.00546 226 PHE A CE2 
1870 C CZ  . PHE A 232 ? 0.22521 0.32777 0.21751 0.01663  -0.00689 -0.01957 226 PHE A CZ  
1871 N N   . PRO A 233 ? 0.26264 0.21895 0.52242 -0.00392 -0.05177 -0.00894 227 PRO A N   
1872 C CA  . PRO A 233 ? 0.26219 0.23217 0.60604 -0.00128 -0.03550 0.02114  227 PRO A CA  
1873 C C   . PRO A 233 ? 0.28578 0.21138 0.60332 -0.02032 -0.08926 0.05515  227 PRO A C   
1874 O O   . PRO A 233 ? 0.29371 0.20672 0.68431 -0.03793 -0.05887 0.01176  227 PRO A O   
1875 C CB  . PRO A 233 ? 0.26292 0.27562 0.64757 0.02096  -0.03165 0.05691  227 PRO A CB  
1876 C CG  . PRO A 233 ? 0.31763 0.27672 0.64966 0.01941  0.04980  0.02530  227 PRO A CG  
1877 C CD  . PRO A 233 ? 0.33013 0.24658 0.61087 0.01790  0.04132  0.01900  227 PRO A CD  
1878 N N   . GLY A 234 ? 0.31218 0.22540 0.54839 -0.04212 -0.11005 0.05780  228 GLY A N   
1879 C CA  . GLY A 234 ? 0.27500 0.23221 0.50090 -0.08070 -0.16579 0.07489  228 GLY A CA  
1880 C C   . GLY A 234 ? 0.40724 0.26817 0.52556 -0.09201 -0.18341 0.07567  228 GLY A C   
1881 O O   . GLY A 234 ? 0.40141 0.30056 0.56648 -0.06518 -0.18758 0.08645  228 GLY A O   
1882 N N   . LYS A 235 ? 0.48734 0.27672 0.49179 -0.12685 -0.21578 0.10449  229 LYS A N   
1883 C CA  . LYS A 235 ? 0.58032 0.29290 0.47828 -0.14365 -0.19406 0.09978  229 LYS A CA  
1884 C C   . LYS A 235 ? 0.65377 0.31356 0.40948 -0.17048 -0.18535 0.10265  229 LYS A C   
1885 O O   . LYS A 235 ? 0.73027 0.35079 0.43911 -0.14759 -0.18834 0.14414  229 LYS A O   
1886 C CB  . LYS A 235 ? 0.59080 0.30464 0.50539 -0.09888 -0.12765 0.07297  229 LYS A CB  
1887 C CG  . LYS A 235 ? 0.60984 0.32697 0.53265 -0.06569 -0.05489 0.09306  229 LYS A CG  
1888 C CD  . LYS A 235 ? 0.61895 0.35565 0.55434 -0.03581 0.02485  0.08852  229 LYS A CD  
1889 C CE  . LYS A 235 ? 0.65049 0.38811 0.57071 -0.01588 0.08729  0.10687  229 LYS A CE  
1890 N NZ  . LYS A 235 ? 0.65445 0.40224 0.58842 -0.00564 0.12461  0.09360  229 LYS A NZ  
1891 N N   . HIS A 236 ? 0.68043 0.29954 0.38295 -0.20058 -0.12845 0.04555  230 HIS A N   
1892 C CA  . HIS A 236 ? 0.71800 0.31465 0.38605 -0.20854 -0.01015 -0.00607 230 HIS A CA  
1893 C C   . HIS A 236 ? 0.70230 0.30124 0.39316 -0.19319 0.07423  -0.04914 230 HIS A C   
1894 O O   . HIS A 236 ? 0.68853 0.28335 0.32632 -0.20145 0.03308  -0.02053 230 HIS A O   
1895 C CB  . HIS A 236 ? 0.76541 0.33212 0.39412 -0.23954 0.02645  -0.02820 230 HIS A CB  
1896 C CG  . HIS A 236 ? 0.74743 0.33918 0.38545 -0.24794 0.05521  -0.04774 230 HIS A CG  
1897 N ND1 . HIS A 236 ? 0.74243 0.34806 0.39309 -0.24473 0.05750  -0.06363 230 HIS A ND1 
1898 C CD2 . HIS A 236 ? 0.70884 0.31750 0.33843 -0.23270 0.05955  -0.04332 230 HIS A CD2 
1899 C CE1 . HIS A 236 ? 0.73707 0.34899 0.38053 -0.24187 0.07595  -0.07788 230 HIS A CE1 
1900 N NE2 . HIS A 236 ? 0.74380 0.32610 0.36164 -0.22754 0.09325  -0.06705 230 HIS A NE2 
1901 N N   A TYR A 237 ? 0.69437 0.33814 0.41908 -0.18394 0.13777  -0.05142 231 TYR A N   
1902 N N   B TYR A 237 ? 0.68539 0.31744 0.40168 -0.16612 0.12289  -0.09024 231 TYR A N   
1903 C CA  A TYR A 237 ? 0.61587 0.39682 0.38363 -0.18792 0.09662  -0.05555 231 TYR A CA  
1904 C CA  B TYR A 237 ? 0.61886 0.33581 0.39959 -0.15710 0.13949  -0.14136 231 TYR A CA  
1905 C C   A TYR A 237 ? 0.46213 0.39959 0.30723 -0.21670 -0.02084 -0.04290 231 TYR A C   
1906 C C   B TYR A 237 ? 0.50153 0.34667 0.38573 -0.11129 0.11791  -0.13550 231 TYR A C   
1907 O O   A TYR A 237 ? 0.39601 0.41380 0.24013 -0.19522 -0.06572 -0.03536 231 TYR A O   
1908 O O   B TYR A 237 ? 0.43700 0.36262 0.38943 -0.06714 0.10639  -0.14285 231 TYR A O   
1909 C CB  A TYR A 237 ? 0.65487 0.43036 0.38218 -0.18688 0.12163  -0.06267 231 TYR A CB  
1910 C CB  B TYR A 237 ? 0.65427 0.35162 0.41040 -0.19510 0.16973  -0.14686 231 TYR A CB  
1911 C CG  A TYR A 237 ? 0.65164 0.46352 0.35171 -0.18975 0.13178  -0.08827 231 TYR A CG  
1912 C CG  B TYR A 237 ? 0.64527 0.40988 0.40807 -0.19778 0.15917  -0.12745 231 TYR A CG  
1913 C CD1 A TYR A 237 ? 0.69131 0.47504 0.32621 -0.17178 0.13220  -0.06920 231 TYR A CD1 
1914 C CD1 B TYR A 237 ? 0.63565 0.42869 0.39335 -0.20437 0.15598  -0.08499 231 TYR A CD1 
1915 C CD2 A TYR A 237 ? 0.60861 0.47883 0.36027 -0.22468 0.15844  -0.12719 231 TYR A CD2 
1916 C CD2 B TYR A 237 ? 0.63299 0.43915 0.44640 -0.21224 0.15299  -0.14008 231 TYR A CD2 
1917 C CE1 A TYR A 237 ? 0.67668 0.49012 0.29998 -0.17987 0.13451  -0.08721 231 TYR A CE1 
1918 C CE1 B TYR A 237 ? 0.63805 0.45372 0.40347 -0.20618 0.14706  -0.08600 231 TYR A CE1 
1919 C CE2 A TYR A 237 ? 0.60095 0.49101 0.35428 -0.24138 0.17624  -0.13589 231 TYR A CE2 
1920 C CE2 B TYR A 237 ? 0.62985 0.45496 0.46495 -0.22125 0.15393  -0.13477 231 TYR A CE2 
1921 C CZ  A TYR A 237 ? 0.62970 0.49779 0.33136 -0.21723 0.17731  -0.12888 231 TYR A CZ  
1922 C CZ  B TYR A 237 ? 0.61503 0.46629 0.44831 -0.22783 0.16142  -0.10334 231 TYR A CZ  
1923 O OH  A TYR A 237 ? 0.62153 0.49749 0.31915 -0.19759 0.18957  -0.14080 231 TYR A OH  
1924 O OH  B TYR A 237 ? 0.59765 0.48245 0.43773 -0.23338 0.17011  -0.08909 231 TYR A OH  
1925 N N   A LEU A 238 ? 0.39447 0.37437 0.32971 -0.21564 -0.04863 -0.03004 232 LEU A N   
1926 N N   B LEU A 238 ? 0.46126 0.32431 0.37483 -0.10588 0.13838  -0.14422 232 LEU A N   
1927 C CA  A LEU A 238 ? 0.34351 0.33375 0.40801 -0.18263 -0.01729 -0.02658 232 LEU A CA  
1928 C CA  B LEU A 238 ? 0.38416 0.29954 0.33288 -0.07719 0.03705  -0.11672 232 LEU A CA  
1929 C C   A LEU A 238 ? 0.33280 0.28395 0.36851 -0.14603 -0.01297 -0.04273 232 LEU A C   
1930 C C   B LEU A 238 ? 0.33868 0.31414 0.34165 -0.04988 0.04522  -0.10858 232 LEU A C   
1931 O O   A LEU A 238 ? 0.26934 0.24270 0.36936 -0.12111 -0.00898 -0.04680 232 LEU A O   
1932 O O   B LEU A 238 ? 0.35949 0.32534 0.40570 -0.03918 0.03934  -0.08530 232 LEU A O   
1933 C CB  A LEU A 238 ? 0.32064 0.36659 0.45513 -0.13872 -0.03778 0.00773  232 LEU A CB  
1934 C CB  B LEU A 238 ? 0.37981 0.26132 0.34126 -0.02422 0.05750  -0.06395 232 LEU A CB  
1935 C CG  A LEU A 238 ? 0.25992 0.38206 0.47910 -0.16771 -0.06718 -0.01261 232 LEU A CG  
1936 C CG  B LEU A 238 ? 0.38199 0.21929 0.33406 0.00120  -0.00324 -0.04907 232 LEU A CG  
1937 C CD1 A LEU A 238 ? 0.31197 0.37786 0.50512 -0.18654 -0.03521 -0.02526 232 LEU A CD1 
1938 C CD1 B LEU A 238 ? 0.37467 0.23212 0.34981 -0.03449 0.00295  -0.01576 232 LEU A CD1 
1939 C CD2 A LEU A 238 ? 0.23307 0.40638 0.52908 -0.15776 -0.03781 0.01404  232 LEU A CD2 
1940 C CD2 B LEU A 238 ? 0.36573 0.16727 0.33396 0.07266  -0.02758 -0.06358 232 LEU A CD2 
1941 N N   A ASP A 239 ? 0.37935 0.29375 0.39098 -0.13805 0.00583  -0.04107 233 ASP A N   
1942 N N   B ASP A 239 ? 0.36654 0.32588 0.32276 -0.05514 0.07939  -0.09005 233 ASP A N   
1943 C CA  A ASP A 239 ? 0.34696 0.29486 0.38315 -0.11177 0.00298  0.00539  233 ASP A CA  
1944 C CA  B ASP A 239 ? 0.33577 0.30993 0.31924 -0.02773 0.09753  -0.06888 233 ASP A CA  
1945 C C   A ASP A 239 ? 0.25011 0.29055 0.34617 -0.09394 -0.06856 0.00890  233 ASP A C   
1946 C C   B ASP A 239 ? 0.31824 0.28863 0.32678 -0.05643 0.06214  -0.04915 233 ASP A C   
1947 O O   A ASP A 239 ? 0.20395 0.31851 0.32858 -0.06436 -0.13319 0.06000  233 ASP A O   
1948 O O   B ASP A 239 ? 0.41431 0.29439 0.32408 -0.03172 0.14762  -0.02395 233 ASP A O   
1949 C CB  A ASP A 239 ? 0.40639 0.31597 0.39582 -0.07653 0.00175  0.06183  233 ASP A CB  
1950 C CB  B ASP A 239 ? 0.29570 0.32915 0.31035 0.01586  0.09564  -0.07148 233 ASP A CB  
1951 C CG  A ASP A 239 ? 0.43246 0.32972 0.40419 -0.06114 -0.02495 0.10462  233 ASP A CG  
1952 C CG  B ASP A 239 ? 0.27985 0.35065 0.34340 0.06332  0.07606  -0.05967 233 ASP A CG  
1953 O OD1 A ASP A 239 ? 0.44769 0.35482 0.40223 -0.04085 -0.04271 0.08961  233 ASP A OD1 
1954 O OD1 B ASP A 239 ? 0.25336 0.37657 0.33442 0.09322  0.03302  -0.04208 233 ASP A OD1 
1955 O OD2 A ASP A 239 ? 0.41881 0.31002 0.39756 -0.11016 -0.04457 0.13888  233 ASP A OD2 
1956 O OD2 B ASP A 239 ? 0.28166 0.34593 0.35745 0.08051  0.11227  -0.06054 233 ASP A OD2 
1957 N N   . GLN A 240 ? 0.25035 0.24119 0.31146 -0.09347 -0.02898 -0.03450 234 GLN A N   
1958 C CA  . GLN A 240 ? 0.23068 0.25802 0.27501 -0.06771 -0.06364 -0.02320 234 GLN A CA  
1959 C C   . GLN A 240 ? 0.22821 0.30924 0.27412 -0.06742 -0.07052 0.01798  234 GLN A C   
1960 O O   . GLN A 240 ? 0.26326 0.32307 0.26691 -0.04585 -0.03290 0.08482  234 GLN A O   
1961 C CB  . GLN A 240 ? 0.24430 0.25636 0.25351 -0.07671 -0.09533 -0.01037 234 GLN A CB  
1962 C CG  . GLN A 240 ? 0.21310 0.24801 0.32588 -0.07115 -0.08064 0.01106  234 GLN A CG  
1963 C CD  . GLN A 240 ? 0.23496 0.26274 0.33422 -0.03266 -0.05503 0.04854  234 GLN A CD  
1964 O OE1 . GLN A 240 ? 0.24574 0.24774 0.39649 -0.03014 -0.04708 0.05388  234 GLN A OE1 
1965 N NE2 . GLN A 240 ? 0.19534 0.28787 0.29456 -0.01826 -0.06059 0.04748  234 GLN A NE2 
1966 N N   . LEU A 241 ? 0.19877 0.33739 0.32660 -0.05349 -0.09508 0.02571  235 LEU A N   
1967 C CA  . LEU A 241 ? 0.18155 0.35379 0.35556 -0.03787 -0.11859 0.08225  235 LEU A CA  
1968 C C   . LEU A 241 ? 0.19995 0.35222 0.38398 -0.04409 -0.09601 0.04923  235 LEU A C   
1969 O O   . LEU A 241 ? 0.21886 0.36174 0.35621 -0.01718 -0.04946 0.08448  235 LEU A O   
1970 C CB  . LEU A 241 ? 0.17771 0.38963 0.41787 -0.03953 -0.11052 0.07251  235 LEU A CB  
1971 C CG  . LEU A 241 ? 0.20185 0.41492 0.48369 -0.10091 -0.05801 -0.01531 235 LEU A CG  
1972 C CD1 . LEU A 241 ? 0.22583 0.40309 0.50320 -0.11089 -0.01931 -0.06450 235 LEU A CD1 
1973 C CD2 . LEU A 241 ? 0.17753 0.43146 0.46420 -0.11370 -0.06489 -0.02446 235 LEU A CD2 
1974 N N   . ASN A 242 ? 0.27208 0.32577 0.40633 -0.07567 -0.03915 -0.01464 236 ASN A N   
1975 C CA  . ASN A 242 ? 0.37251 0.32620 0.35118 -0.04978 -0.02264 -0.01770 236 ASN A CA  
1976 C C   . ASN A 242 ? 0.37969 0.29589 0.28614 -0.08510 -0.02624 -0.02173 236 ASN A C   
1977 O O   . ASN A 242 ? 0.37913 0.31373 0.28585 -0.07899 -0.04695 0.00152  236 ASN A O   
1978 C CB  . ASN A 242 ? 0.32321 0.30222 0.34097 -0.04037 -0.02400 -0.03239 236 ASN A CB  
1979 C CG  . ASN A 242 ? 0.31734 0.31681 0.36904 0.01176  -0.03856 -0.00313 236 ASN A CG  
1980 O OD1 . ASN A 242 ? 0.28370 0.33985 0.46447 0.05063  -0.07314 0.00802  236 ASN A OD1 
1981 N ND2 . ASN A 242 ? 0.30007 0.32353 0.32844 0.00033  0.02216  -0.00859 236 ASN A ND2 
1982 N N   . HIS A 243 ? 0.31979 0.27400 0.28090 -0.05801 -0.05744 -0.00165 237 HIS A N   
1983 C CA  . HIS A 243 ? 0.30129 0.27885 0.30838 -0.02255 -0.04677 -0.00133 237 HIS A CA  
1984 C C   . HIS A 243 ? 0.28766 0.23793 0.29497 -0.01006 -0.02470 -0.01858 237 HIS A C   
1985 O O   . HIS A 243 ? 0.32269 0.21962 0.29589 -0.00488 -0.01613 -0.04114 237 HIS A O   
1986 C CB  . HIS A 243 ? 0.30549 0.28018 0.30452 0.02264  -0.08344 0.01933  237 HIS A CB  
1987 C CG  . HIS A 243 ? 0.34793 0.32299 0.33398 0.04849  0.00002  0.01122  237 HIS A CG  
1988 N ND1 . HIS A 243 ? 0.40355 0.35890 0.39689 0.04034  -0.00418 0.04230  237 HIS A ND1 
1989 C CD2 . HIS A 243 ? 0.38504 0.32827 0.38615 0.03623  0.02901  0.01797  237 HIS A CD2 
1990 C CE1 . HIS A 243 ? 0.42513 0.36208 0.42115 0.01986  0.06076  0.05110  237 HIS A CE1 
1991 N NE2 . HIS A 243 ? 0.39338 0.35811 0.40505 0.01017  0.04731  0.04459  237 HIS A NE2 
1992 N N   . ILE A 244 ? 0.21418 0.23718 0.29030 -0.01623 -0.05714 -0.00623 238 ILE A N   
1993 C CA  . ILE A 244 ? 0.21433 0.21619 0.23610 -0.02356 -0.05034 -0.01836 238 ILE A CA  
1994 C C   . ILE A 244 ? 0.26471 0.25206 0.26528 -0.00575 -0.00080 -0.00873 238 ILE A C   
1995 O O   . ILE A 244 ? 0.26569 0.26673 0.25814 -0.01584 0.01381  -0.00173 238 ILE A O   
1996 C CB  . ILE A 244 ? 0.23967 0.18907 0.21953 -0.00430 -0.02970 0.00325  238 ILE A CB  
1997 C CG1 . ILE A 244 ? 0.21053 0.22300 0.23743 0.00137  -0.01805 -0.04927 238 ILE A CG1 
1998 C CG2 . ILE A 244 ? 0.26323 0.18326 0.24849 -0.01980 0.00703  0.01075  238 ILE A CG2 
1999 C CD1 . ILE A 244 ? 0.19007 0.25441 0.27170 0.00336  -0.00202 -0.05446 238 ILE A CD1 
2000 N N   . LEU A 245 ? 0.27005 0.25984 0.26615 -0.01412 -0.01390 0.00010  239 LEU A N   
2001 C CA  . LEU A 245 ? 0.26157 0.29799 0.25230 -0.00852 -0.05519 -0.02144 239 LEU A CA  
2002 C C   . LEU A 245 ? 0.31216 0.29284 0.28140 -0.01344 -0.03375 -0.02024 239 LEU A C   
2003 O O   . LEU A 245 ? 0.34736 0.27159 0.26326 -0.01368 -0.06708 -0.01690 239 LEU A O   
2004 C CB  . LEU A 245 ? 0.19610 0.33050 0.31387 -0.01621 -0.03864 -0.01530 239 LEU A CB  
2005 C CG  . LEU A 245 ? 0.22625 0.36058 0.34241 0.01924  -0.01568 0.01361  239 LEU A CG  
2006 C CD1 . LEU A 245 ? 0.24208 0.43910 0.36865 0.01957  -0.00489 -0.00771 239 LEU A CD1 
2007 C CD2 . LEU A 245 ? 0.35306 0.37272 0.36092 0.03060  0.04760  0.00904  239 LEU A CD2 
2008 N N   . GLY A 246 ? 0.32133 0.28963 0.27195 -0.02325 0.00140  -0.06519 240 GLY A N   
2009 C CA  . GLY A 246 ? 0.31324 0.32202 0.26924 -0.05710 -0.03242 -0.08209 240 GLY A CA  
2010 C C   . GLY A 246 ? 0.32244 0.33038 0.27579 -0.04861 -0.01078 -0.08108 240 GLY A C   
2011 O O   . GLY A 246 ? 0.38185 0.35624 0.27004 -0.05590 0.02167  -0.10640 240 GLY A O   
2012 N N   . ILE A 247 ? 0.28620 0.29567 0.27178 -0.02387 -0.03975 -0.06004 241 ILE A N   
2013 C CA  . ILE A 247 ? 0.26103 0.29839 0.30020 -0.02005 -0.04123 -0.01682 241 ILE A CA  
2014 C C   . ILE A 247 ? 0.26625 0.29424 0.23471 0.00540  -0.04203 -0.02375 241 ILE A C   
2015 O O   . ILE A 247 ? 0.27066 0.28865 0.23996 0.01330  0.00927  -0.00197 241 ILE A O   
2016 C CB  . ILE A 247 ? 0.21553 0.31450 0.35706 -0.00313 -0.07765 0.00780  241 ILE A CB  
2017 C CG1 . ILE A 247 ? 0.30009 0.36722 0.45291 -0.00410 -0.03984 0.02234  241 ILE A CG1 
2018 C CG2 . ILE A 247 ? 0.25448 0.32732 0.32915 -0.00934 -0.05210 -0.02601 241 ILE A CG2 
2019 C CD1 . ILE A 247 ? 0.35177 0.40483 0.51304 0.03107  0.02448  0.03682  241 ILE A CD1 
2020 N N   . LEU A 248 ? 0.25850 0.29804 0.23270 0.00435  -0.04115 -0.04187 242 LEU A N   
2021 C CA  . LEU A 248 ? 0.24497 0.28596 0.22397 0.00880  -0.03876 -0.04148 242 LEU A CA  
2022 C C   . LEU A 248 ? 0.26339 0.31307 0.22244 -0.02193 -0.04344 -0.05689 242 LEU A C   
2023 O O   . LEU A 248 ? 0.33439 0.31629 0.25779 -0.00936 -0.06264 -0.03222 242 LEU A O   
2024 C CB  A LEU A 248 ? 0.23202 0.25341 0.22185 -0.01039 -0.00664 -0.03408 242 LEU A CB  
2025 C CB  B LEU A 248 ? 0.22682 0.27040 0.19724 -0.02684 0.00253  -0.05186 242 LEU A CB  
2026 C CG  A LEU A 248 ? 0.21596 0.25543 0.21691 -0.02533 -0.03442 -0.00796 242 LEU A CG  
2027 C CG  B LEU A 248 ? 0.22765 0.28668 0.15824 -0.05141 -0.01668 -0.04087 242 LEU A CG  
2028 C CD1 A LEU A 248 ? 0.23659 0.26598 0.19374 -0.00803 -0.04906 -0.01351 242 LEU A CD1 
2029 C CD1 B LEU A 248 ? 0.23674 0.28862 0.17612 -0.03683 -0.00486 -0.07379 242 LEU A CD1 
2030 C CD2 A LEU A 248 ? 0.18723 0.25619 0.26553 -0.05057 -0.02821 -0.00173 242 LEU A CD2 
2031 C CD2 B LEU A 248 ? 0.23057 0.29697 0.18085 -0.07150 -0.06348 -0.02042 242 LEU A CD2 
2032 N N   . GLY A 249 ? 0.21338 0.33350 0.22540 -0.04655 -0.06967 -0.05723 243 GLY A N   
2033 C CA  . GLY A 249 ? 0.23592 0.34970 0.24132 -0.02142 -0.05443 -0.04144 243 GLY A CA  
2034 C C   . GLY A 249 ? 0.27266 0.35385 0.22851 -0.01813 -0.02425 -0.01717 243 GLY A C   
2035 O O   . GLY A 249 ? 0.32597 0.36670 0.19524 0.00579  -0.03390 -0.00728 243 GLY A O   
2036 N N   . SER A 250 ? 0.25624 0.31220 0.24062 -0.00566 -0.06091 -0.01402 244 SER A N   
2037 C CA  . SER A 250 ? 0.25760 0.29029 0.25128 0.02008  -0.05568 -0.01105 244 SER A CA  
2038 C C   . SER A 250 ? 0.27754 0.29964 0.24923 -0.00906 -0.05019 -0.03263 244 SER A C   
2039 O O   . SER A 250 ? 0.29689 0.31831 0.25241 0.00311  0.00155  -0.01785 244 SER A O   
2040 C CB  . SER A 250 ? 0.24914 0.29411 0.26908 -0.01605 -0.02895 -0.04719 244 SER A CB  
