data_8QR8
# 
_entry.id   8QR8 
# 
_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   8QR8         pdb_00008qr8 10.2210/pdb8qr8/pdb 
WWPDB D_1292133719 ?            ?                   
# 
_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                        8QR8 
_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~{S},9~{S},10~{S})-4-methyl-9,10,17,19-tetrakis(oxidanyl)-3-oxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-2,8-dione' 366.406   
1   ? ? ? ? 
4 water       nat water 18.015    314 ? ? ? ? 
# 
_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~{S},9~{S},10~{S})-4-methyl-9,10,17,19-tetrakis(oxidanyl)-3-oxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-2,8-dione' WN2 
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 
WN2 non-polymer         . 
'(4~{S},9~{S},10~{S})-4-methyl-9,10,17,19-tetrakis(oxidanyl)-3-oxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-2,8-dione' ? 
'C19 H26 O7'     366.406 
# 
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 340 334 334 ASP ASP 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        WN2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WN2 
_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 WN2 1   403 1   WN2 509 A . 
E 4 HOH 1   501 365 HOH HOH A . 
E 4 HOH 2   502 259 HOH HOH A . 
E 4 HOH 3   503 163 HOH HOH A . 
E 4 HOH 4   504 141 HOH HOH A . 
E 4 HOH 5   505 145 HOH HOH A . 
E 4 HOH 6   506 160 HOH HOH A . 
E 4 HOH 7   507 69  HOH HOH A . 
E 4 HOH 8   508 147 HOH HOH A . 
E 4 HOH 9   509 290 HOH HOH A . 
E 4 HOH 10  510 28  HOH HOH A . 
E 4 HOH 11  511 40  HOH HOH A . 
E 4 HOH 12  512 88  HOH HOH A . 
E 4 HOH 13  513 133 HOH HOH A . 
E 4 HOH 14  514 86  HOH HOH A . 
E 4 HOH 15  515 98  HOH HOH A . 
E 4 HOH 16  516 239 HOH HOH A . 
E 4 HOH 17  517 267 HOH HOH A . 
E 4 HOH 18  518 220 HOH HOH A . 
E 4 HOH 19  519 85  HOH HOH A . 
E 4 HOH 20  520 180 HOH HOH A . 
E 4 HOH 21  521 9   HOH HOH A . 
E 4 HOH 22  522 289 HOH HOH A . 
E 4 HOH 23  523 205 HOH HOH A . 
E 4 HOH 24  524 216 HOH HOH A . 
E 4 HOH 25  525 202 HOH HOH A . 
E 4 HOH 26  526 131 HOH HOH A . 
E 4 HOH 27  527 203 HOH HOH A . 
E 4 HOH 28  528 411 HOH HOH A . 
E 4 HOH 29  529 236 HOH HOH A . 
E 4 HOH 30  530 77  HOH HOH A . 
E 4 HOH 31  531 105 HOH HOH A . 
E 4 HOH 32  532 412 HOH HOH A . 
E 4 HOH 33  533 138 HOH HOH A . 
E 4 HOH 34  534 6   HOH HOH A . 
E 4 HOH 35  535 237 HOH HOH A . 
E 4 HOH 36  536 161 HOH HOH A . 
E 4 HOH 37  537 358 HOH HOH A . 
E 4 HOH 38  538 100 HOH HOH A . 
E 4 HOH 39  539 401 HOH HOH A . 
E 4 HOH 40  540 437 HOH HOH A . 
E 4 HOH 41  541 142 HOH HOH A . 
E 4 HOH 42  542 46  HOH HOH A . 
E 4 HOH 43  543 41  HOH HOH A . 
E 4 HOH 44  544 14  HOH HOH A . 
E 4 HOH 45  545 24  HOH HOH A . 
E 4 HOH 46  546 132 HOH HOH A . 
E 4 HOH 47  547 54  HOH HOH A . 
E 4 HOH 48  548 379 HOH HOH A . 
E 4 HOH 49  549 66  HOH HOH A . 
E 4 HOH 50  550 316 HOH HOH A . 
E 4 HOH 51  551 51  HOH HOH A . 
E 4 HOH 52  552 226 HOH HOH A . 
E 4 HOH 53  553 136 HOH HOH A . 
E 4 HOH 54  554 113 HOH HOH A . 
E 4 HOH 55  555 170 HOH HOH A . 
E 4 HOH 56  556 84  HOH HOH A . 
E 4 HOH 57  557 217 HOH HOH A . 
E 4 HOH 58  558 43  HOH HOH A . 
E 4 HOH 59  559 53  HOH HOH A . 
E 4 HOH 60  560 25  HOH HOH A . 
E 4 HOH 61  561 230 HOH HOH A . 
E 4 HOH 62  562 256 HOH HOH A . 
E 4 HOH 63  563 59  HOH HOH A . 
E 4 HOH 64  564 49  HOH HOH A . 
E 4 HOH 65  565 251 HOH HOH A . 
E 4 HOH 66  566 168 HOH HOH A . 
E 4 HOH 67  567 102 HOH HOH A . 
E 4 HOH 68  568 191 HOH HOH A . 
E 4 HOH 69  569 71  HOH HOH A . 
E 4 HOH 70  570 95  HOH HOH A . 
E 4 HOH 71  571 22  HOH HOH A . 
E 4 HOH 72  572 210 HOH HOH A . 
E 4 HOH 73  573 79  HOH HOH A . 
E 4 HOH 74  574 80  HOH HOH A . 
E 4 HOH 75  575 11  HOH HOH A . 
E 4 HOH 76  576 47  HOH HOH A . 
E 4 HOH 77  577 293 HOH HOH A . 
E 4 HOH 78  578 108 HOH HOH A . 
E 4 HOH 79  579 221 HOH HOH A . 
E 4 HOH 80  580 50  HOH HOH A . 
E 4 HOH 81  581 29  HOH HOH A . 
E 4 HOH 82  582 153 HOH HOH A . 
E 4 HOH 83  583 15  HOH HOH A . 
E 4 HOH 84  584 235 HOH HOH A . 
E 4 HOH 85  585 8   HOH HOH A . 
E 4 HOH 86  586 78  HOH HOH A . 
E 4 HOH 87  587 3   HOH HOH A . 
E 4 HOH 88  588 74  HOH HOH A . 
E 4 HOH 89  589 2   HOH HOH A . 
E 4 HOH 90  590 157 HOH HOH A . 
E 4 HOH 91  591 30  HOH HOH A . 
E 4 HOH 92  592 122 HOH HOH A . 
E 4 HOH 93  593 4   HOH HOH A . 
E 4 HOH 94  594 35  HOH HOH A . 
E 4 HOH 95  595 232 HOH HOH A . 
E 4 HOH 96  596 127 HOH HOH A . 
E 4 HOH 97  597 175 HOH HOH A . 
E 4 HOH 98  598 90  HOH HOH A . 
E 4 HOH 99  599 399 HOH HOH A . 
E 4 HOH 100 600 130 HOH HOH A . 
E 4 HOH 101 601 10  HOH HOH A . 
E 4 HOH 102 602 229 HOH HOH A . 
E 4 HOH 103 603 129 HOH HOH A . 
E 4 HOH 104 604 101 HOH HOH A . 
E 4 HOH 105 605 18  HOH HOH A . 
E 4 HOH 106 606 117 HOH HOH A . 
E 4 HOH 107 607 12  HOH HOH A . 
E 4 HOH 108 608 23  HOH HOH A . 
E 4 HOH 109 609 422 HOH HOH A . 
E 4 HOH 110 610 185 HOH HOH A . 
E 4 HOH 111 611 355 HOH HOH A . 
E 4 HOH 112 612 31  HOH HOH A . 
E 4 HOH 113 613 91  HOH HOH A . 
E 4 HOH 114 614 192 HOH HOH A . 
E 4 HOH 115 615 82  HOH HOH A . 
E 4 HOH 116 616 38  HOH HOH A . 
E 4 HOH 117 617 33  HOH HOH A . 
E 4 HOH 118 618 1   HOH HOH A . 
E 4 HOH 119 619 223 HOH HOH A . 
E 4 HOH 120 620 73  HOH HOH A . 
E 4 HOH 121 621 159 HOH HOH A . 
E 4 HOH 122 622 310 HOH HOH A . 
E 4 HOH 123 623 265 HOH HOH A . 
E 4 HOH 124 624 240 HOH HOH A . 
E 4 HOH 125 625 32  HOH HOH A . 
E 4 HOH 126 626 234 HOH HOH A . 
E 4 HOH 127 627 249 HOH HOH A . 
E 4 HOH 128 628 277 HOH HOH A . 
E 4 HOH 129 629 97  HOH HOH A . 
E 4 HOH 130 630 164 HOH HOH A . 
E 4 HOH 131 631 278 HOH HOH A . 
E 4 HOH 132 632 39  HOH HOH A . 
E 4 HOH 133 633 115 HOH HOH A . 
E 4 HOH 134 634 173 HOH HOH A . 
E 4 HOH 135 635 93  HOH HOH A . 
E 4 HOH 136 636 87  HOH HOH A . 
E 4 HOH 137 637 45  HOH HOH A . 
E 4 HOH 138 638 252 HOH HOH A . 
E 4 HOH 139 639 20  HOH HOH A . 
E 4 HOH 140 640 5   HOH HOH A . 
E 4 HOH 141 641 119 HOH HOH A . 
E 4 HOH 142 642 63  HOH HOH A . 
E 4 HOH 143 643 116 HOH HOH A . 
E 4 HOH 144 644 123 HOH HOH A . 
E 4 HOH 145 645 172 HOH HOH A . 
E 4 HOH 146 646 83  HOH HOH A . 
E 4 HOH 147 647 307 HOH HOH A . 
E 4 HOH 148 648 148 HOH HOH A . 
E 4 HOH 149 649 186 HOH HOH A . 
E 4 HOH 150 650 250 HOH HOH A . 
E 4 HOH 151 651 37  HOH HOH A . 
E 4 HOH 152 652 19  HOH HOH A . 
E 4 HOH 153 653 7   HOH HOH A . 
E 4 HOH 154 654 13  HOH HOH A . 
E 4 HOH 155 655 17  HOH HOH A . 
E 4 HOH 156 656 111 HOH HOH A . 
E 4 HOH 157 657 165 HOH HOH A . 
E 4 HOH 158 658 158 HOH HOH A . 
E 4 HOH 159 659 244 HOH HOH A . 
E 4 HOH 160 660 415 HOH HOH A . 
E 4 HOH 161 661 418 HOH HOH A . 
E 4 HOH 162 662 36  HOH HOH A . 
E 4 HOH 163 663 324 HOH HOH A . 
E 4 HOH 164 664 367 HOH HOH A . 
E 4 HOH 165 665 16  HOH HOH A . 
E 4 HOH 166 666 65  HOH HOH A . 
E 4 HOH 167 667 124 HOH HOH A . 
E 4 HOH 168 668 114 HOH HOH A . 
E 4 HOH 169 669 106 HOH HOH A . 
E 4 HOH 170 670 199 HOH HOH A . 
E 4 HOH 171 671 107 HOH HOH A . 
E 4 HOH 172 672 421 HOH HOH A . 
E 4 HOH 173 673 27  HOH HOH A . 
E 4 HOH 174 674 187 HOH HOH A . 
E 4 HOH 175 675 81  HOH HOH A . 
E 4 HOH 176 676 169 HOH HOH A . 
E 4 HOH 177 677 26  HOH HOH A . 
E 4 HOH 178 678 135 HOH HOH A . 
E 4 HOH 179 679 167 HOH HOH A . 
E 4 HOH 180 680 227 HOH HOH A . 
E 4 HOH 181 681 48  HOH HOH A . 
E 4 HOH 182 682 281 HOH HOH A . 
E 4 HOH 183 683 34  HOH HOH A . 
E 4 HOH 184 684 21  HOH HOH A . 
E 4 HOH 185 685 143 HOH HOH A . 
E 4 HOH 186 686 137 HOH HOH A . 
E 4 HOH 187 687 89  HOH HOH A . 
E 4 HOH 188 688 155 HOH HOH A . 
E 4 HOH 189 689 385 HOH HOH A . 
E 4 HOH 190 690 140 HOH HOH A . 
E 4 HOH 191 691 308 HOH HOH A . 
E 4 HOH 192 692 42  HOH HOH A . 
E 4 HOH 193 693 299 HOH HOH A . 
E 4 HOH 194 694 335 HOH HOH A . 
E 4 HOH 195 695 125 HOH HOH A . 
E 4 HOH 196 696 56  HOH HOH A . 
E 4 HOH 197 697 416 HOH HOH A . 
E 4 HOH 198 698 346 HOH HOH A . 
E 4 HOH 199 699 419 HOH HOH A . 
E 4 HOH 200 700 99  HOH HOH A . 
E 4 HOH 201 701 118 HOH HOH A . 
E 4 HOH 202 702 44  HOH HOH A . 
E 4 HOH 203 703 317 HOH HOH A . 
E 4 HOH 204 704 332 HOH HOH A . 
E 4 HOH 205 705 436 HOH HOH A . 
E 4 HOH 206 706 139 HOH HOH A . 
E 4 HOH 207 707 146 HOH HOH A . 
E 4 HOH 208 708 420 HOH HOH A . 
E 4 HOH 209 709 190 HOH HOH A . 
E 4 HOH 210 710 247 HOH HOH A . 
E 4 HOH 211 711 315 HOH HOH A . 
E 4 HOH 212 712 326 HOH HOH A . 
E 4 HOH 213 713 150 HOH HOH A . 
E 4 HOH 214 714 189 HOH HOH A . 
E 4 HOH 215 715 194 HOH HOH A . 
E 4 HOH 216 716 255 HOH HOH A . 
E 4 HOH 217 717 322 HOH HOH A . 
E 4 HOH 218 718 201 HOH HOH A . 
E 4 HOH 219 719 156 HOH HOH A . 
E 4 HOH 220 720 424 HOH HOH A . 
E 4 HOH 221 721 246 HOH HOH A . 
E 4 HOH 222 722 61  HOH HOH A . 
E 4 HOH 223 723 429 HOH HOH A . 
E 4 HOH 224 724 298 HOH HOH A . 
E 4 HOH 225 725 224 HOH HOH A . 
E 4 HOH 226 726 58  HOH HOH A . 
E 4 HOH 227 727 231 HOH HOH A . 
E 4 HOH 228 728 287 HOH HOH A . 
E 4 HOH 229 729 177 HOH HOH A . 
E 4 HOH 230 730 126 HOH HOH A . 
E 4 HOH 231 731 112 HOH HOH A . 
E 4 HOH 232 732 291 HOH HOH A . 
E 4 HOH 233 733 383 HOH HOH A . 
E 4 HOH 234 734 384 HOH HOH A . 
E 4 HOH 235 735 233 HOH HOH A . 
E 4 HOH 236 736 128 HOH HOH A . 
E 4 HOH 237 737 179 HOH HOH A . 
E 4 HOH 238 738 151 HOH HOH A . 
E 4 HOH 239 739 360 HOH HOH A . 
E 4 HOH 240 740 441 HOH HOH A . 
E 4 HOH 241 741 184 HOH HOH A . 
E 4 HOH 242 742 366 HOH HOH A . 
E 4 HOH 243 743 373 HOH HOH A . 
E 4 HOH 244 744 52  HOH HOH A . 
E 4 HOH 245 745 432 HOH HOH A . 
E 4 HOH 246 746 262 HOH HOH A . 
E 4 HOH 247 747 57  HOH HOH A . 
E 4 HOH 248 748 120 HOH HOH A . 
E 4 HOH 249 749 178 HOH HOH A . 
E 4 HOH 250 750 406 HOH HOH A . 
E 4 HOH 251 751 96  HOH HOH A . 
E 4 HOH 252 752 171 HOH HOH A . 
E 4 HOH 253 753 154 HOH HOH A . 
E 4 HOH 254 754 209 HOH HOH A . 
E 4 HOH 255 755 342 HOH HOH A . 
E 4 HOH 256 756 55  HOH HOH A . 
E 4 HOH 257 757 343 HOH HOH A . 
E 4 HOH 258 758 369 HOH HOH A . 
E 4 HOH 259 759 279 HOH HOH A . 
E 4 HOH 260 760 407 HOH HOH A . 
E 4 HOH 261 761 64  HOH HOH A . 
E 4 HOH 262 762 347 HOH HOH A . 
E 4 HOH 263 763 328 HOH HOH A . 
E 4 HOH 264 764 391 HOH HOH A . 
E 4 HOH 265 765 440 HOH HOH A . 
E 4 HOH 266 766 204 HOH HOH A . 
E 4 HOH 267 767 430 HOH HOH A . 
E 4 HOH 268 768 183 HOH HOH A . 
E 4 HOH 269 769 431 HOH HOH A . 
E 4 HOH 270 770 197 HOH HOH A . 
E 4 HOH 271 771 60  HOH HOH A . 
E 4 HOH 272 772 370 HOH HOH A . 
E 4 HOH 273 773 273 HOH HOH A . 
E 4 HOH 274 774 188 HOH HOH A . 
E 4 HOH 275 775 427 HOH HOH A . 
E 4 HOH 276 776 214 HOH HOH A . 
E 4 HOH 277 777 334 HOH HOH A . 
E 4 HOH 278 778 211 HOH HOH A . 
E 4 HOH 279 779 417 HOH HOH A . 
E 4 HOH 280 780 162 HOH HOH A . 
E 4 HOH 281 781 325 HOH HOH A . 
E 4 HOH 282 782 309 HOH HOH A . 
E 4 HOH 283 783 435 HOH HOH A . 
E 4 HOH 284 784 103 HOH HOH A . 
E 4 HOH 285 785 198 HOH HOH A . 
E 4 HOH 286 786 68  HOH HOH A . 
E 4 HOH 287 787 261 HOH HOH A . 
E 4 HOH 288 788 94  HOH HOH A . 
E 4 HOH 289 789 303 HOH HOH A . 
E 4 HOH 290 790 338 HOH HOH A . 
E 4 HOH 291 791 275 HOH HOH A . 
E 4 HOH 292 792 104 HOH HOH A . 
E 4 HOH 293 793 144 HOH HOH A . 
E 4 HOH 294 794 62  HOH HOH A . 
E 4 HOH 295 795 72  HOH HOH A . 
E 4 HOH 296 796 152 HOH HOH A . 
E 4 HOH 297 797 434 HOH HOH A . 
E 4 HOH 298 798 110 HOH HOH A . 
E 4 HOH 299 799 149 HOH HOH A . 
E 4 HOH 300 800 245 HOH HOH A . 
E 4 HOH 301 801 193 HOH HOH A . 
E 4 HOH 302 802 295 HOH HOH A . 
E 4 HOH 303 803 297 HOH HOH A . 
E 4 HOH 304 804 258 HOH HOH A . 
E 4 HOH 305 805 241 HOH HOH A . 
E 4 HOH 306 806 215 HOH HOH A . 
E 4 HOH 307 807 305 HOH HOH A . 
E 4 HOH 308 808 285 HOH HOH A . 
E 4 HOH 309 809 208 HOH HOH A . 
E 4 HOH 310 810 439 HOH HOH A . 
E 4 HOH 311 811 426 HOH HOH A . 
E 4 HOH 312 812 181 HOH HOH A . 
E 4 HOH 313 813 433 HOH HOH A . 
E 4 HOH 314 814 225 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 97  ? CG  ? A LYS 103 CG  
2  1 Y 1 A LYS 97  ? CD  ? A LYS 103 CD  
3  1 Y 1 A LYS 97  ? CE  ? A LYS 103 CE  
4  1 Y 1 A LYS 97  ? NZ  ? A LYS 103 NZ  
5  1 Y 1 A LYS 328 ? CG  ? A LYS 334 CG  
6  1 Y 1 A LYS 328 ? CD  ? A LYS 334 CD  
7  1 Y 1 A LYS 328 ? CE  ? A LYS 334 CE  
8  1 Y 1 A LYS 328 ? NZ  ? A LYS 334 NZ  
9  1 Y 1 A PHE 329 ? CG  ? A PHE 335 CG  
10 1 Y 1 A PHE 329 ? CD1 ? A PHE 335 CD1 
11 1 Y 1 A PHE 329 ? CD2 ? A PHE 335 CD2 
12 1 Y 1 A PHE 329 ? CE1 ? A PHE 335 CE1 
13 1 Y 1 A PHE 329 ? CE2 ? A PHE 335 CE2 
14 1 Y 1 A PHE 329 ? CZ  ? A PHE 335 CZ  
15 1 Y 1 A ASP 334 ? CG  ? A ASP 340 CG  
16 1 Y 1 A ASP 334 ? OD1 ? A ASP 340 OD1 
17 1 Y 1 A ASP 334 ? OD2 ? A ASP 340 OD2 
18 1 Y 1 A ASP 335 ? CG  ? A ASP 341 CG  
19 1 Y 1 A ASP 335 ? OD1 ? A ASP 341 OD1 
20 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                   109.660 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QR8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.000 
_cell.length_a_esd                 ? 
_cell.length_b                     70.590 
_cell.length_b_esd                 ? 
_cell.length_c                     60.780 
_cell.length_c_esd                 ? 
_cell.volume                       197977.180 
_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                         8QR8 
_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                   8QR8 
_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             2.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.42 
_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                          19.02 
_reflns.entry_id                                       8QR8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.61 
_reflns.d_resolution_low                               38.62 
_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                                     50322 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_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                          6.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.86 
_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                                0.149 
_reflns.pdbx_Rpim_I_all                                0.080 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       174451 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.978 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.125 
_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                                    1.61 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           8811 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2508 
_reflns_shell.percent_possible_obs                          99.7 
_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                              0.65 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               0.754 
_reflns_shell.pdbx_Rpim_I_all                               0.396 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.715 
_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                                  0.639 
_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                               27.83 
_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                                 8QR8 
_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                            1.61 
_refine.ls_d_res_low                             28.51 
_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                     50257 
_refine.ls_number_reflns_R_free                  2536 
_refine.ls_number_reflns_R_work                  47721 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1579 
_refine.ls_R_factor_R_free                       0.2002 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1557 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 18.8738 
_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                            0.1795 
_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                       1.61 
_refine_hist.d_res_low                        28.51 
_refine_hist.number_atoms_solvent             314 
_refine_hist.number_atoms_total               3136 
_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        2786 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0165 ? 3001 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4062 ? 4078 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0928 ? 449  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0125 ? 518  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.1341 ? 419  ? 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' 1.61 1.64  . . 149 2642 99.39  . . . . 0.2316 . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 1.64 1.67  . . 157 2616 99.78  . . . . 0.2082 . . . . . . . . . . . 0.2853 
'X-RAY DIFFRACTION' 1.67 1.71  . . 162 2596 99.46  . . . . 0.1931 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 1.71 1.75  . . 147 2662 99.72  . . . . 0.1676 . . . . . . . . . . . 0.2091 
'X-RAY DIFFRACTION' 1.75 1.79  . . 130 2641 99.68  . . . . 0.1498 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 1.79 1.84  . . 140 2640 99.61  . . . . 0.1410 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 1.84 1.90  . . 148 2663 99.68  . . . . 0.1449 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 1.90 1.96  . . 144 2625 99.57  . . . . 0.1512 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.96 2.03  . . 133 2651 99.71  . . . . 0.1375 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 2.03 2.11  . . 138 2652 99.86  . . . . 0.1338 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 2.11 2.21  . . 139 2674 99.58  . . . . 0.1433 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 2.21 2.32  . . 138 2649 99.54  . . . . 0.1440 . . . . . . . . . . . 0.2048 
'X-RAY DIFFRACTION' 2.32 2.47  . . 129 2663 99.82  . . . . 0.1483 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 2.47 2.66  . . 164 2648 99.96  . . . . 0.1494 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 2.66 2.92  . . 144 2678 100.00 . . . . 0.1554 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 2.92 3.35  . . 107 2701 100.00 . . . . 0.1553 . . . . . . . . . . . 0.1902 
'X-RAY DIFFRACTION' 3.35 4.22  . . 147 2671 99.79  . . . . 0.1480 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 4.22 28.51 . . 120 2649 95.88  . . . . 0.1761 . . . . . . . . . . . 0.1773 
# 
_struct.entry_id                     8QR8 
_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        8QR8 
_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              8QR8 
_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 8QR8 HIS A 1 ? UNP P63086 ? ? 'expression tag' -5 1 
1 8QR8 HIS A 2 ? UNP P63086 ? ? 'expression tag' -4 2 
1 8QR8 HIS A 3 ? UNP P63086 ? ? 'expression tag' -3 3 
1 8QR8 HIS A 4 ? UNP P63086 ? ? 'expression tag' -2 4 
1 8QR8 HIS A 5 ? UNP P63086 ? ? 'expression tag' -1 5 
1 8QR8 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)' 350   ? 
1 MORE         -23   ? 
1 'SSA (A^2)'  16390 ? 
# 
_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 ? SER A 270 ? ASN A 255 SER A 264 1 ? 10 
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 ? ? ? ? ? ? ? 1.328 ? ? 
covale2 covale both ? A CME 165 C  ? ? ? 1_555 A ASP 166 N  ? ? A CME 159 A ASP 160 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale3 covale none ? A CYS 170 SG ? ? ? 1_555 D WN2 .   C4 ? ? A CYS 164 A WN2 403 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
covale4 covale both ? A ASN 257 C  ? ? ? 1_555 A CME 258 N  ? ? A ASN 251 A CME 252 1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale5 covale both ? A CME 258 C  ? ? ? 1_555 A ILE 259 N  ? ? A CME 252 A ILE 253 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
# 
_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 WN2 D .   ? CYS A 170 ? WN2 A 403 ? 1_555 CYS A 164 ? 1_555 C4 SG CYS 1 WN2 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       -0.77 
# 
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 MET A 17  ? VAL A 18  ? MET A 11  VAL A 12  
AA1 2 GLN A 21  ? VAL A 22  ? GLN A 15  VAL A 16  
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 VAL A 18  ? N VAL A 12  O GLN A 21  ? O GLN A 15  
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 TYR A 106 ? O TYR A 100 N ILE A 94  ? N ILE A 88  
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                   8QR8 
_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 ? ? -150.20 43.32  
2 1 ASP A 165 ? ? 69.13   99.72  
3 1 ALA A 187 ? B 57.88   155.99 
4 1 ASN A 199 ? ? -159.75 21.14  
5 1 LEU A 292 ? ? -94.49  45.18  
6 1 ASP A 316 ? ? -162.73 93.45  
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 813 ? 6.65 . 
2 1 O ? A HOH 814 ? 8.10 . 
# 
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 GLY 355 ? A GLY 361 
20 1 Y 1 A TYR 356 ? A TYR 362 
21 1 Y 1 A ARG 357 ? A ARG 363 
22 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 
WN2 C1   C N N 418 
WN2 C2   C N S 419 
WN2 C3   C N N 420 
WN2 C4   C N N 421 
WN2 C5   C N N 422 
WN2 C6   C N N 423 
WN2 C7   C N S 424 
WN2 C8   C N S 425 
WN2 C9   C N N 426 
WN2 C10  C N N 427 
WN2 C11  C N N 428 
WN2 O1   O N N 429 
WN2 O2   O N N 430 
WN2 O3   O N N 431 
WN2 C12  C N N 432 
WN2 C13  C Y N 433 
WN2 O4   O N N 434 
WN2 O5   O N N 435 
WN2 C14  C Y N 436 
WN2 C15  C Y N 437 
WN2 C16  C Y N 438 
WN2 C17  C Y N 439 
WN2 C18  C Y N 440 
WN2 C19  C N N 441 
WN2 O6   O N N 442 
WN2 O7   O N N 443 
WN2 H1   H N N 444 
WN2 H3   H N N 445 
WN2 H2   H N N 446 
WN2 H4   H N N 447 
WN2 H6   H N N 448 
WN2 H5   H N N 449 
WN2 H7   H N N 450 
WN2 H41  H N N 451 
WN2 H8   H N N 452 
WN2 H51  H N N 453 
WN2 H9   H N N 454 
WN2 H11  H N N 455 
WN2 H13  H N N 456 
WN2 H14  H N N 457 
WN2 H15  H N N 458 
WN2 H16  H N N 459 
WN2 H17  H N N 460 
WN2 H18  H N N 461 
WN2 H10  H N N 462 
WN2 H12  H N N 463 
WN2 H20  H N N 464 
WN2 H19  H N N 465 
WN2 H22  H N N 466 
WN2 H24  H N N 467 
WN2 H21  H N N 468 
WN2 H23  H N N 469 
# 
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 
WN2 C1  C2   sing N N 401 
WN2 C2  C3   sing N N 402 
WN2 C2  O7   sing N N 403 
WN2 C3  C4   sing N N 404 
WN2 C4  C5   sing N N 405 
WN2 C5  C6   sing N N 406 
WN2 C6  O1   doub N N 407 
WN2 C6  C7   sing N N 408 
WN2 C7  O2   sing N N 409 
WN2 C7  C8   sing N N 410 
WN2 C8  O3   sing N N 411 
WN2 C8  C9   sing N N 412 
WN2 C9  C10  sing N N 413 
WN2 C10 C11  sing N N 414 
WN2 C11 C12  sing N N 415 
WN2 C12 C13  sing N N 416 
WN2 C13 C14  doub Y N 417 
WN2 C13 C18  sing Y N 418 
WN2 C14 C15  sing Y N 419 
WN2 C15 O4   sing N N 420 
WN2 C15 C16  doub Y N 421 
WN2 C16 C17  sing Y N 422 
WN2 C17 O5   sing N N 423 
WN2 C17 C18  doub Y N 424 
WN2 C18 C19  sing N N 425 
WN2 C19 O6   doub N N 426 
WN2 C19 O7   sing N N 427 
WN2 C1  H1   sing N N 428 
WN2 C1  H3   sing N N 429 
WN2 C1  H2   sing N N 430 
WN2 C2  H4   sing N N 431 
WN2 C3  H6   sing N N 432 
WN2 C3  H5   sing N N 433 
WN2 C4  H7   sing N N 434 
WN2 C4  H41  sing N N 435 
WN2 C5  H8   sing N N 436 
WN2 C5  H51  sing N N 437 
WN2 C7  H9   sing N N 438 
WN2 C8  H11  sing N N 439 
WN2 C9  H13  sing N N 440 
WN2 C9  H14  sing N N 441 
WN2 C10 H15  sing N N 442 
WN2 C10 H16  sing N N 443 
WN2 C11 H17  sing N N 444 
WN2 C11 H18  sing N N 445 
WN2 O2  H10  sing N N 446 
WN2 O3  H12  sing N N 447 
WN2 C12 H20  sing N N 448 
WN2 C12 H19  sing N N 449 
WN2 O4  H22  sing N N 450 
WN2 O5  H24  sing N N 451 
WN2 C14 H21  sing N N 452 
WN2 C16 H23  sing N N 453 
# 
_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 
# 
_pdbx_initial_refinement_model.accession_code   3QYZ 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_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                    8QR8 
_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]   0.020408 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007291 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014166 
_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]   0.017471 
_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  ? -21.17930 20.97078  20.16166 1.000 60.16258 ? 9   PRO A N   1 
ATOM   2    C CA  . PRO A 1 15  ? -20.95956 20.30212  21.44243 1.000 60.11946 ? 9   PRO A CA  1 
ATOM   3    C C   . PRO A 1 15  ? -21.53044 21.08633  22.59987 1.000 60.22565 ? 9   PRO A C   1 
ATOM   4    O O   . PRO A 1 15  ? -21.51590 22.31589  22.54763 1.000 59.71205 ? 9   PRO A O   1 
ATOM   5    C CB  . PRO A 1 15  ? -19.43450 20.24125  21.54366 1.000 60.29597 ? 9   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 15  ? -18.96704 21.39630  20.73473 1.000 60.47168 ? 9   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 15  ? -19.90639 21.41415  19.56770 1.000 60.26985 ? 9   PRO A CD  1 
ATOM   8    N N   . GLU A 1 16  ? -22.00969 20.39663  23.63141 1.000 60.84076 ? 10  GLU A N   1 
ATOM   9    C CA  . GLU A 1 16  ? -22.52967 21.09017  24.80495 1.000 61.51977 ? 10  GLU A CA  1 
ATOM   10   C C   . GLU A 1 16  ? -21.40068 21.77083  25.57797 1.000 61.25222 ? 10  GLU A C   1 
ATOM   11   O O   . GLU A 1 16  ? -20.27330 21.27432  25.65164 1.000 61.46338 ? 10  GLU A O   1 
ATOM   12   C CB  . GLU A 1 16  ? -23.30490 20.12561  25.70578 0.800 62.01236 ? 10  GLU A CB  1 
ATOM   13   C CG  . GLU A 1 16  ? -24.68697 19.71721  25.15342 0.700 62.36423 ? 10  GLU A CG  1 
ATOM   14   C CD  . GLU A 1 16  ? -25.33536 20.77839  24.25221 0.700 62.56215 ? 10  GLU A CD  1 
ATOM   15   O OE1 . GLU A 1 16  ? -25.59607 21.90351  24.73255 0.700 62.61429 ? 10  GLU A OE1 1 
ATOM   16   O OE2 . GLU A 1 16  ? -25.59874 20.48252  23.06340 0.700 62.68562 ? 10  GLU A OE2 1 
ATOM   17   N N   . MET A 1 17  ? -21.69810 22.94448  26.11169 1.000 60.88440 ? 11  MET A N   1 
ATOM   18   C CA  . MET A 1 17  ? -20.72247 23.76349  26.80746 1.000 60.73094 ? 11  MET A CA  1 
ATOM   19   C C   . MET A 1 17  ? -21.09648 23.84576  28.28181 1.000 60.11328 ? 11  MET A C   1 
ATOM   20   O O   . MET A 1 17  ? -22.27752 23.83982  28.64356 1.000 60.19857 ? 11  MET A O   1 
ATOM   21   C CB  . MET A 1 17  ? -20.63609 25.18025  26.20472 1.000 61.20754 ? 11  MET A CB  1 
ATOM   22   C CG  . MET A 1 17  ? -20.42557 25.30392  24.66812 1.000 61.94840 ? 11  MET A CG  1 
ATOM   23   S SD  . MET A 1 17  ? -18.81683 24.81291  23.94636 1.000 62.64479 ? 11  MET A SD  1 
ATOM   24   C CE  . MET A 1 17  ? -17.85687 26.29210  24.28177 1.000 62.45692 ? 11  MET A CE  1 
ATOM   25   N N   . VAL A 1 18  ? -20.07836 23.88609  29.13642 1.000 59.57713 ? 12  VAL A N   1 
ATOM   26   C CA  . VAL A 1 18  ? -20.27154 24.08833  30.56589 1.000 59.00679 ? 12  VAL A CA  1 
ATOM   27   C C   . VAL A 1 18  ? -19.30146 25.16469  31.02433 1.000 59.25357 ? 12  VAL A C   1 
ATOM   28   O O   . VAL A 1 18  ? -18.08577 25.04177  30.80870 1.000 59.28895 ? 12  VAL A O   1 
ATOM   29   C CB  . VAL A 1 18  ? -20.06549 22.80543  31.38394 1.000 58.46003 ? 12  VAL A CB  1 
ATOM   30   C CG1 . VAL A 1 18  ? -20.15473 23.13757  32.86247 1.000 58.22444 ? 12  VAL A CG1 1 
ATOM   31   C CG2 . VAL A 1 18  ? -21.10241 21.77214  31.01765 1.000 58.12364 ? 12  VAL A CG2 1 
ATOM   32   N N   . ARG A 1 19  ? -19.84819 26.21985  31.64774 1.000 59.05690 ? 13  ARG A N   1 
ATOM   33   C CA  . ARG A 1 19  ? -19.09051 27.36091  32.16900 1.000 58.19898 ? 13  ARG A CA  1 
ATOM   34   C C   . ARG A 1 19  ? -18.07549 27.86960  31.14162 1.000 57.84240 ? 13  ARG A C   1 
ATOM   35   O O   . ARG A 1 19  ? -16.90023 28.09895  31.44349 1.000 58.11721 ? 13  ARG A O   1 
ATOM   36   C CB  . ARG A 1 19  ? -18.42460 26.99937  33.49950 0.800 57.27834 ? 13  ARG A CB  1 
ATOM   37   C CG  . ARG A 1 19  ? -19.44395 26.67949  34.58196 0.700 56.59742 ? 13  ARG A CG  1 
ATOM   38   C CD  . ARG A 1 19  ? -18.85638 26.78648  35.97425 0.600 56.02107 ? 13  ARG A CD  1 
ATOM   39   N NE  . ARG A 1 19  ? -19.85325 26.51374  37.00377 0.500 55.66664 ? 13  ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 19  ? -19.62995 26.64095  38.30295 0.500 55.52606 ? 13  ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 19  ? -18.45337 27.03334  38.76394 0.500 55.76394 ? 13  ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 19  ? -20.60636 26.35980  39.16086 0.500 55.36885 ? 13  ARG A NH2 1 
ATOM   43   N N   . GLY A 1 20  ? -18.53831 28.00630  29.89452 0.700 56.76478 ? 14  GLY A N   1 
ATOM   44   C CA  . GLY A 1 20  ? -17.72998 28.52603  28.81777 0.700 55.92172 ? 14  GLY A CA  1 
ATOM   45   C C   . GLY A 1 20  ? -16.86897 27.51281  28.08770 0.700 55.28339 ? 14  GLY A C   1 
ATOM   46   O O   . GLY A 1 20  ? -16.38520 27.81827  26.98457 0.700 55.32304 ? 14  GLY A O   1 
ATOM   47   N N   . GLN A 1 21  ? -16.66033 26.32251  28.65842 0.700 54.14950 ? 15  GLN A N   1 
ATOM   48   C CA  . GLN A 1 21  ? -15.77192 25.32104  28.08465 0.700 53.05998 ? 15  GLN A CA  1 
ATOM   49   C C   . GLN A 1 21  ? -16.53758 24.25644  27.30794 0.700 50.96604 ? 15  GLN A C   1 
ATOM   50   O O   . GLN A 1 21  ? -17.71517 24.00550  27.55722 0.700 50.69866 ? 15  GLN A O   1 
ATOM   51   C CB  . GLN A 1 21  ? -14.94823 24.63226  29.16811 0.700 53.89270 ? 15  GLN A CB  1 
ATOM   52   C CG  . GLN A 1 21  ? -13.84117 25.45662  29.77243 0.700 54.57811 ? 15  GLN A CG  1 
ATOM   53   C CD  . GLN A 1 21  ? -12.92806 24.58544  30.61115 0.700 55.30222 ? 15  GLN A CD  1 
ATOM   54   O OE1 . GLN A 1 21  ? -13.19445 23.39412  30.78939 0.700 55.67757 ? 15  GLN A OE1 1 
ATOM   55   N NE2 . GLN A 1 21  ? -11.82214 25.15203  31.08323 0.700 55.47818 ? 15  GLN A NE2 1 
ATOM   56   N N   . VAL A 1 22  ? -15.84251 23.61918  26.36433 1.000 49.38501 ? 16  VAL A N   1 
ATOM   57   C CA  . VAL A 1 22  ? -16.41137 22.47749  25.65558 1.000 47.75340 ? 16  VAL A CA  1 
ATOM   58   C C   . VAL A 1 22  ? -16.43845 21.27820  26.59854 1.000 46.00140 ? 16  VAL A C   1 
ATOM   59   O O   . VAL A 1 22  ? -15.44251 20.97676  27.27513 1.000 46.61117 ? 16  VAL A O   1 
ATOM   60   C CB  . VAL A 1 22  ? -15.58653 22.15834  24.39659 1.000 47.91739 ? 16  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 22  ? -15.97859 20.81151  23.84378 1.000 48.19728 ? 16  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 22  ? -15.71313 23.25140  23.33634 1.000 47.94339 ? 16  VAL A CG2 1 
ATOM   63   N N   . PHE A 1 23  ? -17.59415 20.60030  26.67554 1.000 43.93014 ? 17  PHE A N   1 
ATOM   64   C CA  . PHE A 1 23  ? -17.74869 19.38432  27.48523 1.000 42.57721 ? 17  PHE A CA  1 
ATOM   65   C C   . PHE A 1 23  ? -18.50364 18.37401  26.62204 1.000 41.88678 ? 17  PHE A C   1 
ATOM   66   O O   . PHE A 1 23  ? -19.71617 18.19969  26.72021 1.000 42.66255 ? 17  PHE A O   1 
ATOM   67   C CB  . PHE A 1 23  ? -18.45584 19.63948  28.80740 1.000 41.54194 ? 17  PHE A CB  1 
ATOM   68   C CG  . PHE A 1 23  ? -18.00174 18.71753  29.88969 1.000 40.41325 ? 17  PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 23  ? -16.92462 19.03737  30.68570 1.000 40.70593 ? 17  PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 23  ? -18.58788 17.47526  30.03961 1.000 40.17872 ? 17  PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 23  ? -16.47250 18.13721  31.65537 1.000 40.05748 ? 17  PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 23  ? -18.15150 16.57642  31.01470 1.000 39.20137 ? 17  PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 23  ? -17.10415 16.91328  31.81675 1.000 39.48546 ? 17  PHE A CZ  1 
ATOM   74   N N   . ASP A 1 24  ? -17.75000 17.68986  25.77469 1.000 40.34557 ? 18  ASP A N   1 
ATOM   75   C CA  . ASP A 1 24  ? -18.26910 17.08265  24.55921 1.000 38.28404 ? 18  ASP A CA  1 
ATOM   76   C C   . ASP A 1 24  ? -18.51557 15.58110  24.72284 1.000 38.72862 ? 18  ASP A C   1 
ATOM   77   O O   . ASP A 1 24  ? -17.71964 14.75092  24.31933 1.000 38.78530 ? 18  ASP A O   1 
ATOM   78   C CB  . ASP A 1 24  ? -17.28446 17.35106  23.44007 0.800 37.65850 ? 18  ASP A CB  1 
ATOM   79   C CG  . ASP A 1 24  ? -17.87281 17.06050  22.12128 0.800 36.50181 ? 18  ASP A CG  1 
ATOM   80   O OD1 . ASP A 1 24  ? -19.06403 16.71014  22.11994 0.600 37.11030 ? 18  ASP A OD1 1 
ATOM   81   O OD2 . ASP A 1 24  ? -17.16580 17.16730  21.11049 0.600 35.84454 ? 18  ASP A OD2 1 
ATOM   82   N N   . VAL A 1 25  ? -19.64942 15.21610  25.30553 1.000 39.54708 ? 19  VAL A N   1 
ATOM   83   C CA  . VAL A 1 25  ? -19.83844 13.84144  25.75542 1.000 39.36091 ? 19  VAL A CA  1 
ATOM   84   C C   . VAL A 1 25  ? -21.03877 13.18152  25.11669 1.000 40.37805 ? 19  VAL A C   1 
ATOM   85   O O   . VAL A 1 25  ? -21.28312 12.00415  25.36780 1.000 40.34016 ? 19  VAL A O   1 
ATOM   86   C CB  . VAL A 1 25  ? -19.95396 13.74709  27.29509 1.000 37.78943 ? 19  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 25  ? -18.75025 14.34234  27.97817 1.000 38.52470 ? 19  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 25  ? -21.19777 14.43674  27.76627 1.000 38.21823 ? 19  VAL A CG2 1 
ATOM   89   N N   . GLY A 1 26  ? -21.78653 13.88659  24.27747 1.000 42.05150 ? 20  GLY A N   1 
ATOM   90   C CA  . GLY A 1 26  ? -23.05521 13.36501  23.81697 1.000 41.81026 ? 20  GLY A CA  1 
ATOM   91   C C   . GLY A 1 26  ? -22.90497 12.48664  22.59608 1.000 42.81418 ? 20  GLY A C   1 
ATOM   92   O O   . GLY A 1 26  ? -21.80339 12.29587  22.04463 1.000 43.86924 ? 20  GLY A O   1 
ATOM   93   N N   . PRO A 1 27  ? -24.03925 11.94672  22.12563 1.000 41.55210 ? 21  PRO A N   1 
ATOM   94   C CA  . PRO A 1 27  ? -25.40463 12.09496  22.66401 1.000 40.13956 ? 21  PRO A CA  1 
ATOM   95   C C   . PRO A 1 27  ? -25.78362 11.16378  23.83557 1.000 39.53912 ? 21  PRO A C   1 
ATOM   96   O O   . PRO A 1 27  ? -26.89676 11.30597  24.37669 1.000 40.36846 ? 21  PRO A O   1 
ATOM   97   C CB  . PRO A 1 27  ? -26.26883 11.75141  21.45854 1.000 40.88993 ? 21  PRO A CB  1 
ATOM   98   C CG  . PRO A 1 27  ? -25.45765 10.71361  20.71533 1.000 40.59156 ? 21  PRO A CG  1 
ATOM   99   C CD  . PRO A 1 27  ? -24.01997 11.13914  20.88921 1.000 40.82887 ? 21  PRO A CD  1 
ATOM   100  N N   . ARG A 1 28  ? -24.91596 10.20971  24.18763 1.000 38.08391 ? 22  ARG A N   1 
ATOM   101  C CA  . ARG A 1 28  ? -25.27201 9.26050   25.24496 1.000 37.36179 ? 22  ARG A CA  1 
ATOM   102  C C   . ARG A 1 28  ? -25.45510 9.97164   26.58207 1.000 37.98869 ? 22  ARG A C   1 
ATOM   103  O O   . ARG A 1 28  ? -26.37359 9.64372   27.35064 1.000 38.90993 ? 22  ARG A O   1 
ATOM   104  C CB  . ARG A 1 28  ? -24.22417 8.14590   25.35628 1.000 36.56980 ? 22  ARG A CB  1 
ATOM   105  C CG  . ARG A 1 28  ? -24.42067 7.27806   26.60898 1.000 36.56437 ? 22  ARG A CG  1 
ATOM   106  C CD  . ARG A 1 28  ? -23.55326 6.03202   26.56972 1.000 36.81431 ? 22  ARG A CD  1 
ATOM   107  N NE  . ARG A 1 28  ? -23.73811 5.21411   27.75441 1.000 37.03062 ? 22  ARG A NE  1 
ATOM   108  C CZ  . ARG A 1 28  ? -23.03589 4.12584   28.03173 1.000 38.08965 ? 22  ARG A CZ  1 
ATOM   109  N NH1 . ARG A 1 28  ? -22.10392 3.69010   27.21066 1.000 38.81719 ? 22  ARG A NH1 1 
ATOM   110  N NH2 . ARG A 1 28  ? -23.25597 3.48151   29.18442 1.000 38.21710 ? 22  ARG A NH2 1 
ATOM   111  N N   . TYR A 1 29  ? -24.62675 10.97494  26.86518 1.000 38.21787 ? 23  TYR A N   1 
ATOM   112  C CA  . TYR A 1 29  ? -24.64654 11.64804  28.15823 1.000 37.83730 ? 23  TYR A CA  1 
ATOM   113  C C   . TYR A 1 29  ? -25.18633 13.05934  27.97410 1.000 40.76758 ? 23  TYR A C   1 
ATOM   114  O O   . TYR A 1 29  ? -24.61402 13.84822  27.20763 1.000 41.55777 ? 23  TYR A O   1 
ATOM   115  C CB  . TYR A 1 29  ? -23.25078 11.64720  28.78727 1.000 35.38272 ? 23  TYR A CB  1 
ATOM   116  C CG  . TYR A 1 29  ? -22.69319 10.24941  28.93276 1.000 33.44575 ? 23  TYR A CG  1 
ATOM   117  C CD1 . TYR A 1 29  ? -23.07044 9.43624   29.99895 1.000 32.42579 ? 23  TYR A CD1 1 
ATOM   118  C CD2 . TYR A 1 29  ? -21.80522 9.72761   27.98027 1.000 31.60614 ? 23  TYR A CD2 1 
ATOM   119  C CE1 . TYR A 1 29  ? -22.54953 8.12875   30.15499 1.000 31.60498 ? 23  TYR A CE1 1 
ATOM   120  C CE2 . TYR A 1 29  ? -21.27461 8.44296   28.10052 1.000 31.46844 ? 23  TYR A CE2 1 
ATOM   121  C CZ  . TYR A 1 29  ? -21.63972 7.64266   29.20421 1.000 31.20178 ? 23  TYR A CZ  1 
ATOM   122  O OH  . TYR A 1 29  ? -21.14824 6.36638   29.32061 1.000 30.97939 ? 23  TYR A OH  1 
ATOM   123  N N   . THR A 1 30  ? -26.32430 13.34333  28.62429 1.000 43.16822 ? 24  THR A N   1 
ATOM   124  C CA  . THR A 1 30  ? -27.07124 14.59419  28.50901 1.000 44.71956 ? 24  THR A CA  1 
ATOM   125  C C   . THR A 1 30  ? -27.36164 15.18928  29.89036 1.000 46.46242 ? 24  THR A C   1 
ATOM   126  O O   . THR A 1 30  ? -27.02411 14.61390  30.92034 1.000 46.19487 ? 24  THR A O   1 
ATOM   127  C CB  . THR A 1 30  ? -28.37429 14.36537  27.72183 1.000 45.76715 ? 24  THR A CB  1 
ATOM   128  O OG1 . THR A 1 30  ? -29.07654 13.23929  28.27062 1.000 46.09670 ? 24  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 30  ? -28.05436 14.11145  26.27112 1.000 46.00697 ? 24  THR A CG2 1 
ATOM   130  N N   . ASN A 1 31  ? -28.01195 16.35729  29.90461 1.000 48.58019 ? 25  ASN A N   1 
ATOM   131  C CA  . ASN A 1 31  ? -28.46136 17.01889  31.14316 1.000 49.69720 ? 25  ASN A CA  1 
ATOM   132  C C   . ASN A 1 31  ? -27.30544 17.20998  32.12835 1.000 50.30965 ? 25  ASN A C   1 
ATOM   133  O O   . ASN A 1 31  ? -27.34710 16.74380  33.26571 1.000 50.50754 ? 25  ASN A O   1 
ATOM   134  C CB  . ASN A 1 31  ? -29.60258 16.24660  31.81557 0.700 49.65477 ? 25  ASN A CB  1 
ATOM   135  C CG  . ASN A 1 31  ? -30.53125 17.15480  32.62213 0.600 50.58152 ? 25  ASN A CG  1 
ATOM   136  O OD1 . ASN A 1 31  ? -30.18260 18.29242  32.95536 0.600 51.16319 ? 25  ASN A OD1 1 
ATOM   137  N ND2 . ASN A 1 31  ? -31.71414 16.64545  32.95189 0.600 50.47387 ? 25  ASN A ND2 1 
ATOM   138  N N   . LEU A 1 32  ? -26.27857 17.92970  31.67142 1.000 50.84880 ? 26  LEU A N   1 
ATOM   139  C CA  . LEU A 1 32  ? -25.03344 18.09539  32.41181 1.000 51.38212 ? 26  LEU A CA  1 
ATOM   140  C C   . LEU A 1 32  ? -25.16897 19.12198  33.53727 1.000 51.75463 ? 26  LEU A C   1 
ATOM   141  O O   . LEU A 1 32  ? -25.85601 20.13990  33.39222 1.000 52.24097 ? 26  LEU A O   1 
ATOM   142  C CB  . LEU A 1 32  ? -23.91904 18.53586  31.45957 1.000 52.30053 ? 26  LEU A CB  1 
ATOM   143  C CG  . LEU A 1 32  ? -23.10629 17.51773  30.65205 1.000 53.27866 ? 26  LEU A CG  1 
ATOM   144  C CD1 . LEU A 1 32  ? -23.96953 16.37689  30.12575 1.000 53.26911 ? 26  LEU A CD1 1 
ATOM   145  C CD2 . LEU A 1 32  ? -22.42019 18.24256  29.47649 1.000 53.71225 ? 26  LEU A CD2 1 
ATOM   146  N N   . SER A 1 33  ? -24.49392 18.84761  34.66297 1.000 50.96014 ? 27  SER A N   1 
ATOM   147  C CA  . SER A 1 33  ? -24.35751 19.77383  35.78529 1.000 51.30012 ? 27  SER A CA  1 
ATOM   148  C C   . SER A 1 33  ? -22.92107 19.78590  36.27938 1.000 51.78820 ? 27  SER A C   1 
ATOM   149  O O   . SER A 1 33  ? -22.35863 18.73070  36.59074 1.000 51.08713 ? 27  SER A O   1 
ATOM   150  C CB  . SER A 1 33  ? -25.25610 19.39141  36.96376 1.000 51.87063 ? 27  SER A CB  1 
ATOM   151  O OG  . SER A 1 33  ? -26.56038 19.09043  36.53871 1.000 52.75327 ? 27  SER A OG  1 
ATOM   152  N N   . TYR A 1 34  ? -22.34615 20.97198  36.40825 1.000 52.46356 ? 28  TYR A N   1 
ATOM   153  C CA  . TYR A 1 34  ? -21.01443 21.07604  36.99544 1.000 52.85511 ? 28  TYR A CA  1 
ATOM   154  C C   . TYR A 1 34  ? -21.01595 20.58329  38.44443 1.000 52.46632 ? 28  TYR A C   1 
ATOM   155  O O   . TYR A 1 34  ? -21.86510 20.99009  39.24054 1.000 52.92715 ? 28  TYR A O   1 
ATOM   156  C CB  . TYR A 1 34  ? -20.55073 22.52622  36.93512 1.000 53.87449 ? 28  TYR A CB  1 
ATOM   157  C CG  . TYR A 1 34  ? -19.25997 22.80930  37.64901 1.000 55.11177 ? 28  TYR A CG  1 
ATOM   158  C CD1 . TYR A 1 34  ? -18.03552 22.64680  37.00681 1.000 55.50217 ? 28  TYR A CD1 1 
ATOM   159  C CD2 . TYR A 1 34  ? -19.25899 23.23859  38.97546 1.000 55.87115 ? 28  TYR A CD2 1 
ATOM   160  C CE1 . TYR A 1 34  ? -16.84036 22.91526  37.66769 1.000 55.86217 ? 28  TYR A CE1 1 
ATOM   161  C CE2 . TYR A 1 34  ? -18.08777 23.50598  39.63345 1.000 55.93609 ? 28  TYR A CE2 1 
ATOM   162  C CZ  . TYR A 1 34  ? -16.88374 23.35465  38.97717 1.000 56.46619 ? 28  TYR A CZ  1 
ATOM   163  O OH  . TYR A 1 34  ? -15.71791 23.62792  39.65860 1.000 57.31713 ? 28  TYR A OH  1 
ATOM   164  N N   . ILE A 1 35  ? -20.06862 19.70572  38.79725 1.000 51.02163 ? 29  ILE A N   1 
ATOM   165  C CA  . ILE A 1 35  ? -19.99828 19.18220  40.15762 1.000 50.58503 ? 29  ILE A CA  1 
ATOM   166  C C   . ILE A 1 35  ? -18.64256 19.37319  40.83183 1.000 50.28560 ? 29  ILE A C   1 
ATOM   167  O O   . ILE A 1 35  ? -18.49897 18.99822  41.99529 1.000 50.16625 ? 29  ILE A O   1 
ATOM   168  C CB  . ILE A 1 35  ? -20.42744 17.69368  40.25334 1.000 49.80102 ? 29  ILE A CB  1 
ATOM   169  C CG1 . ILE A 1 35  ? -19.48412 16.74617  39.52341 1.000 48.96912 ? 29  ILE A CG1 1 
ATOM   170  C CG2 . ILE A 1 35  ? -21.86495 17.48672  39.76941 1.000 49.66172 ? 29  ILE A CG2 1 
ATOM   171  C CD1 . ILE A 1 35  ? -19.96231 15.29834  39.56580 1.000 48.15721 ? 29  ILE A CD1 1 
ATOM   172  N N   . GLY A 1 36  ? -17.64909 19.95252  40.17513 1.000 50.81132 ? 30  GLY A N   1 
ATOM   173  C CA  . GLY A 1 36  ? -16.35023 20.15424  40.80340 1.000 51.13253 ? 30  GLY A CA  1 
ATOM   174  C C   . GLY A 1 36  ? -15.22758 20.16636  39.78193 1.000 52.00890 ? 30  GLY A C   1 
ATOM   175  O O   . GLY A 1 36  ? -15.45534 20.08346  38.57695 1.000 51.94506 ? 30  GLY A O   1 
ATOM   176  N N   . GLU A 1 37  ? -13.99009 20.27360  40.28408 1.000 53.19712 ? 31  GLU A N   1 
ATOM   177  C CA  . GLU A 1 37  ? -12.81565 20.36280  39.41208 1.000 54.81907 ? 31  GLU A CA  1 
ATOM   178  C C   . GLU A 1 37  ? -11.85011 19.19135  39.58870 1.000 54.95069 ? 31  GLU A C   1 
ATOM   179  O O   . GLU A 1 37  ? -11.46104 18.86204  40.71151 1.000 54.57061 ? 31  GLU A O   1 
ATOM   180  C CB  . GLU A 1 37  ? -12.05613 21.67980  39.61593 1.000 56.09494 ? 31  GLU A CB  1 
ATOM   181  C CG  . GLU A 1 37  ? -12.80942 22.91353  39.16945 1.000 57.44477 ? 31  GLU A CG  1 
ATOM   182  C CD  . GLU A 1 37  ? -12.67495 23.19974  37.66052 1.000 58.79324 ? 31  GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 37  ? -11.57819 22.97030  37.07995 1.000 59.09263 ? 31  GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 37  ? -13.68491 23.64751  37.04864 1.000 59.30419 ? 31  GLU A OE2 1 
ATOM   185  N N   . GLY A 1 38  ? -11.45379 18.57514  38.45856 1.000 55.69617 ? 32  GLY A N   1 
ATOM   186  C CA  . GLY A 1 38  ? -10.39820 17.57338  38.42408 1.000 55.61042 ? 32  GLY A CA  1 
ATOM   187  C C   . GLY A 1 38  ? -9.02154  18.20851  38.27735 1.000 55.54284 ? 32  GLY A C   1 
ATOM   188  O O   . GLY A 1 38  ? -8.85024  19.42222  38.40861 1.000 56.50742 ? 32  GLY A O   1 
ATOM   189  N N   . ALA A 1 39  ? -8.01691  17.36324  38.00158 1.000 54.66922 ? 33  ALA A N   1 
ATOM   190  C CA  . ALA A 1 39  ? -6.64567  17.87009  37.86251 1.000 54.68591 ? 33  ALA A CA  1 
ATOM   191  C C   . ALA A 1 39  ? -6.36960  18.48772  36.49409 1.000 54.78730 ? 33  ALA A C   1 
ATOM   192  O O   . ALA A 1 39  ? -5.54312  19.40127  36.38425 1.000 54.21123 ? 33  ALA A O   1 
ATOM   193  C CB  . ALA A 1 39  ? -5.62533  16.75970  38.08619 1.000 54.97046 ? 33  ALA A CB  1 
ATOM   194  N N   . TYR A 1 40  ? -6.99537  17.96805  35.43829 1.000 54.46455 ? 34  TYR A N   1 
ATOM   195  C CA  . TYR A 1 40  ? -6.77460  18.44044  34.07091 1.000 54.50379 ? 34  TYR A CA  1 
ATOM   196  C C   . TYR A 1 40  ? -8.08319  18.86713  33.42285 1.000 53.51080 ? 34  TYR A C   1 
ATOM   197  O O   . TYR A 1 40  ? -8.20062  18.85721  32.18621 1.000 53.29444 ? 34  TYR A O   1 
ATOM   198  C CB  . TYR A 1 40  ? -6.06475  17.36854  33.21904 1.000 55.29589 ? 34  TYR A CB  1 
ATOM   199  C CG  . TYR A 1 40  ? -4.74295  16.90967  33.82503 1.000 56.26339 ? 34  TYR A CG  1 
ATOM   200  C CD1 . TYR A 1 40  ? -3.88252  17.82812  34.42117 1.000 56.69297 ? 34  TYR A CD1 1 
ATOM   201  C CD2 . TYR A 1 40  ? -4.39934  15.55602  33.88201 1.000 56.61230 ? 34  TYR A CD2 1 
ATOM   202  C CE1 . TYR A 1 40  ? -2.67900  17.42372  35.02064 1.000 57.20728 ? 34  TYR A CE1 1 
ATOM   203  C CE2 . TYR A 1 40  ? -3.20173  15.13439  34.47735 1.000 57.05427 ? 34  TYR A CE2 1 
ATOM   204  C CZ  . TYR A 1 40  ? -2.34494  16.08089  35.04879 1.000 57.22590 ? 34  TYR A CZ  1 
ATOM   205  O OH  . TYR A 1 40  ? -1.15870  15.69858  35.63558 1.000 57.16596 ? 34  TYR A OH  1 
ATOM   206  N N   . GLY A 1 41  ? -9.06179  19.23952  34.23486 1.000 52.73466 ? 35  GLY A N   1 
ATOM   207  C CA  . GLY A 1 41  ? -10.36366 19.61368  33.72059 1.000 51.40027 ? 35  GLY A CA  1 
ATOM   208  C C   . GLY A 1 41  ? -11.41494 19.55902  34.80781 1.000 49.97342 ? 35  GLY A C   1 
ATOM   209  O O   . GLY A 1 41  ? -11.13788 19.25273  35.96832 1.000 49.50402 ? 35  GLY A O   1 
ATOM   210  N N   . MET A 1 42  ? -12.63627 19.87735  34.39943 1.000 48.29757 ? 36  MET A N   1 
ATOM   211  C CA  . MET A 1 42  ? -13.75302 19.91213  35.31991 1.000 47.44222 ? 36  MET A CA  1 
ATOM   212  C C   . MET A 1 42  ? -14.45707 18.55907  35.36432 1.000 45.08839 ? 36  MET A C   1 
ATOM   213  O O   . MET A 1 42  ? -14.25505 17.68157  34.51649 1.000 44.16471 ? 36  MET A O   1 
ATOM   214  C CB  . MET A 1 42  ? -14.72325 21.02921  34.93569 1.000 48.70433 ? 36  MET A CB  1 
ATOM   215  C CG  . MET A 1 42  ? -15.31848 20.91302  33.58371 0.900 50.09243 ? 36  MET A CG  1 
ATOM   216  S SD  . MET A 1 42  ? -16.77935 21.97334  33.40614 0.700 51.70768 ? 36  MET A SD  1 
ATOM   217  C CE  . MET A 1 42  ? -16.00345 23.57832  33.24159 0.650 51.57070 ? 36  MET A CE  1 
ATOM   218  N N   . VAL A 1 43  ? -15.28536 18.39781  36.39086 1.000 43.38818 ? 37  VAL A N   1 
ATOM   219  C CA  . VAL A 1 43  ? -16.09029 17.20566  36.57615 1.000 42.19972 ? 37  VAL A CA  1 
ATOM   220  C C   . VAL A 1 43  ? -17.54417 17.63100  36.54245 1.000 42.30574 ? 37  VAL A C   1 
ATOM   221  O O   . VAL A 1 43  ? -17.90543 18.66047  37.11442 1.000 42.02722 ? 37  VAL A O   1 
ATOM   222  C CB  . VAL A 1 43  ? -15.75848 16.48068  37.89339 1.000 40.46326 ? 37  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 43  ? -16.52145 15.17669  37.97280 1.000 39.46368 ? 37  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 43  ? -14.27566 16.24817  38.00199 1.000 40.94497 ? 37  VAL A CG2 1 
ATOM   225  N N   . CYS A 1 44  ? -18.36277 16.86713  35.82904 1.000 42.32354 ? 38  CYS A N   1 
ATOM   226  C CA  . CYS A 1 44  ? -19.78221 17.13932  35.68887 1.000 42.31456 ? 38  CYS A CA  1 
ATOM   227  C C   . CYS A 1 44  ? -20.56215 15.86759  35.98714 1.000 41.16177 ? 38  CYS A C   1 
ATOM   228  O O   . CYS A 1 44  ? -20.03569 14.75560  35.84279 1.000 40.77630 ? 38  CYS A O   1 
ATOM   229  C CB  . CYS A 1 44  ? -20.10480 17.60368  34.29058 1.000 43.19209 ? 38  CYS A CB  1 
ATOM   230  S SG  . CYS A 1 44  ? -19.59877 19.30172  33.83455 1.000 44.68668 ? 38  CYS A SG  1 
ATOM   231  N N   . SER A 1 45  ? -21.81179 16.03195  36.43348 1.000 39.89812 ? 39  SER A N   1 
ATOM   232  C CA  . SER A 1 45  ? -22.73356 14.90894  36.38931 1.000 40.05632 ? 39  SER A CA  1 
ATOM   233  C C   . SER A 1 45  ? -23.52010 14.96677  35.08906 1.000 40.27287 ? 39  SER A C   1 
ATOM   234  O O   . SER A 1 45  ? -23.53551 15.98184  34.39283 1.000 40.90615 ? 39  SER A O   1 
ATOM   235  C CB  . SER A 1 45  ? -23.66854 14.89584  37.59614 1.000 40.59834 ? 39  SER A CB  1 
ATOM   236  O OG  . SER A 1 45  ? -24.48536 16.06038  37.61927 1.000 41.28324 ? 39  SER A OG  1 
ATOM   237  N N   . ALA A 1 46  ? -24.14901 13.84859  34.74139 1.000 39.83345 ? 40  ALA A N   1 
ATOM   238  C CA  . ALA A 1 46  ? -24.77454 13.73444  33.43217 1.000 39.03082 ? 40  ALA A CA  1 
ATOM   239  C C   . ALA A 1 46  ? -25.72994 12.55804  33.46708 1.000 38.26926 ? 40  ALA A C   1 
ATOM   240  O O   . ALA A 1 46  ? -25.52509 11.60520  34.21352 1.000 38.16885 ? 40  ALA A O   1 
ATOM   241  C CB  . ALA A 1 46  ? -23.73174 13.54009  32.31197 1.000 38.68151 ? 40  ALA A CB  1 
ATOM   242  N N   . TYR A 1 47  ? -26.79922 12.63456  32.68255 1.000 37.59777 ? 41  TYR A N   1 
ATOM   243  C CA  . TYR A 1 47  ? -27.63786 11.46212  32.53763 1.000 37.88381 ? 41  TYR A CA  1 
ATOM   244  C C   . TYR A 1 47  ? -27.12057 10.55283  31.42571 1.000 39.94739 ? 41  TYR A C   1 
ATOM   245  O O   . TYR A 1 47  ? -26.86145 11.00073  30.29545 1.000 40.01950 ? 41  TYR A O   1 
ATOM   246  C CB  . TYR A 1 47  ? -29.10449 11.87166  32.29212 0.800 37.14415 ? 41  TYR A CB  1 
ATOM   247  C CG  . TYR A 1 47  ? -30.05400 10.69999  32.14126 0.700 38.41468 ? 41  TYR A CG  1 
ATOM   248  C CD1 . TYR A 1 47  ? -30.47283 9.98870   33.25554 0.600 38.49821 ? 41  TYR A CD1 1 
ATOM   249  C CD2 . TYR A 1 47  ? -30.69066 10.43783  30.92412 0.600 39.14238 ? 41  TYR A CD2 1 
ATOM   250  C CE1 . TYR A 1 47  ? -31.34690 8.94770   33.15509 0.600 38.48486 ? 41  TYR A CE1 1 
ATOM   251  C CE2 . TYR A 1 47  ? -31.62617 9.41234   30.81466 0.600 39.55544 ? 41  TYR A CE2 1 
ATOM   252  C CZ  . TYR A 1 47  ? -31.94993 8.67283   31.94039 0.600 39.21005 ? 41  TYR A CZ  1 
ATOM   253  O OH  . TYR A 1 47  ? -32.85801 7.63768   31.84281 0.600 38.34902 ? 41  TYR A OH  1 
ATOM   254  N N   . ASP A 1 48  ? -26.97400 9.27434   31.77091 1.000 40.01932 ? 42  ASP A N   1 
ATOM   255  C CA  . ASP A 1 48  ? -26.58037 8.20221   30.86584 1.000 41.03211 ? 42  ASP A CA  1 
ATOM   256  C C   . ASP A 1 48  ? -27.84418 7.58661   30.25442 1.000 42.46183 ? 42  ASP A C   1 
ATOM   257  O O   . ASP A 1 48  ? -28.56392 6.81587   30.91081 1.000 41.79437 ? 42  ASP A O   1 
ATOM   258  C CB  . ASP A 1 48  ? -25.74316 7.19197   31.65608 1.000 41.39894 ? 42  ASP A CB  1 