2041 O OG  . SER A 250 ? 0.31012 0.29629 0.27748 -0.04644 0.01283  -0.06856 244 SER A OG  
2042 N N   . PRO A 251 ? 0.25442 0.28671 0.23811 -0.00225 -0.03505 -0.02557 245 PRO A N   
2043 C CA  . PRO A 251 ? 0.24021 0.30186 0.20549 0.02512  -0.05891 0.01974  245 PRO A CA  
2044 C C   . PRO A 251 ? 0.27169 0.32498 0.21034 -0.01621 -0.02200 0.00250  245 PRO A C   
2045 O O   . PRO A 251 ? 0.26684 0.33954 0.21895 -0.02176 -0.05705 0.00125  245 PRO A O   
2046 C CB  . PRO A 251 ? 0.36647 0.31122 0.16575 0.04319  -0.05680 0.02891  245 PRO A CB  
2047 C CG  . PRO A 251 ? 0.44187 0.29927 0.23415 0.02821  0.02353  0.01814  245 PRO A CG  
2048 C CD  . PRO A 251 ? 0.36169 0.28088 0.20566 0.01477  -0.02313 -0.02889 245 PRO A CD  
2049 N N   . SER A 252 ? 0.26790 0.30677 0.24090 -0.04074 0.00426  0.00220  246 SER A N   
2050 C CA  . SER A 252 ? 0.25031 0.29183 0.26024 -0.03563 -0.04892 0.02335  246 SER A CA  
2051 C C   . SER A 252 ? 0.23815 0.31700 0.28950 -0.03251 -0.10482 0.03178  246 SER A C   
2052 O O   . SER A 252 ? 0.32324 0.29711 0.30319 -0.02489 -0.05862 0.03213  246 SER A O   
2053 C CB  . SER A 252 ? 0.33211 0.28954 0.26920 -0.02764 -0.02446 0.00062  246 SER A CB  
2054 O OG  . SER A 252 ? 0.33735 0.27458 0.27328 -0.04702 -0.02395 -0.00965 246 SER A OG  
2055 N N   . GLN A 253 ? 0.22987 0.35350 0.34213 -0.00907 -0.10811 0.00458  247 GLN A N   
2056 C CA  . GLN A 253 ? 0.27465 0.38137 0.36801 0.01698  -0.10537 -0.00337 247 GLN A CA  
2057 C C   . GLN A 253 ? 0.31691 0.36541 0.35859 0.01527  -0.05162 0.00714  247 GLN A C   
2058 O O   . GLN A 253 ? 0.26025 0.35496 0.36486 0.05296  -0.03971 0.02402  247 GLN A O   
2059 C CB  . GLN A 253 ? 0.27378 0.43835 0.40928 0.04898  -0.13451 0.00048  247 GLN A CB  
2060 C CG  . GLN A 253 ? 0.28140 0.48539 0.43469 0.05562  -0.10206 -0.01995 247 GLN A CG  
2061 C CD  A GLN A 253 ? 0.32205 0.52528 0.43737 0.05574  -0.08439 0.00802  247 GLN A CD  
2062 C CD  B GLN A 253 ? 0.30321 0.49026 0.44100 0.04871  -0.10174 -0.05217 247 GLN A CD  
2063 O OE1 A GLN A 253 ? 0.33982 0.55237 0.46582 0.04960  -0.07736 0.00369  247 GLN A OE1 
2064 O OE1 B GLN A 253 ? 0.33400 0.48592 0.46101 0.04624  -0.07526 -0.08719 247 GLN A OE1 
2065 N NE2 A GLN A 253 ? 0.35649 0.53738 0.41165 0.03704  -0.08702 0.01693  247 GLN A NE2 
2066 N NE2 B GLN A 253 ? 0.28693 0.49672 0.43937 0.04025  -0.12220 -0.04670 247 GLN A NE2 
2067 N N   . GLU A 254 ? 0.34720 0.36459 0.32858 -0.01551 -0.09347 -0.01633 248 GLU A N   
2068 C CA  . GLU A 254 ? 0.40352 0.37467 0.36035 -0.00398 -0.04639 -0.00790 248 GLU A CA  
2069 C C   . GLU A 254 ? 0.34554 0.38065 0.35173 0.00273  -0.02160 0.00309  248 GLU A C   
2070 O O   . GLU A 254 ? 0.32117 0.38954 0.35795 0.05350  -0.03410 -0.01343 248 GLU A O   
2071 C CB  . GLU A 254 ? 0.48226 0.36977 0.41390 -0.03181 -0.00278 -0.00064 248 GLU A CB  
2072 C CG  . GLU A 254 ? 0.49656 0.39955 0.45092 -0.03678 -0.04447 0.03479  248 GLU A CG  
2073 C CD  . GLU A 254 ? 0.49885 0.42604 0.46582 -0.05283 -0.07298 0.10530  248 GLU A CD  
2074 O OE1 . GLU A 254 ? 0.45214 0.42768 0.44938 -0.07143 -0.14597 0.12251  248 GLU A OE1 
2075 O OE2 . GLU A 254 ? 0.57004 0.43987 0.49460 -0.03983 0.00175  0.13840  248 GLU A OE2 
2076 N N   . ASP A 255 ? 0.28499 0.37937 0.29788 0.01410  -0.02028 0.03704  249 ASP A N   
2077 C CA  . ASP A 255 ? 0.25892 0.40087 0.28063 0.00083  -0.01465 0.02620  249 ASP A CA  
2078 C C   . ASP A 255 ? 0.27189 0.35745 0.24875 -0.02904 -0.04705 0.04551  249 ASP A C   
2079 O O   . ASP A 255 ? 0.27314 0.37071 0.24483 -0.05077 -0.03860 0.05598  249 ASP A O   
2080 C CB  . ASP A 255 ? 0.25201 0.44845 0.27876 -0.01043 -0.03046 0.02532  249 ASP A CB  
2081 C CG  . ASP A 255 ? 0.28258 0.48858 0.28365 0.03465  -0.02768 0.03530  249 ASP A CG  
2082 O OD1 . ASP A 255 ? 0.28328 0.47345 0.27192 0.04404  -0.02281 0.05394  249 ASP A OD1 
2083 O OD2 . ASP A 255 ? 0.27185 0.52253 0.31312 0.07417  -0.02357 -0.00379 249 ASP A OD2 
2084 N N   . LEU A 256 ? 0.25538 0.34657 0.27278 0.00355  -0.04536 0.05037  250 LEU A N   
2085 C CA  . LEU A 256 ? 0.26101 0.36572 0.32067 0.03292  -0.02951 0.03725  250 LEU A CA  
2086 C C   . LEU A 256 ? 0.27629 0.39292 0.32223 0.00600  -0.01169 0.04124  250 LEU A C   
2087 O O   . LEU A 256 ? 0.33332 0.38837 0.34142 -0.03526 0.03405  0.06530  250 LEU A O   
2088 C CB  . LEU A 256 ? 0.31999 0.40734 0.34834 0.02105  -0.07633 0.01706  250 LEU A CB  
2089 C CG  . LEU A 256 ? 0.40400 0.43869 0.38178 0.02310  -0.11223 -0.00234 250 LEU A CG  
2090 C CD1 . LEU A 256 ? 0.37819 0.45960 0.41793 0.01383  -0.17186 -0.03518 250 LEU A CD1 
2091 C CD2 . LEU A 256 ? 0.46177 0.46570 0.41504 0.04156  -0.04475 0.00494  250 LEU A CD2 
2092 N N   . ASN A 257 ? 0.27632 0.44933 0.39264 0.02108  -0.00046 0.03091  251 ASN A N   
2093 C CA  . ASN A 257 ? 0.33545 0.51558 0.45626 0.04331  0.05681  -0.00253 251 ASN A CA  
2094 C C   . ASN A 257 ? 0.31015 0.53965 0.47809 0.05704  0.03161  -0.02351 251 ASN A C   
2095 O O   . ASN A 257 ? 0.33635 0.56538 0.52029 0.11845  0.04821  -0.04122 251 ASN A O   
2096 C CB  . ASN A 257 ? 0.39287 0.55554 0.49244 0.05872  0.04360  0.00731  251 ASN A CB  
2097 C CG  . ASN A 257 ? 0.42908 0.58649 0.54325 0.07240  0.03958  0.06541  251 ASN A CG  
2098 O OD1 . ASN A 257 ? 0.38403 0.60154 0.55693 0.02286  0.00231  0.06869  251 ASN A OD1 
2099 N ND2 . ASN A 257 ? 0.48708 0.59322 0.55926 0.12781  0.05582  0.09622  251 ASN A ND2 
2100 N N   . CME A 258 ? 0.26539 0.52497 0.46820 0.02737  -0.02185 -0.00117 252 CME A N   
2101 C CA  . CME A 258 ? 0.31866 0.52927 0.48712 -0.00761 0.01772  -0.02422 252 CME A CA  
2102 C CB  . CME A 258 ? 0.39199 0.55936 0.58979 -0.00449 0.03328  -0.05565 252 CME A CB  
2103 S SG  . CME A 258 ? 0.52518 0.59547 0.69439 0.03481  0.10214  -0.05990 252 CME A SG  
2104 S SD  . CME A 258 ? 0.34327 0.53143 0.59922 0.06147  -0.02257 -0.13404 252 CME A SD  
2105 C CE  . CME A 258 ? 0.33766 0.50627 0.60369 0.16480  -0.06652 -0.11377 252 CME A CE  
2106 C CZ  . CME A 258 ? 0.36866 0.51000 0.59762 0.20397  -0.09684 -0.08375 252 CME A CZ  
2107 O OH  . CME A 258 ? 0.41309 0.53226 0.58317 0.19572  -0.13034 -0.07603 252 CME A OH  
2108 C C   . CME A 258 ? 0.34448 0.51357 0.39801 -0.03363 0.07021  -0.01674 252 CME A C   
2109 O O   . CME A 258 ? 0.46009 0.53026 0.40186 -0.06315 0.06774  -0.05165 252 CME A O   
2110 N N   . ILE A 259 ? 0.22436 0.48390 0.34833 -0.03886 0.02636  0.02174  253 ILE A N   
2111 C CA  . ILE A 259 ? 0.19750 0.46940 0.37450 0.00302  0.01976  0.03125  253 ILE A CA  
2112 C C   . ILE A 259 ? 0.20915 0.50084 0.39543 0.01630  0.02176  0.03826  253 ILE A C   
2113 O O   . ILE A 259 ? 0.22817 0.53246 0.40011 -0.01565 0.03035  0.03810  253 ILE A O   
2114 C CB  . ILE A 259 ? 0.16442 0.44032 0.34645 0.02288  -0.01242 0.00563  253 ILE A CB  
2115 C CG1 . ILE A 259 ? 0.17118 0.42528 0.36197 0.07096  0.01050  -0.00447 253 ILE A CG1 
2116 C CG2 . ILE A 259 ? 0.19770 0.42436 0.33574 -0.02681 0.00846  -0.02478 253 ILE A CG2 
2117 C CD1 . ILE A 259 ? 0.27347 0.43318 0.40767 0.07823  0.09437  -0.04363 253 ILE A CD1 
2118 N N   . ILE A 260 ? 0.23201 0.50596 0.43789 0.03631  0.08637  0.03643  254 ILE A N   
2119 C CA  . ILE A 260 ? 0.22513 0.51476 0.46312 0.06278  0.05838  0.04827  254 ILE A CA  
2120 C C   . ILE A 260 ? 0.26487 0.50067 0.41014 0.05867  0.06557  0.06703  254 ILE A C   
2121 O O   . ILE A 260 ? 0.32627 0.52408 0.44927 0.02265  0.07361  0.10733  254 ILE A O   
2122 C CB  . ILE A 260 ? 0.33325 0.54956 0.54429 0.08951  -0.00897 0.06453  254 ILE A CB  
2123 C CG1 . ILE A 260 ? 0.38004 0.57784 0.61735 0.10939  0.03363  0.04346  254 ILE A CG1 
2124 C CG2 . ILE A 260 ? 0.41503 0.56018 0.57018 0.07959  0.00020  0.05244  254 ILE A CG2 
2125 C CD1 . ILE A 260 ? 0.42230 0.60567 0.64421 0.11046  0.06291  0.04316  254 ILE A CD1 
2126 N N   . ASN A 261 ? 0.25752 0.44781 0.35478 0.04621  0.07775  0.04945  255 ASN A N   
2127 C CA  . ASN A 261 ? 0.22576 0.41971 0.26641 0.05632  0.01075  0.05231  255 ASN A CA  
2128 C C   . ASN A 261 ? 0.16683 0.45147 0.31347 0.02476  -0.01885 0.04194  255 ASN A C   
2129 O O   . ASN A 261 ? 0.20722 0.44772 0.30808 0.04700  0.05660  0.05043  255 ASN A O   
2130 C CB  . ASN A 261 ? 0.27310 0.38800 0.26694 0.01318  -0.00585 0.05099  255 ASN A CB  
2131 C CG  . ASN A 261 ? 0.37130 0.37462 0.28325 -0.00604 0.01855  0.01730  255 ASN A CG  
2132 O OD1 . ASN A 261 ? 0.39521 0.36082 0.27393 0.01139  -0.00482 -0.00394 255 ASN A OD1 
2133 N ND2 . ASN A 261 ? 0.34486 0.37681 0.30185 0.00641  -0.00386 0.02784  255 ASN A ND2 
2134 N N   . LEU A 262 ? 0.20063 0.48603 0.33016 0.00995  -0.01098 0.04689  256 LEU A N   
2135 C CA  . LEU A 262 ? 0.20023 0.52268 0.36263 0.03071  0.01980  0.04196  256 LEU A CA  
2136 C C   . LEU A 262 ? 0.17940 0.53836 0.33056 -0.00441 0.00099  0.02282  256 LEU A C   
2137 O O   . LEU A 262 ? 0.18825 0.57714 0.31279 -0.01801 -0.00343 0.01553  256 LEU A O   
2138 C CB  A LEU A 262 ? 0.19886 0.53899 0.39673 0.06617  0.08910  0.00360  256 LEU A CB  
2139 C CB  B LEU A 262 ? 0.27308 0.50866 0.37822 0.02117  0.01198  0.04235  256 LEU A CB  
2140 C CG  A LEU A 262 ? 0.19113 0.49823 0.40425 0.10066  0.08562  -0.02026 256 LEU A CG  
2141 C CG  B LEU A 262 ? 0.29800 0.46552 0.37414 0.04545  -0.02261 0.05208  256 LEU A CG  
2142 C CD1 A LEU A 262 ? 0.17817 0.46862 0.37858 0.11407  0.04791  -0.02299 256 LEU A CD1 
2143 C CD1 B LEU A 262 ? 0.27856 0.44818 0.35917 0.06536  -0.03996 0.01947  256 LEU A CD1 
2144 C CD2 A LEU A 262 ? 0.23007 0.51872 0.39642 0.11566  0.08340  -0.03378 256 LEU A CD2 
2145 C CD2 B LEU A 262 ? 0.33938 0.44674 0.39108 0.08866  0.00520  0.10426  256 LEU A CD2 
2146 N N   . LYS A 263 ? 0.20200 0.51050 0.29685 -0.03114 -0.00594 0.05192  257 LYS A N   
2147 C CA  . LYS A 263 ? 0.24232 0.45105 0.26311 -0.03461 0.00979  0.07198  257 LYS A CA  
2148 C C   . LYS A 263 ? 0.21406 0.38353 0.26759 -0.01950 -0.00925 0.03896  257 LYS A C   
2149 O O   . LYS A 263 ? 0.21159 0.35935 0.23491 -0.01089 -0.01306 0.00170  257 LYS A O   
2150 C CB  . LYS A 263 ? 0.27689 0.48027 0.27590 -0.09638 0.08311  0.07496  257 LYS A CB  
2151 C CG  . LYS A 263 ? 0.34143 0.52362 0.34106 -0.09433 0.13151  0.11814  257 LYS A CG  
2152 C CD  . LYS A 263 ? 0.34303 0.54745 0.41762 -0.11467 0.13184  0.13032  257 LYS A CD  
2153 C CE  . LYS A 263 ? 0.41882 0.56894 0.48002 -0.08075 0.11096  0.12596  257 LYS A CE  
2154 N NZ  . LYS A 263 ? 0.43216 0.57818 0.49951 -0.04963 0.04057  0.13816  257 LYS A NZ  
2155 N N   . ALA A 264 ? 0.15598 0.37864 0.26866 -0.03476 -0.00295 0.01185  258 ALA A N   
2156 C CA  . ALA A 264 ? 0.17963 0.35879 0.25887 -0.01310 -0.01569 0.02593  258 ALA A CA  
2157 C C   . ALA A 264 ? 0.17467 0.32074 0.24513 -0.01905 -0.02341 0.03665  258 ALA A C   
2158 O O   . ALA A 264 ? 0.17112 0.29006 0.24586 0.00808  -0.01538 0.01167  258 ALA A O   
2159 C CB  . ALA A 264 ? 0.25554 0.33343 0.23470 0.01200  -0.05796 0.01043  258 ALA A CB  
2160 N N   . ARG A 265 ? 0.18907 0.33179 0.19598 0.01989  -0.05385 0.02187  259 ARG A N   
2161 C CA  . ARG A 265 ? 0.21946 0.32186 0.20559 0.05561  -0.04559 0.04383  259 ARG A CA  
2162 C C   . ARG A 265 ? 0.19912 0.31453 0.23078 0.02256  -0.00713 0.02508  259 ARG A C   
2163 O O   . ARG A 265 ? 0.23090 0.29073 0.25606 -0.00019 0.01117  0.03469  259 ARG A O   
2164 C CB  . ARG A 265 ? 0.30804 0.33115 0.19698 0.10143  -0.08959 0.04831  259 ARG A CB  
2165 C CG  . ARG A 265 ? 0.33672 0.33930 0.23196 0.13297  -0.08391 0.05500  259 ARG A CG  
2166 C CD  . ARG A 265 ? 0.33066 0.37048 0.27465 0.05275  -0.10892 0.02465  259 ARG A CD  
2167 N NE  . ARG A 265 ? 0.26124 0.37368 0.36928 -0.01713 -0.04455 0.05557  259 ARG A NE  
2168 C CZ  . ARG A 265 ? 0.28748 0.39822 0.41661 -0.04872 0.00011  0.07627  259 ARG A CZ  
2169 N NH1 . ARG A 265 ? 0.26189 0.43107 0.41635 -0.01832 -0.01218 0.09647  259 ARG A NH1 
2170 N NH2 . ARG A 265 ? 0.32449 0.39027 0.41898 -0.06668 -0.00413 0.05955  259 ARG A NH2 
2171 N N   . ASN A 266 ? 0.20079 0.33964 0.25492 -0.00572 -0.02095 0.01414  260 ASN A N   
2172 C CA  . ASN A 266 ? 0.13199 0.36404 0.28422 -0.01622 -0.04218 0.02933  260 ASN A CA  
2173 C C   . ASN A 266 ? 0.16131 0.31777 0.26384 -0.04589 -0.04415 0.01484  260 ASN A C   
2174 O O   . ASN A 266 ? 0.25278 0.31681 0.24756 -0.03980 0.00257  -0.00150 260 ASN A O   
2175 C CB  . ASN A 266 ? 0.11228 0.40977 0.29402 0.02354  -0.01640 0.04445  260 ASN A CB  
2176 C CG  . ASN A 266 ? 0.24759 0.42767 0.31167 0.02201  0.01383  0.04681  260 ASN A CG  
2177 O OD1 . ASN A 266 ? 0.28886 0.41923 0.37404 0.02511  0.02518  0.03494  260 ASN A OD1 
2178 N ND2 . ASN A 266 ? 0.26382 0.43154 0.29098 0.03124  0.01779  0.04887  260 ASN A ND2 
2179 N N   . TYR A 267 ? 0.17295 0.31885 0.23159 -0.01982 -0.05059 0.02916  261 TYR A N   
2180 C CA  . TYR A 267 ? 0.26399 0.29534 0.20072 0.00384  -0.01676 0.05838  261 TYR A CA  
2181 C C   . TYR A 267 ? 0.26030 0.26767 0.21898 0.01038  0.03801  0.06085  261 TYR A C   
2182 O O   . TYR A 267 ? 0.25256 0.27015 0.24125 -0.00577 0.03016  -0.02688 261 TYR A O   
2183 C CB  . TYR A 267 ? 0.26764 0.28678 0.18319 0.00202  -0.05299 0.03413  261 TYR A CB  
2184 C CG  . TYR A 267 ? 0.31716 0.28526 0.23703 0.02914  -0.01740 0.04080  261 TYR A CG  
2185 C CD1 . TYR A 267 ? 0.30214 0.26831 0.26907 0.03550  -0.05517 0.05290  261 TYR A CD1 
2186 C CD2 . TYR A 267 ? 0.24264 0.30486 0.25684 0.02415  -0.03665 0.01397  261 TYR A CD2 
2187 C CE1 . TYR A 267 ? 0.28927 0.28141 0.29586 0.01916  -0.03953 0.02808  261 TYR A CE1 
2188 C CE2 . TYR A 267 ? 0.27323 0.29041 0.31263 0.00114  -0.01415 0.00467  261 TYR A CE2 
2189 C CZ  . TYR A 267 ? 0.28488 0.27741 0.30155 0.01774  -0.06077 -0.00302 261 TYR A CZ  
2190 O OH  . TYR A 267 ? 0.31795 0.27865 0.35755 0.05618  -0.06185 -0.03424 261 TYR A OH  
2191 N N   . LEU A 268 ? 0.20343 0.25684 0.23682 -0.00528 -0.01131 0.05545  262 LEU A N   
2192 C CA  . LEU A 268 ? 0.20218 0.23585 0.21636 -0.06645 -0.05965 -0.00092 262 LEU A CA  
2193 C C   . LEU A 268 ? 0.24915 0.23437 0.21873 -0.04529 -0.03829 0.00834  262 LEU A C   
2194 O O   . LEU A 268 ? 0.22148 0.26344 0.22489 -0.03117 -0.02134 0.01994  262 LEU A O   
2195 C CB  . LEU A 268 ? 0.18888 0.26879 0.26407 -0.06465 -0.06313 -0.02211 262 LEU A CB  
2196 C CG  . LEU A 268 ? 0.16147 0.30361 0.27216 -0.02824 -0.06804 -0.02856 262 LEU A CG  
2197 C CD1 . LEU A 268 ? 0.30471 0.32364 0.28841 -0.01368 -0.03033 -0.03301 262 LEU A CD1 
2198 C CD2 . LEU A 268 ? 0.15253 0.33884 0.27547 0.01376  -0.04295 -0.03651 262 LEU A CD2 
2199 N N   . LEU A 269 ? 0.25477 0.24375 0.20883 -0.04666 -0.05588 0.01629  263 LEU A N   
2200 C CA  . LEU A 269 ? 0.27015 0.25165 0.25608 -0.01728 -0.04978 -0.01889 263 LEU A CA  
2201 C C   . LEU A 269 ? 0.26166 0.28644 0.28775 -0.00319 -0.03563 -0.01687 263 LEU A C   
2202 O O   . LEU A 269 ? 0.30411 0.32127 0.27898 -0.00945 -0.03267 0.00260  263 LEU A O   
2203 C CB  . LEU A 269 ? 0.24489 0.28526 0.26970 0.01122  -0.06962 0.02833  263 LEU A CB  
2204 C CG  . LEU A 269 ? 0.30665 0.30908 0.29890 0.05632  0.00719  0.04328  263 LEU A CG  
2205 C CD1 . LEU A 269 ? 0.31694 0.33998 0.36095 0.06120  0.04793  0.04665  263 LEU A CD1 
2206 C CD2 . LEU A 269 ? 0.35463 0.32502 0.27875 0.03227  0.04046  0.04318  263 LEU A CD2 
2207 N N   . SER A 270 ? 0.26434 0.25685 0.28069 -0.01201 -0.04509 0.01408  264 SER A N   
2208 C CA  . SER A 270 ? 0.31476 0.28240 0.28425 0.00891  -0.01628 0.01209  264 SER A CA  
2209 C C   . SER A 270 ? 0.31924 0.29586 0.27946 0.00001  -0.02851 -0.00724 264 SER A C   
2210 O O   . SER A 270 ? 0.33739 0.31645 0.30345 0.00057  -0.03148 -0.02404 264 SER A O   
2211 C CB  . SER A 270 ? 0.37163 0.29871 0.28945 0.00279  -0.00946 0.03013  264 SER A CB  
2212 O OG  . SER A 270 ? 0.40543 0.28401 0.27121 -0.00695 0.00850  0.06525  264 SER A OG  
2213 N N   . LEU A 271 ? 0.28085 0.28745 0.21728 -0.02890 -0.03819 0.00468  265 LEU A N   
2214 C CA  . LEU A 271 ? 0.29202 0.29619 0.21950 -0.01255 -0.05256 0.00408  265 LEU A CA  
2215 C C   . LEU A 271 ? 0.31036 0.28700 0.22984 0.00624  -0.03990 0.01709  265 LEU A C   
2216 O O   . LEU A 271 ? 0.32740 0.28782 0.27576 0.00324  -0.03540 0.04132  265 LEU A O   
2217 C CB  . LEU A 271 ? 0.28408 0.30316 0.18724 -0.00891 -0.07135 -0.00001 265 LEU A CB  
2218 C CG  . LEU A 271 ? 0.28240 0.29198 0.22298 -0.05116 -0.06935 -0.01670 265 LEU A CG  
2219 C CD1 . LEU A 271 ? 0.26377 0.32201 0.22072 -0.02551 -0.05159 -0.02449 265 LEU A CD1 
2220 C CD2 . LEU A 271 ? 0.30840 0.31419 0.30675 -0.04528 -0.03781 0.01329  265 LEU A CD2 
2221 N N   . PRO A 272 ? 0.34206 0.27419 0.23230 0.01850  -0.01299 -0.00225 266 PRO A N   
2222 C CA  . PRO A 272 ? 0.36555 0.28990 0.20112 -0.00252 -0.03416 -0.00136 266 PRO A CA  
2223 C C   . PRO A 272 ? 0.36156 0.29802 0.19257 -0.05818 -0.01390 0.04248  266 PRO A C   
2224 O O   . PRO A 272 ? 0.33520 0.32475 0.24028 -0.03725 -0.01558 0.03050  266 PRO A O   
2225 C CB  . PRO A 272 ? 0.44488 0.29400 0.23304 0.04839  0.05577  -0.01254 266 PRO A CB  
2226 C CG  . PRO A 272 ? 0.52404 0.32225 0.26307 0.07594  0.07225  -0.01306 266 PRO A CG  
2227 C CD  . PRO A 272 ? 0.45694 0.30130 0.25698 0.08398  0.06897  -0.01543 266 PRO A CD  
2228 N N   . HIS A 273 ? 0.36424 0.32134 0.20572 -0.09637 0.02214  0.04497  267 HIS A N   
2229 C CA  . HIS A 273 ? 0.40575 0.33925 0.21207 -0.11004 -0.00127 0.00864  267 HIS A CA  
2230 C C   . HIS A 273 ? 0.39749 0.35814 0.25288 -0.11149 0.01394  -0.06865 267 HIS A C   
2231 O O   . HIS A 273 ? 0.51982 0.35150 0.31727 -0.10239 0.02693  -0.09877 267 HIS A O   
2232 C CB  . HIS A 273 ? 0.45963 0.32905 0.21248 -0.09233 -0.00903 0.02198  267 HIS A CB  
2233 C CG  . HIS A 273 ? 0.51848 0.30325 0.25495 -0.07198 0.01041  -0.00145 267 HIS A CG  
2234 N ND1 . HIS A 273 ? 0.51034 0.32205 0.32015 -0.05846 -0.00077 0.01501  267 HIS A ND1 
2235 C CD2 . HIS A 273 ? 0.53367 0.29086 0.31622 -0.06242 0.02027  -0.00097 267 HIS A CD2 
2236 C CE1 . HIS A 273 ? 0.53688 0.30764 0.31954 -0.04558 -0.00176 0.01500  267 HIS A CE1 
2237 N NE2 . HIS A 273 ? 0.56196 0.30516 0.38512 -0.04669 0.03613  0.01706  267 HIS A NE2 
2238 N N   . LYS A 274 ? 0.29557 0.40538 0.28267 -0.13320 0.00138  -0.06595 268 LYS A N   
2239 C CA  . LYS A 274 ? 0.31845 0.44597 0.31319 -0.13768 0.05002  -0.08683 268 LYS A CA  
2240 C C   . LYS A 274 ? 0.32858 0.46417 0.29136 -0.12555 0.04802  -0.07218 268 LYS A C   
2241 O O   . LYS A 274 ? 0.31822 0.45836 0.26928 -0.10483 -0.00945 -0.01811 268 LYS A O   
2242 C CB  . LYS A 274 ? 0.30498 0.46954 0.36761 -0.15569 0.05330  -0.06333 268 LYS A CB  
2243 C CG  . LYS A 274 ? 0.31066 0.48887 0.36130 -0.16824 0.07679  -0.08547 268 LYS A CG  
2244 C CD  . LYS A 274 ? 0.26608 0.51375 0.39370 -0.14878 0.07924  -0.04612 268 LYS A CD  
2245 C CE  . LYS A 274 ? 0.28392 0.51119 0.39741 -0.18016 0.00818  -0.04514 268 LYS A CE  
2246 N NZ  . LYS A 274 ? 0.30976 0.52921 0.41788 -0.16971 -0.00261 -0.01468 268 LYS A NZ  
2247 N N   . ASN A 275 ? 0.41695 0.50044 0.26413 -0.15243 0.07367  -0.09209 269 ASN A N   
2248 C CA  . ASN A 275 ? 0.37254 0.52316 0.24871 -0.15326 0.05917  -0.08979 269 ASN A CA  
2249 C C   . ASN A 275 ? 0.34167 0.47422 0.26279 -0.10229 0.01833  -0.05161 269 ASN A C   
2250 O O   . ASN A 275 ? 0.35746 0.46300 0.34863 -0.08817 -0.00700 -0.07893 269 ASN A O   
2251 C CB  . ASN A 275 ? 0.40649 0.59279 0.25806 -0.15823 0.02959  -0.12865 269 ASN A CB  
2252 C CG  . ASN A 275 ? 0.46533 0.64272 0.34658 -0.10226 0.04739  -0.13760 269 ASN A CG  
2253 O OD1 . ASN A 275 ? 0.45733 0.66333 0.36030 -0.04197 0.04306  -0.11847 269 ASN A OD1 
2254 N ND2 . ASN A 275 ? 0.49392 0.66596 0.41909 -0.09946 0.05616  -0.14191 269 ASN A ND2 
2255 N N   . LYS A 276 ? 0.29677 0.46073 0.24965 -0.07923 0.01516  -0.02408 270 LYS A N   
2256 C CA  . LYS A 276 ? 0.27462 0.45266 0.27532 -0.07129 -0.00528 -0.00743 270 LYS A CA  
2257 C C   . LYS A 276 ? 0.30751 0.47577 0.28150 -0.03740 0.01024  -0.01208 270 LYS A C   
2258 O O   . LYS A 276 ? 0.32562 0.49665 0.30898 -0.03152 0.05729  -0.02937 270 LYS A O   
2259 C CB  . LYS A 276 ? 0.30635 0.45409 0.31420 -0.09354 -0.01442 0.01796  270 LYS A CB  
2260 C CG  . LYS A 276 ? 0.31795 0.46048 0.41333 -0.13439 -0.03613 -0.02387 270 LYS A CG  
2261 C CD  . LYS A 276 ? 0.41295 0.46632 0.47929 -0.14994 -0.03510 -0.06934 270 LYS A CD  
2262 C CE  . LYS A 276 ? 0.48912 0.50905 0.54675 -0.14024 -0.06144 -0.09072 270 LYS A CE  
2263 N NZ  . LYS A 276 ? 0.50132 0.52734 0.55325 -0.15492 -0.12815 -0.12459 270 LYS A NZ  
2264 N N   . VAL A 277 ? 0.27735 0.47308 0.25673 -0.03884 -0.00771 -0.03402 271 VAL A N   
2265 C CA  . VAL A 277 ? 0.25445 0.44945 0.27943 -0.04075 -0.01347 -0.04715 271 VAL A CA  
2266 C C   . VAL A 277 ? 0.27200 0.44099 0.25890 -0.05603 -0.02164 -0.06423 271 VAL A C   
2267 O O   . VAL A 277 ? 0.31808 0.42517 0.29252 -0.04664 0.03174  -0.09025 271 VAL A O   
2268 C CB  . VAL A 277 ? 0.26920 0.44199 0.36775 -0.00891 0.02322  -0.05216 271 VAL A CB  
2269 C CG1 . VAL A 277 ? 0.32669 0.44704 0.42941 0.05195  0.06765  -0.02918 271 VAL A CG1 
2270 C CG2 . VAL A 277 ? 0.31014 0.43889 0.39792 -0.05919 0.06188  -0.10316 271 VAL A CG2 
2271 N N   . PRO A 278 ? 0.29238 0.45479 0.25133 -0.06319 -0.01525 -0.04884 272 PRO A N   
2272 C CA  . PRO A 278 ? 0.30416 0.45415 0.26489 -0.04817 -0.00671 -0.03655 272 PRO A CA  
2273 C C   . PRO A 278 ? 0.30729 0.43784 0.22885 -0.03823 0.01235  -0.05203 272 PRO A C   
2274 O O   . PRO A 278 ? 0.29136 0.44267 0.25552 -0.03473 0.01694  -0.08785 272 PRO A O   
2275 C CB  . PRO A 278 ? 0.37747 0.47616 0.28045 -0.06329 -0.01364 -0.02172 272 PRO A CB  
2276 C CG  . PRO A 278 ? 0.37710 0.48900 0.29204 -0.09312 -0.03273 -0.03382 272 PRO A CG  
2277 C CD  . PRO A 278 ? 0.32184 0.46921 0.23228 -0.08999 -0.05308 -0.03314 272 PRO A CD  
2278 N N   . TRP A 279 ? 0.25672 0.40976 0.22285 -0.02207 -0.05203 -0.05927 273 TRP A N   
2279 C CA  . TRP A 279 ? 0.25877 0.40819 0.22965 -0.00947 -0.02860 -0.09293 273 TRP A CA  
2280 C C   . TRP A 279 ? 0.24911 0.43838 0.24131 0.02338  -0.01133 -0.05368 273 TRP A C   
2281 O O   . TRP A 279 ? 0.26182 0.44546 0.28716 0.02828  0.01664  -0.07941 273 TRP A O   
2282 C CB  . TRP A 279 ? 0.29484 0.42357 0.22771 -0.00345 0.03774  -0.11917 273 TRP A CB  
2283 C CG  . TRP A 279 ? 0.25231 0.47185 0.28611 -0.02819 0.04773  -0.09977 273 TRP A CG  
2284 C CD1 . TRP A 279 ? 0.25831 0.46542 0.30288 -0.03790 0.03386  -0.10325 273 TRP A CD1 
2285 C CD2 . TRP A 279 ? 0.23971 0.51342 0.27481 -0.03672 0.04705  -0.06601 273 TRP A CD2 
2286 N NE1 . TRP A 279 ? 0.24747 0.46026 0.28565 -0.00749 0.02024  -0.10732 273 TRP A NE1 
2287 C CE2 . TRP A 279 ? 0.25552 0.49535 0.26754 -0.02708 0.03076  -0.08919 273 TRP A CE2 
2288 C CE3 . TRP A 279 ? 0.18885 0.54516 0.26395 -0.05616 -0.00595 -0.05043 273 TRP A CE3 
2289 C CZ2 . TRP A 279 ? 0.32795 0.51315 0.29100 -0.06994 0.04328  -0.11694 273 TRP A CZ2 
2290 C CZ3 . TRP A 279 ? 0.25366 0.54631 0.27018 -0.08734 0.03198  -0.04668 273 TRP A CZ3 
2291 C CH2 . TRP A 279 ? 0.29513 0.52875 0.26532 -0.09203 0.01103  -0.07657 273 TRP A CH2 
2292 N N   . ASN A 280 ? 0.26568 0.47517 0.24035 -0.01371 -0.01221 -0.06799 274 ASN A N   
2293 C CA  . ASN A 280 ? 0.29175 0.51240 0.30626 -0.04015 0.05950  -0.06052 274 ASN A CA  
2294 C C   . ASN A 280 ? 0.28182 0.52785 0.36764 -0.02216 0.02859  -0.09714 274 ASN A C   
2295 O O   . ASN A 280 ? 0.26706 0.53513 0.41885 -0.03116 0.05342  -0.11434 274 ASN A O   
2296 C CB  . ASN A 280 ? 0.37296 0.57986 0.31063 -0.06979 0.10180  0.00489  274 ASN A CB  
2297 C CG  . ASN A 280 ? 0.50333 0.64968 0.32849 -0.10528 0.10810  0.03181  274 ASN A CG  
2298 O OD1 . ASN A 280 ? 0.58307 0.67502 0.29294 -0.13428 0.04470  0.00120  274 ASN A OD1 
2299 N ND2 . ASN A 280 ? 0.60338 0.68095 0.34788 -0.10504 0.08775  0.08940  274 ASN A ND2 
2300 N N   . ARG A 281 ? 0.31797 0.51486 0.33718 -0.01755 -0.04261 -0.10658 275 ARG A N   
2301 C CA  . ARG A 281 ? 0.35219 0.53561 0.35130 -0.01548 -0.08124 -0.10701 275 ARG A CA  
2302 C C   . ARG A 281 ? 0.38967 0.48197 0.38400 -0.00518 0.00749  -0.11128 275 ARG A C   
2303 O O   . ARG A 281 ? 0.40158 0.47815 0.39309 0.01476  -0.01618 -0.10411 275 ARG A O   
2304 C CB  . ARG A 281 ? 0.35379 0.59706 0.36436 -0.02601 -0.12778 -0.10993 275 ARG A CB  
2305 C CG  . ARG A 281 ? 0.39950 0.63317 0.42585 -0.04680 -0.15718 -0.15509 275 ARG A CG  
2306 C CD  . ARG A 281 ? 0.46996 0.65641 0.51513 -0.07948 -0.13540 -0.19371 275 ARG A CD  
2307 N NE  . ARG A 281 ? 0.49652 0.66386 0.54123 -0.11466 -0.15478 -0.24215 275 ARG A NE  
2308 C CZ  . ARG A 281 ? 0.52842 0.67487 0.58418 -0.12482 -0.12827 -0.25648 275 ARG A CZ  
2309 N NH1 . ARG A 281 ? 0.52716 0.69301 0.56894 -0.11609 -0.15076 -0.22941 275 ARG A NH1 
2310 N NH2 . ARG A 281 ? 0.50975 0.67195 0.59655 -0.13327 -0.09873 -0.27781 275 ARG A NH2 
2311 N N   . LEU A 282 ? 0.34045 0.44025 0.33806 -0.05687 0.01754  -0.16462 276 LEU A N   
2312 C CA  . LEU A 282 ? 0.31582 0.42111 0.37157 -0.01470 -0.03013 -0.11845 276 LEU A CA  
2313 C C   . LEU A 282 ? 0.36178 0.40203 0.38450 -0.02466 -0.03167 -0.10278 276 LEU A C   
2314 O O   . LEU A 282 ? 0.43346 0.37648 0.43846 -0.01578 0.00753  -0.06358 276 LEU A O   
2315 C CB  . LEU A 282 ? 0.38218 0.44263 0.37314 0.00299  -0.01946 -0.11606 276 LEU A CB  
2316 C CG  . LEU A 282 ? 0.41618 0.46132 0.42542 0.03954  0.01265  -0.10855 276 LEU A CG  
2317 C CD1 . LEU A 282 ? 0.47439 0.46652 0.47275 0.03164  0.08076  -0.15459 276 LEU A CD1 
2318 C CD2 . LEU A 282 ? 0.43897 0.49446 0.45691 0.03075  -0.00232 -0.09538 276 LEU A CD2 
2319 N N   . PHE A 283 ? 0.31159 0.41413 0.34053 -0.06165 -0.00066 -0.12278 277 PHE A N   
2320 C CA  . PHE A 283 ? 0.30401 0.44090 0.31459 -0.01944 0.01946  -0.12583 277 PHE A CA  
2321 C C   . PHE A 283 ? 0.31980 0.48439 0.32135 0.01818  0.03950  -0.13032 277 PHE A C   
2322 O O   . PHE A 283 ? 0.32459 0.50447 0.30671 0.01832  0.02603  -0.12849 277 PHE A O   
2323 C CB  . PHE A 283 ? 0.28219 0.44415 0.27502 -0.00139 0.00815  -0.10333 277 PHE A CB  
2324 C CG  . PHE A 283 ? 0.30593 0.44612 0.28657 -0.01772 0.02431  -0.07422 277 PHE A CG  
2325 C CD1 . PHE A 283 ? 0.32655 0.46090 0.31511 -0.01631 0.05941  -0.03864 277 PHE A CD1 
2326 C CD2 . PHE A 283 ? 0.33835 0.44353 0.29709 -0.01831 0.05638  -0.07914 277 PHE A CD2 
2327 C CE1 . PHE A 283 ? 0.34477 0.44788 0.33592 -0.02163 0.04005  -0.01959 277 PHE A CE1 
2328 C CE2 . PHE A 283 ? 0.34570 0.44200 0.27445 0.00995  0.03478  -0.05604 277 PHE A CE2 
2329 C CZ  . PHE A 283 ? 0.33586 0.42994 0.27771 -0.01944 0.03275  -0.04991 277 PHE A CZ  
2330 N N   . PRO A 284 ? 0.31625 0.51664 0.35525 0.02709  0.02083  -0.14142 278 PRO A N   
2331 C CA  . PRO A 284 ? 0.32541 0.54438 0.38579 0.03005  0.05647  -0.15620 278 PRO A CA  
2332 C C   . PRO A 284 ? 0.31273 0.60671 0.41058 0.01991  0.03387  -0.13312 278 PRO A C   
2333 O O   . PRO A 284 ? 0.36150 0.64816 0.39815 0.03076  0.01276  -0.11173 278 PRO A O   
2334 C CB  . PRO A 284 ? 0.36448 0.51657 0.37253 0.03664  0.07337  -0.15897 278 PRO A CB  
2335 C CG  . PRO A 284 ? 0.37775 0.50217 0.40789 0.05860  0.06178  -0.13083 278 PRO A CG  
2336 C CD  . PRO A 284 ? 0.31963 0.49936 0.36694 0.04297  0.02086  -0.12214 278 PRO A CD  
2337 N N   . ASN A 285 ? 0.24449 0.61135 0.40685 -0.00060 0.00370  -0.14054 279 ASN A N   
2338 C CA  A ASN A 285 ? 0.27266 0.60885 0.42730 -0.02499 0.04046  -0.14934 279 ASN A CA  
2339 C CA  B ASN A 285 ? 0.30530 0.60639 0.43473 -0.02294 0.03977  -0.15345 279 ASN A CA  
2340 C C   . ASN A 285 ? 0.29609 0.60013 0.43625 -0.02980 0.07146  -0.17528 279 ASN A C   
2341 O O   . ASN A 285 ? 0.27557 0.62020 0.53581 -0.02207 0.10168  -0.17198 279 ASN A O   
2342 C CB  A ASN A 285 ? 0.28855 0.62625 0.43954 -0.02551 0.03735  -0.11497 279 ASN A CB  
2343 C CB  B ASN A 285 ? 0.38040 0.61758 0.47013 -0.01774 0.04148  -0.12420 279 ASN A CB  
2344 C CG  A ASN A 285 ? 0.31287 0.64390 0.44017 -0.00485 0.04963  -0.09140 279 ASN A CG  
2345 C CG  B ASN A 285 ? 0.44706 0.62449 0.49883 0.00817  0.05022  -0.10178 279 ASN A CG  
2346 O OD1 A ASN A 285 ? 0.29770 0.66168 0.44147 0.02967  0.07989  -0.06951 279 ASN A OD1 
2347 O OD1 B ASN A 285 ? 0.48253 0.63747 0.51137 0.02755  0.05758  -0.10197 279 ASN A OD1 
2348 N ND2 A ASN A 285 ? 0.37530 0.64210 0.44023 -0.01200 0.07988  -0.10411 279 ASN A ND2 
2349 N ND2 B ASN A 285 ? 0.45525 0.61182 0.52110 0.02009  0.04177  -0.08833 279 ASN A ND2 
2350 N N   . ALA A 286 ? 0.27869 0.56405 0.32858 -0.02393 0.06546  -0.19448 280 ALA A N   
2351 C CA  . ALA A 286 ? 0.28251 0.51342 0.29886 -0.01193 0.08936  -0.16861 280 ALA A CA  
2352 C C   . ALA A 286 ? 0.27040 0.48347 0.27113 -0.04104 0.07778  -0.12145 280 ALA A C   
2353 O O   . ALA A 286 ? 0.33753 0.47809 0.26522 -0.04534 0.03835  -0.08393 280 ALA A O   
2354 C CB  . ALA A 286 ? 0.24032 0.51507 0.28557 -0.01345 0.08124  -0.12924 280 ALA A CB  
2355 N N   . ASP A 287 ? 0.24736 0.46484 0.29408 -0.02922 0.05193  -0.10602 281 ASP A N   
2356 C CA  . ASP A 287 ? 0.26950 0.47894 0.30078 -0.04362 0.05718  -0.08039 281 ASP A CA  
2357 C C   . ASP A 287 ? 0.31916 0.49575 0.25852 -0.02774 0.07377  -0.05150 281 ASP A C   
2358 O O   . ASP A 287 ? 0.30485 0.51162 0.22420 -0.03765 0.06846  -0.05464 281 ASP A O   
2359 C CB  . ASP A 287 ? 0.25488 0.45298 0.31102 -0.05128 0.01778  -0.09217 281 ASP A CB  
2360 C CG  . ASP A 287 ? 0.27836 0.44870 0.42659 -0.04694 -0.02583 -0.07714 281 ASP A CG  
2361 O OD1 . ASP A 287 ? 0.37320 0.43318 0.48558 -0.04736 -0.02719 -0.06887 281 ASP A OD1 
2362 O OD2 . ASP A 287 ? 0.31198 0.47521 0.48001 -0.01541 -0.01323 -0.04369 281 ASP A OD2 
2363 N N   . SER A 288 ? 0.32134 0.46884 0.24753 -0.05761 0.08926  -0.04499 282 SER A N   
2364 C CA  . SER A 288 ? 0.32818 0.44224 0.20352 -0.06537 0.03782  -0.02477 282 SER A CA  
2365 C C   . SER A 288 ? 0.30800 0.39337 0.23685 -0.05985 0.06113  -0.00487 282 SER A C   
2366 O O   . SER A 288 ? 0.30027 0.37598 0.24660 -0.05563 0.04925  -0.00637 282 SER A O   
2367 C CB  . SER A 288 ? 0.45107 0.48351 0.26862 -0.08041 0.03902  0.00844  282 SER A CB  
2368 O OG  . SER A 288 ? 0.55872 0.51052 0.29429 -0.05938 0.08817  -0.00596 282 SER A OG  
2369 N N   . LYS A 289 ? 0.30536 0.37734 0.22261 -0.07532 0.08975  0.00328  283 LYS A N   
2370 C CA  . LYS A 289 ? 0.31339 0.35635 0.23427 -0.08320 0.07908  0.03811  283 LYS A CA  
2371 C C   . LYS A 289 ? 0.30777 0.35759 0.22851 -0.06962 0.06479  0.03486  283 LYS A C   
2372 O O   . LYS A 289 ? 0.25023 0.35640 0.20811 -0.06298 0.01371  0.00257  283 LYS A O   
2373 C CB  . LYS A 289 ? 0.30817 0.35310 0.25498 -0.14449 0.03532  0.06156  283 LYS A CB  
2374 C CG  . LYS A 289 ? 0.41568 0.37461 0.30647 -0.16527 0.04691  0.04337  283 LYS A CG  
2375 C CD  . LYS A 289 ? 0.50121 0.38822 0.36332 -0.19037 0.09534  0.03327  283 LYS A CD  
2376 C CE  . LYS A 289 ? 0.59482 0.41441 0.37769 -0.17201 0.10610  0.03402  283 LYS A CE  
2377 N NZ  . LYS A 289 ? 0.65503 0.43235 0.35870 -0.16532 0.12591  0.03354  283 LYS A NZ  
2378 N N   . ALA A 290 ? 0.26011 0.35203 0.20834 -0.06326 0.02469  0.03738  284 ALA A N   
2379 C CA  . ALA A 290 ? 0.21903 0.34665 0.21106 -0.04962 0.01232  0.00874  284 ALA A CA  
2380 C C   . ALA A 290 ? 0.22769 0.32365 0.18316 -0.05869 -0.00151 -0.01027 284 ALA A C   
2381 O O   . ALA A 290 ? 0.21530 0.31612 0.20337 -0.03580 0.00310  -0.00148 284 ALA A O   