ATOM   259  C CG  . ASP A 1 48  ? -25.35045 5.97896   30.86045 1.000 42.00284 ? 42  ASP A CG  1 
ATOM   260  O OD1 . ASP A 1 48  ? -25.84957 5.78894   29.73657 1.000 42.75251 ? 42  ASP A OD1 1 
ATOM   261  O OD2 . ASP A 1 48  ? -24.55165 5.18927   31.38077 1.000 42.68884 ? 42  ASP A OD2 1 
ATOM   262  N N   . ASN A 1 49  ? -28.09198 7.90674   28.98441 1.000 43.12119 ? 43  ASN A N   1 
ATOM   263  C CA  . ASN A 1 49  ? -29.32069 7.49458   28.31293 1.000 45.09631 ? 43  ASN A CA  1 
ATOM   264  C C   . ASN A 1 49  ? -29.39633 6.00376   28.03290 1.000 46.05578 ? 43  ASN A C   1 
ATOM   265  O O   . ASN A 1 49  ? -30.49515 5.50495   27.78818 1.000 47.15931 ? 43  ASN A O   1 
ATOM   266  C CB  . ASN A 1 49  ? -29.49194 8.27184   27.01309 1.000 45.91203 ? 43  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 49  ? -29.83016 9.72274   27.25902 1.000 46.23900 ? 43  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 49  ? -31.00638 10.07288  27.29406 1.000 47.32417 ? 43  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 49  ? -28.81664 10.56838  27.47186 1.000 45.36836 ? 43  ASN A ND2 1 
ATOM   270  N N   . LEU A 1 50  ? -28.27638 5.28928   28.03298 1.000 45.88589 ? 44  LEU A N   1 
ATOM   271  C CA  . LEU A 1 50  ? -28.29933 3.83487   27.89079 1.000 46.45968 ? 44  LEU A CA  1 
ATOM   272  C C   . LEU A 1 50  ? -28.62816 3.15562   29.21772 1.000 47.52180 ? 44  LEU A C   1 
ATOM   273  O O   . LEU A 1 50  ? -29.59485 2.38354   29.32957 1.000 48.09187 ? 44  LEU A O   1 
ATOM   274  C CB  . LEU A 1 50  ? -26.93666 3.35139   27.39644 1.000 46.86970 ? 44  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 50  ? -26.79621 1.87846   27.04825 1.000 46.85850 ? 44  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 50  ? -27.77090 1.47715   25.95371 1.000 46.58484 ? 44  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 50  ? -25.38295 1.60932   26.61504 1.000 47.06269 ? 44  LEU A CD2 1 
ATOM   278  N N   . ASN A 1 51  ? -27.83323 3.45060   30.24260 1.000 46.78498 ? 45  ASN A N   1 
ATOM   279  C CA  . ASN A 1 51  ? -27.99753 2.76212   31.51427 1.000 46.93686 ? 45  ASN A CA  1 
ATOM   280  C C   . ASN A 1 51  ? -29.08368 3.38653   32.36976 1.000 46.03494 ? 45  ASN A C   1 
ATOM   281  O O   . ASN A 1 51  ? -29.39427 2.83690   33.43053 1.000 45.93218 ? 45  ASN A O   1 
ATOM   282  C CB  . ASN A 1 51  ? -26.67398 2.78423   32.28107 1.000 47.88353 ? 45  ASN A CB  1 
ATOM   283  C CG  . ASN A 1 51  ? -25.72366 1.71370   31.81116 1.000 50.10524 ? 45  ASN A CG  1 
ATOM   284  O OD1 . ASN A 1 51  ? -26.10685 0.81124   31.05121 1.000 51.87435 ? 45  ASN A OD1 1 
ATOM   285  N ND2 . ASN A 1 51  ? -24.46428 1.81433   32.23432 1.000 51.12450 ? 45  ASN A ND2 1 
ATOM   286  N N   . LYS A 1 52  ? -29.58516 4.56241   31.97787 1.000 46.05455 ? 46  LYS A N   1 
ATOM   287  C CA  . LYS A 1 52  ? -30.73119 5.23846   32.61446 1.000 45.70681 ? 46  LYS A CA  1 
ATOM   288  C C   . LYS A 1 52  ? -30.45888 5.58820   34.08048 1.000 44.99074 ? 46  LYS A C   1 
ATOM   289  O O   . LYS A 1 52  ? -31.33033 5.46744   34.95033 1.000 44.41647 ? 46  LYS A O   1 
ATOM   290  C CB  . LYS A 1 52  ? -32.01603 4.41813   32.46104 0.800 45.95150 ? 46  LYS A CB  1 
ATOM   291  C CG  . LYS A 1 52  ? -32.43273 4.25604   31.03438 0.700 46.09670 ? 46  LYS A CG  1 
ATOM   292  C CD  . LYS A 1 52  ? -33.87226 3.76382   30.94451 0.600 46.64096 ? 46  LYS A CD  1 
ATOM   293  C CE  . LYS A 1 52  ? -34.37088 3.79886   29.51452 0.600 47.34794 ? 46  LYS A CE  1 
ATOM   294  N NZ  . LYS A 1 52  ? -35.81409 3.41542   29.39880 0.600 47.52337 ? 46  LYS A NZ  1 
ATOM   295  N N   . VAL A 1 53  ? -29.23402 6.03186   34.34673 1.000 43.60014 ? 47  VAL A N   1 
ATOM   296  C CA  . VAL A 1 53  ? -28.79073 6.52356   35.65084 1.000 43.48760 ? 47  VAL A CA  1 
ATOM   297  C C   . VAL A 1 53  ? -27.91718 7.75310   35.39754 1.000 41.61124 ? 47  VAL A C   1 
ATOM   298  O O   . VAL A 1 53  ? -27.39114 7.95452   34.29710 1.000 40.61958 ? 47  VAL A O   1 
ATOM   299  C CB  . VAL A 1 53  ? -28.00443 5.45738   36.46900 1.000 45.00498 ? 47  VAL A CB  1 
ATOM   300  C CG1 . VAL A 1 53  ? -28.88883 4.24427   36.80367 1.000 46.18779 ? 47  VAL A CG1 1 
ATOM   301  C CG2 . VAL A 1 53  ? -26.77559 5.01689   35.74546 1.000 45.46762 ? 47  VAL A CG2 1 
ATOM   302  N N   . ARG A 1 54  ? -27.78495 8.60639   36.41500 1.000 40.88244 ? 48  ARG A N   1 
ATOM   303  C CA  . ARG A 1 54  ? -26.81928 9.69712   36.30618 1.000 38.97485 ? 48  ARG A CA  1 
ATOM   304  C C   . ARG A 1 54  ? -25.43817 9.18824   36.71952 1.000 36.86337 ? 48  ARG A C   1 
ATOM   305  O O   . ARG A 1 54  ? -25.31511 8.22337   37.48720 1.000 36.27929 ? 48  ARG A O   1 
ATOM   306  C CB  . ARG A 1 54  ? -27.25847 10.92368  37.12972 1.000 39.56347 ? 48  ARG A CB  1 
ATOM   307  C CG  . ARG A 1 54  ? -28.41824 11.73821  36.47152 1.000 41.55360 ? 48  ARG A CG  1 
ATOM   308  C CD  . ARG A 1 54  ? -28.75195 13.07675  37.16794 1.000 42.16307 ? 48  ARG A CD  1 
ATOM   309  N NE  . ARG A 1 54  ? -27.74477 14.12528  37.00224 1.000 42.11809 ? 48  ARG A NE  1 
ATOM   310  C CZ  . ARG A 1 54  ? -27.62100 14.92867  35.94321 1.000 42.86573 ? 48  ARG A CZ  1 
ATOM   311  N NH1 . ARG A 1 54  ? -28.39803 14.80431  34.87233 1.000 43.19100 ? 48  ARG A NH1 1 
ATOM   312  N NH2 . ARG A 1 54  ? -26.68078 15.87665  35.94933 1.000 42.91161 ? 48  ARG A NH2 1 
ATOM   313  N N   . VAL A 1 55  ? -24.39608 9.82894   36.15735 1.000 33.87123 ? 49  VAL A N   1 
ATOM   314  C CA  . VAL A 1 55  ? -22.99931 9.40287   36.26691 1.000 31.86079 ? 49  VAL A CA  1 
ATOM   315  C C   . VAL A 1 55  ? -22.14295 10.63694  36.47769 1.000 30.52075 ? 49  VAL A C   1 
ATOM   316  O O   . VAL A 1 55  ? -22.59402 11.76631  36.29255 1.000 31.11426 ? 49  VAL A O   1 
ATOM   317  C CB  . VAL A 1 55  ? -22.51918 8.65880   35.01164 1.000 31.94001 ? 49  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 55  ? -23.24617 7.34700   34.83058 1.000 32.70863 ? 49  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 55  ? -22.59646 9.59892   33.71963 1.000 31.61687 ? 49  VAL A CG2 1 
ATOM   320  N N   . ALA A 1 56  ? -20.88073 10.40541  36.88311 1.000 29.32511 ? 50  ALA A N   1 
ATOM   321  C CA  . ALA A 1 56  ? -19.84905 11.43277  36.96922 1.000 27.62293 ? 50  ALA A CA  1 
ATOM   322  C C   . ALA A 1 56  ? -18.92458 11.35018  35.75597 1.000 27.27239 ? 50  ALA A C   1 
ATOM   323  O O   . ALA A 1 56  ? -18.56982 10.25215  35.32610 1.000 28.25534 ? 50  ALA A O   1 
ATOM   324  C CB  . ALA A 1 56  ? -19.01505 11.25043  38.23343 1.000 26.60636 ? 50  ALA A CB  1 
ATOM   325  N N   . ILE A 1 57  ? -18.53017 12.50748  35.20704 1.000 26.45856 ? 51  ILE A N   1 
ATOM   326  C CA  . ILE A 1 57  ? -17.63379 12.55210  34.05631 1.000 26.76944 ? 51  ILE A CA  1 
ATOM   327  C C   . ILE A 1 57  ? -16.51545 13.56082  34.31786 1.000 28.06174 ? 51  ILE A C   1 
ATOM   328  O O   . ILE A 1 57  ? -16.77993 14.72284  34.64414 1.000 28.45955 ? 51  ILE A O   1 
ATOM   329  C CB  . ILE A 1 57  ? -18.35604 12.88706  32.75299 1.000 25.41599 ? 51  ILE A CB  1 
ATOM   330  C CG1 . ILE A 1 57  ? -19.57291 11.98805  32.56980 1.000 25.59024 ? 51  ILE A CG1 1 
ATOM   331  C CG2 . ILE A 1 57  ? -17.33804 12.73137  31.62596 1.000 24.11046 ? 51  ILE A CG2 1 
ATOM   332  C CD1 . ILE A 1 57  ? -20.32242 12.17131  31.21143 1.000 25.83213 ? 51  ILE A CD1 1 
ATOM   333  N N   . LYS A 1 58  ? -15.27844 13.09388  34.21570 1.000 27.42834 ? 52  LYS A N   1 
ATOM   334  C CA  . LYS A 1 58  ? -14.06715 13.89033  34.36657 1.000 28.34428 ? 52  LYS A CA  1 
ATOM   335  C C   . LYS A 1 58  ? -13.46057 14.21097  32.98734 1.000 27.90187 ? 52  LYS A C   1 
ATOM   336  O O   . LYS A 1 58  ? -13.13524 13.29404  32.23346 1.000 27.63217 ? 52  LYS A O   1 
ATOM   337  C CB  . LYS A 1 58  ? -13.07909 13.07452  35.21054 1.000 29.43153 ? 52  LYS A CB  1 
ATOM   338  C CG  . LYS A 1 58  ? -11.78072 13.68773  35.41127 1.000 32.46412 ? 52  LYS A CG  1 
ATOM   339  C CD  . LYS A 1 58  ? -10.96197 12.86393  36.42527 1.000 32.70431 ? 52  LYS A CD  1 
ATOM   340  C CE  . LYS A 1 58  ? -10.48881 11.43602  35.95882 1.000 32.26101 ? 52  LYS A CE  1 
ATOM   341  N NZ  . LYS A 1 58  ? -9.53207  10.89603  37.02762 1.000 31.76312 ? 52  LYS A NZ  1 
ATOM   342  N N   . LYS A 1 59  ? -13.26748 15.49438  32.67165 1.000 29.10433 ? 53  LYS A N   1 
ATOM   343  C CA  . LYS A 1 59  ? -12.57303 15.91160  31.43604 1.000 30.83463 ? 53  LYS A CA  1 
ATOM   344  C C   . LYS A 1 59  ? -11.07207 16.07072  31.69657 1.000 31.43147 ? 53  LYS A C   1 
ATOM   345  O O   . LYS A 1 59  ? -10.66414 16.66577  32.71032 1.000 32.03273 ? 53  LYS A O   1 
ATOM   346  C CB  . LYS A 1 59  ? -13.15406 17.22950  30.91132 1.000 31.95779 ? 53  LYS A CB  1 
ATOM   347  C CG  . LYS A 1 59  ? -12.45971 17.81824  29.70473 1.000 33.86677 ? 53  LYS A CG  1 
ATOM   348  C CD  . LYS A 1 59  ? -13.24880 19.08374  29.20523 1.000 36.57006 ? 53  LYS A CD  1 
ATOM   349  C CE  . LYS A 1 59  ? -13.05105 19.32735  27.73495 1.000 39.66245 ? 53  LYS A CE  1 
ATOM   350  N NZ  . LYS A 1 59  ? -11.65148 19.72628  27.48928 1.000 41.19401 ? 53  LYS A NZ  1 
ATOM   351  N N   . ILE A 1 60  ? -10.26456 15.52299  30.80084 1.000 30.78577 ? 54  ILE A N   1 
ATOM   352  C CA  . ILE A 1 60  ? -8.81266  15.47576  30.91043 1.000 31.74303 ? 54  ILE A CA  1 
ATOM   353  C C   . ILE A 1 60  ? -8.26353  16.07341  29.62806 1.000 33.18696 ? 54  ILE A C   1 
ATOM   354  O O   . ILE A 1 60  ? -8.68687  15.66885  28.54623 1.000 31.84601 ? 54  ILE A O   1 
ATOM   355  C CB  . ILE A 1 60  ? -8.31081  14.02525  31.09678 1.000 31.34199 ? 54  ILE A CB  1 
ATOM   356  C CG1 . ILE A 1 60  ? -9.06175  13.35863  32.23315 1.000 32.26144 ? 54  ILE A CG1 1 
ATOM   357  C CG2 . ILE A 1 60  ? -6.79297  13.95702  31.36190 1.000 32.61195 ? 54  ILE A CG2 1 
ATOM   358  C CD1 . ILE A 1 60  ? -8.62451  11.96421  32.45583 1.000 32.63318 ? 54  ILE A CD1 1 
ATOM   359  N N   . SER A 1 61  ? -7.32449  17.03546  29.74062 1.000 34.78517 ? 55  SER A N   1 
ATOM   360  C CA  . SER A 1 61  ? -6.64438  17.62215  28.57631 1.000 37.02741 ? 55  SER A CA  1 
ATOM   361  C C   . SER A 1 61  ? -5.14004  17.57028  28.81828 1.000 37.51033 ? 55  SER A C   1 
ATOM   362  O O   . SER A 1 61  ? -4.54121  18.54156  29.31991 1.000 38.52608 ? 55  SER A O   1 
ATOM   363  C CB  . SER A 1 61  ? -7.11392  19.05912  28.30648 1.000 38.56564 ? 55  SER A CB  1 
ATOM   364  O OG  . SER A 1 61  ? -8.53895  19.13185  28.28995 1.000 39.31721 ? 55  SER A OG  1 
ATOM   365  N N   . PRO A 1 62  ? -4.49687  16.41888  28.53339 1.000 37.53404 ? 56  PRO A N   1 
ATOM   366  C CA  . PRO A 1 62  ? -3.10810  16.21161  28.98764 1.000 37.78244 ? 56  PRO A CA  1 
ATOM   367  C C   . PRO A 1 62  ? -2.01298  16.28802  27.93199 1.000 38.62462 ? 56  PRO A C   1 
ATOM   368  O O   . PRO A 1 62  ? -0.83690  16.15926  28.29169 1.000 39.05915 ? 56  PRO A O   1 
ATOM   369  C CB  . PRO A 1 62  ? -3.16461  14.78610  29.53864 1.000 37.92783 ? 56  PRO A CB  1 
ATOM   370  C CG  . PRO A 1 62  ? -4.06254  14.11775  28.50585 1.000 37.96395 ? 56  PRO A CG  1 
ATOM   371  C CD  . PRO A 1 62  ? -5.14740  15.13978  28.18745 1.000 37.80531 ? 56  PRO A CD  1 
ATOM   372  N N   . PHE A 1 63  ? -2.33710  16.46539  26.64618 1.000 38.64826 ? 57  PHE A N   1 
ATOM   373  C CA  . PHE A 1 63  ? -1.40576  15.99148  25.60919 1.000 39.80042 ? 57  PHE A CA  1 
ATOM   374  C C   . PHE A 1 63  ? -0.22134  16.89246  25.32297 1.000 43.25188 ? 57  PHE A C   1 
ATOM   375  O O   . PHE A 1 63  ? 0.70009   16.45704  24.63075 1.000 44.24478 ? 57  PHE A O   1 
ATOM   376  C CB  . PHE A 1 63  ? -2.15908  15.67935  24.30956 1.000 38.46992 ? 57  PHE A CB  1 
ATOM   377  C CG  . PHE A 1 63  ? -3.24134  14.69187  24.52512 1.000 36.02650 ? 57  PHE A CG  1 
ATOM   378  C CD1 . PHE A 1 63  ? -2.87109  13.39537  24.86745 1.000 35.28757 ? 57  PHE A CD1 1 
ATOM   379  C CD2 . PHE A 1 63  ? -4.60334  15.00324  24.36475 1.000 35.71466 ? 57  PHE A CD2 1 
ATOM   380  C CE1 . PHE A 1 63  ? -3.79629  12.41138  25.08650 1.000 34.43500 ? 57  PHE A CE1 1 
ATOM   381  C CE2 . PHE A 1 63  ? -5.57234  13.99636  24.60199 1.000 35.48826 ? 57  PHE A CE2 1 
ATOM   382  C CZ  . PHE A 1 63  ? -5.15346  12.71297  24.96151 1.000 34.78484 ? 57  PHE A CZ  1 
ATOM   383  N N   . GLU A 1 64  ? -0.21126  18.08703  25.86080 1.000 44.11991 ? 58  GLU A N   1 
ATOM   384  C CA  A GLU A 1 64  ? 0.88577   19.01973  25.69682 0.500 45.66792 ? 58  GLU A CA  1 
ATOM   385  C CA  B GLU A 1 64  ? 0.89757   19.01023  25.68484 0.500 46.10114 ? 58  GLU A CA  1 
ATOM   386  C C   . GLU A 1 64  ? 2.05434   18.74461  26.63351 1.000 46.59914 ? 58  GLU A C   1 
ATOM   387  O O   . GLU A 1 64  ? 3.15574   19.24631  26.37449 1.000 46.46578 ? 58  GLU A O   1 
ATOM   388  C CB  A GLU A 1 64  ? 0.31338   20.42301  25.89414 0.500 45.70625 ? 58  GLU A CB  1 
ATOM   389  C CB  B GLU A 1 64  ? 0.41477   20.44480  25.88850 0.500 46.93957 ? 58  GLU A CB  1 
ATOM   390  C CG  A GLU A 1 64  ? -0.30789  20.63987  27.27990 0.500 45.72070 ? 58  GLU A CG  1 
ATOM   391  C CG  B GLU A 1 64  ? -0.88249  20.74307  25.17782 0.500 47.59207 ? 58  GLU A CG  1 
ATOM   392  C CD  A GLU A 1 64  ? -1.62186  19.84256  27.49159 0.500 45.74779 ? 58  GLU A CD  1 
ATOM   393  C CD  B GLU A 1 64  ? -0.69928  20.97955  23.69786 0.500 48.00939 ? 58  GLU A CD  1 
ATOM   394  O OE1 A GLU A 1 64  ? -2.16007  19.31978  26.50647 0.500 46.57672 ? 58  GLU A OE1 1 
ATOM   395  O OE1 B GLU A 1 64  ? -0.60953  20.00355  22.92184 0.500 48.59847 ? 58  GLU A OE1 1 
ATOM   396  O OE2 A GLU A 1 64  ? -2.12701  19.77675  28.62287 0.500 45.08606 ? 58  GLU A OE2 1 
ATOM   397  O OE2 B GLU A 1 64  ? -0.67584  22.15246  23.30569 0.500 47.97142 ? 58  GLU A OE2 1 
ATOM   398  N N   . HIS A 1 65  ? 1.84769   17.95968  27.70876 1.000 48.03482 ? 59  HIS A N   1 
ATOM   399  C CA  . HIS A 1 65  ? 2.88591   17.76642  28.73044 1.000 48.45782 ? 59  HIS A CA  1 
ATOM   400  C C   . HIS A 1 65  ? 3.13889   16.29828  29.01635 1.000 48.89282 ? 59  HIS A C   1 
ATOM   401  O O   . HIS A 1 65  ? 2.19913   15.54750  29.30848 1.000 47.84965 ? 59  HIS A O   1 
ATOM   402  C CB  . HIS A 1 65  ? 2.52134   18.47484  30.01921 0.900 48.36311 ? 59  HIS A CB  1 
ATOM   403  C CG  . HIS A 1 65  ? 2.34083   19.93666  29.82848 0.800 48.94914 ? 59  HIS A CG  1 
ATOM   404  N ND1 . HIS A 1 65  ? 3.39363   20.77065  29.51331 0.700 49.47668 ? 59  HIS A ND1 1 
ATOM   405  C CD2 . HIS A 1 65  ? 1.25075   20.72607  29.94025 0.700 48.94323 ? 59  HIS A CD2 1 
ATOM   406  C CE1 . HIS A 1 65  ? 2.94630   22.00727  29.39051 0.700 49.51130 ? 59  HIS A CE1 1 
ATOM   407  N NE2 . HIS A 1 65  ? 1.64978   22.00755  29.64466 0.700 49.16083 ? 59  HIS A NE2 1 
ATOM   408  N N   . GLN A 1 66  ? 4.41245   15.90524  28.92962 1.000 49.20232 ? 60  GLN A N   1 
ATOM   409  C CA  . GLN A 1 66  ? 4.77980   14.51071  29.14034 1.000 48.87586 ? 60  GLN A CA  1 
ATOM   410  C C   . GLN A 1 66  ? 4.30166   14.02753  30.49601 1.000 47.82902 ? 60  GLN A C   1 
ATOM   411  O O   . GLN A 1 66  ? 3.89374   12.86866  30.62630 1.000 46.23216 ? 60  GLN A O   1 
ATOM   412  C CB  . GLN A 1 66  ? 6.30520   14.31854  29.03591 1.000 49.41304 ? 60  GLN A CB  1 
ATOM   413  C CG  . GLN A 1 66  ? 6.70409   12.89361  28.65152 0.800 50.67862 ? 60  GLN A CG  1 
ATOM   414  C CD  . GLN A 1 66  ? 7.49916   12.19908  29.71925 0.700 52.62067 ? 60  GLN A CD  1 
ATOM   415  O OE1 . GLN A 1 66  ? 8.22048   12.83709  30.46931 0.700 53.65610 ? 60  GLN A OE1 1 
ATOM   416  N NE2 . GLN A 1 66  ? 7.38108   10.87773  29.79117 0.700 53.89743 ? 60  GLN A NE2 1 
ATOM   417  N N   . THR A 1 67  ? 4.33354   14.90055  31.51521 1.000 48.19647 ? 61  THR A N   1 
ATOM   418  C CA  . THR A 1 67  ? 3.95681   14.47136  32.86669 1.000 48.67896 ? 61  THR A CA  1 
ATOM   419  C C   . THR A 1 67  ? 2.45046   14.34206  33.02675 1.000 46.95525 ? 61  THR A C   1 
ATOM   420  O O   . THR A 1 67  ? 1.98462   13.47686  33.78954 1.000 46.60860 ? 61  THR A O   1 
ATOM   421  C CB  . THR A 1 67  ? 4.54067   15.41386  33.94090 1.000 50.77216 ? 61  THR A CB  1 
ATOM   422  O OG1 . THR A 1 67  ? 4.08931   16.76726  33.74435 1.000 52.68752 ? 61  THR A OG1 1 
ATOM   423  C CG2 . THR A 1 67  ? 6.05075   15.37407  33.91623 1.000 50.20948 ? 61  THR A CG2 1 
ATOM   424  N N   . TYR A 1 68  ? 1.67626   15.15865  32.30561 1.000 45.31497 ? 62  TYR A N   1 
ATOM   425  C CA  . TYR A 1 68  ? 0.23101   15.00003  32.36810 1.000 43.83055 ? 62  TYR A CA  1 
ATOM   426  C C   . TYR A 1 68  ? -0.16238  13.70262  31.69051 1.000 41.82562 ? 62  TYR A C   1 
ATOM   427  O O   . TYR A 1 68  ? -1.01127  12.95844  32.19619 1.000 41.06759 ? 62  TYR A O   1 
ATOM   428  C CB  . TYR A 1 68  ? -0.47631  16.16739  31.68767 0.900 45.52866 ? 62  TYR A CB  1 
ATOM   429  C CG  . TYR A 1 68  ? -0.36450  17.52762  32.34727 0.800 46.97617 ? 62  TYR A CG  1 
ATOM   430  C CD1 . TYR A 1 68  ? 0.24123   17.69042  33.59214 0.700 47.89012 ? 62  TYR A CD1 1 
ATOM   431  C CD2 . TYR A 1 68  ? -0.91053  18.65451  31.72554 0.700 47.74420 ? 62  TYR A CD2 1 
ATOM   432  C CE1 . TYR A 1 68  ? 0.32630   18.94820  34.19396 0.700 48.81986 ? 62  TYR A CE1 1 
ATOM   433  C CE2 . TYR A 1 68  ? -0.83471  19.91089  32.31321 0.700 48.63317 ? 62  TYR A CE2 1 
ATOM   434  C CZ  . TYR A 1 68  ? -0.21981  20.05261  33.55023 0.700 49.27885 ? 62  TYR A CZ  1 
ATOM   435  O OH  . TYR A 1 68  ? -0.14607  21.30667  34.12116 0.700 50.11985 ? 62  TYR A OH  1 
ATOM   436  N N   . CYS A 1 69  ? 0.43862   13.43947  30.52556 1.000 40.69247 ? 63  CYS A N   1 
ATOM   437  C CA  . CYS A 1 69  ? 0.19784   12.19747  29.81655 1.000 40.01246 ? 63  CYS A CA  1 
ATOM   438  C C   . CYS A 1 69  ? 0.56503   11.01315  30.67866 1.000 37.88372 ? 63  CYS A C   1 
ATOM   439  O O   . CYS A 1 69  ? -0.09900  9.97640   30.62475 1.000 37.09749 ? 63  CYS A O   1 
ATOM   440  C CB  . CYS A 1 69  ? 0.99046   12.17100  28.51093 1.000 40.56768 ? 63  CYS A CB  1 
ATOM   441  S SG  . CYS A 1 69  ? 0.37659   13.30928  27.32989 1.000 41.96014 ? 63  CYS A SG  1 
ATOM   442  N N   . GLN A 1 70  ? 1.62582   11.14579  31.47492 1.000 37.13813 ? 64  GLN A N   1 
ATOM   443  C CA  . GLN A 1 70  ? 2.04683   10.03727  32.31916 1.000 37.38155 ? 64  GLN A CA  1 
ATOM   444  C C   . GLN A 1 70  ? 0.98016   9.71553   33.35937 1.000 35.88217 ? 64  GLN A C   1 
ATOM   445  O O   . GLN A 1 70  ? 0.57928   8.55735   33.51142 1.000 36.17076 ? 64  GLN A O   1 
ATOM   446  C CB  . GLN A 1 70  ? 3.35019   10.38509  33.04607 0.800 37.96022 ? 64  GLN A CB  1 
ATOM   447  C CG  . GLN A 1 70  ? 4.65138   10.17592  32.29938 0.700 39.90113 ? 64  GLN A CG  1 
ATOM   448  C CD  . GLN A 1 70  ? 5.74931   11.07433  32.88052 0.600 41.95317 ? 64  GLN A CD  1 
ATOM   449  O OE1 . GLN A 1 70  ? 6.93028   10.91552  32.57561 0.600 41.77163 ? 64  GLN A OE1 1 
ATOM   450  N NE2 . GLN A 1 70  ? 5.36829   11.93269  33.82819 0.600 42.98197 ? 64  GLN A NE2 1 
ATOM   451  N N   . ARG A 1 71  ? 0.52070   10.74441  34.08682 1.000 34.86512 ? 65  ARG A N   1 
ATOM   452  C CA  . ARG A 1 71  ? -0.48952  10.56608  35.13623 1.000 34.59767 ? 65  ARG A CA  1 
ATOM   453  C C   . ARG A 1 71  ? -1.75399  9.95277   34.54769 1.000 33.11639 ? 65  ARG A C   1 
ATOM   454  O O   . ARG A 1 71  ? -2.38236  9.07490   35.16147 1.000 32.29760 ? 65  ARG A O   1 
ATOM   455  C CB  . ARG A 1 71  ? -0.78577  11.92960  35.79112 0.800 35.23418 ? 65  ARG A CB  1 
ATOM   456  C CG  . ARG A 1 71  ? -1.51917  11.93601  37.13900 0.700 36.95547 ? 65  ARG A CG  1 
ATOM   457  C CD  . ARG A 1 71  ? -1.72266  13.35811  37.77985 0.600 37.47119 ? 65  ARG A CD  1 
ATOM   458  N NE  . ARG A 1 71  ? -2.86070  13.36850  38.69667 0.600 37.69500 ? 65  ARG A NE  1 
ATOM   459  C CZ  . ARG A 1 71  ? -2.97916  14.12583  39.78249 0.600 37.65457 ? 65  ARG A CZ  1 
ATOM   460  N NH1 . ARG A 1 71  ? -2.06584  15.04257  40.09898 0.600 37.89377 ? 65  ARG A NH1 1 
ATOM   461  N NH2 . ARG A 1 71  ? -4.04721  13.97405  40.56554 0.600 37.35196 ? 65  ARG A NH2 1 
ATOM   462  N N   . THR A 1 72  ? -2.13068  10.40166  33.34381 1.000 33.19826 ? 66  THR A N   1 
ATOM   463  C CA  . THR A 1 72  ? -3.37755  9.95323   32.72412 1.000 31.06483 ? 66  THR A CA  1 
ATOM   464  C C   . THR A 1 72  ? -3.27154  8.50061   32.30356 1.000 28.48589 ? 66  THR A C   1 
ATOM   465  O O   . THR A 1 72  ? -4.16652  7.69349   32.56274 1.000 27.35858 ? 66  THR A O   1 
ATOM   466  C CB  . THR A 1 72  ? -3.68739  10.81258  31.49745 1.000 31.72094 ? 66  THR A CB  1 
ATOM   467  O OG1 . THR A 1 72  ? -3.85736  12.18034  31.90631 1.000 33.10053 ? 66  THR A OG1 1 
ATOM   468  C CG2 . THR A 1 72  ? -4.97571  10.33028  30.78529 1.000 31.41556 ? 66  THR A CG2 1 
ATOM   469  N N   . LEU A 1 73  ? -2.16844  8.15469   31.65192 1.000 27.38343 ? 67  LEU A N   1 
ATOM   470  C CA  . LEU A 1 73  ? -1.97125  6.78283   31.22156 1.000 27.81717 ? 67  LEU A CA  1 
ATOM   471  C C   . LEU A 1 73  ? -1.90371  5.84131   32.42768 1.000 27.18954 ? 67  LEU A C   1 
ATOM   472  O O   . LEU A 1 73  ? -2.52704  4.77293   32.42106 1.000 25.61679 ? 67  LEU A O   1 
ATOM   473  C CB  . LEU A 1 73  ? -0.67689  6.69016   30.39770 1.000 27.88845 ? 67  LEU A CB  1 
ATOM   474  C CG  . LEU A 1 73  ? -0.43453  5.37580   29.67933 1.000 28.48677 ? 67  LEU A CG  1 
ATOM   475  C CD1 . LEU A 1 73  ? -1.65745  4.78966   28.93408 1.000 28.18250 ? 67  LEU A CD1 1 
ATOM   476  C CD2 . LEU A 1 73  ? 0.83910   5.43483   28.81068 1.000 30.67691 ? 67  LEU A CD2 1 
ATOM   477  N N   . ARG A 1 74  ? -1.08776  6.19545   33.44576 1.000 27.58434 ? 68  ARG A N   1 
ATOM   478  C CA  . ARG A 1 74  ? -0.98058  5.39625   34.65380 1.000 27.79696 ? 68  ARG A CA  1 
ATOM   479  C C   . ARG A 1 74  ? -2.35159  5.06086   35.22730 1.000 25.74963 ? 68  ARG A C   1 
ATOM   480  O O   . ARG A 1 74  ? -2.64497  3.89069   35.52287 1.000 25.62771 ? 68  ARG A O   1 
ATOM   481  C CB  . ARG A 1 74  ? -0.13757  6.15881   35.70691 0.800 30.93236 ? 68  ARG A CB  1 
ATOM   482  C CG  . ARG A 1 74  ? 0.26922   5.38291   36.91799 0.800 34.39594 ? 68  ARG A CG  1 
ATOM   483  C CD  . ARG A 1 74  ? 1.75599   5.51567   37.12339 0.800 36.34289 ? 68  ARG A CD  1 
ATOM   484  N NE  . ARG A 1 74  ? 2.15591   6.91770   37.02684 0.800 37.48007 ? 68  ARG A NE  1 
ATOM   485  C CZ  . ARG A 1 74  ? 3.35811   7.30828   36.63554 0.800 38.42531 ? 68  ARG A CZ  1 
ATOM   486  N NH1 . ARG A 1 74  ? 4.29055   6.42869   36.29303 0.800 39.69351 ? 68  ARG A NH1 1 
ATOM   487  N NH2 . ARG A 1 74  ? 3.62274   8.60847   36.55489 0.800 38.35587 ? 68  ARG A NH2 1 
ATOM   488  N N   . GLU A 1 75  ? -3.21325  6.07839   35.38780 1.000 24.13167 ? 69  GLU A N   1 
ATOM   489  C CA  . GLU A 1 75  ? -4.49885  5.82346   36.01563 1.000 23.09024 ? 69  GLU A CA  1 
ATOM   490  C C   . GLU A 1 75  ? -5.37000  4.94187   35.13401 1.000 21.73021 ? 69  GLU A C   1 
ATOM   491  O O   . GLU A 1 75  ? -6.05731  4.03566   35.63063 1.000 20.93958 ? 69  GLU A O   1 
ATOM   492  C CB  . GLU A 1 75  ? -5.26972  7.11109   36.26795 1.000 25.99064 ? 69  GLU A CB  1 
ATOM   493  C CG  . GLU A 1 75  ? -6.67802  6.80223   36.76569 1.000 28.83355 ? 69  GLU A CG  1 
ATOM   494  C CD  . GLU A 1 75  ? -7.43469  8.00664   37.26432 1.000 29.61385 ? 69  GLU A CD  1 
ATOM   495  O OE1 . GLU A 1 75  ? -7.67160  8.93591   36.43687 1.000 30.79309 ? 69  GLU A OE1 1 
ATOM   496  O OE2 . GLU A 1 75  ? -7.76582  8.05688   38.46239 1.000 28.44237 ? 69  GLU A OE2 1 
ATOM   497  N N   . ILE A 1 76  ? -5.41212  5.23180   33.82330 1.000 20.69214 ? 70  ILE A N   1 
ATOM   498  C CA  . ILE A 1 76  ? -6.24864  4.41176   32.93578 1.000 21.61150 ? 70  ILE A CA  1 
ATOM   499  C C   . ILE A 1 76  ? -5.78427  2.96960   32.97196 1.000 21.76261 ? 70  ILE A C   1 
ATOM   500  O O   . ILE A 1 76  ? -6.59958  2.04893   33.11807 1.000 22.47689 ? 70  ILE A O   1 
ATOM   501  C CB  . ILE A 1 76  ? -6.23331  4.97262   31.49649 1.000 22.13115 ? 70  ILE A CB  1 
ATOM   502  C CG1 . ILE A 1 76  ? -6.95054  6.30819   31.48595 1.000 22.26424 ? 70  ILE A CG1 1 
ATOM   503  C CG2 . ILE A 1 76  ? -6.83936  3.93443   30.52502 1.000 23.24881 ? 70  ILE A CG2 1 
ATOM   504  C CD1 . ILE A 1 76  ? -6.89980  7.01360   30.11851 1.000 23.93234 ? 70  ILE A CD1 1 
ATOM   505  N N   . LYS A 1 77  ? -4.45709  2.74333   32.92868 1.000 21.46609 ? 71  LYS A N   1 
ATOM   506  C CA  . LYS A 1 77  ? -3.99402  1.36539   32.88667 1.000 23.27039 ? 71  LYS A CA  1 
ATOM   507  C C   . LYS A 1 77  ? -4.33553  0.61794   34.17909 1.000 23.90708 ? 71  LYS A C   1 
ATOM   508  O O   . LYS A 1 77  ? -4.77088  -0.54982  34.13951 1.000 26.17458 ? 71  LYS A O   1 
ATOM   509  C CB  . LYS A 1 77  ? -2.48072  1.32127   32.62791 0.900 23.59236 ? 71  LYS A CB  1 
ATOM   510  C CG  . LYS A 1 77  ? -2.05602  1.50943   31.18018 0.800 26.35711 ? 71  LYS A CG  1 
ATOM   511  C CD  . LYS A 1 77  ? -0.54075  1.54238   31.10842 0.700 28.31448 ? 71  LYS A CD  1 
ATOM   512  C CE  . LYS A 1 77  ? 0.07323   0.18111   30.80208 0.600 29.72101 ? 71  LYS A CE  1 
ATOM   513  N NZ  . LYS A 1 77  ? -0.18000  -0.32911  29.41277 0.600 30.71690 ? 71  LYS A NZ  1 
ATOM   514  N N   . ILE A 1 78  ? -4.17657  1.27088   35.33318 1.000 21.58544 ? 72  ILE A N   1 
ATOM   515  C CA  . ILE A 1 78  ? -4.48611  0.62245   36.60909 1.000 21.24770 ? 72  ILE A CA  1 
ATOM   516  C C   . ILE A 1 78  ? -5.98199  0.34007   36.73033 1.000 22.42365 ? 72  ILE A C   1 
ATOM   517  O O   . ILE A 1 78  ? -6.40363  -0.78898  37.04887 1.000 22.36279 ? 72  ILE A O   1 
ATOM   518  C CB  . ILE A 1 78  ? -3.99667  1.51628   37.77333 1.000 21.45018 ? 72  ILE A CB  1 
ATOM   519  C CG1 . ILE A 1 78  ? -2.44884  1.56251   37.80546 1.000 22.32282 ? 72  ILE A CG1 1 
ATOM   520  C CG2 . ILE A 1 78  ? -4.64111  1.08618   39.07873 1.000 22.00549 ? 72  ILE A CG2 1 
ATOM   521  C CD1 . ILE A 1 78  ? -1.86555  2.64242   38.67519 1.000 22.89845 ? 72  ILE A CD1 1 
ATOM   522  N N   . LEU A 1 79  ? -6.81451  1.36598   36.49132 1.000 20.93501 ? 73  LEU A N   1 
ATOM   523  C CA  . LEU A 1 79  ? -8.25858  1.19838   36.68997 1.000 22.62984 ? 73  LEU A CA  1 
ATOM   524  C C   . LEU A 1 79  ? -8.91954  0.24560   35.71664 1.000 25.27383 ? 73  LEU A C   1 
ATOM   525  O O   . LEU A 1 79  ? -9.95287  -0.34243  36.06083 1.000 27.43559 ? 73  LEU A O   1 
ATOM   526  C CB  . LEU A 1 79  ? -8.94088  2.54165   36.62991 1.000 23.19628 ? 73  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 79  ? -8.67025  3.33188   37.91409 1.000 24.51655 ? 73  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 79  ? -9.44264  4.57925   37.85156 1.000 26.03980 ? 73  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 79  ? -8.99642  2.57981   39.23199 1.000 25.78145 ? 73  LEU A CD2 1 
ATOM   530  N N   . LEU A 1 80  ? -8.40744  0.09601   34.49472 1.000 25.64878 ? 74  LEU A N   1 
ATOM   531  C CA  . LEU A 1 80  ? -9.00512  -0.89793  33.60861 1.000 27.21308 ? 74  LEU A CA  1 
ATOM   532  C C   . LEU A 1 80  ? -8.64375  -2.32589  34.01190 1.000 26.78140 ? 74  LEU A C   1 
ATOM   533  O O   . LEU A 1 80  ? -9.33472  -3.27421  33.60764 1.000 28.10471 ? 74  LEU A O   1 
ATOM   534  C CB  . LEU A 1 80  ? -8.60090  -0.59141  32.15744 1.000 28.51335 ? 74  LEU A CB  1 
ATOM   535  C CG  . LEU A 1 80  ? -9.23678  0.69157   31.58143 1.000 29.04411 ? 74  LEU A CG  1 
ATOM   536  C CD1 . LEU A 1 80  ? -8.89508  0.83042   30.09797 1.000 30.18136 ? 74  LEU A CD1 1 
ATOM   537  C CD2 . LEU A 1 80  ? -10.75530 0.74034   31.73716 1.000 29.48912 ? 74  LEU A CD2 1 
ATOM   538  N N   . ARG A 1 81  ? -7.61430  -2.50985  34.81944 1.000 24.93651 ? 75  ARG A N   1 
ATOM   539  C CA  . ARG A 1 81  ? -7.37006  -3.86308  35.30001 1.000 24.42604 ? 75  ARG A CA  1 
ATOM   540  C C   . ARG A 1 81  ? -8.03716  -4.15339  36.64743 1.000 24.43451 ? 75  ARG A C   1 
ATOM   541  O O   . ARG A 1 81  ? -8.42335  -5.30544  36.92322 1.000 27.18475 ? 75  ARG A O   1 
ATOM   542  C CB  . ARG A 1 81  ? -5.86892  -4.11248  35.39900 0.800 25.26484 ? 75  ARG A CB  1 
ATOM   543  C CG  . ARG A 1 81  ? -5.59453  -5.55274  35.72804 0.700 26.03580 ? 75  ARG A CG  1 
ATOM   544  C CD  . ARG A 1 81  ? -4.14414  -5.78545  35.98048 0.600 25.56895 ? 75  ARG A CD  1 
ATOM   545  N NE  . ARG A 1 81  ? -3.36298  -5.63538  34.76072 0.500 24.71356 ? 75  ARG A NE  1 
ATOM   546  C CZ  . ARG A 1 81  ? -2.09230  -5.98577  34.66493 0.500 24.86657 ? 75  ARG A CZ  1 
ATOM   547  N NH1 . ARG A 1 81  ? -1.48090  -6.62143  35.64561 0.500 24.21882 ? 75  ARG A NH1 1 
ATOM   548  N NH2 . ARG A 1 81  ? -1.41376  -5.66537  33.56852 0.500 25.33972 ? 75  ARG A NH2 1 
ATOM   549  N N   . PHE A 1 82  ? -8.19076  -3.15453  37.48374 1.000 21.10518 ? 76  PHE A N   1 
ATOM   550  C CA  . PHE A 1 82  ? -8.73542  -3.35058  38.82804 1.000 19.28788 ? 76  PHE A CA  1 
ATOM   551  C C   . PHE A 1 82  ? -10.24184 -3.54622  38.74870 1.000 19.72371 ? 76  PHE A C   1 
ATOM   552  O O   . PHE A 1 82  ? -10.91952 -2.88567  37.95306 1.000 20.36569 ? 76  PHE A O   1 
ATOM   553  C CB  . PHE A 1 82  ? -8.48122  -2.12632  39.69443 1.000 18.52664 ? 76  PHE A CB  1 
ATOM   554  C CG  . PHE A 1 82  ? -7.08064  -2.03218  40.30207 1.000 19.21664 ? 76  PHE A CG  1 
ATOM   555  C CD1 . PHE A 1 82  ? -6.07429  -2.93981  39.97290 1.000 19.49486 ? 76  PHE A CD1 1 
ATOM   556  C CD2 . PHE A 1 82  ? -6.79947  -1.00139  41.19817 1.000 18.12523 ? 76  PHE A CD2 1 
ATOM   557  C CE1 . PHE A 1 82  ? -4.81615  -2.84603  40.55343 1.000 19.92679 ? 76  PHE A CE1 1 
ATOM   558  C CE2 . PHE A 1 82  ? -5.53108  -0.88124  41.76620 1.000 19.66053 ? 76  PHE A CE2 1 
ATOM   559  C CZ  . PHE A 1 82  ? -4.55028  -1.80601  41.44438 1.000 19.77575 ? 76  PHE A CZ  1 
ATOM   560  N N   . ARG A 1 83  ? -10.76690 -4.39898  39.61857 1.000 19.89691 ? 77  ARG A N   1 
ATOM   561  C CA  . ARG A 1 83  ? -12.20979 -4.50104  39.83753 1.000 20.97734 ? 77  ARG A CA  1 
ATOM   562  C C   . ARG A 1 83  ? -12.44335 -4.75194  41.31903 1.000 19.27470 ? 77  ARG A C   1 
ATOM   563  O O   . ARG A 1 83  ? -12.12840 -5.83108  41.78615 1.000 20.29951 ? 77  ARG A O   1 
ATOM   564  C CB  A ARG A 1 83  ? -12.83490 -5.60749  38.98662 0.500 22.74796 ? 77  ARG A CB  1 
ATOM   565  C CB  B ARG A 1 83  ? -12.81060 -5.64919  39.02606 0.500 23.70468 ? 77  ARG A CB  1 
ATOM   566  C CG  A ARG A 1 83  ? -14.35394 -5.62385  39.06784 0.500 24.47223 ? 77  ARG A CG  1 
ATOM   567  C CG  B ARG A 1 83  ? -13.12323 -5.33034  37.59556 0.500 26.51881 ? 77  ARG A CG  1 
ATOM   568  C CD  A ARG A 1 83  ? -14.98381 -6.62242  38.09663 0.500 27.75921 ? 77  ARG A CD  1 
ATOM   569  C CD  B ARG A 1 83  ? -12.06719 -5.85255  36.63334 0.500 28.88136 ? 77  ARG A CD  1 
ATOM   570  N NE  A ARG A 1 83  ? -14.91433 -7.97858  38.61411 0.500 30.94800 ? 77  ARG A NE  1 
ATOM   571  N NE  B ARG A 1 83  ? -12.48118 -5.57454  35.26360 0.500 30.19484 ? 77  ARG A NE  1 
ATOM   572  C CZ  A ARG A 1 83  ? -14.03950 -8.90123  38.23938 0.500 32.49409 ? 77  ARG A CZ  1 
ATOM   573  C CZ  B ARG A 1 83  ? -12.33177 -4.40559  34.66255 0.500 30.50103 ? 77  ARG A CZ  1 
ATOM   574  N NH1 A ARG A 1 83  ? -13.17246 -8.68062  37.26292 0.500 33.77075 ? 77  ARG A NH1 1 
ATOM   575  N NH1 B ARG A 1 83  ? -11.77919 -3.37645  35.28152 0.500 29.82412 ? 77  ARG A NH1 1 
ATOM   576  N NH2 A ARG A 1 83  ? -14.04572 -10.08072 38.85282 0.500 32.60362 ? 77  ARG A NH2 1 
ATOM   577  N NH2 B ARG A 1 83  ? -12.73196 -4.27182  33.40426 0.500 31.74132 ? 77  ARG A NH2 1 
ATOM   578  N N   . HIS A 1 84  ? -13.01743 -3.79609  42.04147 1.000 18.11767 ? 78  HIS A N   1 
ATOM   579  C CA  . HIS A 1 84  ? -13.19937 -3.96269  43.48074 1.000 17.03521 ? 78  HIS A CA  1 
ATOM   580  C C   . HIS A 1 84  ? -14.29922 -3.04194  43.97961 1.000 16.69396 ? 78  HIS A C   1 
ATOM   581  O O   . HIS A 1 84  ? -14.39107 -1.91284  43.53885 1.000 16.77159 ? 78  HIS A O   1 
ATOM   582  C CB  . HIS A 1 84  ? -11.88639 -3.65143  44.22700 1.000 16.06791 ? 78  HIS A CB  1 
ATOM   583  C CG  . HIS A 1 84  ? -11.90396 -4.04853  45.67160 1.000 15.20288 ? 78  HIS A CG  1 
ATOM   584  N ND1 . HIS A 1 84  ? -12.42885 -3.23122  46.65615 1.000 15.13442 ? 78  HIS A ND1 1 
ATOM   585  C CD2 . HIS A 1 84  ? -11.45911 -5.17237  46.29848 1.000 15.11953 ? 78  HIS A CD2 1 
ATOM   586  C CE1 . HIS A 1 84  ? -12.34805 -3.85901  47.82005 1.000 15.27193 ? 78  HIS A CE1 1 
ATOM   587  N NE2 . HIS A 1 84  ? -11.74244 -5.02709  47.63560 1.000 15.26426 ? 78  HIS A NE2 1 
ATOM   588  N N   . GLU A 1 85  ? -15.11293 -3.52683  44.93538 1.000 17.40382 ? 79  GLU A N   1 
ATOM   589  C CA  . GLU A 1 85  ? -16.25806 -2.74064  45.41855 1.000 16.57006 ? 79  GLU A CA  1 
ATOM   590  C C   . GLU A 1 85  ? -15.85610 -1.40433  46.02935 1.000 16.49825 ? 79  GLU A C   1 
ATOM   591  O O   . GLU A 1 85  ? -16.65718 -0.46595  46.04149 1.000 16.77337 ? 79  GLU A O   1 
ATOM   592  C CB  . GLU A 1 85  ? -17.01983 -3.54612  46.45985 0.900 18.57105 ? 79  GLU A CB  1 
ATOM   593  C CG  . GLU A 1 85  ? -17.76055 -4.76949  45.89361 0.800 20.77856 ? 79  GLU A CG  1 
ATOM   594  C CD  . GLU A 1 85  ? -18.55937 -5.53233  46.98762 0.700 23.03959 ? 79  GLU A CD  1 
ATOM   595  O OE1 . GLU A 1 85  ? -18.25347 -5.34063  48.18565 0.700 24.01015 ? 79  GLU A OE1 1 
ATOM   596  O OE2 . GLU A 1 85  ? -19.50710 -6.29817  46.65045 0.700 25.10064 ? 79  GLU A OE2 1 
ATOM   597  N N   . ASN A 1 86  ? -14.62907 -1.30418  46.58771 1.000 14.68455 ? 80  ASN A N   1 
ATOM   598  C CA  . ASN A 1 86  ? -14.19816 -0.09553  47.27790 1.000 13.44638 ? 80  ASN A CA  1 
ATOM   599  C C   . ASN A 1 86  ? -13.19373 0.70649   46.46276 1.000 14.31510 ? 80  ASN A C   1 
ATOM   600  O O   . ASN A 1 86  ? -12.46702 1.54557   47.02888 1.000 14.87194 ? 80  ASN A O   1 
ATOM   601  C CB  . ASN A 1 86  ? -13.61215 -0.42696  48.66818 1.000 15.26405 ? 80  ASN A CB  1 
ATOM   602  C CG  . ASN A 1 86  ? -14.59405 -1.16706  49.55505 1.000 15.05882 ? 80  ASN A CG  1 
ATOM   603  O OD1 . ASN A 1 86  ? -14.34136 -2.33232  49.92862 1.000 15.45259 ? 80  ASN A OD1 1 
ATOM   604  N ND2 . ASN A 1 86  ? -15.72127 -0.52236  49.90124 1.000 15.48583 ? 80  ASN A ND2 1 
ATOM   605  N N   . ILE A 1 87  ? -13.18995 0.51942   45.13009 1.000 14.11115 ? 81  ILE A N   1 
ATOM   606  C CA  . ILE A 1 87  ? -12.38810 1.31420   44.21895 1.000 14.97385 ? 81  ILE A CA  1 
ATOM   607  C C   . ILE A 1 87  ? -13.29626 1.80391   43.09688 1.000 15.90522 ? 81  ILE A C   1 
ATOM   608  O O   . ILE A 1 87  ? -14.05665 1.00339   42.50468 1.000 15.93821 ? 81  ILE A O   1 
ATOM   609  C CB  . ILE A 1 87  ? -11.18631 0.51362   43.64221 1.000 14.10791 ? 81  ILE A CB  1 
ATOM   610  C CG1 . ILE A 1 87  ? -10.26953 -0.00443  44.78439 1.000 14.77040 ? 81  ILE A CG1 1 
ATOM   611  C CG2 . ILE A 1 87  ? -10.44765 1.39877   42.57596 1.000 16.03991 ? 81  ILE A CG2 1 
ATOM   612  C CD1 . ILE A 1 87  ? -9.22489  -1.00677  44.28798 1.000 16.17551 ? 81  ILE A CD1 1 
ATOM   613  N N   . ILE A 1 88  ? -13.26364 3.10378   42.80320 1.000 16.71361 ? 82  ILE A N   1 
ATOM   614  C CA  . ILE A 1 88  ? -14.23470 3.53488   41.78369 1.000 19.67733 ? 82  ILE A CA  1 
ATOM   615  C C   . ILE A 1 88  ? -13.67893 3.12813   40.42934 1.000 20.71277 ? 82  ILE A C   1 
ATOM   616  O O   . ILE A 1 88  ? -12.49787 3.33188   40.13371 1.000 24.96843 ? 82  ILE A O   1 
ATOM   617  C CB  . ILE A 1 88  ? -14.55765 5.03511   41.88899 1.000 24.71853 ? 82  ILE A CB  1 
ATOM   618  C CG1 . ILE A 1 88  ? -15.60435 5.41794   40.80771 1.000 26.39479 ? 82  ILE A CG1 1 
ATOM   619  C CG2 . ILE A 1 88  ? -13.36249 5.88284   41.74627 1.000 27.44166 ? 82  ILE A CG2 1 
ATOM   620  C CD1 . ILE A 1 88  ? -16.73568 6.53970   41.19717 1.000 28.09519 ? 82  ILE A CD1 1 
ATOM   621  N N   . GLY A 1 89  ? -14.49628 2.48401   39.62609 1.000 19.23303 ? 83  GLY A N   1 
ATOM   622  C CA  . GLY A 1 89  ? -14.04862 1.97923   38.33899 1.000 20.39004 ? 83  GLY A CA  1 
ATOM   623  C C   . GLY A 1 89  ? -14.28738 2.95800   37.20053 1.000 22.13303 ? 83  GLY A C   1 
ATOM   624  O O   . GLY A 1 89  ? -14.87844 4.01470   37.36017 1.000 23.60670 ? 83  GLY A O   1 
ATOM   625  N N   . ILE A 1 90  ? -13.82150 2.57731   36.02724 1.000 20.97271 ? 84  ILE A N   1 
ATOM   626  C CA  . ILE A 1 90  ? -14.08360 3.33191   34.80007 1.000 20.93042 ? 84  ILE A CA  1 
ATOM   627  C C   . ILE A 1 90  ? -15.21216 2.63584   34.05898 1.000 22.94700 ? 84  ILE A C   1 
ATOM   628  O O   . ILE A 1 90  ? -15.06429 1.47972   33.65542 1.000 25.10431 ? 84  ILE A O   1 
ATOM   629  C CB  . ILE A 1 90  ? -12.83721 3.44310   33.91478 1.000 21.01189 ? 84  ILE A CB  1 
ATOM   630  C CG1 . ILE A 1 90  ? -11.77722 4.30920   34.58659 1.000 21.10777 ? 84  ILE A CG1 1 
ATOM   631  C CG2 . ILE A 1 90  ? -13.21783 3.96850   32.48405 1.000 21.01334 ? 84  ILE A CG2 1 
ATOM   632  C CD1 . ILE A 1 90  ? -10.40629 4.31433   33.87459 1.000 21.43898 ? 84  ILE A CD1 1 
ATOM   633  N N   . ASN A 1 91  ? -16.32497 3.34631   33.86874 1.000 22.41501 ? 85  ASN A N   1 
ATOM   634  C CA  . ASN A 1 91  ? -17.48230 2.81186   33.15663 1.000 25.17354 ? 85  ASN A CA  1 
ATOM   635  C C   . ASN A 1 91  ? -17.37921 2.97269   31.64125 1.000 24.35189 ? 85  ASN A C   1 
ATOM   636  O O   . ASN A 1 91  ? -17.91258 2.13645   30.87569 1.000 26.10453 ? 85  ASN A O   1 
ATOM   637  C CB  . ASN A 1 91  ? -18.76721 3.51683   33.61553 1.000 27.45183 ? 85  ASN A CB  1 
ATOM   638  C CG  . ASN A 1 91  ? -19.05758 3.35028   35.11871 1.000 29.45271 ? 85  ASN A CG  1 
ATOM   639  O OD1 . ASN A 1 91  ? -18.40578 2.55813   35.81717 1.000 30.35816 ? 85  ASN A OD1 1 
ATOM   640  N ND2 . ASN A 1 91  ? -20.07445 4.08509   35.60954 1.000 29.99869 ? 85  ASN A ND2 1 
ATOM   641  N N   . ASP A 1 92  ? -16.73716 4.05461   31.19868 1.000 23.82768 ? 86  ASP A N   1 
ATOM   642  C CA  . ASP A 1 92  ? -16.72591 4.44009   29.79779 1.000 23.22877 ? 86  ASP A CA  1 
ATOM   643  C C   . ASP A 1 92  ? -15.60103 5.45410   29.65172 1.000 22.14152 ? 86  ASP A C   1 
ATOM   644  O O   . ASP A 1 92  ? -15.25438 6.14252   30.60846 1.000 20.58710 ? 86  ASP A O   1 
ATOM   645  C CB  . ASP A 1 92  ? -18.07940 5.01919   29.38926 1.000 23.55527 ? 86  ASP A CB  1 
ATOM   646  C CG  . ASP A 1 92  ? -18.24756 5.14658   27.88049 1.000 25.86613 ? 86  ASP A CG  1 
ATOM   647  O OD1 . ASP A 1 92  ? -17.43679 4.58179   27.12911 1.000 25.19124 ? 86  ASP A OD1 1 
ATOM   648  O OD2 . ASP A 1 92  ? -19.26467 5.76104   27.49371 1.000 26.62111 ? 86  ASP A OD2 1 
ATOM   649  N N   . ILE A 1 93  ? -15.00514 5.49766   28.47168 1.000 20.89362 ? 87  ILE A N   1 
ATOM   650  C CA  . ILE A 1 93  ? -14.04716 6.54692   28.12916 1.000 19.54295 ? 87  ILE A CA  1 
ATOM   651  C C   . ILE A 1 93  ? -14.47220 7.10901   26.78137 1.000 20.66483 ? 87  ILE A C   1 
ATOM   652  O O   . ILE A 1 93  ? -14.66157 6.34080   25.82968 1.000 21.59020 ? 87  ILE A O   1 
ATOM   653  C CB  . ILE A 1 93  ? -12.59579 6.03867   28.08602 1.000 20.94558 ? 87  ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 93  ? -12.19885 5.46351   29.44351 1.000 21.02658 ? 87  ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 93  ? -11.67104 7.21794   27.74439 1.000 21.22230 ? 87  ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 93  ? -10.77812 4.91066   29.46561 1.000 23.55313 ? 87  ILE A CD1 1 
ATOM   657  N N   . ILE A 1 94  ? -14.53938 8.44799   26.68882 1.000 20.60191 ? 88  ILE A N   1 
ATOM   658  C CA  . ILE A 1 94  ? -14.96553 9.17035   25.48719 1.000 21.36321 ? 88  ILE A CA  1 
ATOM   659  C C   . ILE A 1 94  ? -13.79009 9.95913   24.91502 1.000 20.87798 ? 88  ILE A C   1 
ATOM   660  O O   . ILE A 1 94  ? -13.15947 10.75110  25.63537 1.000 21.66358 ? 88  ILE A O   1 
ATOM   661  C CB  . ILE A 1 94  ? -16.11646 10.12697  25.83509 1.000 22.45110 ? 88  ILE A CB  1 
ATOM   662  C CG1 . ILE A 1 94  ? -17.23358 9.37222   26.56371 1.000 23.86237 ? 88  ILE A CG1 1 
ATOM   663  C CG2 . ILE A 1 94  ? -16.55196 10.93305  24.63152 1.000 23.16264 ? 88  ILE A CG2 1 
ATOM   664  C CD1 . ILE A 1 94  ? -18.15970 10.30106  27.34708 1.000 24.16183 ? 88  ILE A CD1 1 
ATOM   665  N N   . ARG A 1 95  ? -13.53441 9.80325   23.60840 1.000 19.13459 ? 89  ARG A N   1 
ATOM   666  C CA  . ARG A 1 95  ? -12.56991 10.63798  22.90472 1.000 19.67278 ? 89  ARG A CA  1 
ATOM   667  C C   . ARG A 1 95  ? -12.83988 10.50653  21.41067 1.000 19.73970 ? 89  ARG A C   1 
ATOM   668  O O   . ARG A 1 95  ? -13.64822 9.67580   20.96566 1.000 20.26746 ? 89  ARG A O   1 
ATOM   669  C CB  . ARG A 1 95  ? -11.11342 10.26545  23.27855 1.000 20.90383 ? 89  ARG A CB  1 
ATOM   670  C CG  . ARG A 1 95  ? -10.75372 8.72252   23.27223 1.000 22.28560 ? 89  ARG A CG  1 
ATOM   671  C CD  . ARG A 1 95  ? -10.37028 8.26469   21.95187 1.000 22.35148 ? 89  ARG A CD  1 
ATOM   672  N NE  . ARG A 1 95  ? -9.75715  6.93514   21.91123 1.000 21.68690 ? 89  ARG A NE  1 
ATOM   673  C CZ  . ARG A 1 95  ? -9.83613  6.15853   20.83620 1.000 22.32994 ? 89  ARG A CZ  1 
ATOM   674  N NH1 . ARG A 1 95  ? -10.54672 6.53567   19.77054 1.000 21.80646 ? 89  ARG A NH1 1 
ATOM   675  N NH2 . ARG A 1 95  ? -9.19935  4.98133   20.82740 1.000 21.74516 ? 89  ARG A NH2 1 
ATOM   676  N N   . ALA A 1 96  ? -12.22381 11.40563  20.65772 1.000 20.12651 ? 90  ALA A N   1 
ATOM   677  C CA  . ALA A 1 96  ? -12.33840 11.43081  19.17624 1.000 20.12617 ? 90  ALA A CA  1 
ATOM   678  C C   . ALA A 1 96  ? -11.91303 10.10382  18.54235 1.000 19.93489 ? 90  ALA A C   1 
ATOM   679  O O   . ALA A 1 96  ? -11.20524 9.30626   19.14628 1.000 20.37906 ? 90  ALA A O   1 
ATOM   680  C CB  . ALA A 1 96  ? -11.47699 12.55355  18.62285 1.000 21.56537 ? 90  ALA A CB  1 
ATOM   681  N N   . PRO A 1 97  ? -12.36134 9.83259   17.31565 1.000 18.76295 ? 91  PRO A N   1 
ATOM   682  C CA  . PRO A 1 97  ? -12.04254 8.53524   16.69865 1.000 19.39609 ? 91  PRO A CA  1 
ATOM   683  C C   . PRO A 1 97  ? -10.61723 8.38948   16.21657 1.000 20.02423 ? 91  PRO A C   1 
ATOM   684  O O   . PRO A 1 97  ? -10.23964 7.26923   15.82931 1.000 21.95552 ? 91  PRO A O   1 
ATOM   685  C CB  . PRO A 1 97  ? -12.99321 8.46206   15.50678 1.000 20.43230 ? 91  PRO A CB  1 
ATOM   686  C CG  . PRO A 1 97  ? -13.31359 9.91101   15.17071 1.000 20.18670 ? 91  PRO A CG  1 
ATOM   687  C CD  . PRO A 1 97  ? -13.38475 10.57829  16.54620 1.000 19.26977 ? 91  PRO A CD  1 
ATOM   688  N N   . THR A 1 98  ? -9.87237  9.48537   16.08157 1.000 19.84330 ? 92  THR A N   1 
ATOM   689  C CA  . THR A 1 98  ? -8.52917  9.45344   15.52515 1.000 21.83842 ? 92  THR A CA  1 
ATOM   690  C C   . THR A 1 98  ? -7.57775  10.19359  16.44086 1.000 22.28273 ? 92  THR A C   1 
ATOM   691  O O   . THR A 1 98  ? -7.98868  11.11578  17.14735 1.000 22.57373 ? 92  THR A O   1 
ATOM   692  C CB  . THR A 1 98  ? -8.47292  10.11239  14.13775 1.000 23.04289 ? 92  THR A CB  1 
ATOM   693  O OG1 . THR A 1 98  ? -8.78549  11.52967  14.22559 1.000 23.26942 ? 92  THR A OG1 1 
ATOM   694  C CG2 . THR A 1 98  ? -9.45925  9.40376   13.19305 1.000 24.26820 ? 92  THR A CG2 1 
ATOM   695  N N   . ILE A 1 99  ? -6.28438  9.81763   16.39575 1.000 23.82244 ? 93  ILE A N   1 
ATOM   696  C CA  . ILE A 1 99  ? -5.30464  10.51683  17.23393 1.000 27.81874 ? 93  ILE A CA  1 
ATOM   697  C C   . ILE A 1 99  ? -5.25440  11.99589  16.88004 1.000 27.75855 ? 93  ILE A C   1 
ATOM   698  O O   . ILE A 1 99  ? -5.13101  12.85623  17.76801 1.000 28.41284 ? 93  ILE A O   1 
ATOM   699  C CB  . ILE A 1 99  ? -3.91075  9.90531   17.07378 1.000 30.63690 ? 93  ILE A CB  1 
ATOM   700  C CG1 . ILE A 1 99  ? -3.77949  8.64661   17.85522 1.000 32.96272 ? 93  ILE A CG1 1 
ATOM   701  C CG2 . ILE A 1 99  ? -2.85621  10.84411  17.70300 1.000 31.19864 ? 93  ILE A CG2 1 
ATOM   702  C CD1 . ILE A 1 99  ? -2.31634  8.28282   18.03306 1.000 34.01040 ? 93  ILE A CD1 1 
ATOM   703  N N   . GLU A 1 100 ? -5.33826  12.31422  15.57295 1.000 27.15326 ? 94  GLU A N   1 
ATOM   704  C CA  . GLU A 1 100 ? -5.26584  13.69369  15.13498 1.000 27.61866 ? 94  GLU A CA  1 
ATOM   705  C C   . GLU A 1 100 ? -6.34988  14.54101  15.76418 1.000 28.08070 ? 94  GLU A C   1 
ATOM   706  O O   . GLU A 1 100 ? -6.11969  15.71224  16.08062 1.000 30.07677 ? 94  GLU A O   1 
ATOM   707  C CB  . GLU A 1 100 ? -5.44127  13.78514  13.61498 1.000 28.52863 ? 94  GLU A CB  1 
ATOM   708  C CG  . GLU A 1 100 ? -4.33841  13.28094  12.77680 1.000 32.20274 ? 94  GLU A CG  1 
ATOM   709  C CD  . GLU A 1 100 ? -4.33059  11.77183  12.53870 1.000 34.12496 ? 94  GLU A CD  1 
ATOM   710  O OE1 . GLU A 1 100 ? -3.48364  11.36169  11.69869 1.000 36.14720 ? 94  GLU A OE1 1 
ATOM   711  O OE2 . GLU A 1 100 ? -5.09075  11.00777  13.18402 1.000 33.83637 ? 94  GLU A OE2 1 
ATOM   712  N N   . GLN A 1 101 ? -7.57655  14.00900  15.84031 1.000 25.88876 ? 95  GLN A N   1 
ATOM   713  C CA  . GLN A 1 101 ? -8.69153  14.79608  16.31861 1.000 24.30017 ? 95  GLN A CA  1 
ATOM   714  C C   . GLN A 1 101 ? -8.81570  14.77532  17.83139 1.000 25.35794 ? 95  GLN A C   1 
ATOM   715  O O   . GLN A 1 101 ? -9.69047  15.46174  18.35777 1.000 26.49773 ? 95  GLN A O   1 
ATOM   716  C CB  . GLN A 1 101 ? -10.00887 14.29126  15.69804 1.000 23.94711 ? 95  GLN A CB  1 
ATOM   717  C CG  . GLN A 1 101 ? -10.03942 14.53180  14.18821 1.000 23.58166 ? 95  GLN A CG  1 
ATOM   718  C CD  . GLN A 1 101 ? -11.16387 13.81126  13.49854 1.000 24.49352 ? 95  GLN A CD  1 
ATOM   719  O OE1 . GLN A 1 101 ? -12.07273 14.44307  12.88790 1.000 26.72858 ? 95  GLN A OE1 1 
ATOM   720  N NE2 . GLN A 1 101 ? -11.09618 12.51166  13.50555 1.000 23.12102 ? 95  GLN A NE2 1 
ATOM   721  N N   . MET A 1 102 ? -8.03023  13.94470  18.51586 1.000 25.53489 ? 96  MET A N   1 
ATOM   722  C CA  . MET A 1 102 ? -8.14297  13.75137  19.97466 1.000 25.92543 ? 96  MET A CA  1 
ATOM   723  C C   . MET A 1 102 ? -7.38798  14.83849  20.71741 1.000 29.30183 ? 96  MET A C   1 
ATOM   724  O O   . MET A 1 102 ? -6.15377  14.89072  20.67294 1.000 29.92213 ? 96  MET A O   1 
ATOM   725  C CB  . MET A 1 102 ? -7.66627  12.36026  20.37070 1.000 24.58143 ? 96  MET A CB  1 
ATOM   726  C CG  . MET A 1 102 ? -7.79497  12.11768  21.89479 1.000 24.31904 ? 96  MET A CG  1 
ATOM   727  S SD  . MET A 1 102 ? -7.26235  10.46551  22.47871 1.000 25.04832 ? 96  MET A SD  1 
ATOM   728  C CE  . MET A 1 102 ? -5.50451  10.44767  22.15345 1.000 24.72847 ? 96  MET A CE  1 
ATOM   729  N N   . LYS A 1 103 ? -8.13556  15.70372  21.41669 1.000 31.37507 ? 97  LYS A N   1 
ATOM   730  C CA  . LYS A 1 103 ? -7.54783  16.75694  22.23861 1.000 33.03424 ? 97  LYS A CA  1 
ATOM   731  C C   . LYS A 1 103 ? -7.88329  16.59331  23.70199 1.000 32.96604 ? 97  LYS A C   1 
ATOM   732  O O   . LYS A 1 103 ? -7.12893  17.06786  24.56454 1.000 35.52452 ? 97  LYS A O   1 
ATOM   733  C CB  . LYS A 1 103 ? -8.04514  18.13991  21.78859 0.800 33.30201 ? 97  LYS A CB  1 
ATOM   734  N N   . ASP A 1 104 ? -9.02178  15.99100  23.99381 1.000 30.76140 ? 98  ASP A N   1 
ATOM   735  C CA  . ASP A 1 104 ? -9.48025  15.74653  25.35286 1.000 30.60982 ? 98  ASP A CA  1 
ATOM   736  C C   . ASP A 1 104 ? -9.91704  14.29904  25.48324 1.000 27.21602 ? 98  ASP A C   1 
ATOM   737  O O   . ASP A 1 104 ? -10.26451 13.64681  24.50332 1.000 26.60301 ? 98  ASP A O   1 
ATOM   738  C CB  . ASP A 1 104 ? -10.65776 16.63820  25.71252 1.000 33.70729 ? 98  ASP A CB  1 
ATOM   739  C CG  . ASP A 1 104 ? -10.42669 18.06928  25.34728 1.000 36.52292 ? 98  ASP A CG  1 
ATOM   740  O OD1 . ASP A 1 104 ? -9.51453  18.71945  25.92235 1.000 37.80782 ? 98  ASP A OD1 1 
ATOM   741  O OD2 . ASP A 1 104 ? -11.15196 18.53088  24.46307 1.000 37.88259 ? 98  ASP A OD2 1 
ATOM   742  N N   . VAL A 1 105 ? -9.92310  13.81234  26.71073 1.000 25.99538 ? 99  VAL A N   1 
ATOM   743  C CA  . VAL A 1 105 ? -10.41129 12.47461  27.04540 1.000 24.06799 ? 99  VAL A CA  1 
ATOM   744  C C   . VAL A 1 105 ? -11.39595 12.64870  28.18028 1.000 23.79194 ? 99  VAL A C   1 
ATOM   745  O O   . VAL A 1 105 ? -11.08750 13.34777  29.15136 1.000 25.67452 ? 99  VAL A O   1 
ATOM   746  C CB  . VAL A 1 105 ? -9.25175  11.54839  27.50301 1.000 26.40271 ? 99  VAL A CB  1 
ATOM   747  C CG1 . VAL A 1 105 ? -9.76294  10.19744  27.91750 1.000 27.30079 ? 99  VAL A CG1 1 
ATOM   748  C CG2 . VAL A 1 105 ? -8.18679  11.44046  26.42062 1.000 27.51795 ? 99  VAL A CG2 1 
ATOM   749  N N   . TYR A 1 106 ? -12.54298 11.97300  28.12352 1.000 21.79539 ? 100 TYR A N   1 
ATOM   750  C CA  . TYR A 1 106 ? -13.50033 12.01540  29.23865 1.000 21.04856 ? 100 TYR A CA  1 
ATOM   751  C C   . TYR A 1 106 ? -13.63227 10.64647  29.89184 1.000 21.06420 ? 100 TYR A C   1 
ATOM   752  O O   . TYR A 1 106 ? -13.88739 9.65976   29.20324 1.000 21.52073 ? 100 TYR A O   1 
ATOM   753  C CB  . TYR A 1 106 ? -14.87320 12.47458  28.74943 1.000 20.56267 ? 100 TYR A CB  1 
ATOM   754  C CG  . TYR A 1 106 ? -14.82990 13.81909  28.10793 0.600 19.64687 ? 100 TYR A CG  1 
ATOM   755  C CD1 . TYR A 1 106 ? -14.45184 13.96329  26.76498 0.600 20.08571 ? 100 TYR A CD1 1 
ATOM   756  C CD2 . TYR A 1 106 ? -15.23891 14.95256  28.80526 0.600 20.64997 ? 100 TYR A CD2 1 
ATOM   757  C CE1 . TYR A 1 106 ? -14.41230 15.16773  26.19096 0.600 21.57463 ? 100 TYR A CE1 1 
ATOM   758  C CE2 . TYR A 1 106 ? -15.21013 16.20156  28.20005 0.600 20.88369 ? 100 TYR A CE2 1 
ATOM   759  C CZ  . TYR A 1 106 ? -14.79667 16.28836  26.88386 0.600 22.70617 ? 100 TYR A CZ  1 
ATOM   760  O OH  . TYR A 1 106 ? -14.77478 17.48199  26.20738 0.600 24.69536 ? 100 TYR A OH  1 
ATOM   761  N N   . ILE A 1 107 ? -13.48802 10.58341  31.22299 1.000 20.45888 ? 101 ILE A N   1 