2382 C CB  . ALA A 290 ? 0.26994 0.33619 0.24182 -0.00548 0.06735  0.01229  284 ALA A CB  
2383 N N   . LEU A 291 ? 0.24675 0.32251 0.17208 -0.04306 -0.01989 -0.04965 285 LEU A N   
2384 C CA  . LEU A 291 ? 0.23847 0.34342 0.21663 -0.02668 -0.03128 -0.04009 285 LEU A CA  
2385 C C   . LEU A 291 ? 0.30380 0.32773 0.24700 -0.04103 0.02473  -0.02647 285 LEU A C   
2386 O O   . LEU A 291 ? 0.30676 0.32613 0.20923 -0.04233 0.02074  -0.04478 285 LEU A O   
2387 C CB  . LEU A 291 ? 0.26319 0.37186 0.22208 -0.02628 0.03386  -0.05062 285 LEU A CB  
2388 C CG  . LEU A 291 ? 0.30565 0.37690 0.20807 -0.02058 0.06730  -0.04993 285 LEU A CG  
2389 C CD1 . LEU A 291 ? 0.29263 0.36603 0.22922 0.01026  0.05141  -0.10675 285 LEU A CD1 
2390 C CD2 . LEU A 291 ? 0.28131 0.38713 0.22063 -0.01797 0.02560  -0.00854 285 LEU A CD2 
2391 N N   . ASP A 292 ? 0.32551 0.29323 0.20815 -0.01266 -0.00797 -0.00895 286 ASP A N   
2392 C CA  . ASP A 292 ? 0.30062 0.30087 0.20038 -0.01787 0.02881  0.01624  286 ASP A CA  
2393 C C   . ASP A 292 ? 0.28383 0.26912 0.17439 0.00639  0.02097  -0.00518 286 ASP A C   
2394 O O   . ASP A 292 ? 0.25882 0.27804 0.21873 0.00266  0.01722  -0.02897 286 ASP A O   
2395 C CB  . ASP A 292 ? 0.30804 0.29618 0.19242 -0.04986 0.00432  0.03469  286 ASP A CB  
2396 C CG  . ASP A 292 ? 0.30932 0.32740 0.19184 -0.04961 -0.07093 -0.00589 286 ASP A CG  
2397 O OD1 . ASP A 292 ? 0.37305 0.34764 0.24626 -0.01172 -0.08548 -0.04270 286 ASP A OD1 
2398 O OD2 . ASP A 292 ? 0.31667 0.33191 0.18510 -0.08503 -0.08731 -0.00164 286 ASP A OD2 
2399 N N   . LEU A 293 ? 0.28073 0.24433 0.15994 -0.02058 0.00581  -0.00243 287 LEU A N   
2400 C CA  . LEU A 293 ? 0.25092 0.23816 0.13983 -0.02806 -0.01958 0.00384  287 LEU A CA  
2401 C C   . LEU A 293 ? 0.22986 0.24499 0.21018 -0.03556 0.01386  -0.00600 287 LEU A C   
2402 O O   . LEU A 293 ? 0.19344 0.25791 0.21147 0.00700  0.00403  -0.01148 287 LEU A O   
2403 C CB  . LEU A 293 ? 0.22138 0.27494 0.16847 0.01489  -0.01105 -0.01031 287 LEU A CB  
2404 C CG  . LEU A 293 ? 0.19213 0.29992 0.16155 -0.01961 0.00960  -0.00680 287 LEU A CG  
2405 C CD1 . LEU A 293 ? 0.29678 0.31284 0.21292 0.00035  0.06821  0.00379  287 LEU A CD1 
2406 C CD2 . LEU A 293 ? 0.16691 0.31412 0.18546 -0.02585 -0.00192 0.00247  287 LEU A CD2 
2407 N N   . LEU A 294 ? 0.22486 0.23484 0.21065 -0.05861 -0.00006 -0.00646 288 LEU A N   
2408 C CA  . LEU A 294 ? 0.18985 0.23016 0.23344 0.00877  -0.00455 -0.01461 288 LEU A CA  
2409 C C   . LEU A 294 ? 0.15417 0.26053 0.21785 0.00128  0.01028  -0.00554 288 LEU A C   
2410 O O   . LEU A 294 ? 0.16090 0.28136 0.23527 0.00101  0.03681  -0.01071 288 LEU A O   
2411 C CB  . LEU A 294 ? 0.19542 0.20841 0.21020 0.01432  0.01073  0.00529  288 LEU A CB  
2412 C CG  . LEU A 294 ? 0.25859 0.23580 0.18653 0.00585  0.00851  0.02440  288 LEU A CG  
2413 C CD1 . LEU A 294 ? 0.23836 0.26228 0.16974 -0.02340 0.00900  0.01875  288 LEU A CD1 
2414 C CD2 . LEU A 294 ? 0.24532 0.25813 0.24477 0.05022  0.02564  -0.03393 288 LEU A CD2 
2415 N N   . ASP A 295 ? 0.18352 0.27768 0.20903 -0.02562 -0.03157 -0.02386 289 ASP A N   
2416 C CA  . ASP A 295 ? 0.19221 0.29792 0.17588 -0.00196 -0.04669 -0.00436 289 ASP A CA  
2417 C C   . ASP A 295 ? 0.19244 0.28787 0.23135 -0.01378 -0.01520 -0.00797 289 ASP A C   
2418 O O   . ASP A 295 ? 0.18347 0.29210 0.24586 -0.01997 -0.00306 -0.02479 289 ASP A O   
2419 C CB  . ASP A 295 ? 0.22587 0.36270 0.19814 -0.00822 -0.06246 -0.02289 289 ASP A CB  
2420 C CG  . ASP A 295 ? 0.29374 0.41156 0.27077 0.02512  -0.06291 -0.00021 289 ASP A CG  
2421 O OD1 . ASP A 295 ? 0.33622 0.43085 0.35119 0.01484  -0.05467 -0.08397 289 ASP A OD1 
2422 O OD2 . ASP A 295 ? 0.38801 0.46784 0.33617 0.03407  -0.00657 0.05306  289 ASP A OD2 
2423 N N   . LYS A 296 ? 0.21327 0.28826 0.15580 -0.01391 -0.03211 -0.00669 290 LYS A N   
2424 C CA  . LYS A 296 ? 0.22301 0.28819 0.17335 -0.03079 0.00244  0.00094  290 LYS A CA  
2425 C C   . LYS A 296 ? 0.18650 0.29098 0.18943 -0.03544 -0.02683 0.02043  290 LYS A C   
2426 O O   . LYS A 296 ? 0.14642 0.34049 0.21002 -0.00782 -0.01059 0.01218  290 LYS A O   
2427 C CB  . LYS A 296 ? 0.27653 0.24857 0.17518 -0.03107 -0.00787 0.01412  290 LYS A CB  
2428 C CG  . LYS A 296 ? 0.33463 0.28066 0.22707 -0.02907 -0.01618 0.03082  290 LYS A CG  
2429 C CD  A LYS A 296 ? 0.36219 0.31810 0.25797 -0.06870 -0.04067 0.03828  290 LYS A CD  
2430 C CD  B LYS A 296 ? 0.40794 0.28771 0.28383 -0.02770 -0.02049 -0.01068 290 LYS A CD  
2431 C CE  A LYS A 296 ? 0.37933 0.34317 0.22691 -0.09675 -0.06455 0.05235  290 LYS A CE  
2432 C CE  B LYS A 296 ? 0.47247 0.28800 0.30591 -0.01873 -0.00961 -0.04607 290 LYS A CE  
2433 N NZ  A LYS A 296 ? 0.35691 0.36884 0.19747 -0.08095 -0.12232 0.06606  290 LYS A NZ  
2434 N NZ  B LYS A 296 ? 0.51934 0.30464 0.35210 -0.00568 -0.00392 -0.04699 290 LYS A NZ  
2435 N N   . MET A 297 ? 0.20808 0.24855 0.18384 -0.01505 -0.03566 0.04939  291 MET A N   
2436 C CA  . MET A 297 ? 0.18657 0.25863 0.19563 -0.03798 -0.03541 0.03895  291 MET A CA  
2437 C C   . MET A 297 ? 0.18941 0.26104 0.14831 -0.03258 -0.00792 0.04435  291 MET A C   
2438 O O   . MET A 297 ? 0.21719 0.23688 0.21148 -0.02886 0.04744  0.01946  291 MET A O   
2439 C CB  A MET A 297 ? 0.18921 0.25887 0.22166 -0.05438 -0.04717 0.02936  291 MET A CB  
2440 C CB  B MET A 297 ? 0.15711 0.26083 0.25269 -0.04299 -0.02560 0.02685  291 MET A CB  
2441 C CG  A MET A 297 ? 0.19037 0.25083 0.24624 -0.03527 -0.07222 0.00942  291 MET A CG  
2442 C CG  B MET A 297 ? 0.12878 0.26365 0.30273 -0.01041 -0.04500 0.00553  291 MET A CG  
2443 S SD  A MET A 297 ? 0.23965 0.26642 0.30503 -0.00767 -0.04882 0.01637  291 MET A SD  
2444 S SD  B MET A 297 ? 0.17150 0.27679 0.35043 0.01886  -0.00415 0.00681  291 MET A SD  
2445 C CE  A MET A 297 ? 0.27490 0.24354 0.26260 0.01824  -0.06861 0.04484  291 MET A CE  
2446 C CE  B MET A 297 ? 0.20392 0.28772 0.36311 -0.00479 -0.01928 0.00266  291 MET A CE  
2447 N N   . LEU A 298 ? 0.18466 0.26378 0.18767 -0.03269 -0.02137 -0.01694 292 LEU A N   
2448 C CA  . LEU A 298 ? 0.20195 0.25600 0.18520 0.00034  -0.04141 -0.00628 292 LEU A CA  
2449 C C   . LEU A 298 ? 0.26574 0.25915 0.21091 0.00899  -0.04725 0.00590  292 LEU A C   
2450 O O   . LEU A 298 ? 0.32862 0.28774 0.28788 -0.01673 -0.09785 -0.04202 292 LEU A O   
2451 C CB  . LEU A 298 ? 0.18207 0.25271 0.14858 0.00041  -0.02255 0.00300  292 LEU A CB  
2452 C CG  . LEU A 298 ? 0.21579 0.23702 0.13948 0.01654  0.01234  -0.00095 292 LEU A CG  
2453 C CD1 . LEU A 298 ? 0.27076 0.27841 0.16337 0.01242  0.03398  -0.03123 292 LEU A CD1 
2454 C CD2 . LEU A 298 ? 0.19611 0.27434 0.14161 -0.00117 0.02849  -0.00276 292 LEU A CD2 
2455 N N   . THR A 299 ? 0.23852 0.26867 0.19103 0.00080  -0.03459 0.01821  293 THR A N   
2456 C CA  . THR A 299 ? 0.23471 0.26875 0.24256 0.01579  -0.04490 0.02395  293 THR A CA  
2457 C C   . THR A 299 ? 0.18544 0.26387 0.20202 0.01210  -0.05482 0.01317  293 THR A C   
2458 O O   . THR A 299 ? 0.19187 0.29546 0.17042 0.01428  -0.03540 -0.00262 293 THR A O   
2459 C CB  . THR A 299 ? 0.24982 0.29450 0.28102 -0.01064 -0.05332 0.03895  293 THR A CB  
2460 O OG1 . THR A 299 ? 0.23418 0.34817 0.33486 -0.00869 -0.02290 0.06058  293 THR A OG1 
2461 C CG2 . THR A 299 ? 0.28936 0.28962 0.26674 -0.01784 -0.09789 0.02792  293 THR A CG2 
2462 N N   . PHE A 300 ? 0.16472 0.26444 0.22570 -0.00365 -0.04214 0.01032  294 PHE A N   
2463 C CA  . PHE A 300 ? 0.13967 0.29460 0.20900 -0.01275 -0.05610 -0.02755 294 PHE A CA  
2464 C C   . PHE A 300 ? 0.20163 0.30019 0.21246 0.02011  -0.02503 -0.02699 294 PHE A C   
2465 O O   . PHE A 300 ? 0.21427 0.31069 0.20198 0.00820  -0.02317 -0.02818 294 PHE A O   
2466 C CB  . PHE A 300 ? 0.14806 0.32220 0.23286 -0.03508 -0.03985 -0.01634 294 PHE A CB  
2467 C CG  . PHE A 300 ? 0.18741 0.36265 0.26302 -0.03415 -0.05900 -0.03255 294 PHE A CG  
2468 C CD1 . PHE A 300 ? 0.27357 0.38925 0.23684 -0.04420 -0.04923 -0.03905 294 PHE A CD1 
2469 C CD2 . PHE A 300 ? 0.23133 0.40593 0.29647 -0.05712 -0.08535 -0.03310 294 PHE A CD2 
2470 C CE1 . PHE A 300 ? 0.28357 0.40001 0.24992 -0.03894 -0.04414 -0.00616 294 PHE A CE1 
2471 C CE2 . PHE A 300 ? 0.27285 0.41127 0.29725 -0.04691 -0.05228 -0.01552 294 PHE A CE2 
2472 C CZ  . PHE A 300 ? 0.28774 0.40663 0.23648 -0.06882 -0.07416 0.01497  294 PHE A CZ  
2473 N N   . ASN A 301 ? 0.17755 0.29810 0.21842 0.03977  -0.04634 -0.03435 295 ASN A N   
2474 C CA  . ASN A 301 ? 0.20094 0.31860 0.21664 0.05277  -0.06981 -0.02224 295 ASN A CA  
2475 C C   . ASN A 301 ? 0.18808 0.30978 0.22767 0.02242  -0.04162 0.00354  295 ASN A C   
2476 O O   . ASN A 301 ? 0.23019 0.29082 0.24891 -0.01246 -0.00658 0.02292  295 ASN A O   
2477 C CB  . ASN A 301 ? 0.25346 0.36462 0.27036 0.05193  -0.09907 -0.06951 295 ASN A CB  
2478 C CG  . ASN A 301 ? 0.25002 0.40705 0.35906 0.10166  -0.14415 -0.09987 295 ASN A CG  
2479 O OD1 . ASN A 301 ? 0.30237 0.43540 0.39210 0.14256  -0.09087 -0.11728 295 ASN A OD1 
2480 N ND2 . ASN A 301 ? 0.20375 0.42891 0.44051 0.06108  -0.12949 -0.09404 295 ASN A ND2 
2481 N N   . PRO A 302 ? 0.15802 0.31287 0.20971 -0.00240 -0.01585 -0.01689 296 PRO A N   
2482 C CA  . PRO A 302 ? 0.22361 0.30466 0.20508 -0.01120 -0.01061 -0.02263 296 PRO A CA  
2483 C C   . PRO A 302 ? 0.20480 0.28057 0.26418 0.00327  -0.04539 -0.01107 296 PRO A C   
2484 O O   . PRO A 302 ? 0.24454 0.26136 0.30280 0.01893  -0.03630 -0.02410 296 PRO A O   
2485 C CB  . PRO A 302 ? 0.24645 0.31372 0.21961 -0.05559 0.03417  -0.01569 296 PRO A CB  
2486 C CG  . PRO A 302 ? 0.21732 0.33934 0.22158 -0.00533 0.02546  -0.04123 296 PRO A CG  
2487 C CD  . PRO A 302 ? 0.17681 0.33518 0.19611 -0.00929 0.03316  -0.04956 296 PRO A CD  
2488 N N   . HIS A 303 ? 0.20809 0.29024 0.31845 0.01750  -0.04313 0.00552  297 HIS A N   
2489 C CA  . HIS A 303 ? 0.23648 0.30823 0.32561 0.05222  -0.06341 0.01721  297 HIS A CA  
2490 C C   . HIS A 303 ? 0.27798 0.30965 0.34824 0.04856  -0.03882 0.01240  297 HIS A C   
2491 O O   . HIS A 303 ? 0.40034 0.32612 0.41193 0.05690  0.05922  -0.01051 297 HIS A O   
2492 C CB  . HIS A 303 ? 0.22660 0.34792 0.38162 0.06833  -0.01723 0.00122  297 HIS A CB  
2493 C CG  . HIS A 303 ? 0.29486 0.39882 0.45353 0.06429  0.05292  0.00061  297 HIS A CG  
2494 N ND1 . HIS A 303 ? 0.38722 0.43992 0.48475 0.03537  0.10836  0.00641  297 HIS A ND1 
2495 C CD2 . HIS A 303 ? 0.34038 0.42453 0.51202 0.06523  0.12755  0.00526  297 HIS A CD2 
2496 C CE1 . HIS A 303 ? 0.41273 0.45683 0.52026 0.02284  0.14850  -0.01325 297 HIS A CE1 
2497 N NE2 . HIS A 303 ? 0.40995 0.44720 0.52831 0.03978  0.16120  -0.00936 297 HIS A NE2 
2498 N N   . LYS A 304 ? 0.24584 0.31523 0.30489 0.03194  -0.04255 0.02209  298 LYS A N   
2499 C CA  . LYS A 304 ? 0.17505 0.32308 0.30050 -0.00337 -0.08175 0.02314  298 LYS A CA  
2500 C C   . LYS A 304 ? 0.20930 0.27262 0.28837 0.01706  -0.04277 0.04674  298 LYS A C   
2501 O O   . LYS A 304 ? 0.24532 0.30194 0.30017 0.00802  -0.04060 0.06253  298 LYS A O   
2502 C CB  . LYS A 304 ? 0.19225 0.38768 0.28660 0.01436  -0.10370 0.03772  298 LYS A CB  
2503 C CG  . LYS A 304 ? 0.21229 0.45626 0.35102 -0.02012 -0.09527 0.02566  298 LYS A CG  
2504 C CD  . LYS A 304 ? 0.19654 0.49110 0.39623 -0.06224 -0.12104 0.02038  298 LYS A CD  
2505 C CE  . LYS A 304 ? 0.22908 0.51054 0.42494 -0.11045 -0.12180 -0.02023 298 LYS A CE  
2506 N NZ  . LYS A 304 ? 0.31790 0.53907 0.45499 -0.11096 -0.08083 -0.02246 298 LYS A NZ  
2507 N N   . ARG A 305 ? 0.21393 0.22336 0.24589 0.05405  -0.06865 0.03239  299 ARG A N   
2508 C CA  . ARG A 305 ? 0.16557 0.23699 0.21109 0.05271  -0.08746 0.04293  299 ARG A CA  
2509 C C   . ARG A 305 ? 0.16387 0.22309 0.23156 0.01097  -0.05845 0.01544  299 ARG A C   
2510 O O   . ARG A 305 ? 0.23217 0.22584 0.25481 0.02764  -0.03519 -0.00692 299 ARG A O   
2511 C CB  . ARG A 305 ? 0.17131 0.23458 0.20557 0.02364  -0.07499 0.06425  299 ARG A CB  
2512 C CG  . ARG A 305 ? 0.17798 0.22180 0.21009 0.03545  -0.03820 0.06297  299 ARG A CG  
2513 C CD  . ARG A 305 ? 0.12877 0.23176 0.21367 -0.00591 -0.02967 0.05409  299 ARG A CD  
2514 N NE  . ARG A 305 ? 0.16214 0.25003 0.22566 -0.06250 -0.02479 -0.00150 299 ARG A NE  
2515 C CZ  . ARG A 305 ? 0.18254 0.25304 0.19102 -0.03036 0.00654  0.00846  299 ARG A CZ  
2516 N NH1 . ARG A 305 ? 0.13952 0.26046 0.16918 0.02605  0.01344  0.01521  299 ARG A NH1 
2517 N NH2 . ARG A 305 ? 0.21242 0.21693 0.19010 -0.03325 -0.01606 -0.00662 299 ARG A NH2 
2518 N N   . ILE A 306 ? 0.16453 0.23550 0.20572 -0.00460 -0.05545 0.03363  300 ILE A N   
2519 C CA  . ILE A 306 ? 0.18964 0.22036 0.20050 -0.00720 -0.02949 0.02705  300 ILE A CA  
2520 C C   . ILE A 306 ? 0.20494 0.21212 0.19292 -0.00877 -0.01710 0.00142  300 ILE A C   
2521 O O   . ILE A 306 ? 0.21821 0.21029 0.19538 0.00278  -0.04489 0.01332  300 ILE A O   
2522 C CB  . ILE A 306 ? 0.20265 0.22134 0.22401 -0.01647 -0.00234 0.03754  300 ILE A CB  
2523 C CG1 . ILE A 306 ? 0.18536 0.21068 0.28684 -0.03548 0.03605  0.04032  300 ILE A CG1 
2524 C CG2 . ILE A 306 ? 0.20668 0.25988 0.25014 0.03481  0.00954  0.01070  300 ILE A CG2 
2525 C CD1 . ILE A 306 ? 0.17831 0.22127 0.30428 -0.04565 0.00320  0.04893  300 ILE A CD1 
2526 N N   . GLU A 307 ? 0.18543 0.23318 0.17782 0.01912  -0.00986 -0.00611 301 GLU A N   
2527 C CA  . GLU A 307 ? 0.16211 0.24971 0.22220 0.03782  -0.02598 -0.01151 301 GLU A CA  
2528 C C   . GLU A 307 ? 0.20546 0.22245 0.22834 0.01364  -0.06354 -0.01111 301 GLU A C   
2529 O O   . GLU A 307 ? 0.23501 0.21530 0.20463 0.00339  -0.05686 -0.00071 301 GLU A O   
2530 C CB  . GLU A 307 ? 0.16488 0.28026 0.25510 0.04107  0.00954  -0.00818 301 GLU A CB  
2531 C CG  . GLU A 307 ? 0.20223 0.35731 0.30442 0.06662  0.03920  -0.01802 301 GLU A CG  
2532 C CD  . GLU A 307 ? 0.23649 0.43584 0.35745 0.01800  0.01291  -0.01790 301 GLU A CD  
2533 O OE1 . GLU A 307 ? 0.23327 0.45785 0.38003 -0.01881 0.00888  0.00558  301 GLU A OE1 
2534 O OE2 . GLU A 307 ? 0.25323 0.47510 0.39021 0.00081  0.03089  -0.01835 301 GLU A OE2 
2535 N N   . VAL A 308 ? 0.19620 0.20680 0.22817 0.01769  -0.04870 -0.02152 302 VAL A N   
2536 C CA  . VAL A 308 ? 0.18345 0.22005 0.19329 0.02633  -0.07020 -0.00453 302 VAL A CA  
2537 C C   . VAL A 308 ? 0.12987 0.21239 0.23950 0.00813  -0.02461 -0.01019 302 VAL A C   
2538 O O   . VAL A 308 ? 0.21401 0.21774 0.25001 -0.00550 -0.00760 0.00769  302 VAL A O   
2539 C CB  . VAL A 308 ? 0.15516 0.26293 0.17766 0.02810  -0.04195 -0.00811 302 VAL A CB  
2540 C CG1 . VAL A 308 ? 0.23300 0.23766 0.19304 0.01985  -0.02126 -0.01828 302 VAL A CG1 
2541 C CG2 . VAL A 308 ? 0.15126 0.28872 0.23074 0.02347  -0.04161 0.01123  302 VAL A CG2 
2542 N N   . GLU A 309 ? 0.18394 0.21995 0.26006 -0.00298 -0.01003 0.01177  303 GLU A N   
2543 C CA  . GLU A 309 ? 0.22650 0.22391 0.28379 0.01740  -0.00510 -0.02104 303 GLU A CA  
2544 C C   . GLU A 309 ? 0.24346 0.22780 0.27608 -0.00060 -0.00099 0.02861  303 GLU A C   
2545 O O   . GLU A 309 ? 0.20831 0.23565 0.29315 -0.02549 -0.01385 0.03263  303 GLU A O   
2546 C CB  . GLU A 309 ? 0.25032 0.22885 0.29215 0.03399  -0.00636 -0.03896 303 GLU A CB  
2547 C CG  . GLU A 309 ? 0.25818 0.30511 0.31943 0.01336  -0.01622 -0.07658 303 GLU A CG  
2548 C CD  . GLU A 309 ? 0.34965 0.38708 0.35133 0.03445  0.01709  -0.10779 303 GLU A CD  
2549 O OE1 . GLU A 309 ? 0.45706 0.41710 0.36127 0.08668  0.09116  -0.05424 303 GLU A OE1 
2550 O OE2 . GLU A 309 ? 0.32062 0.43073 0.42735 0.02270  -0.02445 -0.16872 303 GLU A OE2 
2551 N N   . GLN A 310 ? 0.23687 0.23179 0.22461 0.00552  -0.06361 0.01977  304 GLN A N   
2552 C CA  A GLN A 310 ? 0.21625 0.25939 0.19032 0.01341  -0.07981 0.04262  304 GLN A CA  