ATOM   762  C CA  . ILE A 1 107 ? -13.66599 9.33022   31.94847 1.000 20.12050 ? 101 ILE A CA  1 
ATOM   763  C C   . ILE A 1 107 ? -14.99253 9.35007   32.71015 1.000 19.71167 ? 101 ILE A C   1 
ATOM   764  O O   . ILE A 1 107 ? -15.24620 10.26353  33.52490 1.000 21.12911 ? 101 ILE A O   1 
ATOM   765  C CB  . ILE A 1 107 ? -12.45434 9.02987   32.86412 1.000 21.71751 ? 101 ILE A CB  1 
ATOM   766  C CG1 . ILE A 1 107 ? -11.18341 8.99937   31.98677 1.000 24.33070 ? 101 ILE A CG1 1 
ATOM   767  C CG2 . ILE A 1 107 ? -12.60677 7.83259   33.69932 1.000 20.33782 ? 101 ILE A CG2 1 
ATOM   768  C CD1 . ILE A 1 107 ? -9.96828  8.98487   32.76748 1.000 28.19763 ? 101 ILE A CD1 1 
ATOM   769  N N   . VAL A 1 108 ? -15.83304 8.32192   32.46680 1.000 18.98865 ? 102 VAL A N   1 
ATOM   770  C CA  . VAL A 1 108 ? -17.16091 8.22812   33.07741 1.000 19.91793 ? 102 VAL A CA  1 
ATOM   771  C C   . VAL A 1 108 ? -17.08282 7.23634   34.22437 1.000 20.02581 ? 102 VAL A C   1 
ATOM   772  O O   . VAL A 1 108 ? -16.54327 6.12885   34.05397 1.000 20.59851 ? 102 VAL A O   1 
ATOM   773  C CB  . VAL A 1 108 ? -18.20740 7.76969   32.04307 1.000 20.73494 ? 102 VAL A CB  1 
ATOM   774  C CG1 . VAL A 1 108 ? -19.59610 7.76687   32.66234 1.000 21.65651 ? 102 VAL A CG1 1 
ATOM   775  C CG2 . VAL A 1 108 ? -18.15286 8.64624   30.73847 1.000 20.62654 ? 102 VAL A CG2 1 
ATOM   776  N N   . GLN A 1 109 ? -17.63361 7.62513   35.39465 1.000 19.48041 ? 103 GLN A N   1 
ATOM   777  C CA  . GLN A 1 109 ? -17.57220 6.84419   36.63077 1.000 20.45461 ? 103 GLN A CA  1 
ATOM   778  C C   . GLN A 1 109 ? -18.91357 6.96236   37.35009 1.000 23.09608 ? 103 GLN A C   1 
ATOM   779  O O   . GLN A 1 109 ? -19.74660 7.82608   37.00807 1.000 23.53234 ? 103 GLN A O   1 
ATOM   780  C CB  . GLN A 1 109 ? -16.36127 7.28502   37.50844 1.000 20.61390 ? 103 GLN A CB  1 
ATOM   781  C CG  . GLN A 1 109 ? -15.02491 7.17158   36.73850 1.000 22.21746 ? 103 GLN A CG  1 
ATOM   782  C CD  . GLN A 1 109 ? -13.82492 7.58959   37.62909 0.800 23.32470 ? 103 GLN A CD  1 
ATOM   783  O OE1 . GLN A 1 109 ? -13.01586 6.73771   38.12342 0.800 26.09251 ? 103 GLN A OE1 1 
ATOM   784  N NE2 . GLN A 1 109 ? -13.68649 8.86537   37.80734 0.800 21.27009 ? 103 GLN A NE2 1 
ATOM   785  N N   . ASP A 1 110 ? -19.13174 6.08267   38.35104 1.000 24.76776 ? 104 ASP A N   1 
ATOM   786  C CA  . ASP A 1 110 ? -20.35837 6.11858   39.13885 1.000 26.69999 ? 104 ASP A CA  1 
ATOM   787  C C   . ASP A 1 110 ? -20.49967 7.49120   39.78211 1.000 25.57639 ? 104 ASP A C   1 
ATOM   788  O O   . ASP A 1 110 ? -19.51340 8.07907   40.25652 1.000 24.18590 ? 104 ASP A O   1 
ATOM   789  C CB  . ASP A 1 110 ? -20.37090 5.04541   40.25210 1.000 28.74983 ? 104 ASP A CB  1 
ATOM   790  C CG  . ASP A 1 110 ? -20.33301 3.60896   39.70643 1.000 30.50435 ? 104 ASP A CG  1 
ATOM   791  O OD1 . ASP A 1 110 ? -20.66394 3.43076   38.50744 0.780 29.55936 ? 104 ASP A OD1 1 
ATOM   792  O OD2 . ASP A 1 110 ? -19.96020 2.67823   40.48679 0.680 30.96757 ? 104 ASP A OD2 1 
ATOM   793  N N   . LEU A 1 111 ? -21.73750 7.99202   39.81364 1.000 25.88850 ? 105 LEU A N   1 
ATOM   794  C CA  . LEU A 1 111 ? -21.99622 9.22919   40.52709 1.000 26.23208 ? 105 LEU A CA  1 
ATOM   795  C C   . LEU A 1 111 ? -22.21499 8.92166   42.01001 1.000 26.28537 ? 105 LEU A C   1 
ATOM   796  O O   . LEU A 1 111 ? -23.16621 8.20804   42.37183 1.000 26.90447 ? 105 LEU A O   1 
ATOM   797  C CB  . LEU A 1 111 ? -23.22745 9.91784   39.96020 1.000 27.12488 ? 105 LEU A CB  1 
ATOM   798  C CG  . LEU A 1 111 ? -23.58717 11.23238  40.63171 1.000 28.10639 ? 105 LEU A CG  1 
ATOM   799  C CD1 . LEU A 1 111 ? -22.54547 12.29411  40.35285 1.000 28.40741 ? 105 LEU A CD1 1 
ATOM   800  C CD2 . LEU A 1 111 ? -24.97020 11.65164  40.17889 1.000 29.62045 ? 105 LEU A CD2 1 
ATOM   801  N N   . MET A 1 112 ? -21.34594 9.45978   42.85547 1.000 25.06613 ? 106 MET A N   1 
ATOM   802  C CA  . MET A 1 112 ? -21.44220 9.28006   44.29709 1.000 23.16816 ? 106 MET A CA  1 
ATOM   803  C C   . MET A 1 112 ? -22.21438 10.47319  44.86901 1.000 25.67584 ? 106 MET A C   1 
ATOM   804  O O   . MET A 1 112 ? -22.65284 11.35449  44.12169 1.000 28.63630 ? 106 MET A O   1 
ATOM   805  C CB  . MET A 1 112 ? -20.02089 9.13402   44.82883 1.000 23.29617 ? 106 MET A CB  1 
ATOM   806  C CG  . MET A 1 112 ? -19.33541 7.89349   44.28159 1.000 22.59137 ? 106 MET A CG  1 
ATOM   807  S SD  . MET A 1 112 ? -20.15688 6.29472   44.68394 1.000 23.65632 ? 106 MET A SD  1 
ATOM   808  C CE  . MET A 1 112 ? -19.19811 5.97782   46.19519 1.000 23.40616 ? 106 MET A CE  1 
ATOM   809  N N   . GLU A 1 113 ? -22.50148 10.44032  46.17601 1.000 23.65671 ? 107 GLU A N   1 
ATOM   810  C CA  . GLU A 1 113 ? -23.17576 11.54822  46.87638 1.000 24.12982 ? 107 GLU A CA  1 
ATOM   811  C C   . GLU A 1 113 ? -22.23353 12.63600  47.38266 1.000 23.79817 ? 107 GLU A C   1 
ATOM   812  O O   . GLU A 1 113 ? -22.55376 13.82298  47.26028 1.000 24.58829 ? 107 GLU A O   1 
ATOM   813  C CB  . GLU A 1 113 ? -24.01089 11.05372  48.07783 0.800 23.69429 ? 107 GLU A CB  1 
ATOM   814  C CG  . GLU A 1 113 ? -24.87354 12.14753  48.70838 0.700 25.49509 ? 107 GLU A CG  1 
ATOM   815  C CD  . GLU A 1 113 ? -25.89300 11.67640  49.74780 0.500 27.05383 ? 107 GLU A CD  1 
ATOM   816  O OE1 . GLU A 1 113 ? -25.61790 11.74011  50.97142 0.500 27.38339 ? 107 GLU A OE1 1 
ATOM   817  O OE2 . GLU A 1 113 ? -27.02108 11.35684  49.37111 0.500 28.57951 ? 107 GLU A OE2 1 
ATOM   818  N N   . THR A 1 114 ? -21.07868 12.27590  47.94902 1.000 21.05977 ? 108 THR A N   1 
ATOM   819  C CA  . THR A 1 114 ? -20.20496 13.25445  48.57387 1.000 20.15185 ? 108 THR A CA  1 
ATOM   820  C C   . THR A 1 114 ? -18.83337 12.59849  48.68259 1.000 19.39590 ? 108 THR A C   1 
ATOM   821  O O   . THR A 1 114 ? -18.60915 11.50806  48.14905 1.000 17.86534 ? 108 THR A O   1 
ATOM   822  C CB  . THR A 1 114 ? -20.76984 13.69194  49.94265 1.000 22.83969 ? 108 THR A CB  1 
ATOM   823  O OG1 . THR A 1 114 ? -20.04706 14.80648  50.45485 1.000 24.85126 ? 108 THR A OG1 1 
ATOM   824  C CG2 . THR A 1 114 ? -20.71157 12.54845  50.93608 1.000 22.48647 ? 108 THR A CG2 1 
ATOM   825  N N   . ASP A 1 115 ? -17.92653 13.27683  49.34493 1.000 19.92308 ? 109 ASP A N   1 
ATOM   826  C CA  . ASP A 1 115 ? -16.61808 12.69406  49.70315 1.000 19.90303 ? 109 ASP A CA  1 
ATOM   827  C C   . ASP A 1 115 ? -16.32185 12.99332  51.17229 1.000 19.83596 ? 109 ASP A C   1 
ATOM   828  O O   . ASP A 1 115 ? -17.01293 13.80299  51.82709 1.000 20.97726 ? 109 ASP A O   1 
ATOM   829  C CB  . ASP A 1 115 ? -15.48490 13.19301  48.78139 1.000 22.57171 ? 109 ASP A CB  1 
ATOM   830  C CG  . ASP A 1 115 ? -15.22856 14.70209  48.89950 1.000 23.69631 ? 109 ASP A CG  1 
ATOM   831  O OD1 . ASP A 1 115 ? -14.86953 15.17369  49.99416 1.000 23.80047 ? 109 ASP A OD1 1 
ATOM   832  O OD2 . ASP A 1 115 ? -15.30918 15.40627  47.87030 1.000 25.82332 ? 109 ASP A OD2 1 
ATOM   833  N N   . LEU A 1 116 ? -15.27422 12.34004  51.71464 1.000 18.38673 ? 110 LEU A N   1 
ATOM   834  C CA  . LEU A 1 116 ? -15.05484 12.45125  53.15085 1.000 17.98857 ? 110 LEU A CA  1 
ATOM   835  C C   . LEU A 1 116 ? -14.51931 13.84073  53.52141 1.000 18.68444 ? 110 LEU A C   1 
ATOM   836  O O   . LEU A 1 116 ? -14.69951 14.29489  54.64861 1.000 20.40056 ? 110 LEU A O   1 
ATOM   837  C CB  . LEU A 1 116 ? -14.05163 11.38212  53.60537 1.000 19.26305 ? 110 LEU A CB  1 
ATOM   838  C CG  . LEU A 1 116 ? -13.88473 11.15651  55.12175 1.000 19.15161 ? 110 LEU A CG  1 
ATOM   839  C CD1 . LEU A 1 116 ? -15.23498 10.67956  55.80526 1.000 20.09533 ? 110 LEU A CD1 1 
ATOM   840  C CD2 . LEU A 1 116 ? -12.75261 10.12320  55.30305 1.000 19.27243 ? 110 LEU A CD2 1 
ATOM   841  N N   . TYR A 1 117 ? -13.85518 14.53926  52.59763 1.000 19.00380 ? 111 TYR A N   1 
ATOM   842  C CA  . TYR A 1 117 ? -13.41104 15.91240  52.88334 1.000 19.83000 ? 111 TYR A CA  1 
ATOM   843  C C   . TYR A 1 117 ? -14.62940 16.80950  53.12416 1.000 19.33780 ? 111 TYR A C   1 
ATOM   844  O O   . TYR A 1 117 ? -14.71732 17.54911  54.11532 1.000 21.08582 ? 111 TYR A O   1 
ATOM   845  C CB  . TYR A 1 117 ? -12.58464 16.45792  51.69046 1.000 22.27699 ? 111 TYR A CB  1 
ATOM   846  C CG  . TYR A 1 117 ? -12.20267 17.91421  51.79151 1.000 25.32769 ? 111 TYR A CG  1 
ATOM   847  C CD1 . TYR A 1 117 ? -11.13841 18.30409  52.57059 1.000 28.50736 ? 111 TYR A CD1 1 
ATOM   848  C CD2 . TYR A 1 117 ? -12.92241 18.90056  51.13406 1.000 27.41597 ? 111 TYR A CD2 1 
ATOM   849  C CE1 . TYR A 1 117 ? -10.77739 19.64673  52.69828 1.000 30.53287 ? 111 TYR A CE1 1 
ATOM   850  C CE2 . TYR A 1 117 ? -12.58750 20.24871  51.25235 1.000 29.25198 ? 111 TYR A CE2 1 
ATOM   851  C CZ  . TYR A 1 117 ? -11.50248 20.61473  52.03602 1.000 31.07217 ? 111 TYR A CZ  1 
ATOM   852  O OH  . TYR A 1 117 ? -11.15392 21.93514  52.16225 0.490 31.76697 ? 111 TYR A OH  1 
ATOM   853  N N   . LYS A 1 118 ? -15.61098 16.70999  52.24447 1.000 19.59277 ? 112 LYS A N   1 
ATOM   854  C CA  . LYS A 1 118 ? -16.82585 17.51606  52.36259 1.000 20.84530 ? 112 LYS A CA  1 
ATOM   855  C C   . LYS A 1 118 ? -17.60775 17.13310  53.60107 1.000 21.77562 ? 112 LYS A C   1 
ATOM   856  O O   . LYS A 1 118 ? -18.14040 18.00100  54.32639 1.000 22.84434 ? 112 LYS A O   1 
ATOM   857  C CB  . LYS A 1 118 ? -17.66609 17.25268  51.12888 0.900 21.42777 ? 112 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 118 ? -17.19671 18.00369  49.95425 0.600 21.32189 ? 112 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 118 ? -18.08659 17.57162  48.77343 0.500 22.92149 ? 112 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 118 ? -17.76323 18.34276  47.53942 0.500 25.48527 ? 112 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 118 ? -18.62833 17.92163  46.38150 0.500 25.96074 ? 112 LYS A NZ  1 
ATOM   862  N N   . LEU A 1 119 ? -17.73224 15.82388  53.82652 1.000 21.92101 ? 113 LEU A N   1 
ATOM   863  C CA  . LEU A 1 119 ? -18.46315 15.33615  54.99128 1.000 22.52834 ? 113 LEU A CA  1 
ATOM   864  C C   . LEU A 1 119 ? -17.84330 15.84348  56.28571 1.000 23.22483 ? 113 LEU A C   1 
ATOM   865  O O   . LEU A 1 119 ? -18.54494 16.35986  57.15908 1.000 24.32726 ? 113 LEU A O   1 
ATOM   866  C CB  . LEU A 1 119 ? -18.51779 13.82047  54.91979 1.000 24.34048 ? 113 LEU A CB  1 
ATOM   867  C CG  . LEU A 1 119 ? -19.57852 13.06674  55.65250 1.000 25.81412 ? 113 LEU A CG  1 
ATOM   868  C CD1 . LEU A 1 119 ? -20.98680 13.49040  55.18890 1.000 25.45744 ? 113 LEU A CD1 1 
ATOM   869  C CD2 . LEU A 1 119 ? -19.30806 11.53005  55.42316 1.000 26.28847 ? 113 LEU A CD2 1 
ATOM   870  N N   . LEU A 1 120 ? -16.52487 15.75168  56.41663 1.000 21.60263 ? 114 LEU A N   1 
ATOM   871  C CA  . LEU A 1 120 ? -15.89951 16.15148  57.69530 1.000 22.56614 ? 114 LEU A CA  1 
ATOM   872  C C   . LEU A 1 120 ? -15.96189 17.65967  57.94278 1.000 23.02739 ? 114 LEU A C   1 
ATOM   873  O O   . LEU A 1 120 ? -15.78608 18.09991  59.09110 1.000 23.32546 ? 114 LEU A O   1 
ATOM   874  C CB  . LEU A 1 120 ? -14.44587 15.67778  57.75489 1.000 23.63980 ? 114 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 120 ? -14.30404 14.15160  57.85957 1.000 24.86126 ? 114 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 120 ? -12.80371 13.75569  57.79020 1.000 24.34782 ? 114 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 120 ? -14.86150 13.65275  59.23131 1.000 27.09863 ? 114 LEU A CD2 1 
ATOM   878  N N   . LYS A 1 121 ? -16.20796 18.46435  56.90254 1.000 25.11397 ? 115 LYS A N   1 
ATOM   879  C CA  . LYS A 1 121 ? -16.35424 19.90834  57.09295 1.000 27.00416 ? 115 LYS A CA  1 
ATOM   880  C C   . LYS A 1 121 ? -17.56269 20.26051  57.95209 1.000 28.03391 ? 115 LYS A C   1 
ATOM   881  O O   . LYS A 1 121 ? -17.55652 21.31085  58.61872 1.000 30.11290 ? 115 LYS A O   1 
ATOM   882  C CB  . LYS A 1 121 ? -16.47635 20.63887  55.74738 0.800 28.37482 ? 115 LYS A CB  1 
ATOM   883  C CG  . LYS A 1 121 ? -15.20863 20.70907  54.94311 0.700 29.64169 ? 115 LYS A CG  1 
ATOM   884  C CD  . LYS A 1 121 ? -14.18317 21.71838  55.51176 0.600 30.76474 ? 115 LYS A CD  1 
ATOM   885  C CE  . LYS A 1 121 ? -12.87708 21.04342  55.94229 0.500 30.48385 ? 115 LYS A CE  1 
ATOM   886  N NZ  . LYS A 1 121 ? -11.63314 21.77652  55.69771 0.500 30.11090 ? 115 LYS A NZ  1 
ATOM   887  N N   . THR A 1 122 ? -18.62365 19.44730  57.92553 1.000 26.95067 ? 116 THR A N   1 
ATOM   888  C CA  . THR A 1 122 ? -19.80214 19.81424  58.70762 1.000 26.93152 ? 116 THR A CA  1 
ATOM   889  C C   . THR A 1 122 ? -20.44140 18.68901  59.51677 1.000 26.10339 ? 116 THR A C   1 
ATOM   890  O O   . THR A 1 122 ? -21.38643 18.98015  60.25963 1.000 27.85992 ? 116 THR A O   1 
ATOM   891  C CB  . THR A 1 122 ? -20.91192 20.42575  57.81725 0.800 27.17827 ? 116 THR A CB  1 
ATOM   892  O OG1 . THR A 1 122 ? -21.34360 19.46563  56.83238 0.800 27.59511 ? 116 THR A OG1 1 
ATOM   893  C CG2 . THR A 1 122 ? -20.41382 21.69186  57.10996 0.800 27.70382 ? 116 THR A CG2 1 
ATOM   894  N N   . GLN A 1 123 ? -20.02566 17.43020  59.38117 1.000 22.76644 ? 117 GLN A N   1 
ATOM   895  C CA  . GLN A 1 123 ? -20.71855 16.31887  60.00457 1.000 22.52928 ? 117 GLN A CA  1 
ATOM   896  C C   . GLN A 1 123 ? -19.82108 15.60571  61.01052 1.000 21.55539 ? 117 GLN A C   1 
ATOM   897  O O   . GLN A 1 123 ? -18.69042 15.18816  60.68215 1.000 22.73508 ? 117 GLN A O   1 
ATOM   898  C CB  . GLN A 1 123 ? -21.25087 15.31594  58.95370 1.000 23.63311 ? 117 GLN A CB  1 
ATOM   899  C CG  . GLN A 1 123 ? -22.10270 15.93493  57.84977 1.000 24.55339 ? 117 GLN A CG  1 
ATOM   900  C CD  . GLN A 1 123 ? -23.37548 16.52247  58.35951 1.000 25.35387 ? 117 GLN A CD  1 
ATOM   901  O OE1 . GLN A 1 123 ? -23.99769 15.98982  59.29344 1.000 24.56502 ? 117 GLN A OE1 1 
ATOM   902  N NE2 . GLN A 1 123 ? -23.76358 17.65974  57.78577 1.000 26.71770 ? 117 GLN A NE2 1 
ATOM   903  N N   . HIS A 1 124 ? -20.30439 15.50633  62.25061 1.000 21.79407 ? 118 HIS A N   1 
ATOM   904  C CA  . HIS A 1 124 ? -19.69468 14.60811  63.23561 1.000 23.46479 ? 118 HIS A CA  1 
ATOM   905  C C   . HIS A 1 124 ? -19.99744 13.14432  62.88023 1.000 22.99992 ? 118 HIS A C   1 
ATOM   906  O O   . HIS A 1 124 ? -21.14149 12.78808  62.58180 1.000 24.08920 ? 118 HIS A O   1 
ATOM   907  C CB  . HIS A 1 124 ? -20.24604 14.97929  64.61982 0.800 25.33505 ? 118 HIS A CB  1 
ATOM   908  C CG  . HIS A 1 124 ? -19.83106 14.05486  65.71776 0.700 28.12697 ? 118 HIS A CG  1 
ATOM   909  N ND1 . HIS A 1 124 ? -20.67151 13.09457  66.24588 0.700 28.90429 ? 118 HIS A ND1 1 
ATOM   910  C CD2 . HIS A 1 124 ? -18.67100 13.96568  66.41040 0.700 29.66601 ? 118 HIS A CD2 1 
ATOM   911  C CE1 . HIS A 1 124 ? -20.03687 12.43281  67.20040 0.700 29.29875 ? 118 HIS A CE1 1 
ATOM   912  N NE2 . HIS A 1 124 ? -18.81648 12.94004  67.31767 0.700 30.53886 ? 118 HIS A NE2 1 
ATOM   913  N N   . LEU A 1 125 ? -18.98159 12.29246  62.84219 1.000 22.39167 ? 119 LEU A N   1 
ATOM   914  C CA  . LEU A 1 125 ? -19.20795 10.86873  62.59789 1.000 21.68516 ? 119 LEU A CA  1 
ATOM   915  C C   . LEU A 1 125 ? -19.46603 10.10996  63.89375 1.000 22.75031 ? 119 LEU A C   1 
ATOM   916  O O   . LEU A 1 125 ? -18.73993 10.27907  64.87819 1.000 23.42894 ? 119 LEU A O   1 
ATOM   917  C CB  . LEU A 1 125 ? -17.98876 10.24832  61.89677 1.000 22.52562 ? 119 LEU A CB  1 
ATOM   918  C CG  . LEU A 1 125 ? -17.44594 10.94212  60.63349 1.000 25.55522 ? 119 LEU A CG  1 
ATOM   919  C CD1 . LEU A 1 125 ? -16.42943 10.02873  59.84822 1.000 24.88197 ? 119 LEU A CD1 1 
ATOM   920  C CD2 . LEU A 1 125 ? -18.47782 11.49437  59.71482 1.000 28.52717 ? 119 LEU A CD2 1 
ATOM   921  N N   . SER A 1 126 ? -20.45011 9.21145   63.87372 1.000 22.47145 ? 120 SER A N   1 
ATOM   922  C CA  . SER A 1 126 ? -20.58308 8.25884   64.97002 1.000 22.89904 ? 120 SER A CA  1 
ATOM   923  C C   . SER A 1 126 ? -19.40093 7.27597   64.94027 1.000 23.50142 ? 120 SER A C   1 
ATOM   924  O O   . SER A 1 126 ? -18.81435 7.01999   63.89267 1.000 21.64947 ? 120 SER A O   1 
ATOM   925  C CB  . SER A 1 126 ? -21.90600 7.46892   64.86386 1.000 23.53136 ? 120 SER A CB  1 
ATOM   926  O OG  . SER A 1 126 ? -21.84918 6.49236   63.82037 1.000 23.11964 ? 120 SER A OG  1 
ATOM   927  N N   . ASN A 1 127 ? -19.08256 6.66998   66.09501 1.000 24.09502 ? 121 ASN A N   1 
ATOM   928  C CA  . ASN A 1 127 ? -18.07342 5.61820   66.06827 1.000 23.02164 ? 121 ASN A CA  1 
ATOM   929  C C   . ASN A 1 127 ? -18.43841 4.49850   65.10184 1.000 21.85026 ? 121 ASN A C   1 
ATOM   930  O O   . ASN A 1 127 ? -17.54310 3.91895   64.47941 1.000 22.36745 ? 121 ASN A O   1 
ATOM   931  C CB  . ASN A 1 127 ? -17.84256 5.02880   67.46535 1.000 24.62718 ? 121 ASN A CB  1 
ATOM   932  C CG  . ASN A 1 127 ? -16.76085 3.91995   67.45473 0.800 24.40796 ? 121 ASN A CG  1 
ATOM   933  O OD1 . ASN A 1 127 ? -15.60516 4.14752   67.06713 0.800 22.57951 ? 121 ASN A OD1 1 
ATOM   934  N ND2 . ASN A 1 127 ? -17.14682 2.71457   67.87461 0.800 26.25276 ? 121 ASN A ND2 1 
ATOM   935  N N   . ASP A 1 128 ? -19.74708 4.17403   64.92868 1.000 22.17785 ? 122 ASP A N   1 
ATOM   936  C CA  . ASP A 1 128 ? -20.08915 3.13947   63.95238 1.000 22.65083 ? 122 ASP A CA  1 
ATOM   937  C C   . ASP A 1 128 ? -19.71917 3.56870   62.53043 1.000 21.42077 ? 122 ASP A C   1 
ATOM   938  O O   . ASP A 1 128 ? -19.32900 2.73854   61.71017 1.000 22.14382 ? 122 ASP A O   1 
ATOM   939  C CB  . ASP A 1 128 ? -21.57878 2.80615   64.01019 1.000 23.31851 ? 122 ASP A CB  1 
ATOM   940  C CG  . ASP A 1 128 ? -21.96022 1.99482   65.25656 0.700 23.30221 ? 122 ASP A CG  1 
ATOM   941  O OD1 . ASP A 1 128 ? -21.10465 1.27924   65.83810 0.500 24.05053 ? 122 ASP A OD1 1 
ATOM   942  O OD2 . ASP A 1 128 ? -23.13863 2.10065   65.65203 0.500 23.21839 ? 122 ASP A OD2 1 
ATOM   943  N N   . HIS A 1 129 ? -19.85861 4.84972   62.21413 1.000 19.26010 ? 123 HIS A N   1 
ATOM   944  C CA  . HIS A 1 129 ? -19.48964 5.30438   60.86666 1.000 17.45490 ? 123 HIS A CA  1 
ATOM   945  C C   . HIS A 1 129 ? -17.98961 5.28889   60.70086 1.000 16.51192 ? 123 HIS A C   1 
ATOM   946  O O   . HIS A 1 129 ? -17.50064 4.89275   59.64626 1.000 16.68526 ? 123 HIS A O   1 
ATOM   947  C CB  . HIS A 1 129 ? -19.98829 6.72588   60.57716 1.000 17.70911 ? 123 HIS A CB  1 
ATOM   948  C CG  . HIS A 1 129 ? -21.46256 6.78277   60.24508 1.000 20.02424 ? 123 HIS A CG  1 
ATOM   949  N ND1 . HIS A 1 129 ? -22.42428 6.93475   61.22386 1.000 21.40541 ? 123 HIS A ND1 1 
ATOM   950  C CD2 . HIS A 1 129 ? -22.11848 6.75379   59.06043 1.000 20.86298 ? 123 HIS A CD2 1 
ATOM   951  C CE1 . HIS A 1 129 ? -23.61668 6.96825   60.64911 1.000 22.55323 ? 123 HIS A CE1 1 
ATOM   952  N NE2 . HIS A 1 129 ? -23.45213 6.84356   59.33815 1.000 21.43944 ? 123 HIS A NE2 1 
ATOM   953  N N   . ILE A 1 130 ? -17.25789 5.65766   61.75154 1.000 16.69848 ? 124 ILE A N   1 
ATOM   954  C CA  . ILE A 1 130 ? -15.79822 5.67232   61.65731 1.000 15.78128 ? 124 ILE A CA  1 
ATOM   955  C C   . ILE A 1 130 ? -15.29273 4.27074   61.37573 1.000 16.11472 ? 124 ILE A C   1 
ATOM   956  O O   . ILE A 1 130 ? -14.42325 4.05739   60.51351 1.000 17.41739 ? 124 ILE A O   1 
ATOM   957  C CB  . ILE A 1 130 ? -15.16504 6.24866   62.94203 1.000 16.68530 ? 124 ILE A CB  1 
ATOM   958  C CG1 . ILE A 1 130 ? -15.52604 7.73331   63.08926 1.000 17.94246 ? 124 ILE A CG1 1 
ATOM   959  C CG2 . ILE A 1 130 ? -13.65127 6.15651   62.91108 1.000 17.06969 ? 124 ILE A CG2 1 
ATOM   960  C CD1 . ILE A 1 130 ? -15.10157 8.39041   64.37298 1.000 19.20573 ? 124 ILE A CD1 1 
ATOM   961  N N   . CYS A 1 131 ? -15.76398 3.30946   62.17200 1.000 16.07553 ? 125 CYS A N   1 
ATOM   962  C CA  . CYS A 1 131 ? -15.38631 1.91253   62.00275 1.000 16.99303 ? 125 CYS A CA  1 
ATOM   963  C C   . CYS A 1 131 ? -15.69705 1.40995   60.57748 1.000 16.32294 ? 125 CYS A C   1 
ATOM   964  O O   . CYS A 1 131 ? -14.86519 0.75561   59.93854 1.000 16.33900 ? 125 CYS A O   1 
ATOM   965  C CB  . CYS A 1 131 ? -16.14127 1.10086   63.09209 1.000 18.40262 ? 125 CYS A CB  1 
ATOM   966  S SG  . CYS A 1 131 ? -15.60619 -0.55921  63.25331 1.000 21.82596 ? 125 CYS A SG  1 
ATOM   967  N N   . TYR A 1 132 ? -16.91589 1.65666   60.07519 1.000 17.34815 ? 126 TYR A N   1 
ATOM   968  C CA  . TYR A 1 132 ? -17.27492 1.14413   58.75576 1.000 16.57832 ? 126 TYR A CA  1 
ATOM   969  C C   . TYR A 1 132 ? -16.48421 1.83255   57.63991 1.000 16.65601 ? 126 TYR A C   1 
ATOM   970  O O   . TYR A 1 132 ? -16.08141 1.17156   56.65481 1.000 16.03878 ? 126 TYR A O   1 
ATOM   971  C CB  . TYR A 1 132 ? -18.80260 1.33027   58.53969 1.000 19.61034 ? 126 TYR A CB  1 
ATOM   972  C CG  . TYR A 1 132 ? -19.35664 0.77552   57.25637 1.000 21.98309 ? 126 TYR A CG  1 
ATOM   973  C CD1 . TYR A 1 132 ? -19.02800 -0.51114  56.81315 1.000 24.56121 ? 126 TYR A CD1 1 
ATOM   974  C CD2 . TYR A 1 132 ? -20.22118 1.54093   56.47559 1.000 23.95731 ? 126 TYR A CD2 1 
ATOM   975  C CE1 . TYR A 1 132 ? -19.55400 -1.01881  55.59933 1.000 25.22057 ? 126 TYR A CE1 1 
ATOM   976  C CE2 . TYR A 1 132 ? -20.78039 1.03871   55.29161 1.000 24.94420 ? 126 TYR A CE2 1 
ATOM   977  C CZ  . TYR A 1 132 ? -20.42883 -0.22543  54.86930 1.000 27.08452 ? 126 TYR A CZ  1 
ATOM   978  O OH  . TYR A 1 132 ? -20.93541 -0.72028  53.69844 1.000 30.44380 ? 126 TYR A OH  1 
ATOM   979  N N   . PHE A 1 133 ? -16.25644 3.15404   57.76066 1.000 15.20195 ? 127 PHE A N   1 
ATOM   980  C CA  . PHE A 1 133 ? -15.42353 3.85701   56.76486 1.000 14.80138 ? 127 PHE A CA  1 
ATOM   981  C C   . PHE A 1 133 ? -14.00647 3.28875   56.76802 1.000 14.73999 ? 127 PHE A C   1 
ATOM   982  O O   . PHE A 1 133 ? -13.42815 3.01381   55.70625 1.000 15.05828 ? 127 PHE A O   1 
ATOM   983  C CB  . PHE A 1 133 ? -15.35393 5.37750   57.03066 1.000 15.81528 ? 127 PHE A CB  1 
ATOM   984  C CG  . PHE A 1 133 ? -16.66682 6.13411   56.75515 1.000 18.55586 ? 127 PHE A CG  1 
ATOM   985  C CD1 . PHE A 1 133 ? -17.68995 5.56624   56.01993 1.000 20.65006 ? 127 PHE A CD1 1 
ATOM   986  C CD2 . PHE A 1 133 ? -16.85213 7.39869   57.23942 1.000 20.08101 ? 127 PHE A CD2 1 
ATOM   987  C CE1 . PHE A 1 133 ? -18.86530 6.28302   55.79352 1.000 21.24364 ? 127 PHE A CE1 1 
ATOM   988  C CE2 . PHE A 1 133 ? -18.03094 8.11562   56.99505 1.000 20.10065 ? 127 PHE A CE2 1 
ATOM   989  C CZ  . PHE A 1 133 ? -19.02263 7.54966   56.28096 1.000 20.31087 ? 127 PHE A CZ  1 
ATOM   990  N N   . LEU A 1 134 ? -13.41713 3.13453   57.95760 1.000 15.07962 ? 128 LEU A N   1 
ATOM   991  C CA  . LEU A 1 134 ? -12.03702 2.64447   58.02502 1.000 13.97331 ? 128 LEU A CA  1 
ATOM   992  C C   . LEU A 1 134 ? -11.94303 1.22933   57.46858 1.000 14.08706 ? 128 LEU A C   1 
ATOM   993  O O   . LEU A 1 134 ? -10.99520 0.89414   56.72858 1.000 14.75047 ? 128 LEU A O   1 
ATOM   994  C CB  . LEU A 1 134 ? -11.53560 2.64888   59.48319 1.000 14.18463 ? 128 LEU A CB  1 
ATOM   995  C CG  . LEU A 1 134 ? -10.08019 2.20336   59.65888 1.000 14.76923 ? 128 LEU A CG  1 
ATOM   996  C CD1 . LEU A 1 134 ? -9.06067  3.18295   58.99196 1.000 15.97804 ? 128 LEU A CD1 1 
ATOM   997  C CD2 . LEU A 1 134 ? -9.67770  2.08768   61.21352 1.000 16.58086 ? 128 LEU A CD2 1 
ATOM   998  N N   . TYR A 1 135 ? -12.92249 0.36959   57.81476 1.000 12.59179 ? 129 TYR A N   1 
ATOM   999  C CA  . TYR A 1 135 ? -12.92538 -0.97440  57.25079 1.000 12.97753 ? 129 TYR A CA  1 
ATOM   1000 C C   . TYR A 1 135 ? -12.87919 -0.91955  55.71605 1.000 13.54258 ? 129 TYR A C   1 
ATOM   1001 O O   . TYR A 1 135 ? -12.11939 -1.66570  55.07588 1.000 13.95949 ? 129 TYR A O   1 
ATOM   1002 C CB  . TYR A 1 135 ? -14.17452 -1.74433  57.73793 1.000 14.40893 ? 129 TYR A CB  1 
ATOM   1003 C CG  . TYR A 1 135 ? -14.27704 -3.10624  57.07454 1.000 14.68320 ? 129 TYR A CG  1 
ATOM   1004 C CD1 . TYR A 1 135 ? -13.35911 -4.11271  57.40859 1.000 15.76444 ? 129 TYR A CD1 1 
ATOM   1005 C CD2 . TYR A 1 135 ? -15.24329 -3.37862  56.09204 1.000 14.48383 ? 129 TYR A CD2 1 
ATOM   1006 C CE1 . TYR A 1 135 ? -13.39269 -5.37037  56.82229 1.000 15.96338 ? 129 TYR A CE1 1 
ATOM   1007 C CE2 . TYR A 1 135 ? -15.29381 -4.64033  55.47465 1.000 15.57021 ? 129 TYR A CE2 1 
ATOM   1008 C CZ  . TYR A 1 135 ? -14.35772 -5.61176  55.79503 1.000 15.99081 ? 129 TYR A CZ  1 
ATOM   1009 O OH  . TYR A 1 135 ? -14.40324 -6.81719  55.17374 1.000 17.16762 ? 129 TYR A OH  1 
ATOM   1010 N N   . GLN A 1 136 ? -13.76832 -0.09665  55.10321 1.000 12.01971 ? 130 GLN A N   1 
ATOM   1011 C CA  . GLN A 1 136 ? -13.83283 -0.08436  53.63839 1.000 12.27706 ? 130 GLN A CA  1 
ATOM   1012 C C   . GLN A 1 136 ? -12.57001 0.49024   53.01021 1.000 13.13151 ? 130 GLN A C   1 
ATOM   1013 O O   . GLN A 1 136 ? -12.13767 0.01449   51.94720 1.000 13.51336 ? 130 GLN A O   1 
ATOM   1014 C CB  . GLN A 1 136 ? -15.04528 0.71593   53.19934 1.000 13.62325 ? 130 GLN A CB  1 
ATOM   1015 C CG  . GLN A 1 136 ? -16.35563 0.06597   53.62427 0.900 14.33694 ? 130 GLN A CG  1 
ATOM   1016 C CD  . GLN A 1 136 ? -17.52139 0.94556   53.13501 0.900 14.64568 ? 130 GLN A CD  1 
ATOM   1017 O OE1 . GLN A 1 136 ? -17.97309 0.84123   51.96038 0.800 14.05618 ? 130 GLN A OE1 1 
ATOM   1018 N NE2 . GLN A 1 136 ? -17.93640 1.87008   53.98410 0.800 14.95358 ? 130 GLN A NE2 1 
ATOM   1019 N N   . ILE A 1 137 ? -11.94665 1.48646   53.65887 1.000 11.87907 ? 131 ILE A N   1 
ATOM   1020 C CA  . ILE A 1 137 ? -10.67945 2.02092   53.15328 1.000 12.14526 ? 131 ILE A CA  1 
ATOM   1021 C C   . ILE A 1 137 ? -9.62741  0.90629   53.12351 1.000 12.00453 ? 131 ILE A C   1 
ATOM   1022 O O   . ILE A 1 137 ? -8.94244  0.70162   52.12040 1.000 12.33280 ? 131 ILE A O   1 
ATOM   1023 C CB  . ILE A 1 137 ? -10.17843 3.19348   54.04026 1.000 12.64314 ? 131 ILE A CB  1 
ATOM   1024 C CG1 . ILE A 1 137 ? -11.11248 4.41427   54.00233 1.000 13.05334 ? 131 ILE A CG1 1 
ATOM   1025 C CG2 . ILE A 1 137 ? -8.79384  3.62285   53.58515 1.000 13.56514 ? 131 ILE A CG2 1 
ATOM   1026 C CD1 . ILE A 1 137 ? -10.93656 5.45801   55.08494 1.000 12.71645 ? 131 ILE A CD1 1 
ATOM   1027 N N   . LEU A 1 138 ? -9.49213  0.16878   54.23799 1.000 12.93634 ? 132 LEU A N   1 
ATOM   1028 C CA  . LEU A 1 138 ? -8.47552  -0.90259  54.33172 1.000 12.35711 ? 132 LEU A CA  1 
ATOM   1029 C C   . LEU A 1 138 ? -8.80968  -2.07532  53.42235 1.000 12.58626 ? 132 LEU A C   1 
ATOM   1030 O O   . LEU A 1 138 ? -7.91434  -2.72669  52.88136 1.000 12.09770 ? 132 LEU A O   1 
ATOM   1031 C CB  . LEU A 1 138 ? -8.34663  -1.40008  55.79125 1.000 13.22628 ? 132 LEU A CB  1 
ATOM   1032 C CG  . LEU A 1 138 ? -7.76060  -0.34503  56.73221 1.000 13.31470 ? 132 LEU A CG  1 
ATOM   1033 C CD1 . LEU A 1 138 ? -8.01414  -0.79544  58.20491 1.000 13.43383 ? 132 LEU A CD1 1 
ATOM   1034 C CD2 . LEU A 1 138 ? -6.23218  -0.09683  56.44457 1.000 14.28700 ? 132 LEU A CD2 1 
ATOM   1035 N N   . ARG A 1 139 ? -10.10132 -2.35264  53.20894 1.000 12.19284 ? 133 ARG A N   1 
ATOM   1036 C CA  . ARG A 1 139 ? -10.47439 -3.44804  52.32091 1.000 11.73592 ? 133 ARG A CA  1 
ATOM   1037 C C   . ARG A 1 139 ? -10.06077 -3.10623  50.87959 1.000 12.07933 ? 133 ARG A C   1 
ATOM   1038 O O   . ARG A 1 139 ? -9.49117  -3.93991  50.15621 1.000 12.51076 ? 133 ARG A O   1 
ATOM   1039 C CB  . ARG A 1 139 ? -12.00332 -3.65368  52.42407 1.000 11.77918 ? 133 ARG A CB  1 
ATOM   1040 C CG  . ARG A 1 139 ? -12.51471 -4.79582  51.58623 0.900 11.83634 ? 133 ARG A CG  1 
ATOM   1041 C CD  . ARG A 1 139 ? -14.00310 -5.10226  51.90640 0.900 12.79423 ? 133 ARG A CD  1 
ATOM   1042 N NE  . ARG A 1 139 ? -14.55880 -6.22511  51.15561 0.800 13.05509 ? 133 ARG A NE  1 
ATOM   1043 C CZ  . ARG A 1 139 ? -15.41115 -6.07120  50.15866 0.700 14.66702 ? 133 ARG A CZ  1 
ATOM   1044 N NH1 . ARG A 1 139 ? -15.74807 -4.86539  49.73068 0.700 15.93526 ? 133 ARG A NH1 1 
ATOM   1045 N NH2 . ARG A 1 139 ? -15.95172 -7.14737  49.59383 0.700 15.08725 ? 133 ARG A NH2 1 
ATOM   1046 N N   . GLY A 1 140 ? -10.34377 -1.87970  50.43579 1.000 12.40847 ? 134 GLY A N   1 
ATOM   1047 C CA  . GLY A 1 140 ? -9.84963  -1.46724  49.10337 1.000 12.39732 ? 134 GLY A CA  1 
ATOM   1048 C C   . GLY A 1 140 ? -8.33156  -1.43678  49.03143 1.000 12.25634 ? 134 GLY A C   1 
ATOM   1049 O O   . GLY A 1 140 ? -7.72235  -1.86461  48.03101 1.000 12.33540 ? 134 GLY A O   1 
ATOM   1050 N N   . LEU A 1 141 ? -7.70070  -0.89959  50.07181 1.000 12.82383 ? 135 LEU A N   1 
ATOM   1051 C CA  . LEU A 1 141 ? -6.22893  -0.84496  50.08215 1.000 12.65667 ? 135 LEU A CA  1 
ATOM   1052 C C   . LEU A 1 141 ? -5.60573  -2.24874  50.06106 1.000 12.63334 ? 135 LEU A C   1 
ATOM   1053 O O   . LEU A 1 141 ? -4.53839  -2.44420  49.45458 1.000 14.28365 ? 135 LEU A O   1 
ATOM   1054 C CB  . LEU A 1 141 ? -5.77705  -0.04269  51.30934 1.000 12.81688 ? 135 LEU A CB  1 
ATOM   1055 C CG  . LEU A 1 141 ? -4.26094  0.31217   51.28416 1.000 11.54636 ? 135 LEU A CG  1 
ATOM   1056 C CD1 . LEU A 1 141 ? -3.97887  1.20637   50.02034 1.000 14.21829 ? 135 LEU A CD1 1 
ATOM   1057 C CD2 . LEU A 1 141 ? -3.78295  1.04220   52.55592 1.000 14.63609 ? 135 LEU A CD2 1 
ATOM   1058 N N   . LYS A 1 142 ? -6.24019  -3.25788  50.70743 1.000 12.50995 ? 136 LYS A N   1 
ATOM   1059 C CA  . LYS A 1 142 ? -5.68937  -4.61322  50.64568 1.000 12.92176 ? 136 LYS A CA  1 
ATOM   1060 C C   . LYS A 1 142 ? -5.59056  -5.06300  49.18910 1.000 13.94744 ? 136 LYS A C   1 
ATOM   1061 O O   . LYS A 1 142 ? -4.60484  -5.67622  48.77001 1.000 14.09462 ? 136 LYS A O   1 
ATOM   1062 C CB  . LYS A 1 142 ? -6.57294  -5.58031  51.42188 1.000 12.13851 ? 136 LYS A CB  1 
ATOM   1063 C CG  . LYS A 1 142 ? -6.11538  -7.00631  51.32516 1.000 13.19619 ? 136 LYS A CG  1 
ATOM   1064 C CD  . LYS A 1 142 ? -7.07558  -8.02884  51.94995 1.000 13.83656 ? 136 LYS A CD  1 
ATOM   1065 C CE  . LYS A 1 142 ? -6.55453  -9.51219  51.79808 1.000 15.18006 ? 136 LYS A CE  1 
ATOM   1066 N NZ  . LYS A 1 142 ? -7.53772  -10.51942 52.35514 1.000 15.96573 ? 136 LYS A NZ  1 
ATOM   1067 N N   . TYR A 1 143 ? -6.63407  -4.78287  48.41267 1.000 13.68120 ? 137 TYR A N   1 
ATOM   1068 C CA  . TYR A 1 143 ? -6.63686  -5.16584  46.99870 1.000 13.16693 ? 137 TYR A CA  1 
ATOM   1069 C C   . TYR A 1 143 ? -5.54281  -4.41997  46.22042 1.000 14.43493 ? 137 TYR A C   1 
ATOM   1070 O O   . TYR A 1 143 ? -4.76538  -5.03560  45.46903 1.000 14.56777 ? 137 TYR A O   1 
ATOM   1071 C CB  . TYR A 1 143 ? -8.04377  -4.87673  46.41596 1.000 13.31596 ? 137 TYR A CB  1 
ATOM   1072 C CG  . TYR A 1 143 ? -8.19310  -5.25521  44.94987 1.000 14.51852 ? 137 TYR A CG  1 
ATOM   1073 C CD1 . TYR A 1 143 ? -7.90973  -4.34790  43.91971 1.000 14.85663 ? 137 TYR A CD1 1 
ATOM   1074 C CD2 . TYR A 1 143 ? -8.63719  -6.53121  44.59668 1.000 14.97163 ? 137 TYR A CD2 1 
ATOM   1075 C CE1 . TYR A 1 143 ? -8.10044  -4.71082  42.57077 1.000 16.85074 ? 137 TYR A CE1 1 
ATOM   1076 C CE2 . TYR A 1 143 ? -8.80361  -6.90550  43.24309 1.000 15.25331 ? 137 TYR A CE2 1 
ATOM   1077 C CZ  . TYR A 1 143 ? -8.54152  -5.95487  42.25833 1.000 17.17431 ? 137 TYR A CZ  1 
ATOM   1078 O OH  . TYR A 1 143 ? -8.67005  -6.22731  40.91518 1.000 17.36735 ? 137 TYR A OH  1 
ATOM   1079 N N   . ILE A 1 144 ? -5.43967  -3.09687  46.42838 1.000 13.49679 ? 138 ILE A N   1 
ATOM   1080 C CA  . ILE A 1 144 ? -4.42741  -2.29649  45.74825 1.000 13.44088 ? 138 ILE A CA  1 
ATOM   1081 C C   . ILE A 1 144 ? -3.02573  -2.82700  46.04775 1.000 13.64082 ? 138 ILE A C   1 
ATOM   1082 O O   . ILE A 1 144 ? -2.22948  -3.09491  45.13723 1.000 15.25462 ? 138 ILE A O   1 
ATOM   1083 C CB  . ILE A 1 144 ? -4.55769  -0.81971  46.17693 1.000 12.22953 ? 138 ILE A CB  1 
ATOM   1084 C CG1 . ILE A 1 144 ? -5.94319  -0.28000  45.80929 1.000 12.53272 ? 138 ILE A CG1 1 
ATOM   1085 C CG2 . ILE A 1 144 ? -3.42382  0.03239   45.61488 1.000 12.95166 ? 138 ILE A CG2 1 
ATOM   1086 C CD1 . ILE A 1 144 ? -6.20258  1.04371   46.50324 1.000 14.60961 ? 138 ILE A CD1 1 
ATOM   1087 N N   . HIS A 1 145 ? -2.71104  -3.01846  47.33934 1.000 12.15385 ? 139 HIS A N   1 
ATOM   1088 C CA  . HIS A 1 145 ? -1.36499  -3.49939  47.69533 1.000 11.92867 ? 139 HIS A CA  1 
ATOM   1089 C C   . HIS A 1 145 ? -1.13652  -4.93740  47.21158 1.000 14.37899 ? 139 HIS A C   1 
ATOM   1090 O O   . HIS A 1 145 ? 0.01088   -5.32878  46.90323 1.000 16.04022 ? 139 HIS A O   1 
ATOM   1091 C CB  . HIS A 1 145 ? -1.18038  -3.43301  49.22471 1.000 12.79678 ? 139 HIS A CB  1 
ATOM   1092 C CG  . HIS A 1 145 ? -0.92551  -2.05595  49.70670 1.000 13.71052 ? 139 HIS A CG  1 
ATOM   1093 N ND1 . HIS A 1 145 ? -0.73509  -1.74057  51.04633 1.000 13.38485 ? 139 HIS A ND1 1 
ATOM   1094 C CD2 . HIS A 1 145 ? -0.82929  -0.88904  49.01897 1.000 13.78351 ? 139 HIS A CD2 1 
ATOM   1095 C CE1 . HIS A 1 145 ? -0.50835  -0.44617  51.15623 1.000 14.43620 ? 139 HIS A CE1 1 
ATOM   1096 N NE2 . HIS A 1 145 ? -0.54460  0.09841   49.94357 1.000 13.57877 ? 139 HIS A NE2 1 
ATOM   1097 N N   . SER A 1 146 ? -2.18811  -5.74383  47.13904 1.000 14.81349 ? 140 SER A N   1 
ATOM   1098 C CA  . SER A 1 146 ? -2.00708  -7.12017  46.64339 1.000 14.40122 ? 140 SER A CA  1 
ATOM   1099 C C   . SER A 1 146 ? -1.64110  -7.12160  45.15545 1.000 16.57338 ? 140 SER A C   1 
ATOM   1100 O O   . SER A 1 146 ? -1.09970  -8.10752  44.63947 1.000 18.87465 ? 140 SER A O   1 
ATOM   1101 C CB  . SER A 1 146 ? -3.29027  -7.95992  46.85675 1.000 14.62509 ? 140 SER A CB  1 
ATOM   1102 O OG  . SER A 1 146 ? -4.31290  -7.56561  45.92810 1.000 16.72652 ? 140 SER A OG  1 
ATOM   1103 N N   . ALA A 1 147 ? -1.93857  -6.02820  44.45681 1.000 15.67900 ? 141 ALA A N   1 
ATOM   1104 C CA  . ALA A 1 147 ? -1.53009  -5.88876  43.06685 1.000 16.32592 ? 141 ALA A CA  1 
ATOM   1105 C C   . ALA A 1 147 ? -0.14683  -5.29790  42.94137 1.000 18.01707 ? 141 ALA A C   1 
ATOM   1106 O O   . ALA A 1 147 ? 0.27808   -5.02246  41.81722 1.000 20.17788 ? 141 ALA A O   1 
ATOM   1107 C CB  . ALA A 1 147 ? -2.52854  -5.00569  42.29726 1.000 16.81124 ? 141 ALA A CB  1 
ATOM   1108 N N   . ASN A 1 148 ? 0.56516   -5.11974  44.05269 1.000 18.08382 ? 142 ASN A N   1 
ATOM   1109 C CA  . ASN A 1 148 ? 1.91129   -4.53301  44.04753 1.000 19.16973 ? 142 ASN A CA  1 
ATOM   1110 C C   . ASN A 1 148 ? 1.86963   -3.06605  43.65123 1.000 18.48750 ? 142 ASN A C   1 
ATOM   1111 O O   . ASN A 1 148 ? 2.83639   -2.53553  43.10580 1.000 18.93307 ? 142 ASN A O   1 
ATOM   1112 C CB  . ASN A 1 148 ? 2.85266   -5.30166  43.10324 1.000 21.45501 ? 142 ASN A CB  1 
ATOM   1113 C CG  . ASN A 1 148 ? 4.31106   -5.12899  43.49611 0.800 24.31591 ? 142 ASN A CG  1 
ATOM   1114 O OD1 . ASN A 1 148 ? 4.61309   -5.05154  44.68068 0.800 24.83332 ? 142 ASN A OD1 1 
ATOM   1115 N ND2 . ASN A 1 148 ? 5.22219   -5.08368  42.49625 0.800 26.19986 ? 142 ASN A ND2 1 
ATOM   1116 N N   . VAL A 1 149 ? 0.73591   -2.40310  43.89056 1.000 17.57263 ? 143 VAL A N   1 
ATOM   1117 C CA  . VAL A 1 149 ? 0.53598   -0.99186  43.55980 1.000 16.27811 ? 143 VAL A CA  1 
ATOM   1118 C C   . VAL A 1 149 ? 0.41976   -0.17971  44.85265 1.000 16.21228 ? 143 VAL A C   1 
ATOM   1119 O O   . VAL A 1 149 ? -0.12585  -0.66667  45.85426 1.000 15.99650 ? 143 VAL A O   1 
ATOM   1120 C CB  . VAL A 1 149 ? -0.75315  -0.83863  42.68636 1.000 16.97584 ? 143 VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 149 ? -1.15040  0.62411   42.56215 1.000 18.04257 ? 143 VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 149 ? -0.51456  -1.45561  41.33269 1.000 17.84808 ? 143 VAL A CG2 1 
ATOM   1123 N N   . LEU A 1 150 ? 0.94147   1.05218   44.83335 1.000 15.89900 ? 144 LEU A N   1 
ATOM   1124 C CA  . LEU A 1 150 ? 0.82525   2.03931   45.90687 1.000 15.10558 ? 144 LEU A CA  1 
ATOM   1125 C C   . LEU A 1 150 ? -0.06075  3.17268   45.42099 1.000 14.07889 ? 144 LEU A C   1 
ATOM   1126 O O   . LEU A 1 150 ? 0.15231   3.64814   44.30795 1.000 15.67903 ? 144 LEU A O   1 
ATOM   1127 C CB  . LEU A 1 150 ? 2.20372   2.64038   46.22895 1.000 17.18769 ? 144 LEU A CB  1 
ATOM   1128 C CG  . LEU A 1 150 ? 3.32309   1.59921   46.36387 1.000 18.88631 ? 144 LEU A CG  1 
ATOM   1129 C CD1 . LEU A 1 150 ? 4.62733   2.31820   46.51304 1.000 18.24091 ? 144 LEU A CD1 1 
ATOM   1130 C CD2 . LEU A 1 150 ? 2.96801   0.77766   47.60312 1.000 20.84915 ? 144 LEU A CD2 1 
ATOM   1131 N N   . HIS A 1 151 ? -1.05234  3.59226   46.22430 1.000 13.15837 ? 145 HIS A N   1 
ATOM   1132 C CA  . HIS A 1 151 ? -1.90371  4.69083   45.78512 1.000 13.31262 ? 145 HIS A CA  1 
ATOM   1133 C C   . HIS A 1 151 ? -1.13953  6.02466   45.82094 1.000 14.33899 ? 145 HIS A C   1 
ATOM   1134 O O   . HIS A 1 151 ? -1.16397  6.82101   44.84773 1.000 14.38239 ? 145 HIS A O   1 
ATOM   1135 C CB  . HIS A 1 151 ? -3.17849  4.74156   46.65664 1.000 12.40922 ? 145 HIS A CB  1 
ATOM   1136 C CG  . HIS A 1 151 ? -4.15130  5.80658   46.25508 1.000 11.92439 ? 145 HIS A CG  1 
ATOM   1137 N ND1 . HIS A 1 151 ? -3.92976  7.13900   46.54516 1.000 12.60329 ? 145 HIS A ND1 1 
ATOM   1138 C CD2 . HIS A 1 151 ? -5.34962  5.74022   45.60453 1.000 12.85057 ? 145 HIS A CD2 1 
ATOM   1139 C CE1 . HIS A 1 151 ? -4.96402  7.84604   46.10042 1.000 13.80713 ? 145 HIS A CE1 1 
ATOM   1140 N NE2 . HIS A 1 151 ? -5.83454  7.01632   45.52463 1.000 13.90713 ? 145 HIS A NE2 1 
ATOM   1141 N N   . ARG A 1 152 ? -0.46694  6.27881   46.94572 1.000 13.40636 ? 146 ARG A N   1 
ATOM   1142 C CA  . ARG A 1 152 ? 0.44003   7.39931   47.15421 1.000 14.15459 ? 146 ARG A CA  1 
ATOM   1143 C C   . ARG A 1 152 ? -0.24259  8.74629   47.28244 1.000 16.65987 ? 146 ARG A C   1 
ATOM   1144 O O   . ARG A 1 152 ? 0.46321   9.75912   47.36567 1.000 19.70321 ? 146 ARG A O   1 
ATOM   1145 C CB  . ARG A 1 152 ? 1.53823   7.48411   46.08956 0.900 14.99974 ? 146 ARG A CB  1 
ATOM   1146 C CG  . ARG A 1 152 ? 2.42381   6.27095   46.17982 0.900 16.73517 ? 146 ARG A CG  1 
ATOM   1147 C CD  . ARG A 1 152 ? 3.47531   6.18344   45.07415 0.800 19.18764 ? 146 ARG A CD  1 
ATOM   1148 N NE  . ARG A 1 152 ? 4.63490   6.99196   45.38477 0.700 23.38957 ? 146 ARG A NE  1 
ATOM   1149 C CZ  . ARG A 1 152 ? 5.05934   7.97354   44.60684 0.700 24.53434 ? 146 ARG A CZ  1 
ATOM   1150 N NH1 . ARG A 1 152 ? 4.36476   8.36316   43.57753 0.700 25.04867 ? 146 ARG A NH1 1 
ATOM   1151 N NH2 . ARG A 1 152 ? 6.23480   8.54537   44.84895 0.700 23.56413 ? 146 ARG A NH2 1 
ATOM   1152 N N   . ASP A 1 153 ? -1.58219  8.82078   47.33100 1.000 14.62940 ? 147 ASP A N   1 
ATOM   1153 C CA  . ASP A 1 153 ? -2.20399  10.12904  47.60479 1.000 15.09446 ? 147 ASP A CA  1 
ATOM   1154 C C   . ASP A 1 153 ? -3.52409  9.93253   48.32103 1.000 14.58698 ? 147 ASP A C   1 
ATOM   1155 O O   . ASP A 1 153 ? -4.51099  10.63390  48.04152 1.000 14.97395 ? 147 ASP A O   1 
ATOM   1156 C CB  . ASP A 1 153 ? -2.40998  10.97715  46.32261 1.000 15.64658 ? 147 ASP A CB  1 
ATOM   1157 C CG  . ASP A 1 153 ? -2.54223  12.48188  46.61086 1.000 17.73925 ? 147 ASP A CG  1 
ATOM   1158 O OD1 . ASP A 1 153 ? -2.14251  12.95734  47.71589 1.000 17.90626 ? 147 ASP A OD1 1 
ATOM   1159 O OD2 . ASP A 1 153 ? -3.06280  13.22664  45.71793 1.000 19.28339 ? 147 ASP A OD2 1 
ATOM   1160 N N   . LEU A 1 154 ? -3.55144  9.02911   49.30326 1.000 14.05859 ? 148 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 154 ? -4.79609  8.82431   50.06103 1.000 13.96191 ? 148 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 154 ? -5.04627  10.02157  50.97792 1.000 15.02798 ? 148 LEU A C   1 
ATOM   1163 O O   . LEU A 1 154 ? -4.12692  10.46765  51.68584 1.000 14.29840 ? 148 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 154 ? -4.72186  7.54546   50.88321 1.000 14.21830 ? 148 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 154 ? -4.61374  6.24910   50.04588 1.000 12.80055 ? 148 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 154 ? -4.25357  5.03688   50.96158 1.000 13.22721 ? 148 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 154 ? -5.98409  5.97441   49.27312 1.000 13.57407 ? 148 LEU A CD2 1 
ATOM   1168 N N   . LYS A 1 155 ? -6.28258  10.53226  50.98056 1.000 14.26561 ? 149 LYS A N   1 
ATOM   1169 C CA  . LYS A 1 155 ? -6.69541  11.69254  51.77029 1.000 13.23893 ? 149 LYS A CA  1 
ATOM   1170 C C   . LYS A 1 155 ? -8.22384  11.77851  51.68834 1.000 13.87188 ? 149 LYS A C   1 
ATOM   1171 O O   . LYS A 1 155 ? -8.81987  11.13196  50.84458 1.000 13.65642 ? 149 LYS A O   1 
ATOM   1172 C CB  . LYS A 1 155 ? -6.06795  12.99069  51.24732 1.000 14.56805 ? 149 LYS A CB  1 
ATOM   1173 C CG  . LYS A 1 155 ? -6.38736  13.31644  49.75285 1.000 15.36159 ? 149 LYS A CG  1 
ATOM   1174 C CD  . LYS A 1 155 ? -5.58254  14.52867  49.29047 1.000 17.03592 ? 149 LYS A CD  1 
ATOM   1175 C CE  . LYS A 1 155 ? -5.71333  14.73973  47.78230 1.000 18.57619 ? 149 LYS A CE  1 
ATOM   1176 N NZ  . LYS A 1 155 ? -5.01233  16.02527  47.39817 1.000 20.99861 ? 149 LYS A NZ  1 
ATOM   1177 N N   . PRO A 1 156 ? -8.85531  12.56208  52.55160 1.000 14.75014 ? 150 PRO A N   1 
ATOM   1178 C CA  . PRO A 1 156 ? -10.32892 12.52617  52.58104 1.000 14.95664 ? 150 PRO A CA  1 
ATOM   1179 C C   . PRO A 1 156 ? -11.00255 12.84066  51.24999 1.000 15.36748 ? 150 PRO A C   1 
ATOM   1180 O O   . PRO A 1 156 ? -12.05176 12.22261  50.92012 1.000 16.03995 ? 150 PRO A O   1 
ATOM   1181 C CB  . PRO A 1 156 ? -10.66686 13.52082  53.71152 1.000 16.35026 ? 150 PRO A CB  1 
ATOM   1182 C CG  . PRO A 1 156 ? -9.46131  13.36859  54.67290 1.000 14.72286 ? 150 PRO A CG  1 
ATOM   1183 C CD  . PRO A 1 156 ? -8.27055  13.25492  53.73390 1.000 15.10885 ? 150 PRO A CD  1 
ATOM   1184 N N   . SER A 1 157 ? -10.46079 13.79151  50.47980 1.000 14.80051 ? 151 SER A N   1 
ATOM   1185 C CA  . SER A 1 157 ? -11.13569 14.19527  49.22976 1.000 17.16067 ? 151 SER A CA  1 
ATOM   1186 C C   . SER A 1 157 ? -11.02747 13.10094  48.14251 1.000 16.51533 ? 151 SER A C   1 
ATOM   1187 O O   . SER A 1 157 ? -11.71295 13.20205  47.10579 1.000 17.83989 ? 151 SER A O   1 
ATOM   1188 C CB  . SER A 1 157 ? -10.55535 15.53615  48.71131 1.000 18.89038 ? 151 SER A CB  1 
ATOM   1189 O OG  . SER A 1 157 ? -9.17479  15.37761  48.28609 1.000 19.33164 ? 151 SER A OG  1 
ATOM   1190 N N   . ASN A 1 158 ? -10.22756 12.05065  48.36632 1.000 16.02569 ? 152 ASN A N   1 
ATOM   1191 C CA  . ASN A 1 158 ? -10.14823 10.91153  47.44749 1.000 15.10206 ? 152 ASN A CA  1 
ATOM   1192 C C   . ASN A 1 158 ? -10.95650 9.71057   47.90995 1.000 16.97936 ? 152 ASN A C   1 
ATOM   1193 O O   . ASN A 1 158 ? -10.78986 8.60400   47.35884 1.000 16.86108 ? 152 ASN A O   1 
ATOM   1194 C CB  . ASN A 1 158 ? -8.68053  10.49586  47.19662 1.000 15.02004 ? 152 ASN A CB  1 
ATOM   1195 C CG  . ASN A 1 158 ? -8.02278  11.39669  46.16715 1.000 16.23911 ? 152 ASN A CG  1 
ATOM   1196 O OD1 . ASN A 1 158 ? -8.72562  12.01406  45.32566 1.000 18.71028 ? 152 ASN A OD1 1 
ATOM   1197 N ND2 . ASN A 1 158 ? -6.70336  11.53719  46.24167 1.000 16.45746 ? 152 ASN A ND2 1 
ATOM   1198 N N   . LEU A 1 159 ? -11.83408 9.90574   48.90921 1.000 15.49215 ? 153 LEU A N   1 
ATOM   1199 C CA  . LEU A 1 159 ? -12.70168 8.84969   49.43451 1.000 15.13044 ? 153 LEU A CA  1 
ATOM   1200 C C   . LEU A 1 159 ? -14.13336 9.30402   49.16389 1.000 16.05580 ? 153 LEU A C   1 
ATOM   1201 O O   . LEU A 1 159 ? -14.62118 10.23820  49.80811 1.000 18.27189 ? 153 LEU A O   1 
ATOM   1202 C CB  . LEU A 1 159 ? -12.43814 8.58648   50.93754 1.000 14.82369 ? 153 LEU A CB  1 
ATOM   1203 C CG  . LEU A 1 159 ? -10.94259 8.24971   51.23040 1.000 14.52663 ? 153 LEU A CG  1 
ATOM   1204 C CD1 . LEU A 1 159 ? -10.67458 8.08957   52.73869 1.000 14.35025 ? 153 LEU A CD1 1 
ATOM   1205 C CD2 . LEU A 1 159 ? -10.51458 6.97166   50.47788 1.000 16.17402 ? 153 LEU A CD2 1 
ATOM   1206 N N   . LEU A 1 160 ? -14.78127 8.67079   48.19946 1.000 15.02791 ? 154 LEU A N   1 
ATOM   1207 C CA  . LEU A 1 160 ? -16.15472 9.01147   47.82841 1.000 15.98957 ? 154 LEU A CA  1 
ATOM   1208 C C   . LEU A 1 160 ? -17.14712 8.11461   48.57427 1.000 17.02132 ? 154 LEU A C   1 
ATOM   1209 O O   . LEU A 1 160 ? -16.87210 6.93821   48.83054 1.000 17.05094 ? 154 LEU A O   1 
ATOM   1210 C CB  . LEU A 1 160 ? -16.36000 8.80005   46.32930 1.000 17.46549 ? 154 LEU A CB  1 
ATOM   1211 C CG  . LEU A 1 160 ? -15.44853 9.56088   45.37127 1.000 22.78200 ? 154 LEU A CG  1 
ATOM   1212 C CD1 . LEU A 1 160 ? -15.53763 9.04634   43.84693 1.000 23.88689 ? 154 LEU A CD1 1 
ATOM   1213 C CD2 . LEU A 1 160 ? -15.68212 11.00211  45.46632 1.000 26.57281 ? 154 LEU A CD2 1 
ATOM   1214 N N   . LEU A 1 161 ? -18.34543 8.67973   48.86855 1.000 18.15605 ? 155 LEU A N   1 
ATOM   1215 C CA  . LEU A 1 161 ? -19.40079 8.01070   49.61071 1.000 18.92230 ? 155 LEU A CA  1 
ATOM   1216 C C   . LEU A 1 161 ? -20.70203 8.15514   48.86365 1.000 19.98732 ? 155 LEU A C   1 
ATOM   1217 O O   . LEU A 1 161 ? -21.00429 9.24305   48.35812 1.000 21.15599 ? 155 LEU A O   1 
ATOM   1218 C CB  . LEU A 1 161 ? -19.58873 8.60738   51.01614 1.000 20.00739 ? 155 LEU A CB  1 
ATOM   1219 C CG  . LEU A 1 161 ? -18.24552 8.49111   51.72459 1.000 22.80314 ? 155 LEU A CG  1 
ATOM   1220 C CD1 . LEU A 1 161 ? -18.00858 9.66908   52.61733 1.000 25.54232 ? 155 LEU A CD1 1 
ATOM   1221 C CD2 . LEU A 1 161 ? -18.20292 7.16070   52.40329 1.000 23.52859 ? 155 LEU A CD2 1 
ATOM   1222 N N   . ASN A 1 162 ? -21.49465 7.07414   48.84201 1.000 20.05792 ? 156 ASN A N   1 
ATOM   1223 C CA  . ASN A 1 162 ? -22.85809 7.20170   48.31270 1.000 20.97668 ? 156 ASN A CA  1 
ATOM   1224 C C   . ASN A 1 162 ? -23.84011 7.43657   49.45851 1.000 22.16132 ? 156 ASN A C   1 
ATOM   1225 O O   . ASN A 1 162 ? -23.42320 7.63508   50.61359 1.000 22.28103 ? 156 ASN A O   1 
ATOM   1226 C CB  . ASN A 1 162 ? -23.24398 6.00024   47.46241 1.000 22.33296 ? 156 ASN A CB  1 
ATOM   1227 C CG  . ASN A 1 162 ? -23.35853 4.74509   48.24186 1.000 25.17155 ? 156 ASN A CG  1 
ATOM   1228 O OD1 . ASN A 1 162 ? -23.42675 4.74825   49.47282 1.000 24.41143 ? 156 ASN A OD1 1 
ATOM   1229 N ND2 . ASN A 1 162 ? -23.42294 3.62803   47.51795 1.000 27.42988 ? 156 ASN A ND2 1 
ATOM   1230 N N   . THR A 1 163 ? -25.17517 7.39856   49.13863 1.000 23.40065 ? 157 THR A N   1 
ATOM   1231 C CA  . THR A 1 163 ? -26.16392 7.87293   50.13423 1.000 24.28456 ? 157 THR A CA  1 
ATOM   1232 C C   . THR A 1 163 ? -26.29265 6.87671   51.28195 1.000 24.58808 ? 157 THR A C   1 
ATOM   1233 O O   . THR A 1 163 ? -26.83261 7.22516   52.33614 1.000 26.01132 ? 157 THR A O   1 
ATOM   1234 C CB  . THR A 1 163 ? -27.60698 8.14617   49.54421 1.000 29.44557 ? 157 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 163 ? -28.19620 6.94848   49.06074 1.000 31.90823 ? 157 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 163 ? -27.44826 8.90863   48.31123 1.000 31.80013 ? 157 THR A CG2 1 
ATOM   1237 N N   . THR A 1 164 ? -25.78443 5.65207   51.11025 1.000 24.12189 ? 158 THR A N   1 
ATOM   1238 C CA  . THR A 1 164 ? -25.83132 4.62758   52.14951 1.000 24.74250 ? 158 THR A CA  1 
ATOM   1239 C C   . THR A 1 164 ? -24.44967 4.35642   52.68225 1.000 23.93935 ? 158 THR A C   1 
ATOM   1240 O O   . THR A 1 164 ? -24.22079 3.31230   53.25938 1.000 25.98645 ? 158 THR A O   1 
ATOM   1241 C CB  . THR A 1 164 ? -26.43649 3.29563   51.62995 1.000 26.04652 ? 158 THR A CB  1 
ATOM   1242 O OG1 . THR A 1 164 ? -25.89975 3.00359   50.34955 1.000 26.15974 ? 158 THR A OG1 1 
ATOM   1243 C CG2 . THR A 1 164 ? -27.92160 3.42360   51.43067 1.000 27.62666 ? 158 THR A CG2 1 
HETATM 1244 N N   . CME A 1 165 ? -23.54355 5.30693   52.48595 1.000 21.58802 ? 159 CME A N   1 
HETATM 1245 C CA  . CME A 1 165 ? -22.19816 5.27198   53.12017 1.000 22.79138 ? 159 CME A CA  1 
HETATM 1246 C CB  . CME A 1 165 ? -22.32837 5.20776   54.67298 1.000 26.69364 ? 159 CME A CB  1 
HETATM 1247 S SG  . CME A 1 165 ? -23.21682 6.60557   55.38020 1.000 29.79258 ? 159 CME A SG  1 
HETATM 1248 S SD  . CME A 1 165 ? -22.19630 8.40240   54.90786 1.000 32.84235 ? 159 CME A SD  1 
HETATM 1249 C CE  . CME A 1 165 ? -22.60043 9.21423   53.39229 1.000 30.51019 ? 159 CME A CE  1 
HETATM 1250 C CZ  . CME A 1 165 ? -23.98251 9.79315   53.32328 1.000 28.80074 ? 159 CME A CZ  1 
HETATM 1251 O OH  . CME A 1 165 ? -24.22993 10.45622  54.57164 1.000 28.31216 ? 159 CME A OH  1 
HETATM 1252 C C   . CME A 1 165 ? -21.28923 4.14634   52.64019 1.000 20.44639 ? 159 CME A C   1 
HETATM 1253 O O   . CME A 1 165 ? -20.29506 3.77357   53.30069 1.000 19.72799 ? 159 CME A O   1 
ATOM   1254 N N   . ASP A 1 166 ? -21.56412 3.63107   51.44041 1.000 19.70810 ? 160 ASP A N   1 
ATOM   1255 C CA  . ASP A 1 166 ? -20.56590 2.77033   50.78888 1.000 19.47454 ? 160 ASP A CA  1 
ATOM   1256 C C   . ASP A 1 166 ? -19.44804 3.69474   50.27721 1.000 17.53679 ? 160 ASP A C   1 
ATOM   1257 O O   . ASP A 1 166 ? -19.72391 4.77828   49.77246 1.000 17.77488 ? 160 ASP A O   1 
ATOM   1258 C CB  . ASP A 1 166 ? -21.18522 1.96729   49.64932 0.700 20.77259 ? 160 ASP A CB  1 
ATOM   1259 C CG  . ASP A 1 166 ? -22.34511 1.10773   50.13560 0.700 24.22794 ? 160 ASP A CG  1 
ATOM   1260 O OD1 . ASP A 1 166 ? -22.20481 0.36489   51.10794 0.700 25.81133 ? 160 ASP A OD1 1 
ATOM   1261 O OD2 . ASP A 1 166 ? -23.43671 1.26258   49.59859 0.700 26.60942 ? 160 ASP A OD2 1 
ATOM   1262 N N   . LEU A 1 167 ? -18.18554 3.25276   50.41947 1.000 16.59337 ? 161 LEU A N   1 
ATOM   1263 C CA  . LEU A 1 167 ? -16.99815 4.06521   50.22017 1.000 15.16340 ? 161 LEU A CA  1 