2553 C CA  B GLN A 310 ? 0.24309 0.25085 0.26239 0.00523  -0.06562 0.04091  304 GLN A CA  
2554 C C   . GLN A 310 ? 0.24814 0.23587 0.22135 0.00651  -0.05678 0.03131  304 GLN A C   
2555 O O   . GLN A 310 ? 0.29382 0.24038 0.24161 -0.03881 -0.04366 0.03694  304 GLN A O   
2556 C CB  A GLN A 310 ? 0.24233 0.27918 0.26863 -0.01757 -0.04880 0.01543  304 GLN A CB  
2557 C CB  B GLN A 310 ? 0.28018 0.27834 0.35356 -0.01327 -0.04499 0.05525  304 GLN A CB  
2558 C CG  A GLN A 310 ? 0.27097 0.24022 0.27066 0.01156  -0.06616 0.00661  304 GLN A CG  
2559 C CG  B GLN A 310 ? 0.32498 0.28518 0.40690 -0.01466 -0.01417 0.08963  304 GLN A CG  
2560 C CD  A GLN A 310 ? 0.33959 0.18800 0.25147 0.01349  -0.06659 0.02623  304 GLN A CD  
2561 C CD  B GLN A 310 ? 0.37850 0.28803 0.44286 -0.00661 -0.04228 0.09926  304 GLN A CD  
2562 O OE1 A GLN A 310 ? 0.32548 0.15498 0.24655 0.01424  -0.08877 0.05585  304 GLN A OE1 
2563 O OE1 B GLN A 310 ? 0.45338 0.29140 0.47961 -0.01410 -0.02467 0.10299  304 GLN A OE1 
2564 N NE2 A GLN A 310 ? 0.40280 0.21004 0.25520 0.00792  -0.04187 0.00094  304 GLN A NE2 
2565 N NE2 B GLN A 310 ? 0.40760 0.27767 0.41108 0.00354  -0.04463 0.12047  304 GLN A NE2 
2566 N N   . ALA A 311 ? 0.23563 0.23389 0.23945 0.00954  -0.03798 0.04917  305 ALA A N   
2567 C CA  . ALA A 311 ? 0.23126 0.22741 0.23541 0.00321  -0.03397 0.05875  305 ALA A CA  
2568 C C   . ALA A 311 ? 0.22971 0.23137 0.23603 -0.03808 -0.02743 0.05150  305 ALA A C   
2569 O O   . ALA A 311 ? 0.21410 0.26215 0.20299 -0.05723 0.01763  0.03539  305 ALA A O   
2570 C CB  . ALA A 311 ? 0.24006 0.19565 0.19695 -0.01742 -0.00887 0.05514  305 ALA A CB  
2571 N N   . LEU A 312 ? 0.18570 0.20856 0.21173 -0.06063 -0.03078 0.03578  306 LEU A N   
2572 C CA  . LEU A 312 ? 0.24735 0.21889 0.15451 -0.05880 0.05693  -0.00857 306 LEU A CA  
2573 C C   . LEU A 312 ? 0.26384 0.20863 0.20290 -0.05318 0.04028  0.01882  306 LEU A C   
2574 O O   . LEU A 312 ? 0.26000 0.24839 0.19543 -0.04908 0.01857  0.03914  306 LEU A O   
2575 C CB  . LEU A 312 ? 0.27839 0.23092 0.16822 -0.01814 0.02276  -0.00395 306 LEU A CB  
2576 C CG  . LEU A 312 ? 0.19088 0.23273 0.15393 0.01183  -0.02122 -0.02196 306 LEU A CG  
2577 C CD1 . LEU A 312 ? 0.26536 0.24399 0.16117 0.03513  -0.03207 -0.03941 306 LEU A CD1 
2578 C CD2 . LEU A 312 ? 0.12154 0.27102 0.22632 0.01774  0.00361  -0.01847 306 LEU A CD2 
2579 N N   . ALA A 313 ? 0.29680 0.20903 0.20468 -0.03604 0.00596  -0.01300 307 ALA A N   
2580 C CA  . ALA A 313 ? 0.26654 0.23138 0.21611 -0.02848 0.01507  0.03722  307 ALA A CA  
2581 C C   . ALA A 313 ? 0.26877 0.25615 0.21596 -0.06095 -0.02129 0.02921  307 ALA A C   
2582 O O   . ALA A 313 ? 0.28909 0.29895 0.25804 -0.06019 -0.00589 0.03153  307 ALA A O   
2583 C CB  . ALA A 313 ? 0.29519 0.21912 0.27016 -0.02185 0.01444  0.03691  307 ALA A CB  
2584 N N   . HIS A 314 ? 0.25039 0.24699 0.20161 -0.06664 -0.01786 0.00789  308 HIS A N   
2585 C CA  . HIS A 314 ? 0.26918 0.26515 0.22733 -0.06942 0.02439  0.04760  308 HIS A CA  
2586 C C   . HIS A 314 ? 0.27315 0.28668 0.21135 -0.09165 0.00202  0.04996  308 HIS A C   
2587 O O   . HIS A 314 ? 0.25273 0.29047 0.24607 -0.06559 0.01551  0.03453  308 HIS A O   
2588 C CB  . HIS A 314 ? 0.29746 0.26877 0.18980 -0.08335 0.03859  0.02969  308 HIS A CB  
2589 C CG  . HIS A 314 ? 0.28062 0.29467 0.18159 -0.05207 0.02926  0.01296  308 HIS A CG  
2590 N ND1 . HIS A 314 ? 0.24393 0.27123 0.20220 -0.03936 -0.01664 0.03125  308 HIS A ND1 
2591 C CD2 . HIS A 314 ? 0.31608 0.30090 0.20793 -0.01901 0.02503  0.01217  308 HIS A CD2 
2592 C CE1 . HIS A 314 ? 0.29907 0.28498 0.21268 -0.05006 -0.01999 0.02667  308 HIS A CE1 
2593 N NE2 . HIS A 314 ? 0.33941 0.28532 0.21858 -0.01729 0.00543  0.03563  308 HIS A NE2 
2594 N N   . PRO A 315 ? 0.29577 0.33331 0.21964 -0.06200 0.01792  0.09508  309 PRO A N   
2595 C CA  . PRO A 315 ? 0.31311 0.33509 0.18412 -0.04167 0.01455  0.08389  309 PRO A CA  
2596 C C   . PRO A 315 ? 0.27501 0.30681 0.20185 -0.05154 0.02446  0.09307  309 PRO A C   
2597 O O   . PRO A 315 ? 0.29040 0.32613 0.22798 -0.05475 0.03859  0.04902  309 PRO A O   
2598 C CB  . PRO A 315 ? 0.33438 0.37696 0.19881 -0.01233 0.01028  0.08618  309 PRO A CB  
2599 C CG  . PRO A 315 ? 0.32320 0.39362 0.21812 -0.02994 -0.01232 0.09935  309 PRO A CG  
2600 C CD  . PRO A 315 ? 0.34775 0.37617 0.18607 -0.02489 0.02893  0.09021  309 PRO A CD  
2601 N N   . TYR A 316 ? 0.28552 0.31003 0.21080 -0.05080 -0.00789 0.05939  310 TYR A N   
2602 C CA  . TYR A 316 ? 0.26239 0.29769 0.21497 -0.05846 -0.02569 -0.00820 310 TYR A CA  
2603 C C   . TYR A 316 ? 0.25253 0.30318 0.21013 -0.06272 0.01968  -0.02982 310 TYR A C   
2604 O O   . TYR A 316 ? 0.26695 0.30361 0.24525 -0.04665 0.06566  -0.00872 310 TYR A O   
2605 C CB  . TYR A 316 ? 0.28234 0.28156 0.21797 -0.06256 0.03011  -0.00010 310 TYR A CB  
2606 C CG  . TYR A 316 ? 0.33150 0.28843 0.22672 -0.03758 -0.00018 0.00566  310 TYR A CG  
2607 C CD1 . TYR A 316 ? 0.35727 0.26783 0.25166 0.02321  0.00031  -0.02059 310 TYR A CD1 
2608 C CD2 . TYR A 316 ? 0.29589 0.30850 0.22114 -0.03713 -0.04501 0.01779  310 TYR A CD2 
2609 C CE1 . TYR A 316 ? 0.34192 0.27274 0.28294 -0.00295 0.00594  -0.01048 310 TYR A CE1 
2610 C CE2 . TYR A 316 ? 0.30295 0.31606 0.27175 -0.00424 0.00304  -0.00266 310 TYR A CE2 
2611 C CZ  . TYR A 316 ? 0.36806 0.32788 0.30803 0.01617  -0.00787 -0.02040 310 TYR A CZ  
2612 O OH  . TYR A 316 ? 0.38219 0.37811 0.31672 0.01756  -0.00739 -0.03263 310 TYR A OH  
2613 N N   . LEU A 317 ? 0.30823 0.27653 0.18775 -0.09667 0.01999  -0.03269 311 LEU A N   
2614 C CA  . LEU A 317 ? 0.27817 0.29310 0.20318 -0.09602 0.04634  -0.00115 311 LEU A CA  
2615 C C   . LEU A 317 ? 0.25498 0.32725 0.22863 -0.07362 0.04899  0.02632  311 LEU A C   
2616 O O   . LEU A 317 ? 0.25398 0.34687 0.20128 -0.07382 0.01709  -0.01325 311 LEU A O   
2617 C CB  . LEU A 317 ? 0.25874 0.27924 0.22369 -0.05506 0.04453  0.04442  311 LEU A CB  
2618 C CG  . LEU A 317 ? 0.21837 0.31872 0.20650 -0.01096 0.01699  0.02096  311 LEU A CG  
2619 C CD1 . LEU A 317 ? 0.24935 0.32830 0.22843 -0.03106 0.06113  0.01995  311 LEU A CD1 
2620 C CD2 . LEU A 317 ? 0.19291 0.34365 0.24776 0.02442  -0.03745 0.03297  311 LEU A CD2 
2621 N N   . GLU A 318 ? 0.25925 0.34170 0.25163 -0.06045 0.03005  0.07186  312 GLU A N   
2622 C CA  . GLU A 318 ? 0.30763 0.36728 0.25482 -0.10331 0.04192  0.03595  312 GLU A CA  
2623 C C   . GLU A 318 ? 0.29872 0.38240 0.24521 -0.10724 0.03396  0.03692  312 GLU A C   
2624 O O   . GLU A 318 ? 0.36568 0.38804 0.27582 -0.15665 0.04023  0.01793  312 GLU A O   
2625 C CB  A GLU A 318 ? 0.40674 0.36161 0.27289 -0.12665 0.03248  0.00411  312 GLU A CB  
2626 C CB  B GLU A 318 ? 0.39510 0.40080 0.24681 -0.08785 0.05311  0.03646  312 GLU A CB  
2627 C CG  A GLU A 318 ? 0.54118 0.36253 0.29450 -0.11746 0.07971  -0.01342 312 GLU A CG  
2628 C CG  B GLU A 318 ? 0.51017 0.42522 0.23748 -0.05710 0.11405  0.05170  312 GLU A CG  
2629 C CD  A GLU A 318 ? 0.67089 0.38861 0.38363 -0.09826 0.12362  -0.04427 312 GLU A CD  
2630 C CD  B GLU A 318 ? 0.64629 0.44000 0.27471 -0.02142 0.14828  0.05920  312 GLU A CD  
2631 O OE1 A GLU A 318 ? 0.72232 0.40796 0.43576 -0.07542 0.12566  -0.07210 312 GLU A OE1 
2632 O OE1 B GLU A 318 ? 0.73405 0.46014 0.30177 0.04394  0.13816  0.07831  312 GLU A OE1 
2633 O OE2 A GLU A 318 ? 0.72500 0.39790 0.40955 -0.10151 0.16380  -0.03034 312 GLU A OE2 
2634 O OE2 B GLU A 318 ? 0.60434 0.42963 0.23525 -0.06290 0.15799  0.02498  312 GLU A OE2 
2635 N N   . GLN A 319 ? 0.22822 0.39675 0.26226 -0.06598 0.04839  0.01430  313 GLN A N   
2636 C CA  . GLN A 319 ? 0.26845 0.39136 0.29111 -0.03037 0.07507  -0.01829 313 GLN A CA  
2637 C C   . GLN A 319 ? 0.26663 0.35905 0.29557 -0.05552 0.03067  -0.00722 313 GLN A C   
2638 O O   . GLN A 319 ? 0.30156 0.39900 0.35937 -0.10537 0.00913  0.00596  313 GLN A O   
2639 C CB  . GLN A 319 ? 0.20998 0.44901 0.32704 0.01185  0.07476  -0.01211 313 GLN A CB  
2640 C CG  . GLN A 319 ? 0.26487 0.46526 0.37082 -0.02921 0.11907  -0.01486 313 GLN A CG  
2641 C CD  . GLN A 319 ? 0.34705 0.49806 0.43672 -0.03423 0.13327  0.00138  313 GLN A CD  
2642 O OE1 . GLN A 319 ? 0.31354 0.50589 0.48921 -0.03964 0.12666  0.02069  313 GLN A OE1 
2643 N NE2 . GLN A 319 ? 0.39327 0.51923 0.45470 -0.03369 0.12091  -0.02500 313 GLN A NE2 
2644 N N   . TYR A 320 ? 0.25691 0.32466 0.32783 -0.04908 0.12034  -0.02647 314 TYR A N   
2645 C CA  . TYR A 320 ? 0.26192 0.33020 0.25980 -0.07142 0.06066  0.00209  314 TYR A CA  
2646 C C   . TYR A 320 ? 0.26589 0.33611 0.27840 -0.06374 0.01298  -0.00768 314 TYR A C   
2647 O O   . TYR A 320 ? 0.24832 0.34642 0.28621 -0.06139 0.00684  -0.02174 314 TYR A O   
2648 C CB  . TYR A 320 ? 0.25837 0.34982 0.28706 -0.07014 0.06632  -0.01262 314 TYR A CB  
2649 C CG  . TYR A 320 ? 0.23923 0.39041 0.32821 -0.06599 0.05025  -0.00690 314 TYR A CG  
2650 C CD1 . TYR A 320 ? 0.28299 0.41672 0.35696 -0.05231 0.05370  0.01741  314 TYR A CD1 
2651 C CD2 . TYR A 320 ? 0.23511 0.39339 0.37289 -0.05650 0.04792  -0.00964 314 TYR A CD2 
2652 C CE1 . TYR A 320 ? 0.31424 0.43749 0.43443 -0.00931 0.04452  0.03621  314 TYR A CE1 
2653 C CE2 . TYR A 320 ? 0.22724 0.40427 0.40738 -0.02648 0.02841  0.04380  314 TYR A CE2 
2654 C CZ  . TYR A 320 ? 0.28113 0.42594 0.45509 0.02331  0.03377  0.03383  314 TYR A CZ  
2655 O OH  . TYR A 320 ? 0.31357 0.43733 0.52268 0.06929  0.02290  0.05925  314 TYR A OH  
2656 N N   . TYR A 321 ? 0.23910 0.32140 0.26625 -0.05907 0.02309  0.01497  315 TYR A N   
2657 C CA  . TYR A 321 ? 0.25634 0.30705 0.27886 -0.06950 0.02729  -0.00353 315 TYR A CA  
2658 C C   . TYR A 321 ? 0.29107 0.31750 0.25371 -0.08940 0.06346  -0.02989 315 TYR A C   
2659 O O   . TYR A 321 ? 0.38779 0.37603 0.24691 -0.11050 0.05446  -0.02578 315 TYR A O   
2660 C CB  . TYR A 321 ? 0.26587 0.31328 0.27288 -0.03462 -0.03264 0.01559  315 TYR A CB  
2661 C CG  . TYR A 321 ? 0.28241 0.27835 0.29055 -0.04721 -0.02855 0.03071  315 TYR A CG  
2662 C CD1 . TYR A 321 ? 0.32781 0.26384 0.28883 -0.03651 -0.02346 0.02795  315 TYR A CD1 
2663 C CD2 . TYR A 321 ? 0.36061 0.27002 0.30525 -0.02343 0.01831  0.01633  315 TYR A CD2 
2664 C CE1 . TYR A 321 ? 0.35276 0.23925 0.30612 -0.04108 -0.02697 0.02777  315 TYR A CE1 
2665 C CE2 . TYR A 321 ? 0.34435 0.22478 0.31270 -0.03629 0.01956  0.01297  315 TYR A CE2 
2666 C CZ  . TYR A 321 ? 0.37072 0.22723 0.34827 -0.02989 0.00469  0.01725  315 TYR A CZ  
2667 O OH  . TYR A 321 ? 0.38211 0.22201 0.39385 -0.02581 -0.09426 0.03931  315 TYR A OH  
2668 N N   . ASP A 322 ? 0.31243 0.27670 0.20985 -0.02543 0.02404  -0.04134 316 ASP A N   
2669 C CA  . ASP A 322 ? 0.33788 0.27296 0.26364 -0.05764 0.01746  -0.06180 316 ASP A CA  
2670 C C   . ASP A 322 ? 0.35427 0.26334 0.24917 -0.04374 0.03475  -0.00284 316 ASP A C   
2671 O O   . ASP A 322 ? 0.37862 0.22910 0.25664 -0.02966 0.01852  -0.00340 316 ASP A O   
2672 C CB  . ASP A 322 ? 0.35849 0.31165 0.29260 -0.11883 -0.00387 -0.07660 316 ASP A CB  
2673 C CG  . ASP A 322 ? 0.39726 0.32527 0.28152 -0.15498 -0.01396 -0.03861 316 ASP A CG  
2674 O OD1 . ASP A 322 ? 0.49135 0.34107 0.25941 -0.13320 0.00423  -0.02415 316 ASP A OD1 
2675 O OD2 . ASP A 322 ? 0.37722 0.34348 0.31394 -0.18845 0.03189  -0.02370 316 ASP A OD2 
2676 N N   . PRO A 323 ? 0.34614 0.30305 0.23638 -0.01794 0.02393  0.04506  317 PRO A N   
2677 C CA  . PRO A 323 ? 0.29779 0.31463 0.25725 0.03573  -0.02824 0.04251  317 PRO A CA  
2678 C C   . PRO A 323 ? 0.31280 0.29557 0.28834 0.05170  -0.01416 0.07695  317 PRO A C   
2679 O O   . PRO A 323 ? 0.31541 0.30482 0.28450 0.01280  0.00233  0.05469  317 PRO A O   
2680 C CB  . PRO A 323 ? 0.33045 0.38125 0.23730 0.04005  -0.08697 0.01685  317 PRO A CB  
2681 C CG  . PRO A 323 ? 0.35316 0.37649 0.24398 0.00019  -0.06913 0.02927  317 PRO A CG  
2682 C CD  . PRO A 323 ? 0.32145 0.34838 0.24568 0.00660  -0.06008 0.04256  317 PRO A CD  
2683 N N   . SER A 324 ? 0.35906 0.26438 0.29126 0.05826  -0.04931 0.03685  318 SER A N   
2684 C CA  . SER A 324 ? 0.38867 0.27079 0.26489 0.04661  -0.02090 0.01477  318 SER A CA  
2685 C C   . SER A 324 ? 0.36761 0.23712 0.27977 0.02777  -0.03123 0.00294  318 SER A C   
2686 O O   . SER A 324 ? 0.42294 0.24787 0.29480 0.04167  -0.04893 -0.01496 318 SER A O   
2687 C CB  . SER A 324 ? 0.35850 0.30357 0.33171 0.00384  0.06553  -0.02411 318 SER A CB  
2688 O OG  . SER A 324 ? 0.43788 0.34422 0.40316 -0.01697 0.04166  -0.06281 318 SER A OG  
2689 N N   . ASP A 325 ? 0.25756 0.22554 0.29783 -0.00450 0.01006  0.01021  319 ASP A N   
2690 C CA  . ASP A 325 ? 0.22663 0.26992 0.31858 -0.05435 -0.01864 -0.00179 319 ASP A CA  
2691 C C   . ASP A 325 ? 0.23015 0.25823 0.28284 -0.04644 -0.00805 0.03199  319 ASP A C   
2692 O O   . ASP A 325 ? 0.23002 0.22246 0.29816 -0.02623 -0.01257 0.02644  319 ASP A O   
2693 C CB  . ASP A 325 ? 0.21185 0.34292 0.38144 -0.01187 -0.00728 0.02335  319 ASP A CB  
2694 C CG  . ASP A 325 ? 0.26803 0.40853 0.45861 -0.02929 0.02538  -0.01558 319 ASP A CG  
2695 O OD1 . ASP A 325 ? 0.29279 0.42199 0.44857 -0.03702 0.04315  -0.05249 319 ASP A OD1 
2696 O OD2 . ASP A 325 ? 0.29705 0.45164 0.51097 0.00319  0.01263  0.00202  319 ASP A OD2 
2697 N N   . GLU A 326 ? 0.23648 0.29089 0.25831 -0.04283 -0.01709 0.03997  320 GLU A N   
2698 C CA  . GLU A 326 ? 0.24121 0.30501 0.20130 -0.02162 0.00351  0.00618  320 GLU A CA  
2699 C C   . GLU A 326 ? 0.23863 0.28038 0.23739 -0.01420 0.01337  0.00595  320 GLU A C   
2700 O O   . GLU A 326 ? 0.23173 0.28171 0.26242 0.02782  0.01132  0.03146  320 GLU A O   
2701 C CB  . GLU A 326 ? 0.25909 0.32831 0.20782 0.00901  -0.01486 -0.00260 320 GLU A CB  
2702 C CG  . GLU A 326 ? 0.28978 0.34930 0.24123 0.01685  0.02106  0.00450  320 GLU A CG  
2703 C CD  . GLU A 326 ? 0.30544 0.34537 0.31307 -0.00947 0.04136  0.01696  320 GLU A CD  
2704 O OE1 . GLU A 326 ? 0.28926 0.35822 0.31456 -0.01416 -0.02511 0.01117  320 GLU A OE1 
2705 O OE2 . GLU A 326 ? 0.27432 0.35058 0.24701 -0.03101 0.00426  0.03405  320 GLU A OE2 
2706 N N   . PRO A 327 ? 0.20025 0.26155 0.23500 0.00259  -0.02545 0.02389  321 PRO A N   
2707 C CA  . PRO A 327 ? 0.26864 0.27095 0.23131 -0.01460 -0.01174 0.01360  321 PRO A CA  
2708 C C   . PRO A 327 ? 0.25334 0.24581 0.24235 0.02877  -0.01505 0.02417  321 PRO A C   
2709 O O   . PRO A 327 ? 0.30554 0.24319 0.22147 -0.00431 0.04610  0.01768  321 PRO A O   
2710 C CB  . PRO A 327 ? 0.32004 0.30526 0.25411 0.03113  -0.04631 0.00460  321 PRO A CB  
2711 C CG  . PRO A 327 ? 0.31590 0.30503 0.22601 0.04365  -0.02579 0.03297  321 PRO A CG  
2712 C CD  . PRO A 327 ? 0.24908 0.28599 0.17490 0.02157  -0.03030 0.05270  321 PRO A CD  
2713 N N   . ILE A 328 ? 0.21173 0.23332 0.23593 -0.03941 -0.00280 0.01197  322 ILE A N   
2714 C CA  . ILE A 328 ? 0.23142 0.25231 0.22287 -0.02166 -0.02021 -0.01871 322 ILE A CA  
2715 C C   . ILE A 328 ? 0.26173 0.24006 0.21817 -0.03599 -0.06629 -0.01864 322 ILE A C   
2716 O O   . ILE A 328 ? 0.31053 0.26412 0.21187 -0.05999 -0.03218 -0.01627 322 ILE A O   
2717 C CB  . ILE A 328 ? 0.28059 0.25429 0.22326 0.01161  0.00059  -0.03118 322 ILE A CB  
2718 C CG1 . ILE A 328 ? 0.30172 0.24332 0.26208 0.04879  -0.03298 0.01490  322 ILE A CG1 
2719 C CG2 . ILE A 328 ? 0.30952 0.28693 0.20304 -0.03623 0.01108  -0.06110 322 ILE A CG2 
2720 C CD1 . ILE A 328 ? 0.40361 0.25754 0.29559 0.04602  -0.04097 -0.00312 322 ILE A CD1 
2721 N N   . ALA A 329 ? 0.26277 0.23280 0.20830 -0.04117 0.00238  -0.01170 323 ALA A N   
2722 C CA  . ALA A 329 ? 0.29921 0.26595 0.22548 -0.02851 0.01255  -0.01737 323 ALA A CA  
2723 C C   . ALA A 329 ? 0.38131 0.29793 0.28909 -0.04351 0.00636  -0.02010 323 ALA A C   