ATOM   1264 C C   . LEU A 1 167 ? -16.18126 3.51702   49.06317 1.000 16.00169 ? 161 LEU A C   1 
ATOM   1265 O O   . LEU A 1 167 ? -15.98861 2.29179   48.95021 1.000 17.43395 ? 161 LEU A O   1 
ATOM   1266 C CB  . LEU A 1 167 ? -16.15144 4.06615   51.53620 1.000 14.96098 ? 161 LEU A CB  1 
ATOM   1267 C CG  . LEU A 1 167 ? -14.84670 4.88883   51.48420 1.000 15.95800 ? 161 LEU A CG  1 
ATOM   1268 C CD1 . LEU A 1 167 ? -14.48059 5.38418   52.93281 1.000 16.61221 ? 161 LEU A CD1 1 
ATOM   1269 C CD2 . LEU A 1 167 ? -13.65263 4.10537   50.87126 1.000 16.66023 ? 161 LEU A CD2 1 
ATOM   1270 N N   . LYS A 1 168 ? -15.69754 4.42601   48.20233 1.000 14.27331 ? 162 LYS A N   1 
ATOM   1271 C CA  . LYS A 1 168 ? -14.85076 4.04199   47.06226 1.000 14.57737 ? 162 LYS A CA  1 
ATOM   1272 C C   . LYS A 1 168 ? -13.64064 4.97582   46.95693 1.000 15.00682 ? 162 LYS A C   1 
ATOM   1273 O O   . LYS A 1 168 ? -13.76530 6.19568   47.09106 1.000 15.78427 ? 162 LYS A O   1 
ATOM   1274 C CB  . LYS A 1 168 ? -15.63386 4.07840   45.73718 1.000 16.33536 ? 162 LYS A CB  1 
ATOM   1275 C CG  . LYS A 1 168 ? -16.81065 3.09572   45.67000 1.000 17.61887 ? 162 LYS A CG  1 
ATOM   1276 C CD  . LYS A 1 168 ? -17.33523 3.07024   44.22722 1.000 20.36739 ? 162 LYS A CD  1 
ATOM   1277 C CE  . LYS A 1 168 ? -18.69932 2.44683   44.09552 1.000 23.50689 ? 162 LYS A CE  1 
ATOM   1278 N NZ  . LYS A 1 168 ? -18.65301 0.96699   44.29141 1.000 25.65575 ? 162 LYS A NZ  1 
ATOM   1279 N N   . ILE A 1 169 ? -12.46947 4.39187   46.67520 1.000 14.04245 ? 163 ILE A N   1 
ATOM   1280 C CA  . ILE A 1 169 ? -11.20811 5.14633   46.57608 1.000 13.46820 ? 163 ILE A CA  1 
ATOM   1281 C C   . ILE A 1 169 ? -11.08058 5.69755   45.16691 1.000 14.49104 ? 163 ILE A C   1 
ATOM   1282 O O   . ILE A 1 169 ? -11.24004 4.94867   44.20005 1.000 14.97555 ? 163 ILE A O   1 
ATOM   1283 C CB  . ILE A 1 169 ? -10.02185 4.22071   46.90923 1.000 13.37165 ? 163 ILE A CB  1 
ATOM   1284 C CG1 . ILE A 1 169 ? -10.04284 3.76297   48.37522 1.000 12.16182 ? 163 ILE A CG1 1 
ATOM   1285 C CG2 . ILE A 1 169 ? -8.62622  4.88105   46.61643 1.000 15.04130 ? 163 ILE A CG2 1 
ATOM   1286 C CD1 . ILE A 1 169 ? -9.15434  2.53580   48.63851 1.000 14.31299 ? 163 ILE A CD1 1 
ATOM   1287 N N   . CYS A 1 170 ? -10.81230 7.00473   45.05948 1.000 14.88348 ? 164 CYS A N   1 
ATOM   1288 C CA  . CYS A 1 170 ? -10.65413 7.74438   43.81276 1.000 16.17450 ? 164 CYS A CA  1 
ATOM   1289 C C   . CYS A 1 170 ? -9.18489  8.09290   43.57473 1.000 15.88994 ? 164 CYS A C   1 
ATOM   1290 O O   . CYS A 1 170 ? -8.38224  8.19186   44.50201 1.000 15.16447 ? 164 CYS A O   1 
ATOM   1291 C CB  . CYS A 1 170 ? -11.43096 9.07152   43.86076 1.000 17.69862 ? 164 CYS A CB  1 
ATOM   1292 S SG  . CYS A 1 170 ? -11.58768 9.85332   42.26510 1.000 23.41194 ? 164 CYS A SG  1 
ATOM   1293 N N   . ASP A 1 171 ? -8.88512  8.31252   42.29880 1.000 18.13067 ? 165 ASP A N   1 
ATOM   1294 C CA  . ASP A 1 171 ? -7.65766  8.90076   41.73980 1.000 20.24401 ? 165 ASP A CA  1 
ATOM   1295 C C   . ASP A 1 171 ? -6.38263  8.08489   41.84065 1.000 21.58843 ? 165 ASP A C   1 
ATOM   1296 O O   . ASP A 1 171 ? -5.68542  8.13138   42.85959 1.000 23.32431 ? 165 ASP A O   1 
ATOM   1297 C CB  . ASP A 1 171 ? -7.34630  10.23065  42.34927 1.000 21.69636 ? 165 ASP A CB  1 
ATOM   1298 C CG  . ASP A 1 171 ? -6.27273  10.96417  41.54141 1.000 24.38584 ? 165 ASP A CG  1 
ATOM   1299 O OD1 . ASP A 1 171 ? -5.78855  10.41774  40.48807 1.000 24.64828 ? 165 ASP A OD1 1 
ATOM   1300 O OD2 . ASP A 1 171 ? -5.99144  12.10456  41.90386 1.000 25.81945 ? 165 ASP A OD2 1 
ATOM   1301 N N   . PHE A 1 172 ? -6.00122  7.41319   40.76873 1.000 21.38847 ? 166 PHE A N   1 
ATOM   1302 C CA  . PHE A 1 172 ? -4.73590  6.67651   40.76053 1.000 21.10895 ? 166 PHE A CA  1 
ATOM   1303 C C   . PHE A 1 172 ? -3.67602  7.37797   39.91813 1.000 23.76460 ? 166 PHE A C   1 
ATOM   1304 O O   . PHE A 1 172 ? -2.74190  6.75922   39.43453 1.000 22.89107 ? 166 PHE A O   1 
ATOM   1305 C CB  . PHE A 1 172 ? -4.97235  5.23982   40.30634 1.000 20.59121 ? 166 PHE A CB  1 
ATOM   1306 C CG  . PHE A 1 172 ? -5.66831  4.38457   41.39442 1.000 18.31279 ? 166 PHE A CG  1 
ATOM   1307 C CD1 . PHE A 1 172 ? -7.03413  4.54442   41.68448 1.000 18.98672 ? 166 PHE A CD1 1 
ATOM   1308 C CD2 . PHE A 1 172 ? -4.93353  3.49814   42.15946 1.000 17.65588 ? 166 PHE A CD2 1 
ATOM   1309 C CE1 . PHE A 1 172 ? -7.65059  3.83360   42.70937 1.000 17.94463 ? 166 PHE A CE1 1 
ATOM   1310 C CE2 . PHE A 1 172 ? -5.49700  2.78148   43.17010 1.000 16.32178 ? 166 PHE A CE2 1 
ATOM   1311 C CZ  . PHE A 1 172 ? -6.88197  2.92206   43.45657 1.000 16.83157 ? 166 PHE A CZ  1 
ATOM   1312 N N   . GLY A 1 173 ? -3.80940  8.69001   39.75579 1.000 24.95863 ? 167 GLY A N   1 
ATOM   1313 C CA  . GLY A 1 173 ? -2.86131  9.43941   38.94631 1.000 24.34878 ? 167 GLY A CA  1 
ATOM   1314 C C   . GLY A 1 173 ? -1.46666  9.54739   39.54113 1.000 24.59493 ? 167 GLY A C   1 
ATOM   1315 O O   . GLY A 1 173 ? -0.50528  9.74891   38.78117 1.000 26.37519 ? 167 GLY A O   1 
ATOM   1316 N N   . LEU A 1 174 ? -1.32106  9.40535   40.86817 1.000 22.23969 ? 168 LEU A N   1 
ATOM   1317 C CA  . LEU A 1 174 ? 0.00632   9.40363   41.48833 1.000 22.98423 ? 168 LEU A CA  1 
ATOM   1318 C C   . LEU A 1 174 ? 0.50820   8.01161   41.88053 1.000 20.73052 ? 168 LEU A C   1 
ATOM   1319 O O   . LEU A 1 174 ? 1.56924   7.90498   42.52092 1.000 20.03359 ? 168 LEU A O   1 
ATOM   1320 C CB  . LEU A 1 174 ? 0.05814   10.32941  42.71015 0.800 24.13062 ? 168 LEU A CB  1 
ATOM   1321 C CG  . LEU A 1 174 ? -0.36895  11.78060  42.48009 0.600 25.71946 ? 168 LEU A CG  1 
ATOM   1322 C CD1 . LEU A 1 174 ? 0.07618   12.58911  43.71926 0.600 26.73857 ? 168 LEU A CD1 1 
ATOM   1323 C CD2 . LEU A 1 174 ? 0.19786   12.34661  41.19428 0.600 26.30066 ? 168 LEU A CD2 1 
ATOM   1324 N N   . ALA A 1 175 ? -0.22349  6.95781   41.52443 1.000 18.43921 ? 169 ALA A N   1 
ATOM   1325 C CA  . ALA A 1 175 ? 0.11826   5.59156   41.90384 1.000 18.02563 ? 169 ALA A CA  1 
ATOM   1326 C C   . ALA A 1 175 ? 1.40557   5.14038   41.22949 1.000 19.37837 ? 169 ALA A C   1 
ATOM   1327 O O   . ALA A 1 175 ? 1.79985   5.67687   40.17666 1.000 20.19293 ? 169 ALA A O   1 
ATOM   1328 C CB  . ALA A 1 175 ? -1.05720  4.64073   41.56805 1.000 19.30455 ? 169 ALA A CB  1 
ATOM   1329 N N   . ARG A 1 176 ? 2.05930   4.16199   41.85552 1.000 18.85294 ? 170 ARG A N   1 
ATOM   1330 C CA  . ARG A 1 176 ? 3.27337   3.53627   41.32059 1.000 19.65945 ? 170 ARG A CA  1 
ATOM   1331 C C   . ARG A 1 176 ? 3.30728   2.06399   41.71308 1.000 19.06296 ? 170 ARG A C   1 
ATOM   1332 O O   . ARG A 1 176 ? 2.68135   1.64820   42.68210 1.000 19.16353 ? 170 ARG A O   1 
ATOM   1333 C CB  . ARG A 1 176 ? 4.58350   4.16624   41.86934 1.000 21.43131 ? 170 ARG A CB  1 
ATOM   1334 C CG  . ARG A 1 176 ? 4.82052   5.64532   41.57523 0.900 23.39116 ? 170 ARG A CG  1 
ATOM   1335 C CD  . ARG A 1 176 ? 5.12922   5.93180   40.09745 0.800 26.09197 ? 170 ARG A CD  1 
ATOM   1336 N NE  . ARG A 1 176 ? 5.62280   7.29603   39.98259 0.800 27.96196 ? 170 ARG A NE  1 
ATOM   1337 C CZ  . ARG A 1 176 ? 4.87310   8.36966   39.80681 0.700 28.33683 ? 170 ARG A CZ  1 
ATOM   1338 N NH1 . ARG A 1 176 ? 3.55194   8.29950   39.81001 0.600 26.83687 ? 170 ARG A NH1 1 
ATOM   1339 N NH2 . ARG A 1 176 ? 5.46845   9.55553   39.69846 0.500 27.54352 ? 170 ARG A NH2 1 
ATOM   1340 N N   . VAL A 1 177 ? 4.04876   1.26995   40.94562 1.000 19.70987 ? 171 VAL A N   1 
ATOM   1341 C CA  . VAL A 1 177 ? 4.36347   -0.09681  41.34524 1.000 20.08916 ? 171 VAL A CA  1 
ATOM   1342 C C   . VAL A 1 177 ? 5.37267   -0.06797  42.48410 1.000 20.94959 ? 171 VAL A C   1 
ATOM   1343 O O   . VAL A 1 177 ? 6.34275   0.70705   42.44976 1.000 22.21474 ? 171 VAL A O   1 
ATOM   1344 C CB  . VAL A 1 177 ? 4.91576   -0.89963  40.15215 1.000 21.45227 ? 171 VAL A CB  1 
ATOM   1345 C CG1 . VAL A 1 177 ? 5.37655   -2.26641  40.61976 1.000 21.52918 ? 171 VAL A CG1 1 
ATOM   1346 C CG2 . VAL A 1 177 ? 3.83557   -1.06115  39.08207 1.000 22.76567 ? 171 VAL A CG2 1 
ATOM   1347 N N   . ALA A 1 178 ? 5.12617   -0.85956  43.52457 1.000 20.99212 ? 172 ALA A N   1 
ATOM   1348 C CA  . ALA A 1 178 ? 6.00852   -0.83079  44.69577 1.000 23.09657 ? 172 ALA A CA  1 
ATOM   1349 C C   . ALA A 1 178 ? 7.43903   -1.22373  44.33301 1.000 24.51493 ? 172 ALA A C   1 
ATOM   1350 O O   . ALA A 1 178 ? 7.67451   -2.11198  43.49401 1.000 24.29052 ? 172 ALA A O   1 
ATOM   1351 C CB  . ALA A 1 178 ? 5.45962   -1.79158  45.75603 1.000 23.50117 ? 172 ALA A CB  1 
ATOM   1352 N N   . ASP A 1 179 ? 8.40687   -0.56121  44.97747 1.000 24.40410 ? 173 ASP A N   1 
ATOM   1353 C CA  . ASP A 1 179 ? 9.82668   -0.80060  44.70298 1.000 26.22766 ? 173 ASP A CA  1 
ATOM   1354 C C   . ASP A 1 179 ? 10.66077  -0.64679  45.97156 1.000 26.57933 ? 173 ASP A C   1 
ATOM   1355 O O   . ASP A 1 179 ? 11.50174  0.25259   46.08148 1.000 26.18421 ? 173 ASP A O   1 
ATOM   1356 C CB  . ASP A 1 179 ? 10.29940  0.15661   43.61383 1.000 28.66012 ? 173 ASP A CB  1 
ATOM   1357 C CG  . ASP A 1 179 ? 11.69204  -0.21509  43.06296 1.000 31.06950 ? 173 ASP A CG  1 
ATOM   1358 O OD1 . ASP A 1 179 ? 12.25439  -1.25912  43.48061 1.000 31.77212 ? 173 ASP A OD1 1 
ATOM   1359 O OD2 . ASP A 1 179 ? 12.18690  0.51141   42.17720 1.000 32.20283 ? 173 ASP A OD2 1 
ATOM   1360 N N   . PRO A 1 180 ? 10.46573  -1.53151  46.95328 1.000 27.84707 ? 174 PRO A N   1 
ATOM   1361 C CA  . PRO A 1 180 ? 11.13992  -1.33347  48.25478 1.000 29.14909 ? 174 PRO A CA  1 
ATOM   1362 C C   . PRO A 1 180 ? 12.65207  -1.36901  48.18637 1.000 30.48857 ? 174 PRO A C   1 
ATOM   1363 O O   . PRO A 1 180 ? 13.30781  -0.73768  49.03911 1.000 30.82537 ? 174 PRO A O   1 
ATOM   1364 C CB  . PRO A 1 180 ? 10.61371  -2.49302  49.11160 1.000 28.66184 ? 174 PRO A CB  1 
ATOM   1365 C CG  . PRO A 1 180 ? 10.16189  -3.55245  48.10959 1.000 28.43877 ? 174 PRO A CG  1 
ATOM   1366 C CD  . PRO A 1 180 ? 9.64900   -2.76980  46.91988 1.000 27.69087 ? 174 PRO A CD  1 
ATOM   1367 N N   . ASP A 1 181 ? 13.22870  -2.11144  47.22900 1.000 32.01318 ? 175 ASP A N   1 
ATOM   1368 C CA  . ASP A 1 181 ? 14.69504  -2.19259  47.18342 1.000 33.17336 ? 175 ASP A CA  1 
ATOM   1369 C C   . ASP A 1 181 ? 15.33459  -0.92288  46.65416 1.000 32.30041 ? 175 ASP A C   1 
ATOM   1370 O O   . ASP A 1 181 ? 16.55340  -0.75118  46.80807 1.000 34.14311 ? 175 ASP A O   1 
ATOM   1371 C CB  . ASP A 1 181 ? 15.14963  -3.38046  46.31617 0.800 35.83050 ? 175 ASP A CB  1 
ATOM   1372 C CG  . ASP A 1 181 ? 14.72186  -4.70213  46.89502 0.800 38.53129 ? 175 ASP A CG  1 
ATOM   1373 O OD1 . ASP A 1 181 ? 14.51935  -5.64443  46.11139 0.700 40.16171 ? 175 ASP A OD1 1 
ATOM   1374 O OD2 . ASP A 1 181 ? 14.52870  -4.77638  48.12998 0.700 38.88375 ? 175 ASP A OD2 1 
ATOM   1375 N N   . HIS A 1 182 ? 14.55928  -0.01570  46.07331 1.000 31.10615 ? 176 HIS A N   1 
ATOM   1376 C CA  . HIS A 1 182 ? 15.06201  1.25521   45.56800 1.000 31.86946 ? 176 HIS A CA  1 
ATOM   1377 C C   . HIS A 1 182 ? 14.36999  2.44995   46.23906 1.000 29.84144 ? 176 HIS A C   1 
ATOM   1378 O O   . HIS A 1 182 ? 14.23717  3.51823   45.64163 1.000 31.51682 ? 176 HIS A O   1 
ATOM   1379 C CB  A HIS A 1 182 ? 14.93102  1.30312   44.04745 0.500 33.22372 ? 176 HIS A CB  1 
ATOM   1380 C CB  B HIS A 1 182 ? 14.89730  1.32027   44.05441 0.500 33.95512 ? 176 HIS A CB  1 
ATOM   1381 C CG  A HIS A 1 182 ? 15.54528  0.11802   43.36559 0.500 34.40677 ? 176 HIS A CG  1 
ATOM   1382 C CG  B HIS A 1 182 ? 15.69975  0.29601   43.32203 0.500 35.79134 ? 176 HIS A CG  1 
ATOM   1383 N ND1 A HIS A 1 182 ? 14.94331  -1.12578  43.34338 0.500 34.06345 ? 176 HIS A ND1 1 
ATOM   1384 N ND1 B HIS A 1 182 ? 15.24635  -0.33329  42.18009 0.500 36.48225 ? 176 HIS A ND1 1 
ATOM   1385 C CD2 A HIS A 1 182 ? 16.74648  -0.03296  42.74773 0.500 35.35564 ? 176 HIS A CD2 1 
ATOM   1386 C CD2 B HIS A 1 182 ? 16.96753  -0.14694  43.52230 0.500 36.12029 ? 176 HIS A CD2 1 
ATOM   1387 C CE1 A HIS A 1 182 ? 15.72714  -1.97840  42.70715 0.500 34.77522 ? 176 HIS A CE1 1 
ATOM   1388 C CE1 B HIS A 1 182 ? 16.18151  -1.15846  41.73928 0.500 36.95430 ? 176 HIS A CE1 1 
ATOM   1389 N NE2 A HIS A 1 182 ? 16.83227  -1.34555  42.34570 0.500 36.14415 ? 176 HIS A NE2 1 
ATOM   1390 N NE2 B HIS A 1 182 ? 17.24077  -1.05723  42.53081 0.500 36.65685 ? 176 HIS A NE2 1 
ATOM   1391 N N   . ASP A 1 183 ? 14.00801  2.30943   47.51618 1.000 25.75777 ? 177 ASP A N   1 
ATOM   1392 C CA  . ASP A 1 183 ? 13.27409  3.34350   48.24089 1.000 24.42733 ? 177 ASP A CA  1 
ATOM   1393 C C   . ASP A 1 183 ? 14.15351  4.41329   48.88137 1.000 23.36207 ? 177 ASP A C   1 
ATOM   1394 O O   . ASP A 1 183 ? 13.65255  5.47680   49.23262 1.000 21.91585 ? 177 ASP A O   1 
ATOM   1395 C CB  . ASP A 1 183 ? 12.40435  2.68918   49.32920 1.000 25.47148 ? 177 ASP A CB  1 
ATOM   1396 C CG  . ASP A 1 183 ? 11.50458  3.67551   50.01691 1.000 25.76481 ? 177 ASP A CG  1 
ATOM   1397 O OD1 . ASP A 1 183 ? 10.57615  4.11512   49.35915 1.000 25.69424 ? 177 ASP A OD1 1 
ATOM   1398 O OD2 . ASP A 1 183 ? 11.71524  4.02121   51.21662 1.000 26.84766 ? 177 ASP A OD2 1 
ATOM   1399 N N   . HIS A 1 184 ? 15.46489  4.19154   48.99459 1.000 23.10739 ? 178 HIS A N   1 
ATOM   1400 C CA  . HIS A 1 184 ? 16.28564  5.09033   49.81312 1.000 23.24441 ? 178 HIS A CA  1 
ATOM   1401 C C   . HIS A 1 184 ? 16.72039  6.31661   49.01169 1.000 22.94680 ? 178 HIS A C   1 
ATOM   1402 O O   . HIS A 1 184 ? 17.03199  6.22777   47.81321 1.000 24.02680 ? 178 HIS A O   1 
ATOM   1403 C CB  . HIS A 1 184 ? 17.57744  4.42325   50.34018 0.900 26.05406 ? 178 HIS A CB  1 
ATOM   1404 C CG  . HIS A 1 184 ? 17.37570  3.42084   51.44463 0.700 30.08300 ? 178 HIS A CG  1 
ATOM   1405 N ND1 . HIS A 1 184 ? 17.42397  2.06026   51.22160 0.700 31.63309 ? 178 HIS A ND1 1 
ATOM   1406 C CD2 . HIS A 1 184 ? 17.10563  3.57417   52.76843 0.700 32.66276 ? 178 HIS A CD2 1 
ATOM   1407 C CE1 . HIS A 1 184 ? 17.22943  1.41773   52.36322 0.700 33.23190 ? 178 HIS A CE1 1 
ATOM   1408 N NE2 . HIS A 1 184 ? 17.00858  2.31081   53.31302 0.700 33.62694 ? 178 HIS A NE2 1 
ATOM   1409 N N   . THR A 1 185 ? 16.79720  7.45432   49.69544 1.000 21.25112 ? 179 THR A N   1 
ATOM   1410 C CA  . THR A 1 185 ? 17.21699  8.71046   49.09987 1.000 22.51799 ? 179 THR A CA  1 
ATOM   1411 C C   . THR A 1 185 ? 17.73774  9.60867   50.22521 1.000 22.48268 ? 179 THR A C   1 
ATOM   1412 O O   . THR A 1 185 ? 17.75564  9.22805   51.40843 1.000 21.88140 ? 179 THR A O   1 
ATOM   1413 C CB  . THR A 1 185 ? 16.06785  9.37519   48.31185 1.000 23.37830 ? 179 THR A CB  1 
ATOM   1414 O OG1 . THR A 1 185 ? 16.56049  10.50771  47.56646 1.000 25.18299 ? 179 THR A OG1 1 
ATOM   1415 C CG2 . THR A 1 185 ? 14.94557  9.88603   49.25117 1.000 22.25592 ? 179 THR A CG2 1 
ATOM   1416 N N   . GLY A 1 186 ? 18.18134  10.79983  49.83234 1.000 23.27267 ? 180 GLY A N   1 
ATOM   1417 C CA  . GLY A 1 186 ? 18.72565  11.78625  50.74147 1.000 23.69719 ? 180 GLY A CA  1 
ATOM   1418 C C   . GLY A 1 186 ? 17.68619  12.60861  51.48105 1.000 22.90707 ? 180 GLY A C   1 
ATOM   1419 O O   . GLY A 1 186 ? 16.47055  12.50401  51.29178 1.000 22.89214 ? 180 GLY A O   1 
ATOM   1420 N N   . PHE A 1 187 ? 18.19898  13.41049  52.39103 1.000 22.69570 ? 181 PHE A N   1 
ATOM   1421 C CA  . PHE A 1 187 ? 17.39292  14.23403  53.28908 1.000 22.02413 ? 181 PHE A CA  1 
ATOM   1422 C C   . PHE A 1 187 ? 16.78371  15.42267  52.52983 1.000 23.54723 ? 181 PHE A C   1 
ATOM   1423 O O   . PHE A 1 187 ? 17.45891  16.06619  51.69221 1.000 25.91469 ? 181 PHE A O   1 
ATOM   1424 C CB  . PHE A 1 187 ? 18.35633  14.69776  54.40570 1.000 19.83156 ? 181 PHE A CB  1 
ATOM   1425 C CG  . PHE A 1 187 ? 17.77941  15.62597  55.45164 1.000 20.88572 ? 181 PHE A CG  1 
ATOM   1426 C CD1 . PHE A 1 187 ? 16.62803  15.31200  56.15914 1.000 20.39424 ? 181 PHE A CD1 1 
ATOM   1427 C CD2 . PHE A 1 187 ? 18.47795  16.78831  55.79247 1.000 20.97942 ? 181 PHE A CD2 1 
ATOM   1428 C CE1 . PHE A 1 187 ? 16.15886  16.17757  57.16721 1.000 20.38681 ? 181 PHE A CE1 1 
ATOM   1429 C CE2 . PHE A 1 187 ? 18.02575  17.64910  56.80625 1.000 21.34043 ? 181 PHE A CE2 1 
ATOM   1430 C CZ  . PHE A 1 187 ? 16.86361  17.34158  57.48490 1.000 20.88368 ? 181 PHE A CZ  1 
ATOM   1431 N N   . LEU A 1 188 ? 15.50382  15.70812  52.80730 1.000 24.85958 ? 182 LEU A N   1 
ATOM   1432 C CA  . LEU A 1 188 ? 14.79218  16.85996  52.23650 1.000 26.54623 ? 182 LEU A CA  1 
ATOM   1433 C C   . LEU A 1 188 ? 14.65353  16.77614  50.70906 1.000 26.86623 ? 182 LEU A C   1 
ATOM   1434 O O   . LEU A 1 188 ? 14.74959  17.79499  50.00962 1.000 28.49942 ? 182 LEU A O   1 
ATOM   1435 C CB  . LEU A 1 188 ? 15.44561  18.19235  52.65565 1.000 29.04976 ? 182 LEU A CB  1 
ATOM   1436 C CG  . LEU A 1 188 ? 15.54554  18.43481  54.18080 1.000 30.72881 ? 182 LEU A CG  1 
ATOM   1437 C CD1 . LEU A 1 188 ? 16.22010  19.79508  54.50487 1.000 31.39199 ? 182 LEU A CD1 1 
ATOM   1438 C CD2 . LEU A 1 188 ? 14.19150  18.27988  54.86711 1.000 30.57826 ? 182 LEU A CD2 1 
ATOM   1439 N N   A THR A 1 189 ? 14.46666  15.53207  50.22476 0.400 23.61351 ? 183 THR A N   1 
ATOM   1440 N N   B THR A 1 189 ? 14.33559  15.60508  50.17085 0.600 27.90489 ? 183 THR A N   1 
ATOM   1441 C CA  A THR A 1 189 ? 14.12898  15.22891  48.83131 0.400 21.77402 ? 183 THR A CA  1 
ATOM   1442 C CA  B THR A 1 189 ? 14.31215  15.43534  48.71297 0.600 29.84550 ? 183 THR A CA  1 
ATOM   1443 C C   A THR A 1 189 ? 12.69556  15.62849  48.55028 0.400 20.48171 ? 183 THR A C   1 
ATOM   1444 C C   B THR A 1 189 ? 12.90548  15.40931  48.13153 0.600 29.18005 ? 183 THR A C   1 
ATOM   1445 O O   A THR A 1 189 ? 11.77435  15.23516  49.26956 0.400 19.66295 ? 183 THR A O   1 
ATOM   1446 O O   B THR A 1 189 ? 12.65411  15.97536  47.06076 0.600 29.18221 ? 183 THR A O   1 
ATOM   1447 C CB  A THR A 1 189 ? 14.26678  13.72199  48.51544 0.400 20.48571 ? 183 THR A CB  1 
ATOM   1448 C CB  B THR A 1 189 ? 14.95880  14.10332  48.32436 0.600 32.22871 ? 183 THR A CB  1 
ATOM   1449 O OG1 A THR A 1 189 ? 15.61841  13.29580  48.69141 0.400 20.46133 ? 183 THR A OG1 1 
ATOM   1450 O OG1 B THR A 1 189 ? 16.27477  14.03669  48.83355 0.600 33.83439 ? 183 THR A OG1 1 
ATOM   1451 C CG2 A THR A 1 189 ? 13.87064  13.40924  47.08311 0.400 18.89717 ? 183 THR A CG2 1 
ATOM   1452 C CG2 B THR A 1 189 ? 15.01064  13.97968  46.84365 0.600 33.31753 ? 183 THR A CG2 1 
ATOM   1453 N N   A GLU A 1 190 ? 12.53347  16.36152  47.46003 0.400 20.49830 ? 184 GLU A N   1 
ATOM   1454 N N   B GLU A 1 190 ? 12.00693  14.69528  48.79908 0.600 28.17762 ? 184 GLU A N   1 
ATOM   1455 C CA  A GLU A 1 190 ? 11.26295  16.85775  46.96997 0.400 20.74060 ? 184 GLU A CA  1 
ATOM   1456 C CA  B GLU A 1 190 ? 10.85742  14.04296  48.19029 0.600 27.96480 ? 184 GLU A CA  1 
ATOM   1457 C C   A GLU A 1 190 ? 10.26837  15.71287  46.77967 0.400 20.15360 ? 184 GLU A C   1 
ATOM   1458 C C   B GLU A 1 190 ? 9.54670   14.70536  48.59657 0.600 28.62628 ? 184 GLU A C   1 
ATOM   1459 O O   A GLU A 1 190 ? 10.64076  14.60455  46.39361 0.400 20.98440 ? 184 GLU A O   1 
ATOM   1460 O O   B GLU A 1 190 ? 9.44328   15.24148  49.70014 0.600 28.64143 ? 184 GLU A O   1 
ATOM   1461 C CB  A GLU A 1 190 ? 11.55139  17.55151  45.64011 0.400 22.90813 ? 184 GLU A CB  1 
ATOM   1462 C CB  B GLU A 1 190 ? 10.86960  12.54843  48.56721 0.600 28.38486 ? 184 GLU A CB  1 
ATOM   1463 C CG  A GLU A 1 190 ? 12.59559  18.69798  45.76019 0.400 25.26659 ? 184 GLU A CG  1 
ATOM   1464 C CG  B GLU A 1 190 ? 12.08195  11.83231  48.10130 0.600 29.04663 ? 184 GLU A CG  1 
ATOM   1465 C CD  A GLU A 1 190 ? 14.11859  18.26709  45.73317 0.400 27.94065 ? 184 GLU A CD  1 
ATOM   1466 C CD  B GLU A 1 190 ? 11.93934  11.54389  46.59447 0.600 29.33994 ? 184 GLU A CD  1 
ATOM   1467 O OE1 A GLU A 1 190 ? 14.47539  17.06152  45.71510 0.400 28.36346 ? 184 GLU A OE1 1 
ATOM   1468 O OE1 B GLU A 1 190 ? 10.81799  11.65584  46.06914 0.600 27.76090 ? 184 GLU A OE1 1 
ATOM   1469 O OE2 A GLU A 1 190 ? 14.98292  19.18250  45.71032 0.400 30.02354 ? 184 GLU A OE2 1 
ATOM   1470 O OE2 B GLU A 1 190 ? 12.91838  11.16584  45.93605 0.600 31.49806 ? 184 GLU A OE2 1 
ATOM   1471 N N   A TYR A 1 191 ? 8.98458   15.98451  47.04390 0.400 19.19283 ? 185 TYR A N   1 
ATOM   1472 N N   B TYR A 1 191 ? 8.54098   14.66494  47.68767 0.400 28.90830 ? 185 TYR A N   1 
ATOM   1473 C CA  A TYR A 1 191 ? 7.95276   14.94492  47.00813 0.400 19.15323 ? 185 TYR A CA  1 
ATOM   1474 C CA  B TYR A 1 191 ? 7.27703   15.39601  47.84553 0.400 30.35472 ? 185 TYR A CA  1 
ATOM   1475 C C   A TYR A 1 191 ? 6.65593   15.51467  46.43299 0.400 20.64136 ? 185 TYR A C   1 
ATOM   1476 C C   B TYR A 1 191 ? 6.03562   14.49720  47.79168 0.400 28.75161 ? 185 TYR A C   1 
ATOM   1477 O O   A TYR A 1 191 ? 6.39464   16.71926  46.53078 0.400 21.95409 ? 185 TYR A O   1 
ATOM   1478 O O   B TYR A 1 191 ? 4.91497   15.02267  47.70393 0.400 29.08184 ? 185 TYR A O   1 
ATOM   1479 C CB  A TYR A 1 191 ? 7.68314   14.34307  48.40279 0.400 17.68607 ? 185 TYR A CB  1 
ATOM   1480 C CB  B TYR A 1 191 ? 7.07838   16.43879  46.72909 0.400 33.05370 ? 185 TYR A CB  1 
ATOM   1481 C CG  A TYR A 1 191 ? 7.00040   12.95806  48.34651 0.400 16.99117 ? 185 TYR A CG  1 
ATOM   1482 C CG  B TYR A 1 191 ? 6.61259   15.79827  45.41840 0.400 35.37288 ? 185 TYR A CG  1 
ATOM   1483 C CD1 A TYR A 1 191 ? 7.61834   11.88136  47.72507 0.400 16.53370 ? 185 TYR A CD1 1 
ATOM   1484 C CD1 B TYR A 1 191 ? 7.45880   15.01367  44.65020 0.400 36.40481 ? 185 TYR A CD1 1 
ATOM   1485 C CD2 A TYR A 1 191 ? 5.75420   12.73314  48.93901 0.400 16.37433 ? 185 TYR A CD2 1 
ATOM   1486 C CD2 B TYR A 1 191 ? 5.29143   15.96029  44.97451 0.400 36.34221 ? 185 TYR A CD2 1 
ATOM   1487 C CE1 A TYR A 1 191 ? 7.05582   10.63131  47.68617 0.400 17.15065 ? 185 TYR A CE1 1 
ATOM   1488 C CE1 B TYR A 1 191 ? 7.00411   14.40650  43.46695 0.400 36.63233 ? 185 TYR A CE1 1 
ATOM   1489 C CE2 A TYR A 1 191 ? 5.17072   11.45374  48.89419 0.400 17.70612 ? 185 TYR A CE2 1 
ATOM   1490 C CE2 B TYR A 1 191 ? 4.83151   15.36261  43.79431 0.400 36.40915 ? 185 TYR A CE2 1 
ATOM   1491 C CZ  A TYR A 1 191 ? 5.82759   10.40940  48.26123 0.400 16.94494 ? 185 TYR A CZ  1 
ATOM   1492 C CZ  B TYR A 1 191 ? 5.69445   14.59745  43.04300 0.400 36.86682 ? 185 TYR A CZ  1 
ATOM   1493 O OH  A TYR A 1 191 ? 5.24284   9.14682   48.20070 0.400 17.53421 ? 185 TYR A OH  1 
ATOM   1494 O OH  B TYR A 1 191 ? 5.24419   14.00075  41.87655 0.400 36.46463 ? 185 TYR A OH  1 
ATOM   1495 N N   A VAL A 1 192 ? 5.84708   14.63801  45.83633 0.400 20.49200 ? 186 VAL A N   1 
ATOM   1496 N N   B VAL A 1 192 ? 6.19797   13.17331  47.76797 0.600 26.47704 ? 186 VAL A N   1 
ATOM   1497 C CA  A VAL A 1 192 ? 4.64779   15.03923  45.07596 0.400 20.40191 ? 186 VAL A CA  1 
ATOM   1498 C CA  B VAL A 1 192 ? 5.12014   12.19468  47.58080 0.600 24.38365 ? 186 VAL A CA  1 
ATOM   1499 C C   A VAL A 1 192 ? 3.35234   15.04869  45.91113 0.400 19.10074 ? 186 VAL A C   1 
ATOM   1500 C C   B VAL A 1 192 ? 3.93267   12.56601  48.45757 0.600 23.92587 ? 186 VAL A C   1 
ATOM   1501 O O   A VAL A 1 192 ? 2.55407   15.97346  45.78686 0.400 19.87768 ? 186 VAL A O   1 
ATOM   1502 O O   B VAL A 1 192 ? 4.13089   13.12879  49.53789 0.600 24.44186 ? 186 VAL A O   1 
ATOM   1503 C CB  A VAL A 1 192 ? 4.46908   14.15502  43.82446 0.400 21.31541 ? 186 VAL A CB  1 
ATOM   1504 C CB  B VAL A 1 192 ? 5.64299   10.78791  47.92179 0.600 24.50820 ? 186 VAL A CB  1 
ATOM   1505 C CG1 A VAL A 1 192 ? 3.41367   14.80643  42.92312 0.400 21.44376 ? 186 VAL A CG1 1 
ATOM   1506 C CG1 B VAL A 1 192 ? 4.61817   9.67568   47.57129 0.600 24.41313 ? 186 VAL A CG1 1 
ATOM   1507 C CG2 A VAL A 1 192 ? 5.77124   13.95825  43.10298 0.400 24.24609 ? 186 VAL A CG2 1 
ATOM   1508 C CG2 B VAL A 1 192 ? 6.98875   10.56699  47.24393 0.600 25.22746 ? 186 VAL A CG2 1 
ATOM   1509 N N   A ALA A 1 193 ? 3.09482   14.02456  46.72208 0.400 18.98243 ? 187 ALA A N   1 
ATOM   1510 N N   B ALA A 1 193 ? 2.71123   12.25518  48.01570 0.600 22.82651 ? 187 ALA A N   1 
ATOM   1511 C CA  A ALA A 1 193 ? 1.75738   13.73558  47.26556 0.400 18.49703 ? 187 ALA A CA  1 
ATOM   1512 C CA  B ALA A 1 193 ? 1.47803   12.67316  48.69426 0.600 22.00211 ? 187 ALA A CA  1 
ATOM   1513 C C   A ALA A 1 193 ? 1.34457   14.72774  48.37618 0.400 20.04920 ? 187 ALA A C   1 
ATOM   1514 C C   B ALA A 1 193 ? 1.35482   14.19677  48.84836 0.600 21.85454 ? 187 ALA A C   1 
ATOM   1515 O O   A ALA A 1 193 ? 2.11519   15.60050  48.74594 0.400 20.78202 ? 187 ALA A O   1 
ATOM   1516 O O   B ALA A 1 193 ? 2.29248   14.98189  48.69882 0.600 22.11470 ? 187 ALA A O   1 
ATOM   1517 C CB  A ALA A 1 193 ? 1.71813   12.29827  47.76886 0.400 17.86835 ? 187 ALA A CB  1 
ATOM   1518 C CB  B ALA A 1 193 ? 1.30877   11.96857  50.08560 0.600 21.47269 ? 187 ALA A CB  1 
ATOM   1519 N N   . THR A 1 194 ? 0.11614   14.61106  48.97446 1.000 22.47100 ? 188 THR A N   1 
ATOM   1520 C CA  . THR A 1 194 ? -0.35417  15.80491  49.70595 1.000 20.41187 ? 188 THR A CA  1 
ATOM   1521 C C   . THR A 1 194 ? 0.23890   15.94895  51.11433 1.000 21.26441 ? 188 THR A C   1 
ATOM   1522 O O   . THR A 1 194 ? 0.25589   14.98531  51.89510 1.000 22.43860 ? 188 THR A O   1 
ATOM   1523 C CB  . THR A 1 194 ? -1.88513  15.74027  49.74778 1.000 17.76605 ? 188 THR A CB  1 
ATOM   1524 O OG1 . THR A 1 194 ? -2.33783  15.55755  48.39224 1.000 17.49741 ? 188 THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 194 ? -2.50576  17.01635  50.33460 1.000 18.16670 ? 188 THR A CG2 1 
ATOM   1526 N N   . ARG A 1 195 ? 0.67345   17.18222  51.43568 1.000 19.94692 ? 189 ARG A N   1 
ATOM   1527 C CA  . ARG A 1 195 ? 1.52829   17.42455  52.59819 1.000 19.96088 ? 189 ARG A CA  1 
ATOM   1528 C C   . ARG A 1 195 ? 1.00457   16.80427  53.89223 1.000 19.01143 ? 189 ARG A C   1 
ATOM   1529 O O   . ARG A 1 195 ? 1.75302   16.08685  54.58456 1.000 20.69907 ? 189 ARG A O   1 
ATOM   1530 C CB  A ARG A 1 195 ? 1.64525   18.93866  52.80613 0.500 19.82623 ? 189 ARG A CB  1 
ATOM   1531 C CB  B ARG A 1 195 ? 1.79184   18.92752  52.76476 0.500 21.91789 ? 189 ARG A CB  1 
ATOM   1532 C CG  A ARG A 1 195 ? 2.68989   19.36720  53.83292 0.500 19.98716 ? 189 ARG A CG  1 
ATOM   1533 C CG  B ARG A 1 195 ? 2.78418   19.21411  53.91223 0.500 23.26677 ? 189 ARG A CG  1 
ATOM   1534 C CD  A ARG A 1 195 ? 2.42240   20.84080  54.23163 0.500 20.04954 ? 189 ARG A CD  1 
ATOM   1535 C CD  B ARG A 1 195 ? 3.83928   20.28114  53.55233 0.500 25.27900 ? 189 ARG A CD  1 
ATOM   1536 N NE  A ARG A 1 195 ? 2.25948   21.70882  53.05355 0.500 21.51198 ? 189 ARG A NE  1 
ATOM   1537 N NE  B ARG A 1 195 ? 3.39798   21.54328  52.97156 0.500 27.65625 ? 189 ARG A NE  1 
ATOM   1538 C CZ  A ARG A 1 195 ? 1.38818   22.68937  52.90869 0.500 22.16031 ? 189 ARG A CZ  1 
ATOM   1539 C CZ  B ARG A 1 195 ? 3.36774   21.81719  51.67204 0.500 29.69930 ? 189 ARG A CZ  1 
ATOM   1540 N NH1 A ARG A 1 195 ? 0.62619   23.09544  53.89905 0.500 23.86738 ? 189 ARG A NH1 1 
ATOM   1541 N NH1 B ARG A 1 195 ? 3.52659   20.86833  50.75727 0.500 29.69424 ? 189 ARG A NH1 1 
ATOM   1542 N NH2 A ARG A 1 195 ? 1.23753   23.24071  51.71386 0.500 23.40940 ? 189 ARG A NH2 1 
ATOM   1543 N NH2 B ARG A 1 195 ? 3.14421   23.06791  51.27621 0.500 30.17523 ? 189 ARG A NH2 1 
ATOM   1544 N N   . TRP A 1 196 ? -0.25283  17.10398  54.27272 1.000 19.62876 ? 190 TRP A N   1 
ATOM   1545 C CA  . TRP A 1 196 ? -0.77698  16.70538  55.58343 1.000 18.90235 ? 190 TRP A CA  1 
ATOM   1546 C C   . TRP A 1 196 ? -0.77824  15.19041  55.79050 1.000 17.09661 ? 190 TRP A C   1 
ATOM   1547 O O   . TRP A 1 196 ? -0.83125  14.73958  56.94069 1.000 15.76815 ? 190 TRP A O   1 
ATOM   1548 C CB  . TRP A 1 196 ? -2.19938  17.26026  55.75601 1.000 20.00166 ? 190 TRP A CB  1 
ATOM   1549 C CG  . TRP A 1 196 ? -2.21949  18.77528  55.86413 1.000 21.83219 ? 190 TRP A CG  1 
ATOM   1550 C CD1 . TRP A 1 196 ? -1.14600  19.62500  55.96736 1.000 23.76811 ? 190 TRP A CD1 1 
ATOM   1551 C CD2 . TRP A 1 196 ? -3.38176  19.59106  55.83065 1.000 24.29193 ? 190 TRP A CD2 1 
ATOM   1552 N NE1 . TRP A 1 196 ? -1.58971  20.92928  56.02143 1.000 25.18861 ? 190 TRP A NE1 1 
ATOM   1553 C CE2 . TRP A 1 196 ? -2.96727  20.92826  55.92901 1.000 25.42905 ? 190 TRP A CE2 1 
ATOM   1554 C CE3 . TRP A 1 196 ? -4.73989  19.31493  55.67708 1.000 26.01900 ? 190 TRP A CE3 1 
ATOM   1555 C CZ2 . TRP A 1 196 ? -3.87887  21.99958  55.90572 1.000 26.70067 ? 190 TRP A CZ2 1 
ATOM   1556 C CZ3 . TRP A 1 196 ? -5.63591  20.35324  55.67159 1.000 27.36844 ? 190 TRP A CZ3 1 
ATOM   1557 C CH2 . TRP A 1 196 ? -5.20661  21.67938  55.77773 1.000 27.53563 ? 190 TRP A CH2 1 
ATOM   1558 N N   . TYR A 1 197 ? -0.73362  14.40374  54.72153 1.000 16.30541 ? 191 TYR A N   1 
ATOM   1559 C CA  . TYR A 1 197 ? -0.88214  12.94638  54.74436 1.000 15.36348 ? 191 TYR A CA  1 
ATOM   1560 C C   . TYR A 1 197 ? 0.44451   12.23058  54.43394 1.000 15.82046 ? 191 TYR A C   1 
ATOM   1561 O O   . TYR A 1 197 ? 0.45069   11.01350  54.27481 1.000 15.43328 ? 191 TYR A O   1 
ATOM   1562 C CB  . TYR A 1 197 ? -2.00924  12.54248  53.76619 1.000 14.58873 ? 191 TYR A CB  1 
ATOM   1563 C CG  . TYR A 1 197 ? -3.29420  13.32598  54.11917 1.000 16.72987 ? 191 TYR A CG  1 
ATOM   1564 C CD1 . TYR A 1 197 ? -4.12340  12.89904  55.17892 1.000 17.54278 ? 191 TYR A CD1 1 
ATOM   1565 C CD2 . TYR A 1 197 ? -3.62304  14.52948  53.46303 1.000 16.79937 ? 191 TYR A CD2 1 
ATOM   1566 C CE1 . TYR A 1 197 ? -5.22344  13.68067  55.60810 1.000 15.80638 ? 191 TYR A CE1 1 
ATOM   1567 C CE2 . TYR A 1 197 ? -4.64547  15.33453  53.90126 1.000 17.78966 ? 191 TYR A CE2 1 
ATOM   1568 C CZ  . TYR A 1 197 ? -5.49763  14.88686  54.94488 1.000 16.80875 ? 191 TYR A CZ  1 
ATOM   1569 O OH  . TYR A 1 197 ? -6.54665  15.69401  55.35063 1.000 18.17373 ? 191 TYR A OH  1 
ATOM   1570 N N   . ARG A 1 198 ? 1.57506   12.97618  54.40487 1.000 16.54901 ? 192 ARG A N   1 
ATOM   1571 C CA  . ARG A 1 198 ? 2.91987   12.44024  54.11977 1.000 17.44768 ? 192 ARG A CA  1 
ATOM   1572 C C   . ARG A 1 198 ? 3.59243   11.83730  55.35353 1.000 15.87516 ? 192 ARG A C   1 
ATOM   1573 O O   . ARG A 1 198 ? 3.71476   12.51160  56.37832 1.000 16.58528 ? 192 ARG A O   1 
ATOM   1574 C CB  . ARG A 1 198 ? 3.87996   13.55859  53.69497 1.000 19.96478 ? 192 ARG A CB  1 
ATOM   1575 C CG  . ARG A 1 198 ? 3.95406   13.91463  52.36891 0.900 20.19835 ? 192 ARG A CG  1 
ATOM   1576 C CD  . ARG A 1 198 ? 4.92150   15.07876  52.09617 0.900 18.85984 ? 192 ARG A CD  1 
ATOM   1577 N NE  . ARG A 1 198 ? 4.45173   15.70258  50.87478 0.900 17.15204 ? 192 ARG A NE  1 
ATOM   1578 C CZ  . ARG A 1 198 ? 4.71773   16.94676  50.52740 0.600 19.00650 ? 192 ARG A CZ  1 
ATOM   1579 N NH1 . ARG A 1 198 ? 5.57516   17.68326  51.21142 0.600 19.83971 ? 192 ARG A NH1 1 
ATOM   1580 N NH2 . ARG A 1 198 ? 4.19381   17.43132  49.40479 0.600 20.27601 ? 192 ARG A NH2 1 
ATOM   1581 N N   . ALA A 1 199 ? 4.10542   10.62514  55.20722 1.000 14.22478 ? 193 ALA A N   1 
ATOM   1582 C CA  . ALA A 1 199 ? 4.80637   9.93145   56.28288 1.000 14.43310 ? 193 ALA A CA  1 
ATOM   1583 C C   . ALA A 1 199 ? 6.13163   10.63757  56.60853 1.000 14.70992 ? 193 ALA A C   1 
ATOM   1584 O O   . ALA A 1 199 ? 6.78248   11.23439  55.73496 1.000 16.50010 ? 193 ALA A O   1 
ATOM   1585 C CB  . ALA A 1 199 ? 5.06720   8.47900   55.87914 1.000 15.78519 ? 193 ALA A CB  1 
ATOM   1586 N N   . PRO A 1 200 ? 6.58601   10.53736  57.85222 1.000 14.44654 ? 194 PRO A N   1 
ATOM   1587 C CA  . PRO A 1 200 ? 7.80817   11.26905  58.22286 1.000 14.15887 ? 194 PRO A CA  1 
ATOM   1588 C C   . PRO A 1 200 ? 9.01822   10.87874  57.37479 1.000 15.19014 ? 194 PRO A C   1 
ATOM   1589 O O   . PRO A 1 200 ? 9.86733   11.73700  57.07493 1.000 15.18515 ? 194 PRO A O   1 
ATOM   1590 C CB  . PRO A 1 200 ? 8.01569   10.86796  59.69885 1.000 16.35548 ? 194 PRO A CB  1 
ATOM   1591 C CG  . PRO A 1 200 ? 7.19691   9.62178   59.93297 1.000 16.16732 ? 194 PRO A CG  1 
ATOM   1592 C CD  . PRO A 1 200 ? 6.01389   9.75280   58.97368 1.000 14.38620 ? 194 PRO A CD  1 
ATOM   1593 N N   . GLU A 1 201 ? 9.11960   9.59525   56.98299 1.000 15.45228 ? 195 GLU A N   1 
ATOM   1594 C CA  . GLU A 1 201 ? 10.30564  9.20583   56.24048 1.000 16.97117 ? 195 GLU A CA  1 
ATOM   1595 C C   . GLU A 1 201 ? 10.41477  9.88763   54.86637 1.000 18.04619 ? 195 GLU A C   1 
ATOM   1596 O O   . GLU A 1 201 ? 11.52339  9.96259   54.32178 1.000 17.57191 ? 195 GLU A O   1 
ATOM   1597 C CB  . GLU A 1 201 ? 10.35589  7.68456   56.10485 1.000 15.61916 ? 195 GLU A CB  1 
ATOM   1598 C CG  . GLU A 1 201 ? 9.18535   7.09301   55.33747 1.000 15.50223 ? 195 GLU A CG  1 
ATOM   1599 C CD  . GLU A 1 201 ? 7.99451   6.69719   56.22156 1.000 16.53574 ? 195 GLU A CD  1 
ATOM   1600 O OE1 . GLU A 1 201 ? 7.88746   7.17153   57.38643 1.000 16.88983 ? 195 GLU A OE1 1 
ATOM   1601 O OE2 . GLU A 1 201 ? 7.13581   5.92466   55.71465 1.000 16.78326 ? 195 GLU A OE2 1 
ATOM   1602 N N   . ILE A 1 202 ? 9.31062   10.42425  54.31613 1.000 16.78724 ? 196 ILE A N   1 
ATOM   1603 C CA  . ILE A 1 202 ? 9.41060   11.11651  53.02121 1.000 16.68113 ? 196 ILE A CA  1 
ATOM   1604 C C   . ILE A 1 202 ? 10.40170  12.28959  53.11684 1.000 17.96352 ? 196 ILE A C   1 
ATOM   1605 O O   . ILE A 1 202 ? 11.12803  12.59692  52.16643 1.000 19.41059 ? 196 ILE A O   1 
ATOM   1606 C CB  . ILE A 1 202 ? 8.01116   11.58377  52.58331 1.000 17.28786 ? 196 ILE A CB  1 
ATOM   1607 C CG1 . ILE A 1 202 ? 7.14990   10.38034  52.18738 1.000 16.86238 ? 196 ILE A CG1 1 
ATOM   1608 C CG2 . ILE A 1 202 ? 8.07741   12.58264  51.42278 1.000 19.31688 ? 196 ILE A CG2 1 
ATOM   1609 C CD1 . ILE A 1 202 ? 7.69158   9.61377   51.01607 1.000 18.66943 ? 196 ILE A CD1 1 
ATOM   1610 N N   . MET A 1 203 ? 10.41409  12.97824  54.25583 1.000 18.70239 ? 197 MET A N   1 
ATOM   1611 C CA  . MET A 1 203 ? 11.24951  14.14383  54.48679 1.000 19.22985 ? 197 MET A CA  1 
ATOM   1612 C C   . MET A 1 203 ? 12.66279  13.72015  54.92726 1.000 19.68219 ? 197 MET A C   1 
ATOM   1613 O O   . MET A 1 203 ? 13.55398  14.57549  54.99232 1.000 21.01947 ? 197 MET A O   1 
ATOM   1614 C CB  . MET A 1 203 ? 10.57998  14.97647  55.58688 1.000 19.92140 ? 197 MET A CB  1 
ATOM   1615 C CG  . MET A 1 203 ? 9.37695   15.90887  55.13473 1.000 19.43578 ? 197 MET A CG  1 
ATOM   1616 S SD  . MET A 1 203 ? 7.86914   14.83243  54.92480 1.000 21.51006 ? 197 MET A SD  1 
ATOM   1617 C CE  . MET A 1 203 ? 7.26094   14.81501  56.61249 1.000 21.95383 ? 197 MET A CE  1 
ATOM   1618 N N   . LEU A 1 204 ? 12.86245  12.44454  55.26860 1.000 18.03709 ? 198 LEU A N   1 
ATOM   1619 C CA  . LEU A 1 204 ? 14.14221  11.97440  55.81153 1.000 17.28108 ? 198 LEU A CA  1 
ATOM   1620 C C   . LEU A 1 204 ? 14.95408  11.16848  54.80540 1.000 18.08347 ? 198 LEU A C   1 
ATOM   1621 O O   . LEU A 1 204 ? 16.16331  11.47564  54.58493 1.000 19.69840 ? 198 LEU A O   1 
ATOM   1622 C CB  . LEU A 1 204 ? 13.88582  11.15996  57.08564 1.000 18.41914 ? 198 LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 204 ? 13.26697  11.98834  58.21212 1.000 18.73157 ? 198 LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 204 ? 12.69555  11.03532  59.27308 1.000 18.15575 ? 198 LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 204 ? 14.29713  12.89831  58.85375 1.000 19.46699 ? 198 LEU A CD2 1 
ATOM   1626 N N   . ASN A 1 205 ? 14.37260  10.07604  54.27360 1.000 18.05805 ? 199 ASN A N   1 
ATOM   1627 C CA  . ASN A 1 205 ? 15.19060  9.14145   53.47843 1.000 19.23698 ? 199 ASN A CA  1 
ATOM   1628 C C   . ASN A 1 205 ? 14.40422  8.23559   52.53943 1.000 18.98900 ? 199 ASN A C   1 
ATOM   1629 O O   . ASN A 1 205 ? 14.95488  7.21279   52.12256 1.000 19.05390 ? 199 ASN A O   1 
ATOM   1630 C CB  . ASN A 1 205 ? 16.02280  8.27805   54.43348 1.000 19.65796 ? 199 ASN A CB  1 
ATOM   1631 C CG  . ASN A 1 205 ? 15.17195  7.34524   55.27610 0.800 19.36363 ? 199 ASN A CG  1 
ATOM   1632 O OD1 . ASN A 1 205 ? 13.95571  7.47127   55.31842 0.800 20.77662 ? 199 ASN A OD1 1 
ATOM   1633 N ND2 . ASN A 1 205 ? 15.83284  6.43332   56.01264 0.800 19.67094 ? 199 ASN A ND2 1 
ATOM   1634 N N   . SER A 1 206 ? 13.15862  8.57350   52.14729 1.000 18.20422 ? 200 SER A N   1 
ATOM   1635 C CA  . SER A 1 206 ? 12.30325  7.65524   51.41250 1.000 19.29024 ? 200 SER A CA  1 
ATOM   1636 C C   . SER A 1 206 ? 11.72869  8.34121   50.18048 1.000 20.27386 ? 200 SER A C   1 
ATOM   1637 O O   . SER A 1 206 ? 11.23659  9.48291   50.27763 1.000 20.04956 ? 200 SER A O   1 
ATOM   1638 C CB  . SER A 1 206 ? 11.13392  7.18173   52.30139 1.000 18.97547 ? 200 SER A CB  1 
ATOM   1639 O OG  . SER A 1 206 ? 10.26907  6.32963   51.57741 1.000 19.16309 ? 200 SER A OG  1 
ATOM   1640 N N   . LYS A 1 207 ? 11.71027  7.60016   49.04551 1.000 19.90117 ? 201 LYS A N   1 
ATOM   1641 C CA  . LYS A 1 207 ? 11.03351  8.00947   47.82068 1.000 20.71507 ? 201 LYS A CA  1 
ATOM   1642 C C   . LYS A 1 207 ? 9.55246   7.64076   47.79895 1.000 21.31828 ? 201 LYS A C   1 
ATOM   1643 O O   . LYS A 1 207 ? 8.87487   7.91359   46.79373 1.000 22.57089 ? 201 LYS A O   1 
ATOM   1644 C CB  . LYS A 1 207 ? 11.72246  7.35127   46.61848 1.000 21.18566 ? 201 LYS A CB  1 
ATOM   1645 C CG  . LYS A 1 207 ? 13.13624  7.96981   46.40512 1.000 24.53114 ? 201 LYS A CG  1 
ATOM   1646 C CD  . LYS A 1 207 ? 13.74229  7.73796   45.08852 1.000 28.82373 ? 201 LYS A CD  1 
ATOM   1647 C CE  . LYS A 1 207 ? 13.80505  6.32579   44.69618 0.600 30.73831 ? 201 LYS A CE  1 
ATOM   1648 N NZ  . LYS A 1 207 ? 13.56388  6.29691   43.21644 0.400 32.06650 ? 201 LYS A NZ  1 
ATOM   1649 N N   . GLY A 1 208 ? 9.02258   7.03167   48.85659 1.000 19.69650 ? 202 GLY A N   1 
ATOM   1650 C CA  . GLY A 1 208 ? 7.60886   6.68568   48.81866 1.000 21.12140 ? 202 GLY A CA  1 
ATOM   1651 C C   . GLY A 1 208 ? 7.29132   5.50704   47.94494 1.000 19.61839 ? 202 GLY A C   1 
ATOM   1652 O O   . GLY A 1 208 ? 6.20908   5.45609   47.34688 1.000 20.67258 ? 202 GLY A O   1 
ATOM   1653 N N   . TYR A 1 209 ? 8.19348   4.53621   47.87484 1.000 18.09449 ? 203 TYR A N   1 
ATOM   1654 C CA  . TYR A 1 209 ? 8.05146   3.35133   47.02918 1.000 17.71359 ? 203 TYR A CA  1 
ATOM   1655 C C   . TYR A 1 209 ? 7.73142   2.08938   47.81799 1.000 18.98239 ? 203 TYR A C   1 
ATOM   1656 O O   . TYR A 1 209 ? 7.85014   0.97537   47.26582 1.000 19.61151 ? 203 TYR A O   1 
ATOM   1657 C CB  . TYR A 1 209 ? 9.36196   3.11760   46.23354 0.800 18.14078 ? 203 TYR A CB  1 
ATOM   1658 C CG  . TYR A 1 209 ? 9.69310   4.09887   45.13241 0.700 20.29584 ? 203 TYR A CG  1 
ATOM   1659 C CD1 . TYR A 1 209 ? 8.90116   5.16647   44.83341 0.700 21.72027 ? 203 TYR A CD1 1 
ATOM   1660 C CD2 . TYR A 1 209 ? 10.84900  3.93527   44.39998 0.700 22.12682 ? 203 TYR A CD2 1 
ATOM   1661 C CE1 . TYR A 1 209 ? 9.20702   6.03454   43.79370 0.700 23.31534 ? 203 TYR A CE1 1 
ATOM   1662 C CE2 . TYR A 1 209 ? 11.15715  4.78646   43.33612 0.700 25.10746 ? 203 TYR A CE2 1 
ATOM   1663 C CZ  . TYR A 1 209 ? 10.33284  5.86745   43.07716 0.700 25.79432 ? 203 TYR A CZ  1 
ATOM   1664 O OH  . TYR A 1 209 ? 10.60949  6.74292   42.04514 0.700 28.44886 ? 203 TYR A OH  1 
ATOM   1665 N N   . THR A 1 210 ? 7.30633   2.21645   49.09259 1.000 18.78139 ? 204 THR A N   1 
ATOM   1666 C CA  . THR A 1 210 ? 6.86343   1.04102   49.84483 1.000 20.72332 ? 204 THR A CA  1 
ATOM   1667 C C   . THR A 1 210 ? 5.43180   1.22798   50.38304 1.000 19.31702 ? 204 THR A C   1 
ATOM   1668 O O   . THR A 1 210 ? 4.92342   2.33751   50.56471 1.000 18.93483 ? 204 THR A O   1 
ATOM   1669 C CB  . THR A 1 210 ? 7.81371   0.69731   51.01822 1.000 24.15253 ? 204 THR A CB  1 
ATOM   1670 O OG1 . THR A 1 210 ? 7.52049   1.55682   52.10185 1.000 26.39375 ? 204 THR A OG1 1 
ATOM   1671 C CG2 . THR A 1 210 ? 9.33214   0.85097   50.61174 1.000 24.49465 ? 204 THR A CG2 1 
ATOM   1672 N N   . LYS A 1 211 ? 4.80476   0.09685   50.65655 1.000 16.35786 ? 205 LYS A N   1 
ATOM   1673 C CA  . LYS A 1 211 ? 3.38366   0.08230   51.05165 1.000 15.57744 ? 205 LYS A CA  1 
ATOM   1674 C C   . LYS A 1 211 ? 3.13652   0.86382   52.34476 1.000 14.56502 ? 205 LYS A C   1 
ATOM   1675 O O   . LYS A 1 211 ? 2.04876   1.43907   52.54344 1.000 14.60946 ? 205 LYS A O   1 
ATOM   1676 C CB  . LYS A 1 211 ? 2.93472   -1.36641  51.17154 1.000 16.59288 ? 205 LYS A CB  1 
ATOM   1677 C CG  . LYS A 1 211 ? 2.90507   -2.06831  49.79759 1.000 16.68182 ? 205 LYS A CG  1 
ATOM   1678 C CD  . LYS A 1 211 ? 2.63201   -3.56225  49.97721 1.000 17.38016 ? 205 LYS A CD  1 
ATOM   1679 C CE  . LYS A 1 211 ? 2.61403   -4.29430  48.63117 1.000 18.70483 ? 205 LYS A CE  1 
ATOM   1680 N NZ  . LYS A 1 211 ? 2.39937   -5.77294  48.70296 1.000 18.88290 ? 205 LYS A NZ  1 
ATOM   1681 N N   . SER A 1 212 ? 4.15671   0.95013   53.22150 1.000 15.44740 ? 206 SER A N   1 
ATOM   1682 C CA  . SER A 1 212 ? 3.97995   1.68452   54.46359 1.000 15.03233 ? 206 SER A CA  1 
ATOM   1683 C C   . SER A 1 212 ? 3.63823   3.14856   54.24861 1.000 15.30056 ? 206 SER A C   1 
ATOM   1684 O O   . SER A 1 212 ? 3.10485   3.77764   55.16903 1.000 15.51748 ? 206 SER A O   1 
ATOM   1685 C CB  . SER A 1 212 ? 5.26850   1.53083   55.32808 1.000 17.18589 ? 206 SER A CB  1 
ATOM   1686 O OG  . SER A 1 212 ? 6.42336   1.94273   54.60869 1.000 18.20443 ? 206 SER A OG  1 
ATOM   1687 N N   . ILE A 1 213 ? 3.91832   3.72300   53.07031 1.000 16.33049 ? 207 ILE A N   1 
ATOM   1688 C CA  . ILE A 1 213 ? 3.54496   5.11281   52.82718 1.000 15.92580 ? 207 ILE A CA  1 
ATOM   1689 C C   . ILE A 1 213 ? 2.01526   5.27406   52.84891 1.000 14.54633 ? 207 ILE A C   1 
ATOM   1690 O O   . ILE A 1 213 ? 1.48258   6.27748   53.33730 1.000 15.86374 ? 207 ILE A O   1 
ATOM   1691 C CB  . ILE A 1 213 ? 4.15927   5.56705   51.47889 1.000 19.18717 ? 207 ILE A CB  1 
ATOM   1692 C CG1 . ILE A 1 213 ? 4.29051   7.03803   51.48168 1.000 24.16412 ? 207 ILE A CG1 1 
ATOM   1693 C CG2 . ILE A 1 213 ? 3.41173   5.11698   50.24769 1.000 20.41085 ? 207 ILE A CG2 1 
ATOM   1694 C CD1 . ILE A 1 213 ? 5.60194   7.26839   52.20895 1.000 25.21495 ? 207 ILE A CD1 1 
ATOM   1695 N N   . ASP A 1 214 ? 1.31634   4.27987   52.35177 1.000 13.01157 ? 208 ASP A N   1 
ATOM   1696 C CA  . ASP A 1 214 ? -0.14796  4.39584   52.27705 1.000 11.65602 ? 208 ASP A CA  1 
ATOM   1697 C C   . ASP A 1 214 ? -0.75533  4.18558   53.65664 1.000 12.61435 ? 208 ASP A C   1 
ATOM   1698 O O   . ASP A 1 214 ? -1.77756  4.79753   53.98195 1.000 13.30363 ? 208 ASP A O   1 
ATOM   1699 C CB  . ASP A 1 214 ? -0.70648  3.33951   51.31780 1.000 11.01606 ? 208 ASP A CB  1 
ATOM   1700 C CG  . ASP A 1 214 ? -0.63232  3.73135   49.84155 1.000 12.89630 ? 208 ASP A CG  1 
ATOM   1701 O OD1 . ASP A 1 214 ? -0.58347  4.92830   49.47925 1.000 13.47694 ? 208 ASP A OD1 1 
ATOM   1702 O OD2 . ASP A 1 214 ? -0.60751  2.77597   49.03483 1.000 13.38616 ? 208 ASP A OD2 1 
ATOM   1703 N N   . ILE A 1 215 ? -0.16558  3.27836   54.45679 1.000 11.84915 ? 209 ILE A N   1 
ATOM   1704 C CA  . ILE A 1 215 ? -0.71286  3.03639   55.79214 1.000 11.38690 ? 209 ILE A CA  1 
ATOM   1705 C C   . ILE A 1 215 ? -0.61946  4.30778   56.63493 1.000 12.37685 ? 209 ILE A C   1 
ATOM   1706 O O   . ILE A 1 215 ? -1.53477  4.61627   57.40227 1.000 12.69087 ? 209 ILE A O   1 
ATOM   1707 C CB  . ILE A 1 215 ? -0.01778  1.84082   56.47599 1.000 11.89694 ? 209 ILE A CB  1 
ATOM   1708 C CG1 . ILE A 1 215 ? -0.34275  0.53384   55.75819 1.000 11.54893 ? 209 ILE A CG1 1 
ATOM   1709 C CG2 . ILE A 1 215 ? -0.43143  1.76784   57.97697 1.000 11.69678 ? 209 ILE A CG2 1 
ATOM   1710 C CD1 . ILE A 1 215 ? -1.80879  0.10076   55.84135 1.000 13.27986 ? 209 ILE A CD1 1 
ATOM   1711 N N   . TRP A 1 216 ? 0.49168   5.07660   56.52288 1.000 11.94294 ? 210 TRP A N   1 
ATOM   1712 C CA  . TRP A 1 216 ? 0.56064   6.34911   57.25134 1.000 12.88382 ? 210 TRP A CA  1 
ATOM   1713 C C   . TRP A 1 216 ? -0.61520  7.25636   56.87794 1.000 13.48110 ? 210 TRP A C   1 
ATOM   1714 O O   . TRP A 1 216 ? -1.26509  7.86131   57.75188 1.000 13.24827 ? 210 TRP A O   1 
ATOM   1715 C CB  . TRP A 1 216 ? 1.91432   7.06189   56.98706 1.000 12.43030 ? 210 TRP A CB  1 
ATOM   1716 C CG  . TRP A 1 216 ? 2.02738   8.38504   57.74422 1.000 12.31844 ? 210 TRP A CG  1 
ATOM   1717 C CD1 . TRP A 1 216 ? 1.58255   9.60286   57.35464 1.000 13.80070 ? 210 TRP A CD1 1 
ATOM   1718 C CD2 . TRP A 1 216 ? 2.54784   8.55489   59.06289 1.000 11.90780 ? 210 TRP A CD2 1 
ATOM   1719 N NE1 . TRP A 1 216 ? 1.84855   10.54943  58.31861 1.000 13.54383 ? 210 TRP A NE1 1 
ATOM   1720 C CE2 . TRP A 1 216 ? 2.42095   9.92289   59.39186 1.000 12.94006 ? 210 TRP A CE2 1 
ATOM   1721 C CE3 . TRP A 1 216 ? 3.13647   7.67337   59.98975 1.000 13.47574 ? 210 TRP A CE3 1 
ATOM   1722 C CZ2 . TRP A 1 216 ? 2.82463   10.44439  60.63348 1.000 13.61300 ? 210 TRP A CZ2 1 
ATOM   1723 C CZ3 . TRP A 1 216 ? 3.55447   8.17610   61.22280 1.000 15.01968 ? 210 TRP A CZ3 1 
ATOM   1724 C CH2 . TRP A 1 216 ? 3.39813   9.56044   61.53236 1.000 15.11375 ? 210 TRP A CH2 1 
ATOM   1725 N N   . SER A 1 217 ? -0.89681  7.37887   55.57381 1.000 12.98934 ? 211 SER A N   1 
ATOM   1726 C CA  . SER A 1 217 ? -1.97388  8.24499   55.14819 1.000 12.38296 ? 211 SER A CA  1 
ATOM   1727 C C   . SER A 1 217 ? -3.31166  7.80329   55.75968 1.000 13.51438 ? 211 SER A C   1 
ATOM   1728 O O   . SER A 1 217 ? -4.09183  8.65548   56.19931 1.000 14.02843 ? 211 SER A O   1 
ATOM   1729 C CB  . SER A 1 217 ? -2.07215  8.27225   53.59545 1.000 12.28296 ? 211 SER A CB  1 
ATOM   1730 O OG  . SER A 1 217 ? -0.84862  8.74757   53.01769 1.000 14.07058 ? 211 SER A OG  1 
ATOM   1731 N N   . VAL A 1 218 ? -3.60102  6.50064   55.75641 1.000 12.81046 ? 212 VAL A N   1 
ATOM   1732 C CA  . VAL A 1 218 ? -4.84534  5.99043   56.36623 1.000 12.82011 ? 212 VAL A CA  1 
ATOM   1733 C C   . VAL A 1 218 ? -4.89092  6.34996   57.85814 1.000 11.50325 ? 212 VAL A C   1 
ATOM   1734 O O   . VAL A 1 218 ? -5.93681  6.69355   58.40733 1.000 13.25628 ? 212 VAL A O   1 
ATOM   1735 C CB  . VAL A 1 218 ? -4.94822  4.46386   56.17580 1.000 13.40116 ? 212 VAL A CB  1 
ATOM   1736 C CG1 . VAL A 1 218 ? -6.21203  3.90957   56.86893 1.000 15.04573 ? 212 VAL A CG1 1 
ATOM   1737 C CG2 . VAL A 1 218 ? -4.99328  4.12848   54.70299 1.000 14.87407 ? 212 VAL A CG2 1 
ATOM   1738 N N   . GLY A 1 219 ? -3.73182  6.26922   58.54551 1.000 10.95824 ? 213 GLY A N   1 
ATOM   1739 C CA  . GLY A 1 219 ? -3.73071  6.65372   59.94872 1.000 11.98884 ? 213 GLY A CA  1 
ATOM   1740 C C   . GLY A 1 219 ? -4.09423  8.11868   60.12548 1.000 13.23571 ? 213 GLY A C   1 
ATOM   1741 O O   . GLY A 1 219 ? -4.82990  8.47849   61.04752 1.000 14.31381 ? 213 GLY A O   1 
ATOM   1742 N N   . CYS A 1 220 ? -3.57444  8.99364   59.23964 1.000 12.27997 ? 214 CYS A N   1 
ATOM   1743 C CA  . CYS A 1 220 ? -3.94499  10.41334  59.28517 1.000 12.40885 ? 214 CYS A CA  1 
ATOM   1744 C C   . CYS A 1 220 ? -5.43432  10.59807  59.06649 1.000 13.93136 ? 214 CYS A C   1 
ATOM   1745 O O   . CYS A 1 220 ? -6.05688  11.48638  59.68268 1.000 14.62330 ? 214 CYS A O   1 
ATOM   1746 C CB  . CYS A 1 220 ? -3.18984  11.19477  58.20065 1.000 11.91103 ? 214 CYS A CB  1 
ATOM   1747 S SG  . CYS A 1 220 ? -1.36198  11.28030  58.56803 1.000 13.94289 ? 214 CYS A SG  1 
ATOM   1748 N N   . ILE A 1 221 ? -6.00573  9.81298   58.15427 1.000 13.35822 ? 215 ILE A N   1 
ATOM   1749 C CA  . ILE A 1 221 ? -7.45028  9.89755   57.86253 1.000 12.59375 ? 215 ILE A CA  1 
ATOM   1750 C C   . ILE A 1 221 ? -8.27097  9.44932   59.06712 1.000 13.38222 ? 215 ILE A C   1 
ATOM   1751 O O   . ILE A 1 221 ? -9.30003  10.07034  59.41062 1.000 14.63905 ? 215 ILE A O   1 
ATOM   1752 C CB  . ILE A 1 221 ? -7.77766  9.06534   56.58327 1.000 12.16588 ? 215 ILE A CB  1 
ATOM   1753 C CG1 . ILE A 1 221 ? -7.11028  9.70323   55.37469 1.000 13.08004 ? 215 ILE A CG1 1 
ATOM   1754 C CG2 . ILE A 1 221 ? -9.32756  8.94906   56.38394 1.000 14.65670 ? 215 ILE A CG2 1 
ATOM   1755 C CD1 . ILE A 1 221 ? -6.94395  8.81176   54.15981 1.000 13.81554 ? 215 ILE A CD1 1 
ATOM   1756 N N   . LEU A 1 222 ? -7.87052  8.34889   59.70187 1.000 13.39874 ? 216 LEU A N   1 
ATOM   1757 C CA  . LEU A 1 222 ? -8.56315  7.90455   60.91703 1.000 13.03177 ? 216 LEU A CA  1 
ATOM   1758 C C   . LEU A 1 222 ? -8.56181  8.99337   61.98915 1.000 14.35918 ? 216 LEU A C   1 
ATOM   1759 O O   . LEU A 1 222 ? -9.60524  9.27213   62.60921 1.000 14.29938 ? 216 LEU A O   1 
ATOM   1760 C CB  . LEU A 1 222 ? -7.89153  6.62035   61.43301 1.000 13.83975 ? 216 LEU A CB  1 
ATOM   1761 C CG  . LEU A 1 222 ? -8.37145  6.11750   62.81685 1.000 12.85988 ? 216 LEU A CG  1 
ATOM   1762 C CD1 . LEU A 1 222 ? -9.96691  5.90392   62.80031 1.000 13.53683 ? 216 LEU A CD1 1 
ATOM   1763 C CD2 . LEU A 1 222 ? -7.67534  4.80284   63.23086 1.000 14.40462 ? 216 LEU A CD2 1 
ATOM   1764 N N   . ALA A 1 223 ? -7.38658  9.60312   62.25602 1.000 14.81421 ? 217 ALA A N   1 
ATOM   1765 C CA  . ALA A 1 223 ? -7.34664  10.68587  63.24862 1.000 15.27447 ? 217 ALA A CA  1 
ATOM   1766 C C   . ALA A 1 223 ? -8.32236  11.79465  62.89213 1.000 16.64632 ? 217 ALA A C   1 
ATOM   1767 O O   . ALA A 1 223 ? -8.99299  12.35128  63.77632 1.000 17.06650 ? 217 ALA A O   1 
ATOM   1768 C CB  . ALA A 1 223 ? -5.90458  11.28119  63.39334 1.000 15.68901 ? 217 ALA A CB  1 
ATOM   1769 N N   . GLU A 1 224 ? -8.36283  12.17128  61.60761 1.000 16.85146 ? 218 GLU A N   1 
ATOM   1770 C CA  . GLU A 1 224 ? -9.21881  13.24173  61.14126 1.000 16.44039 ? 218 GLU A CA  1 
ATOM   1771 C C   . GLU A 1 224 ? -10.69717 12.84856  61.26063 1.000 17.87446 ? 218 GLU A C   1 
ATOM   1772 O O   . GLU A 1 224 ? -11.55139 13.70095  61.55682 1.000 20.60075 ? 218 GLU A O   1 
ATOM   1773 C CB  . GLU A 1 224 ? -8.83910  13.59790  59.69256 1.000 16.09977 ? 218 GLU A CB  1 
ATOM   1774 C CG  . GLU A 1 224 ? -9.43949  14.92538  59.19871 1.000 17.47891 ? 218 GLU A CG  1 
ATOM   1775 C CD  . GLU A 1 224 ? -8.69941  15.43589  57.96890 1.000 19.51148 ? 218 GLU A CD  1 
ATOM   1776 O OE1 . GLU A 1 224 ? -7.54468  14.99577  57.66290 1.000 19.76391 ? 218 GLU A OE1 1 
ATOM   1777 O OE2 . GLU A 1 224 ? -9.24415  16.31960  57.32838 1.000 21.30922 ? 218 GLU A OE2 1 
ATOM   1778 N N   . MET A 1 225 ? -11.02154 11.56944  61.05065 1.000 17.24126 ? 219 MET A N   1 
ATOM   1779 C CA  . MET A 1 225 ? -12.40847 11.17369  61.37934 1.000 17.30639 ? 219 MET A CA  1 
ATOM   1780 C C   . MET A 1 225 ? -12.75849 11.24713  62.85690 1.000 19.02438 ? 219 MET A C   1 
ATOM   1781 O O   . MET A 1 225 ? -13.94729 11.52011  63.19656 1.000 20.31929 ? 219 MET A O   1 
ATOM   1782 C CB  . MET A 1 225 ? -12.91965 9.86773   60.75919 1.000 18.55464 ? 219 MET A CB  1 
ATOM   1783 C CG  . MET A 1 225 ? -12.63323 9.59068   59.27902 1.000 16.61254 ? 219 MET A CG  1 
ATOM   1784 S SD  . MET A 1 225 ? -13.30107 7.97953   58.78345 1.000 18.12430 ? 219 MET A SD  1 
ATOM   1785 C CE  . MET A 1 225 ? -11.91306 6.86347   59.23276 1.000 17.93868 ? 219 MET A CE  1 
ATOM   1786 N N   . LEU A 1 226 ? -11.77224 11.09371  63.72659 1.000 18.70362 ? 220 LEU A N   1 
ATOM   1787 C CA  . LEU A 1 226 ? -12.07079 11.15653  65.16092 1.000 20.18124 ? 220 LEU A CA  1 
ATOM   1788 C C   . LEU A 1 226 ? -12.34976 12.57959  65.62735 1.000 22.08281 ? 220 LEU A C   1 
ATOM   1789 O O   . LEU A 1 226 ? -13.13901 12.78995  66.56417 1.000 25.08178 ? 220 LEU A O   1 
ATOM   1790 C CB  . LEU A 1 226 ? -10.91085 10.54734  65.93073 1.000 20.23408 ? 220 LEU A CB  1 
ATOM   1791 C CG  . LEU A 1 226 ? -10.74094 9.03147   65.77591 1.000 20.41463 ? 220 LEU A CG  1 
ATOM   1792 C CD1 . LEU A 1 226 ? -9.29664  8.63675   66.34632 1.000 20.43267 ? 220 LEU A CD1 1 
ATOM   1793 C CD2 . LEU A 1 226 ? -11.85478 8.24284   66.49985 1.000 20.80177 ? 220 LEU A CD2 1 
ATOM   1794 N N   . SER A 1 227 ? -11.76468 13.57725  64.98360 1.000 21.62611 ? 221 SER A N   1 
ATOM   1795 C CA  . SER A 1 227 ? -11.91363 14.92237  65.50101 1.000 23.96001 ? 221 SER A CA  1 
ATOM   1796 C C   . SER A 1 227 ? -12.38138 15.99851  64.53280 1.000 24.24652 ? 221 SER A C   1 
ATOM   1797 O O   . SER A 1 227 ? -12.54855 17.15518  64.96862 1.000 24.88762 ? 221 SER A O   1 
ATOM   1798 C CB  . SER A 1 227 ? -10.57559 15.36571  66.09448 1.000 25.25504 ? 221 SER A CB  1 
ATOM   1799 O OG  . SER A 1 227 ? -9.66934  15.48434  65.04182 1.000 26.07706 ? 221 SER A OG  1 
ATOM   1800 N N   . ASN A 1 228 ? -12.58638 15.67686  63.25646 1.000 23.19778 ? 222 ASN A N   1 
ATOM   1801 C CA  . ASN A 1 228 ? -12.93464 16.61486  62.19015 1.000 22.93538 ? 222 ASN A CA  1 
ATOM   1802 C C   . ASN A 1 228 ? -11.84036 17.65003  61.89980 1.000 25.99332 ? 222 ASN A C   1 
ATOM   1803 O O   . ASN A 1 228 ? -12.12191 18.67969  61.28992 1.000 29.23963 ? 222 ASN A O   1 
ATOM   1804 C CB  . ASN A 1 228 ? -14.28885 17.32964  62.47563 1.000 23.66102 ? 222 ASN A CB  1 
ATOM   1805 C CG  . ASN A 1 228 ? -15.44327 16.39725  62.39354 1.000 24.03674 ? 222 ASN A CG  1 
ATOM   1806 O OD1 . ASN A 1 228 ? -15.72501 15.65493  63.34233 1.000 24.30749 ? 222 ASN A OD1 1 
ATOM   1807 N ND2 . ASN A 1 228 ? -16.16526 16.44432  61.27648 1.000 24.18319 ? 222 ASN A ND2 1 
ATOM   1808 N N   . ARG A 1 229 ? -10.58581 17.43810  62.31079 1.000 24.38131 ? 223 ARG A N   1 
ATOM   1809 C CA  . ARG A 1 229 ? -9.49780  18.36861  62.01504 1.000 24.21494 ? 223 ARG A CA  1 
ATOM   1810 C C   . ARG A 1 229 ? -8.29655  17.52859  61.57829 1.000 21.84672 ? 223 ARG A C   1 
ATOM   1811 O O   . ARG A 1 229 ? -8.07288  16.44620  62.12307 1.000 20.69934 ? 223 ARG A O   1 
ATOM   1812 C CB  . ARG A 1 229 ? -9.12804  19.20068  63.25027 0.800 25.94930 ? 223 ARG A CB  1 
ATOM   1813 C CG  . ARG A 1 229 ? -8.93138  18.29663  64.45397 0.700 28.18661 ? 223 ARG A CG  1 
ATOM   1814 C CD  . ARG A 1 229 ? -8.14187  18.85850  65.65139 0.600 30.11157 ? 223 ARG A CD  1 
ATOM   1815 N NE  . ARG A 1 229 ? -7.46853  17.78379  66.38766 0.500 31.14391 ? 223 ARG A NE  1 
ATOM   1816 C CZ  . ARG A 1 229 ? -7.82479  17.37162  67.59688 0.500 31.27350 ? 223 ARG A CZ  1 
ATOM   1817 N NH1 . ARG A 1 229 ? -8.86394  17.90104  68.23269 0.500 31.41856 ? 223 ARG A NH1 1 
ATOM   1818 N NH2 . ARG A 1 229 ? -7.10310  16.43059  68.19860 0.500 30.63896 ? 223 ARG A NH2 1 
ATOM   1819 N N   . PRO A 1 230 ? -7.52108  17.97497  60.60534 1.000 21.02766 ? 224 PRO A N   1 
ATOM   1820 C CA  . PRO A 1 230 ? -6.26731  17.25232  60.30796 1.000 20.99663 ? 224 PRO A CA  1 
ATOM   1821 C C   . PRO A 1 230 ? -5.35672  17.16778  61.53307 1.000 20.39339 ? 224 PRO A C   1 
ATOM   1822 O O   . PRO A 1 230 ? -5.14167  18.17272  62.22956 1.000 21.37296 ? 224 PRO A O   1 
ATOM   1823 C CB  . PRO A 1 230 ? -5.63548  18.08545  59.18640 1.000 21.60770 ? 224 PRO A CB  1 
ATOM   1824 C CG  . PRO A 1 230 ? -6.34381  19.43636  59.26737 1.000 24.02558 ? 224 PRO A CG  1 
ATOM   1825 C CD  . PRO A 1 230 ? -7.72961  19.16562  59.75208 1.000 23.20736 ? 224 PRO A CD  1 
ATOM   1826 N N   . ILE A 1 231 ? -4.75659  15.97796  61.74615 1.000 19.68347 ? 225 ILE A N   1 
ATOM   1827 C CA  . ILE A 1 231 ? -3.88059  15.76387  62.91460 1.000 17.75976 ? 225 ILE A CA  1 
ATOM   1828 C C   . ILE A 1 231 ? -2.51358  16.45120  62.75633 1.000 18.32161 ? 225 ILE A C   1 
ATOM   1829 O O   . ILE A 1 231 ? -1.96267  16.98095  63.73455 1.000 18.46227 ? 225 ILE A O   1 
ATOM   1830 C CB  . ILE A 1 231 ? -3.74132  14.23473  63.20695 1.000 17.53772 ? 225 ILE A CB  1 
ATOM   1831 C CG1 . ILE A 1 231 ? -2.83410  14.03837  64.43290 1.000 18.72832 ? 225 ILE A CG1 1 
ATOM   1832 C CG2 . ILE A 1 231 ? -3.21838  13.39413  61.98709 1.000 17.04140 ? 225 ILE A CG2 1 
ATOM   1833 C CD1 . ILE A 1 231 ? -2.63656  12.63735  64.89776 1.000 20.53934 ? 225 ILE A CD1 1 
ATOM   1834 N N   . PHE A 1 232 ? -1.98274  16.53740  61.53590 1.000 17.33972 ? 226 PHE A N   1 
ATOM   1835 C CA  . PHE A 1 232 ? -0.65161  17.11751  61.26931 1.000 17.30172 ? 226 PHE A CA  1 
ATOM   1836 C C   . PHE A 1 232 ? -0.72814  18.18956  60.16835 1.000 21.07293 ? 226 PHE A C   1 
ATOM   1837 O O   . PHE A 1 232 ? -0.26935  17.97274  59.04113 1.000 20.42897 ? 226 PHE A O   1 
ATOM   1838 C CB  . PHE A 1 232 ? 0.34457   16.03746  60.83778 1.000 16.88662 ? 226 PHE A CB  1 
ATOM   1839 C CG  . PHE A 1 232 ? 0.44366   14.84208  61.75676 1.000 16.56092 ? 226 PHE A CG  1 
ATOM   1840 C CD1 . PHE A 1 232 ? 0.81800   14.99275  63.11028 1.000 16.35502 ? 226 PHE A CD1 1 
ATOM   1841 C CD2 . PHE A 1 232 ? 0.27923   13.56685  61.25237 1.000 15.34274 ? 226 PHE A CD2 1 
ATOM   1842 C CE1 . PHE A 1 232 ? 0.97092   13.86822  63.94047 1.000 15.73703 ? 226 PHE A CE1 1 
ATOM   1843 C CE2 . PHE A 1 232 ? 0.39123   12.41847  62.07988 1.000 14.74751 ? 226 PHE A CE2 1 
ATOM   1844 C CZ  . PHE A 1 232 ? 0.76369   12.56409  63.43252 1.000 14.59804 ? 226 PHE A CZ  1 
ATOM   1845 N N   . PRO A 1 233 ? -1.33715  19.35934  60.45618 1.000 24.25117 ? 227 PRO A N   1 
ATOM   1846 C CA  . PRO A 1 233 ? -1.55952  20.35774  59.37989 1.000 25.54288 ? 227 PRO A CA  1 
ATOM   1847 C C   . PRO A 1 233 ? -0.33587  21.25798  59.17792 1.000 26.23980 ? 227 PRO A C   1 
ATOM   1848 O O   . PRO A 1 233 ? -0.32761  22.46304  59.50356 1.000 27.44609 ? 227 PRO A O   1 
ATOM   1849 C CB  . PRO A 1 233 ? -2.77852  21.13026  59.90496 1.000 27.47956 ? 227 PRO A CB  1 
ATOM   1850 C CG  . PRO A 1 233 ? -2.56721  21.10921  61.43047 1.000 27.18620 ? 227 PRO A CG  1 
ATOM   1851 C CD  . PRO A 1 233 ? -1.95471  19.75249  61.73393 1.000 25.40107 ? 227 PRO A CD  1 
ATOM   1852 N N   . GLY A 1 234 ? 0.75270   20.68553  58.67087 1.000 25.42604 ? 228 GLY A N   1 
ATOM   1853 C CA  . GLY A 1 234 ? 1.94064   21.48996  58.42289 1.000 26.63046 ? 228 GLY A CA  1 
ATOM   1854 C C   . GLY A 1 234 ? 1.64317   22.58839  57.41413 1.000 29.59312 ? 228 GLY A C   1 
ATOM   1855 O O   . GLY A 1 234 ? 0.92114   22.37734  56.43356 1.000 30.36868 ? 228 GLY A O   1 
ATOM   1856 N N   . LYS A 1 235 ? 2.22101   23.77165  57.65552 1.000 31.35380 ? 229 LYS A N   1 
ATOM   1857 C CA  . LYS A 1 235 ? 1.93195   24.95646  56.84952 1.000 34.25835 ? 229 LYS A CA  1 
ATOM   1858 C C   . LYS A 1 235 ? 2.76922   25.02348  55.59086 1.000 35.44792 ? 229 LYS A C   1 
ATOM   1859 O O   . LYS A 1 235 ? 2.50950   25.89671  54.74040 1.000 37.68781 ? 229 LYS A O   1 
ATOM   1860 C CB  . LYS A 1 235 ? 2.16200   26.24653  57.64678 1.000 35.00687 ? 229 LYS A CB  1 
ATOM   1861 C CG  . LYS A 1 235 ? 1.35320   26.38559  58.93223 0.700 35.85758 ? 229 LYS A CG  1 
ATOM   1862 C CD  . LYS A 1 235 ? 0.35248   27.52579  58.82874 0.600 36.39337 ? 229 LYS A CD  1 
ATOM   1863 C CE  . LYS A 1 235 ? 0.25397   28.21992  60.14958 0.600 36.86978 ? 229 LYS A CE  1 
ATOM   1864 N NZ  . LYS A 1 235 ? 0.11405   27.15584  61.16519 0.600 37.40258 ? 229 LYS A NZ  1 
ATOM   1865 N N   . HIS A 1 236 ? 3.79949   24.18983  55.49309 1.000 34.60363 ? 230 HIS A N   1 
ATOM   1866 C CA  . HIS A 1 236 ? 4.71543   24.12351  54.35794 1.000 35.54454 ? 230 HIS A CA  1 
ATOM   1867 C C   . HIS A 1 236 ? 5.53964   22.84945  54.54113 1.000 36.03317 ? 230 HIS A C   1 
ATOM   1868 O O   . HIS A 1 236 ? 5.47737   22.20668  55.59988 1.000 34.13976 ? 230 HIS A O   1 
ATOM   1869 C CB  . HIS A 1 236 ? 5.60599   25.38685  54.24370 1.000 35.95537 ? 230 HIS A CB  1 
ATOM   1870 C CG  . HIS A 1 236 ? 6.30642   25.75805  55.51996 1.000 35.81105 ? 230 HIS A CG  1 
ATOM   1871 N ND1 . HIS A 1 236 ? 7.44458   25.10862  55.96836 1.000 35.08099 ? 230 HIS A ND1 1 
ATOM   1872 C CD2 . HIS A 1 236 ? 6.02535   26.71063  56.44875 1.000 34.93555 ? 230 HIS A CD2 1 
ATOM   1873 C CE1 . HIS A 1 236 ? 7.80678   25.61776  57.13177 1.000 34.21781 ? 230 HIS A CE1 1 
ATOM   1874 N NE2 . HIS A 1 236 ? 6.98953   26.61903  57.42274 1.000 34.44231 ? 230 HIS A NE2 1 
ATOM   1875 N N   . TYR A 1 237 ? 6.24968   22.44164  53.46131 1.000 37.89342 ? 231 TYR A N   1 
ATOM   1876 C CA  . TYR A 1 237 ? 7.03087   21.18294  53.42359 1.000 37.48053 ? 231 TYR A CA  1 
ATOM   1877 C C   . TYR A 1 237 ? 7.75328   20.89169  54.71203 1.000 34.76268 ? 231 TYR A C   1 
ATOM   1878 O O   . TYR A 1 237 ? 7.72994   19.77580  55.26012 1.000 31.58218 ? 231 TYR A O   1 
ATOM   1879 C CB  . TYR A 1 237 ? 8.08935   21.25225  52.31204 1.000 39.80675 ? 231 TYR A CB  1 
ATOM   1880 C CG  . TYR A 1 237 ? 8.92396   19.97934  52.11947 1.000 40.76743 ? 231 TYR A CG  1 
ATOM   1881 C CD1 . TYR A 1 237 ? 10.10184  19.76526  52.82927 1.000 40.76850 ? 231 TYR A CD1 1 
ATOM   1882 C CD2 . TYR A 1 237 ? 8.47801   18.95929  51.27252 1.000 40.83493 ? 231 TYR A CD2 1 
ATOM   1883 C CE1 . TYR A 1 237 ? 10.83029  18.57199  52.68761 1.000 41.05076 ? 231 TYR A CE1 1 
ATOM   1884 C CE2 . TYR A 1 237 ? 9.21193   17.78386  51.08134 1.000 40.88183 ? 231 TYR A CE2 1 
ATOM   1885 C CZ  . TYR A 1 237 ? 10.39174  17.58834  51.77322 0.900 40.52985 ? 231 TYR A CZ  1 
ATOM   1886 O OH  . TYR A 1 237 ? 11.08765  16.39767  51.60352 1.000 39.33358 ? 231 TYR A OH  1 
ATOM   1887 N N   . LEU A 1 238 ? 8.44639   21.92041  55.16101 1.000 35.11380 ? 232 LEU A N   1 
ATOM   1888 C CA  . LEU A 1 238 ? 9.39890   21.79517  56.23675 1.000 33.07492 ? 232 LEU A CA  1 
ATOM   1889 C C   . LEU A 1 238 ? 8.66688   21.66596  57.57354 1.000 32.89328 ? 232 LEU A C   1 
ATOM   1890 O O   . LEU A 1 238 ? 9.03051   20.84626  58.42679 1.000 33.62161 ? 232 LEU A O   1 
ATOM   1891 C CB  . LEU A 1 238 ? 10.32846  23.02726  56.18709 1.000 32.99634 ? 232 LEU A CB  1 
ATOM   1892 C CG  . LEU A 1 238 ? 11.06125  23.25032  54.83948 1.000 32.64926 ? 232 LEU A CG  1 
ATOM   1893 C CD1 . LEU A 1 238 ? 11.72358  24.65902  54.70940 1.000 33.28189 ? 232 LEU A CD1 1 
ATOM   1894 C CD2 . LEU A 1 238 ? 12.12199  22.17663  54.54948 1.000 34.03708 ? 232 LEU A CD2 1 
ATOM   1895 N N   . ASP A 1 239 ? 7.54377   22.36631  57.70010 1.000 31.12023 ? 233 ASP A N   1 
ATOM   1896 C CA  . ASP A 1 239 ? 6.73020   22.32824  58.91087 1.000 27.17472 ? 233 ASP A CA  1 
ATOM   1897 C C   . ASP A 1 239 ? 6.12034   20.95180  59.18222 1.000 24.03377 ? 233 ASP A C   1 
ATOM   1898 O O   . ASP A 1 239 ? 5.76909   20.66320  60.33002 1.000 23.28695 ? 233 ASP A O   1 
ATOM   1899 C CB  . ASP A 1 239 ? 5.62968   23.37190  58.75578 1.000 26.92973 ? 233 ASP A CB  1 
ATOM   1900 C CG  . ASP A 1 239 ? 5.02447   23.80632  60.04926 1.000 27.25217 ? 233 ASP A CG  1 
ATOM   1901 O OD1 . ASP A 1 239 ? 5.69820   23.89914  61.10748 1.000 27.58790 ? 233 ASP A OD1 1 
ATOM   1902 O OD2 . ASP A 1 239 ? 3.81768   24.06121  60.00403 1.000 27.92332 ? 233 ASP A OD2 1 
ATOM   1903 N N   . GLN A 1 240 ? 5.95475   20.10946  58.15179 1.000 21.79177 ? 234 GLN A N   1 
ATOM   1904 C CA  . GLN A 1 240 ? 5.19144   18.86163  58.32654 1.000 20.41205 ? 234 GLN A CA  1 
ATOM   1905 C C   . GLN A 1 240 ? 5.85634   17.94875  59.34364 1.000 21.15408 ? 234 GLN A C   1 
ATOM   1906 O O   . GLN A 1 240 ? 5.16677   17.32598  60.17040 1.000 22.53862 ? 234 GLN A O   1 
ATOM   1907 C CB  . GLN A 1 240 ? 5.05161   18.14828  56.98323 1.000 19.39081 ? 234 GLN A CB  1 
ATOM   1908 C CG  . GLN A 1 240 ? 4.08166   16.99167  56.99893 1.000 18.96506 ? 234 GLN A CG  1 
ATOM   1909 C CD  . GLN A 1 240 ? 2.64786   17.43022  57.35471 1.000 19.24298 ? 234 GLN A CD  1 
ATOM   1910 O OE1 . GLN A 1 240 ? 2.24278   18.60175  57.11660 1.000 20.20317 ? 234 GLN A OE1 1 
ATOM   1911 N NE2 . GLN A 1 240 ? 1.89994   16.52712  58.01815 1.000 19.03509 ? 234 GLN A NE2 1 
ATOM   1912 N N   . LEU A 1 241 ? 7.20650   17.85163  59.29549 1.000 21.76904 ? 235 LEU A N   1 
ATOM   1913 C CA  . LEU A 1 241 ? 7.89283   17.00897  60.27563 0.850 22.68078 ? 235 LEU A CA  1 
ATOM   1914 C C   . LEU A 1 241 ? 7.77514   17.56639  61.68889 1.000 23.84730 ? 235 LEU A C   1 
ATOM   1915 O O   . LEU A 1 241 ? 7.69195   16.77300  62.64455 1.000 24.10430 ? 235 LEU A O   1 
ATOM   1916 C CB  . LEU A 1 241 ? 9.36346   16.82641  59.86980 1.000 24.59327 ? 235 LEU A CB  1 
ATOM   1917 C CG  . LEU A 1 241 ? 10.19182  15.75313  60.57066 1.000 25.14569 ? 235 LEU A CG  1 
ATOM   1918 C CD1 . LEU A 1 241 ? 9.60443   14.34195  60.48400 1.000 26.08754 ? 235 LEU A CD1 1 
ATOM   1919 C CD2 . LEU A 1 241 ? 11.56586  15.79784  59.93526 1.000 24.46016 ? 235 LEU A CD2 1 
ATOM   1920 N N   . ASN A 1 242 ? 7.73713   18.90938  61.84646 1.000 24.88040 ? 236 ASN A N   1 
ATOM   1921 C CA  . ASN A 1 242 ? 7.51967   19.52037  63.17424 1.000 24.33484 ? 236 ASN A CA  1 
ATOM   1922 C C   . ASN A 1 242 ? 6.19471   19.03900  63.77045 1.000 23.40410 ? 236 ASN A C   1 
ATOM   1923 O O   . ASN A 1 242 ? 6.07915   18.74114  64.97063 1.000 23.54454 ? 236 ASN A O   1 
ATOM   1924 C CB  . ASN A 1 242 ? 7.49363   21.09069  63.15402 0.800 23.68802 ? 236 ASN A CB  1 
ATOM   1925 C CG  . ASN A 1 242 ? 8.74830   21.82536  62.48676 0.700 24.20444 ? 236 ASN A CG  1 
ATOM   1926 O OD1 . ASN A 1 242 ? 9.91418   21.38668  62.59680 0.700 24.68147 ? 236 ASN A OD1 1 
ATOM   1927 N ND2 . ASN A 1 242 ? 8.49143   23.05893  61.94042 0.700 22.17422 ? 236 ASN A ND2 1 
ATOM   1928 N N   . HIS A 1 243 ? 5.16319   19.01300  62.96698 1.000 21.59094 ? 237 HIS A N   1 
ATOM   1929 C CA  . HIS A 1 243 ? 3.88311   18.56523  63.49918 1.000 20.31379 ? 237 HIS A CA  1 
ATOM   1930 C C   . HIS A 1 243 ? 3.91750   17.09031  63.89558 1.000 20.25691 ? 237 HIS A C   1 
ATOM   1931 O O   . HIS A 1 243 ? 3.38654   16.71213  64.95864 1.000 19.45669 ? 237 HIS A O   1 
ATOM   1932 C CB  . HIS A 1 243 ? 2.78555   18.85069  62.47129 1.000 20.68091 ? 237 HIS A CB  1 
ATOM   1933 C CG  . HIS A 1 243 ? 2.38541   20.27869  62.43115 1.000 23.52886 ? 237 HIS A CG  1 
ATOM   1934 N ND1 . HIS A 1 243 ? 1.24206   20.74646  63.04653 1.000 26.30022 ? 237 HIS A ND1 1 
ATOM   1935 C CD2 . HIS A 1 243 ? 2.96469   21.34898  61.83400 1.000 25.07988 ? 237 HIS A CD2 1 
ATOM   1936 C CE1 . HIS A 1 243 ? 1.14565   22.04987  62.84920 1.000 27.65582 ? 237 HIS A CE1 1 
ATOM   1937 N NE2 . HIS A 1 243 ? 2.17153   22.43983  62.10484 1.000 27.48120 ? 237 HIS A NE2 1 
ATOM   1938 N N   . ILE A 1 244 ? 4.53277   16.24513  63.06845 1.000 18.63470 ? 238 ILE A N   1 
ATOM   1939 C CA  . ILE A 1 244 ? 4.56033   14.80647  63.36669 1.000 18.16619 ? 238 ILE A CA  1 
ATOM   1940 C C   . ILE A 1 244 ? 5.28246   14.55535  64.68292 1.000 18.39316 ? 238 ILE A C   1 
ATOM   1941 O O   . ILE A 1 244 ? 4.78346   13.85018  65.57530 1.000 18.54207 ? 238 ILE A O   1 
ATOM   1942 C CB  . ILE A 1 244 ? 5.20167   14.02896  62.20071 1.000 16.83669 ? 238 ILE A CB  1 
ATOM   1943 C CG1 . ILE A 1 244 ? 4.26986   14.15405  60.96225 1.000 16.74689 ? 238 ILE A CG1 1 
ATOM   1944 C CG2 . ILE A 1 244 ? 5.33557   12.58281  62.54254 1.000 15.75847 ? 238 ILE A CG2 1 
ATOM   1945 C CD1 . ILE A 1 244 ? 4.91297   13.58609  59.66537 1.000 16.74193 ? 238 ILE A CD1 1 
ATOM   1946 N N   . LEU A 1 245 ? 6.49415   15.09521  64.79395 1.000 17.89287 ? 239 LEU A N   1 
ATOM   1947 C CA  . LEU A 1 245 ? 7.28768   14.86489  65.99241 1.000 18.25661 ? 239 LEU A CA  1 
ATOM   1948 C C   . LEU A 1 245 ? 6.67508   15.54430  67.21321 1.000 18.95331 ? 239 LEU A C   1 
ATOM   1949 O O   . LEU A 1 245 ? 6.88287   15.07842  68.33586 1.000 20.38160 ? 239 LEU A O   1 
ATOM   1950 C CB  . LEU A 1 245 ? 8.73860   15.35629  65.77821 1.000 19.16340 ? 239 LEU A CB  1 
ATOM   1951 C CG  . LEU A 1 245 ? 9.49645   14.68994  64.64381 1.000 20.26789 ? 239 LEU A CG  1 
ATOM   1952 C CD1 . LEU A 1 245 ? 10.88315  15.35573  64.41344 1.000 20.80395 ? 239 LEU A CD1 1 
ATOM   1953 C CD2 . LEU A 1 245 ? 9.65062   13.23397  64.92265 1.000 22.61146 ? 239 LEU A CD2 1 
ATOM   1954 N N   . GLY A 1 246 ? 5.89615   16.61058  67.03588 1.000 19.10539 ? 240 GLY A N   1 
ATOM   1955 C CA  . GLY A 1 246 ? 5.26678   17.24338  68.20247 1.000 19.53476 ? 240 GLY A CA  1 
ATOM   1956 C C   . GLY A 1 246 ? 4.21516   16.37841  68.88568 1.000 20.07508 ? 240 GLY A C   1 
ATOM   1957 O O   . GLY A 1 246 ? 3.86414   16.63098  70.05589 1.000 21.66213 ? 240 GLY A O   1 
ATOM   1958 N N   . ILE A 1 247 ? 3.69543   15.37391  68.18109 1.000 19.91864 ? 241 ILE A N   1 
ATOM   1959 C CA  . ILE A 1 247 ? 2.74118   14.44722  68.74082 1.000 19.48482 ? 241 ILE A CA  1 
ATOM   1960 C C   . ILE A 1 247 ? 3.38416   13.10468  69.05500 1.000 19.54281 ? 241 ILE A C   1 
ATOM   1961 O O   . ILE A 1 247 ? 3.20664   12.57167  70.15286 1.000 20.99425 ? 241 ILE A O   1 
ATOM   1962 C CB  . ILE A 1 247 ? 1.50506   14.31534  67.81490 1.000 19.89890 ? 241 ILE A CB  1 
ATOM   1963 C CG1 . ILE A 1 247 ? 0.61359   15.55710  67.99723 1.000 22.58258 ? 241 ILE A CG1 1 
ATOM   1964 C CG2 . ILE A 1 247 ? 0.70947   13.02571  68.12485 1.000 20.01740 ? 241 ILE A CG2 1 
ATOM   1965 C CD1 . ILE A 1 247 ? -0.40185  15.75640  66.95924 1.000 25.11228 ? 241 ILE A CD1 1 
ATOM   1966 N N   . LEU A 1 248 ? 4.18310   12.53935  68.12504 1.000 19.37689 ? 242 LEU A N   1 
ATOM   1967 C CA  . LEU A 1 248 ? 4.80010   11.24834  68.40864 1.000 18.87350 ? 242 LEU A CA  1 
ATOM   1968 C C   . LEU A 1 248 ? 5.94932   11.36690  69.43068 1.000 19.55134 ? 242 LEU A C   1 
ATOM   1969 O O   . LEU A 1 248 ? 6.29780   10.37637  70.06415 1.000 20.68515 ? 242 LEU A O   1 
ATOM   1970 C CB  A LEU A 1 248 ? 5.32279   10.62663  67.10524 0.500 18.04153 ? 242 LEU A CB  1 
ATOM   1971 C CB  B LEU A 1 248 ? 5.36471   10.58731  67.13780 0.500 18.44770 ? 242 LEU A CB  1 
ATOM   1972 C CG  A LEU A 1 248 ? 4.38754   9.72325   66.29663 0.500 17.38358 ? 242 LEU A CG  1 
ATOM   1973 C CG  B LEU A 1 248 ? 4.38722   10.21285  66.02748 0.500 18.41585 ? 242 LEU A CG  1 
ATOM   1974 C CD1 A LEU A 1 248 ? 3.09759   10.44679  65.77776 0.500 17.13662 ? 242 LEU A CD1 1 
ATOM   1975 C CD1 B LEU A 1 248 ? 5.05749   9.41142   64.89970 0.500 18.31999 ? 242 LEU A CD1 1 
ATOM   1976 C CD2 A LEU A 1 248 ? 5.14754   9.07226   65.13056 0.500 17.30786 ? 242 LEU A CD2 1 
ATOM   1977 C CD2 B LEU A 1 248 ? 3.17547   9.45811   66.59385 0.500 19.22020 ? 242 LEU A CD2 1 
ATOM   1978 N N   . GLY A 1 249 ? 6.54337   12.53756  69.57299 1.000 19.17071 ? 243 GLY A N   1 
ATOM   1979 C CA  . GLY A 1 249 ? 7.74134   12.70445  70.38476 1.000 18.83840 ? 243 GLY A CA  1 
ATOM   1980 C C   . GLY A 1 249 ? 8.98701   12.30761  69.64946 1.000 18.78471 ? 243 GLY A C   1 
ATOM   1981 O O   . GLY A 1 249 ? 8.96329   11.87042  68.50417 1.000 19.48918 ? 243 GLY A O   1 
ATOM   1982 N N   . SER A 1 250 ? 10.11531  12.44008  70.36266 1.000 18.44033 ? 244 SER A N   1 
ATOM   1983 C CA  . SER A 1 250 ? 11.42835  12.11420  69.78603 1.000 19.08407 ? 244 SER A CA  1 
ATOM   1984 C C   . SER A 1 250 ? 11.52793  10.63263  69.43043 1.000 18.93270 ? 244 SER A C   1 
ATOM   1985 O O   . SER A 1 250 ? 11.13702  9.77727   70.23739 1.000 18.90342 ? 244 SER A O   1 
ATOM   1986 C CB  . SER A 1 250 ? 12.53157  12.45450  70.80517 1.000 18.60426 ? 244 SER A CB  1 
ATOM   1987 O OG  . SER A 1 250 ? 12.51036  13.84481  71.05502 1.000 21.13431 ? 244 SER A OG  1 
ATOM   1988 N N   . PRO A 1 251 ? 12.10147  10.29374  68.27178 1.000 18.07469 ? 245 PRO A N   1 
ATOM   1989 C CA  . PRO A 1 251 ? 12.35161  8.88101   67.94258 1.000 17.84352 ? 245 PRO A CA  1 
ATOM   1990 C C   . PRO A 1 251 ? 13.36708  8.23505   68.87182 1.000 18.01975 ? 245 PRO A C   1 
ATOM   1991 O O   . PRO A 1 251 ? 14.30247  8.87900   69.35548 1.000 17.69437 ? 245 PRO A O   1 
ATOM   1992 C CB  . PRO A 1 251 ? 12.91684  8.92963   66.50278 1.000 19.67539 ? 245 PRO A CB  1 
ATOM   1993 C CG  . PRO A 1 251 ? 12.59920  10.26535  66.00603 1.000 21.34940 ? 245 PRO A CG  1 
ATOM   1994 C CD  . PRO A 1 251 ? 12.45139  11.20642  67.16185 1.000 19.02918 ? 245 PRO A CD  1 
ATOM   1995 N N   . SER A 1 252 ? 13.14497  6.94727   69.12350 1.000 16.78334 ? 246 SER A N   1 
ATOM   1996 C CA  . SER A 1 252 ? 14.02888  6.13934   69.94837 1.000 16.91316 ? 246 SER A CA  1 
ATOM   1997 C C   . SER A 1 252 ? 15.40104  6.00020   69.29431 1.000 18.20163 ? 246 SER A C   1 
ATOM   1998 O O   . SER A 1 252 ? 15.58891  6.22464   68.08722 1.000 18.08369 ? 246 SER A O   1 
ATOM   1999 C CB  . SER A 1 252 ? 13.41935  4.75231   70.16147 1.000 17.26770 ? 246 SER A CB  1 
ATOM   2000 O OG  . SER A 1 252 ? 13.34584  3.99925   68.95565 1.000 19.28522 ? 246 SER A OG  1 
ATOM   2001 N N   . GLN A 1 253 ? 16.36883  5.59542   70.10814 1.000 19.50886 ? 247 GLN A N   1 
ATOM   2002 C CA  . GLN A 1 253 ? 17.68449  5.27834   69.56567 1.000 20.85761 ? 247 GLN A CA  1 
ATOM   2003 C C   . GLN A 1 253 ? 17.59233  4.21689   68.49075 1.000 20.91527 ? 247 GLN A C   1 
ATOM   2004 O O   . GLN A 1 253 ? 18.25757  4.31795   67.45790 1.000 20.91109 ? 247 GLN A O   1 
ATOM   2005 C CB  . GLN A 1 253 ? 18.61169  4.78200   70.69048 1.000 23.89027 ? 247 GLN A CB  1 
ATOM   2006 C CG  . GLN A 1 253 ? 20.02131  4.47910   70.23880 1.000 26.78362 ? 247 GLN A CG  1 
ATOM   2007 C CD  A GLN A 1 253 ? 20.90264  4.09256   71.40685 0.600 29.27667 ? 247 GLN A CD  1 
ATOM   2008 C CD  B GLN A 1 253 ? 20.82719  5.72838   69.81594 0.400 27.04370 ? 247 GLN A CD  1 
ATOM   2009 O OE1 A GLN A 1 253 ? 20.53293  3.27009   72.25563 0.600 30.69632 ? 247 GLN A OE1 1 
ATOM   2010 O OE1 B GLN A 1 253 ? 21.12478  5.94008   68.63318 0.400 26.78070 ? 247 GLN A OE1 1 
ATOM   2011 N NE2 A GLN A 1 253 ? 22.04134  4.71989   71.48680 0.600 30.64617 ? 247 GLN A NE2 1 
ATOM   2012 N NE2 B GLN A 1 253 ? 21.19616  6.54671   70.80138 0.400 27.19992 ? 247 GLN A NE2 1 
ATOM   2013 N N   . GLU A 1 254 ? 16.78476  3.18095   68.72250 1.000 20.54422 ? 248 GLU A N   1 
ATOM   2014 C CA  . GLU A 1 254 ? 16.69808  2.09011   67.75982 1.000 21.49557 ? 248 GLU A CA  1 
ATOM   2015 C C   . GLU A 1 254 ? 16.13894  2.58883   66.44719 1.000 20.73562 ? 248 GLU A C   1 
ATOM   2016 O O   . GLU A 1 254 ? 16.62804  2.23208   65.38223 1.000 22.17472 ? 248 GLU A O   1 
ATOM   2017 C CB  . GLU A 1 254 ? 15.80941  0.95824   68.30268 1.000 22.65387 ? 248 GLU A CB  1 
ATOM   2018 C CG  . GLU A 1 254 ? 15.59696  -0.17335  67.30660 0.700 24.71628 ? 248 GLU A CG  1 
ATOM   2019 C CD  . GLU A 1 254 ? 15.01658  -1.39942  67.95304 0.600 27.04610 ? 248 GLU A CD  1 
ATOM   2020 O OE1 . GLU A 1 254 ? 15.75497  -2.13129  68.67439 0.600 28.33836 ? 248 GLU A OE1 1 
ATOM   2021 O OE2 . GLU A 1 254 ? 13.80079  -1.57775  67.82716 0.600 27.20205 ? 248 GLU A OE2 1 
ATOM   2022 N N   . ASP A 1 255 ? 15.12334  3.44278   66.51091 1.000 19.01633 ? 249 ASP A N   1 
ATOM   2023 C CA  . ASP A 1 255 ? 14.54444  3.95986   65.29508 1.000 19.90086 ? 249 ASP A CA  1 
ATOM   2024 C C   . ASP A 1 255 ? 15.50469  4.89745   64.57800 1.000 19.51931 ? 249 ASP A C   1 
ATOM   2025 O O   . ASP A 1 255 ? 15.57081  4.88472   63.33168 1.000 20.30456 ? 249 ASP A O   1 
ATOM   2026 C CB  . ASP A 1 255 ? 13.21327  4.62899   65.61383 1.000 19.42167 ? 249 ASP A CB  1 
ATOM   2027 C CG  . ASP A 1 255 ? 12.11083  3.61224   65.90463 0.800 18.95840 ? 249 ASP A CG  1 
ATOM   2028 O OD1 . ASP A 1 255 ? 12.31916  2.38515   65.68766 0.800 17.88394 ? 249 ASP A OD1 1 
ATOM   2029 O OD2 . ASP A 1 255 ? 10.99505  4.05595   66.27478 0.800 20.48935 ? 249 ASP A OD2 1 
ATOM   2030 N N   . LEU A 1 256 ? 16.26280  5.71579   65.33629 1.000 19.34473 ? 250 LEU A N   1 
ATOM   2031 C CA  . LEU A 1 256 ? 17.32225  6.52368   64.71630 1.000 22.28043 ? 250 LEU A CA  1 
ATOM   2032 C C   . LEU A 1 256 ? 18.38531  5.66035   64.04912 1.000 23.57206 ? 250 LEU A C   1 
ATOM   2033 O O   . LEU A 1 256 ? 18.84049  5.97140   62.94304 1.000 24.15792 ? 250 LEU A O   1 
ATOM   2034 C CB  . LEU A 1 256 ? 18.00635  7.41090   65.75386 1.000 22.88995 ? 250 LEU A CB  1 
ATOM   2035 C CG  . LEU A 1 256 ? 17.15529  8.61106   66.13570 1.000 23.61495 ? 250 LEU A CG  1 
ATOM   2036 C CD1 . LEU A 1 256 ? 17.84281  9.41030   67.24557 1.000 24.27219 ? 250 LEU A CD1 1 
ATOM   2037 C CD2 . LEU A 1 256 ? 16.86552  9.52796   64.91969 1.000 25.90665 ? 250 LEU A CD2 1 
ATOM   2038 N N   . ASN A 1 257 ? 18.79160  4.58289   64.68881 1.000 24.63724 ? 251 ASN A N   1 
ATOM   2039 C CA  . ASN A 1 257 ? 19.86515  3.75292   64.10871 1.000 26.46987 ? 251 ASN A CA  1 
ATOM   2040 C C   . ASN A 1 257 ? 19.45358  3.16760   62.77035 1.000 27.53987 ? 251 ASN A C   1 
ATOM   2041 O O   . ASN A 1 257 ? 20.33116  2.87210   61.91642 1.000 29.30545 ? 251 ASN A O   1 
ATOM   2042 C CB  . ASN A 1 257 ? 20.26885  2.65228   65.07338 1.000 28.08741 ? 251 ASN A CB  1 
ATOM   2043 C CG  . ASN A 1 257 ? 21.10737  3.18272   66.20858 0.900 30.06508 ? 251 ASN A CG  1 
ATOM   2044 O OD1 . ASN A 1 257 ? 21.65902  4.28135   66.11557 0.900 30.93727 ? 251 ASN A OD1 1 
ATOM   2045 N ND2 . ASN A 1 257 ? 21.17039  2.44129   67.29652 0.900 31.06463 ? 251 ASN A ND2 1 
HETATM 2046 N N   . CME A 1 258 ? 18.13203  3.02995   62.55000 1.000 27.24325 ? 252 CME A N   1 
HETATM 2047 C CA  . CME A 1 258 ? 17.60903  2.49640   61.30756 1.000 27.41259 ? 252 CME A CA  1 
HETATM 2048 C CB  . CME A 1 258 ? 16.09950  2.06391   61.39435 1.000 29.19034 ? 252 CME A CB  1 
HETATM 2049 S SG  . CME A 1 258 ? 15.80649  0.63744   62.38724 0.700 30.66937 ? 252 CME A SG  1 
HETATM 2050 S SD  . CME A 1 258 ? 16.53551  -0.89886  61.16904 0.600 37.13114 ? 252 CME A SD  1 
HETATM 2051 C CE  . CME A 1 258 ? 15.57913  -0.89668  59.68517 0.500 36.66906 ? 252 CME A CE  1 
HETATM 2052 C CZ  . CME A 1 258 ? 15.16299  -2.28170  59.24849 0.500 36.08302 ? 252 CME A CZ  1 
HETATM 2053 O OH  . CME A 1 258 ? 14.36487  -2.78142  60.31743 0.400 37.37226 ? 252 CME A OH  1 
HETATM 2054 C C   . CME A 1 258 ? 17.76211  3.52341   60.16338 1.000 28.12931 ? 252 CME A C   1 
HETATM 2055 O O   . CME A 1 258 ? 17.65208  3.17548   58.99301 1.000 30.22901 ? 252 CME A O   1 
ATOM   2056 N N   . ILE A 1 259 ? 18.02438  4.79486   60.49386 1.000 25.31262 ? 253 ILE A N   1 
ATOM   2057 C CA  . ILE A 1 259 ? 18.25784  5.84065   59.51078 1.000 24.25949 ? 253 ILE A CA  1 
ATOM   2058 C C   . ILE A 1 259 ? 19.76855  5.99198   59.29715 1.000 25.27865 ? 253 ILE A C   1 
ATOM   2059 O O   . ILE A 1 259 ? 20.42177  6.66785   60.07666 1.000 25.93837 ? 253 ILE A O   1 
ATOM   2060 C CB  . ILE A 1 259 ? 17.63066  7.17906   59.95811 1.000 23.06407 ? 253 ILE A CB  1 
ATOM   2061 C CG1 . ILE A 1 259 ? 16.10966  7.03535   60.12327 1.000 22.60173 ? 253 ILE A CG1 1 
ATOM   2062 C CG2 . ILE A 1 259 ? 17.93940  8.27892   58.95214 1.000 22.23917 ? 253 ILE A CG2 1 
ATOM   2063 C CD1 . ILE A 1 259 ? 15.49223  8.27565   60.71014 1.000 23.16921 ? 253 ILE A CD1 1 
ATOM   2064 N N   . ILE A 1 260 ? 20.31024  5.36013   58.25999 1.000 25.22425 ? 254 ILE A N   1 
ATOM   2065 C CA  . ILE A 1 260 ? 21.75947  5.43342   58.05953 1.000 25.56021 ? 254 ILE A CA  1 
ATOM   2066 C C   . ILE A 1 260 ? 22.20377  6.75145   57.42511 1.000 23.96898 ? 254 ILE A C   1 
ATOM   2067 O O   . ILE A 1 260 ? 23.34357  7.18399   57.65216 1.000 24.95987 ? 254 ILE A O   1 
ATOM   2068 C CB  . ILE A 1 260 ? 22.22902  4.19969   57.27260 1.000 29.32240 ? 254 ILE A CB  1 
ATOM   2069 C CG1 . ILE A 1 260 ? 23.76525  3.98931   57.49211 1.000 31.74276 ? 254 ILE A CG1 1 
ATOM   2070 C CG2 . ILE A 1 260 ? 21.73630  4.25030   55.82455 1.000 31.45546 ? 254 ILE A CG2 1 
ATOM   2071 C CD1 . ILE A 1 260 ? 24.43217  2.81204   56.74894 1.000 32.85276 ? 254 ILE A CD1 1 
ATOM   2072 N N   . ASN A 1 261 ? 21.34830  7.42250   56.66369 1.000 24.01797 ? 255 ASN A N   1 
ATOM   2073 C CA  A ASN A 1 261 ? 21.71791  8.71529   56.10566 0.500 23.26933 ? 255 ASN A CA  1 
ATOM   2074 C CA  B ASN A 1 261 ? 21.67792  8.73524   56.10099 0.500 24.52114 ? 255 ASN A CA  1 
ATOM   2075 C C   . ASN A 1 261 ? 22.06562  9.72920   57.20366 1.000 23.60819 ? 255 ASN A C   1 
ATOM   2076 O O   . ASN A 1 261 ? 21.26802  10.01208  58.09601 1.000 23.17192 ? 255 ASN A O   1 
ATOM   2077 C CB  A ASN A 1 261 ? 20.57299  9.21679   55.24084 0.500 22.96170 ? 255 ASN A CB  1 
ATOM   2078 C CB  B ASN A 1 261 ? 20.45512  9.20872   55.29969 0.500 26.60859 ? 255 ASN A CB  1 
ATOM   2079 C CG  A ASN A 1 261 ? 20.92078  10.47151  54.54364 0.500 21.85002 ? 255 ASN A CG  1 
ATOM   2080 C CG  B ASN A 1 261 ? 20.54211  10.65376  54.83150 0.500 28.02898 ? 255 ASN A CG  1 
ATOM   2081 O OD1 A ASN A 1 261 ? 20.71705  11.58203  55.10390 0.500 20.62507 ? 255 ASN A OD1 1 
ATOM   2082 O OD1 B ASN A 1 261 ? 21.61351  11.26255  54.79003 0.500 28.57508 ? 255 ASN A OD1 1 
ATOM   2083 N ND2 A ASN A 1 261 ? 21.48614  10.33798  53.32292 0.500 21.43363 ? 255 ASN A ND2 1 
ATOM   2084 N ND2 B ASN A 1 261 ? 19.39259  11.19627  54.42475 0.500 28.22803 ? 255 ASN A ND2 1 
ATOM   2085 N N   . LEU A 1 262 ? 23.27660  10.28311  57.12588 1.000 24.02557 ? 256 LEU A N   1 
ATOM   2086 C CA  . LEU A 1 262 ? 23.83297  11.11677  58.19934 1.000 24.87315 ? 256 LEU A CA  1 
ATOM   2087 C C   . LEU A 1 262 ? 23.11436  12.45522  58.29445 1.000 22.68690 ? 256 LEU A C   1 
ATOM   2088 O O   . LEU A 1 262 ? 22.89308  12.98289  59.39623 1.000 23.06153 ? 256 LEU A O   1 
ATOM   2089 C CB  . LEU A 1 262 ? 25.32240  11.31208  57.90055 1.000 27.45466 ? 256 LEU A CB  1 
ATOM   2090 C CG  . LEU A 1 262 ? 26.23987  10.43393  58.68261 1.000 28.61026 ? 256 LEU A CG  1 
ATOM   2091 C CD1 . LEU A 1 262 ? 27.61113  10.88705  58.26235 1.000 31.03610 ? 256 LEU A CD1 1 
ATOM   2092 C CD2 . LEU A 1 262 ? 26.07724  10.48896  60.27302 1.000 26.70306 ? 256 LEU A CD2 1 
ATOM   2093 N N   . LYS A 1 263 ? 22.81583  13.07692  57.15611 1.000 22.01867 ? 257 LYS A N   1 
ATOM   2094 C CA  . LYS A 1 263 ? 22.10604  14.34826  57.22747 1.000 22.22353 ? 257 LYS A CA  1 
ATOM   2095 C C   . LYS A 1 263 ? 20.75801  14.18939  57.92102 1.000 20.54968 ? 257 LYS A C   1 
ATOM   2096 O O   . LYS A 1 263 ? 20.39708  15.01129  58.76389 1.000 21.10018 ? 257 LYS A O   1 
ATOM   2097 C CB  . LYS A 1 263 ? 21.94012  14.95201  55.83751 1.000 24.33755 ? 257 LYS A CB  1 
ATOM   2098 C CG  . LYS A 1 263 ? 23.14253  15.73501  55.41692 0.900 27.04174 ? 257 LYS A CG  1 
ATOM   2099 C CD  . LYS A 1 263 ? 22.95359  16.43310  54.04808 0.900 28.01536 ? 257 LYS A CD  1 
ATOM   2100 C CE  . LYS A 1 263 ? 24.09819  17.42494  53.83993 0.600 28.09469 ? 257 LYS A CE  1 
ATOM   2101 N NZ  . LYS A 1 263 ? 24.00777  18.14268  52.52886 0.600 28.55986 ? 257 LYS A NZ  1 
ATOM   2102 N N   . ALA A 1 264 ? 20.01733  13.13239  57.59348 1.000 18.85888 ? 258 ALA A N   1 
ATOM   2103 C CA  . ALA A 1 264 ? 18.71288  12.95276  58.21821 1.000 18.43165 ? 258 ALA A CA  1 
ATOM   2104 C C   . ALA A 1 264 ? 18.85499  12.62507  59.69307 1.000 18.45554 ? 258 ALA A C   1 
ATOM   2105 O O   . ALA A 1 264 ? 18.13506  13.18373  60.53764 1.000 17.72401 ? 258 ALA A O   1 
ATOM   2106 C CB  . ALA A 1 264 ? 17.93328  11.84460  57.52076 1.000 18.24689 ? 258 ALA A CB  1 
ATOM   2107 N N   . ARG A 1 265 ? 19.76540  11.69248  60.01853 1.000 17.84238 ? 259 ARG A N   1 
ATOM   2108 C CA  . ARG A 1 265 ? 19.91051  11.29309  61.42081 1.000 17.82097 ? 259 ARG A CA  1 
ATOM   2109 C C   . ARG A 1 265 ? 20.40186  12.46508  62.27618 1.000 16.70207 ? 259 ARG A C   1 
ATOM   2110 O O   . ARG A 1 265 ? 19.85823  12.71377  63.37467 1.000 16.66585 ? 259 ARG A O   1 
ATOM   2111 C CB  . ARG A 1 265 ? 20.87701  10.09431  61.55527 0.900 18.60546 ? 259 ARG A CB  1 
ATOM   2112 C CG  . ARG A 1 265 ? 20.73376  9.51308   62.97860 0.800 19.65832 ? 259 ARG A CG  1 
ATOM   2113 C CD  . ARG A 1 265 ? 21.88227  8.65425   63.33174 0.800 19.75310 ? 259 ARG A CD  1 
ATOM   2114 N NE  . ARG A 1 265 ? 21.83524  7.43715   62.53708 0.800 20.79849 ? 259 ARG A NE  1 
ATOM   2115 C CZ  . ARG A 1 265 ? 22.58089  6.38207   62.77255 0.700 21.38036 ? 259 ARG A CZ  1 
ATOM   2116 N NH1 . ARG A 1 265 ? 23.51353  6.39676   63.71833 0.700 21.97681 ? 259 ARG A NH1 1 
ATOM   2117 N NH2 . ARG A 1 265 ? 22.39849  5.29220   62.03772 0.700 20.90358 ? 259 ARG A NH2 1 
ATOM   2118 N N   . ASN A 1 266 ? 21.40075  13.23712  61.78678 1.000 17.49932 ? 260 ASN A N   1 
ATOM   2119 C CA  . ASN A 1 266 ? 21.89176  14.35181  62.59965 1.000 17.11315 ? 260 ASN A CA  1 
ATOM   2120 C C   . ASN A 1 266 ? 20.87760  15.47180  62.72008 1.000 16.69609 ? 260 ASN A C   1 
ATOM   2121 O O   . ASN A 1 266 ? 20.90047  16.20033  63.72528 1.000 17.17401 ? 260 ASN A O   1 
ATOM   2122 C CB  . ASN A 1 266 ? 23.20043  14.90798  62.02420 1.000 17.57969 ? 260 ASN A CB  1 
ATOM   2123 C CG  . ASN A 1 266 ? 24.38110  14.01091  62.33583 1.000 19.36587 ? 260 ASN A CG  1 
ATOM   2124 O OD1 . ASN A 1 266 ? 24.33624  13.19726  63.26505 1.000 21.25528 ? 260 ASN A OD1 1 
ATOM   2125 N ND2 . ASN A 1 266 ? 25.40634  14.11293  61.52516 1.000 18.22631 ? 260 ASN A ND2 1 
ATOM   2126 N N   . TYR A 1 267 ? 19.99295  15.65063  61.72865 1.000 15.86778 ? 261 TYR A N   1 
ATOM   2127 C CA  . TYR A 1 267 ? 18.89916  16.60304  61.92445 1.000 16.00996 ? 261 TYR A CA  1 
ATOM   2128 C C   . TYR A 1 267 ? 18.06353  16.19565  63.13843 1.000 16.04080 ? 261 TYR A C   1 
ATOM   2129 O O   . TYR A 1 267 ? 17.81552  17.00506  64.06089 1.000 16.60062 ? 261 TYR A O   1 
ATOM   2130 C CB  . TYR A 1 267 ? 18.00189  16.70873  60.66298 1.000 16.15273 ? 261 TYR A CB  1 
ATOM   2131 C CG  . TYR A 1 267 ? 16.82495  17.58063  60.96355 1.000 16.34248 ? 261 TYR A CG  1 
ATOM   2132 C CD1 . TYR A 1 267 ? 17.01933  18.96206  61.16404 1.000 17.62725 ? 261 TYR A CD1 1 
ATOM   2133 C CD2 . TYR A 1 267 ? 15.52533  17.05357  61.13691 1.000 16.44766 ? 261 TYR A CD2 1 
ATOM   2134 C CE1 . TYR A 1 267 ? 15.98260  19.78689  61.52479 1.000 18.66422 ? 261 TYR A CE1 1 
ATOM   2135 C CE2 . TYR A 1 267 ? 14.47610  17.87613  61.50484 1.000 17.24488 ? 261 TYR A CE2 1 
ATOM   2136 C CZ  . TYR A 1 267 ? 14.71536  19.23518  61.69218 1.000 17.90523 ? 261 TYR A CZ  1 
ATOM   2137 O OH  . TYR A 1 267 ? 13.71543  20.10863  62.03228 1.000 19.21508 ? 261 TYR A OH  1 
ATOM   2138 N N   . LEU A 1 268 ? 17.64919  14.92862  63.18226 1.000 14.68363 ? 262 LEU A N   1 
ATOM   2139 C CA  . LEU A 1 268 ? 16.82888  14.50547  64.32073 1.000 14.37347 ? 262 LEU A CA  1 
ATOM   2140 C C   . LEU A 1 268 ? 17.60662  14.60660  65.63647 1.000 13.96513 ? 262 LEU A C   1 
ATOM   2141 O O   . LEU A 1 268 ? 17.04434  14.99004  66.68059 1.000 14.71046 ? 262 LEU A O   1 
ATOM   2142 C CB  . LEU A 1 268 ? 16.33997  13.07586  64.06144 1.000 14.73521 ? 262 LEU A CB  1 
ATOM   2143 C CG  . LEU A 1 268 ? 15.42321  12.93608  62.86848 1.000 16.18956 ? 262 LEU A CG  1 
ATOM   2144 C CD1 . LEU A 1 268 ? 15.25166  11.41392  62.50648 1.000 17.52937 ? 262 LEU A CD1 1 
ATOM   2145 C CD2 . LEU A 1 268 ? 14.05958  13.67108  63.14643 1.000 17.98590 ? 262 LEU A CD2 1 
ATOM   2146 N N   . LEU A 1 269 ? 18.91091  14.27343  65.61534 1.000 14.06335 ? 263 LEU A N   1 
ATOM   2147 C CA  . LEU A 1 269 ? 19.68149  14.33602  66.86325 1.000 14.55279 ? 263 LEU A CA  1 
ATOM   2148 C C   . LEU A 1 269 ? 19.87609  15.77129  67.37194 1.000 16.40131 ? 263 LEU A C   1 
ATOM   2149 O O   . LEU A 1 269 ? 20.14594  15.98840  68.58562 1.000 17.88925 ? 263 LEU A O   1 
ATOM   2150 C CB  . LEU A 1 269 ? 21.04910  13.71245  66.62231 1.000 15.13150 ? 263 LEU A CB  1 
ATOM   2151 C CG  . LEU A 1 269 ? 21.07111  12.19911  66.48884 1.000 15.47728 ? 263 LEU A CG  1 
ATOM   2152 C CD1 . LEU A 1 269 ? 22.51882  11.75596  66.08931 1.000 17.19713 ? 263 LEU A CD1 1 
ATOM   2153 C CD2 . LEU A 1 269 ? 20.68724  11.51912  67.83747 1.000 16.94411 ? 263 LEU A CD2 1 
ATOM   2154 N N   . SER A 1 270 ? 19.77108  16.75295  66.46995 1.000 16.64675 ? 264 SER A N   1 
ATOM   2155 C CA  . SER A 1 270 ? 19.94608  18.15606  66.80744 1.000 17.09828 ? 264 SER A CA  1 
ATOM   2156 C C   . SER A 1 270 ? 18.74267  18.76335  67.53623 1.000 17.71077 ? 264 SER A C   1 
ATOM   2157 O O   . SER A 1 270 ? 18.86091  19.88427  68.08193 1.000 19.07327 ? 264 SER A O   1 
ATOM   2158 C CB  . SER A 1 270 ? 20.22109  18.98005  65.53374 1.000 18.61219 ? 264 SER A CB  1 
ATOM   2159 O OG  . SER A 1 270 ? 19.00568  19.27748  64.79307 1.000 19.01825 ? 264 SER A OG  1 
ATOM   2160 N N   . LEU A 1 271 ? 17.55591  18.05802  67.55964 1.000 16.70002 ? 265 LEU A N   1 
ATOM   2161 C CA  . LEU A 1 271 ? 16.31910  18.61837  68.11828 1.000 17.60713 ? 265 LEU A CA  1 
ATOM   2162 C C   . LEU A 1 271 ? 16.27737  18.40020  69.62696 1.000 17.58650 ? 265 LEU A C   1 
ATOM   2163 O O   . LEU A 1 271 ? 16.79492  17.39455  70.13485 1.000 18.18348 ? 265 LEU A O   1 
ATOM   2164 C CB  . LEU A 1 271 ? 15.08058  17.95156  67.47728 1.000 15.99349 ? 265 LEU A CB  1 
ATOM   2165 C CG  . LEU A 1 271 ? 14.97565  18.11451  65.93730 1.000 17.38870 ? 265 LEU A CG  1 
ATOM   2166 C CD1 . LEU A 1 271 ? 13.79652  17.28494  65.34682 1.000 18.03083 ? 265 LEU A CD1 1 
ATOM   2167 C CD2 . LEU A 1 271 ? 14.75829  19.60500  65.62459 1.000 18.88179 ? 265 LEU A CD2 1 
ATOM   2168 N N   . PRO A 1 272 ? 15.69531  19.34085  70.35941 1.000 18.02838 ? 266 PRO A N   1 
ATOM   2169 C CA  . PRO A 1 272 ? 15.46409  19.10324  71.78276 1.000 18.17461 ? 266 PRO A CA  1 
ATOM   2170 C C   . PRO A 1 272 ? 14.51300  17.92001  71.95755 1.000 19.66888 ? 266 PRO A C   1 
ATOM   2171 O O   . PRO A 1 272 ? 13.71419  17.59275  71.06183 1.000 21.72483 ? 266 PRO A O   1 
ATOM   2172 C CB  . PRO A 1 272 ? 14.82081  20.41771  72.27588 1.000 20.20124 ? 266 PRO A CB  1 
ATOM   2173 C CG  . PRO A 1 272 ? 15.12509  21.42766  71.19947 1.000 21.24339 ? 266 PRO A CG  1 
ATOM   2174 C CD  . PRO A 1 272 ? 15.21688  20.66150  69.89210 1.000 18.41905 ? 266 PRO A CD  1 
ATOM   2175 N N   . HIS A 1 273 ? 14.59460  17.27213  73.12307 1.000 19.47420 ? 267 HIS A N   1 
ATOM   2176 C CA  . HIS A 1 273 ? 13.67687  16.18358  73.43018 1.000 20.48229 ? 267 HIS A CA  1 
ATOM   2177 C C   . HIS A 1 273 ? 12.22156  16.65568  73.42662 1.000 21.48614 ? 267 HIS A C   1 
ATOM   2178 O O   . HIS A 1 273 ? 11.90424  17.70234  74.00889 1.000 23.87179 ? 267 HIS A O   1 
ATOM   2179 C CB  . HIS A 1 273 ? 13.98874  15.64790  74.83255 0.800 20.39605 ? 267 HIS A CB  1 
ATOM   2180 C CG  . HIS A 1 273 ? 13.09322  14.52476  75.22415 0.600 20.99315 ? 267 HIS A CG  1 
ATOM   2181 N ND1 . HIS A 1 273 ? 13.08600  13.32146  74.55869 0.600 20.85649 ? 267 HIS A ND1 1 
ATOM   2182 C CD2 . HIS A 1 273 ? 12.05417  14.48026  76.08410 0.600 22.95660 ? 267 HIS A CD2 1 
ATOM   2183 C CE1 . HIS A 1 273 ? 12.15656  12.53952  75.06765 0.600 20.57802 ? 267 HIS A CE1 1 
ATOM   2184 N NE2 . HIS A 1 273 ? 11.49953  13.22396  75.98283 0.600 22.92702 ? 267 HIS A NE2 1 
ATOM   2185 N N   . LYS A 1 274 ? 11.33689  15.85956  72.79926 1.000 20.22180 ? 268 LYS A N   1 
ATOM   2186 C CA  . LYS A 1 274 ? 9.88347   16.04188  72.77651 1.000 21.98595 ? 268 LYS A CA  1 
ATOM   2187 C C   . LYS A 1 274 ? 9.21652   14.78472  73.32567 1.000 23.30243 ? 268 LYS A C   1 
ATOM   2188 O O   . LYS A 1 274 ? 9.51177   13.67498  72.86509 1.000 22.84531 ? 268 LYS A O   1 
ATOM   2189 C CB  . LYS A 1 274 ? 9.34835   16.26783  71.34403 0.900 21.80583 ? 268 LYS A CB  1 
ATOM   2190 C CG  . LYS A 1 274 ? 10.01918  17.38463  70.52346 0.800 23.15632 ? 268 LYS A CG  1 
ATOM   2191 C CD  . LYS A 1 274 ? 9.68656   17.30739  68.98587 0.700 23.82817 ? 268 LYS A CD  1 
ATOM   2192 C CE  . LYS A 1 274 ? 10.62138  18.18403  68.14875 0.600 24.46749 ? 268 LYS A CE  1 
ATOM   2193 N NZ  . LYS A 1 274 ? 10.32163  19.64346  68.35689 0.500 24.18680 ? 268 LYS A NZ  1 
ATOM   2194 N N   . ASN A 1 275 ? 8.25762   14.95826  74.24794 1.000 23.81287 ? 269 ASN A N   1 
ATOM   2195 C CA  . ASN A 1 275 ? 7.46769   13.83588  74.73495 1.000 24.97680 ? 269 ASN A CA  1 
ATOM   2196 C C   . ASN A 1 275 ? 6.31636   13.50720  73.80899 1.000 23.83589 ? 269 ASN A C   1 
ATOM   2197 O O   . ASN A 1 275 ? 5.77605   14.37510  73.12382 1.000 24.95857 ? 269 ASN A O   1 
ATOM   2198 C CB  . ASN A 1 275 ? 6.83787   14.12790  76.08563 0.800 25.79117 ? 269 ASN A CB  1 
ATOM   2199 C CG  . ASN A 1 275 ? 7.82281   14.66576  77.03334 0.600 27.02334 ? 269 ASN A CG  1 
ATOM   2200 O OD1 . ASN A 1 275 ? 7.75097   15.83994  77.38222 0.600 29.27977 ? 269 ASN A OD1 1 
ATOM   2201 N ND2 . ASN A 1 275 ? 8.80974   13.85265  77.40005 0.600 26.30760 ? 269 ASN A ND2 1 
ATOM   2202 N N   . LYS A 1 276 ? 5.95931   12.22806  73.81379 1.000 23.74029 ? 270 LYS A N   1 
ATOM   2203 C CA  . LYS A 1 276 ? 4.76113   11.74942  73.15584 1.000 24.10391 ? 270 LYS A CA  1 
ATOM   2204 C C   . LYS A 1 276 ? 3.51197   12.36151  73.80620 1.000 23.36831 ? 270 LYS A C   1 
ATOM   2205 O O   . LYS A 1 276 ? 3.43277   12.50111  75.03586 1.000 24.57262 ? 270 LYS A O   1 
ATOM   2206 C CB  . LYS A 1 276 ? 4.74614   10.21894  73.23690 1.000 26.40778 ? 270 LYS A CB  1 
ATOM   2207 C CG  . LYS A 1 276 ? 3.55873   9.54406   72.48104 1.000 29.37212 ? 270 LYS A CG  1 
ATOM   2208 C CD  . LYS A 1 276 ? 3.66680   8.01747   72.48488 1.000 31.62947 ? 270 LYS A CD  1 
ATOM   2209 C CE  . LYS A 1 276 ? 2.50020   7.36718   71.65060 1.000 33.74170 ? 270 LYS A CE  1 
ATOM   2210 N NZ  . LYS A 1 276 ? 2.50575   7.73057   70.11616 1.000 33.98034 ? 270 LYS A NZ  1 
ATOM   2211 N N   . VAL A 1 277 ? 2.54778   12.75209  72.97429 1.000 22.72945 ? 271 VAL A N   1 
ATOM   2212 C CA  . VAL A 1 277 ? 1.23596   13.20338  73.44158 1.000 22.86643 ? 271 VAL A CA  1 
ATOM   2213 C C   . VAL A 1 277 ? 0.31511   11.98811  73.41031 1.000 23.03112 ? 271 VAL A C   1 
ATOM   2214 O O   . VAL A 1 277 ? 0.11039   11.42782  72.34418 1.000 23.84917 ? 271 VAL A O   1 
ATOM   2215 C CB  . VAL A 1 277 ? 0.66838   14.33973  72.56769 1.000 24.15704 ? 271 VAL A CB  1 
ATOM   2216 C CG1 . VAL A 1 277 ? -0.78566  14.68779  72.97201 1.000 24.90588 ? 271 VAL A CG1 1 
ATOM   2217 C CG2 . VAL A 1 277 ? 1.57736   15.62783  72.56024 1.000 25.27491 ? 271 VAL A CG2 1 
ATOM   2218 N N   . PRO A 1 278 ? -0.25634  11.56978  74.52516 1.000 23.39690 ? 272 PRO A N   1 
ATOM   2219 C CA  . PRO A 1 278 ? -1.08971  10.35536  74.53372 1.000 23.27728 ? 272 PRO A CA  1 
ATOM   2220 C C   . PRO A 1 278 ? -2.29128  10.49197  73.62372 1.000 22.84020 ? 272 PRO A C   1 
ATOM   2221 O O   . PRO A 1 278 ? -2.97534  11.51610  73.63571 1.000 23.97829 ? 272 PRO A O   1 
ATOM   2222 C CB  . PRO A 1 278 ? -1.55671  10.25682  75.99051 1.000 25.09688 ? 272 PRO A CB  1 
ATOM   2223 C CG  . PRO A 1 278 ? -0.56432  10.97625  76.77799 1.000 25.53231 ? 272 PRO A CG  1 
ATOM   2224 C CD  . PRO A 1 278 ? -0.10141  12.14560  75.87936 1.000 24.50109 ? 272 PRO A CD  1 
ATOM   2225 N N   . TRP A 1 279 ? -2.60335  9.42194   72.89273 1.000 22.13172 ? 273 TRP A N   1 
ATOM   2226 C CA  . TRP A 1 279 ? -3.74719  9.50252   71.96493 1.000 22.10584 ? 273 TRP A CA  1 
ATOM   2227 C C   . TRP A 1 279 ? -5.06254  9.79839   72.69788 1.000 24.00466 ? 273 TRP A C   1 
ATOM   2228 O O   . TRP A 1 279 ? -5.91483  10.50495  72.15825 1.000 24.26813 ? 273 TRP A O   1 
ATOM   2229 C CB  . TRP A 1 279 ? -3.91073  8.20496   71.17209 1.000 22.84515 ? 273 TRP A CB  1 
ATOM   2230 C CG  . TRP A 1 279 ? -2.72362  7.88639   70.31082 1.000 21.69571 ? 273 TRP A CG  1 
ATOM   2231 C CD1 . TRP A 1 279 ? -1.84640  6.82608   70.45033 1.000 21.44522 ? 273 TRP A CD1 1 
ATOM   2232 C CD2 . TRP A 1 279 ? -2.26880  8.63763   69.15843 1.000 20.73211 ? 273 TRP A CD2 1 
ATOM   2233 N NE1 . TRP A 1 279 ? -0.89843  6.87639   69.44944 1.000 21.69903 ? 273 TRP A NE1 1 
ATOM   2234 C CE2 . TRP A 1 279 ? -1.12675  7.97530   68.65306 1.000 20.80061 ? 273 TRP A CE2 1 
ATOM   2235 C CE3 . TRP A 1 279 ? -2.72378  9.78895   68.51580 1.000 20.57451 ? 273 TRP A CE3 1 
ATOM   2236 C CZ2 . TRP A 1 279 ? -0.41582  8.44428   67.52254 1.000 20.96683 ? 273 TRP A CZ2 1 
ATOM   2237 C CZ3 . TRP A 1 279 ? -2.01212  10.26040  67.38442 1.000 21.25294 ? 273 TRP A CZ3 1 
ATOM   2238 C CH2 . TRP A 1 279 ? -0.88643  9.58404   66.90101 1.000 21.35837 ? 273 TRP A CH2 1 
ATOM   2239 N N   . ASN A 1 280 ? -5.24216  9.29598   73.94055 1.000 25.32477 ? 274 ASN A N   1 
ATOM   2240 C CA  . ASN A 1 280 ? -6.52597  9.52320   74.59451 1.000 26.93741 ? 274 ASN A CA  1 
ATOM   2241 C C   . ASN A 1 280 ? -6.63019  10.91704  75.18554 1.000 27.07877 ? 274 ASN A C   1 
ATOM   2242 O O   . ASN A 1 280 ? -7.73412  11.37288  75.49967 1.000 27.27915 ? 274 ASN A O   1 
ATOM   2243 C CB  . ASN A 1 280 ? -6.75414  8.42676   75.62928 1.000 30.29578 ? 274 ASN A CB  1 
ATOM   2244 C CG  . ASN A 1 280 ? -5.99839  8.64730   76.89407 1.000 34.01283 ? 274 ASN A CG  1 
ATOM   2245 O OD1 . ASN A 1 280 ? -4.88677  9.16576   76.88621 1.000 35.20794 ? 274 ASN A OD1 1 
ATOM   2246 N ND2 . ASN A 1 280 ? -6.58304  8.19562   78.01512 1.000 36.77474 ? 274 ASN A ND2 1 
ATOM   2247 N N   . ARG A 1 281 ? -5.52759  11.63960  75.26297 1.000 26.99375 ? 275 ARG A N   1 
ATOM   2248 C CA  . ARG A 1 281 ? -5.59339  13.05945  75.57564 1.000 28.63355 ? 275 ARG A CA  1 
ATOM   2249 C C   . ARG A 1 281 ? -5.96902  13.88782  74.34649 1.000 28.33751 ? 275 ARG A C   1 
ATOM   2250 O O   . ARG A 1 281 ? -6.73804  14.85105  74.46068 1.000 29.10946 ? 275 ARG A O   1 
ATOM   2251 C CB  . ARG A 1 281 ? -4.25029  13.52536  76.15898 1.000 30.46029 ? 275 ARG A CB  1 
ATOM   2252 C CG  . ARG A 1 281 ? -4.32219  14.79004  76.93889 0.700 33.29664 ? 275 ARG A CG  1 
ATOM   2253 C CD  . ARG A 1 281 ? -3.20268  14.85048  77.99696 0.700 35.80680 ? 275 ARG A CD  1 
ATOM   2254 N NE  . ARG A 1 281 ? -1.98427  15.31696  77.35222 0.700 37.67269 ? 275 ARG A NE  1 
ATOM   2255 C CZ  . ARG A 1 281 ? -0.76978  15.31072  77.88461 0.700 37.93617 ? 275 ARG A CZ  1 
ATOM   2256 N NH1 . ARG A 1 281 ? -0.55772  14.88781  79.12146 0.700 38.37793 ? 275 ARG A NH1 1 
ATOM   2257 N NH2 . ARG A 1 281 ? 0.25408   15.73890  77.15126 0.700 38.04539 ? 275 ARG A NH2 1 
ATOM   2258 N N   . LEU A 1 282 ? -5.45888  13.51228  73.15464 1.000 26.59069 ? 276 LEU A N   1 
ATOM   2259 C CA  . LEU A 1 282 ? -5.83786  14.19235  71.92587 1.000 27.71482 ? 276 LEU A CA  1 
ATOM   2260 C C   . LEU A 1 282 ? -7.25056  13.87443  71.51681 1.000 27.64899 ? 276 LEU A C   1 
ATOM   2261 O O   . LEU A 1 282 ? -7.88605  14.69347  70.82885 1.000 29.26378 ? 276 LEU A O   1 
ATOM   2262 C CB  . LEU A 1 282 ? -4.93194  13.76102  70.76859 1.000 30.06805 ? 276 LEU A CB  1 
ATOM   2263 C CG  . LEU A 1 282 ? -3.55670  14.39546  70.61504 1.000 32.81405 ? 276 LEU A CG  1 
ATOM   2264 C CD1 . LEU A 1 282 ? -2.85124  13.69659  69.48643 1.000 34.43443 ? 276 LEU A CD1 1 
ATOM   2265 C CD2 . LEU A 1 282 ? -3.56521  15.94319  70.39639 1.000 33.38200 ? 276 LEU A CD2 1 
ATOM   2266 N N   . PHE A 1 283 ? -7.73018  12.66204  71.85390 1.000 24.97845 ? 277 PHE A N   1 
ATOM   2267 C CA  . PHE A 1 283 ? -9.02903  12.14801  71.37728 1.000 24.15011 ? 277 PHE A CA  1 
ATOM   2268 C C   . PHE A 1 283 ? -9.78218  11.54709  72.55226 1.000 25.09039 ? 277 PHE A C   1 
ATOM   2269 O O   . PHE A 1 283 ? -9.96552  10.33572  72.64356 1.000 25.25431 ? 277 PHE A O   1 
ATOM   2270 C CB  . PHE A 1 283 ? -8.86104  11.10912  70.25241 1.000 22.74640 ? 277 PHE A CB  1 
ATOM   2271 C CG  . PHE A 1 283 ? -8.06804  11.60735  69.05313 1.000 22.75347 ? 277 PHE A CG  1 