2724 O O   . ALA A 329 ? 0.39895 0.29482 0.31811 -0.01000 0.03916  -0.06494 323 ALA A O   
2725 C CB  . ALA A 329 ? 0.32984 0.29208 0.26742 -0.02813 -0.02628 -0.00659 323 ALA A CB  
2726 N N   . GLU A 330 ? 0.47565 0.36667 0.26701 -0.06468 -0.00752 -0.03478 324 GLU A N   
2727 C CA  . GLU A 330 ? 0.59026 0.44723 0.33467 -0.09973 0.01660  -0.04519 324 GLU A CA  
2728 C C   . GLU A 330 ? 0.67945 0.48869 0.41845 -0.09203 0.16116  -0.03147 324 GLU A C   
2729 O O   . GLU A 330 ? 0.70945 0.51029 0.48969 -0.04587 0.16412  0.00832  324 GLU A O   
2730 C CB  . GLU A 330 ? 0.62039 0.49261 0.38050 -0.09880 -0.05035 -0.06525 324 GLU A CB  
2731 C CG  . GLU A 330 ? 0.66361 0.51176 0.46688 -0.07927 -0.07665 -0.07947 324 GLU A CG  
2732 C CD  . GLU A 330 ? 0.71194 0.51776 0.55448 -0.05350 -0.04626 -0.06392 324 GLU A CD  
2733 O OE1 . GLU A 330 ? 0.73494 0.52463 0.59851 -0.05303 -0.04090 -0.06032 324 GLU A OE1 
2734 O OE2 . GLU A 330 ? 0.72623 0.51288 0.59568 -0.04601 -0.03674 -0.06306 324 GLU A OE2 
2735 N N   . ALA A 331 ? 0.71192 0.49856 0.39548 -0.15460 0.26367  -0.03451 325 ALA A N   
2736 C CA  . ALA A 331 ? 0.72350 0.53679 0.36076 -0.14272 0.21926  -0.04097 325 ALA A CA  
2737 C C   . ALA A 331 ? 0.69864 0.57305 0.34548 -0.10450 0.10927  -0.00553 325 ALA A C   
2738 O O   . ALA A 331 ? 0.68193 0.61705 0.34675 -0.10537 0.02721  0.01668  325 ALA A O   
2739 C CB  . ALA A 331 ? 0.75413 0.53338 0.33329 -0.15446 0.19443  -0.03876 325 ALA A CB  
2740 N N   . PRO A 332 ? 0.70011 0.55345 0.27655 -0.04083 0.07674  0.01559  326 PRO A N   
2741 C CA  . PRO A 332 ? 0.64793 0.54286 0.28783 -0.00350 0.07361  -0.01194 326 PRO A CA  
2742 C C   . PRO A 332 ? 0.47621 0.51602 0.32229 0.04705  0.11635  -0.09287 326 PRO A C   
2743 O O   . PRO A 332 ? 0.50564 0.46597 0.38942 0.06684  0.12583  -0.15221 326 PRO A O   
2744 C CB  . PRO A 332 ? 0.68143 0.53478 0.32801 0.02043  0.05121  0.03485  326 PRO A CB  
2745 C CG  . PRO A 332 ? 0.70537 0.53374 0.32606 0.02232  0.06454  0.03683  326 PRO A CG  
2746 C CD  . PRO A 332 ? 0.71410 0.53886 0.26859 -0.00034 0.08236  0.02846  326 PRO A CD  
2747 N N   . PHE A 333 ? 0.40754 0.54754 0.26773 0.05824  0.06630  -0.08411 327 PHE A N   
2748 C CA  . PHE A 333 ? 0.47163 0.62255 0.29552 0.08096  0.07129  -0.05002 327 PHE A CA  
2749 C C   . PHE A 333 ? 0.52340 0.67994 0.42981 0.07529  0.12421  -0.06670 327 PHE A C   
2750 O O   . PHE A 333 ? 0.52693 0.69475 0.48900 0.12483  0.13287  -0.07413 327 PHE A O   
2751 C CB  . PHE A 333 ? 0.53374 0.66395 0.27606 0.04859  0.03281  -0.02036 327 PHE A CB  
2752 C CG  . PHE A 333 ? 0.51404 0.70474 0.27887 0.02487  -0.04824 -0.05390 327 PHE A CG  
2753 C CD1 . PHE A 333 ? 0.47233 0.70094 0.26100 -0.00327 -0.07328 -0.07590 327 PHE A CD1 
2754 C CD2 . PHE A 333 ? 0.52730 0.73321 0.32173 0.02868  -0.08043 -0.00528 327 PHE A CD2 
2755 C CE1 . PHE A 333 ? 0.52239 0.71115 0.25231 0.03394  -0.08257 -0.02580 327 PHE A CE1 
2756 C CE2 . PHE A 333 ? 0.53085 0.74098 0.31668 0.02355  -0.09304 -0.02738 327 PHE A CE2 
2757 C CZ  . PHE A 333 ? 0.50794 0.73038 0.28833 0.02818  -0.08887 -0.03334 327 PHE A CZ  
2758 N N   . LYS A 334 ? 0.55353 0.70496 0.49549 0.05712  0.15880  -0.08379 328 LYS A N   
2759 C CA  . LYS A 334 ? 0.64309 0.74074 0.55295 0.03087  0.18631  -0.07744 328 LYS A CA  
2760 C C   . LYS A 334 ? 0.69375 0.75510 0.55584 0.02161  0.22738  -0.05080 328 LYS A C   
2761 O O   . LYS A 334 ? 0.73372 0.76350 0.56213 0.01676  0.23201  -0.04718 328 LYS A O   
2762 C CB  . LYS A 334 ? 0.67238 0.75849 0.58246 0.01905  0.20136  -0.09679 328 LYS A CB  
2763 C CG  . LYS A 334 ? 0.71008 0.77671 0.60990 0.02046  0.19771  -0.09027 328 LYS A CG  
2764 C CD  . LYS A 334 ? 0.73740 0.78560 0.62594 0.02515  0.17869  -0.08769 328 LYS A CD  
2765 C CE  . LYS A 334 ? 0.75360 0.79139 0.64660 0.02460  0.17872  -0.08222 328 LYS A CE  
2766 N NZ  . LYS A 334 ? 0.77251 0.79695 0.67093 0.03013  0.18717  -0.07479 328 LYS A NZ  
2767 N N   . PHE A 335 ? 0.68828 0.75734 0.53710 0.02380  0.27161  -0.03659 329 PHE A N   
2768 C CA  . PHE A 335 ? 0.67173 0.75803 0.53375 0.01621  0.27254  -0.03792 329 PHE A CA  
2769 C C   . PHE A 335 ? 0.66557 0.74466 0.52451 0.01794  0.28214  -0.02947 329 PHE A C   
2770 O O   . PHE A 335 ? 0.69707 0.73975 0.53799 0.00960  0.30378  -0.03877 329 PHE A O   
2771 C CB  . PHE A 335 ? 0.68457 0.76527 0.55691 -0.00574 0.24715  -0.03977 329 PHE A CB  
2772 N N   . ASP A 341 ? 0.39941 0.78840 0.76531 -0.03610 -0.19904 0.08563  335 ASP A N   
2773 C CA  . ASP A 341 ? 0.46957 0.78637 0.78623 -0.03716 -0.08014 0.07927  335 ASP A CA  
2774 C C   . ASP A 341 ? 0.48552 0.79481 0.80092 -0.04748 -0.01266 0.06327  335 ASP A C   
2775 O O   . ASP A 341 ? 0.48902 0.80278 0.80417 -0.03587 0.02520  0.07910  335 ASP A O   
2776 C CB  . ASP A 341 ? 0.50336 0.77772 0.80092 -0.03284 -0.01294 0.07982  335 ASP A CB  
2777 N N   . LEU A 342 ? 0.48724 0.79091 0.79277 -0.04705 -0.01398 0.03915  336 LEU A N   
2778 C CA  . LEU A 342 ? 0.47346 0.77527 0.79128 -0.04919 0.00328  0.00865  336 LEU A CA  
2779 C C   . LEU A 342 ? 0.41830 0.76598 0.74137 -0.03156 -0.02470 0.00046  336 LEU A C   
2780 O O   . LEU A 342 ? 0.36116 0.77977 0.69934 -0.00453 -0.10540 -0.01594 336 LEU A O   
2781 C CB  . LEU A 342 ? 0.50100 0.75881 0.79551 -0.06171 0.00603  -0.01502 336 LEU A CB  
2782 C CG  . LEU A 342 ? 0.54639 0.75581 0.79054 -0.05182 0.03215  -0.02615 336 LEU A CG  
2783 C CD1 . LEU A 342 ? 0.57499 0.75565 0.79310 -0.02428 0.04167  -0.02444 336 LEU A CD1 
2784 C CD2 . LEU A 342 ? 0.54603 0.75749 0.79291 -0.05816 0.05999  -0.02888 336 LEU A CD2 
2785 N N   . PRO A 343 ? 0.40178 0.74583 0.71282 -0.03255 0.00413  0.00649  337 PRO A N   
2786 C CA  . PRO A 343 ? 0.36329 0.72095 0.68042 -0.04431 0.02148  0.00509  337 PRO A CA  
2787 C C   . PRO A 343 ? 0.33076 0.69544 0.63101 -0.03689 0.03376  0.00421  337 PRO A C   
2788 O O   . PRO A 343 ? 0.32129 0.68213 0.63930 -0.04934 0.02114  -0.01052 337 PRO A O   
2789 C CB  . PRO A 343 ? 0.40806 0.72489 0.73606 -0.04026 0.11350  0.02169  337 PRO A CB  
2790 C CG  . PRO A 343 ? 0.47276 0.73296 0.75317 -0.03280 0.13851  0.02527  337 PRO A CG  
2791 C CD  . PRO A 343 ? 0.45028 0.74235 0.72656 -0.02264 0.06921  0.02273  337 PRO A CD  
2792 N N   . LYS A 344 ? 0.30691 0.66603 0.56546 -0.03432 0.01014  0.02479  338 LYS A N   
2793 C CA  . LYS A 344 ? 0.29727 0.65299 0.50881 -0.06680 -0.00683 0.00216  338 LYS A CA  
2794 C C   . LYS A 344 ? 0.33625 0.66729 0.47053 -0.10566 0.08022  -0.03181 338 LYS A C   
2795 O O   . LYS A 344 ? 0.34707 0.66751 0.47199 -0.11027 0.11262  -0.03062 338 LYS A O   
2796 C CB  . LYS A 344 ? 0.29640 0.61860 0.54952 -0.06278 -0.00374 0.05008  338 LYS A CB  
2797 C CG  . LYS A 344 ? 0.31814 0.58952 0.59102 -0.08704 0.06743  0.06824  338 LYS A CG  
2798 C CD  . LYS A 344 ? 0.31891 0.55546 0.59754 -0.08086 0.07472  0.08658  338 LYS A CD  
2799 C CE  . LYS A 344 ? 0.31885 0.54903 0.61944 -0.08254 0.09837  0.08859  338 LYS A CE  
2800 N NZ  . LYS A 344 ? 0.31782 0.55212 0.64902 -0.09604 0.10487  0.08175  338 LYS A NZ  
2801 N N   . GLU A 345 ? 0.32533 0.65390 0.40914 -0.14703 0.11892  -0.05512 339 GLU A N   
2802 C CA  . GLU A 345 ? 0.37535 0.64424 0.44741 -0.12949 0.13535  -0.00116 339 GLU A CA  
2803 C C   . GLU A 345 ? 0.35451 0.65137 0.44485 -0.07449 0.10714  0.01142  339 GLU A C   
2804 O O   . GLU A 345 ? 0.36480 0.65820 0.41766 -0.04356 0.09308  0.02195  339 GLU A O   
2805 C CB  . GLU A 345 ? 0.40049 0.62426 0.44405 -0.15088 0.14813  0.01499  339 GLU A CB  
2806 C CG  . GLU A 345 ? 0.42517 0.62557 0.45907 -0.17739 0.13091  -0.02441 339 GLU A CG  
2807 C CD  . GLU A 345 ? 0.45433 0.63118 0.47717 -0.15778 0.16960  -0.06163 339 GLU A CD  
2808 O OE1 . GLU A 345 ? 0.41308 0.62746 0.44888 -0.10889 0.17541  -0.07111 339 GLU A OE1 
2809 O OE2 . GLU A 345 ? 0.51272 0.64102 0.50673 -0.17824 0.15375  -0.08589 339 GLU A OE2 
2810 N N   . LYS A 346 ? 0.33658 0.64773 0.44731 -0.01211 0.09356  0.04415  340 LYS A N   
2811 C CA  . LYS A 346 ? 0.26234 0.64214 0.48321 0.01067  0.09381  0.04957  340 LYS A CA  
2812 C C   . LYS A 346 ? 0.26710 0.63296 0.48580 0.00230  0.06572  0.03843  340 LYS A C   
2813 O O   . LYS A 346 ? 0.25214 0.63844 0.52454 0.00397  0.04370  0.03823  340 LYS A O   
2814 C CB  . LYS A 346 ? 0.19731 0.61456 0.46250 0.06083  0.09664  0.04447  340 LYS A CB  
2815 C CG  . LYS A 346 ? 0.27621 0.64641 0.47963 0.05514  0.11775  0.04938  340 LYS A CG  
2816 C CD  . LYS A 346 ? 0.38384 0.65270 0.46078 0.07309  0.11531  0.05278  340 LYS A CD  
2817 C CE  . LYS A 346 ? 0.47063 0.65445 0.46373 0.07932  0.12018  0.07244  340 LYS A CE  
2818 N NZ  . LYS A 346 ? 0.53841 0.65931 0.47325 0.10042  0.12122  0.08626  340 LYS A NZ  
2819 N N   . LEU A 347 ? 0.24688 0.60992 0.44439 0.02872  0.05971  0.01345  341 LEU A N   
2820 C CA  . LEU A 347 ? 0.24387 0.60912 0.43368 0.00649  0.01767  0.01302  341 LEU A CA  
2821 C C   . LEU A 347 ? 0.23877 0.58631 0.37983 -0.01014 0.02421  0.01469  341 LEU A C   
2822 O O   . LEU A 347 ? 0.20056 0.59618 0.35307 -0.02743 0.01132  0.04152  341 LEU A O   
2823 C CB  . LEU A 347 ? 0.27380 0.62285 0.45799 -0.00327 -0.02625 0.00623  341 LEU A CB  
2824 C CG  . LEU A 347 ? 0.30713 0.63365 0.51696 0.01862  -0.00023 -0.00102 341 LEU A CG  
2825 C CD1 . LEU A 347 ? 0.33604 0.63070 0.51774 0.01881  -0.02338 -0.02897 341 LEU A CD1 
2826 C CD2 . LEU A 347 ? 0.28539 0.62874 0.53717 0.03324  0.02764  0.00720  341 LEU A CD2 
2827 N N   . LYS A 348 ? 0.24609 0.54569 0.33409 -0.02118 -0.00139 0.02437  342 LYS A N   
2828 C CA  . LYS A 348 ? 0.24957 0.53165 0.30581 -0.03242 -0.05942 0.04076  342 LYS A CA  
2829 C C   . LYS A 348 ? 0.26072 0.54032 0.31037 -0.03612 0.00057  0.02376  342 LYS A C   
2830 O O   . LYS A 348 ? 0.27190 0.52546 0.29006 -0.05815 0.01498  0.06010  342 LYS A O   
2831 C CB  . LYS A 348 ? 0.25538 0.52101 0.31958 -0.03661 -0.04372 0.05044  342 LYS A CB  
2832 C CG  . LYS A 348 ? 0.25841 0.52035 0.28217 -0.03613 -0.09203 0.08009  342 LYS A CG  
2833 C CD  . LYS A 348 ? 0.28983 0.52526 0.30814 -0.02401 -0.06662 0.08764  342 LYS A CD  
2834 C CE  . LYS A 348 ? 0.33651 0.51609 0.30884 -0.03687 -0.04702 0.09244  342 LYS A CE  
2835 N NZ  . LYS A 348 ? 0.37722 0.51818 0.31262 -0.04439 -0.02013 0.06739  342 LYS A NZ  
2836 N N   . GLU A 349 ? 0.29061 0.58080 0.36648 0.00038  0.03878  -0.00027 343 GLU A N   
2837 C CA  . GLU A 349 ? 0.33174 0.63909 0.40088 0.01927  0.11240  -0.01796 343 GLU A CA  
2838 C C   . GLU A 349 ? 0.31400 0.65268 0.38234 0.03665  0.09130  0.00904  343 GLU A C   
2839 O O   . GLU A 349 ? 0.30338 0.65612 0.37122 0.07601  0.06402  0.01453  343 GLU A O   
2840 C CB  . GLU A 349 ? 0.33086 0.69040 0.48863 0.04353  0.14327  -0.06480 343 GLU A CB  
2841 C CG  . GLU A 349 ? 0.44667 0.74880 0.57474 0.05865  0.18844  -0.09756 343 GLU A CG  
2842 C CD  . GLU A 349 ? 0.62883 0.79983 0.63020 0.07141  0.20479  -0.11706 343 GLU A CD  
2843 O OE1 . GLU A 349 ? 0.60980 0.79544 0.62660 0.13721  0.16856  -0.13761 343 GLU A OE1 
2844 O OE2 . GLU A 349 ? 0.78246 0.84276 0.68721 0.01580  0.30255  -0.11473 343 GLU A OE2 
2845 N N   . LEU A 350 ? 0.25523 0.64556 0.35274 0.06887  0.02405  0.03357  344 LEU A N   
2846 C CA  . LEU A 350 ? 0.26525 0.62557 0.37786 0.08886  -0.02619 0.04833  344 LEU A CA  
2847 C C   . LEU A 350 ? 0.28563 0.56584 0.36857 0.08088  0.00051  0.05139  344 LEU A C   
2848 O O   . LEU A 350 ? 0.31912 0.54005 0.40240 0.09799  -0.02549 0.04420  344 LEU A O   
2849 C CB  . LEU A 350 ? 0.24051 0.64051 0.41223 0.14111  -0.02504 0.09065  344 LEU A CB  
2850 C CG  . LEU A 350 ? 0.32034 0.65811 0.48578 0.15785  -0.00164 0.07253  344 LEU A CG  
2851 C CD1 . LEU A 350 ? 0.33866 0.67287 0.52401 0.12944  0.00006  0.08086  344 LEU A CD1 
2852 C CD2 . LEU A 350 ? 0.36664 0.66386 0.48989 0.17064  0.01295  0.03591  344 LEU A CD2 
2853 N N   . ILE A 351 ? 0.22172 0.51561 0.32720 0.06613  -0.01702 0.04598  345 ILE A N   
2854 C CA  . ILE A 351 ? 0.22212 0.46938 0.28167 0.02595  -0.02462 0.06268  345 ILE A CA  
2855 C C   . ILE A 351 ? 0.28242 0.44677 0.24316 0.00397  0.01353  0.07883  345 ILE A C   
2856 O O   . ILE A 351 ? 0.29236 0.44291 0.24927 -0.00720 0.00392  0.07729  345 ILE A O   
2857 C CB  . ILE A 351 ? 0.23699 0.45385 0.24299 0.00798  -0.04047 0.03218  345 ILE A CB  
2858 C CG1 . ILE A 351 ? 0.30584 0.46762 0.26585 0.02080  -0.00240 0.01662  345 ILE A CG1 
2859 C CG2 . ILE A 351 ? 0.29007 0.43137 0.26031 -0.01740 0.02792  0.02404  345 ILE A CG2 
2860 C CD1 . ILE A 351 ? 0.32613 0.45188 0.25420 0.03102  0.02553  -0.00428 345 ILE A CD1 
2861 N N   . PHE A 352 ? 0.29787 0.43590 0.22880 0.02384  0.00430  0.06521  346 PHE A N   
2862 C CA  . PHE A 352 ? 0.32290 0.42357 0.23013 0.00775  -0.01602 0.06854  346 PHE A CA  
2863 C C   . PHE A 352 ? 0.33279 0.42510 0.28822 0.02594  -0.03153 0.05222  346 PHE A C   
2864 O O   . PHE A 352 ? 0.32775 0.39001 0.30022 0.03152  -0.02954 0.03712  346 PHE A O   
2865 C CB  . PHE A 352 ? 0.39119 0.42355 0.24520 0.01894  0.00553  0.09802  346 PHE A CB  
2866 C CG  . PHE A 352 ? 0.38894 0.42190 0.27066 0.02494  -0.01472 0.08926  346 PHE A CG  
2867 C CD1 . PHE A 352 ? 0.34468 0.38558 0.28806 0.01916  -0.04056 0.08733  346 PHE A CD1 
2868 C CD2 . PHE A 352 ? 0.38985 0.44090 0.27034 0.03996  -0.02164 0.07265  346 PHE A CD2 
2869 C CE1 . PHE A 352 ? 0.33205 0.38199 0.31299 0.03743  0.00214  0.06443  346 PHE A CE1 
2870 C CE2 . PHE A 352 ? 0.39671 0.43260 0.29601 0.02754  0.01530  0.05856  346 PHE A CE2 
2871 C CZ  . PHE A 352 ? 0.38412 0.41346 0.31349 0.01128  0.01887  0.05405  346 PHE A CZ  
2872 N N   . GLU A 353 ? 0.33702 0.43461 0.32305 0.07668  -0.01893 0.05364  347 GLU A N   
2873 C CA  . GLU A 353 ? 0.40873 0.47828 0.40547 0.10703  -0.01366 0.05529  347 GLU A CA  
2874 C C   . GLU A 353 ? 0.41520 0.45485 0.38781 0.09681  -0.02051 0.04839  347 GLU A C   
2875 O O   . GLU A 353 ? 0.49241 0.44328 0.40868 0.07977  0.00636  0.04344  347 GLU A O   
2876 C CB  . GLU A 353 ? 0.45507 0.53022 0.51032 0.13259  -0.03104 0.03052  347 GLU A CB  
2877 C CG  . GLU A 353 ? 0.57773 0.60616 0.62577 0.14164  0.05601  -0.00302 347 GLU A CG  
2878 C CD  . GLU A 353 ? 0.67668 0.64600 0.70352 0.16840  0.10924  -0.02552 347 GLU A CD  
2879 O OE1 . GLU A 353 ? 0.74225 0.66772 0.73351 0.14973  0.12429  -0.04469 347 GLU A OE1 
2880 O OE2 . GLU A 353 ? 0.66958 0.65135 0.72640 0.21453  0.12872  -0.01728 347 GLU A OE2 
2881 N N   . GLU A 354 ? 0.41683 0.45737 0.33275 0.06820  -0.04386 0.03126  348 GLU A N   
2882 C CA  . GLU A 354 ? 0.37090 0.43953 0.37741 0.03166  -0.02832 0.03943  348 GLU A CA  
2883 C C   . GLU A 354 ? 0.37119 0.40495 0.37343 0.03421  -0.02818 0.07081  348 GLU A C   
2884 O O   . GLU A 354 ? 0.44922 0.43073 0.41634 0.04185  -0.03462 0.09977  348 GLU A O   
2885 C CB  . GLU A 354 ? 0.38034 0.47000 0.42273 0.01227  -0.03797 0.01932  348 GLU A CB  
2886 C CG  . GLU A 354 ? 0.49491 0.51716 0.45330 0.00506  -0.00541 0.00971  348 GLU A CG  
2887 C CD  . GLU A 354 ? 0.55186 0.55066 0.46622 0.01465  0.00137  0.03077  348 GLU A CD  
2888 O OE1 . GLU A 354 ? 0.60287 0.57064 0.43944 0.00532  -0.06127 0.01028  348 GLU A OE1 
2889 O OE2 . GLU A 354 ? 0.54376 0.56670 0.51237 0.01851  0.06506  0.04774  348 GLU A OE2 
2890 N N   . THR A 355 ? 0.32259 0.35195 0.32655 0.06000  -0.05358 0.07635  349 THR A N   
2891 C CA  . THR A 355 ? 0.31084 0.33787 0.31234 0.01545  -0.05471 0.04112  349 THR A CA  
2892 C C   . THR A 355 ? 0.30504 0.32549 0.33050 0.03408  -0.05312 0.03114  349 THR A C   
2893 O O   . THR A 355 ? 0.30299 0.32676 0.32469 0.02611  -0.05722 0.03304  349 THR A O   