ATOM   2272 C CD1 . PHE A 1 283 ? -8.60242  12.54646  68.17632 1.000 23.98613 ? 277 PHE A CD1 1 
ATOM   2273 C CD2 . PHE A 1 283 ? -6.81634  11.12691  68.80048 1.000 21.52256 ? 277 PHE A CD2 1 
ATOM   2274 C CE1 . PHE A 1 283 ? -7.86127  12.97839  67.04884 1.000 23.43144 ? 277 PHE A CE1 1 
ATOM   2275 C CE2 . PHE A 1 283 ? -6.06620  11.56766  67.68738 1.000 21.84571 ? 277 PHE A CE2 1 
ATOM   2276 C CZ  . PHE A 1 283 ? -6.55679  12.49622  66.83961 1.000 22.04798 ? 277 PHE A CZ  1 
ATOM   2277 N N   . PRO A 1 284 ? -10.26458 12.37487  73.46235 1.000 26.95393 ? 278 PRO A N   1 
ATOM   2278 C CA  . PRO A 1 284 ? -10.80746 11.81967  74.71121 1.000 28.20473 ? 278 PRO A CA  1 
ATOM   2279 C C   . PRO A 1 284 ? -12.16177 11.09718  74.54309 1.000 29.48508 ? 278 PRO A C   1 
ATOM   2280 O O   . PRO A 1 284 ? -12.53227 10.29041  75.41405 1.000 31.00818 ? 278 PRO A O   1 
ATOM   2281 C CB  . PRO A 1 284 ? -10.90620 13.04767  75.62517 1.000 29.53205 ? 278 PRO A CB  1 
ATOM   2282 C CG  . PRO A 1 284 ? -10.96326 14.23835  74.70812 1.000 29.34225 ? 278 PRO A CG  1 
ATOM   2283 C CD  . PRO A 1 284 ? -10.21109 13.85219  73.44698 1.000 29.00356 ? 278 PRO A CD  1 
ATOM   2284 N N   . ASN A 1 285 ? -12.87544 11.27612  73.42965 1.000 28.39073 ? 279 ASN A N   1 
ATOM   2285 C CA  . ASN A 1 285 ? -14.15346 10.56903  73.23628 1.000 30.13013 ? 279 ASN A CA  1 
ATOM   2286 C C   . ASN A 1 285 ? -14.00487 9.35674   72.30134 1.000 28.73496 ? 279 ASN A C   1 
ATOM   2287 O O   . ASN A 1 285 ? -15.00556 8.66493   72.02835 1.000 29.98582 ? 279 ASN A O   1 
ATOM   2288 C CB  . ASN A 1 285 ? -15.24339 11.53407  72.69551 0.800 32.26870 ? 279 ASN A CB  1 
ATOM   2289 C CG  . ASN A 1 285 ? -16.68281 10.99804  72.86131 0.700 35.63614 ? 279 ASN A CG  1 
ATOM   2290 O OD1 . ASN A 1 285 ? -16.99728 10.18971  73.76657 0.600 36.90952 ? 279 ASN A OD1 1 
ATOM   2291 N ND2 . ASN A 1 285 ? -17.57359 11.46690  71.98254 0.600 35.67613 ? 279 ASN A ND2 1 
ATOM   2292 N N   . ALA A 1 286 ? -12.77337 9.04090   71.86805 1.000 26.63220 ? 280 ALA A N   1 
ATOM   2293 C CA  . ALA A 1 286 ? -12.58330 7.95640   70.92548 1.000 25.41599 ? 280 ALA A CA  1 
ATOM   2294 C C   . ALA A 1 286 ? -12.65889 6.58716   71.59875 1.000 25.12940 ? 280 ALA A C   1 
ATOM   2295 O O   . ALA A 1 286 ? -12.32538 6.41951   72.77678 1.000 25.18312 ? 280 ALA A O   1 
ATOM   2296 C CB  . ALA A 1 286 ? -11.22094 8.09182   70.21570 1.000 24.49389 ? 280 ALA A CB  1 
ATOM   2297 N N   . ASP A 1 287 ? -13.08127 5.60775   70.81445 1.000 24.10782 ? 281 ASP A N   1 
ATOM   2298 C CA  . ASP A 1 287 ? -13.02548 4.19659   71.17517 1.000 23.34197 ? 281 ASP A CA  1 
ATOM   2299 C C   . ASP A 1 287 ? -11.57652 3.77043   71.43417 1.000 22.13818 ? 281 ASP A C   1 
ATOM   2300 O O   . ASP A 1 287 ? -10.68699 4.04927   70.63367 1.000 21.77671 ? 281 ASP A O   1 
ATOM   2301 C CB  . ASP A 1 287 ? -13.60452 3.37479   70.01512 0.800 22.81853 ? 281 ASP A CB  1 
ATOM   2302 C CG  . ASP A 1 287 ? -13.72061 1.92479   70.32748 0.700 25.05092 ? 281 ASP A CG  1 
ATOM   2303 O OD1 . ASP A 1 287 ? -12.71250 1.22270   70.34175 0.600 26.13534 ? 281 ASP A OD1 1 
ATOM   2304 O OD2 . ASP A 1 287 ? -14.84347 1.42923   70.41422 0.600 28.00499 ? 281 ASP A OD2 1 
ATOM   2305 N N   . SER A 1 288 ? -11.32871 3.10131   72.56022 1.000 22.95363 ? 282 SER A N   1 
ATOM   2306 C CA  . SER A 1 288 ? -9.95684  2.77363   72.90136 1.000 22.67336 ? 282 SER A CA  1 
ATOM   2307 C C   . SER A 1 288 ? -9.33995  1.81244   71.88312 1.000 20.67497 ? 282 SER A C   1 
ATOM   2308 O O   . SER A 1 288 ? -8.11934  1.87066   71.63877 1.000 20.57054 ? 282 SER A O   1 
ATOM   2309 C CB  . SER A 1 288 ? -9.88605  2.19849   74.32524 1.000 25.91581 ? 282 SER A CB  1 
ATOM   2310 O OG  . SER A 1 288 ? -10.56408 0.95003   74.39956 1.000 28.73346 ? 282 SER A OG  1 
ATOM   2311 N N   . LYS A 1 289 ? -10.14872 0.92828   71.27768 1.000 19.94520 ? 283 LYS A N   1 
ATOM   2312 C CA  . LYS A 1 289 ? -9.60232  0.03302   70.25306 1.000 19.67183 ? 283 LYS A CA  1 
ATOM   2313 C C   . LYS A 1 289 ? -9.25263  0.80148   69.00044 1.000 18.63482 ? 283 LYS A C   1 
ATOM   2314 O O   . LYS A 1 289 ? -8.25629  0.46289   68.33735 1.000 18.70889 ? 283 LYS A O   1 
ATOM   2315 C CB  . LYS A 1 289 ? -10.56728 -1.10271  69.90578 1.000 19.75276 ? 283 LYS A CB  1 
ATOM   2316 C CG  . LYS A 1 289 ? -10.93496 -1.98535  71.06911 1.000 22.15004 ? 283 LYS A CG  1 
ATOM   2317 C CD  . LYS A 1 289 ? -11.91497 -3.10967  70.65743 1.000 24.99595 ? 283 LYS A CD  1 
ATOM   2318 C CE  . LYS A 1 289 ? -12.33715 -3.85491  71.92148 0.800 27.02762 ? 283 LYS A CE  1 
ATOM   2319 N NZ  . LYS A 1 289 ? -13.31735 -4.98328  71.73077 0.700 28.80477 ? 283 LYS A NZ  1 
ATOM   2320 N N   . ALA A 1 290 ? -10.02535 1.86556   68.67672 1.000 17.26818 ? 284 ALA A N   1 
ATOM   2321 C CA  . ALA A 1 290 ? -9.64257  2.71928   67.55346 1.000 16.64682 ? 284 ALA A CA  1 
ATOM   2322 C C   . ALA A 1 290 ? -8.27757  3.37172   67.77717 1.000 16.70917 ? 284 ALA A C   1 
ATOM   2323 O O   . ALA A 1 290 ? -7.47555  3.48372   66.82981 1.000 16.85350 ? 284 ALA A O   1 
ATOM   2324 C CB  . ALA A 1 290 ? -10.69648 3.80178   67.28944 1.000 16.23961 ? 284 ALA A CB  1 
ATOM   2325 N N   . LEU A 1 291 ? -8.01898  3.86106   69.00267 1.000 16.89465 ? 285 LEU A N   1 
ATOM   2326 C CA  . LEU A 1 291 ? -6.74650  4.52937   69.26897 1.000 16.48179 ? 285 LEU A CA  1 
ATOM   2327 C C   . LEU A 1 291 ? -5.57967  3.56613   69.25440 1.000 17.12558 ? 285 LEU A C   1 
ATOM   2328 O O   . LEU A 1 291 ? -4.43793  3.97534   68.96013 1.000 18.06125 ? 285 LEU A O   1 
ATOM   2329 C CB  . LEU A 1 291 ? -6.80557  5.26587   70.61132 1.000 17.71207 ? 285 LEU A CB  1 
ATOM   2330 C CG  . LEU A 1 291 ? -7.85787  6.35437   70.67961 1.000 18.46604 ? 285 LEU A CG  1 
ATOM   2331 C CD1 . LEU A 1 291 ? -7.81649  7.00398   72.05579 1.000 18.38114 ? 285 LEU A CD1 1 
ATOM   2332 C CD2 . LEU A 1 291 ? -7.62850  7.34739   69.55251 1.000 19.29831 ? 285 LEU A CD2 1 
ATOM   2333 N N   . ASP A 1 292 ? -5.80755  2.30932   69.63056 1.000 17.02556 ? 286 ASP A N   1 
ATOM   2334 C CA  . ASP A 1 292 ? -4.72306  1.33044   69.57029 1.000 17.46138 ? 286 ASP A CA  1 
ATOM   2335 C C   . ASP A 1 292 ? -4.33572  1.06759   68.13072 1.000 16.67860 ? 286 ASP A C   1 
ATOM   2336 O O   . ASP A 1 292 ? -3.14521  0.99759   67.80188 1.000 17.22312 ? 286 ASP A O   1 
ATOM   2337 C CB  . ASP A 1 292 ? -5.17740  0.01880   70.20943 1.000 20.12099 ? 286 ASP A CB  1 
ATOM   2338 C CG  . ASP A 1 292 ? -4.06022  -0.96528  70.33807 1.000 21.75943 ? 286 ASP A CG  1 
ATOM   2339 O OD1 . ASP A 1 292 ? -3.29030  -0.89209  71.33732 1.000 24.72166 ? 286 ASP A OD1 1 
ATOM   2340 O OD2 . ASP A 1 292 ? -3.93874  -1.84316  69.46147 1.000 21.85152 ? 286 ASP A OD2 1 
ATOM   2341 N N   . LEU A 1 293 ? -5.33479  0.98460   67.25052 1.000 15.31212 ? 287 LEU A N   1 
ATOM   2342 C CA  . LEU A 1 293 ? -5.03788  0.81994   65.82864 1.000 14.31969 ? 287 LEU A CA  1 
ATOM   2343 C C   . LEU A 1 293 ? -4.40389  2.07646   65.23914 1.000 15.20109 ? 287 LEU A C   1 
ATOM   2344 O O   . LEU A 1 293 ? -3.46029  1.97411   64.44347 1.000 15.87205 ? 287 LEU A O   1 
ATOM   2345 C CB  . LEU A 1 293 ? -6.32863  0.45689   65.07827 1.000 15.04870 ? 287 LEU A CB  1 
ATOM   2346 C CG  . LEU A 1 293 ? -6.18041  0.24038   63.52960 1.000 15.05759 ? 287 LEU A CG  1 
ATOM   2347 C CD1 . LEU A 1 293 ? -5.04828  -0.72416  63.17472 1.000 14.97053 ? 287 LEU A CD1 1 
ATOM   2348 C CD2 . LEU A 1 293 ? -7.47018  -0.35773  62.96797 1.000 15.82623 ? 287 LEU A CD2 1 
ATOM   2349 N N   . LEU A 1 294 ? -4.89733  3.27379   65.61343 1.000 14.63688 ? 288 LEU A N   1 
ATOM   2350 C CA  . LEU A 1 294 ? -4.29279  4.52763   65.18667 1.000 13.49072 ? 288 LEU A CA  1 
ATOM   2351 C C   . LEU A 1 294 ? -2.80163  4.56239   65.51159 1.000 13.54774 ? 288 LEU A C   1 
ATOM   2352 O O   . LEU A 1 294 ? -1.97281  4.94649   64.67152 1.000 14.99657 ? 288 LEU A O   1 
ATOM   2353 C CB  . LEU A 1 294 ? -5.00765  5.70296   65.89033 1.000 14.27612 ? 288 LEU A CB  1 
ATOM   2354 C CG  . LEU A 1 294 ? -4.46704  7.10228   65.48166 1.000 13.94130 ? 288 LEU A CG  1 
ATOM   2355 C CD1 . LEU A 1 294 ? -4.64341  7.39238   63.96829 1.000 13.85211 ? 288 LEU A CD1 1 
ATOM   2356 C CD2 . LEU A 1 294 ? -5.15596  8.23741   66.33090 1.000 15.25573 ? 288 LEU A CD2 1 
ATOM   2357 N N   . ASP A 1 295 ? -2.44254  4.15420   66.73425 1.000 12.97788 ? 289 ASP A N   1 
ATOM   2358 C CA  . ASP A 1 295 ? -1.05192  4.16620   67.14993 1.000 14.25895 ? 289 ASP A CA  1 
ATOM   2359 C C   . ASP A 1 295 ? -0.20148  3.27427   66.26160 1.000 16.08302 ? 289 ASP A C   1 
ATOM   2360 O O   . ASP A 1 295 ? 0.93688   3.63171   65.93171 1.000 15.55173 ? 289 ASP A O   1 
ATOM   2361 C CB  . ASP A 1 295 ? -0.94837  3.67054   68.61142 1.000 17.60808 ? 289 ASP A CB  1 
ATOM   2362 C CG  . ASP A 1 295 ? 0.49543   3.70317   69.12119 1.000 21.46840 ? 289 ASP A CG  1 
ATOM   2363 O OD1 . ASP A 1 295 ? 0.99801   4.78835   69.31282 1.000 23.03371 ? 289 ASP A OD1 1 
ATOM   2364 O OD2 . ASP A 1 295 ? 1.10777   2.64686   69.28475 1.000 24.90150 ? 289 ASP A OD2 1 
ATOM   2365 N N   . LYS A 1 296 ? -0.73186  2.09706   65.88592 1.000 15.49354 ? 290 LYS A N   1 
ATOM   2366 C CA  . LYS A 1 296 ? 0.02379   1.16802   65.04104 1.000 15.94268 ? 290 LYS A CA  1 
ATOM   2367 C C   . LYS A 1 296 ? 0.14293   1.65852   63.59044 1.000 16.26761 ? 290 LYS A C   1 
ATOM   2368 O O   . LYS A 1 296 ? 1.13230   1.35840   62.90552 1.000 17.38929 ? 290 LYS A O   1 
ATOM   2369 C CB  . LYS A 1 296 ? -0.64186  -0.19483  65.12030 1.000 16.70599 ? 290 LYS A CB  1 
ATOM   2370 C CG  . LYS A 1 296 ? -0.49502  -0.79678  66.51874 1.000 18.36260 ? 290 LYS A CG  1 
ATOM   2371 C CD  A LYS A 1 296 ? -1.16044  -2.16836  66.55551 0.500 18.57549 ? 290 LYS A CD  1 
ATOM   2372 C CD  B LYS A 1 296 ? -1.38960  -2.00057  66.69398 0.500 21.11669 ? 290 LYS A CD  1 
ATOM   2373 C CE  A LYS A 1 296 ? -0.71306  -3.04364  67.77198 0.500 18.29551 ? 290 LYS A CE  1 
ATOM   2374 C CE  B LYS A 1 296 ? -1.08427  -2.72555  68.01741 0.500 23.70000 ? 290 LYS A CE  1 
ATOM   2375 N NZ  A LYS A 1 296 ? -1.12287  -2.50326  69.11020 0.500 17.51010 ? 290 LYS A NZ  1 
ATOM   2376 N NZ  B LYS A 1 296 ? -1.90324  -3.95342  68.21901 0.500 25.47464 ? 290 LYS A NZ  1 
ATOM   2377 N N   . MET A 1 297 ? -0.82131  2.43999   63.11554 1.000 14.38336 ? 291 MET A N   1 
ATOM   2378 C CA  . MET A 1 297 ? -0.70084  3.02451   61.76163 1.000 12.96210 ? 291 MET A CA  1 
ATOM   2379 C C   . MET A 1 297 ? 0.25223   4.22852   61.75008 1.000 12.90171 ? 291 MET A C   1 
ATOM   2380 O O   . MET A 1 297 ? 0.95758   4.44660   60.76061 1.000 14.64411 ? 291 MET A O   1 
ATOM   2381 C CB  A MET A 1 297 ? -2.09026  3.42020   61.23375 0.550 13.13528 ? 291 MET A CB  1 
ATOM   2382 C CB  B MET A 1 297 ? -2.07338  3.46813   61.25297 0.450 12.73871 ? 291 MET A CB  1 
ATOM   2383 C CG  A MET A 1 297 ? -2.94183  2.19407   60.98008 0.550 15.11185 ? 291 MET A CG  1 
ATOM   2384 C CG  B MET A 1 297 ? -2.98036  2.32628   61.02832 0.450 13.96224 ? 291 MET A CG  1 
ATOM   2385 S SD  A MET A 1 297 ? -4.45241  2.43203   59.97598 0.550 17.33173 ? 291 MET A SD  1 
ATOM   2386 S SD  B MET A 1 297 ? -4.65564  2.89081   60.61171 0.450 15.04025 ? 291 MET A SD  1 
ATOM   2387 C CE  A MET A 1 297 ? -5.40834  3.47360   61.03469 0.550 17.00740 ? 291 MET A CE  1 
ATOM   2388 C CE  B MET A 1 297 ? -5.29456  1.39812   59.93182 0.450 15.62587 ? 291 MET A CE  1 
ATOM   2389 N N   . LEU A 1 298 ? 0.23009   5.05753   62.79799 1.000 13.65432 ? 292 LEU A N   1 
ATOM   2390 C CA  . LEU A 1 298 ? 1.07189   6.23738   62.89587 1.000 14.24382 ? 292 LEU A CA  1 
ATOM   2391 C C   . LEU A 1 298 ? 2.36248   5.92661   63.67103 1.000 16.97390 ? 292 LEU A C   1 
ATOM   2392 O O   . LEU A 1 298 ? 2.78774   6.64462   64.56599 1.000 19.90854 ? 292 LEU A O   1 
ATOM   2393 C CB  . LEU A 1 298 ? 0.28558   7.39419   63.51783 1.000 13.72677 ? 292 LEU A CB  1 
ATOM   2394 C CG  . LEU A 1 298 ? -0.90920  7.91501   62.67191 1.000 13.19274 ? 292 LEU A CG  1 
ATOM   2395 C CD1 . LEU A 1 298 ? -1.59724  9.10691   63.32882 1.000 14.44403 ? 292 LEU A CD1 1 
ATOM   2396 C CD2 . LEU A 1 298 ? -0.45633  8.23242   61.20658 1.000 13.18275 ? 292 LEU A CD2 1 
ATOM   2397 N N   . THR A 1 299 ? 2.97393   4.80768   63.34145 1.000 16.00270 ? 293 THR A N   1 
ATOM   2398 C CA  A THR A 1 299 ? 4.26512   4.47166   63.91314 0.500 15.71714 ? 293 THR A CA  1 
ATOM   2399 C CA  B THR A 1 299 ? 4.28596   4.47240   63.90941 0.500 17.65447 ? 293 THR A CA  1 
ATOM   2400 C C   . THR A 1 299 ? 5.37414   5.15219   63.10622 1.000 15.74861 ? 293 THR A C   1 
ATOM   2401 O O   . THR A 1 299 ? 5.34697   5.13008   61.86086 1.000 16.48351 ? 293 THR A O   1 
ATOM   2402 C CB  A THR A 1 299 ? 4.35628   2.94325   63.97034 0.500 14.69209 ? 293 THR A CB  1 
ATOM   2403 C CB  B THR A 1 299 ? 4.59643   2.97525   63.89400 0.500 20.82157 ? 293 THR A CB  1 
ATOM   2404 O OG1 A THR A 1 299 ? 3.50277   2.49025   65.04574 0.500 15.64890 ? 293 THR A OG1 1 
ATOM   2405 O OG1 B THR A 1 299 ? 4.93328   2.59029   62.55311 0.500 22.83045 ? 293 THR A OG1 1 
ATOM   2406 C CG2 A THR A 1 299 ? 5.79815   2.42892   64.18465 0.500 12.56706 ? 293 THR A CG2 1 
ATOM   2407 C CG2 B THR A 1 299 ? 3.47426   2.13078   64.48193 0.500 21.70145 ? 293 THR A CG2 1 
ATOM   2408 N N   . PHE A 1 300 ? 6.36939   5.75820   63.83079 1.000 15.97095 ? 294 PHE A N   1 
ATOM   2409 C CA  . PHE A 1 300 ? 7.41747   6.50968   63.14308 1.000 16.96587 ? 294 PHE A CA  1 
ATOM   2410 C C   . PHE A 1 300 ? 8.25204   5.61521   62.21374 1.000 17.21154 ? 294 PHE A C   1 
ATOM   2411 O O   . PHE A 1 300 ? 8.50746   5.96628   61.05273 1.000 18.31779 ? 294 PHE A O   1 
ATOM   2412 C CB  . PHE A 1 300 ? 8.33391   7.17258   64.19354 1.000 17.74086 ? 294 PHE A CB  1 
ATOM   2413 C CG  . PHE A 1 300 ? 9.48758   7.93097   63.60904 1.000 20.39371 ? 294 PHE A CG  1 
ATOM   2414 C CD1 . PHE A 1 300 ? 9.35146   9.23801   63.24920 1.000 21.03260 ? 294 PHE A CD1 1 
ATOM   2415 C CD2 . PHE A 1 300 ? 10.72045  7.33221   63.49340 1.000 21.60521 ? 294 PHE A CD2 1 
ATOM   2416 C CE1 . PHE A 1 300 ? 10.42560  9.96031   62.70144 1.000 22.04538 ? 294 PHE A CE1 1 
ATOM   2417 C CE2 . PHE A 1 300 ? 11.79376  8.03219   62.93174 1.000 21.94593 ? 294 PHE A CE2 1 
ATOM   2418 C CZ  . PHE A 1 300 ? 11.63915  9.37901   62.57631 1.000 22.26921 ? 294 PHE A CZ  1 
ATOM   2419 N N   . ASN A 1 301 ? 8.71225   4.48171   62.70761 1.000 16.96709 ? 295 ASN A N   1 
ATOM   2420 C CA  . ASN A 1 301 ? 9.58867   3.58571   61.91109 1.000 17.96253 ? 295 ASN A CA  1 
ATOM   2421 C C   . ASN A 1 301 ? 8.72428   2.84016   60.89813 1.000 17.83964 ? 295 ASN A C   1 
ATOM   2422 O O   . ASN A 1 301 ? 7.87479   2.05034   61.30339 1.000 18.20530 ? 295 ASN A O   1 
ATOM   2423 C CB  . ASN A 1 301 ? 10.28367  2.59931   62.84284 1.000 20.16235 ? 295 ASN A CB  1 
ATOM   2424 C CG  . ASN A 1 301 ? 11.32029  1.72998   62.14338 1.000 22.17214 ? 295 ASN A CG  1 
ATOM   2425 O OD1 . ASN A 1 301 ? 11.26183  1.48403   60.93812 1.000 24.02757 ? 295 ASN A OD1 1 
ATOM   2426 N ND2 . ASN A 1 301 ? 12.27536  1.22981   62.92885 1.000 21.90014 ? 295 ASN A ND2 1 
ATOM   2427 N N   . PRO A 1 302 ? 8.94716   3.00678   59.58715 1.000 16.60393 ? 296 PRO A N   1 
ATOM   2428 C CA  . PRO A 1 302 ? 8.03813   2.37039   58.62291 1.000 17.10057 ? 296 PRO A CA  1 
ATOM   2429 C C   . PRO A 1 302 ? 8.15126   0.86879   58.64512 1.000 18.12714 ? 296 PRO A C   1 
ATOM   2430 O O   . PRO A 1 302 ? 7.21276   0.18398   58.24390 1.000 20.53168 ? 296 PRO A O   1 
ATOM   2431 C CB  . PRO A 1 302 ? 8.48419   2.94323   57.26761 1.000 18.26509 ? 296 PRO A CB  1 
ATOM   2432 C CG  . PRO A 1 302 ? 9.95761   3.42245   57.51409 1.000 17.18438 ? 296 PRO A CG  1 
ATOM   2433 C CD  . PRO A 1 302 ? 9.92929   3.90261   58.97294 1.000 17.47901 ? 296 PRO A CD  1 
ATOM   2434 N N   . HIS A 1 303 ? 9.28141   0.30942   59.08674 1.000 18.92985 ? 297 HIS A N   1 
ATOM   2435 C CA  . HIS A 1 303 ? 9.39234   -1.14385  59.18708 1.000 20.48521 ? 297 HIS A CA  1 
ATOM   2436 C C   . HIS A 1 303 ? 8.59637   -1.71248  60.35285 1.000 22.03047 ? 297 HIS A C   1 
ATOM   2437 O O   . HIS A 1 303 ? 8.26445   -2.89502  60.33340 1.000 25.12727 ? 297 HIS A O   1 
ATOM   2438 C CB  . HIS A 1 303 ? 10.86974  -1.54354  59.33518 0.800 22.97175 ? 297 HIS A CB  1 
ATOM   2439 C CG  . HIS A 1 303 ? 11.73226  -1.01137  58.24319 0.600 26.10708 ? 297 HIS A CG  1 
ATOM   2440 N ND1 . HIS A 1 303 ? 12.48907  0.13338   58.37805 0.600 28.53922 ? 297 HIS A ND1 1 
ATOM   2441 C CD2 . HIS A 1 303 ? 11.91410  -1.43993  56.97119 0.600 27.44779 ? 297 HIS A CD2 1 
ATOM   2442 C CE1 . HIS A 1 303 ? 13.12783  0.36555   57.24815 0.600 28.92756 ? 297 HIS A CE1 1 
ATOM   2443 N NE2 . HIS A 1 303 ? 12.77960  -0.56309  56.37305 0.600 29.00749 ? 297 HIS A NE2 1 
ATOM   2444 N N   . LYS A 1 304 ? 8.27523   -0.90632  61.35299 1.000 19.21365 ? 298 LYS A N   1 
ATOM   2445 C CA  . LYS A 1 304 ? 7.45713   -1.35829  62.48567 1.000 19.26713 ? 298 LYS A CA  1 
ATOM   2446 C C   . LYS A 1 304 ? 5.97105   -1.05018  62.29474 1.000 17.94494 ? 298 LYS A C   1 
ATOM   2447 O O   . LYS A 1 304 ? 5.15883   -1.53975  63.07256 1.000 18.78025 ? 298 LYS A O   1 
ATOM   2448 C CB  . LYS A 1 304 ? 7.96254   -0.73301  63.78066 1.000 20.53616 ? 298 LYS A CB  1 
ATOM   2449 C CG  . LYS A 1 304 ? 9.44310   -1.12633  64.16060 1.000 22.91129 ? 298 LYS A CG  1 
ATOM   2450 C CD  . LYS A 1 304 ? 9.88149   -0.43131  65.47938 0.800 23.10126 ? 298 LYS A CD  1 
ATOM   2451 C CE  . LYS A 1 304 ? 11.26042  -0.86724  65.91698 0.700 23.63491 ? 298 LYS A CE  1 
ATOM   2452 N NZ  . LYS A 1 304 ? 11.75272  0.06244   66.98088 0.700 24.76694 ? 298 LYS A NZ  1 
ATOM   2453 N N   . ARG A 1 305 ? 5.63928   -0.24105  61.30442 1.000 17.18076 ? 299 ARG A N   1 
ATOM   2454 C CA  . ARG A 1 305 ? 4.27443   0.17206   61.03163 1.000 14.37589 ? 299 ARG A CA  1 
ATOM   2455 C C   . ARG A 1 305 ? 3.41472   -1.02155  60.62131 1.000 15.29243 ? 299 ARG A C   1 
ATOM   2456 O O   . ARG A 1 305 ? 3.86272   -1.89452  59.88438 1.000 17.53552 ? 299 ARG A O   1 
ATOM   2457 C CB  . ARG A 1 305 ? 4.30586   1.27544   59.94050 1.000 13.94086 ? 299 ARG A CB  1 
ATOM   2458 C CG  . ARG A 1 305 ? 2.98034   2.14191   59.82644 1.000 13.84769 ? 299 ARG A CG  1 
ATOM   2459 C CD  . ARG A 1 305 ? 3.23294   3.29352   58.81316 1.000 13.13402 ? 299 ARG A CD  1 
ATOM   2460 N NE  . ARG A 1 305 ? 4.31656   4.15259   59.28682 1.000 13.38677 ? 299 ARG A NE  1 
ATOM   2461 C CZ  . ARG A 1 305 ? 5.13553   4.85394   58.50593 1.000 13.48153 ? 299 ARG A CZ  1 
ATOM   2462 N NH1 . ARG A 1 305 ? 5.03173   4.85826   57.15736 1.000 14.39805 ? 299 ARG A NH1 1 
ATOM   2463 N NH2 . ARG A 1 305 ? 6.10959   5.54550   59.07078 1.000 13.52611 ? 299 ARG A NH2 1 
ATOM   2464 N N   . ILE A 1 306 ? 2.14675   -1.03887  61.06975 1.000 13.73250 ? 300 ILE A N   1 
ATOM   2465 C CA  . ILE A 1 306 ? 1.25273   -2.16605  60.76102 1.000 14.34399 ? 300 ILE A CA  1 
ATOM   2466 C C   . ILE A 1 306 ? 0.99367   -2.20612  59.24828 1.000 14.99352 ? 300 ILE A C   1 
ATOM   2467 O O   . ILE A 1 306 ? 0.95755   -1.14977  58.58516 1.000 15.40563 ? 300 ILE A O   1 
ATOM   2468 C CB  . ILE A 1 306 ? -0.07215  -1.96176  61.54400 1.000 14.85827 ? 300 ILE A CB  1 
ATOM   2469 C CG1 . ILE A 1 306 ? -0.92162  -3.24723  61.59863 1.000 15.46710 ? 300 ILE A CG1 1 
ATOM   2470 C CG2 . ILE A 1 306 ? -0.89954  -0.72186  61.03135 1.000 15.86632 ? 300 ILE A CG2 1 
ATOM   2471 C CD1 . ILE A 1 306 ? -2.01241  -3.17677  62.66473 1.000 17.51886 ? 300 ILE A CD1 1 
ATOM   2472 N N   . GLU A 1 307 ? 0.84978   -3.43951  58.69360 1.000 13.52187 ? 301 GLU A N   1 
ATOM   2473 C CA  . GLU A 1 307 ? 0.49304   -3.62725  57.28117 1.000 13.35520 ? 301 GLU A CA  1 
ATOM   2474 C C   . GLU A 1 307 ? -1.01617  -3.77126  57.14011 1.000 14.34474 ? 301 GLU A C   1 
ATOM   2475 O O   . GLU A 1 307 ? -1.74069  -3.97864  58.11851 1.000 15.42918 ? 301 GLU A O   1 
ATOM   2476 C CB  . GLU A 1 307 ? 1.17428   -4.87295  56.67882 1.000 16.01338 ? 301 GLU A CB  1 
ATOM   2477 C CG  . GLU A 1 307 ? 2.69858   -4.78674  56.73088 1.000 18.64257 ? 301 GLU A CG  1 
ATOM   2478 C CD  . GLU A 1 307 ? 3.42671   -5.71973  55.81522 0.900 21.09933 ? 301 GLU A CD  1 
ATOM   2479 O OE1 . GLU A 1 307 ? 2.86002   -6.74265  55.37620 0.700 21.21683 ? 301 GLU A OE1 1 
ATOM   2480 O OE2 . GLU A 1 307 ? 4.60686   -5.45977  55.57193 0.700 23.04370 ? 301 GLU A OE2 1 
ATOM   2481 N N   . VAL A 1 308 ? -1.49268  -3.65933  55.88449 1.000 14.19645 ? 302 VAL A N   1 
ATOM   2482 C CA  . VAL A 1 308 ? -2.93388  -3.59242  55.65766 1.000 13.92127 ? 302 VAL A CA  1 
ATOM   2483 C C   . VAL A 1 308 ? -3.66220  -4.84225  56.16718 1.000 14.93339 ? 302 VAL A C   1 
ATOM   2484 O O   . VAL A 1 308 ? -4.76947  -4.72688  56.73580 1.000 15.71539 ? 302 VAL A O   1 
ATOM   2485 C CB  . VAL A 1 308 ? -3.23250  -3.27327  54.18109 1.000 13.39083 ? 302 VAL A CB  1 
ATOM   2486 C CG1 . VAL A 1 308 ? -2.82151  -4.44700  53.23677 1.000 13.98738 ? 302 VAL A CG1 1 
ATOM   2487 C CG2 . VAL A 1 308 ? -4.73021  -2.88504  54.02796 1.000 15.14768 ? 302 VAL A CG2 1 
ATOM   2488 N N   . GLU A 1 309 ? -3.10271  -6.06091  55.94453 1.000 15.32674 ? 303 GLU A N   1 
ATOM   2489 C CA  A GLU A 1 309 ? -3.81549  -7.25085  56.38395 0.500 17.12272 ? 303 GLU A CA  1 
ATOM   2490 C CA  B GLU A 1 309 ? -3.79546  -7.26670  56.39209 0.500 17.15349 ? 303 GLU A CA  1 
ATOM   2491 C C   . GLU A 1 309 ? -3.84692  -7.35614  57.90537 1.000 16.47765 ? 303 GLU A C   1 
ATOM   2492 O O   . GLU A 1 309 ? -4.83652  -7.85986  58.46005 1.000 17.19319 ? 303 GLU A O   1 
ATOM   2493 C CB  A GLU A 1 309 ? -3.20457  -8.50153  55.73497 0.500 19.01222 ? 303 GLU A CB  1 
ATOM   2494 C CB  B GLU A 1 309 ? -3.12614  -8.51585  55.81703 0.500 19.20775 ? 303 GLU A CB  1 
ATOM   2495 C CG  A GLU A 1 309 ? -3.69274  -8.64056  54.25891 0.500 20.06504 ? 303 GLU A CG  1 
ATOM   2496 C CG  B GLU A 1 309 ? -3.39284  -8.66564  54.31728 0.500 20.72968 ? 303 GLU A CG  1 
ATOM   2497 C CD  A GLU A 1 309 ? -2.66675  -9.26960  53.28911 0.500 22.11626 ? 303 GLU A CD  1 
ATOM   2498 C CD  B GLU A 1 309 ? -2.83289  -9.98039  53.74806 0.500 22.83808 ? 303 GLU A CD  1 
ATOM   2499 O OE1 A GLU A 1 309 ? -1.61951  -9.73660  53.75874 0.500 22.09928 ? 303 GLU A OE1 1 
ATOM   2500 O OE1 B GLU A 1 309 ? -1.81072  -10.44966 54.24352 0.500 24.97041 ? 303 GLU A OE1 1 
ATOM   2501 O OE2 A GLU A 1 309 ? -2.91385  -9.31183  52.04655 0.500 23.64258 ? 303 GLU A OE2 1 
ATOM   2502 O OE2 B GLU A 1 309 ? -3.38204  -10.54439 52.80052 0.500 23.94431 ? 303 GLU A OE2 1 
ATOM   2503 N N   . GLN A 1 310 ? -2.80187  -6.86921  58.59396 1.000 15.52952 ? 304 GLN A N   1 
ATOM   2504 C CA  . GLN A 1 310 ? -2.84081  -6.84362  60.06457 1.000 16.73118 ? 304 GLN A CA  1 
ATOM   2505 C C   . GLN A 1 310 ? -3.87892  -5.86444  60.57590 1.000 17.03524 ? 304 GLN A C   1 
ATOM   2506 O O   . GLN A 1 310 ? -4.55490  -6.12459  61.59889 1.000 17.88439 ? 304 GLN A O   1 
ATOM   2507 C CB  . GLN A 1 310 ? -1.48630  -6.42405  60.62914 1.000 18.42491 ? 304 GLN A CB  1 
ATOM   2508 C CG  . GLN A 1 310 ? -0.41159  -7.36315  60.43570 0.900 18.04056 ? 304 GLN A CG  1 
ATOM   2509 C CD  . GLN A 1 310 ? 0.92055   -6.73725  60.85611 0.700 16.21372 ? 304 GLN A CD  1 
ATOM   2510 O OE1 . GLN A 1 310 ? 1.42942   -5.82300  60.20616 0.700 15.90446 ? 304 GLN A OE1 1 
ATOM   2511 N NE2 . GLN A 1 310 ? 1.46172   -7.19408  61.97175 0.700 17.02314 ? 304 GLN A NE2 1 
ATOM   2512 N N   . ALA A 1 311 ? -3.99397  -4.71442  59.89107 1.000 15.60577 ? 305 ALA A N   1 
ATOM   2513 C CA  . ALA A 1 311 ? -4.97198  -3.69335  60.27443 1.000 14.02756 ? 305 ALA A CA  1 
ATOM   2514 C C   . ALA A 1 311 ? -6.39773  -4.23220  60.18516 1.000 14.69680 ? 305 ALA A C   1 
ATOM   2515 O O   . ALA A 1 311 ? -7.20247  -4.02839  61.12503 1.000 14.88224 ? 305 ALA A O   1 
ATOM   2516 C CB  . ALA A 1 311 ? -4.76298  -2.43754  59.40692 1.000 13.59379 ? 305 ALA A CB  1 
ATOM   2517 N N   . LEU A 1 312 ? -6.71298  -4.96075  59.09685 1.000 14.60211 ? 306 LEU A N   1 
ATOM   2518 C CA  . LEU A 1 312 ? -8.06018  -5.52560  58.92029 1.000 14.59859 ? 306 LEU A CA  1 
ATOM   2519 C C   . LEU A 1 312 ? -8.41199  -6.49587  60.05785 1.000 15.49338 ? 306 LEU A C   1 
ATOM   2520 O O   . LEU A 1 312 ? -9.59428  -6.60869  60.45336 1.000 16.64458 ? 306 LEU A O   1 
ATOM   2521 C CB  . LEU A 1 312 ? -8.16080  -6.23357  57.55759 1.000 14.79439 ? 306 LEU A CB  1 
ATOM   2522 C CG  . LEU A 1 312 ? -8.35485  -5.28634  56.35816 1.000 13.88259 ? 306 LEU A CG  1 
ATOM   2523 C CD1 . LEU A 1 312 ? -8.03027  -5.97018  55.00711 1.000 12.65307 ? 306 LEU A CD1 1 
ATOM   2524 C CD2 . LEU A 1 312 ? -9.82405  -4.72272  56.36409 1.000 15.77548 ? 306 LEU A CD2 1 
ATOM   2525 N N   . ALA A 1 313 ? -7.40689  -7.16891  60.61066 1.000 16.30788 ? 307 ALA A N   1 
ATOM   2526 C CA  . ALA A 1 313 ? -7.56219  -8.17461  61.66493 1.000 16.72688 ? 307 ALA A CA  1 
ATOM   2527 C C   . ALA A 1 313 ? -7.52684  -7.55656  63.05684 1.000 18.19435 ? 307 ALA A C   1 
ATOM   2528 O O   . ALA A 1 313 ? -7.59255  -8.29188  64.05174 1.000 19.36343 ? 307 ALA A O   1 
ATOM   2529 C CB  . ALA A 1 313 ? -6.43077  -9.23382  61.56662 1.000 17.44185 ? 307 ALA A CB  1 
ATOM   2530 N N   . HIS A 1 314 ? -7.41012  -6.24552  63.14595 1.000 18.07296 ? 308 HIS A N   1 
ATOM   2531 C CA  . HIS A 1 314 ? -7.32064  -5.60710  64.47032 1.000 17.20329 ? 308 HIS A CA  1 
ATOM   2532 C C   . HIS A 1 314 ? -8.68979  -5.65861  65.17657 1.000 19.04305 ? 308 HIS A C   1 
ATOM   2533 O O   . HIS A 1 314 ? -9.73456  -5.53095  64.51677 1.000 20.19925 ? 308 HIS A O   1 
ATOM   2534 C CB  . HIS A 1 314 ? -6.85095  -4.15567  64.28209 1.000 17.31985 ? 308 HIS A CB  1 
ATOM   2535 C CG  . HIS A 1 314 ? -6.57601  -3.43818  65.56580 1.000 17.46135 ? 308 HIS A CG  1 
ATOM   2536 N ND1 . HIS A 1 314 ? -7.57004  -2.89113  66.34795 1.000 17.70238 ? 308 HIS A ND1 1 
ATOM   2537 C CD2 . HIS A 1 314 ? -5.41219  -3.22150  66.22625 1.000 17.61958 ? 308 HIS A CD2 1 
ATOM   2538 C CE1 . HIS A 1 314 ? -7.03767  -2.37941  67.45252 1.000 18.24388 ? 308 HIS A CE1 1 
ATOM   2539 N NE2 . HIS A 1 314 ? -5.72380  -2.54666  67.39170 1.000 17.67103 ? 308 HIS A NE2 1 
ATOM   2540 N N   . PRO A 1 315 ? -8.72536  -5.82699  66.52275 1.000 19.49879 ? 309 PRO A N   1 
ATOM   2541 C CA  . PRO A 1 315 ? -10.01911 -5.90037  67.23594 1.000 19.67945 ? 309 PRO A CA  1 
ATOM   2542 C C   . PRO A 1 315 ? -11.00701 -4.76284  66.93274 1.000 19.05350 ? 309 PRO A C   1 
ATOM   2543 O O   . PRO A 1 315 ? -12.22256 -4.97499  67.03058 1.000 19.29972 ? 309 PRO A O   1 
ATOM   2544 C CB  . PRO A 1 315 ? -9.58667  -5.88054  68.71710 1.000 21.30192 ? 309 PRO A CB  1 
ATOM   2545 C CG  . PRO A 1 315 ? -8.21800  -6.59476  68.69346 1.000 20.89802 ? 309 PRO A CG  1 
ATOM   2546 C CD  . PRO A 1 315 ? -7.57821  -6.05796  67.41544 1.000 19.75137 ? 309 PRO A CD  1 
ATOM   2547 N N   . TYR A 1 316 ? -10.52711 -3.56261  66.59709 1.000 18.67608 ? 310 TYR A N   1 
ATOM   2548 C CA  . TYR A 1 316 ? -11.44876 -2.46604  66.32940 1.000 16.81466 ? 310 TYR A CA  1 
ATOM   2549 C C   . TYR A 1 316 ? -12.39111 -2.83014  65.18758 1.000 16.96499 ? 310 TYR A C   1 
ATOM   2550 O O   . TYR A 1 316 ? -13.54860 -2.40807  65.19234 1.000 18.07765 ? 310 TYR A O   1 
ATOM   2551 C CB  . TYR A 1 316 ? -10.67764 -1.15959  65.98590 1.000 17.12000 ? 310 TYR A CB  1 
ATOM   2552 C CG  . TYR A 1 316 ? -11.59549 0.04713   65.69153 1.000 18.00892 ? 310 TYR A CG  1 
ATOM   2553 C CD1 . TYR A 1 316 ? -12.56016 0.48657   66.62731 1.000 18.36278 ? 310 TYR A CD1 1 
ATOM   2554 C CD2 . TYR A 1 316 ? -11.50873 0.75730   64.48452 1.000 17.65258 ? 310 TYR A CD2 1 
ATOM   2555 C CE1 . TYR A 1 316 ? -13.39510 1.58678   66.36618 1.000 18.43266 ? 310 TYR A CE1 1 
ATOM   2556 C CE2 . TYR A 1 316 ? -12.30813 1.86177   64.23389 1.000 19.01964 ? 310 TYR A CE2 1 
ATOM   2557 C CZ  . TYR A 1 316 ? -13.26136 2.28058   65.16497 1.000 19.90806 ? 310 TYR A CZ  1 
ATOM   2558 O OH  . TYR A 1 316 ? -14.07885 3.37229   64.86178 1.000 21.97511 ? 310 TYR A OH  1 
ATOM   2559 N N   . LEU A 1 317 ? -11.90610 -3.63215  64.21560 1.000 16.01803 ? 311 LEU A N   1 
ATOM   2560 C CA  . LEU A 1 317 ? -12.67937 -3.97776  63.01312 1.000 17.08395 ? 311 LEU A CA  1 
ATOM   2561 C C   . LEU A 1 317 ? -13.35283 -5.35093  63.09091 1.000 18.70250 ? 311 LEU A C   1 
ATOM   2562 O O   . LEU A 1 317 ? -13.80933 -5.85492  62.06726 1.000 18.89062 ? 311 LEU A O   1 
ATOM   2563 C CB  . LEU A 1 317 ? -11.78315 -3.90853  61.76140 1.000 16.83848 ? 311 LEU A CB  1 
ATOM   2564 C CG  . LEU A 1 317 ? -11.19939 -2.48848  61.55849 1.000 15.77520 ? 311 LEU A CG  1 
ATOM   2565 C CD1 . LEU A 1 317 ? -10.31121 -2.43975  60.37437 1.000 17.20427 ? 311 LEU A CD1 1 
ATOM   2566 C CD2 . LEU A 1 317 ? -12.31720 -1.47818  61.37676 1.000 16.17257 ? 311 LEU A CD2 1 
ATOM   2567 N N   . GLU A 1 318 ? -13.49247 -5.92782  64.27642 1.000 19.58435 ? 312 GLU A N   1 
ATOM   2568 C CA  . GLU A 1 318 ? -13.95665 -7.31500  64.40399 1.000 20.30926 ? 312 GLU A CA  1 
ATOM   2569 C C   . GLU A 1 318 ? -15.36550 -7.52041  63.87489 1.000 21.56680 ? 312 GLU A C   1 
ATOM   2570 O O   . GLU A 1 318 ? -15.71251 -8.62877  63.44433 1.000 22.98624 ? 312 GLU A O   1 
ATOM   2571 C CB  . GLU A 1 318 ? -13.87725 -7.73610  65.88707 1.000 22.09114 ? 312 GLU A CB  1 
ATOM   2572 C CG  . GLU A 1 318 ? -14.33768 -9.19182  66.15411 0.800 25.41562 ? 312 GLU A CG  1 
ATOM   2573 C CD  . GLU A 1 318 ? -14.17205 -9.61550  67.61462 0.600 27.60356 ? 312 GLU A CD  1 
ATOM   2574 O OE1 . GLU A 1 318 ? -13.59132 -8.82714  68.37556 0.600 28.36115 ? 312 GLU A OE1 1 
ATOM   2575 O OE2 . GLU A 1 318 ? -14.60603 -10.73983 67.99659 0.600 29.83253 ? 312 GLU A OE2 1 
ATOM   2576 N N   . GLN A 1 319 ? -16.20711 -6.49722  63.93646 1.000 20.44598 ? 313 GLN A N   1 
ATOM   2577 C CA  . GLN A 1 319 ? -17.57039 -6.65208  63.40630 1.000 21.46801 ? 313 GLN A CA  1 
ATOM   2578 C C   . GLN A 1 319 ? -17.61290 -6.85687  61.90889 1.000 21.37574 ? 313 GLN A C   1 
ATOM   2579 O O   . GLN A 1 319 ? -18.61449 -7.37931  61.42195 1.000 23.29460 ? 313 GLN A O   1 
ATOM   2580 C CB  . GLN A 1 319 ? -18.43198 -5.46078  63.78243 1.000 21.74265 ? 313 GLN A CB  1 
ATOM   2581 C CG  . GLN A 1 319 ? -18.34331 -5.11776  65.29580 0.700 24.12817 ? 313 GLN A CG  1 
ATOM   2582 C CD  . GLN A 1 319 ? -18.92722 -3.79461  65.60507 0.600 25.08267 ? 313 GLN A CD  1 
ATOM   2583 O OE1 . GLN A 1 319 ? -18.47964 -2.78124  65.03287 0.600 24.78497 ? 313 GLN A OE1 1 
ATOM   2584 N NE2 . GLN A 1 319 ? -19.95912 -3.76336  66.47648 0.600 26.76776 ? 313 GLN A NE2 1 
ATOM   2585 N N   . TYR A 1 320 ? -16.57261 -6.45010  61.18373 1.000 20.40308 ? 314 TYR A N   1 
ATOM   2586 C CA  . TYR A 1 320 ? -16.55550 -6.53357  59.72108 1.000 19.74027 ? 314 TYR A CA  1 
ATOM   2587 C C   . TYR A 1 320 ? -15.56091 -7.54579  59.16119 1.000 20.08735 ? 314 TYR A C   1 
ATOM   2588 O O   . TYR A 1 320 ? -15.77505 -8.06470  58.05460 1.000 21.56577 ? 314 TYR A O   1 
ATOM   2589 C CB  . TYR A 1 320 ? -16.23742 -5.15080  59.11247 1.000 19.91011 ? 314 TYR A CB  1 
ATOM   2590 C CG  . TYR A 1 320 ? -17.28301 -4.12274  59.45107 1.000 22.12665 ? 314 TYR A CG  1 
ATOM   2591 C CD1 . TYR A 1 320 ? -18.54166 -4.15804  58.83829 1.000 24.42238 ? 314 TYR A CD1 1 
ATOM   2592 C CD2 . TYR A 1 320 ? -17.05087 -3.13959  60.37729 1.000 23.14510 ? 314 TYR A CD2 1 
ATOM   2593 C CE1 . TYR A 1 320 ? -19.52125 -3.25867  59.17288 1.000 25.02563 ? 314 TYR A CE1 1 
ATOM   2594 C CE2 . TYR A 1 320 ? -18.04467 -2.21052  60.70833 1.000 23.93691 ? 314 TYR A CE2 1 
ATOM   2595 C CZ  . TYR A 1 320 ? -19.25707 -2.27786  60.09163 1.000 25.02238 ? 314 TYR A CZ  1 
ATOM   2596 O OH  . TYR A 1 320 ? -20.23772 -1.35748  60.37396 1.000 28.06802 ? 314 TYR A OH  1 
ATOM   2597 N N   . TYR A 1 321 ? -14.48180 -7.83025  59.88460 1.000 18.47737 ? 315 TYR A N   1 
ATOM   2598 C CA  . TYR A 1 321 ? -13.37345 -8.63664  59.35215 1.000 18.54123 ? 315 TYR A CA  1 
ATOM   2599 C C   . TYR A 1 321 ? -13.82579 -9.99956  58.86003 1.000 20.07600 ? 315 TYR A C   1 
ATOM   2600 O O   . TYR A 1 321 ? -14.40896 -10.80583 59.61310 1.000 22.25893 ? 315 TYR A O   1 
ATOM   2601 C CB  . TYR A 1 321 ? -12.32852 -8.83527  60.44773 1.000 19.19030 ? 315 TYR A CB  1 
ATOM   2602 C CG  . TYR A 1 321 ? -11.08976 -9.58619  60.05423 1.000 20.30246 ? 315 TYR A CG  1 
ATOM   2603 C CD1 . TYR A 1 321 ? -10.35085 -9.20983  58.93089 1.000 20.22678 ? 315 TYR A CD1 1 
ATOM   2604 C CD2 . TYR A 1 321 ? -10.63518 -10.66447 60.81512 1.000 21.37167 ? 315 TYR A CD2 1 
ATOM   2605 C CE1 . TYR A 1 321 ? -9.17467  -9.90114  58.57239 1.000 20.10707 ? 315 TYR A CE1 1 
ATOM   2606 C CE2 . TYR A 1 321 ? -9.45843  -11.35195 60.47509 1.000 21.31745 ? 315 TYR A CE2 1 
ATOM   2607 C CZ  . TYR A 1 321 ? -8.73855  -10.97323 59.35641 1.000 21.83056 ? 315 TYR A CZ  1 
ATOM   2608 O OH  . TYR A 1 321 ? -7.57614  -11.65425 59.02267 1.000 23.08696 ? 315 TYR A OH  1 
ATOM   2609 N N   . ASP A 1 322 ? -13.44252 -10.29873 57.64115 1.000 18.53455 ? 316 ASP A N   1 
ATOM   2610 C CA  . ASP A 1 322 ? -13.74869 -11.56371 57.01142 1.000 20.21204 ? 316 ASP A CA  1 
ATOM   2611 C C   . ASP A 1 322 ? -12.82091 -11.75396 55.81594 1.000 20.09031 ? 316 ASP A C   1 
ATOM   2612 O O   . ASP A 1 322 ? -13.13834 -11.24175 54.72955 1.000 19.61935 ? 316 ASP A O   1 
ATOM   2613 C CB  . ASP A 1 322 ? -15.21276 -11.62003 56.55755 1.000 20.46509 ? 316 ASP A CB  1 
ATOM   2614 C CG  . ASP A 1 322 ? -15.54168 -12.90429 55.82643 0.800 21.32211 ? 316 ASP A CG  1 
ATOM   2615 O OD1 . ASP A 1 322 ? -14.64952 -13.77698 55.69577 0.700 21.44821 ? 316 ASP A OD1 1 
ATOM   2616 O OD2 . ASP A 1 322 ? -16.69077 -13.02437 55.38513 0.700 21.08066 ? 316 ASP A OD2 1 
ATOM   2617 N N   . PRO A 1 323 ? -11.65993 -12.44040 55.99032 1.000 19.75589 ? 317 PRO A N   1 
ATOM   2618 C CA  . PRO A 1 323 ? -10.63371 -12.44193 54.92850 1.000 20.08904 ? 317 PRO A CA  1 
ATOM   2619 C C   . PRO A 1 323 ? -11.12032 -13.05038 53.62206 1.000 20.62260 ? 317 PRO A C   1 
ATOM   2620 O O   . PRO A 1 323 ? -10.62648 -12.67704 52.55149 1.000 21.98165 ? 317 PRO A O   1 
ATOM   2621 C CB  . PRO A 1 323 ? -9.49166  -13.28253 55.53616 1.000 21.77955 ? 317 PRO A CB  1 
ATOM   2622 C CG  . PRO A 1 323 ? -9.72057  -13.23952 57.03261 1.000 21.57659 ? 317 PRO A CG  1 
ATOM   2623 C CD  . PRO A 1 323 ? -11.19073 -13.08950 57.22902 1.000 19.62717 ? 317 PRO A CD  1 
ATOM   2624 N N   . SER A 1 324 ? -12.05628 -13.99891 53.68069 1.000 20.79813 ? 318 SER A N   1 
ATOM   2625 C CA  . SER A 1 324 ? -12.62764 -14.56815 52.46302 1.000 20.91879 ? 318 SER A CA  1 
ATOM   2626 C C   . SER A 1 324 ? -13.52111 -13.60258 51.69341 1.000 20.80155 ? 318 SER A C   1 
ATOM   2627 O O   . SER A 1 324 ? -13.86632 -13.91842 50.53929 1.000 21.84220 ? 318 SER A O   1 
ATOM   2628 C CB  . SER A 1 324 ? -13.49054 -15.79421 52.77580 1.000 21.97894 ? 318 SER A CB  1 
ATOM   2629 O OG  . SER A 1 324 ? -14.75752 -15.29111 53.24742 1.000 26.10276 ? 318 SER A OG  1 
ATOM   2630 N N   . ASP A 1 325 ? -13.98441 -12.50584 52.31600 1.000 18.51487 ? 319 ASP A N   1 
ATOM   2631 C CA  . ASP A 1 325 ? -14.73679 -11.44700 51.63939 1.000 18.60288 ? 319 ASP A CA  1 
ATOM   2632 C C   . ASP A 1 325 ? -13.90510 -10.18233 51.45696 1.000 16.79473 ? 319 ASP A C   1 
ATOM   2633 O O   . ASP A 1 325 ? -14.46369 -9.08584  51.41259 1.000 17.14701 ? 319 ASP A O   1 
ATOM   2634 C CB  . ASP A 1 325 ? -16.01459 -11.12021 52.43472 1.000 20.36990 ? 319 ASP A CB  1 
ATOM   2635 C CG  . ASP A 1 325 ? -17.01790 -10.27061 51.65590 1.000 22.76718 ? 319 ASP A CG  1 
ATOM   2636 O OD1 . ASP A 1 325 ? -17.15334 -10.46253 50.41865 1.000 24.49647 ? 319 ASP A OD1 1 
ATOM   2637 O OD2 . ASP A 1 325 ? -17.69049 -9.41662  52.27068 1.000 23.15893 ? 319 ASP A OD2 1 
ATOM   2638 N N   . GLU A 1 326 ? -12.57257 -10.30116 51.45159 1.000 16.17165 ? 320 GLU A N   1 
ATOM   2639 C CA  . GLU A 1 326 ? -11.67200 -9.16858  51.30181 1.000 16.32576 ? 320 GLU A CA  1 
ATOM   2640 C C   . GLU A 1 326 ? -10.73412 -9.55142  50.16905 1.000 17.09218 ? 320 GLU A C   1 
ATOM   2641 O O   . GLU A 1 326 ? -9.62690  -10.05989 50.40269 1.000 17.10150 ? 320 GLU A O   1 
ATOM   2642 C CB  . GLU A 1 326 ? -10.91285 -8.88200  52.60927 1.000 17.52492 ? 320 GLU A CB  1 
ATOM   2643 C CG  . GLU A 1 326 ? -11.91199 -8.30577  53.66810 1.000 17.53640 ? 320 GLU A CG  1 
ATOM   2644 C CD  . GLU A 1 326 ? -11.50800 -8.53616  55.14997 1.000 18.27584 ? 320 GLU A CD  1 
ATOM   2645 O OE1 . GLU A 1 326 ? -10.36686 -8.97734  55.43781 1.000 19.35697 ? 320 GLU A OE1 1 
ATOM   2646 O OE2 . GLU A 1 326 ? -12.34545 -8.19871  56.00921 1.000 17.91443 ? 320 GLU A OE2 1 
ATOM   2647 N N   . PRO A 1 327 ? -11.19509 -9.44522  48.93491 1.000 16.85958 ? 321 PRO A N   1 
ATOM   2648 C CA  . PRO A 1 327 ? -10.46735 -10.06164 47.81958 1.000 17.20808 ? 321 PRO A CA  1 
ATOM   2649 C C   . PRO A 1 327 ? -9.15362  -9.37541  47.44658 1.000 17.97507 ? 321 PRO A C   1 
ATOM   2650 O O   . PRO A 1 327 ? -8.92274  -8.19126  47.73089 1.000 18.43707 ? 321 PRO A O   1 
ATOM   2651 C CB  . PRO A 1 327 ? -11.46403 -9.96306  46.65760 1.000 18.38703 ? 321 PRO A CB  1 
ATOM   2652 C CG  . PRO A 1 327 ? -12.48325 -8.95210  47.08175 1.000 18.96576 ? 321 PRO A CG  1 
ATOM   2653 C CD  . PRO A 1 327 ? -12.55447 -8.98118  48.56406 1.000 17.25440 ? 321 PRO A CD  1 
ATOM   2654 N N   . ILE A 1 328 ? -8.31509  -10.15540 46.74389 1.000 17.83868 ? 322 ILE A N   1 
ATOM   2655 C CA  . ILE A 1 328 ? -7.04063  -9.67551  46.22499 1.000 17.20266 ? 322 ILE A CA  1 
ATOM   2656 C C   . ILE A 1 328 ? -7.05760  -9.72450  44.69775 1.000 17.46733 ? 322 ILE A C   1 
ATOM   2657 O O   . ILE A 1 328 ? -7.94510  -10.32916 44.05704 1.000 18.33152 ? 322 ILE A O   1 
ATOM   2658 C CB  . ILE A 1 328 ? -5.83012  -10.43425 46.80922 1.000 18.11969 ? 322 ILE A CB  1 
ATOM   2659 C CG1 . ILE A 1 328 ? -5.88352  -11.93476 46.49228 1.000 18.99270 ? 322 ILE A CG1 1 
ATOM   2660 C CG2 . ILE A 1 328 ? -5.80909  -10.25445 48.32883 1.000 18.27718 ? 322 ILE A CG2 1 
ATOM   2661 C CD1 . ILE A 1 328 ? -4.63968  -12.70616 46.94187 1.000 20.31216 ? 322 ILE A CD1 1 
ATOM   2662 N N   . ALA A 1 329 ? -6.05900  -9.07238  44.13347 1.000 17.12455 ? 323 ALA A N   1 
ATOM   2663 C CA  . ALA A 1 329 ? -5.94167  -8.92991  42.69541 1.000 19.05999 ? 323 ALA A CA  1 
ATOM   2664 C C   . ALA A 1 329 ? -5.51665  -10.24719 42.06514 1.000 23.23795 ? 323 ALA A C   1 
ATOM   2665 O O   . ALA A 1 329 ? -4.67557  -10.96671 42.60108 1.000 24.10330 ? 323 ALA A O   1 
ATOM   2666 C CB  . ALA A 1 329 ? -4.90811  -7.84838  42.36132 1.000 18.56467 ? 323 ALA A CB  1 
ATOM   2667 N N   . GLU A 1 330 ? -6.10660  -10.54356 40.90865 1.000 25.61093 ? 324 GLU A N   1 
ATOM   2668 C CA  . GLU A 1 330 ? -5.76705  -11.75455 40.18612 1.000 30.68387 ? 324 GLU A CA  1 
ATOM   2669 C C   . GLU A 1 330 ? -4.40665  -11.62100 39.53120 1.000 33.89100 ? 324 GLU A C   1 
ATOM   2670 O O   . GLU A 1 330 ? -3.66700  -12.61986 39.39982 1.000 35.08348 ? 324 GLU A O   1 
ATOM   2671 C CB  . GLU A 1 330 ? -6.85144  -12.02448 39.12048 1.000 32.68018 ? 324 GLU A CB  1 
ATOM   2672 C CG  . GLU A 1 330 ? -6.42310  -12.95253 38.00734 0.700 35.70065 ? 324 GLU A CG  1 
ATOM   2673 C CD  . GLU A 1 330 ? -7.44652  -13.05563 36.88077 0.600 37.83172 ? 324 GLU A CD  1 
ATOM   2674 O OE1 . GLU A 1 330 ? -7.71132  -14.17468 36.40834 0.600 39.59360 ? 324 GLU A OE1 1 
ATOM   2675 O OE2 . GLU A 1 330 ? -7.98687  -12.01515 36.45718 0.600 38.70033 ? 324 GLU A OE2 1 
ATOM   2676 N N   . ALA A 1 331 ? -4.08121  -10.38920 39.10566 1.000 34.59404 ? 325 ALA A N   1 
ATOM   2677 C CA  . ALA A 1 331 ? -2.98970  -10.11162 38.16807 1.000 35.30833 ? 325 ALA A CA  1 
ATOM   2678 C C   . ALA A 1 331 ? -2.25190  -8.87321  38.65762 1.000 34.75757 ? 325 ALA A C   1 
ATOM   2679 O O   . ALA A 1 331 ? -2.47373  -7.75612  38.16943 1.000 35.68171 ? 325 ALA A O   1 
ATOM   2680 C CB  . ALA A 1 331 ? -3.51409  -9.92326  36.73350 1.000 35.98221 ? 325 ALA A CB  1 
ATOM   2681 N N   . PRO A 1 332 ? -1.35413  -9.03822  39.62924 1.000 32.31622 ? 326 PRO A N   1 
ATOM   2682 C CA  . PRO A 1 332 ? -0.50957  -7.91849  40.07157 1.000 31.89591 ? 326 PRO A CA  1 
ATOM   2683 C C   . PRO A 1 332 ? 0.29743   -7.26709  38.94565 1.000 29.38768 ? 326 PRO A C   1 
ATOM   2684 O O   . PRO A 1 332 ? 0.62830   -7.89055  37.93335 1.000 29.69050 ? 326 PRO A O   1 
ATOM   2685 C CB  . PRO A 1 332 ? 0.44756   -8.55852  41.07472 1.000 32.32410 ? 326 PRO A CB  1 
ATOM   2686 C CG  . PRO A 1 332 ? -0.18676  -9.83458  41.51664 1.000 33.12456 ? 326 PRO A CG  1 
ATOM   2687 C CD  . PRO A 1 332 ? -1.16066  -10.26853 40.40427 1.000 32.66950 ? 326 PRO A CD  1 
ATOM   2688 N N   . PHE A 1 333 ? 0.65211   -5.99343  39.14706 1.000 27.65201 ? 327 PHE A N   1 
ATOM   2689 C CA  . PHE A 1 333 ? 1.47863   -5.26237  38.17489 1.000 29.58077 ? 327 PHE A CA  1 
ATOM   2690 C C   . PHE A 1 333 ? 2.94559   -5.56914  38.43350 1.000 32.66716 ? 327 PHE A C   1 
ATOM   2691 O O   . PHE A 1 333 ? 3.42538   -5.40465  39.56174 1.000 33.92975 ? 327 PHE A O   1 
ATOM   2692 C CB  . PHE A 1 333 ? 1.25792   -3.74713  38.25395 1.000 29.66081 ? 327 PHE A CB  1 
ATOM   2693 C CG  . PHE A 1 333 ? 0.03900   -3.29525  37.52343 1.000 29.34705 ? 327 PHE A CG  1 
ATOM   2694 C CD1 . PHE A 1 333 ? 0.08793   -3.07454  36.15615 1.000 29.98033 ? 327 PHE A CD1 1 
ATOM   2695 C CD2 . PHE A 1 333 ? -1.13641  -3.17527  38.15952 1.000 28.84849 ? 327 PHE A CD2 1 
ATOM   2696 C CE1 . PHE A 1 333 ? -1.06009  -2.67629  35.45232 1.000 29.91834 ? 327 PHE A CE1 1 
ATOM   2697 C CE2 . PHE A 1 333 ? -2.25959  -2.79920  37.47883 1.000 28.79812 ? 327 PHE A CE2 1 
ATOM   2698 C CZ  . PHE A 1 333 ? -2.22271  -2.54452  36.13110 1.000 29.72783 ? 327 PHE A CZ  1 
ATOM   2699 N N   . LYS A 1 334 ? 3.66256   -6.00924  37.38393 0.500 34.09686 ? 328 LYS A N   1 
ATOM   2700 C CA  . LYS A 1 334 ? 4.98914   -6.60922  37.55840 0.500 35.97996 ? 328 LYS A CA  1 
ATOM   2701 C C   . LYS A 1 334 ? 6.08197   -5.56645  37.78821 0.500 37.77960 ? 328 LYS A C   1 
ATOM   2702 O O   . LYS A 1 334 ? 6.88481   -5.70310  38.72165 0.500 39.09719 ? 328 LYS A O   1 
ATOM   2703 C CB  . LYS A 1 334 ? 5.32807   -7.48201  36.35440 0.500 35.85080 ? 328 LYS A CB  1 
ATOM   2704 N N   . PHE A 1 335 ? 6.14689   -4.52910  36.95672 0.500 38.05848 ? 329 PHE A N   1 
ATOM   2705 C CA  . PHE A 1 335 ? 7.07157   -3.41466  37.20565 0.500 38.24074 ? 329 PHE A CA  1 
ATOM   2706 C C   . PHE A 1 335 ? 6.48154   -2.07400  36.78616 0.500 38.26880 ? 329 PHE A C   1 
ATOM   2707 O O   . PHE A 1 335 ? 5.46508   -2.02424  36.10537 0.500 38.53081 ? 329 PHE A O   1 
ATOM   2708 C CB  . PHE A 1 335 ? 8.40057   -3.61646  36.48221 0.500 38.13185 ? 329 PHE A CB  1 
ATOM   2709 N N   . ASP A 1 340 ? 7.85471   3.88502   33.46377 1.000 65.08693 ? 334 ASP A N   1 
ATOM   2710 C CA  . ASP A 1 340 ? 8.36144   4.05568   32.10042 1.000 64.87251 ? 334 ASP A CA  1 
ATOM   2711 C C   . ASP A 1 340 ? 8.14902   5.50789   31.57263 1.000 64.45937 ? 334 ASP A C   1 
ATOM   2712 O O   . ASP A 1 340 ? 7.01726   5.92382   31.32972 1.000 64.24729 ? 334 ASP A O   1 
ATOM   2713 C CB  . ASP A 1 340 ? 7.69630   3.02324   31.17688 1.000 64.51666 ? 334 ASP A CB  1 
ATOM   2714 N N   . ASP A 1 341 ? 9.24760   6.26555   31.39946 1.000 63.86781 ? 335 ASP A N   1 
ATOM   2715 C CA  . ASP A 1 341 ? 9.21167   7.67138   30.97679 1.000 62.56751 ? 335 ASP A CA  1 
ATOM   2716 C C   . ASP A 1 341 ? 9.78691   7.83326   29.56209 1.000 60.64534 ? 335 ASP A C   1 
ATOM   2717 O O   . ASP A 1 341 ? 10.98262  7.58714   29.34013 1.000 60.21197 ? 335 ASP A O   1 
ATOM   2718 C CB  . ASP A 1 341 ? 9.96903   8.56519   31.96446 1.000 62.17565 ? 335 ASP A CB  1 
ATOM   2719 N N   . LEU A 1 342 ? 8.93446   8.31170   28.64538 1.000 57.88538 ? 336 LEU A N   1 
ATOM   2720 C CA  . LEU A 1 342 ? 9.17960   8.43831   27.21236 1.000 55.31884 ? 336 LEU A CA  1 
ATOM   2721 C C   . LEU A 1 342 ? 8.29333   9.56965   26.70295 1.000 51.91954 ? 336 LEU A C   1 
ATOM   2722 O O   . LEU A 1 342 ? 7.46241   10.09498  27.45252 1.000 50.36281 ? 336 LEU A O   1 
ATOM   2723 C CB  . LEU A 1 342 ? 8.89361   7.10949   26.49860 1.000 55.57430 ? 336 LEU A CB  1 
ATOM   2724 C CG  . LEU A 1 342 ? 7.67885   6.25778   26.83786 1.000 56.15396 ? 336 LEU A CG  1 
ATOM   2725 C CD1 . LEU A 1 342 ? 6.47399   6.83365   26.20452 1.000 57.00199 ? 336 LEU A CD1 1 
ATOM   2726 C CD2 . LEU A 1 342 ? 7.91224   4.83431   26.37247 1.000 56.65183 ? 336 LEU A CD2 1 
ATOM   2727 N N   . PRO A 1 343 ? 8.46432   10.01027  25.45214 1.000 50.64566 ? 337 PRO A N   1 
ATOM   2728 C CA  . PRO A 1 343 ? 7.93273   11.32738  25.09841 1.000 48.88300 ? 337 PRO A CA  1 
ATOM   2729 C C   . PRO A 1 343 ? 6.43073   11.29964  24.87570 1.000 46.82836 ? 337 PRO A C   1 
ATOM   2730 O O   . PRO A 1 343 ? 5.81518   10.26002  24.61632 1.000 45.41411 ? 337 PRO A O   1 
ATOM   2731 C CB  . PRO A 1 343 ? 8.67998   11.69657  23.81284 1.000 50.28537 ? 337 PRO A CB  1 
ATOM   2732 C CG  . PRO A 1 343 ? 9.20000   10.41263  23.26711 1.000 51.43027 ? 337 PRO A CG  1 
ATOM   2733 C CD  . PRO A 1 343 ? 8.84522   9.29848   24.21412 1.000 51.44581 ? 337 PRO A CD  1 
ATOM   2734 N N   . LYS A 1 344 ? 5.85769   12.49206  24.99738 1.000 45.10365 ? 338 LYS A N   1 
ATOM   2735 C CA  . LYS A 1 344 ? 4.42115   12.66262  24.93248 1.000 44.61421 ? 338 LYS A CA  1 
ATOM   2736 C C   . LYS A 1 344 ? 3.78607   12.08700  23.65950 1.000 42.40534 ? 338 LYS A C   1 
ATOM   2737 O O   . LYS A 1 344 ? 2.63361   11.62011  23.73506 1.000 41.42995 ? 338 LYS A O   1 
ATOM   2738 C CB  . LYS A 1 344 ? 4.10179   14.14523  25.11762 1.000 46.35744 ? 338 LYS A CB  1 
ATOM   2739 C CG  . LYS A 1 344 ? 4.71021   14.96341  24.04678 1.000 48.10515 ? 338 LYS A CG  1 
ATOM   2740 C CD  . LYS A 1 344 ? 4.36672   16.43028  24.13995 1.000 49.15058 ? 338 LYS A CD  1 
ATOM   2741 C CE  . LYS A 1 344 ? 5.27254   17.16256  23.09491 1.000 49.71622 ? 338 LYS A CE  1 
ATOM   2742 N NZ  . LYS A 1 344 ? 5.03295   16.68106  21.71031 1.000 49.98541 ? 338 LYS A NZ  1 
ATOM   2743 N N   . GLU A 1 345 ? 4.49649   12.07003  22.50916 1.000 40.95203 ? 339 GLU A N   1 
ATOM   2744 C CA  . GLU A 1 345 ? 3.86024   11.58696  21.28039 1.000 41.20902 ? 339 GLU A CA  1 
ATOM   2745 C C   . GLU A 1 345 ? 3.57140   10.10046  21.37952 1.000 40.64649 ? 339 GLU A C   1 
ATOM   2746 O O   . GLU A 1 345 ? 2.47835   9.63781   20.99674 1.000 39.62941 ? 339 GLU A O   1 
ATOM   2747 C CB  . GLU A 1 345 ? 4.69834   11.87551  20.02044 0.800 41.34902 ? 339 GLU A CB  1 
ATOM   2748 C CG  . GLU A 1 345 ? 4.85525   13.33953  19.72778 0.600 40.65758 ? 339 GLU A CG  1 
ATOM   2749 C CD  . GLU A 1 345 ? 6.01829   13.95742  20.47962 0.500 40.13046 ? 339 GLU A CD  1 
ATOM   2750 O OE1 . GLU A 1 345 ? 6.69807   13.27100  21.26532 0.500 38.93396 ? 339 GLU A OE1 1 
ATOM   2751 O OE2 . GLU A 1 345 ? 6.19322   15.16773  20.33120 0.500 41.59595 ? 339 GLU A OE2 1 
ATOM   2752 N N   . LYS A 1 346 ? 4.54023   9.33998   21.89028 1.000 39.69178 ? 340 LYS A N   1 
ATOM   2753 C CA  A LYS A 1 346 ? 4.28842   7.93051   22.12896 0.500 39.32384 ? 340 LYS A CA  1 
ATOM   2754 C CA  B LYS A 1 346 ? 4.30044   7.92793   22.13981 0.500 39.77344 ? 340 LYS A CA  1 
ATOM   2755 C C   . LYS A 1 346 ? 3.24008   7.73680   23.21038 1.000 39.25721 ? 340 LYS A C   1 
ATOM   2756 O O   . LYS A 1 346 ? 2.45997   6.80232   23.12279 1.000 39.90002 ? 340 LYS A O   1 
ATOM   2757 C CB  A LYS A 1 346 ? 5.58423   7.20705   22.47996 0.500 39.18828 ? 340 LYS A CB  1 
ATOM   2758 C CB  B LYS A 1 346 ? 5.59247   7.22141   22.54103 0.500 40.47687 ? 340 LYS A CB  1 
ATOM   2759 C CG  A LYS A 1 346 ? 6.63430   7.20530   21.36755 0.500 39.56463 ? 340 LYS A CG  1 
ATOM   2760 C CG  B LYS A 1 346 ? 5.42393   5.72106   22.76371 0.500 41.51678 ? 340 LYS A CG  1 
ATOM   2761 C CD  A LYS A 1 346 ? 6.11292   6.48860   20.13268 0.500 39.72647 ? 340 LYS A CD  1 
ATOM   2762 C CD  B LYS A 1 346 ? 5.20909   4.95722   21.45948 0.500 42.51434 ? 340 LYS A CD  1 
ATOM   2763 C CE  A LYS A 1 346 ? 7.16903   6.44805   19.04316 0.500 40.36904 ? 340 LYS A CE  1 
ATOM   2764 C CE  B LYS A 1 346 ? 4.85248   3.50407   21.71419 0.500 43.06976 ? 340 LYS A CE  1 
ATOM   2765 N NZ  A LYS A 1 346 ? 6.72296   5.68216   17.84258 0.500 40.94435 ? 340 LYS A NZ  1 
ATOM   2766 N NZ  B LYS A 1 346 ? 5.83579   2.90248   22.63501 0.500 43.62084 ? 340 LYS A NZ  1 
ATOM   2767 N N   . LEU A 1 347 ? 3.19743   8.62601   24.21378 1.000 38.26081 ? 341 LEU A N   1 
ATOM   2768 C CA  . LEU A 1 347 ? 2.23319   8.49096   25.31338 1.000 36.90036 ? 341 LEU A CA  1 
ATOM   2769 C C   . LEU A 1 347 ? 0.81672   8.80601   24.84631 1.000 36.38924 ? 341 LEU A C   1 
ATOM   2770 O O   . LEU A 1 347 ? -0.15613  8.18996   25.31239 1.000 36.34821 ? 341 LEU A O   1 
ATOM   2771 C CB  . LEU A 1 347 ? 2.59986   9.42909   26.46059 0.800 36.48078 ? 341 LEU A CB  1 
ATOM   2772 C CG  . LEU A 1 347 ? 3.88795   9.25146   27.27211 0.700 36.88670 ? 341 LEU A CG  1 
ATOM   2773 C CD1 . LEU A 1 347 ? 3.99147   10.32279  28.34218 0.700 36.46552 ? 341 LEU A CD1 1 
ATOM   2774 C CD2 . LEU A 1 347 ? 3.85694   7.90724   27.97359 0.700 37.90673 ? 341 LEU A CD2 1 
ATOM   2775 N N   . LYS A 1 348 ? 0.67723   9.80480   23.97092 1.000 36.77129 ? 342 LYS A N   1 
ATOM   2776 C CA  . LYS A 1 348 ? -0.63605  10.05647  23.37925 1.000 36.67761 ? 342 LYS A CA  1 
ATOM   2777 C C   . LYS A 1 348 ? -1.10555  8.83624   22.61984 1.000 37.45053 ? 342 LYS A C   1 
ATOM   2778 O O   . LYS A 1 348 ? -2.29340  8.45548   22.67745 1.000 36.15411 ? 342 LYS A O   1 
ATOM   2779 C CB  . LYS A 1 348 ? -0.58854  11.27098  22.44728 1.000 37.14948 ? 342 LYS A CB  1 
ATOM   2780 C CG  . LYS A 1 348 ? -1.96578  11.57861  21.79143 1.000 37.07234 ? 342 LYS A CG  1 
ATOM   2781 C CD  . LYS A 1 348 ? -2.00619  12.90175  21.00649 1.000 37.03718 ? 342 LYS A CD  1 
ATOM   2782 C CE  . LYS A 1 348 ? -3.47223  13.22360  20.62001 1.000 37.04090 ? 342 LYS A CE  1 
ATOM   2783 N NZ  . LYS A 1 348 ? -3.55583  14.41660  19.73118 1.000 37.21063 ? 342 LYS A NZ  1 
ATOM   2784 N N   . GLU A 1 349 ? -0.18184  8.23007   21.87959 1.000 38.39474 ? 343 GLU A N   1 
ATOM   2785 C CA  . GLU A 1 349 ? -0.45891  7.00884   21.14530 1.000 39.12693 ? 343 GLU A CA  1 
ATOM   2786 C C   . GLU A 1 349 ? -0.87506  5.89621   22.10517 1.000 37.42017 ? 343 GLU A C   1 
ATOM   2787 O O   . GLU A 1 349 ? -1.87073  5.18856   21.87525 1.000 36.84147 ? 343 GLU A O   1 
ATOM   2788 C CB  . GLU A 1 349 ? 0.80077   6.67552   20.32890 1.000 42.32078 ? 343 GLU A CB  1 
ATOM   2789 C CG  . GLU A 1 349 ? 0.72674   5.49261   19.42137 0.800 44.57922 ? 343 GLU A CG  1 
ATOM   2790 C CD  . GLU A 1 349 ? 2.01091   5.27798   18.62553 0.700 46.33066 ? 343 GLU A CD  1 
ATOM   2791 O OE1 . GLU A 1 349 ? 2.98640   6.03885   18.81251 0.600 46.23129 ? 343 GLU A OE1 1 
ATOM   2792 O OE2 . GLU A 1 349 ? 2.03418   4.34487   17.80167 0.600 47.89456 ? 343 GLU A OE2 1 
ATOM   2793 N N   . LEU A 1 350 ? -0.18186  5.80045   23.24502 1.000 36.04968 ? 344 LEU A N   1 
ATOM   2794 C CA  . LEU A 1 350 ? -0.50159  4.78128   24.23440 1.000 34.63883 ? 344 LEU A CA  1 
ATOM   2795 C C   . LEU A 1 350 ? -1.85945  5.04156   24.87606 1.000 32.79415 ? 344 LEU A C   1 
ATOM   2796 O O   . LEU A 1 350 ? -2.62526  4.10166   25.13398 1.000 34.52608 ? 344 LEU A O   1 
ATOM   2797 C CB  . LEU A 1 350 ? 0.59830   4.73096   25.28919 1.000 35.20044 ? 344 LEU A CB  1 
ATOM   2798 C CG  . LEU A 1 350 ? 1.92800   4.22831   24.68439 1.000 37.30566 ? 344 LEU A CG  1 
ATOM   2799 C CD1 . LEU A 1 350 ? 2.97864   4.06251   25.75584 1.000 37.53524 ? 344 LEU A CD1 1 
ATOM   2800 C CD2 . LEU A 1 350 ? 1.69966   2.93281   23.93967 1.000 38.38798 ? 344 LEU A CD2 1 
ATOM   2801 N N   . ILE A 1 351 ? -2.19180  6.30683   25.12611 1.000 30.94476 ? 345 ILE A N   1 
ATOM   2802 C CA  . ILE A 1 351 ? -3.52108  6.61358   25.67807 1.000 28.32603 ? 345 ILE A CA  1 
ATOM   2803 C C   . ILE A 1 351 ? -4.60913  6.31927   24.65341 1.000 27.78131 ? 345 ILE A C   1 
ATOM   2804 O O   . ILE A 1 351 ? -5.68933  5.82819   24.99563 1.000 27.14197 ? 345 ILE A O   1 
ATOM   2805 C CB  . ILE A 1 351 ? -3.55406  8.08163   26.14822 1.000 27.82468 ? 345 ILE A CB  1 
ATOM   2806 C CG1 . ILE A 1 351 ? -2.64059  8.22170   27.39244 1.000 29.25819 ? 345 ILE A CG1 1 
ATOM   2807 C CG2 . ILE A 1 351 ? -5.02338  8.57473   26.38497 1.000 26.80985 ? 345 ILE A CG2 1 
ATOM   2808 C CD1 . ILE A 1 351 ? -2.28620  9.61692   27.77046 1.000 29.50049 ? 345 ILE A CD1 1 
ATOM   2809 N N   . PHE A 1 352 ? -4.35364  6.62973   23.38077 1.000 27.71119 ? 346 PHE A N   1 
ATOM   2810 C CA  . PHE A 1 352 ? -5.32263  6.29135   22.34374 1.000 26.78723 ? 346 PHE A CA  1 
ATOM   2811 C C   . PHE A 1 352 ? -5.57437  4.77809   22.30526 1.000 27.23505 ? 346 PHE A C   1 
ATOM   2812 O O   . PHE A 1 352 ? -6.72511  4.31588   22.20182 1.000 27.97532 ? 346 PHE A O   1 
ATOM   2813 C CB  . PHE A 1 352 ? -4.80149  6.81797   20.97911 1.000 27.17749 ? 346 PHE A CB  1 
ATOM   2814 C CG  . PHE A 1 352 ? -5.75977  6.64895   19.84268 1.000 26.04502 ? 346 PHE A CG  1 
ATOM   2815 C CD1 . PHE A 1 352 ? -6.74766  7.57813   19.60607 1.000 26.31675 ? 346 PHE A CD1 1 
ATOM   2816 C CD2 . PHE A 1 352 ? -5.60833  5.58583   18.95816 1.000 26.42034 ? 346 PHE A CD2 1 
ATOM   2817 C CE1 . PHE A 1 352 ? -7.63340  7.42723   18.49651 1.000 26.92275 ? 346 PHE A CE1 1 
ATOM   2818 C CE2 . PHE A 1 352 ? -6.46138  5.41754   17.86974 1.000 26.80385 ? 346 PHE A CE2 1 
ATOM   2819 C CZ  . PHE A 1 352 ? -7.49447  6.34762   17.63418 1.000 27.15634 ? 346 PHE A CZ  1 
ATOM   2820 N N   . GLU A 1 353 ? -4.50377  3.98923   22.34111 1.000 28.33329 ? 347 GLU A N   1 
ATOM   2821 C CA  . GLU A 1 353 ? -4.63667  2.54496   22.27727 1.000 30.72438 ? 347 GLU A CA  1 
ATOM   2822 C C   . GLU A 1 353 ? -5.31613  1.97745   23.51189 1.000 29.89167 ? 347 GLU A C   1 
ATOM   2823 O O   . GLU A 1 353 ? -6.15813  1.07861   23.39139 1.000 31.08093 ? 347 GLU A O   1 
ATOM   2824 C CB  . GLU A 1 353 ? -3.24202  1.90474   22.07107 1.000 33.43076 ? 347 GLU A CB  1 
ATOM   2825 C CG  . GLU A 1 353 ? -2.70151  2.11650   20.67320 1.000 36.48618 ? 347 GLU A CG  1 
ATOM   2826 C CD  . GLU A 1 353 ? -1.30442  1.51983   20.45012 0.700 38.62927 ? 347 GLU A CD  1 
ATOM   2827 O OE1 . GLU A 1 353 ? -0.61486  1.16095   21.43713 0.600 39.46374 ? 347 GLU A OE1 1 
ATOM   2828 O OE2 . GLU A 1 353 ? -0.89612  1.38487   19.27036 0.600 39.82519 ? 347 GLU A OE2 1 
ATOM   2829 N N   . GLU A 1 354 ? -4.98672  2.49711   24.70973 1.000 29.17490 ? 348 GLU A N   1 
ATOM   2830 C CA  . GLU A 1 354 ? -5.58204  1.97165   25.93538 1.000 29.22982 ? 348 GLU A CA  1 
ATOM   2831 C C   . GLU A 1 354 ? -7.06222  2.28488   26.01250 1.000 27.84740 ? 348 GLU A C   1 
ATOM   2832 O O   . GLU A 1 354 ? -7.79317  1.59509   26.74226 1.000 28.80827 ? 348 GLU A O   1 
ATOM   2833 C CB  . GLU A 1 354 ? -4.86499  2.53335   27.17672 1.000 31.02313 ? 348 GLU A CB  1 
ATOM   2834 C CG  . GLU A 1 354 ? -3.57706  1.84676   27.57500 0.800 34.40514 ? 348 GLU A CG  1 
ATOM   2835 C CD  . GLU A 1 354 ? -3.74136  0.40748   27.99027 0.750 36.16426 ? 348 GLU A CD  1 
ATOM   2836 O OE1 . GLU A 1 354 ? -4.50584  0.09148   28.91116 0.750 37.32630 ? 348 GLU A OE1 1 
ATOM   2837 O OE2 . GLU A 1 354 ? -3.11669  -0.42080  27.34681 0.750 37.35055 ? 348 GLU A OE2 1 
ATOM   2838 N N   . THR A 1 355 ? -7.52703  3.30473   25.28957 1.000 24.70541 ? 349 THR A N   1 
ATOM   2839 C CA  . THR A 1 355 ? -8.93048  3.69972   25.36217 1.000 24.21783 ? 349 THR A CA  1 
ATOM   2840 C C   . THR A 1 355 ? -9.75737  3.17590   24.21462 1.000 25.45034 ? 349 THR A C   1 
ATOM   2841 O O   . THR A 1 355 ? -10.97910 3.42166   24.18252 1.000 25.15571 ? 349 THR A O   1 
ATOM   2842 C CB  . THR A 1 355 ? -9.04748  5.22571   25.44390 1.000 23.28977 ? 349 THR A CB  1 
ATOM   2843 O OG1 . THR A 1 355 ? -8.40699  5.82772   24.30369 1.000 23.73430 ? 349 THR A OG1 1 
ATOM   2844 C CG2 . THR A 1 355 ? -8.39451  5.71888   26.77389 1.000 22.71867 ? 349 THR A CG2 1 
ATOM   2845 N N   . ALA A 1 356 ? -9.14730  2.39130   23.31868 1.000 26.89439 ? 350 ALA A N   1 
ATOM   2846 C CA  . ALA A 1 356 ? -9.84098  1.91613   22.13364 1.000 28.56471 ? 350 ALA A CA  1 
ATOM   2847 C C   . ALA A 1 356 ? -11.04160 1.02696   22.43787 1.000 30.35045 ? 350 ALA A C   1 
ATOM   2848 O O   . ALA A 1 356 ? -11.98264 0.99625   21.63452 1.000 29.82065 ? 350 ALA A O   1 
ATOM   2849 C CB  . ALA A 1 356 ? -8.85028  1.18220   21.23285 1.000 28.02040 ? 350 ALA A CB  1 
ATOM   2850 N N   . ARG A 1 357 ? -11.05866 0.32476   23.58304 1.000 31.44502 ? 351 ARG A N   1 
ATOM   2851 C CA  . ARG A 1 357 ? -12.07878 -0.68815  23.80658 1.000 31.87882 ? 351 ARG A CA  1 
ATOM   2852 C C   . ARG A 1 357 ? -13.45984 -0.07151  23.97233 1.000 31.33834 ? 351 ARG A C   1 
ATOM   2853 O O   . ARG A 1 357 ? -14.46686 -0.78888  23.88633 1.000 32.24855 ? 351 ARG A O   1 
ATOM   2854 C CB  . ARG A 1 357 ? -11.70381 -1.55104  25.03866 0.800 32.09341 ? 351 ARG A CB  1 
ATOM   2855 C CG  . ARG A 1 357 ? -11.86473 -0.82102  26.37774 0.700 32.29066 ? 351 ARG A CG  1 
ATOM   2856 C CD  . ARG A 1 357 ? -11.71414 -1.72321  27.61021 0.700 33.42094 ? 351 ARG A CD  1 
ATOM   2857 N NE  . ARG A 1 357 ? -10.31157 -2.00080  27.88452 0.600 33.77410 ? 351 ARG A NE  1 
ATOM   2858 C CZ  . ARG A 1 357 ? -9.86236  -2.59081  28.99054 0.600 34.49465 ? 351 ARG A CZ  1 
ATOM   2859 N NH1 . ARG A 1 357 ? -10.67911 -2.91628  29.98421 0.600 35.40026 ? 351 ARG A NH1 1 
ATOM   2860 N NH2 . ARG A 1 357 ? -8.56012  -2.84994  29.10790 0.600 33.80756 ? 351 ARG A NH2 1 
ATOM   2861 N N   . PHE A 1 358 ? -13.53241 1.22987   24.21896 1.000 28.54866 ? 352 PHE A N   1 
ATOM   2862 C CA  . PHE A 1 358 ? -14.80360 1.87650   24.48539 1.000 26.96205 ? 352 PHE A CA  1 
ATOM   2863 C C   . PHE A 1 358 ? -15.39384 2.50045   23.24202 1.000 27.32533 ? 352 PHE A C   1 
ATOM   2864 O O   . PHE A 1 358 ? -16.46939 3.11219   23.31903 1.000 27.66562 ? 352 PHE A O   1 
ATOM   2865 C CB  . PHE A 1 358 ? -14.64234 2.93034   25.58709 1.000 25.73443 ? 352 PHE A CB  1 
ATOM   2866 C CG  . PHE A 1 358 ? -14.23199 2.33607   26.91522 1.000 26.63914 ? 352 PHE A CG  1 
ATOM   2867 C CD1 . PHE A 1 358 ? -15.18907 1.81156   27.74764 1.000 27.33483 ? 352 PHE A CD1 1 
ATOM   2868 C CD2 . PHE A 1 358 ? -12.90642 2.30125   27.31864 1.000 27.78451 ? 352 PHE A CD2 1 
ATOM   2869 C CE1 . PHE A 1 358 ? -14.86000 1.25552   28.95743 1.000 28.74662 ? 352 PHE A CE1 1 
ATOM   2870 C CE2 . PHE A 1 358 ? -12.55596 1.73256   28.52255 1.000 29.09484 ? 352 PHE A CE2 1 
ATOM   2871 C CZ  . PHE A 1 358 ? -13.52703 1.22173   29.36567 1.000 29.45799 ? 352 PHE A CZ  1 
ATOM   2872 N N   . GLN A 1 359 ? -14.72227 2.37830   22.11598 1.000 27.32326 ? 353 GLN A N   1 
ATOM   2873 C CA  . GLN A 1 359 ? -15.31018 2.96012   20.89902 1.000 29.96693 ? 353 GLN A CA  1 
ATOM   2874 C C   . GLN A 1 359 ? -16.44534 2.08074   20.36902 1.000 34.30757 ? 353 GLN A C   1 
ATOM   2875 O O   . GLN A 1 359 ? -16.34104 0.84857   20.40544 1.000 36.52401 ? 353 GLN A O   1 
ATOM   2876 C CB  . GLN A 1 359 ? -14.22968 3.13645   19.81645 1.000 27.83741 ? 353 GLN A CB  1 
ATOM   2877 C CG  . GLN A 1 359 ? -13.17854 4.23492   20.18092 1.000 25.38207 ? 353 GLN A CG  1 
ATOM   2878 C CD  . GLN A 1 359 ? -13.83998 5.61139   20.32003 1.000 25.04849 ? 353 GLN A CD  1 
ATOM   2879 O OE1 . GLN A 1 359 ? -13.82508 6.26131   21.40622 1.000 26.64433 ? 353 GLN A OE1 1 
ATOM   2880 N NE2 . GLN A 1 359 ? -14.49380 6.02644   19.26609 1.000 22.72594 ? 353 GLN A NE2 1 
ATOM   2881 N N   . PRO A 1 360 ? -17.51236 2.68774   19.80472 0.700 35.09103 ? 354 PRO A N   1 
ATOM   2882 C CA  . PRO A 1 360 ? -18.60744 1.96723   19.13211 0.700 36.37178 ? 354 PRO A CA  1 
ATOM   2883 C C   . PRO A 1 360 ? -18.17655 1.21379   17.84715 0.700 37.00283 ? 354 PRO A C   1 
ATOM   2884 O O   . PRO A 1 360 ? -17.32340 0.29905   17.86986 0.700 37.76878 ? 354 PRO A O   1 
ATOM   2885 C CB  . PRO A 1 360 ? -19.59847 3.09871   18.78782 0.700 36.37148 ? 354 PRO A CB  1 
ATOM   2886 C CG  . PRO A 1 360 ? -19.24314 4.22918   19.70140 0.700 36.14974 ? 354 PRO A CG  1 
ATOM   2887 C CD  . PRO A 1 360 ? -17.76499 4.14000   19.85014 0.700 35.15855 ? 354 PRO A CD  1 
HETATM 2888 S S   A SO4 B 2 .   ? 3.92034   20.93145  49.81691 0.300 15.89623 ? 401 SO4 A S   1 
HETATM 2889 S S   B SO4 B 2 .   ? 6.06009   20.96951  49.57976 0.500 24.33418 ? 401 SO4 A S   1 
HETATM 2890 O O1  A SO4 B 2 .   ? 4.75949   22.08509  49.52543 0.300 16.04797 ? 401 SO4 A O1  1 
HETATM 2891 O O1  B SO4 B 2 .   ? 7.27831   21.82960  49.51701 0.500 23.38159 ? 401 SO4 A O1  1 
HETATM 2892 O O2  A SO4 B 2 .   ? 4.24599   19.81182  48.93675 0.300 15.94457 ? 401 SO4 A O2  1 
HETATM 2893 O O2  B SO4 B 2 .   ? 6.21393   19.76923  48.73603 0.500 23.32900 ? 401 SO4 A O2  1 
HETATM 2894 O O3  A SO4 B 2 .   ? 2.55603   21.41197  49.56248 0.300 16.05020 ? 401 SO4 A O3  1 
HETATM 2895 O O3  B SO4 B 2 .   ? 4.89593   21.74758  49.14000 0.500 24.36448 ? 401 SO4 A O3  1 
HETATM 2896 O O4  A SO4 B 2 .   ? 4.10589   20.51078  51.21866 0.300 15.94159 ? 401 SO4 A O4  1 
HETATM 2897 O O4  B SO4 B 2 .   ? 5.78402   20.48702  50.91530 0.500 24.56796 ? 401 SO4 A O4  1 
HETATM 2898 S S   . SO4 C 2 .   ? 7.32686   10.41276  41.69589 1.000 72.46705 ? 402 SO4 A S   1 
HETATM 2899 O O1  . SO4 C 2 .   ? 8.23243   9.76871   40.72658 1.000 72.81782 ? 402 SO4 A O1  1 
HETATM 2900 O O2  . SO4 C 2 .   ? 6.99759   11.77961  41.27208 1.000 72.42193 ? 402 SO4 A O2  1 
HETATM 2901 O O3  . SO4 C 2 .   ? 6.08231   9.66652   41.83226 1.000 72.23935 ? 402 SO4 A O3  1 
HETATM 2902 O O4  . SO4 C 2 .   ? 7.96222   10.39338  43.02040 1.000 73.53358 ? 402 SO4 A O4  1 
HETATM 2903 C C1  . WN2 D 3 .   ? -14.33031 11.78993  39.18936 1.000 23.04835 ? 403 WN2 A C1  1 
HETATM 2904 C C2  . WN2 D 3 .   ? -14.18191 11.51099  40.67532 1.000 22.71608 ? 403 WN2 A C2  1 
HETATM 2905 C C3  . WN2 D 3 .   ? -12.81944 11.94050  41.24439 1.000 22.30320 ? 403 WN2 A C3  1 
HETATM 2906 C C4  . WN2 D 3 .   ? -12.51242 11.51420  42.69154 1.000 23.78583 ? 403 WN2 A C4  1 
HETATM 2907 C C5  . WN2 D 3 .   ? -11.82089 12.56752  43.55758 1.000 25.28664 ? 403 WN2 A C5  1 
HETATM 2908 C C6  . WN2 D 3 .   ? -12.78005 13.57753  44.14415 1.000 28.33618 ? 403 WN2 A C6  1 
HETATM 2909 C C7  . WN2 D 3 .   ? -12.30888 14.98872  44.48943 1.000 29.04764 ? 403 WN2 A C7  1 
HETATM 2910 C C8  . WN2 D 3 .   ? -13.36657 16.02181  44.06498 1.000 30.49854 ? 403 WN2 A C8  1 
HETATM 2911 C C9  . WN2 D 3 .   ? -13.40142 16.20006  42.53654 1.000 30.14308 ? 403 WN2 A C9  1 
HETATM 2912 C C10 . WN2 D 3 .   ? -14.61960 16.92914  42.02231 1.000 31.46512 ? 403 WN2 A C10 1 
HETATM 2913 C C11 . WN2 D 3 .   ? -15.93953 16.30179  42.45056 1.000 31.95296 ? 403 WN2 A C11 1 
HETATM 2914 O O1  . WN2 D 3 .   ? -13.94651 13.29834  44.36121 1.000 30.12839 ? 403 WN2 A O1  1 
HETATM 2915 O O2  . WN2 D 3 .   ? -11.03270 15.24331  43.94979 1.000 29.35188 ? 403 WN2 A O2  1 
HETATM 2916 O O3  . WN2 D 3 .   ? -13.10412 17.29943  44.67826 1.000 31.40541 ? 403 WN2 A O3  1 
HETATM 2917 C C12 . WN2 D 3 .   ? -15.99909 14.85628  42.04249 1.000 31.85442 ? 403 WN2 A C12 1 
HETATM 2918 C C13 . WN2 D 3 .   ? -17.32880 14.15445  42.28885 1.000 30.80891 ? 403 WN2 A C13 1 
HETATM 2919 O O4  . WN2 D 3 .   ? -20.70772 14.96164  43.55589 1.000 34.04570 ? 403 WN2 A O4  1 
HETATM 2920 O O5  . WN2 D 3 .   ? -18.99404 10.90067  41.92678 1.000 27.15009 ? 403 WN2 A O5  1 
HETATM 2921 C C14 . WN2 D 3 .   ? -18.41435 14.86820  42.81236 1.000 30.25720 ? 403 WN2 A C14 1 
HETATM 2922 C C15 . WN2 D 3 .   ? -19.64860 14.25892  43.02740 1.000 31.43806 ? 403 WN2 A C15 1 
HETATM 2923 C C16 . WN2 D 3 .   ? -19.80726 12.91666  42.75111 1.000 30.10291 ? 403 WN2 A C16 1 
HETATM 2924 C C17 . WN2 D 3 .   ? -18.75209 12.20252  42.20863 1.000 27.84552 ? 403 WN2 A C17 1 
HETATM 2925 C C18 . WN2 D 3 .   ? -17.49611 12.78408  41.96912 1.000 28.56023 ? 403 WN2 A C18 1 
HETATM 2926 C C19 . WN2 D 3 .   ? -16.46792 11.86016  41.40450 1.000 25.34917 ? 403 WN2 A C19 1 
HETATM 2927 O O6  . WN2 D 3 .   ? -16.76926 10.77264  40.98249 1.000 23.95984 ? 403 WN2 A O6  1 
HETATM 2928 O O7  . WN2 D 3 .   ? -15.19229 12.27285  41.42247 1.000 24.72332 ? 403 WN2 A O7  1 
HETATM 2929 O O   . HOH E 4 .   ? 10.88119  1.98830   41.07968 1.000 52.70014 ? 501 HOH A O   1 
HETATM 2930 O O   . HOH E 4 .   ? 6.18215   -4.26453  56.84693 1.000 39.39839 ? 502 HOH A O   1 
HETATM 2931 O O   . HOH E 4 .   ? -2.54223  15.81014  42.30611 1.000 57.59750 ? 503 HOH A O   1 
HETATM 2932 O O   . HOH E 4 .   ? -5.65636  11.76022  38.50017 1.000 35.00657 ? 504 HOH A O   1 
HETATM 2933 O O   . HOH E 4 .   ? -9.33194  18.18600  55.80412 1.000 51.45105 ? 505 HOH A O   1 
HETATM 2934 O O   . HOH E 4 .   ? 7.63989   17.33726  75.48237 1.000 51.58691 ? 506 HOH A O   1 
HETATM 2935 O O   . HOH E 4 .   ? 12.20406  -3.30699  44.78207 1.000 45.11291 ? 507 HOH A O   1 
HETATM 2936 O O   . HOH E 4 .   ? -20.39434 19.60902  54.59803 1.000 48.55619 ? 508 HOH A O   1 
HETATM 2937 O O   . HOH E 4 .   ? 8.43019   19.11996  47.86373 1.000 56.29643 ? 509 HOH A O   1 
HETATM 2938 O O   . HOH E 4 .   ? -20.00258 0.16736   62.31274 1.000 34.43728 ? 510 HOH A O   1 
HETATM 2939 O O   . HOH E 4 .   ? -24.73113 3.89335   64.96496 1.000 45.29299 ? 511 HOH A O   1 
HETATM 2940 O O   . HOH E 4 .   ? -13.46153 17.77645  23.80863 1.000 37.93862 ? 512 HOH A O   1 
HETATM 2941 O O   . HOH E 4 .   ? 1.05077   9.79181   70.26545 1.000 35.06115 ? 513 HOH A O   1 
HETATM 2942 O O   . HOH E 4 .   ? 9.48478   9.62707   44.89300 1.000 31.03733 ? 514 HOH A O   1 
HETATM 2943 O O   . HOH E 4 .   ? -10.02265 -11.48196 43.17911 1.000 50.02347 ? 515 HOH A O   1 
HETATM 2944 O O   . HOH E 4 .   ? -17.49204 19.23827  44.53890 1.000 51.74942 ? 516 HOH A O   1 
HETATM 2945 O O   . HOH E 4 .   ? -3.66792  -12.07756 50.79454 1.000 42.10724 ? 517 HOH A O   1 
HETATM 2946 O O   . HOH E 4 .   ? -25.10158 12.84133  54.43292 1.000 47.68557 ? 518 HOH A O   1 
HETATM 2947 O O   . HOH E 4 .   ? -14.95883 8.49793   18.82095 1.000 35.47723 ? 519 HOH A O   1 
HETATM 2948 O O   . HOH E 4 .   ? -19.08353 -0.35222  64.52465 1.000 46.72398 ? 520 HOH A O   1 
HETATM 2949 O O   . HOH E 4 .   ? 12.83985  15.35466  69.00183 1.000 25.80573 ? 521 HOH A O   1 
HETATM 2950 O O   . HOH E 4 .   ? 0.80559   14.15150  23.49364 1.000 46.06088 ? 522 HOH A O   1 
HETATM 2951 O O   . HOH E 4 .   ? -2.13697  15.36551  44.61735 1.000 48.31227 ? 523 HOH A O   1 
HETATM 2952 O O   . HOH E 4 .   ? -16.43037 14.64093  45.66291 1.000 34.70329 ? 524 HOH A O   1 
HETATM 2953 O O   . HOH E 4 .   ? -4.94101  -1.90903  31.93957 1.000 50.06700 ? 525 HOH A O   1 
HETATM 2954 O O   . HOH E 4 .   ? 8.55865   3.53703   65.55126 1.000 17.98826 ? 526 HOH A O   1 
HETATM 2955 O O   . HOH E 4 .   ? 11.14070  19.08513  62.53095 1.000 34.18435 ? 527 HOH A O   1 
HETATM 2956 O O   . HOH E 4 .   ? -7.56734  -1.52546  27.08479 1.000 58.87264 ? 528 HOH A O   1 
HETATM 2957 O O   . HOH E 4 .   ? -33.11280 8.77309   26.45178 1.000 54.75272 ? 529 HOH A O   1 
HETATM 2958 O O   . HOH E 4 .   ? -11.02551 13.62655  21.99537 1.000 25.78188 ? 530 HOH A O   1 
HETATM 2959 O O   . HOH E 4 .   ? 10.47063  5.75175   68.20332 1.000 21.31989 ? 531 HOH A O   1 
HETATM 2960 O O   . HOH E 4 .   ? 15.46064  11.18536  45.28532 1.000 53.68088 ? 532 HOH A O   1 
HETATM 2961 O O   . HOH E 4 .   ? -13.49025 -6.29418  69.09114 1.000 41.84045 ? 533 HOH A O   1 
HETATM 2962 O O   . HOH E 4 .   ? -16.24377 13.07189  63.40222 1.000 28.73178 ? 534 HOH A O   1 
HETATM 2963 O O   . HOH E 4 .   ? -19.47190 -6.29518  50.32083 1.000 50.05335 ? 535 HOH A O   1 
HETATM 2964 O O   . HOH E 4 .   ? 11.98986  1.79672   69.48191 1.000 38.80269 ? 536 HOH A O   1 
HETATM 2965 O O   . HOH E 4 .   ? -26.56785 5.43109   47.64075 1.000 55.61938 ? 537 HOH A O   1 
HETATM 2966 O O   . HOH E 4 .   ? -15.77799 -3.78383  64.82416 1.000 28.23116 ? 538 HOH A O   1 
HETATM 2967 O O   . HOH E 4 .   ? 8.37066   6.07780   40.80158 1.000 60.94985 ? 539 HOH A O   1 
HETATM 2968 O O   . HOH E 4 .   ? -8.63911  -0.56417  24.18494 1.000 50.97320 ? 540 HOH A O   1 
HETATM 2969 O O   . HOH E 4 .   ? -8.86770  14.77263  45.72656 1.000 27.60407 ? 541 HOH A O   1 
HETATM 2970 O O   . HOH E 4 .   ? -10.77753 5.11606   17.28693 1.000 30.17800 ? 542 HOH A O   1 
HETATM 2971 O O   . HOH E 4 .   ? -15.64213 -10.59646 48.23609 1.000 34.38271 ? 543 HOH A O   1 
HETATM 2972 O O   . HOH E 4 .   ? -12.59049 -0.02426  35.93500 1.000 25.16920 ? 544 HOH A O   1 
HETATM 2973 O O   . HOH E 4 .   ? -7.84718  -9.72291  55.01194 1.000 22.09959 ? 545 HOH A O   1 
HETATM 2974 O O   . HOH E 4 .   ? 2.76684   6.06886   67.16687 1.000 28.51555 ? 546 HOH A O   1 
HETATM 2975 O O   . HOH E 4 .   ? -14.55884 -10.83664 62.49042 1.000 29.65945 ? 547 HOH A O   1 
HETATM 2976 O O   . HOH E 4 .   ? -16.06365 15.75585  65.98764 1.000 56.62393 ? 548 HOH A O   1 
HETATM 2977 O O   . HOH E 4 .   ? -3.71088  -5.91437  68.32563 1.000 38.47329 ? 549 HOH A O   1 
HETATM 2978 O O   . HOH E 4 .   ? -16.97919 0.30932   36.11268 1.000 59.33581 ? 550 HOH A O   1 
HETATM 2979 O O   . HOH E 4 .   ? 7.76780   4.15559   53.80338 1.000 21.81352 ? 551 HOH A O   1 
HETATM 2980 O O   . HOH E 4 .   ? -24.46438 17.84377  61.17626 1.000 48.79305 ? 552 HOH A O   1 
HETATM 2981 O O   . HOH E 4 .   ? -8.02304  17.21898  53.70291 1.000 28.63551 ? 553 HOH A O   1 
HETATM 2982 O O   . HOH E 4 .   ? -5.41863  13.13346  44.32122 1.000 29.51967 ? 554 HOH A O   1 
HETATM 2983 O O   . HOH E 4 .   ? -0.60727  24.56513  61.24673 1.000 42.40218 ? 555 HOH A O   1 
HETATM 2984 O O   . HOH E 4 .   ? -16.68035 -7.42036  53.76984 1.000 26.86152 ? 556 HOH A O   1 
HETATM 2985 O O   . HOH E 4 .   ? -13.61184 17.47319  47.53376 1.000 34.46279 ? 557 HOH A O   1 
HETATM 2986 O O   . HOH E 4 .   ? -17.88524 -7.85526  56.38866 1.000 33.06733 ? 558 HOH A O   1 
HETATM 2987 O O   . HOH E 4 .   ? -10.69725 -7.44017  62.87231 1.000 18.64960 ? 559 HOH A O   1 
HETATM 2988 O O   . HOH E 4 .   ? -18.41533 2.76109   25.39234 1.000 46.03460 ? 560 HOH A O   1 
HETATM 2989 O O   . HOH E 4 .   ? -11.21660 18.95146  43.67847 1.000 48.51494 ? 561 HOH A O   1 
HETATM 2990 O O   . HOH E 4 .   ? 12.01109  8.35226   72.36222 1.000 38.22863 ? 562 HOH A O   1 
HETATM 2991 O O   . HOH E 4 .   ? -3.80197  -7.03733  64.03139 1.000 31.74660 ? 563 HOH A O   1 
HETATM 2992 O O   . HOH E 4 .   ? 5.35777   16.95188  72.29300 1.000 27.29296 ? 564 HOH A O   1 
HETATM 2993 O O   . HOH E 4 .   ? -19.34884 -9.23215  49.41244 1.000 50.40041 ? 565 HOH A O   1 
HETATM 2994 O O   . HOH E 4 .   ? -11.19403 9.66395   38.78601 1.000 32.69309 ? 566 HOH A O   1 
HETATM 2995 O O   . HOH E 4 .   ? 25.79037  11.02683  64.02827 1.000 30.25837 ? 567 HOH A O   1 
HETATM 2996 O O   . HOH E 4 .   ? -18.52610 18.03731  18.91827 1.000 35.78929 ? 568 HOH A O   1 
HETATM 2997 O O   . HOH E 4 .   ? 8.50130   9.08550   71.00851 1.000 44.47416 ? 569 HOH A O   1 
HETATM 2998 O O   . HOH E 4 .   ? -8.01401  15.75637  76.68988 1.000 50.15821 ? 570 HOH A O   1 
HETATM 2999 O O   . HOH E 4 .   ? 13.88075  13.17705  51.79901 1.000 26.33372 ? 571 HOH A O   1 
HETATM 3000 O O   . HOH E 4 .   ? -21.25358 -0.93861  67.41303 1.000 44.54134 ? 572 HOH A O   1 
HETATM 3001 O O   . HOH E 4 .   ? 10.22046  7.58390   59.67258 1.000 27.56480 ? 573 HOH A O   1 
HETATM 3002 O O   . HOH E 4 .   ? 5.43559   -1.78415  57.57291 1.000 23.13029 ? 574 HOH A O   1 
HETATM 3003 O O   . HOH E 4 .   ? 21.95150  17.24406  59.06148 1.000 26.77634 ? 575 HOH A O   1 
HETATM 3004 O O   . HOH E 4 .   ? 21.02388  21.52401  68.43258 1.000 32.19688 ? 576 HOH A O   1 
HETATM 3005 O O   . HOH E 4 .   ? 6.96959   -5.46346  46.01107 1.000 41.07151 ? 577 HOH A O   1 
HETATM 3006 O O   . HOH E 4 .   ? -15.17900 5.21154   16.74164 1.000 30.00442 ? 578 HOH A O   1 
HETATM 3007 O O   . HOH E 4 .   ? -13.51719 0.13218   72.72379 1.000 57.08982 ? 579 HOH A O   1 
HETATM 3008 O O   . HOH E 4 .   ? 5.57033   7.74719   69.79196 1.000 42.55466 ? 580 HOH A O   1 
HETATM 3009 O O   . HOH E 4 .   ? -12.63161 18.36764  55.69806 1.000 28.01360 ? 581 HOH A O   1 
HETATM 3010 O O   . HOH E 4 .   ? -19.55552 6.76553   24.95722 1.000 34.07662 ? 582 HOH A O   1 
HETATM 3011 O O   . HOH E 4 .   ? 14.05345  4.54089   52.55670 1.000 32.25597 ? 583 HOH A O   1 
HETATM 3012 O O   . HOH E 4 .   ? -24.69764 16.14654  25.70701 1.000 51.55196 ? 584 HOH A O   1 
HETATM 3013 O O   . HOH E 4 .   ? 14.72526  13.85780  67.62120 1.000 17.86096 ? 585 HOH A O   1 
HETATM 3014 O O   . HOH E 4 .   ? 9.04087   9.86290   66.62606 1.000 22.47463 ? 586 HOH A O   1 
HETATM 3015 O O   . HOH E 4 .   ? -17.43314 3.78598   38.35905 1.000 26.37019 ? 587 HOH A O   1 
HETATM 3016 O O   . HOH E 4 .   ? 2.76112   15.20825  76.14611 1.000 37.92829 ? 588 HOH A O   1 
HETATM 3017 O O   . HOH E 4 .   ? -10.24834 -6.66355  49.60185 1.000 15.86682 ? 589 HOH A O   1 
HETATM 3018 O O   . HOH E 4 .   ? 11.13309  20.22741  73.22030 1.000 37.96799 ? 590 HOH A O   1 
HETATM 3019 O O   . HOH E 4 .   ? -14.05835 6.13630   68.18343 1.000 33.20874 ? 591 HOH A O   1 
HETATM 3020 O O   . HOH E 4 .   ? -13.61916 -12.51585 48.17761 1.000 38.91758 ? 592 HOH A O   1 
HETATM 3021 O O   . HOH E 4 .   ? 1.59972   13.45005  57.88133 1.000 14.66069 ? 593 HOH A O   1 
HETATM 3022 O O   . HOH E 4 .   ? -6.14529  2.65037   73.40256 1.000 30.51022 ? 594 HOH A O   1 
HETATM 3023 O O   . HOH E 4 .   ? -27.08956 2.80611   47.86124 1.000 47.11057 ? 595 HOH A O   1 
HETATM 3024 O O   . HOH E 4 .   ? -4.74722  17.84380  25.73796 1.000 45.22369 ? 596 HOH A O   1 
HETATM 3025 O O   . HOH E 4 .   ? 1.62179   -8.51196  44.98328 1.000 42.30850 ? 597 HOH A O   1 
HETATM 3026 O O   . HOH E 4 .   ? -23.80658 6.12111   38.48454 1.000 39.07603 ? 598 HOH A O   1 
HETATM 3027 O O   . HOH E 4 .   ? -5.06054  12.31552  34.40183 1.000 51.53488 ? 599 HOH A O   1 
HETATM 3028 O O   . HOH E 4 .   ? -8.04086  20.99977  25.33439 1.000 44.10174 ? 600 HOH A O   1 
HETATM 3029 O O   . HOH E 4 .   ? 2.74436   -1.12725  64.38590 1.000 26.44673 ? 601 HOH A O   1 
HETATM 3030 O O   . HOH E 4 .   ? -21.51571 15.88235  52.56200 1.000 45.37900 ? 602 HOH A O   1 
HETATM 3031 O O   . HOH E 4 .   ? -2.82139  8.22776   43.10732 1.000 30.05109 ? 603 HOH A O   1 
HETATM 3032 O O   . HOH E 4 .   ? 3.23026   -6.92237  46.21471 1.000 25.45010 ? 604 HOH A O   1 
HETATM 3033 O O   . HOH E 4 .   ? -12.62314 5.66009   23.93527 1.000 20.45016 ? 605 HOH A O   1 
HETATM 3034 O O   . HOH E 4 .   ? -7.01946  14.81877  64.13321 1.000 23.72495 ? 606 HOH A O   1 
HETATM 3035 O O   . HOH E 4 .   ? -2.14743  12.17347  50.39988 1.000 15.49904 ? 607 HOH A O   1 
HETATM 3036 O O   . HOH E 4 .   ? -8.67871  11.06448  78.11468 1.000 45.10404 ? 608 HOH A O   1 
HETATM 3037 O O   . HOH E 4 .   ? -9.19150  -1.48847  74.37294 1.000 47.50699 ? 609 HOH A O   1 
HETATM 3038 O O   . HOH E 4 .   ? 18.17997  -0.09245  65.21150 1.000 49.27076 ? 610 HOH A O   1 
HETATM 3039 O O   . HOH E 4 .   ? 12.47922  -0.22673  51.66480 1.000 58.67061 ? 611 HOH A O   1 
HETATM 3040 O O   . HOH E 4 .   ? 2.08761   18.58726  66.58313 1.000 25.37323 ? 612 HOH A O   1 
HETATM 3041 O O   . HOH E 4 .   ? 14.42534  22.44327  63.40756 1.000 26.46571 ? 613 HOH A O   1 
HETATM 3042 O O   . HOH E 4 .   ? -17.06706 -0.60615  22.68895 1.000 45.58114 ? 614 HOH A O   1 
HETATM 3043 O O   . HOH E 4 .   ? 3.02423   -0.33505  56.87521 1.000 18.36580 ? 615 HOH A O   1 
HETATM 3044 O O   . HOH E 4 .   ? 0.19074   0.04588   69.80331 1.000 42.99445 ? 616 HOH A O   1 
HETATM 3045 O O   . HOH E 4 .   ? 3.46928   2.03403   67.89671 1.000 37.11513 ? 617 HOH A O   1 
HETATM 3046 O O   . HOH E 4 .   ? -5.33458  14.15962  59.21295 1.000 16.79029 ? 618 HOH A O   1 
HETATM 3047 O O   . HOH E 4 .   ? -15.76133 2.28343   16.62650 1.000 52.29236 ? 619 HOH A O   1 
HETATM 3048 O O   . HOH E 4 .   ? -1.82468  14.25028  17.51686 1.000 43.82129 ? 620 HOH A O   1 
HETATM 3049 O O   . HOH E 4 .   ? 6.53027   5.64648   66.64079 1.000 22.41735 ? 621 HOH A O   1 
HETATM 3050 O O   . HOH E 4 .   ? -0.16033  18.84232  64.84280 1.000 34.97852 ? 622 HOH A O   1 
HETATM 3051 O O   . HOH E 4 .   ? 24.95087  14.62381  65.63724 1.000 43.44349 ? 623 HOH A O   1 
HETATM 3052 O O   . HOH E 4 .   ? 10.11284  -1.18798  68.92860 1.000 56.46805 ? 624 HOH A O   1 
HETATM 3053 O O   . HOH E 4 .   ? -11.45841 17.69916  58.44213 1.000 36.03691 ? 625 HOH A O   1 
HETATM 3054 O O   . HOH E 4 .   ? -15.10015 19.31530  44.76149 1.000 45.28964 ? 626 HOH A O   1 
HETATM 3055 O O   . HOH E 4 .   ? -8.45553  13.25821  42.71994 1.000 47.12405 ? 627 HOH A O   1 
HETATM 3056 O O   . HOH E 4 .   ? 16.93022  4.56962   45.50889 1.000 54.58041 ? 628 HOH A O   1 
HETATM 3057 O O   . HOH E 4 .   ? 7.34038   10.93105  75.93138 1.000 45.01665 ? 629 HOH A O   1 
HETATM 3058 O O   . HOH E 4 .   ? 23.16705  16.74643  65.34957 1.000 28.14059 ? 630 HOH A O   1 
HETATM 3059 O O   . HOH E 4 .   ? 17.40642  22.30661  67.71202 1.000 36.69314 ? 631 HOH A O   1 
HETATM 3060 O O   . HOH E 4 .   ? -6.09692  -10.11056 57.13771 1.000 24.40971 ? 632 HOH A O   1 
HETATM 3061 O O   . HOH E 4 .   ? 6.41739   17.44330  53.92406 1.000 21.98958 ? 633 HOH A O   1 
HETATM 3062 O O   . HOH E 4 .   ? 7.71754   19.60433  67.14179 1.000 49.95794 ? 634 HOH A O   1 
HETATM 3063 O O   . HOH E 4 .   ? 4.63372   -6.61893  50.26855 1.000 35.90470 ? 635 HOH A O   1 
HETATM 3064 O O   . HOH E 4 .   ? -18.53921 0.82274   47.76094 1.000 36.56355 ? 636 HOH A O   1 
HETATM 3065 O O   . HOH E 4 .   ? 16.61331  19.80450  49.20226 1.000 43.40723 ? 637 HOH A O   1 
HETATM 3066 O O   . HOH E 4 .   ? -19.93082 2.03549   68.34333 1.000 47.00179 ? 638 HOH A O   1 
HETATM 3067 O O   . HOH E 4 .   ? 2.34350   9.01093   53.45827 1.000 15.77302 ? 639 HOH A O   1 
HETATM 3068 O O   . HOH E 4 .   ? -13.12375 11.42664  11.79043 1.000 18.48413 ? 640 HOH A O   1 
HETATM 3069 O O   . HOH E 4 .   ? 0.17925   -2.92580  53.50436 1.000 17.67059 ? 641 HOH A O   1 
HETATM 3070 O O   . HOH E 4 .   ? -8.51177  -10.99710 64.40361 1.000 33.77001 ? 642 HOH A O   1 
HETATM 3071 O O   . HOH E 4 .   ? -2.77946  15.37417  58.96305 1.000 18.58714 ? 643 HOH A O   1 
HETATM 3072 O O   . HOH E 4 .   ? -12.44058 -7.53636  44.08609 1.000 24.64651 ? 644 HOH A O   1 
HETATM 3073 O O   . HOH E 4 .   ? -21.35366 4.36885   24.51349 1.000 42.77494 ? 645 HOH A O   1 
HETATM 3074 O O   . HOH E 4 .   ? -6.30681  15.84745  44.82983 1.000 37.80744 ? 646 HOH A O   1 
HETATM 3075 O O   . HOH E 4 .   ? 23.13169  2.85810   69.57263 1.000 52.17850 ? 647 HOH A O   1 
HETATM 3076 O O   . HOH E 4 .   ? -2.78434  -10.55407 44.73948 1.000 41.88515 ? 648 HOH A O   1 
HETATM 3077 O O   . HOH E 4 .   ? -15.01102 -1.67528  67.56898 1.000 39.08701 ? 649 HOH A O   1 
HETATM 3078 O O   . HOH E 4 .   ? -1.81337  24.24993  57.79005 1.000 45.33367 ? 650 HOH A O   1 
HETATM 3079 O O   . HOH E 4 .   ? 15.96113  2.36665   71.36915 1.000 26.66546 ? 651 HOH A O   1 
HETATM 3080 O O   . HOH E 4 .   ? -1.17984  7.62849   50.34895 1.000 14.19755 ? 652 HOH A O   1 
HETATM 3081 O O   . HOH E 4 .   ? 0.67066   19.21666  49.35548 1.000 25.78485 ? 653 HOH A O   1 
HETATM 3082 O O   . HOH E 4 .   ? -0.68734  -6.96296  54.61409 1.000 23.21390 ? 654 HOH A O   1 
HETATM 3083 O O   . HOH E 4 .   ? -22.56594 17.11700  63.09904 1.000 27.31438 ? 655 HOH A O   1 
HETATM 3084 O O   . HOH E 4 .   ? -14.80196 -6.36958  45.44282 1.000 27.99224 ? 656 HOH A O   1 
HETATM 3085 O O   . HOH E 4 .   ? -10.42425 4.98762   41.31617 1.000 27.26081 ? 657 HOH A O   1 
HETATM 3086 O O   . HOH E 4 .   ? -20.39822 7.48224   68.55909 1.000 35.79292 ? 658 HOH A O   1 
HETATM 3087 O O   . HOH E 4 .   ? -7.16322  -9.24913  36.08587 1.000 41.74282 ? 659 HOH A O   1 
HETATM 3088 O O   . HOH E 4 .   ? 10.57841  0.63558   54.89429 1.000 54.76883 ? 660 HOH A O   1 
HETATM 3089 O O   . HOH E 4 .   ? -2.54399  -6.85617  50.45240 1.000 20.94737 ? 661 HOH A O   1 
HETATM 3090 O O   . HOH E 4 .   ? -17.08665 1.45306   40.47589 1.000 36.67237 ? 662 HOH A O   1 
HETATM 3091 O O   . HOH E 4 .   ? 21.28590  13.21140  52.64183 1.000 28.83082 ? 663 HOH A O   1 
HETATM 3092 O O   . HOH E 4 .   ? -20.71828 19.81914  47.13807 1.000 53.08345 ? 664 HOH A O   1 
HETATM 3093 O O   . HOH E 4 .   ? -21.73066 4.69583   67.01286 1.000 36.10428 ? 665 HOH A O   1 
HETATM 3094 O O   . HOH E 4 .   ? -2.65082  -5.25331  65.70312 1.000 31.33940 ? 666 HOH A O   1 
HETATM 3095 O O   . HOH E 4 .   ? -13.39515 -1.21890  40.69023 1.000 20.44212 ? 667 HOH A O   1 
HETATM 3096 O O   . HOH E 4 .   ? -8.54160  15.82178  51.38499 1.000 16.88353 ? 668 HOH A O   1 
HETATM 3097 O O   . HOH E 4 .   ? -10.27848 7.42924   39.86153 1.000 27.39784 ? 669 HOH A O   1 
HETATM 3098 O O   . HOH E 4 .   ? 8.05572   4.30111   51.17752 1.000 25.05893 ? 670 HOH A O   1 
HETATM 3099 O O   . HOH E 4 .   ? -9.58204  3.31499   18.42946 1.000 42.23350 ? 671 HOH A O   1 
HETATM 3100 O O   . HOH E 4 .   ? -10.28779 7.83247   74.36890 1.000 40.62823 ? 672 HOH A O   1 
HETATM 3101 O O   . HOH E 4 .   ? -16.93994 6.03135   23.98050 1.000 29.04287 ? 673 HOH A O   1 
HETATM 3102 O O   . HOH E 4 .   ? -4.35963  0.50761   73.70957 1.000 42.68176 ? 674 HOH A O   1 
HETATM 3103 O O   . HOH E 4 .   ? -16.67265 -0.36980  42.40686 1.000 26.59351 ? 675 HOH A O   1 
HETATM 3104 O O   . HOH E 4 .   ? -11.44396 1.38671   18.75338 1.000 34.47909 ? 676 HOH A O   1 
HETATM 3105 O O   . HOH E 4 .   ? 15.78717  4.69621   72.86496 1.000 27.66173 ? 677 HOH A O   1 
HETATM 3106 O O   . HOH E 4 .   ? -18.47092 -10.69972 54.94401 1.000 45.14545 ? 678 HOH A O   1 
HETATM 3107 O O   . HOH E 4 .   ? 23.81008  8.05708   66.15255 1.000 27.10341 ? 679 HOH A O   1 
HETATM 3108 O O   . HOH E 4 .   ? -20.41737 17.94813  44.01526 1.000 50.23623 ? 680 HOH A O   1 
HETATM 3109 O O   . HOH E 4 .   ? 13.13693  5.56149   57.43835 1.000 37.49156 ? 681 HOH A O   1 
HETATM 3110 O O   . HOH E 4 .   ? -9.81792  15.02052  41.24719 1.000 46.84517 ? 682 HOH A O   1 
HETATM 3111 O O   . HOH E 4 .   ? -15.92155 8.12727   22.39151 1.000 23.36602 ? 683 HOH A O   1 
HETATM 3112 O O   . HOH E 4 .   ? 10.49201  3.21064   53.81324 1.000 26.38912 ? 684 HOH A O   1 
HETATM 3113 O O   . HOH E 4 .   ? 17.58014  1.92997   48.24205 1.000 52.01946 ? 685 HOH A O   1 
HETATM 3114 O O   . HOH E 4 .   ? -13.50949 2.60219   74.54434 1.000 35.70028 ? 686 HOH A O   1 
HETATM 3115 O O   . HOH E 4 .   ? -13.35108 10.88934  68.86995 1.000 35.29410 ? 687 HOH A O   1 
HETATM 3116 O O   . HOH E 4 .   ? 13.05780  4.65827   61.70951 1.000 27.29617 ? 688 HOH A O   1 
HETATM 3117 O O   . HOH E 4 .   ? 10.85351  19.53498  65.40460 1.000 54.62430 ? 689 HOH A O   1 
HETATM 3118 O O   . HOH E 4 .   ? 18.70356  3.66734   56.22376 1.000 35.86326 ? 690 HOH A O   1 
HETATM 3119 O O   . HOH E 4 .   ? -9.20442  -9.00772  39.91354 1.000 37.41863 ? 691 HOH A O   1 
HETATM 3120 O O   . HOH E 4 .   ? -12.22778 12.41697  70.72390 1.000 33.37029 ? 692 HOH A O   1 
HETATM 3121 O O   . HOH E 4 .   ? -3.60355  17.65428  66.16510 1.000 55.03309 ? 693 HOH A O   1 
HETATM 3122 O O   . HOH E 4 .   ? -15.99394 11.96917  66.05535 1.000 52.47709 ? 694 HOH A O   1 
HETATM 3123 O O   . HOH E 4 .   ? -11.38374 -0.13583  39.09666 1.000 27.61551 ? 695 HOH A O   1 
HETATM 3124 O O   . HOH E 4 .   ? -0.90550  7.07391   73.73580 1.000 36.36999 ? 696 HOH A O   1 
HETATM 3125 O O   . HOH E 4 .   ? -21.26760 4.47706   31.67301 1.000 52.88199 ? 697 HOH A O   1 
HETATM 3126 O O   . HOH E 4 .   ? 18.92308  12.81764  47.71031 1.000 56.21746 ? 698 HOH A O   1 
HETATM 3127 O O   . HOH E 4 .   ? -0.00527  -6.66368  50.30138 1.000 29.00972 ? 699 HOH A O   1 
HETATM 3128 O O   . HOH E 4 .   ? -3.70313  6.83096   74.77908 1.000 35.39189 ? 700 HOH A O   1 
HETATM 3129 O O   . HOH E 4 .   ? 6.39415   -2.33712  49.79988 1.000 25.02107 ? 701 HOH A O   1 
HETATM 3130 O O   . HOH E 4 .   ? -13.28913 -0.94258  33.20910 1.000 55.36567 ? 702 HOH A O   1 
HETATM 3131 O O   . HOH E 4 .   ? 3.55908   18.83592  45.97250 1.000 51.21495 ? 703 HOH A O   1 
HETATM 3132 O O   . HOH E 4 .   ? -17.64805 -0.82717  31.55526 1.000 52.98367 ? 704 HOH A O   1 
HETATM 3133 O O   . HOH E 4 .   ? -17.73033 -14.67335 52.89568 1.000 50.44348 ? 705 HOH A O   1 
HETATM 3134 O O   . HOH E 4 .   ? 4.90358   -2.80507  54.08578 1.000 33.82196 ? 706 HOH A O   1 
HETATM 3135 O O   . HOH E 4 .   ? 6.33140   -1.18489  53.50135 1.000 32.35260 ? 707 HOH A O   1 
HETATM 3136 O O   . HOH E 4 .   ? 17.51788  21.94058  64.54134 1.000 39.05420 ? 708 HOH A O   1 
HETATM 3137 O O   . HOH E 4 .   ? -15.73503 -16.04825 49.36698 1.000 45.30629 ? 709 HOH A O   1 
HETATM 3138 O O   . HOH E 4 .   ? 24.49770  15.75189  50.66802 1.000 41.39606 ? 710 HOH A O   1 
HETATM 3139 O O   . HOH E 4 .   ? -19.83995 9.08512   73.41298 1.000 55.72304 ? 711 HOH A O   1 
HETATM 3140 O O   . HOH E 4 .   ? 5.65498   2.46780   38.60055 1.000 49.48212 ? 712 HOH A O   1 
HETATM 3141 O O   . HOH E 4 .   ? 23.16328  16.69880  68.48339 1.000 51.26590 ? 713 HOH A O   1 
HETATM 3142 O O   . HOH E 4 .   ? 13.56245  2.93251   59.42613 1.000 45.72015 ? 714 HOH A O   1 
HETATM 3143 O O   . HOH E 4 .   ? -4.94551  -8.80336  65.60773 1.000 55.40092 ? 715 HOH A O   1 
HETATM 3144 O O   . HOH E 4 .   ? 5.74791   -3.44055  65.46899 1.000 52.05153 ? 716 HOH A O   1 
HETATM 3145 O O   . HOH E 4 .   ? -16.54340 6.37903   70.56305 1.000 47.66951 ? 717 HOH A O   1 
HETATM 3146 O O   . HOH E 4 .   ? 19.23812  6.70958   52.50855 1.000 30.15803 ? 718 HOH A O   1 
HETATM 3147 O O   . HOH E 4 .   ? 18.87045  6.04094   55.33882 1.000 30.31162 ? 719 HOH A O   1 
HETATM 3148 O O   . HOH E 4 .   ? 7.63193   24.33172  51.38109 1.000 50.68849 ? 720 HOH A O   1 
HETATM 3149 O O   . HOH E 4 .   ? -17.83188 -2.39872  51.26339 1.000 45.03683 ? 721 HOH A O   1 
HETATM 3150 O O   . HOH E 4 .   ? -5.01383  -4.69928  70.20114 1.000 37.13326 ? 722 HOH A O   1 
HETATM 3151 O O   . HOH E 4 .   ? 19.73982  -0.36376  67.11948 1.000 50.79473 ? 723 HOH A O   1 
HETATM 3152 O O   . HOH E 4 .   ? -0.73323  -7.84208  64.17995 1.000 53.07265 ? 724 HOH A O   1 
HETATM 3153 O O   . HOH E 4 .   ? 5.30015   17.63784  76.41838 1.000 57.61479 ? 725 HOH A O   1 
HETATM 3154 O O   . HOH E 4 .   ? -10.70602 -9.28511  67.09629 1.000 38.10822 ? 726 HOH A O   1 
HETATM 3155 O O   . HOH E 4 .   ? 11.45456  21.12413  70.94547 1.000 44.65913 ? 727 HOH A O   1 
HETATM 3156 O O   . HOH E 4 .   ? -17.07940 -0.27545  66.69412 1.000 46.39651 ? 728 HOH A O   1 
HETATM 3157 O O   . HOH E 4 .   ? 18.33471  0.97298   71.75020 1.000 40.38125 ? 729 HOH A O   1 
HETATM 3158 O O   . HOH E 4 .   ? -6.04196  -7.86949  38.68930 1.000 50.50637 ? 730 HOH A O   1 
HETATM 3159 O O   . HOH E 4 .   ? -16.39602 -8.31685  46.59212 1.000 31.84361 ? 731 HOH A O   1 
HETATM 3160 O O   . HOH E 4 .   ? 0.28244   -8.72266  51.31396 1.000 52.47373 ? 732 HOH A O   1 
HETATM 3161 O O   . HOH E 4 .   ? 0.94999   15.44385  38.92924 1.000 51.54141 ? 733 HOH A O   1 
HETATM 3162 O O   . HOH E 4 .   ? 18.89837  8.02617   45.82962 1.000 55.19671 ? 734 HOH A O   1 
HETATM 3163 O O   . HOH E 4 .   ? -8.40385  22.30598  53.91029 1.000 45.28632 ? 735 HOH A O   1 
HETATM 3164 O O   . HOH E 4 .   ? -11.72949 17.94479  17.61924 1.000 41.12790 ? 736 HOH A O   1 
HETATM 3165 O O   . HOH E 4 .   ? 8.42119   -0.61756  55.20136 1.000 38.12023 ? 737 HOH A O   1 
HETATM 3166 O O   . HOH E 4 .   ? -7.62539  13.45339  37.89392 1.000 48.39680 ? 738 HOH A O   1 
HETATM 3167 O O   . HOH E 4 .   ? -24.98094 8.38152   45.43098 1.000 52.26626 ? 739 HOH A O   1 
HETATM 3168 O O   . HOH E 4 .   ? 1.92154   -6.90163  34.60825 1.000 54.68480 ? 740 HOH A O   1 
HETATM 3169 O O   . HOH E 4 .   ? 27.33279  18.75601  52.06095 1.000 46.81998 ? 741 HOH A O   1 
HETATM 3170 O O   . HOH E 4 .   ? -0.80002  11.76002  80.54495 1.000 59.34176 ? 742 HOH A O   1 
HETATM 3171 O O   . HOH E 4 .   ? -20.85270 0.41746   34.63536 1.000 55.88185 ? 743 HOH A O   1 
HETATM 3172 O O   . HOH E 4 .   ? 2.39382   -1.76247  54.49413 1.000 21.54801 ? 744 HOH A O   1 
HETATM 3173 O O   . HOH E 4 .   ? -23.12802 3.68567   44.05441 1.000 59.40697 ? 745 HOH A O   1 
HETATM 3174 O O   . HOH E 4 .   ? -2.01104  19.73767  52.78203 1.000 34.56333 ? 746 HOH A O   1 
HETATM 3175 O O   . HOH E 4 .   ? 12.51460  4.29936   55.22359 1.000 31.83872 ? 747 HOH A O   1 
HETATM 3176 O O   . HOH E 4 .   ? 0.84599   -5.45130  52.84059 1.000 19.72901 ? 748 HOH A O   1 
HETATM 3177 O O   . HOH E 4 .   ? -0.13253  -5.39007  65.57723 1.000 35.47483 ? 749 HOH A O   1 
HETATM 3178 O O   . HOH E 4 .   ? -15.49016 -2.06551  26.97534 1.000 57.25682 ? 750 HOH A O   1 
HETATM 3179 O O   . HOH E 4 .   ? 3.50752   -0.43024  66.98911 1.000 28.78485 ? 751 HOH A O   1 
HETATM 3180 O O   . HOH E 4 .   ? -18.02630 -5.05025  52.51676 1.000 40.77951 ? 752 HOH A O   1 
HETATM 3181 O O   . HOH E 4 .   ? -17.14200 -3.37815  41.67565 1.000 48.32504 ? 753 HOH A O   1 
HETATM 3182 O O   . HOH E 4 .   ? 2.38959   -1.49384  69.00700 1.000 44.54187 ? 754 HOH A O   1 
HETATM 3183 O O   . HOH E 4 .   ? -18.17695 -10.53896 59.63359 1.000 53.80759 ? 755 HOH A O   1 
HETATM 3184 O O   . HOH E 4 .   ? -10.97296 -9.73407  64.38990 1.000 29.81917 ? 756 HOH A O   1 
HETATM 3185 O O   . HOH E 4 .   ? -21.55219 -6.29865  59.46061 1.000 53.68624 ? 757 HOH A O   1 
HETATM 3186 O O   . HOH E 4 .   ? 8.86025   -6.38668  35.16665 1.000 65.63195 ? 758 HOH A O   1 
HETATM 3187 O O   . HOH E 4 .   ? -15.25950 8.85719   68.26983 1.000 36.47075 ? 759 HOH A O   1 
HETATM 3188 O O   . HOH E 4 .   ? 23.76038  1.98715   63.25168 1.000 58.82340 ? 760 HOH A O   1 
HETATM 3189 O O   . HOH E 4 .   ? 5.97982   -4.64875  48.19788 1.000 43.02878 ? 761 HOH A O   1 
HETATM 3190 O O   . HOH E 4 .   ? 12.70471  20.89492  50.78472 1.000 55.83365 ? 762 HOH A O   1 
HETATM 3191 O O   . HOH E 4 .   ? -1.60488  -10.40850 48.65786 1.000 56.53677 ? 763 HOH A O   1 
HETATM 3192 O O   . HOH E 4 .   ? -16.11996 -6.10614  42.33269 1.000 48.13371 ? 764 HOH A O   1 
HETATM 3193 O O   . HOH E 4 .   ? -27.31727 5.60018   24.34598 1.000 55.19532 ? 765 HOH A O   1 
HETATM 3194 O O   . HOH E 4 .   ? -6.96676  -1.63332  72.67231 1.000 44.05443 ? 766 HOH A O   1 
HETATM 3195 O O   . HOH E 4 .   ? -6.46818  22.01375  33.73102 1.000 65.59227 ? 767 HOH A O   1 
HETATM 3196 O O   . HOH E 4 .   ? 13.24131  0.83051   71.11793 1.000 45.86923 ? 768 HOH A O   1 
HETATM 3197 O O   . HOH E 4 .   ? -14.45065 14.48406  21.77901 1.000 58.35264 ? 769 HOH A O   1 
HETATM 3198 O O   . HOH E 4 .   ? -7.11810  13.60753  35.62475 1.000 51.26713 ? 770 HOH A O   1 
HETATM 3199 O O   . HOH E 4 .   ? -7.44146  -3.54006  70.74983 1.000 32.64611 ? 771 HOH A O   1 
HETATM 3200 O O   . HOH E 4 .   ? -29.89713 4.74298   23.98138 1.000 57.26835 ? 772 HOH A O   1 
HETATM 3201 O O   . HOH E 4 .   ? -23.08217 -1.28458  63.09289 1.000 51.72552 ? 773 HOH A O   1 
HETATM 3202 O O   . HOH E 4 .   ? -17.31472 -0.24433  38.35748 1.000 38.51758 ? 774 HOH A O   1 
HETATM 3203 O O   . HOH E 4 .   ? 5.57167   3.23124   68.33651 1.000 51.80622 ? 775 HOH A O   1 
HETATM 3204 O O   . HOH E 4 .   ? 4.71271   -9.05302  63.26815 1.000 48.84841 ? 776 HOH A O   1 
HETATM 3205 O O   . HOH E 4 .   ? -1.12889  12.08181  14.81168 1.000 52.45135 ? 777 HOH A O   1 
HETATM 3206 O O   . HOH E 4 .   ? 4.23914   17.82110  74.37549 1.000 52.46591 ? 778 HOH A O   1 
HETATM 3207 O O   . HOH E 4 .   ? 2.84406   26.00218  63.93384 1.000 54.49012 ? 779 HOH A O   1 
HETATM 3208 O O   . HOH E 4 .   ? 12.33618  6.47656   59.79035 1.000 28.90371 ? 780 HOH A O   1 
HETATM 3209 O O   . HOH E 4 .   ? 1.70297   -3.85735  64.29288 1.000 37.69302 ? 781 HOH A O   1 
HETATM 3210 O O   . HOH E 4 .   ? -16.21772 -4.96740  67.93089 1.000 53.59153 ? 782 HOH A O   1 
HETATM 3211 O O   . HOH E 4 .   ? 10.83221  20.29944  48.04802 1.000 58.56346 ? 783 HOH A O   1 
HETATM 3212 O O   . HOH E 4 .   ? 6.31684   -0.94257  67.07566 1.000 36.76420 ? 784 HOH A O   1 
HETATM 3213 O O   . HOH E 4 .   ? -24.06795 5.71950   67.64216 1.000 49.11628 ? 785 HOH A O   1 
HETATM 3214 O O   . HOH E 4 .   ? -15.36382 -1.75461  39.15253 1.000 35.94729 ? 786 HOH A O   1 
HETATM 3215 O O   . HOH E 4 .   ? -3.92391  19.96011  48.60213 1.000 49.49081 ? 787 HOH A O   1 
HETATM 3216 O O   . HOH E 4 .   ? 8.37612   7.40229   67.80264 1.000 24.43394 ? 788 HOH A O   1 
HETATM 3217 O O   . HOH E 4 .   ? 25.26023  14.05123  52.69419 1.000 46.67497 ? 789 HOH A O   1 
HETATM 3218 O O   . HOH E 4 .   ? -10.40046 -12.82408 40.00802 1.000 50.19946 ? 790 HOH A O   1 
HETATM 3219 O O   . HOH E 4 .   ? -14.70251 20.05712  47.68207 1.000 48.30441 ? 791 HOH A O   1 
HETATM 3220 O O   . HOH E 4 .   ? 7.53084   1.52688   67.25771 1.000 36.04435 ? 792 HOH A O   1 
HETATM 3221 O O   . HOH E 4 .   ? 0.88671   12.93028  18.53229 1.000 41.57939 ? 793 HOH A O   1 
HETATM 3222 O O   . HOH E 4 .   ? -12.53366 -11.65970 63.86364 1.000 33.49052 ? 794 HOH A O   1 
HETATM 3223 O O   . HOH E 4 .   ? 1.00126   7.48488   75.80675 1.000 46.41654 ? 795 HOH A O   1 
HETATM 3224 O O   . HOH E 4 .   ? -12.37529 -10.08709 43.12239 1.000 35.09212 ? 796 HOH A O   1 
HETATM 3225 O O   . HOH E 4 .   ? -16.85123 9.68836   17.33226 1.000 52.15688 ? 797 HOH A O   1 
HETATM 3226 O O   . HOH E 4 .   ? -8.82776  -5.34064  72.21024 1.000 39.99642 ? 798 HOH A O   1 
HETATM 3227 O O   . HOH E 4 .   ? 23.44754  19.97581  67.90660 1.000 55.91527 ? 799 HOH A O   1 
HETATM 3228 O O   . HOH E 4 .   ? 8.80710   -3.04790  55.34874 1.000 54.33257 ? 800 HOH A O   1 
HETATM 3229 O O   . HOH E 4 .   ? -19.61128 6.06550   70.66072 1.000 53.17016 ? 801 HOH A O   1 
HETATM 3230 O O   . HOH E 4 .   ? -8.04423  -13.30604 63.39154 1.000 44.91027 ? 802 HOH A O   1 
HETATM 3231 O O   . HOH E 4 .   ? -5.50026  18.82206  51.99929 1.000 44.13464 ? 803 HOH A O   1 
HETATM 3232 O O   . HOH E 4 .   ? 10.43011  24.74777  51.93397 1.000 46.82004 ? 804 HOH A O   1 
HETATM 3233 O O   . HOH E 4 .   ? 27.79807  19.43660  50.01794 1.000 53.49896 ? 805 HOH A O   1 
HETATM 3234 O O   . HOH E 4 .   ? 25.69292  9.96957   66.64770 1.000 38.89294 ? 806 HOH A O   1 
HETATM 3235 O O   . HOH E 4 .   ? -4.77646  -8.56349  68.04944 1.000 65.84429 ? 807 HOH A O   1 
HETATM 3236 O O   . HOH E 4 .   ? -6.82695  1.92421   17.78255 1.000 46.11183 ? 808 HOH A O   1 
HETATM 3237 O O   . HOH E 4 .   ? -0.23427  7.24959   78.10532 1.000 38.33333 ? 809 HOH A O   1 
HETATM 3238 O O   . HOH E 4 .   ? -0.96787  18.57499  70.42819 1.000 50.38562 ? 810 HOH A O   1 
HETATM 3239 O O   . HOH E 4 .   ? 2.04982   15.14807  16.52440 1.000 53.38697 ? 811 HOH A O   1 
HETATM 3240 O O   . HOH E 4 .   ? 2.90307   -11.29051 50.76108 1.000 48.06106 ? 812 HOH A O   1 
HETATM 3241 O O   . HOH E 4 .   ? 23.29739  24.71889  69.16666 1.000 51.78420 ? 813 HOH A O   1 
HETATM 3242 O O   . HOH E 4 .   ? 4.18530   -13.66867 48.62658 1.000 56.42470 ? 814 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  ? 0.89963 0.65779 0.72849 0.15478  -0.06579 0.05976  9   PRO A N   
2    C CA  . PRO A 15  ? 0.89358 0.66023 0.73045 0.15962  -0.07395 0.06150  9   PRO A CA  
3    C C   . PRO A 15  ? 0.88933 0.66402 0.73495 0.16678  -0.08290 0.06698  9   PRO A C   
4    O O   . PRO A 15  ? 0.88439 0.65943 0.72496 0.17947  -0.09677 0.07549  9   PRO A O   
5    C CB  . PRO A 15  ? 0.89919 0.66162 0.73016 0.15556  -0.06981 0.06154  9   PRO A CB  
6    C CG  . PRO A 15  ? 0.90338 0.66171 0.73256 0.15473  -0.06625 0.05914  9   PRO A CG  
7    C CD  . PRO A 15  ? 0.90135 0.66007 0.72856 0.15451  -0.07000 0.05863  9   PRO A CD  
8    N N   . GLU A 16  ? 0.88993 0.66958 0.75216 0.16244  -0.07489 0.06616  10  GLU A N   
9    C CA  . GLU A 16  ? 0.89316 0.67797 0.76634 0.16237  -0.06786 0.07057  10  GLU A CA  
10   C C   . GLU A 16  ? 0.90377 0.67730 0.74623 0.17496  -0.08052 0.08448  10  GLU A C   
11   O O   . GLU A 16  ? 0.91289 0.67861 0.74383 0.18468  -0.08001 0.08647  10  GLU A O   
12   C CB  . GLU A 16  ? 0.88704 0.68435 0.78480 0.15309  -0.05566 0.06208  10  GLU A CB  
13   C CG  . GLU A 16  ? 0.88147 0.68953 0.79855 0.14007  -0.04751 0.05197  10  GLU A CG  
14   C CD  . GLU A 16  ? 0.87745 0.69260 0.80703 0.13111  -0.03817 0.04730  10  GLU A CD  
15   O OE1 . GLU A 16  ? 0.87276 0.69524 0.81105 0.12912  -0.03390 0.04489  10  GLU A OE1 
16   O OE2 . GLU A 16  ? 0.87950 0.69391 0.80835 0.12575  -0.03234 0.04605  10  GLU A OE2 
17   N N   . MET A 17  ? 0.90355 0.67454 0.73524 0.17398  -0.08727 0.09525  11  MET A N   
18   C CA  . MET A 17  ? 0.90573 0.67209 0.72968 0.16927  -0.09094 0.10338  11  MET A CA  
19   C C   . MET A 17  ? 0.90313 0.65365 0.72725 0.17617  -0.10070 0.10455  11  MET A C   
20   O O   . MET A 17  ? 0.90677 0.65178 0.72872 0.18482  -0.10268 0.11226  11  MET A O   
21   C CB  . MET A 17  ? 0.91365 0.68523 0.72672 0.15762  -0.08164 0.11143  11  MET A CB  
22   C CG  . MET A 17  ? 0.92764 0.69769 0.72843 0.14701  -0.06915 0.12186  11  MET A CG  
23   S SD  . MET A 17  ? 0.94571 0.70923 0.72528 0.12895  -0.05205 0.12784  11  MET A SD  
24   C CE  . MET A 17  ? 0.94207 0.70652 0.72449 0.12275  -0.05086 0.12992  11  MET A CE  
25   N N   . VAL A 18  ? 0.90161 0.63426 0.72779 0.17398  -0.10111 0.09337  12  VAL A N   
26   C CA  . VAL A 18  ? 0.89843 0.61648 0.72708 0.17308  -0.09813 0.08531  12  VAL A CA  
27   C C   . VAL A 18  ? 0.90436 0.60665 0.74035 0.16171  -0.08815 0.06804  12  VAL A C   
28   O O   . VAL A 18  ? 0.90546 0.61101 0.73624 0.17141  -0.09923 0.07165  12  VAL A O   
29   C CB  . VAL A 18  ? 0.88658 0.61588 0.71876 0.18624  -0.10952 0.09496  12  VAL A CB  
30   C CG1 . VAL A 18  ? 0.88503 0.61773 0.70950 0.19373  -0.11338 0.10054  12  VAL A CG1 
31   C CG2 . VAL A 18  ? 0.87776 0.61174 0.71893 0.18247  -0.11605 0.09510  12  VAL A CG2 
32   N N   . ARG A 19  ? 0.90458 0.58891 0.75040 0.13930  -0.07496 0.04660  13  ARG A N   
33   C CA  . ARG A 19  ? 0.89560 0.56648 0.74922 0.12790  -0.07276 0.03072  13  ARG A CA  
34   C C   . ARG A 19  ? 0.89669 0.55870 0.74236 0.11748  -0.06943 0.02995  13  ARG A C   
35   O O   . ARG A 19  ? 0.89801 0.55606 0.75412 0.11545  -0.07107 0.01679  13  ARG A O   
36   C CB  . ARG A 19  ? 0.88055 0.54884 0.74693 0.13377  -0.08704 0.02954  13  ARG A CB  
37   C CG  . ARG A 19  ? 0.87005 0.53242 0.74798 0.13820  -0.09723 0.03029  13  ARG A CG  
38   C CD  . ARG A 19  ? 0.85724 0.51830 0.75301 0.14898  -0.10806 0.03316  13  ARG A CD  
39   N NE  . ARG A 19  ? 0.84981 0.50863 0.75663 0.15151  -0.10987 0.03075  13  ARG A NE  
40   C CZ  . ARG A 19  ? 0.84452 0.50280 0.76242 0.15087  -0.11142 0.02562  13  ARG A CZ  
41   N NH1 . ARG A 19  ? 0.85094 0.50116 0.76668 0.14412  -0.10608 0.02211  13  ARG A NH1 