2894 C CB  . THR A 355 ? 0.32613 0.36083 0.24973 -0.01588 -0.06588 0.03631  349 THR A CB  
2895 O OG1 . THR A 355 ? 0.33185 0.34778 0.24972 -0.00932 -0.01524 0.04843  349 THR A OG1 
2896 C CG2 . THR A 355 ? 0.33962 0.39644 0.25351 -0.05124 -0.08668 0.03430  349 THR A CG2 
2897 N N   . ALA A 356 ? 0.38593 0.31296 0.34762 0.01514  0.03602  0.00424  350 ALA A N   
2898 C CA  . ALA A 356 ? 0.36843 0.33503 0.38145 -0.01087 -0.00793 -0.01119 350 ALA A CA  
2899 C C   . ALA A 356 ? 0.45275 0.36257 0.40493 -0.02353 0.00085  0.00215  350 ALA A C   
2900 O O   . ALA A 356 ? 0.46952 0.38514 0.40738 -0.01976 -0.01019 0.00040  350 ALA A O   
2901 C CB  . ALA A 356 ? 0.37375 0.32652 0.40420 0.03083  0.04948  -0.00125 350 ALA A CB  
2902 N N   . ARG A 357 ? 0.46103 0.35361 0.39534 -0.03606 -0.01177 0.03996  351 ARG A N   
2903 C CA  . ARG A 357 ? 0.49723 0.37402 0.39147 -0.01098 -0.05440 0.04414  351 ARG A CA  
2904 C C   . ARG A 357 ? 0.48673 0.39594 0.38513 -0.04401 -0.08719 0.00421  351 ARG A C   
2905 O O   . ARG A 357 ? 0.53056 0.42900 0.39783 -0.07710 -0.11452 -0.03257 351 ARG A O   
2906 C CB  . ARG A 357 ? 0.55151 0.36606 0.34375 0.00345  -0.07374 0.07186  351 ARG A CB  
2907 C CG  . ARG A 357 ? 0.58798 0.37009 0.35565 -0.00779 -0.09474 0.10083  351 ARG A CG  
2908 C CD  . ARG A 357 ? 0.59876 0.37595 0.34574 0.01435  -0.15102 0.11631  351 ARG A CD  
2909 N NE  . ARG A 357 ? 0.60847 0.38390 0.34725 0.02556  -0.16280 0.14301  351 ARG A NE  
2910 C CZ  . ARG A 357 ? 0.65774 0.41496 0.43693 0.02588  -0.07563 0.13632  351 ARG A CZ  
2911 N NH1 . ARG A 357 ? 0.70712 0.41954 0.47884 0.03064  -0.01689 0.14699  351 ARG A NH1 
2912 N NH2 . ARG A 357 ? 0.62487 0.42665 0.43972 0.03620  -0.08881 0.12039  351 ARG A NH2 
2913 N N   . PHE A 358 ? 0.45782 0.38472 0.34832 -0.04389 -0.04556 0.02277  352 PHE A N   
2914 C CA  . PHE A 358 ? 0.42235 0.39287 0.29183 -0.04687 -0.09896 0.00358  352 PHE A CA  
2915 C C   . PHE A 358 ? 0.44401 0.44619 0.30932 -0.05768 -0.08228 0.00266  352 PHE A C   
2916 O O   . PHE A 358 ? 0.42729 0.49121 0.32024 -0.03943 -0.07739 0.03709  352 PHE A O   
2917 C CB  . PHE A 358 ? 0.40575 0.38102 0.29054 -0.04691 -0.13115 -0.00830 352 PHE A CB  
2918 C CG  . PHE A 358 ? 0.46693 0.37505 0.33405 -0.03788 -0.09901 0.03123  352 PHE A CG  
2919 C CD1 . PHE A 358 ? 0.48667 0.34348 0.33238 -0.04481 -0.11565 0.04143  352 PHE A CD1 
2920 C CD2 . PHE A 358 ? 0.50477 0.40663 0.34579 -0.05759 -0.10184 0.04566  352 PHE A CD2 
2921 C CE1 . PHE A 358 ? 0.51482 0.35199 0.32418 -0.07370 -0.11588 0.06452  352 PHE A CE1 
2922 C CE2 . PHE A 358 ? 0.54304 0.41311 0.32590 -0.06940 -0.04994 0.08236  352 PHE A CE2 
2923 C CZ  . PHE A 358 ? 0.54246 0.38458 0.31310 -0.09157 -0.08856 0.07821  352 PHE A CZ  
2924 N N   . GLN A 359 ? 0.48742 0.46197 0.27187 -0.07902 -0.09849 0.00558  353 GLN A N   
2925 C CA  . GLN A 359 ? 0.54191 0.49742 0.37405 -0.08271 -0.12939 -0.00787 353 GLN A CA  
2926 C C   . GLN A 359 ? 0.61359 0.54932 0.49546 -0.10704 -0.21189 -0.04397 353 GLN A C   
2927 O O   . GLN A 359 ? 0.65880 0.57354 0.57935 -0.14452 -0.20128 -0.08631 353 GLN A O   
2928 C CB  . GLN A 359 ? 0.51681 0.46308 0.32756 -0.05634 -0.06631 0.02648  353 GLN A CB  
2929 C CG  . GLN A 359 ? 0.50268 0.45501 0.31918 -0.06885 -0.03452 0.01303  353 GLN A CG  
2930 C CD  . GLN A 359 ? 0.51844 0.47887 0.30414 -0.07293 -0.06678 0.02211  353 GLN A CD  
2931 O OE1 . GLN A 359 ? 0.56632 0.52229 0.30408 -0.03729 -0.10428 0.01695  353 GLN A OE1 
2932 N NE2 . GLN A 359 ? 0.45105 0.43866 0.24189 -0.14036 -0.10229 -0.00937 353 GLN A NE2 
2933 N N   . PRO A 360 ? 0.64168 0.57938 0.53481 -0.08320 -0.25562 -0.04425 354 PRO A N   
2934 C CA  . PRO A 360 ? 0.66444 0.59377 0.56372 -0.07365 -0.22325 -0.04729 354 PRO A CA  
2935 C C   . PRO A 360 ? 0.70374 0.60086 0.59035 -0.05951 -0.15735 -0.07577 354 PRO A C   
2936 O O   . PRO A 360 ? 0.71781 0.61871 0.64510 -0.05658 -0.11489 -0.05794 354 PRO A O   
2937 C CB  . PRO A 360 ? 0.64367 0.59560 0.52659 -0.05885 -0.27106 -0.01712 354 PRO A CB  
2938 C CG  . PRO A 360 ? 0.62351 0.59117 0.51384 -0.06221 -0.30678 -0.02442 354 PRO A CG  
2939 C CD  . PRO A 360 ? 0.62955 0.58554 0.52613 -0.05628 -0.30174 -0.03017 354 PRO A CD  
2940 S S   A SO4 B .   ? 0.30260 0.42275 0.28965 -0.05378 -0.06140 0.05158  401 SO4 A S   
2941 S S   B SO4 B .   ? 0.46870 0.34047 0.28186 -0.10241 -0.04125 0.07377  401 SO4 A S   
2942 O O1  A SO4 B .   ? 0.37954 0.42903 0.31509 -0.05955 -0.06540 0.03299  401 SO4 A O1  
2943 O O1  B SO4 B .   ? 0.48778 0.33891 0.28788 -0.10760 -0.07360 0.08957  401 SO4 A O1  
2944 O O2  A SO4 B .   ? 0.30447 0.45138 0.30193 -0.06189 -0.01211 0.03335  401 SO4 A O2  
2945 O O2  B SO4 B .   ? 0.44115 0.31761 0.26909 -0.10374 -0.06209 0.09470  401 SO4 A O2  
2946 O O3  A SO4 B .   ? 0.31272 0.42819 0.29585 -0.03229 -0.08642 0.05404  401 SO4 A O3  
2947 O O3  B SO4 B .   ? 0.49892 0.34551 0.30298 -0.07064 -0.00321 0.08783  401 SO4 A O3  
2948 O O4  A SO4 B .   ? 0.25555 0.41656 0.32342 -0.02783 -0.04937 0.12230  401 SO4 A O4  
2949 O O4  B SO4 B .   ? 0.47880 0.34230 0.28135 -0.08808 -0.04396 0.04494  401 SO4 A O4  
2950 S S   . SO4 C .   ? 0.61659 0.75335 0.85228 -0.23586 -0.02919 0.00964  402 SO4 A S   
2951 O O1  . SO4 C .   ? 0.59683 0.75514 0.81055 -0.24697 -0.03481 0.00192  402 SO4 A O1  
2952 O O2  . SO4 C .   ? 0.61425 0.73464 0.84296 -0.23708 -0.06135 0.01398  402 SO4 A O2  
2953 O O3  . SO4 C .   ? 0.60260 0.75339 0.82891 -0.25848 -0.05349 0.01968  402 SO4 A O3  
2954 O O4  . SO4 C .   ? 0.60546 0.74562 0.87185 -0.21192 -0.03036 0.00967  402 SO4 A O4  
2955 C C15 . WM6 D .   ? 0.33892 0.38929 0.41927 -0.04702 -0.08422 0.08468  403 WM6 A C15 
2956 C C1  . WM6 D .   ? 0.31235 0.36640 0.42458 -0.02920 -0.08943 0.06855  403 WM6 A C1  
2957 C C2  . WM6 D .   ? 0.27734 0.33461 0.40151 -0.04845 -0.07663 0.06100  403 WM6 A C2  
2958 C C3  . WM6 D .   ? 0.26426 0.38536 0.32524 0.06097  -0.05845 0.04942  403 WM6 A C3  
2959 C C8  . WM6 D .   ? 0.21893 0.41538 0.29254 0.05062  -0.07321 0.03444  403 WM6 A C8  
2960 C C4  . WM6 D .   ? 0.31489 0.40106 0.35280 0.07797  0.03477  0.02389  403 WM6 A C4  
2961 C C5  . WM6 D .   ? 0.29650 0.41665 0.35579 0.09229  0.05741  0.02521  403 WM6 A C5  
2962 C C6  . WM6 D .   ? 0.27700 0.42589 0.30101 0.06884  0.00079  0.01958  403 WM6 A C6  
2963 C C7  . WM6 D .   ? 0.20386 0.44345 0.27826 0.05551  -0.03889 0.01200  403 WM6 A C7  
2964 C C9  . WM6 D .   ? 0.22913 0.42333 0.27160 0.02451  -0.04254 0.05638  403 WM6 A C9  
2965 C C10 . WM6 D .   ? 0.16494 0.40216 0.28977 0.03611  -0.02790 0.05645  403 WM6 A C10 
2966 C C11 . WM6 D .   ? 0.16056 0.40771 0.27957 0.04275  -0.05178 0.09733  403 WM6 A C11 
2967 C C12 . WM6 D .   ? 0.19872 0.36976 0.32698 0.01315  -0.03290 0.07331  403 WM6 A C12 
2968 C C13 . WM6 D .   ? 0.24785 0.37831 0.34536 -0.03395 -0.03613 0.07597  403 WM6 A C13 
2969 C C14 . WM6 D .   ? 0.33264 0.39587 0.39806 -0.06884 -0.03299 0.07595  403 WM6 A C14 
2970 C C16 . WM6 D .   ? 0.33544 0.38709 0.38046 -0.00399 -0.10971 0.06708  403 WM6 A C16 
2971 O O1  . WM6 D .   ? 0.37913 0.40624 0.45777 0.00442  -0.08184 0.06808  403 WM6 A O1  
2972 O O2  . WM6 D .   ? 0.27179 0.34638 0.34994 -0.00865 -0.03185 0.06871  403 WM6 A O2  
2973 O O3  . WM6 D .   ? 0.30225 0.42638 0.41331 0.08074  0.08230  0.03649  403 WM6 A O3  
2974 O O4  . WM6 D .   ? 0.20232 0.48705 0.28082 0.03652  -0.03551 0.03940  403 WM6 A O4  
2975 O O5  . WM6 D .   ? 0.21534 0.43787 0.26204 0.00901  -0.03868 0.05699  403 WM6 A O5  
2976 O O6  . WM6 D .   ? 0.23037 0.40664 0.27890 0.02791  -0.04831 0.06538  403 WM6 A O6  
2977 O O7  . WM6 D .   ? 0.37364 0.45014 0.43157 -0.11979 -0.00638 0.07425  403 WM6 A O7  
2978 O O8  . WM6 D .   ? 0.32261 0.38288 0.49902 -0.03366 -0.08820 0.08291  403 WM6 A O8  
2979 O O9  . WM6 D .   ? 0.37301 0.38880 0.36577 0.07055  -0.10269 0.05151  403 WM6 A O9  
2980 O O   . HOH E .   ? 0.35986 0.47666 0.60543 0.02180  0.05656  -0.09433 501 HOH A O   
2981 O O   . HOH E .   ? 0.33473 0.30565 0.48516 -0.00176 -0.15192 -0.07351 502 HOH A O   
2982 O O   . HOH E .   ? 0.42085 0.59342 0.68956 -0.12277 0.08311  -0.21914 503 HOH A O   
2983 O O   . HOH E .   ? 0.37091 0.61972 0.43485 -0.07757 -0.09241 0.00642  504 HOH A O   
2984 O O   . HOH E .   ? 0.53682 0.77694 0.45183 0.08144  0.17516  0.27218  505 HOH A O   
2985 O O   . HOH E .   ? 0.55736 0.60022 0.41878 -0.18713 -0.12478 0.06876  506 HOH A O   
2986 O O   . HOH E .   ? 0.52174 0.51588 0.74274 -0.01600 0.17945  -0.00635 507 HOH A O   
2987 O O   . HOH E .   ? 0.30024 0.87282 0.72186 -0.10325 0.04829  -0.13899 508 HOH A O   
2988 O O   . HOH E .   ? 0.35571 0.39032 0.82288 0.14886  -0.04094 -0.12641 509 HOH A O   
2989 O O   . HOH E .   ? 0.34057 0.68078 0.82851 0.05478  -0.06643 -0.30542 510 HOH A O   
2990 O O   . HOH E .   ? 0.49729 0.61112 0.53354 0.01408  0.03013  0.17214  511 HOH A O   
2991 O O   . HOH E .   ? 0.74179 0.89775 0.92863 -0.17073 -0.12294 0.20999  512 HOH A O   
2992 O O   . HOH E .   ? 0.44440 0.56183 0.45816 0.12545  0.03719  -0.05268 513 HOH A O   
2993 O O   . HOH E .   ? 0.39280 0.53326 0.31898 -0.04229 -0.03692 0.02062  514 HOH A O   
2994 O O   . HOH E .   ? 0.66558 0.77411 0.72845 0.23437  -0.14771 0.12504  515 HOH A O   
2995 O O   . HOH E .   ? 0.90058 0.63745 0.49545 -0.14884 0.03734  0.02804  516 HOH A O   
2996 O O   . HOH E .   ? 0.47444 0.31103 0.25589 -0.00722 -0.01101 -0.02870 517 HOH A O   
2997 O O   . HOH E .   ? 0.45728 0.42255 0.27195 0.03180  -0.11718 -0.01114 518 HOH A O   
2998 O O   . HOH E .   ? 0.28144 0.41529 0.47569 -0.05160 -0.01935 -0.07251 519 HOH A O   
2999 O O   . HOH E .   ? 1.09294 0.45294 0.53489 0.18998  0.38532  0.07943  520 HOH A O   
3000 O O   . HOH E .   ? 0.34619 0.53104 0.51157 0.00380  0.05867  -0.06818 521 HOH A O   
3001 O O   . HOH E .   ? 0.76667 0.33485 0.60523 0.09458  -0.11604 -0.05130 522 HOH A O   
3002 O O   . HOH E .   ? 0.51821 0.48026 0.44460 -0.07524 0.04878  -0.03129 523 HOH A O   
3003 O O   . HOH E .   ? 0.38521 0.63490 0.76732 0.13399  0.05479  -0.23436 524 HOH A O   
3004 O O   . HOH E .   ? 0.47551 0.64606 0.52124 0.22617  0.04518  0.16598  525 HOH A O   
3005 O O   . HOH E .   ? 0.48350 0.86782 0.90676 -0.17833 -0.19873 -0.00034 526 HOH A O   
3006 O O   . HOH E .   ? 0.27871 0.44687 0.29948 0.01204  0.01255  0.04982  527 HOH A O   
3007 O O   . HOH E .   ? 1.06920 0.60489 0.56269 0.06988  0.25581  0.24722  528 HOH A O   
3008 O O   . HOH E .   ? 0.48447 0.81228 0.57501 0.32640  0.10344  0.21635  529 HOH A O   
3009 O O   . HOH E .   ? 0.63623 0.41723 1.01645 -0.02460 -0.20524 0.04039  530 HOH A O   
3010 O O   . HOH E .   ? 0.62615 0.44666 0.28619 -0.07999 0.08401  0.03842  531 HOH A O   
3011 O O   . HOH E .   ? 0.26992 0.34708 0.25501 0.01096  -0.02283 0.00902  532 HOH A O   
3012 O O   . HOH E .   ? 0.38733 0.47352 0.36424 0.08635  0.03951  0.03481  533 HOH A O   
3013 O O   . HOH E .   ? 0.31582 0.32300 0.44381 0.01095  0.07334  0.01700  534 HOH A O   
3014 O O   . HOH E .   ? 1.00234 0.65383 0.42830 0.02373  0.02343  0.13618  535 HOH A O   
3015 O O   . HOH E .   ? 0.38025 0.68298 0.41228 -0.05289 -0.12444 0.17864  536 HOH A O   
3016 O O   . HOH E .   ? 0.81134 0.33957 0.56592 0.06867  -0.32588 -0.05644 537 HOH A O   
3017 O O   . HOH E .   ? 0.50974 0.38607 0.49183 0.09722  0.03886  -0.01190 538 HOH A O   
3018 O O   . HOH E .   ? 0.36430 0.37785 0.38310 -0.05371 -0.08309 0.00456  539 HOH A O   
3019 O O   . HOH E .   ? 0.59389 0.46207 0.91712 -0.17372 0.04139  0.25127  540 HOH A O   
3020 O O   . HOH E .   ? 0.88515 0.44327 0.57100 -0.25837 -0.10484 0.14333  541 HOH A O   
3021 O O   . HOH E .   ? 0.68811 1.08900 0.35089 -0.11048 -0.14316 0.13209  542 HOH A O   
3022 O O   . HOH E .   ? 0.29123 0.69545 0.68898 -0.05125 0.09512  -0.26704 543 HOH A O   
3023 O O   . HOH E .   ? 0.77386 0.39214 0.38929 0.03441  -0.06805 0.04596  544 HOH A O   
3024 O O   . HOH E .   ? 0.69301 0.96438 0.44176 0.09149  -0.02198 -0.14212 545 HOH A O   
3025 O O   . HOH E .   ? 0.80387 0.62030 0.88735 0.03498  0.09640  0.41340  546 HOH A O   
3026 O O   . HOH E .   ? 0.37545 0.48746 0.35472 -0.05608 0.00140  -0.06503 547 HOH A O   
3027 O O   . HOH E .   ? 0.27740 0.32741 0.31224 -0.00165 -0.01633 -0.06518 548 HOH A O   
3028 O O   . HOH E .   ? 0.52131 0.78611 0.75855 -0.07683 0.34312  -0.15703 549 HOH A O   
3029 O O   . HOH E .   ? 1.08575 0.31608 0.34186 0.04147  -0.12326 0.03459  550 HOH A O   
3030 O O   . HOH E .   ? 0.50891 0.35458 0.32151 0.10847  -0.12203 0.02014  551 HOH A O   
3031 O O   . HOH E .   ? 0.28784 0.34028 0.20892 0.00216  0.01609  0.03823  552 HOH A O   
3032 O O   . HOH E .   ? 0.29465 0.50103 0.26948 -0.02664 -0.01194 0.02746  553 HOH A O   
3033 O O   . HOH E .   ? 0.27266 0.49523 0.34765 -0.04873 -0.07203 0.06589  554 HOH A O   
3034 O O   . HOH E .   ? 1.05969 0.48399 0.70515 -0.31674 0.31244  -0.13440 555 HOH A O   
3035 O O   . HOH E .   ? 0.46517 1.03834 0.51227 -0.03124 -0.01624 -0.14000 556 HOH A O   
3036 O O   . HOH E .   ? 0.81801 0.36698 0.69128 -0.13937 0.38255  -0.03229 557 HOH A O   
3037 O O   . HOH E .   ? 0.81771 0.50768 0.44276 0.08053  -0.07706 0.04493  558 HOH A O   
3038 O O   . HOH E .   ? 0.68986 0.69969 0.48295 -0.24913 0.13880  -0.03667 559 HOH A O   
3039 O O   . HOH E .   ? 0.44951 0.56965 0.71409 -0.08396 -0.01037 0.32811  560 HOH A O   
3040 O O   . HOH E .   ? 0.54371 0.39919 0.51095 -0.21976 -0.02595 0.02145  561 HOH A O   
3041 O O   . HOH E .   ? 0.53288 0.53006 0.46912 -0.04742 -0.12719 -0.14981 562 HOH A O   
3042 O O   . HOH E .   ? 0.41322 0.29468 0.25679 0.01374  0.02866  -0.01739 563 HOH A O   
3043 O O   . HOH E .   ? 0.41129 0.45406 0.59755 0.02908  0.03741  -0.15231 564 HOH A O   
3044 O O   . HOH E .   ? 0.51231 0.38241 0.26923 0.01558  -0.04037 0.01909  565 HOH A O   
3045 O O   . HOH E .   ? 0.60353 0.35146 0.22238 -0.01445 -0.09880 0.01111  566 HOH A O   
3046 O O   . HOH E .   ? 0.37187 0.48253 0.35070 -0.00732 -0.00891 -0.00335 567 HOH A O   
3047 O O   . HOH E .   ? 0.37914 0.87880 0.51697 0.12542  -0.08638 -0.12160 568 HOH A O   
3048 O O   . HOH E .   ? 0.53866 0.68209 0.55579 -0.07699 0.11046  0.10839  569 HOH A O   
3049 O O   . HOH E .   ? 0.48761 0.41590 0.40008 -0.05043 -0.07763 0.03288  570 HOH A O   
3050 O O   . HOH E .   ? 0.29731 0.36840 0.23752 -0.07927 -0.05375 0.01325  571 HOH A O   
3051 O O   . HOH E .   ? 0.48184 0.37299 0.44052 0.03889  0.04424  0.10678  572 HOH A O   
3052 O O   . HOH E .   ? 0.85432 0.66839 0.31472 -0.17310 -0.13294 -0.04062 573 HOH A O   
3053 O O   . HOH E .   ? 0.44274 0.45281 0.70024 0.11418  0.18485  0.15353  574 HOH A O   
3054 O O   . HOH E .   ? 0.53009 1.05169 0.59493 -0.31511 0.19781  -0.13026 575 HOH A O   
3055 O O   . HOH E .   ? 0.60475 0.92684 0.63540 0.05208  0.02446  0.06004  576 HOH A O   
3056 O O   . HOH E .   ? 0.33263 0.35860 0.31490 -0.02894 0.01150  -0.00233 577 HOH A O   
3057 O O   . HOH E .   ? 0.30400 0.48631 0.23537 0.01346  -0.06476 -0.07547 578 HOH A O   
3058 O O   . HOH E .   ? 0.37574 0.35103 0.33197 -0.04923 0.03318  0.06240  579 HOH A O   
3059 O O   . HOH E .   ? 0.45320 0.74533 0.68001 -0.16555 -0.00623 0.04868  580 HOH A O   
3060 O O   . HOH E .   ? 0.49722 0.55488 0.44439 -0.11578 0.03129  0.05494  581 HOH A O   
3061 O O   . HOH E .   ? 0.22023 0.35794 0.66447 -0.07261 0.06689  -0.06674 582 HOH A O   
3062 O O   . HOH E .   ? 1.03090 0.47794 0.47498 -0.12913 -0.25542 0.12580  583 HOH A O   
3063 O O   . HOH E .   ? 0.26002 0.29246 0.22614 -0.00265 -0.02549 0.00993  584 HOH A O   
3064 O O   . HOH E .   ? 0.68647 0.63994 0.66213 0.12037  0.27014  -0.15448 585 HOH A O   
3065 O O   . HOH E .   ? 0.44991 0.55903 0.75873 -0.12446 -0.22870 0.09447  586 HOH A O   
3066 O O   . HOH E .   ? 0.29964 0.81203 0.44828 0.02022  -0.01156 -0.03445 587 HOH A O   
3067 O O   . HOH E .   ? 0.44613 0.85323 0.62736 -0.03780 0.14876  0.15007  588 HOH A O   
3068 O O   . HOH E .   ? 0.30083 0.53321 0.40594 0.00448  -0.14138 0.03401  589 HOH A O   
3069 O O   . HOH E .   ? 0.47890 0.42148 0.42222 -0.03154 0.01975  0.06578  590 HOH A O   
3070 O O   . HOH E .   ? 0.68318 0.32253 0.47381 -0.05934 -0.00882 -0.00008 591 HOH A O   
3071 O O   . HOH E .   ? 0.21731 0.25395 0.23742 0.02029  -0.00645 0.03299  592 HOH A O   
3072 O O   . HOH E .   ? 0.19975 0.26887 0.21574 0.01773  -0.03464 0.01289  593 HOH A O   
3073 O O   . HOH E .   ? 0.50355 0.22495 0.34330 -0.02331 -0.05012 0.02619  594 HOH A O   
3074 O O   . HOH E .   ? 0.45537 0.65944 0.91824 -0.01331 -0.02440 0.45453  595 HOH A O   
3075 O O   . HOH E .   ? 0.80005 0.37043 0.41024 -0.02898 0.08653  0.12356  596 HOH A O   
3076 O O   . HOH E .   ? 0.46920 0.42071 0.46785 0.03226  0.12228  -0.06472 597 HOH A O   
3077 O O   . HOH E .   ? 0.39957 0.79350 0.94039 0.16818  -0.06364 -0.23750 598 HOH A O   
3078 O O   . HOH E .   ? 0.40492 0.80264 0.33050 0.02420  -0.00386 -0.08246 599 HOH A O   
3079 O O   . HOH E .   ? 0.36034 0.70461 0.27381 -0.02360 -0.07721 -0.07749 600 HOH A O   
3080 O O   . HOH E .   ? 0.47499 0.51452 0.59642 -0.02808 0.02788  -0.08706 601 HOH A O   
3081 O O   . HOH E .   ? 0.33743 0.45631 0.64487 0.12266  0.11583  -0.03156 602 HOH A O   
3082 O O   . HOH E .   ? 0.49177 0.38971 0.47654 -0.11827 -0.12855 0.05060  603 HOH A O   
3083 O O   . HOH E .   ? 0.25797 0.51724 0.42666 -0.00341 -0.04896 -0.03727 604 HOH A O   
3084 O O   . HOH E .   ? 0.57037 0.50920 0.36352 0.01452  -0.04194 0.01528  605 HOH A O   
3085 O O   . HOH E .   ? 0.57836 0.63085 0.39611 0.13088  -0.02906 0.01008  606 HOH A O   
3086 O O   . HOH E .   ? 0.74133 0.73108 0.55462 0.16124  -0.13079 -0.12854 607 HOH A O   
3087 O O   . HOH E .   ? 0.40459 0.39431 0.81039 0.04104  0.02196  0.15965  608 HOH A O   
3088 O O   . HOH E .   ? 0.18035 0.23837 0.22279 0.01056  0.00252  0.00995  609 HOH A O   
3089 O O   . HOH E .   ? 0.53247 0.81782 0.41602 -0.31089 -0.18165 0.18764  610 HOH A O   
3090 O O   . HOH E .   ? 0.59919 0.73152 0.84734 0.08928  0.06054  0.46425  611 HOH A O   
3091 O O   . HOH E .   ? 0.27308 0.58143 0.23825 0.06858  0.03975  0.14871  612 HOH A O   
3092 O O   . HOH E .   ? 0.43601 0.40600 0.76260 0.15129  -0.01239 -0.06631 613 HOH A O   
3093 O O   . HOH E .   ? 0.46463 0.90064 0.42261 -0.13701 0.08844  -0.15483 614 HOH A O   
3094 O O   . HOH E .   ? 0.37216 0.79572 0.65364 0.14920  0.05926  0.27968  615 HOH A O   
3095 O O   . HOH E .   ? 0.21815 0.22115 0.35265 0.00422  0.02875  0.01886  616 HOH A O   
3096 O O   . HOH E .   ? 0.31801 0.39692 0.27736 0.00584  0.02460  0.04152  617 HOH A O   
3097 O O   . HOH E .   ? 0.81344 0.77635 0.75438 0.21773  0.03839  -0.04715 618 HOH A O   
3098 O O   . HOH E .   ? 0.60923 0.46054 0.30678 0.13915  0.13536  0.03485  619 HOH A O   
3099 O O   . HOH E .   ? 0.24884 0.33123 0.33314 -0.03031 -0.01370 -0.04826 620 HOH A O   
3100 O O   . HOH E .   ? 0.73894 0.37136 0.95225 0.05199  0.06178  0.10065  621 HOH A O   
3101 O O   . HOH E .   ? 0.25994 0.29985 0.21604 -0.03983 -0.02529 0.02327  622 HOH A O   
3102 O O   . HOH E .   ? 0.29777 0.53012 0.28828 0.10031  0.03947  0.09004  623 HOH A O   
3103 O O   . HOH E .   ? 0.30910 0.29074 0.23963 0.00101  -0.06351 -0.01496 624 HOH A O   
3104 O O   . HOH E .   ? 0.34644 0.32587 0.29378 -0.07397 -0.03649 0.04623  625 HOH A O   
3105 O O   . HOH E .   ? 0.23418 0.26942 0.25068 -0.06129 -0.00141 0.01534  626 HOH A O   
3106 O O   . HOH E .   ? 0.37194 0.21344 0.25755 0.02150  -0.04187 -0.01785 627 HOH A O   
3107 O O   . HOH E .   ? 0.83371 0.58407 0.57267 -0.12636 0.28717  -0.12562 628 HOH A O   
3108 O O   . HOH E .   ? 0.41794 1.07753 0.52017 0.10229  -0.13461 0.06593  629 HOH A O   
3109 O O   . HOH E .   ? 1.17850 0.75719 0.37905 0.46928  0.06006  0.01763  630 HOH A O   
3110 O O   . HOH E .   ? 0.17328 0.23641 0.29978 -0.01137 -0.05268 -0.02648 631 HOH A O   
3111 O O   . HOH E .   ? 0.64418 0.76165 0.52010 0.00944  0.27758  -0.20759 632 HOH A O   
3112 O O   . HOH E .   ? 0.50201 0.70274 0.42383 0.03209  0.05177  0.18996  633 HOH A O   
3113 O O   . HOH E .   ? 0.30733 0.48288 0.25199 -0.02872 -0.03169 0.04561  634 HOH A O   
3114 O O   . HOH E .   ? 0.43089 0.96134 0.44244 -0.22587 -0.11620 0.07338  635 HOH A O   
3115 O O   . HOH E .   ? 0.45101 0.53841 0.31475 -0.04186 -0.03589 -0.04115 636 HOH A O   
3116 O O   A HOH E .   ? 0.34339 0.32273 0.47792 -0.16753 -0.12909 0.05436  637 HOH A O   
3117 O O   B HOH E .   ? 0.69247 0.60164 0.24927 -0.18472 -0.10633 0.09055  637 HOH A O   
3118 O O   . HOH E .   ? 0.82771 0.34253 0.50940 0.07406  -0.05391 -0.01076 638 HOH A O   
3119 O O   . HOH E .   ? 0.85327 0.34312 0.42897 0.00557  0.16465  0.03718  639 HOH A O   
3120 O O   . HOH E .   ? 0.54118 0.84838 0.69987 0.32507  -0.03238 0.17453  640 HOH A O   
3121 O O   . HOH E .   ? 0.58724 1.02013 0.64060 0.38503  -0.19041 -0.14819 641 HOH A O   
3122 O O   . HOH E .   ? 0.55163 0.63905 0.62760 0.05363  -0.08225 -0.11980 642 HOH A O   
3123 O O   . HOH E .   ? 0.41830 0.48505 0.46400 0.00827  0.02859  -0.10200 643 HOH A O   
3124 O O   . HOH E .   ? 0.62905 0.58605 0.39496 -0.18824 0.14095  -0.00369 644 HOH A O   
3125 O O   . HOH E .   ? 0.42799 0.42453 0.21000 -0.04739 -0.05035 0.04108  645 HOH A O   
3126 O O   . HOH E .   ? 0.24999 0.41842 0.37275 -0.03245 -0.05639 -0.02520 646 HOH A O   
3127 O O   . HOH E .   ? 0.60673 0.69549 0.45548 0.11556  -0.08765 0.15606  647 HOH A O   
3128 O O   . HOH E .   ? 0.39327 0.57779 0.37519 0.06074  -0.00893 -0.05915 648 HOH A O   
3129 O O   . HOH E .   ? 0.19179 0.23643 0.22508 -0.01337 -0.03241 0.00572  649 HOH A O   
3130 O O   . HOH E .   ? 0.51422 0.45567 0.30340 -0.00312 -0.13717 0.10390  650 HOH A O   
3131 O O   . HOH E .   ? 0.40500 0.30658 0.52107 -0.03533 -0.09913 0.11109  651 HOH A O   
3132 O O   . HOH E .   ? 0.88753 0.50573 0.58596 -0.13714 0.06929  -0.19745 652 HOH A O   
3133 O O   . HOH E .   ? 0.72091 0.59553 0.80414 0.02290  -0.16349 -0.10920 653 HOH A O   
3134 O O   . HOH E .   ? 0.50676 0.53477 0.45649 -0.03368 0.20291  -0.08821 654 HOH A O   
3135 O O   . HOH E .   ? 0.60060 0.56975 0.63035 -0.05579 -0.08351 0.30569  655 HOH A O   
3136 O O   . HOH E .   ? 0.71362 0.46707 0.37218 -0.12577 -0.09766 -0.02803 656 HOH A O   
3137 O O   . HOH E .   ? 0.47990 1.05585 0.60890 -0.03542 -0.11515 -0.29943 657 HOH A O   
3138 O O   . HOH E .   ? 0.53387 0.85192 0.32022 -0.16867 -0.13993 0.09779  658 HOH A O   
3139 O O   . HOH E .   ? 0.53355 0.96700 0.74830 0.05691  0.19374  0.38062  659 HOH A O   
3140 O O   . HOH E .   ? 0.40725 0.88265 0.41181 -0.17273 0.02960  0.07594  660 HOH A O   
3141 O O   . HOH E .   ? 0.46532 0.77696 0.36775 0.00433  0.19319  0.11145  661 HOH A O   
3142 O O   . HOH E .   ? 0.40818 0.30563 0.87394 -0.06167 0.28663  -0.15052 662 HOH A O   
3143 O O   . HOH E .   ? 0.72977 0.82876 0.48364 0.42129  0.17290  0.24949  663 HOH A O   
3144 O O   . HOH E .   ? 0.37102 0.28467 0.34108 0.00344  0.01442  0.01791  664 HOH A O   
3145 O O   . HOH E .   ? 0.53107 0.58610 0.39359 0.15674  0.13158  -0.04297 665 HOH A O   
3146 O O   . HOH E .   ? 0.27740 0.27547 0.39169 0.02440  0.00715  -0.02446 666 HOH A O   
3147 O O   . HOH E .   ? 0.44251 0.59972 0.38811 -0.14090 -0.07574 0.08685  667 HOH A O   
3148 O O   . HOH E .   ? 0.23276 0.20777 0.35813 -0.00540 0.01470  -0.02948 668 HOH A O   
3149 O O   . HOH E .   ? 0.62609 0.92657 0.68487 0.36223  -0.03647 0.23611  669 HOH A O   
3150 O O   . HOH E .   ? 0.53381 0.79448 0.64834 -0.12554 -0.01650 -0.08362 670 HOH A O   
3151 O O   . HOH E .   ? 0.64242 0.61824 0.73294 -0.13168 0.00666  0.25552  671 HOH A O   
3152 O O   . HOH E .   ? 0.25774 0.51700 0.52889 -0.00040 -0.10077 0.11140  672 HOH A O   
3153 O O   . HOH E .   ? 0.37085 0.79860 0.68116 0.01220  0.27263  0.01474  673 HOH A O   
3154 O O   . HOH E .   ? 0.26346 0.46498 0.37371 -0.03905 0.01991  -0.02557 674 HOH A O   
3155 O O   . HOH E .   ? 0.39016 0.51150 0.34195 0.04858  0.01566  -0.00095 675 HOH A O   
3156 O O   . HOH E .   ? 0.39675 0.44930 0.35743 0.03009  -0.06067 0.08870  676 HOH A O   
3157 O O   . HOH E .   ? 0.48125 0.37453 1.14128 -0.04677 -0.20337 -0.05494 677 HOH A O   
3158 O O   . HOH E .   ? 0.86077 0.58121 0.55882 0.04316  0.12314  -0.13584 678 HOH A O   
3159 O O   . HOH E .   ? 1.02337 0.66113 0.55288 -0.12635 -0.29541 0.11603  679 HOH A O   
3160 O O   . HOH E .   ? 0.62117 0.43358 0.59088 -0.03803 -0.05065 0.17350  680 HOH A O   
3161 O O   . HOH E .   ? 0.59658 0.82144 0.76558 -0.30353 -0.30515 0.18127  681 HOH A O   
3162 O O   . HOH E .   ? 0.71830 0.89815 0.43841 0.12677  0.04764  0.22040  682 HOH A O   
3163 O O   . HOH E .   ? 0.37931 0.49964 0.28238 0.23975  0.11860  0.15541  683 HOH A O   
3164 O O   . HOH E .   ? 1.14480 0.65222 0.49447 -0.13953 0.21971  0.16631  684 HOH A O   
3165 O O   . HOH E .   ? 0.42570 0.42929 0.58733 0.05013  -0.06706 0.03946  685 HOH A O   
3166 O O   . HOH E .   ? 0.23425 0.35403 0.43508 0.06531  -0.01955 -0.08452 686 HOH A O   
3167 O O   . HOH E .   ? 0.33982 0.96295 0.64124 -0.07888 0.01825  0.25772  687 HOH A O   
3168 O O   . HOH E .   ? 0.61547 0.45474 0.41420 -0.10189 0.28302  -0.07602 688 HOH A O   
3169 O O   . HOH E .   ? 0.49919 0.46816 0.41025 0.06220  -0.10020 -0.02920 689 HOH A O   
3170 O O   . HOH E .   ? 0.43007 1.08223 0.63291 -0.05660 0.20806  0.13750  690 HOH A O   
3171 O O   . HOH E .   ? 0.44453 0.67702 0.47669 -0.24019 0.12348  -0.21062 691 HOH A O   
3172 O O   . HOH E .   ? 1.02095 0.46388 0.36699 0.32022  -0.17233 -0.09636 692 HOH A O   
3173 O O   . HOH E .   ? 0.62688 0.79171 0.68451 0.13307  -0.22600 0.02979  693 HOH A O   
3174 O O   . HOH E .   ? 0.90522 0.92906 0.40108 0.50120  -0.07554 -0.11473 694 HOH A O   
3175 O O   . HOH E .   ? 0.51033 0.58129 0.70551 -0.00991 0.29313  0.15635  695 HOH A O   
3176 O O   . HOH E .   ? 1.08278 0.56343 0.39403 0.01091  0.02328  0.10067  696 HOH A O   
3177 O O   . HOH E .   ? 0.41694 0.66644 0.59656 -0.13244 0.10563  -0.07301 697 HOH A O   
3178 O O   . HOH E .   ? 0.89415 0.78104 0.62997 0.13963  0.09879  0.15803  698 HOH A O   
3179 O O   . HOH E .   ? 0.77453 0.62078 0.80303 0.02019  -0.18026 0.37778  699 HOH A O   
3180 O O   . HOH E .   ? 0.60871 0.85605 0.54744 -0.01257 0.00130  -0.07568 700 HOH A O   
3181 O O   . HOH E .   ? 0.57368 0.71893 0.79074 0.01433  -0.07649 0.18064  701 HOH A O   
3182 O O   . HOH E .   ? 0.45301 0.64439 0.38006 -0.18062 -0.08827 0.10029  702 HOH A O   
3183 O O   . HOH E .   ? 0.53840 0.69621 0.63616 -0.11756 -0.25714 0.06830  703 HOH A O   
3184 O O   . HOH E .   ? 0.51141 0.91799 0.77816 -0.31514 0.17036  -0.27413 704 HOH A O   
3185 O O   . HOH E .   ? 0.23180 0.29573 0.30590 0.05028  0.00302  -0.00430 705 HOH A O   
3186 O O   . HOH E .   ? 0.80230 0.76225 0.84884 -0.16840 -0.16758 0.00436  706 HOH A O   
3187 O O   . HOH E .   ? 0.56910 1.13879 0.43214 -0.11540 -0.05550 0.24893  707 HOH A O   
3188 O O   . HOH E .   ? 0.54950 0.96533 0.66403 0.19231  0.05898  -0.09913 708 HOH A O   
3189 O O   . HOH E .   ? 0.53544 0.85406 0.50137 0.34569  -0.14158 -0.05642 709 HOH A O   
3190 O O   . HOH E .   ? 0.30717 0.84025 0.37089 0.10661  -0.10549 0.00575  710 HOH A O   
3191 O O   . HOH E .   ? 1.23414 0.84785 0.46088 0.13498  0.19634  0.22599  711 HOH A O   
3192 O O   . HOH E .   ? 0.19937 0.36152 0.24161 -0.04171 -0.00223 0.01737  712 HOH A O   
3193 O O   . HOH E .   ? 0.37802 0.63556 0.42299 -0.01227 -0.09486 -0.04748 713 HOH A O   
3194 O O   . HOH E .   ? 0.58919 0.48479 0.85218 0.15469  -0.02825 -0.18106 714 HOH A O   
3195 O O   . HOH E .   ? 0.44489 0.53851 0.75630 0.04104  -0.22579 0.08943  715 HOH A O   
3196 O O   . HOH E .   ? 1.12854 0.60254 0.45167 0.03750  0.05396  0.09879  716 HOH A O   
3197 O O   . HOH E .   ? 0.69371 0.77699 0.56638 -0.04341 0.25478  -0.07721 717 HOH A O   
3198 O O   . HOH E .   ? 0.47131 0.76925 0.49033 0.15428  -0.00169 0.00616  718 HOH A O   
3199 O O   . HOH E .   ? 0.89344 0.47734 0.79881 0.03769  -0.03251 -0.29246 719 HOH A O   
3200 O O   . HOH E .   ? 0.46187 1.05912 0.63541 -0.06108 -0.19178 0.19729  720 HOH A O   
3201 O O   . HOH E .   ? 0.56936 0.35615 0.31499 -0.10293 0.07147  0.02786  721 HOH A O   
3202 O O   . HOH E .   ? 0.81113 0.89605 0.50378 -0.32233 -0.26845 0.06030  722 HOH A O   
3203 O O   . HOH E .   ? 0.95885 0.48339 0.85239 -0.19997 0.11794  0.05856  723 HOH A O   
3204 O O   . HOH E .   ? 0.57398 0.44861 0.74649 -0.06078 -0.17811 0.12441  724 HOH A O   
3205 O O   . HOH E .   ? 0.74942 0.49420 0.81678 0.03566  0.05370  -0.25050 725 HOH A O   
3206 O O   . HOH E .   ? 0.85718 0.45679 0.49359 -0.17459 0.27669  -0.04011 726 HOH A O   
3207 O O   . HOH E .   ? 0.46690 0.73364 0.24849 0.00517  0.04437  0.07724  727 HOH A O   
3208 O O   . HOH E .   ? 0.72996 0.58169 0.38180 -0.01266 0.14509  -0.05719 728 HOH A O   
3209 O O   . HOH E .   ? 0.51427 0.80766 0.45943 -0.01507 -0.11303 0.00123  729 HOH A O   
3210 O O   . HOH E .   ? 0.86007 0.55759 0.65977 -0.03606 -0.27565 -0.10934 730 HOH A O   
3211 O O   . HOH E .   ? 1.07710 0.42579 0.56324 -0.18078 0.03706  0.16031  731 HOH A O   
3212 O O   . HOH E .   ? 0.61877 0.55938 0.92747 -0.25496 -0.29974 0.24669  732 HOH A O   
3213 O O   . HOH E .   ? 0.97316 0.54723 0.88942 0.04978  0.44868  -0.06031 733 HOH A O   
3214 O O   . HOH E .   ? 0.52644 0.79510 0.57006 -0.05555 -0.16410 -0.20302 734 HOH A O   
3215 O O   . HOH E .   ? 1.06066 0.53425 0.40283 0.04835  0.16451  0.15607  735 HOH A O   
3216 O O   . HOH E .   ? 0.45893 0.42477 0.30949 0.00009  -0.08086 -0.01248 736 HOH A O   
3217 O O   . HOH E .   ? 0.31438 0.51935 0.41878 -0.09973 -0.04471 -0.03527 737 HOH A O   
3218 O O   . HOH E .   ? 0.62076 0.59199 0.56228 -0.15048 0.20267  0.03546  738 HOH A O   
3219 O O   . HOH E .   ? 0.44966 0.44036 0.86456 0.00301  -0.09274 -0.11319 739 HOH A O   
3220 O O   . HOH E .   ? 0.52012 0.55786 0.49611 0.11731  0.08756  0.04572  740 HOH A O   
3221 O O   . HOH E .   ? 0.74353 0.54582 0.52111 -0.21831 -0.11567 0.16719  741 HOH A O   
3222 O O   . HOH E .   ? 0.86113 0.56572 0.37508 -0.11816 -0.00922 -0.09161 742 HOH A O   
3223 O O   . HOH E .   ? 0.77145 0.69839 0.54966 0.01147  -0.12769 -0.03485 743 HOH A O   
3224 O O   . HOH E .   ? 0.48282 0.74519 0.63536 0.07255  0.02835  0.00152  744 HOH A O   
3225 O O   . HOH E .   ? 0.79856 0.74969 0.72912 0.41773  0.26503  0.13733  745 HOH A O   
3226 O O   . HOH E .   ? 0.40230 0.80652 0.69778 0.10718  0.01550  0.18936  746 HOH A O   
3227 O O   . HOH E .   ? 0.52133 0.70349 0.49522 0.16561  0.16690  0.02418  747 HOH A O   
3228 O O   . HOH E .   ? 0.41063 0.35551 0.78501 0.03697  -0.00992 0.11893  748 HOH A O   
3229 O O   . HOH E .   ? 0.99904 0.78409 0.47399 0.18356  -0.15515 0.11634  749 HOH A O   
3230 O O   . HOH E .   ? 0.80266 0.71901 0.36861 0.34742  0.02272  -0.10894 750 HOH A O   
3231 O O   . HOH E .   ? 1.04975 0.75659 0.60593 -0.00853 0.03637  0.10159  751 HOH A O   
3232 O O   . HOH E .   ? 0.83935 0.60873 0.73637 -0.08890 0.35905  0.03547  752 HOH A O   
3233 O O   . HOH E .   ? 0.61105 0.69463 0.64700 -0.06897 -0.10442 0.12164  753 HOH A O   
3234 O O   . HOH E .   ? 0.62151 0.74023 0.50269 -0.11965 0.03499  0.19666  754 HOH A O   
3235 O O   . HOH E .   ? 0.87165 0.54500 0.84594 0.11147  -0.13494 0.07224  755 HOH A O   
# 