42   N NH2 . ARG A 19  ? 0.83878 0.50049 0.76449 0.15376  -0.11280 0.02150  13  ARG A NH2 
43   N N   . GLY A 20  ? 0.89098 0.55072 0.71510 0.11990  -0.06943 0.05017  14  GLY A N   
44   C CA  . GLY A 20  ? 0.88868 0.54419 0.69190 0.11958  -0.06148 0.06157  14  GLY A CA  
45   C C   . GLY A 20  ? 0.89186 0.54183 0.66682 0.11208  -0.05389 0.07046  14  GLY A C   
46   O O   . GLY A 20  ? 0.89391 0.54177 0.66634 0.11026  -0.05186 0.06584  14  GLY A O   
47   N N   . GLN A 21  ? 0.88691 0.53483 0.63570 0.11296  -0.05249 0.09017  15  GLN A N   
48   C CA  . GLN A 21  ? 0.88477 0.52880 0.60247 0.11051  -0.04686 0.10866  15  GLN A CA  
49   C C   . GLN A 21  ? 0.86739 0.51085 0.55824 0.12245  -0.05237 0.13138  15  GLN A C   
50   O O   . GLN A 21  ? 0.86103 0.51364 0.55164 0.12118  -0.07098 0.13790  15  GLN A O   
51   C CB  . GLN A 21  ? 0.89579 0.53991 0.61198 0.09630  -0.04015 0.10186  15  GLN A CB  
52   C CG  . GLN A 21  ? 0.90886 0.54670 0.61816 0.08058  -0.03086 0.09507  15  GLN A CG  
53   C CD  . GLN A 21  ? 0.92398 0.55528 0.62197 0.06635  -0.02244 0.09437  15  GLN A CD  
54   O OE1 . GLN A 21  ? 0.93472 0.55744 0.62334 0.05685  -0.01495 0.09828  15  GLN A OE1 
55   N NE2 . GLN A 21  ? 0.92326 0.55893 0.62573 0.06170  -0.02250 0.09245  15  GLN A NE2 
56   N N   . VAL A 22  ? 0.86039 0.49251 0.52351 0.13729  -0.04239 0.14543  16  VAL A N   
57   C CA  . VAL A 22  ? 0.84290 0.48173 0.48978 0.13891  -0.02876 0.14939  16  VAL A CA  
58   C C   . VAL A 22  ? 0.81303 0.47296 0.46186 0.14048  -0.01273 0.14056  16  VAL A C   
59   O O   . VAL A 22  ? 0.82826 0.46823 0.47452 0.14668  0.00072  0.13730  16  VAL A O   
60   C CB  . VAL A 22  ? 0.85434 0.47826 0.48805 0.14098  -0.03514 0.16103  16  VAL A CB  
61   C CG1 . VAL A 22  ? 0.85208 0.47835 0.50085 0.14428  -0.02675 0.15417  16  VAL A CG1 
62   C CG2 . VAL A 22  ? 0.86338 0.47840 0.47985 0.13021  -0.03939 0.17131  16  VAL A CG2 
63   N N   . PHE A 23  ? 0.76878 0.47077 0.42960 0.13337  -0.00622 0.13424  17  PHE A N   
64   C CA  . PHE A 23  ? 0.73088 0.47393 0.41293 0.13004  0.00967  0.12780  17  PHE A CA  
65   C C   . PHE A 23  ? 0.70965 0.48497 0.39689 0.09163  0.01324  0.12985  17  PHE A C   
66   O O   . PHE A 23  ? 0.71632 0.48909 0.41557 0.07440  0.02993  0.13517  17  PHE A O   
67   C CB  . PHE A 23  ? 0.71364 0.46287 0.40189 0.15407  0.01998  0.12130  17  PHE A CB  
68   C CG  . PHE A 23  ? 0.69336 0.45118 0.39098 0.18150  0.02885  0.12053  17  PHE A CG  
69   C CD1 . PHE A 23  ? 0.69771 0.44950 0.39943 0.18828  0.04404  0.11721  17  PHE A CD1 
70   C CD2 . PHE A 23  ? 0.68544 0.44663 0.39454 0.18858  0.04157  0.11511  17  PHE A CD2 
71   C CE1 . PHE A 23  ? 0.68668 0.43949 0.39584 0.20327  0.05232  0.12681  17  PHE A CE1 
72   C CE2 . PHE A 23  ? 0.66824 0.43641 0.38482 0.21253  0.03948  0.12218  17  PHE A CE2 
73   C CZ  . PHE A 23  ? 0.67359 0.43515 0.39153 0.21836  0.04755  0.12852  17  PHE A CZ  
74   N N   . ASP A 24  ? 0.68791 0.49010 0.35494 0.07410  0.00389  0.12357  18  ASP A N   
75   C CA  . ASP A 24  ? 0.64998 0.51112 0.29352 0.04901  -0.03240 0.12971  18  ASP A CA  
76   C C   . ASP A 24  ? 0.63246 0.54830 0.29075 0.04736  -0.00548 0.13404  18  ASP A C   
77   O O   . ASP A 24  ? 0.64732 0.55242 0.27393 0.02777  0.01837  0.11141  18  ASP A O   
78   C CB  . ASP A 24  ? 0.63545 0.49915 0.29626 0.01925  -0.04899 0.10828  18  ASP A CB  
79   C CG  . ASP A 24  ? 0.62141 0.48529 0.28019 -0.00821 -0.06217 0.10216  18  ASP A CG  
80   O OD1 . ASP A 24  ? 0.62355 0.48230 0.30418 -0.01330 -0.04855 0.10825  18  ASP A OD1 
81   O OD2 . ASP A 24  ? 0.61747 0.47070 0.27375 -0.03440 -0.04897 0.08964  18  ASP A OD2 
82   N N   . VAL A 25  ? 0.60154 0.58536 0.31572 0.06163  -0.01397 0.15296  19  VAL A N   
83   C CA  . VAL A 25  ? 0.57851 0.61773 0.29929 0.06634  -0.02687 0.18231  19  VAL A CA  
84   C C   . VAL A 25  ? 0.57705 0.66396 0.29317 0.05023  -0.04603 0.18134  19  VAL A C   
85   O O   . VAL A 25  ? 0.60694 0.66813 0.25767 0.04424  -0.04838 0.17347  19  VAL A O   
86   C CB  . VAL A 25  ? 0.55397 0.60067 0.28119 0.08199  -0.04799 0.18742  19  VAL A CB  
87   C CG1 . VAL A 25  ? 0.55447 0.60757 0.30172 0.09185  -0.03223 0.19177  19  VAL A CG1 
88   C CG2 . VAL A 25  ? 0.56582 0.60427 0.28203 0.08041  -0.02834 0.19416  19  VAL A CG2 
89   N N   . GLY A 26  ? 0.53944 0.70670 0.35163 0.04636  -0.04514 0.17792  20  GLY A N   
90   C CA  . GLY A 26  ? 0.47936 0.74334 0.36590 0.05158  -0.08086 0.17523  20  GLY A CA  
91   C C   . GLY A 26  ? 0.44261 0.77587 0.40827 0.04415  -0.06427 0.17102  20  GLY A C   
92   O O   . GLY A 26  ? 0.43542 0.78307 0.44835 0.05749  -0.04991 0.17739  20  GLY A O   
93   N N   . PRO A 27  ? 0.39911 0.79767 0.38201 0.03179  -0.08198 0.18004  21  PRO A N   
94   C CA  . PRO A 27  ? 0.36468 0.80038 0.36007 0.02188  -0.09985 0.18972  21  PRO A CA  
95   C C   . PRO A 27  ? 0.34352 0.80846 0.35033 -0.01507 -0.10034 0.18099  21  PRO A C   
96   O O   . PRO A 27  ? 0.34920 0.82480 0.35982 -0.02566 -0.06481 0.18210  21  PRO A O   
97   C CB  . PRO A 27  ? 0.38243 0.80718 0.36403 0.02987  -0.09253 0.18297  21  PRO A CB  
98   C CG  . PRO A 27  ? 0.38667 0.79613 0.35950 0.04340  -0.10049 0.18933  21  PRO A CG  
99   C CD  . PRO A 27  ? 0.39158 0.80172 0.35801 0.03291  -0.08907 0.18861  21  PRO A CD  
100  N N   . ARG A 28  ? 0.33874 0.77250 0.33578 -0.04472 -0.11105 0.16301  22  ARG A N   
101  C CA  . ARG A 28  ? 0.33150 0.76214 0.32594 -0.04838 -0.10340 0.16648  22  ARG A CA  
102  C C   . ARG A 28  ? 0.34593 0.76570 0.33177 -0.02889 -0.10682 0.16913  22  ARG A C   
103  O O   . ARG A 28  ? 0.37094 0.77742 0.33004 -0.02949 -0.10353 0.18268  22  ARG A O   
104  C CB  . ARG A 28  ? 0.31224 0.75835 0.31890 -0.06370 -0.09683 0.16183  22  ARG A CB  
105  C CG  . ARG A 28  ? 0.29865 0.76307 0.32756 -0.06572 -0.08760 0.15651  22  ARG A CG  
106  C CD  . ARG A 28  ? 0.29550 0.75546 0.34782 -0.08153 -0.07049 0.13719  22  ARG A CD  
107  N NE  . ARG A 28  ? 0.30597 0.74743 0.35360 -0.08112 -0.05892 0.11557  22  ARG A NE  
108  C CZ  . ARG A 28  ? 0.32706 0.73418 0.38600 -0.07654 -0.02809 0.09696  22  ARG A CZ  
109  N NH1 . ARG A 28  ? 0.32457 0.73070 0.41961 -0.06832 -0.01888 0.08411  22  ARG A NH1 
110  N NH2 . ARG A 28  ? 0.34049 0.73123 0.38036 -0.07770 -0.05414 0.09276  22  ARG A NH2 
111  N N   . TYR A 29  ? 0.35446 0.76585 0.33180 0.00881  -0.09839 0.17300  23  TYR A N   
112  C CA  . TYR A 29  ? 0.34598 0.74464 0.34703 0.04088  -0.10010 0.16932  23  TYR A CA  
113  C C   . TYR A 29  ? 0.38079 0.76975 0.39845 0.08162  -0.09078 0.21135  23  TYR A C   
114  O O   . TYR A 29  ? 0.37582 0.77260 0.43058 0.08256  -0.08094 0.21497  23  TYR A O   
115  C CB  . TYR A 29  ? 0.30417 0.71448 0.32573 0.04309  -0.09147 0.13998  23  TYR A CB  
116  C CG  . TYR A 29  ? 0.28075 0.69840 0.29164 0.03253  -0.07836 0.12170  23  TYR A CG  
117  C CD1 . TYR A 29  ? 0.26307 0.70582 0.26315 0.03557  -0.05975 0.10476  23  TYR A CD1 
118  C CD2 . TYR A 29  ? 0.24843 0.67429 0.27817 0.01835  -0.07164 0.10474  23  TYR A CD2 
119  C CE1 . TYR A 29  ? 0.26523 0.68423 0.25138 0.02938  -0.06551 0.09113  23  TYR A CE1 
120  C CE2 . TYR A 29  ? 0.26502 0.67685 0.25380 0.00263  -0.07408 0.09117  23  TYR A CE2 
121  C CZ  . TYR A 29  ? 0.26140 0.67535 0.24877 0.01455  -0.06703 0.09303  23  TYR A CZ  
122  O OH  . TYR A 29  ? 0.26894 0.66269 0.24544 -0.00193 -0.07746 0.08207  23  TYR A OH  
123  N N   . THR A 30  ? 0.43348 0.78410 0.42262 0.11512  -0.08277 0.22265  24  THR A N   
124  C CA  . THR A 30  ? 0.46283 0.79489 0.44142 0.13073  -0.11567 0.21350  24  THR A CA  
125  C C   . THR A 30  ? 0.49677 0.79782 0.47077 0.16620  -0.09334 0.21397  24  THR A C   
126  O O   . THR A 30  ? 0.50458 0.79739 0.45323 0.17027  -0.08759 0.22953  24  THR A O   
127  C CB  . THR A 30  ? 0.47900 0.81448 0.44546 0.11829  -0.13209 0.21271  24  THR A CB  
128  O OG1 . THR A 30  ? 0.47439 0.82413 0.45295 0.10585  -0.14287 0.21081  24  THR A OG1 
129  C CG2 . THR A 30  ? 0.50287 0.81000 0.43519 0.11831  -0.13857 0.20879  24  THR A CG2 
130  N N   . ASN A 31  ? 0.54601 0.79144 0.50838 0.18581  -0.06818 0.19329  25  ASN A N   
131  C CA  . ASN A 31  ? 0.57680 0.78261 0.52886 0.21127  -0.06332 0.17649  25  ASN A CA  
132  C C   . ASN A 31  ? 0.59846 0.76847 0.54460 0.24033  -0.05295 0.17426  25  ASN A C   
133  O O   . ASN A 31  ? 0.60173 0.76969 0.54763 0.25244  -0.03159 0.17617  25  ASN A O   
134  C CB  . ASN A 31  ? 0.57173 0.78652 0.52841 0.20541  -0.07682 0.16616  25  ASN A CB  
135  C CG  . ASN A 31  ? 0.59201 0.79210 0.53776 0.18988  -0.06337 0.14790  25  ASN A CG  
136  O OD1 . ASN A 31  ? 0.60295 0.79567 0.54535 0.18148  -0.06064 0.13582  25  ASN A OD1 
137  N ND2 . ASN A 31  ? 0.59079 0.79280 0.53419 0.19255  -0.05845 0.14903  25  ASN A ND2 
138  N N   . LEU A 32  ? 0.62214 0.74949 0.56040 0.25134  -0.03712 0.16585  26  LEU A N   
139  C CA  . LEU A 32  ? 0.64760 0.73396 0.57073 0.26424  -0.02644 0.14836  26  LEU A CA  
140  C C   . LEU A 32  ? 0.67094 0.72336 0.57214 0.28753  -0.02692 0.15538  26  LEU A C   
141  O O   . LEU A 32  ? 0.69474 0.72149 0.56869 0.29365  -0.01183 0.16624  26  LEU A O   
142  C CB  . LEU A 32  ? 0.65909 0.73517 0.59292 0.24657  -0.00487 0.12539  26  LEU A CB  
143  C CG  . LEU A 32  ? 0.67352 0.73848 0.61234 0.22972  0.02190  0.10399  26  LEU A CG  
144  C CD1 . LEU A 32  ? 0.67050 0.74002 0.61346 0.22814  0.02048  0.10015  26  LEU A CD1 
145  C CD2 . LEU A 32  ? 0.68027 0.73967 0.62088 0.22735  0.03009  0.09695  26  LEU A CD2 
146  N N   . SER A 33  ? 0.66701 0.71089 0.55835 0.29838  -0.05354 0.15362  27  SER A N   
147  C CA  . SER A 33  ? 0.67853 0.70755 0.56309 0.29578  -0.04986 0.13173  27  SER A CA  
148  C C   . SER A 33  ? 0.70239 0.70206 0.56327 0.28314  -0.02344 0.08426  27  SER A C   
149  O O   . SER A 33  ? 0.68336 0.70063 0.55709 0.30835  -0.04892 0.09122  27  SER A O   
150  C CB  . SER A 33  ? 0.67519 0.71664 0.57901 0.28372  -0.05926 0.13661  27  SER A CB  
151  O OG  . SER A 33  ? 0.68464 0.72016 0.59958 0.28067  -0.04729 0.13908  27  SER A OG  
152  N N   . TYR A 34  ? 0.73377 0.69674 0.56286 0.26236  -0.00288 0.04885  28  TYR A N   
153  C CA  . TYR A 34  ? 0.75674 0.69065 0.56086 0.25101  -0.01795 0.02528  28  TYR A CA  
154  C C   . TYR A 34  ? 0.76955 0.67835 0.54558 0.23765  -0.00395 0.00716  28  TYR A C   
155  O O   . TYR A 34  ? 0.77386 0.68181 0.55532 0.25174  0.00708  -0.00677 28  TYR A O   
156  C CB  . TYR A 34  ? 0.77681 0.69322 0.57696 0.24305  -0.03052 0.00766  28  TYR A CB  
157  C CG  . TYR A 34  ? 0.80277 0.69890 0.59232 0.22942  -0.03636 -0.01681 28  TYR A CG  
158  C CD1 . TYR A 34  ? 0.81148 0.70066 0.59668 0.22513  -0.04395 -0.02179 28  TYR A CD1 
159  C CD2 . TYR A 34  ? 0.81560 0.70508 0.60217 0.22342  -0.03984 -0.02944 28  TYR A CD2 
160  C CE1 . TYR A 34  ? 0.81883 0.70673 0.59694 0.21997  -0.05580 -0.02844 28  TYR A CE1 
161  C CE2 . TYR A 34  ? 0.81526 0.70918 0.60088 0.22082  -0.05756 -0.03676 28  TYR A CE2 
162  C CZ  . TYR A 34  ? 0.82615 0.71311 0.60620 0.21506  -0.06372 -0.03830 28  TYR A CZ  
163  O OH  . TYR A 34  ? 0.83902 0.71951 0.61926 0.20675  -0.06733 -0.04563 28  TYR A OH  
164  N N   . ILE A 35  ? 0.77142 0.65841 0.50876 0.21599  -0.02405 0.00750  29  ILE A N   
165  C CA  . ILE A 35  ? 0.79003 0.64033 0.49164 0.19678  -0.02101 0.00405  29  ILE A CA  
166  C C   . ILE A 35  ? 0.80350 0.62563 0.48150 0.17947  -0.03732 0.00255  29  ILE A C   
167  O O   . ILE A 35  ? 0.81275 0.62621 0.46712 0.17393  -0.03419 0.00192  29  ILE A O   
168  C CB  . ILE A 35  ? 0.78081 0.63747 0.47393 0.20089  -0.03135 0.00352  29  ILE A CB  
169  C CG1 . ILE A 35  ? 0.76830 0.63267 0.45964 0.20429  -0.04508 0.00502  29  ILE A CG1 
170  C CG2 . ILE A 35  ? 0.78781 0.63795 0.46115 0.20010  -0.04471 0.00711  29  ILE A CG2 
171  C CD1 . ILE A 35  ? 0.75411 0.63131 0.44433 0.20852  -0.06969 0.01245  29  ILE A CD1 
172  N N   . GLY A 36  ? 0.82797 0.61722 0.48541 0.16010  -0.04174 0.00395  30  GLY A N   
173  C CA  . GLY A 36  ? 0.84219 0.61465 0.48597 0.13621  -0.06738 0.00434  30  GLY A CA  
174  C C   . GLY A 36  ? 0.85986 0.61735 0.49889 0.11109  -0.07542 0.00381  30  GLY A C   
175  O O   . GLY A 36  ? 0.86371 0.61050 0.49947 0.12020  -0.07987 -0.00214 30  GLY A O   
176  N N   . GLU A 37  ? 0.87715 0.63092 0.51317 0.07128  -0.07549 0.00092  31  GLU A N   
177  C CA  . GLU A 37  ? 0.89292 0.65022 0.53974 0.03332  -0.07824 -0.00590 31  GLU A CA  
178  C C   . GLU A 37  ? 0.89703 0.65685 0.53399 -0.00303 -0.08535 -0.00897 31  GLU A C   
179  O O   . GLU A 37  ? 0.90322 0.66249 0.50773 -0.01608 -0.09421 -0.01870 31  GLU A O   
180  C CB  . GLU A 37  ? 0.90356 0.66493 0.56287 0.03464  -0.08307 -0.00249 31  GLU A CB  
181  C CG  . GLU A 37  ? 0.91437 0.67800 0.59027 0.03928  -0.07530 0.00313  31  GLU A CG  
182  C CD  . GLU A 37  ? 0.92650 0.69012 0.61725 0.04247  -0.06901 0.01052  31  GLU A CD  
183  O OE1 . GLU A 37  ? 0.92293 0.69748 0.62484 0.04400  -0.06271 0.01258  31  GLU A OE1 
184  O OE2 . GLU A 37  ? 0.93787 0.68912 0.62629 0.04175  -0.06871 0.01505  31  GLU A OE2 
185  N N   . GLY A 38  ? 0.89796 0.65838 0.55985 -0.02369 -0.08231 -0.00061 32  GLY A N   
186  C CA  . GLY A 38  ? 0.89117 0.65239 0.56938 -0.04049 -0.08732 -0.00144 32  GLY A CA  
187  C C   . GLY A 38  ? 0.88440 0.64524 0.58074 -0.06112 -0.09343 -0.00785 32  GLY A C   
188  O O   . GLY A 38  ? 0.88554 0.64861 0.61287 -0.06437 -0.08332 -0.00690 32  GLY A O   
189  N N   . ALA A 39  ? 0.88479 0.63221 0.56018 -0.07364 -0.10723 -0.01214 33  ALA A N   
190  C CA  . ALA A 39  ? 0.89041 0.62564 0.56176 -0.08299 -0.11469 -0.01453 33  ALA A CA  
191  C C   . ALA A 39  ? 0.88968 0.61420 0.57778 -0.10479 -0.13100 -0.04073 33  ALA A C   
192  O O   . ALA A 39  ? 0.87852 0.61007 0.57119 -0.11291 -0.15998 -0.06208 33  ALA A O   
193  C CB  . ALA A 39  ? 0.89850 0.62692 0.56321 -0.08007 -0.10501 -0.00940 33  ALA A CB  
194  N N   . TYR A 40  ? 0.88777 0.60334 0.57830 -0.12470 -0.14136 -0.05501 34  TYR A N   
195  C CA  . TYR A 40  ? 0.87865 0.59267 0.59957 -0.12816 -0.14265 -0.04407 34  TYR A CA  
196  C C   . TYR A 40  ? 0.87408 0.56574 0.59335 -0.13131 -0.13116 -0.04965 34  TYR A C   
197  O O   . TYR A 40  ? 0.88042 0.55846 0.58607 -0.14051 -0.13411 -0.05449 34  TYR A O   
198  C CB  . TYR A 40  ? 0.86673 0.61087 0.62339 -0.13149 -0.16085 -0.04292 34  TYR A CB  
199  C CG  . TYR A 40  ? 0.85630 0.63083 0.65062 -0.13375 -0.17520 -0.04427 34  TYR A CG  
200  C CD1 . TYR A 40  ? 0.85429 0.64089 0.65889 -0.13547 -0.18296 -0.04425 34  TYR A CD1 
201  C CD2 . TYR A 40  ? 0.85283 0.63954 0.65865 -0.13800 -0.18275 -0.04674 34  TYR A CD2 
202  C CE1 . TYR A 40  ? 0.85521 0.64857 0.66983 -0.13891 -0.17946 -0.04760 34  TYR A CE1 
203  C CE2 . TYR A 40  ? 0.85424 0.64777 0.66579 -0.14145 -0.18064 -0.04781 34  TYR A CE2 
204  C CZ  . TYR A 40  ? 0.85370 0.65415 0.66647 -0.13801 -0.18589 -0.04409 34  TYR A CZ  
205  O OH  . TYR A 40  ? 0.85090 0.66277 0.65837 -0.14225 -0.19525 -0.04109 34  TYR A OH  
206  N N   . GLY A 41  ? 0.87151 0.54740 0.58477 -0.11841 -0.11497 -0.04690 35  GLY A N   
207  C CA  . GLY A 41  ? 0.86266 0.53615 0.55417 -0.10171 -0.10632 -0.04131 35  GLY A CA  
208  C C   . GLY A 41  ? 0.85179 0.52605 0.52093 -0.08207 -0.09952 -0.02365 35  GLY A C   
209  O O   . GLY A 41  ? 0.85735 0.52737 0.49620 -0.08101 -0.12410 -0.01908 35  GLY A O   
210  N N   . MET A 42  ? 0.82906 0.51297 0.49306 -0.05649 -0.08668 -0.00836 36  MET A N   
211  C CA  . MET A 42  ? 0.81426 0.50614 0.48218 -0.02226 -0.05985 0.01304  36  MET A CA  
212  C C   . MET A 42  ? 0.79566 0.49569 0.42180 0.02047  -0.03323 0.03387  36  MET A C   
213  O O   . MET A 42  ? 0.78268 0.49322 0.40216 0.03374  -0.02465 0.05614  36  MET A O   
214  C CB  . MET A 42  ? 0.81964 0.51292 0.51798 -0.02919 -0.05660 0.01870  36  MET A CB  
215  C CG  . MET A 42  ? 0.82742 0.52399 0.55187 -0.02574 -0.04564 0.02076  36  MET A CG  
216  S SD  . MET A 42  ? 0.83826 0.53874 0.58765 -0.02051 -0.03557 0.01997  36  MET A SD  
217  C CE  . MET A 42  ? 0.83552 0.53515 0.58879 -0.01857 -0.03847 0.02140  36  MET A CE  
218  N N   . VAL A 43  ? 0.78921 0.48894 0.37041 0.05392  -0.01409 0.03699  37  VAL A N   
219  C CA  . VAL A 43  ? 0.77231 0.48773 0.34336 0.10445  0.00682  0.04826  37  VAL A CA  
220  C C   . VAL A 43  ? 0.76841 0.49429 0.34472 0.15255  0.03323  0.07022  37  VAL A C   
221  O O   . VAL A 43  ? 0.77343 0.48374 0.33967 0.16515  0.05782  0.06723  37  VAL A O   
222  C CB  . VAL A 43  ? 0.75434 0.47495 0.30813 0.10221  0.00578  0.04732  37  VAL A CB  
223  C CG1 . VAL A 43  ? 0.74310 0.47044 0.28591 0.10455  -0.00331 0.05014  37  VAL A CG1 
224  C CG2 . VAL A 43  ? 0.76474 0.47220 0.31878 0.09373  0.01086  0.03973  37  VAL A CG2 
225  N N   . CYS A 44  ? 0.75265 0.51081 0.34464 0.19164  0.02238  0.09468  38  CYS A N   
226  C CA  . CYS A 44  ? 0.73158 0.52709 0.34909 0.22810  0.01075  0.09761  38  CYS A CA  
227  C C   . CYS A 44  ? 0.67725 0.55801 0.32870 0.24941  -0.02756 0.09181  38  CYS A C   
228  O O   . CYS A 44  ? 0.65714 0.56304 0.32914 0.27170  -0.05603 0.07911  38  CYS A O   
229  C CB  . CYS A 44  ? 0.76485 0.50960 0.36665 0.25463  0.02945  0.10425  38  CYS A CB  
230  S SG  . CYS A 44  ? 0.79667 0.50026 0.40097 0.27034  0.06250  0.08483  38  CYS A SG  
231  N N   . SER A 45  ? 0.62823 0.57854 0.30917 0.26509  -0.02174 0.11007  39  SER A N   
232  C CA  . SER A 45  ? 0.58654 0.60370 0.33172 0.26040  0.01086  0.11415  39  SER A CA  
233  C C   . SER A 45  ? 0.54214 0.62339 0.36465 0.24673  0.02354  0.13260  39  SER A C   
234  O O   . SER A 45  ? 0.55849 0.62095 0.37481 0.24467  0.04157  0.13227  39  SER A O   
235  C CB  . SER A 45  ? 0.60114 0.60584 0.33557 0.27928  0.02237  0.09812  39  SER A CB  
236  O OG  . SER A 45  ? 0.62500 0.60456 0.33901 0.29239  0.02764  0.10152  39  SER A OG  
237  N N   . ALA A 46  ? 0.48129 0.65063 0.38157 0.23039  0.01951  0.15103  40  ALA A N   
238  C CA  . ALA A 46  ? 0.40698 0.67920 0.39681 0.20893  -0.00127 0.16369  40  ALA A CA  
239  C C   . ALA A 46  ? 0.33214 0.70700 0.41492 0.17645  -0.03635 0.16626  40  ALA A C   
240  O O   . ALA A 46  ? 0.32440 0.71474 0.41111 0.17768  -0.03510 0.15827  40  ALA A O   
241  C CB  . ALA A 46  ? 0.41507 0.67793 0.37673 0.19865  0.02793  0.16504  40  ALA A CB  
242  N N   . TYR A 47  ? 0.29018 0.70502 0.43334 0.12956  -0.06365 0.15512  41  TYR A N   
243  C CA  . TYR A 47  ? 0.27834 0.72811 0.43297 0.08891  -0.07791 0.16121  41  TYR A CA  
244  C C   . TYR A 47  ? 0.28080 0.79030 0.44672 0.06550  -0.06077 0.20120  41  TYR A C   
245  O O   . TYR A 47  ? 0.27737 0.80359 0.43960 0.06803  -0.03231 0.21499  41  TYR A O   
246  C CB  . TYR A 47  ? 0.27814 0.71233 0.42084 0.06496  -0.09621 0.15259  41  TYR A CB  
247  C CG  . TYR A 47  ? 0.27375 0.76574 0.42009 0.05030  -0.08022 0.17182  41  TYR A CG  
248  C CD1 . TYR A 47  ? 0.27362 0.77850 0.41063 0.04182  -0.07780 0.17419  41  TYR A CD1 
249  C CD2 . TYR A 47  ? 0.27490 0.78560 0.42674 0.03006  -0.06778 0.16169  41  TYR A CD2 
250  C CE1 . TYR A 47  ? 0.25333 0.78690 0.42201 0.01978  -0.06781 0.17121  41  TYR A CE1 
251  C CE2 . TYR A 47  ? 0.27129 0.78875 0.44289 0.01641  -0.03580 0.16275  41  TYR A CE2 
252  C CZ  . TYR A 47  ? 0.26349 0.79002 0.43629 0.00588  -0.03894 0.15991  41  TYR A CZ  
253  O OH  . TYR A 47  ? 0.23453 0.79348 0.42907 -0.00439 -0.05572 0.14660  41  TYR A OH  
254  N N   . ASP A 48  ? 0.29380 0.79319 0.43357 0.03030  -0.08615 0.20594  42  ASP A N   
255  C CA  . ASP A 48  ? 0.29824 0.81550 0.44529 -0.00264 -0.09767 0.20864  42  ASP A CA  
256  C C   . ASP A 48  ? 0.32180 0.82504 0.46652 -0.03692 -0.10729 0.21005  42  ASP A C   
257  O O   . ASP A 48  ? 0.30455 0.82611 0.45734 -0.05646 -0.11488 0.21564  42  ASP A O   
258  C CB  . ASP A 48  ? 0.31673 0.82352 0.43272 -0.00985 -0.07371 0.19798  42  ASP A CB  
259  C CG  . ASP A 48  ? 0.34061 0.82887 0.42644 -0.01700 -0.04250 0.18860  42  ASP A CG  
260  O OD1 . ASP A 48  ? 0.35600 0.82956 0.43884 -0.02779 -0.02795 0.17336  42  ASP A OD1 
261  O OD2 . ASP A 48  ? 0.37195 0.83169 0.41834 -0.02077 -0.01433 0.19151  42  ASP A OD2 
262  N N   . ASN A 49  ? 0.34003 0.82522 0.47316 -0.05424 -0.13171 0.20861  43  ASN A N   
263  C CA  . ASN A 49  ? 0.39207 0.82763 0.49375 -0.08013 -0.13402 0.19181  43  ASN A CA  
264  C C   . ASN A 49  ? 0.42140 0.82455 0.50396 -0.11085 -0.14270 0.16891  43  ASN A C   
265  O O   . ASN A 49  ? 0.45372 0.82620 0.51192 -0.12373 -0.14430 0.14729  43  ASN A O   
266  C CB  . ASN A 49  ? 0.40832 0.83592 0.50021 -0.06324 -0.13384 0.21170  43  ASN A CB  
267  C CG  . ASN A 49  ? 0.40785 0.84410 0.50492 -0.04699 -0.16389 0.23412  43  ASN A CG  
268  O OD1 . ASN A 49  ? 0.43326 0.85579 0.50906 -0.04204 -0.14463 0.24365  43  ASN A OD1 
269  N ND2 . ASN A 49  ? 0.40614 0.81849 0.49916 -0.04200 -0.18184 0.22458  43  ASN A ND2 
270  N N   . LEU A 50  ? 0.43231 0.82005 0.49110 -0.12015 -0.15199 0.17285  44  LEU A N   
271  C CA  . LEU A 50  ? 0.44360 0.81574 0.50591 -0.14944 -0.14031 0.15573  44  LEU A CA  
272  C C   . LEU A 50  ? 0.46419 0.82070 0.52072 -0.16252 -0.14247 0.15005  44  LEU A C   
273  O O   . LEU A 50  ? 0.46637 0.81788 0.54302 -0.17791 -0.12935 0.15069  44  LEU A O   
274  C CB  . LEU A 50  ? 0.44710 0.81017 0.52357 -0.15655 -0.12639 0.13574  44  LEU A CB  
275  C CG  . LEU A 50  ? 0.44296 0.80297 0.53448 -0.16855 -0.12470 0.12212  44  LEU A CG  
276  C CD1 . LEU A 50  ? 0.43587 0.80635 0.52779 -0.17008 -0.12920 0.11796  44  LEU A CD1 
277  C CD2 . LEU A 50  ? 0.44537 0.79701 0.54579 -0.17913 -0.11477 0.11617  44  LEU A CD2 
278  N N   . ASN A 51  ? 0.46036 0.82334 0.49392 -0.16592 -0.16269 0.14930  45  ASN A N   
279  C CA  . ASN A 51  ? 0.46911 0.81858 0.49570 -0.17099 -0.12946 0.15158  45  ASN A CA  
280  C C   . ASN A 51  ? 0.42280 0.82354 0.50278 -0.16467 -0.10876 0.15735  45  ASN A C   
281  O O   . ASN A 51  ? 0.40800 0.82211 0.51510 -0.18382 -0.09231 0.15505  45  ASN A O   
282  C CB  . ASN A 51  ? 0.51021 0.81089 0.49826 -0.17558 -0.12482 0.15313  45  ASN A CB  
283  C CG  . ASN A 51  ? 0.56499 0.80934 0.52944 -0.17508 -0.10376 0.15372  45  ASN A CG  
284  O OD1 . ASN A 51  ? 0.60797 0.81341 0.54960 -0.16292 -0.08119 0.15584  45  ASN A OD1 
285  N ND2 . ASN A 51  ? 0.58477 0.80816 0.54956 -0.18047 -0.07660 0.14807  45  ASN A ND2 
286  N N   . LYS A 52  ? 0.41088 0.83030 0.50869 -0.13860 -0.07880 0.16225  46  LYS A N   
287  C CA  . LYS A 52  ? 0.39131 0.83087 0.51447 -0.12160 -0.05451 0.15488  46  LYS A CA  
288  C C   . LYS A 52  ? 0.37039 0.82513 0.51392 -0.10896 -0.03952 0.14257  46  LYS A C   
289  O O   . LYS A 52  ? 0.33271 0.82815 0.52676 -0.11920 -0.06378 0.12502  46  LYS A O   
290  C CB  . LYS A 52  ? 0.38787 0.83372 0.52436 -0.11282 -0.04667 0.15308  46  LYS A CB  
291  C CG  . LYS A 52  ? 0.38759 0.83473 0.52915 -0.10543 -0.03751 0.15042  46  LYS A CG  
292  C CD  . LYS A 52  ? 0.40137 0.83323 0.53754 -0.09929 -0.02271 0.15205  46  LYS A CD  
293  C CE  . LYS A 52  ? 0.41510 0.83301 0.55090 -0.09082 -0.00695 0.15711  46  LYS A CE  
294  N NZ  . LYS A 52  ? 0.41431 0.83191 0.55945 -0.08546 -0.00138 0.16238  46  LYS A NZ  
295  N N   . VAL A 53  ? 0.34963 0.81528 0.49170 -0.08100 -0.04990 0.14466  47  VAL A N   
296  C CA  . VAL A 53  ? 0.36267 0.80613 0.48353 -0.04988 -0.02024 0.15207  47  VAL A CA  
297  C C   . VAL A 53  ? 0.32984 0.79548 0.45572 -0.01092 -0.03840 0.15895  47  VAL A C   
298  O O   . VAL A 53  ? 0.30352 0.79656 0.44328 -0.00051 -0.04983 0.18208  47  VAL A O   
299  C CB  . VAL A 53  ? 0.39165 0.80815 0.51018 -0.06129 0.01575  0.13936  47  VAL A CB  
300  C CG1 . VAL A 53  ? 0.42624 0.80974 0.51894 -0.06685 0.04581  0.14663  47  VAL A CG1 
301  C CG2 . VAL A 53  ? 0.39735 0.80805 0.52216 -0.05782 0.02928  0.13112  47  VAL A CG2 
302  N N   . ARG A 54  ? 0.32668 0.78034 0.44632 0.02129  -0.01683 0.15921  48  ARG A N   
303  C CA  . ARG A 54  ? 0.29949 0.76211 0.41927 0.05554  -0.02991 0.16203  48  ARG A CA  
304  C C   . ARG A 54  ? 0.27903 0.73981 0.38180 0.05720  -0.01449 0.15839  48  ARG A C   
305  O O   . ARG A 54  ? 0.26197 0.74311 0.37337 0.03911  -0.01433 0.15898  48  ARG A O   
306  C CB  . ARG A 54  ? 0.30398 0.76492 0.43433 0.09423  -0.03282 0.16733  48  ARG A CB  
307  C CG  . ARG A 54  ? 0.32660 0.77099 0.48126 0.12099  0.01099  0.16057  48  ARG A CG  
308  C CD  . ARG A 54  ? 0.32288 0.77718 0.50194 0.14764  0.03466  0.15655  48  ARG A CD  
309  N NE  . ARG A 54  ? 0.29635 0.78367 0.52028 0.16636  0.04084  0.15004  48  ARG A NE  
310  C CZ  . ARG A 54  ? 0.29457 0.79226 0.54188 0.18746  0.03480  0.15213  48  ARG A CZ  
311  N NH1 . ARG A 54  ? 0.29778 0.78710 0.55618 0.19201  0.02451  0.14508  48  ARG A NH1 
312  N NH2 . ARG A 54  ? 0.30030 0.78902 0.54113 0.19313  0.05158  0.15799  48  ARG A NH2 
313  N N   . VAL A 55  ? 0.24093 0.71353 0.33249 0.07288  -0.03513 0.15536  49  VAL A N   
314  C CA  . VAL A 55  ? 0.24638 0.68033 0.28385 0.06810  -0.03562 0.13101  49  VAL A CA  
315  C C   . VAL A 55  ? 0.25934 0.64404 0.25627 0.09592  -0.03196 0.11313  49  VAL A C   
316  O O   . VAL A 55  ? 0.26334 0.65619 0.26267 0.09724  -0.05010 0.09423  49  VAL A O   
317  C CB  . VAL A 55  ? 0.25371 0.68205 0.27781 0.04133  -0.03789 0.14488  49  VAL A CB  
318  C CG1 . VAL A 55  ? 0.27945 0.67933 0.28400 0.01311  -0.01734 0.14227  49  VAL A CG1 
319  C CG2 . VAL A 55  ? 0.26296 0.66426 0.27408 0.04705  -0.04719 0.14802  49  VAL A CG2 
320  N N   . ALA A 56  ? 0.28824 0.59474 0.23124 0.10356  -0.01355 0.10563  50  ALA A N   
321  C CA  . ALA A 56  ? 0.29006 0.54233 0.21715 0.11706  0.00780  0.10035  50  ALA A CA  
322  C C   . ALA A 56  ? 0.29978 0.50731 0.22914 0.09766  0.00195  0.09505  50  ALA A C   
323  O O   . ALA A 56  ? 0.31954 0.50122 0.25281 0.08585  0.04431  0.09544  50  ALA A O   
324  C CB  . ALA A 56  ? 0.28200 0.52103 0.20789 0.15048  0.00565  0.10275  50  ALA A CB  
325  N N   . ILE A 57  ? 0.29997 0.47902 0.22632 0.07843  -0.01072 0.08801  51  ILE A N   
326  C CA  . ILE A 57  ? 0.34497 0.45427 0.21787 0.06904  -0.02847 0.07366  51  ILE A CA  
327  C C   . ILE A 57  ? 0.38706 0.43471 0.24445 0.05127  -0.02734 0.07463  51  ILE A C   
328  O O   . ILE A 57  ? 0.41422 0.42222 0.24489 0.06025  -0.05185 0.07767  51  ILE A O   
329  C CB  . ILE A 57  ? 0.33085 0.44819 0.18665 0.07795  -0.02950 0.07600  51  ILE A CB  
330  C CG1 . ILE A 57  ? 0.34527 0.44906 0.17798 0.07739  -0.03768 0.07540  51  ILE A CG1 
331  C CG2 . ILE A 57  ? 0.31683 0.44899 0.15027 0.08863  -0.03347 0.05734  51  ILE A CG2 
332  C CD1 . ILE A 57  ? 0.36212 0.44785 0.17153 0.09194  -0.03780 0.07796  51  ILE A CD1 
333  N N   . LYS A 58  ? 0.37083 0.42536 0.24596 0.04488  -0.03256 0.07184  52  LYS A N   
334  C CA  . LYS A 58  ? 0.40836 0.43595 0.23264 0.03405  -0.06034 0.06689  52  LYS A CA  
335  C C   . LYS A 58  ? 0.43553 0.41266 0.21196 0.00809  -0.03169 0.09449  52  LYS A C   
336  O O   . LYS A 58  ? 0.45053 0.40332 0.19605 -0.00483 0.00129  0.09349  52  LYS A O   
337  C CB  . LYS A 58  ? 0.39989 0.46770 0.25068 0.03197  -0.11171 0.04358  52  LYS A CB  
338  C CG  . LYS A 58  ? 0.44506 0.49123 0.29721 0.05208  -0.08956 0.04305  52  LYS A CG  
339  C CD  . LYS A 58  ? 0.44730 0.49057 0.30474 0.08382  -0.09531 0.04483  52  LYS A CD  
340  C CE  . LYS A 58  ? 0.44325 0.48748 0.29504 0.08092  -0.11359 0.03581  52  LYS A CE  
341  N NZ  . LYS A 58  ? 0.41161 0.48582 0.30943 0.08589  -0.13740 0.02175  52  LYS A NZ  
342  N N   . LYS A 59  ? 0.46955 0.40767 0.22861 -0.01070 -0.02557 0.09819  53  LYS A N   
343  C CA  . LYS A 59  ? 0.52064 0.41003 0.24091 -0.02929 -0.03246 0.08263  53  LYS A CA  
344  C C   . LYS A 59  ? 0.53409 0.41514 0.24502 -0.07153 -0.04725 0.04958  53  LYS A C   
345  O O   . LYS A 59  ? 0.55683 0.41789 0.24238 -0.08574 -0.05123 0.01127  53  LYS A O   
346  C CB  . LYS A 59  ? 0.55526 0.40842 0.25057 -0.03228 -0.01171 0.10552  53  LYS A CB  
347  C CG  . LYS A 59  ? 0.57722 0.41195 0.29761 -0.03040 0.00006  0.12401  53  LYS A CG  
348  C CD  . LYS A 59  ? 0.61628 0.43366 0.33955 -0.03497 0.03771  0.11502  53  LYS A CD  
349  C CE  . LYS A 59  ? 0.64470 0.45999 0.40230 -0.04409 0.07515  0.08799  53  LYS A CE  
350  N NZ  . LYS A 59  ? 0.66040 0.47873 0.42605 -0.04875 0.07895  0.06692  53  LYS A NZ  
351  N N   . ILE A 60  ? 0.51498 0.41459 0.24015 -0.10817 -0.03936 0.05906  54  ILE A N   
352  C CA  . ILE A 60  ? 0.51755 0.42219 0.26635 -0.15355 -0.02194 0.05248  54  ILE A CA  
353  C C   . ILE A 60  ? 0.53558 0.43936 0.28602 -0.18861 -0.03260 0.06526  54  ILE A C   
354  O O   . ILE A 60  ? 0.51083 0.43744 0.26174 -0.19426 -0.07076 0.06525  54  ILE A O   
355  C CB  . ILE A 60  ? 0.49172 0.41927 0.27986 -0.15266 -0.02576 0.04970  54  ILE A CB  
356  C CG1 . ILE A 60  ? 0.49620 0.41463 0.31495 -0.14477 -0.02074 0.05330  54  ILE A CG1 
357  C CG2 . ILE A 60  ? 0.50878 0.42995 0.30038 -0.14236 -0.00753 0.03745  54  ILE A CG2 
358  C CD1 . ILE A 60  ? 0.49348 0.41265 0.33378 -0.15766 -0.00802 0.05843  54  ILE A CD1 
359  N N   . SER A 61  ? 0.55720 0.45931 0.30516 -0.23143 -0.03098 0.07257  55  SER A N   
360  C CA  . SER A 61  ? 0.58709 0.48927 0.33051 -0.24275 -0.03371 0.07516  55  SER A CA  
361  C C   . SER A 61  ? 0.59632 0.49508 0.33382 -0.28515 -0.07558 0.04069  55  SER A C   
362  O O   . SER A 61  ? 0.62625 0.47555 0.36201 -0.30467 -0.08213 0.03029  55  SER A O   
363  C CB  . SER A 61  ? 0.60099 0.51415 0.35019 -0.22170 -0.02160 0.08563  55  SER A CB  
364  O OG  . SER A 61  ? 0.60738 0.53191 0.35458 -0.21144 -0.03428 0.09097  55  SER A OG  
365  N N   . PRO A 62  ? 0.58995 0.52097 0.31520 -0.30568 -0.07489 0.03055  56  PRO A N   
366  C CA  . PRO A 62  ? 0.58037 0.53830 0.31689 -0.30757 -0.08203 0.05917  56  PRO A CA  
367  C C   . PRO A 62  ? 0.57232 0.56692 0.32832 -0.31627 -0.08849 0.09569  56  PRO A C   
368  O O   . PRO A 62  ? 0.57686 0.58039 0.32682 -0.31485 -0.07831 0.11807  56  PRO A O   
369  C CB  . PRO A 62  ? 0.58660 0.52879 0.32569 -0.31713 -0.06994 0.04463  56  PRO A CB  
370  C CG  . PRO A 62  ? 0.59666 0.52826 0.31755 -0.30530 -0.05364 0.05410  56  PRO A CG  
371  C CD  . PRO A 62  ? 0.59542 0.52288 0.31812 -0.30705 -0.05759 0.04315  56  PRO A CD  
372  N N   . PHE A 63  ? 0.55951 0.58215 0.32680 -0.30785 -0.10869 0.12511  57  PHE A N   
373  C CA  . PHE A 63  ? 0.54269 0.60034 0.36921 -0.31036 -0.08022 0.14945  57  PHE A CA  
374  C C   . PHE A 63  ? 0.57485 0.61001 0.45852 -0.29699 -0.02625 0.16594  57  PHE A C   
375  O O   . PHE A 63  ? 0.58986 0.61552 0.47572 -0.27782 0.02510  0.18505  57  PHE A O   
376  C CB  . PHE A 63  ? 0.52411 0.60876 0.32881 -0.29702 -0.07991 0.15804  57  PHE A CB  
377  C CG  . PHE A 63  ? 0.47133 0.61068 0.28684 -0.30055 -0.10507 0.14413  57  PHE A CG  
378  C CD1 . PHE A 63  ? 0.46283 0.60983 0.26810 -0.29165 -0.09859 0.13382  57  PHE A CD1 
379  C CD2 . PHE A 63  ? 0.46505 0.60565 0.28629 -0.29552 -0.09903 0.14255  57  PHE A CD2 
380  C CE1 . PHE A 63  ? 0.45946 0.59441 0.25450 -0.29996 -0.08918 0.11393  57  PHE A CE1 
381  C CE2 . PHE A 63  ? 0.46868 0.61143 0.26828 -0.30554 -0.10207 0.12765  57  PHE A CE2 
382  C CZ  . PHE A 63  ? 0.46324 0.60130 0.25712 -0.30311 -0.09301 0.11700  57  PHE A CZ  
383  N N   . GLU A 64  ? 0.57309 0.59659 0.50668 -0.32238 -0.04768 0.15404  58  GLU A N   
384  C CA  A GLU A 64  ? 0.59147 0.59898 0.54473 -0.32308 -0.03651 0.16335  58  GLU A CA  
385  C CA  B GLU A 64  ? 0.59799 0.60845 0.54519 -0.31001 -0.03592 0.16434  58  GLU A CA  
386  C C   . GLU A 64  ? 0.60068 0.61653 0.55335 -0.32656 -0.04125 0.16674  58  GLU A C   
387  O O   . GLU A 64  ? 0.57988 0.61861 0.56700 -0.33641 -0.05286 0.14947  58  GLU A O   
388  C CB  A GLU A 64  ? 0.59417 0.57535 0.56710 -0.31620 -0.02506 0.15877  58  GLU A CB  
389  C CB  B GLU A 64  ? 0.61535 0.60304 0.56510 -0.28794 -0.02371 0.17085  58  GLU A CB  
390  C CG  A GLU A 64  ? 0.59668 0.55639 0.58411 -0.31036 -0.01454 0.15463  58  GLU A CG  
391  C CG  B GLU A 64  ? 0.63383 0.60063 0.57383 -0.26357 -0.01420 0.17910  58  GLU A CG  
392  C CD  A GLU A 64  ? 0.60103 0.54095 0.59623 -0.30647 -0.00916 0.15147  58  GLU A CD  
393  C CD  B GLU A 64  ? 0.64738 0.59511 0.58165 -0.25009 0.00609  0.19067  58  GLU A CD  
394  O OE1 A GLU A 64  ? 0.61795 0.54194 0.60980 -0.31645 -0.01139 0.14135  58  GLU A OE1 
395  O OE1 B GLU A 64  ? 0.65657 0.59809 0.59187 -0.23592 0.01922  0.19799  58  GLU A OE1 
396  O OE2 A GLU A 64  ? 0.59065 0.52391 0.59851 -0.28850 0.01527  0.15780  58  GLU A OE2 
397  O OE2 B GLU A 64  ? 0.65537 0.59029 0.57704 -0.24675 0.01075  0.19607  58  GLU A OE2 
398  N N   . HIS A 65  ? 0.62318 0.63360 0.56832 -0.32696 -0.04481 0.16699  59  HIS A N   
399  C CA  . HIS A 65  ? 0.62580 0.64362 0.57175 -0.33763 -0.05747 0.15819  59  HIS A CA  
400  C C   . HIS A 65  ? 0.61760 0.66027 0.57984 -0.33727 -0.06874 0.17443  59  HIS A C   
401  O O   . HIS A 65  ? 0.60430 0.65276 0.56101 -0.34413 -0.06928 0.18287  59  HIS A O   
402  C CB  . HIS A 65  ? 0.63360 0.63926 0.56471 -0.32975 -0.04638 0.14765  59  HIS A CB  
403  C CG  . HIS A 65  ? 0.64707 0.64061 0.57216 -0.30413 -0.03449 0.14163  59  HIS A CG  
404  N ND1 . HIS A 65  ? 0.65863 0.63945 0.58181 -0.29637 -0.02440 0.13968  59  HIS A ND1 
405  C CD2 . HIS A 65  ? 0.64595 0.64088 0.57280 -0.29917 -0.03544 0.13420  59  HIS A CD2 
406  C CE1 . HIS A 65  ? 0.65443 0.64099 0.58578 -0.29366 -0.02532 0.13723  59  HIS A CE1 
407  N NE2 . HIS A 65  ? 0.64551 0.64252 0.57986 -0.29327 -0.03773 0.13224  59  HIS A NE2 
408  N N   . GLN A 66  ? 0.60828 0.67468 0.58650 -0.33830 -0.08745 0.16257  60  GLN A N   
409  C CA  . GLN A 66  ? 0.59957 0.67960 0.57789 -0.34287 -0.08840 0.14963  60  GLN A CA  
410  C C   . GLN A 66  ? 0.60128 0.68586 0.53014 -0.35999 -0.10702 0.14153  60  GLN A C   
411  O O   . GLN A 66  ? 0.57491 0.68788 0.49382 -0.35941 -0.13604 0.13557  60  GLN A O   
412  C CB  . GLN A 66  ? 0.59111 0.67857 0.60779 -0.30683 -0.07053 0.14664  60  GLN A CB  
413  C CG  . GLN A 66  ? 0.60844 0.68780 0.62931 -0.25603 -0.05572 0.15341  60  GLN A CG  
414  C CD  . GLN A 66  ? 0.64525 0.71095 0.64315 -0.20873 -0.02529 0.15391  60  GLN A CD  
415  O OE1 . GLN A 66  ? 0.65175 0.72265 0.66430 -0.19503 -0.00698 0.14228  60  GLN A OE1 
416  N NE2 . GLN A 66  ? 0.67705 0.72225 0.64856 -0.19003 -0.01083 0.15680  60  GLN A NE2 
417  N N   . THR A 67  ? 0.62899 0.68123 0.52102 -0.37154 -0.08572 0.12359  61  THR A N   
418  C CA  . THR A 67  ? 0.65013 0.67996 0.51949 -0.36857 -0.07754 0.10887  61  THR A CA  
419  C C   . THR A 67  ? 0.62738 0.67343 0.48328 -0.37611 -0.08201 0.10466  61  THR A C   
420  O O   . THR A 67  ? 0.62189 0.67479 0.47423 -0.37747 -0.05732 0.11023  61  THR A O   
421  C CB  . THR A 67  ? 0.69191 0.68569 0.55150 -0.34777 -0.05519 0.11133  61  THR A CB  
422  O OG1 . THR A 67  ? 0.72456 0.69241 0.58492 -0.33190 -0.02830 0.11768  61  THR A OG1 
423  C CG2 . THR A 67  ? 0.68232 0.68179 0.54362 -0.35312 -0.07526 0.10207  61  THR A CG2 
424  N N   . TYR A 68  ? 0.61131 0.66903 0.44142 -0.37189 -0.11604 0.08925  62  TYR A N   
425  C CA  . TYR A 68  ? 0.59322 0.66623 0.40591 -0.35559 -0.13159 0.08273  62  TYR A CA  
426  C C   . TYR A 68  ? 0.55051 0.66534 0.37333 -0.34284 -0.13057 0.11399  62  TYR A C   
427  O O   . TYR A 68  ? 0.55818 0.65535 0.34685 -0.34566 -0.12793 0.12088  62  TYR A O   
428  C CB  . TYR A 68  ? 0.63487 0.66513 0.42988 -0.34515 -0.12125 0.06865  62  TYR A CB  
429  C CG  . TYR A 68  ? 0.66976 0.66565 0.44948 -0.33032 -0.11055 0.05794  62  TYR A CG  
430  C CD1 . TYR A 68  ? 0.69412 0.66625 0.45923 -0.32104 -0.09779 0.05127  62  TYR A CD1 
431  C CD2 . TYR A 68  ? 0.68802 0.66816 0.45788 -0.31866 -0.10643 0.05279  62  TYR A CD2 
432  C CE1 . TYR A 68  ? 0.71379 0.67251 0.46863 -0.30188 -0.08707 0.05294  62  TYR A CE1 
433  C CE2 . TYR A 68  ? 0.71131 0.67117 0.46536 -0.29964 -0.09314 0.05047  62  TYR A CE2 
434  C CZ  . TYR A 68  ? 0.72519 0.67608 0.47111 -0.29271 -0.08764 0.04629  62  TYR A CZ  
435  O OH  . TYR A 68  ? 0.74535 0.68395 0.47503 -0.27654 -0.08117 0.03722  62  TYR A OH  
436  N N   . CYS A 69  ? 0.50566 0.67869 0.36178 -0.31952 -0.14047 0.13614  63  CYS A N   
437  C CA  . CYS A 69  ? 0.45912 0.70432 0.35686 -0.29827 -0.13104 0.18434  63  CYS A CA  
438  C C   . CYS A 69  ? 0.41414 0.69792 0.32735 -0.27831 -0.12352 0.19526  63  CYS A C   
439  O O   . CYS A 69  ? 0.39224 0.69532 0.32197 -0.26653 -0.11538 0.19945  63  CYS A O   
440  C CB  . CYS A 69  ? 0.46720 0.71876 0.35543 -0.29576 -0.13918 0.21465  63  CYS A CB  
441  S SG  . CYS A 69  ? 0.49826 0.72405 0.37198 -0.31288 -0.10550 0.20198  63  CYS A SG  
442  N N   . GLN A 70  ? 0.39764 0.68051 0.33293 -0.25204 -0.13007 0.19074  64  GLN A N   
443  C CA  . GLN A 70  ? 0.39885 0.68449 0.33699 -0.25298 -0.13129 0.17977  64  GLN A CA  
444  C C   . GLN A 70  ? 0.41787 0.65329 0.29220 -0.26320 -0.11122 0.16830  64  GLN A C   
445  O O   . GLN A 70  ? 0.43264 0.65641 0.28528 -0.25195 -0.11369 0.15377  64  GLN A O   
446  C CB  . GLN A 70  ? 0.38127 0.68722 0.37382 -0.22715 -0.14429 0.16697  64  GLN A CB  
447  C CG  . GLN A 70  ? 0.38152 0.72468 0.40986 -0.21494 -0.15283 0.16780  64  GLN A CG  
448  C CD  . GLN A 70  ? 0.38522 0.73916 0.46965 -0.20077 -0.11536 0.16075  64  GLN A CD  
449  O OE1 . GLN A 70  ? 0.35449 0.74680 0.48584 -0.19436 -0.13257 0.15878  64  GLN A OE1 
450  N NE2 . GLN A 70  ? 0.39658 0.74408 0.49246 -0.19284 -0.10456 0.15732  64  GLN A NE2 
451  N N   . ARG A 71  ? 0.42675 0.61524 0.28272 -0.26883 -0.09060 0.15451  65  ARG A N   
452  C CA  . ARG A 71  ? 0.44388 0.58145 0.28923 -0.25250 -0.08184 0.13891  65  ARG A CA  
453  C C   . ARG A 71  ? 0.42914 0.56309 0.26605 -0.23803 -0.08748 0.13214  65  ARG A C   
454  O O   . ARG A 71  ? 0.42675 0.54392 0.25649 -0.22546 -0.09108 0.14629  65  ARG A O   
455  C CB  . ARG A 71  ? 0.48659 0.56004 0.29210 -0.24255 -0.06762 0.13962  65  ARG A CB  
456  C CG  . ARG A 71  ? 0.53542 0.53245 0.33627 -0.24211 -0.03500 0.12539  65  ARG A CG  
457  C CD  . ARG A 71  ? 0.56944 0.49459 0.35971 -0.25122 -0.01468 0.11138  65  ARG A CD  
458  N NE  . ARG A 71  ? 0.59851 0.46373 0.37000 -0.26147 -0.00580 0.11226  65  ARG A NE  
459  C CZ  . ARG A 71  ? 0.60808 0.44459 0.37804 -0.26942 -0.00497 0.10363  65  ARG A CZ  
460  N NH1 . ARG A 71  ? 0.61057 0.44396 0.38526 -0.27675 -0.00692 0.09542  65  ARG A NH1 
461  N NH2 . ARG A 71  ? 0.61642 0.42961 0.37317 -0.25417 0.00961  0.10569  65  ARG A NH2 
462  N N   . THR A 72  ? 0.42956 0.56080 0.27102 -0.21921 -0.04308 0.11946  66  THR A N   
463  C CA  . THR A 72  ? 0.37678 0.55158 0.25197 -0.19667 -0.06369 0.11550  66  THR A CA  
464  C C   . THR A 72  ? 0.30572 0.55172 0.22489 -0.15607 -0.05505 0.10803  66  THR A C   
465  O O   . THR A 72  ? 0.28042 0.54293 0.21615 -0.15019 -0.04443 0.09464  66  THR A O   
466  C CB  . THR A 72  ? 0.39658 0.55155 0.25712 -0.21027 -0.09341 0.10829  66  THR A CB  
467  O OG1 . THR A 72  ? 0.42424 0.55252 0.28092 -0.22471 -0.07927 0.12301  66  THR A OG1 
468  C CG2 . THR A 72  ? 0.38745 0.54860 0.25759 -0.22564 -0.10508 0.08855  66  THR A CG2 
469  N N   . LEU A 73  ? 0.26112 0.56155 0.21777 -0.11250 -0.06046 0.11213  67  LEU A N   
470  C CA  . LEU A 73  ? 0.23650 0.57079 0.24963 -0.08576 -0.01292 0.12302  67  LEU A CA  
471  C C   . LEU A 73  ? 0.23313 0.55674 0.24320 -0.08310 -0.03330 0.10107  67  LEU A C   
472  O O   . LEU A 73  ? 0.17583 0.55570 0.24179 -0.07773 -0.02402 0.11288  67  LEU A O   
473  C CB  . LEU A 73  ? 0.20356 0.59031 0.26576 -0.07502 0.00613  0.12092  67  LEU A CB  
474  C CG  . LEU A 73  ? 0.18850 0.59943 0.29444 -0.05391 0.01882  0.11082  67  LEU A CG  
475  C CD1 . LEU A 73  ? 0.17452 0.59182 0.30447 -0.05725 0.01543  0.10747  67  LEU A CD1 
476  C CD2 . LEU A 73  ? 0.20731 0.61656 0.34171 -0.04555 0.04586  0.09813  67  LEU A CD2 
477  N N   . ARG A 74  ? 0.26303 0.54479 0.24025 -0.08780 -0.05415 0.08345  68  ARG A N   
478  C CA  . ARG A 74  ? 0.29730 0.52705 0.23180 -0.09668 -0.09168 0.05081  68  ARG A CA  
479  C C   . ARG A 74  ? 0.28596 0.48139 0.21102 -0.07424 -0.07291 0.04577  68  ARG A C   
480  O O   . ARG A 74  ? 0.27419 0.48552 0.21402 -0.04690 -0.06337 0.06581  68  ARG A O   
481  C CB  . ARG A 74  ? 0.36647 0.55545 0.25337 -0.10742 -0.09596 0.05827  68  ARG A CB  
482  C CG  . ARG A 74  ? 0.40894 0.57750 0.32044 -0.11688 -0.09582 0.05000  68  ARG A CG  
483  C CD  . ARG A 74  ? 0.44470 0.59455 0.34161 -0.12817 -0.10049 0.04026  68  ARG A CD  
484  N NE  . ARG A 74  ? 0.47958 0.60642 0.33807 -0.13099 -0.09261 0.03577  68  ARG A NE  
485  C CZ  . ARG A 74  ? 0.50556 0.61555 0.33888 -0.12039 -0.07839 0.04515  68  ARG A CZ  
486  N NH1 . ARG A 74  ? 0.53040 0.62526 0.35251 -0.11952 -0.06655 0.05592  68  ARG A NH1 
487  N NH2 . ARG A 74  ? 0.51357 0.61601 0.32778 -0.10519 -0.07973 0.04863  68  ARG A NH2 
488  N N   . GLU A 75  ? 0.29931 0.43090 0.18668 -0.07965 -0.05732 0.01254  69  GLU A N   
489  C CA  . GLU A 75  ? 0.29695 0.39416 0.18621 -0.04008 -0.02376 0.00964  69  GLU A CA  
490  C C   . GLU A 75  ? 0.28377 0.37882 0.16306 -0.01703 -0.01722 0.02310  69  GLU A C   
491  O O   . GLU A 75  ? 0.27165 0.37260 0.15136 0.00019  -0.01359 0.02338  69  GLU A O   
492  C CB  . GLU A 75  ? 0.34990 0.38274 0.25488 -0.01666 0.01428  0.02030  69  GLU A CB  
493  C CG  . GLU A 75  ? 0.41513 0.38521 0.29520 -0.00865 0.03016  0.02245  69  GLU A CG  
494  C CD  . GLU A 75  ? 0.44017 0.39188 0.29314 0.00156  0.02804  0.03118  69  GLU A CD  
495  O OE1 . GLU A 75  ? 0.44074 0.41698 0.31227 0.01539  -0.02517 0.01843  69  GLU A OE1 
496  O OE2 . GLU A 75  ? 0.44015 0.38252 0.25801 -0.01033 0.03876  0.05051  69  GLU A OE2 
497  N N   . ILE A 76  ? 0.26872 0.37669 0.14080 -0.01445 -0.04271 0.03995  70  ILE A N   
498  C CA  . ILE A 76  ? 0.27994 0.38629 0.15490 -0.01623 -0.04971 0.06346  70  ILE A CA  
499  C C   . ILE A 76  ? 0.27375 0.38006 0.17307 -0.00570 -0.05276 0.05394  70  ILE A C   
500  O O   . ILE A 76  ? 0.28795 0.37433 0.19175 -0.00603 -0.05854 0.03865  70  ILE A O   
501  C CB  . ILE A 76  ? 0.29115 0.39826 0.15147 -0.05694 -0.04251 0.07349  70  ILE A CB  
502  C CG1 . ILE A 76  ? 0.27999 0.40351 0.16244 -0.05571 0.00371  0.10794  70  ILE A CG1 
503  C CG2 . ILE A 76  ? 0.32845 0.40560 0.14931 -0.05853 -0.06021 0.07840  70  ILE A CG2 
504  C CD1 . ILE A 76  ? 0.30282 0.41747 0.18903 -0.06654 0.02514  0.09758  70  ILE A CD1 
505  N N   . LYS A 77  ? 0.26691 0.39059 0.15812 0.00779  -0.06002 0.06319  71  LYS A N   
506  C CA  . LYS A 77  ? 0.29390 0.39731 0.19297 0.00947  -0.03122 0.05781  71  LYS A CA  
507  C C   . LYS A 77  ? 0.31422 0.38241 0.21173 0.00564  -0.03712 0.04249  71  LYS A C   
508  O O   . LYS A 77  ? 0.37212 0.38277 0.23962 0.01439  -0.02209 0.02895  71  LYS A O   
509  C CB  . LYS A 77  ? 0.28165 0.41402 0.20074 0.00106  -0.03025 0.07027  71  LYS A CB  
510  C CG  . LYS A 77  ? 0.31683 0.42876 0.25586 -0.00261 -0.00664 0.06245  71  LYS A CG  
511  C CD  . LYS A 77  ? 0.35176 0.43678 0.28728 -0.00093 0.01080  0.06794  71  LYS A CD  
512  C CE  . LYS A 77  ? 0.39298 0.44128 0.29500 0.00693  0.02974  0.07733  71  LYS A CE  
513  N NZ  . LYS A 77  ? 0.41767 0.44605 0.30339 0.01002  0.03615  0.07050  71  LYS A NZ  
514  N N   . ILE A 78  ? 0.27780 0.35913 0.18321 -0.00659 -0.06498 0.03534  72  ILE A N   
515  C CA  . ILE A 78  ? 0.28531 0.34757 0.17444 -0.04623 -0.07215 0.03160  72  ILE A CA  
516  C C   . ILE A 78  ? 0.29993 0.35066 0.20141 -0.06310 -0.04534 0.06561  72  ILE A C   
517  O O   . ILE A 78  ? 0.30028 0.34135 0.20805 -0.08381 -0.07637 0.05450  72  ILE A O   
518  C CB  . ILE A 78  ? 0.30871 0.34349 0.16281 -0.06221 -0.05271 0.01511  72  ILE A CB  
519  C CG1 . ILE A 78  ? 0.32714 0.34782 0.17320 -0.06122 -0.04131 -0.01661 72  ILE A CG1 
520  C CG2 . ILE A 78  ? 0.32395 0.33308 0.17908 -0.07406 -0.03606 0.03088  72  ILE A CG2 
521  C CD1 . ILE A 78  ? 0.33915 0.34679 0.18410 -0.06196 -0.03888 -0.01854 72  ILE A CD1 
522  N N   . LEU A 79  ? 0.25091 0.35001 0.19451 -0.05158 -0.06938 0.11280  73  LEU A N   
523  C CA  . LEU A 79  ? 0.25804 0.36197 0.23983 -0.07138 -0.06165 0.09689  73  LEU A CA  
524  C C   . LEU A 79  ? 0.31120 0.37227 0.27681 -0.08420 -0.05002 0.09906  73  LEU A C   
525  O O   . LEU A 79  ? 0.32907 0.39381 0.31955 -0.07852 -0.03434 0.10176  73  LEU A O   
526  C CB  . LEU A 79  ? 0.25633 0.37010 0.25492 -0.06398 -0.06019 0.09288  73  LEU A CB  
527  C CG  . LEU A 79  ? 0.28992 0.37796 0.26364 -0.05605 -0.04362 0.08883  73  LEU A CG  
528  C CD1 . LEU A 79  ? 0.31121 0.38714 0.29105 -0.02729 -0.02676 0.05091  73  LEU A CD1 
529  C CD2 . LEU A 79  ? 0.29832 0.39153 0.28973 -0.06136 -0.03279 0.09828  73  LEU A CD2 
530  N N   . LEU A 80  ? 0.36067 0.36134 0.25253 -0.08699 -0.08557 0.08445  74  LEU A N   
531  C CA  . LEU A 80  ? 0.40458 0.35717 0.27223 -0.08881 -0.07203 0.07601  74  LEU A CA  
532  C C   . LEU A 80  ? 0.40518 0.34323 0.26917 -0.08926 -0.05439 0.04390  74  LEU A C   
533  O O   . LEU A 80  ? 0.41280 0.35151 0.30354 -0.10262 -0.06032 0.03109  74  LEU A O   
534  C CB  . LEU A 80  ? 0.43622 0.37533 0.27182 -0.08584 -0.05740 0.07272  74  LEU A CB  
535  C CG  . LEU A 80  ? 0.43952 0.39277 0.27125 -0.08059 -0.04623 0.08164  74  LEU A CG  
536  C CD1 . LEU A 80  ? 0.46862 0.41242 0.26571 -0.06897 -0.02386 0.06778  74  LEU A CD1 
537  C CD2 . LEU A 80  ? 0.44394 0.39183 0.28468 -0.07639 -0.04762 0.07954  74  LEU A CD2 
538  N N   . ARG A 81  ? 0.39061 0.32821 0.22866 -0.07224 -0.01087 0.03231  75  ARG A N   
539  C CA  . ARG A 81  ? 0.39635 0.33052 0.20121 -0.05145 -0.00851 0.01774  75  ARG A CA  
540  C C   . ARG A 81  ? 0.39755 0.31148 0.21937 -0.06498 0.03293  0.00597  75  ARG A C   
541  O O   . ARG A 81  ? 0.48584 0.31585 0.23121 -0.04108 0.08850  -0.00824 75  ARG A O   
542  C CB  . ARG A 81  ? 0.40481 0.34417 0.21096 -0.04848 -0.00574 -0.00303 75  ARG A CB  
543  C CG  . ARG A 81  ? 0.41000 0.35253 0.22671 -0.04712 -0.01332 -0.02149 75  ARG A CG  
544  C CD  . ARG A 81  ? 0.39775 0.35617 0.21758 -0.05520 -0.00994 -0.03960 75  ARG A CD  
545  N NE  . ARG A 81  ? 0.39322 0.35449 0.19129 -0.05514 -0.00487 -0.04970 75  ARG A NE  
546  C CZ  . ARG A 81  ? 0.39301 0.35039 0.20141 -0.04362 -0.00643 -0.05480 75  ARG A CZ  
547  N NH1 . ARG A 81  ? 0.38524 0.34729 0.18768 -0.04098 -0.06090 -0.06603 75  ARG A NH1 
548  N NH2 . ARG A 81  ? 0.38259 0.35133 0.22887 -0.04188 0.02484  -0.04677 75  ARG A NH2 
549  N N   . PHE A 82  ? 0.32247 0.28271 0.19673 -0.05992 -0.01535 0.00311  76  PHE A N   
550  C CA  . PHE A 82  ? 0.25322 0.27979 0.19984 -0.06325 -0.03991 0.00870  76  PHE A CA  
551  C C   . PHE A 82  ? 0.25849 0.28842 0.20250 -0.03707 -0.01554 0.02076  76  PHE A C   
552  O O   . PHE A 82  ? 0.27051 0.30523 0.19806 -0.03868 -0.01180 0.01198  76  PHE A O   
553  C CB  . PHE A 82  ? 0.23418 0.27047 0.19927 -0.06599 -0.04092 0.00473  76  PHE A CB  
554  C CG  . PHE A 82  ? 0.25099 0.26803 0.21112 -0.05742 -0.02473 0.02013  76  PHE A CG  
555  C CD1 . PHE A 82  ? 0.24854 0.26341 0.22876 -0.05730 -0.00663 0.01619  76  PHE A CD1 
556  C CD2 . PHE A 82  ? 0.24057 0.25964 0.18847 -0.06805 -0.03076 0.01234  76  PHE A CD2 
557  C CE1 . PHE A 82  ? 0.27280 0.26249 0.22184 -0.06070 0.00202  0.00163  76  PHE A CE1 
558  C CE2 . PHE A 82  ? 0.26920 0.27181 0.20600 -0.05239 0.00098  0.02212  76  PHE A CE2 
559  C CZ  . PHE A 82  ? 0.26569 0.27006 0.21564 -0.06367 -0.00452 -0.00343 76  PHE A CZ  
560  N N   . ARG A 83  ? 0.27941 0.27761 0.19898 -0.03529 -0.01461 0.02566  77  ARG A N   
561  C CA  . ARG A 83  ? 0.30923 0.28611 0.20170 -0.03844 -0.01023 0.02138  77  ARG A CA  
562  C C   . ARG A 83  ? 0.29640 0.25904 0.17691 -0.01953 -0.02310 0.02367  77  ARG A C   
563  O O   . ARG A 83  ? 0.33032 0.24630 0.19466 -0.00659 -0.00937 0.02118  77  ARG A O   
564  C CB  A ARG A 83  ? 0.34460 0.31021 0.20951 -0.03822 0.00039  0.01794  77  ARG A CB  
565  C CB  B ARG A 83  ? 0.36701 0.30431 0.22934 -0.04309 0.00031  0.01657  77  ARG A CB  
566  C CG  A ARG A 83  ? 0.36941 0.33485 0.22558 -0.03358 0.00162  0.01576  77  ARG A CG  
567  C CG  B ARG A 83  ? 0.41830 0.32403 0.26526 -0.04292 0.00410  0.01393  77  ARG A CG  
568  C CD  A ARG A 83  ? 0.41373 0.36321 0.27778 -0.02763 0.03654  0.01910  77  ARG A CD  
569  C CD  B ARG A 83  ? 0.46622 0.34253 0.28861 -0.03152 -0.01201 0.02656  77  ARG A CD  
570  N NE  A ARG A 83  ? 0.45269 0.39334 0.32985 -0.01546 0.05793  0.02129  77  ARG A NE  
571  N NE  B ARG A 83  ? 0.49454 0.36003 0.29269 -0.01599 -0.03454 0.03716  77  ARG A NE  
572  C CZ  A ARG A 83  ? 0.47068 0.41156 0.35239 -0.00098 0.04551  0.03206  77  ARG A CZ  
573  C CZ  B ARG A 83  ? 0.50336 0.36170 0.29384 0.00894  -0.06176 0.05416  77  ARG A CZ  
574  N NH1 A ARG A 83  ? 0.49030 0.42365 0.36919 0.01406  0.04595  0.04714  77  ARG A NH1 
575  N NH1 B ARG A 83  ? 0.49476 0.35131 0.28711 0.00884  -0.08801 0.06632  77  ARG A NH1 
576  N NH2 A ARG A 83  ? 0.47073 0.41514 0.35292 -0.00271 0.01934  0.02316  77  ARG A NH2 
577  N NH2 B ARG A 83  ? 0.51480 0.37684 0.31439 0.03002  -0.06426 0.04856  77  ARG A NH2 
578  N N   . HIS A 84  ? 0.25964 0.24595 0.18279 -0.02105 -0.03856 0.02664  78  HIS A N   
579  C CA  . HIS A 84  ? 0.22333 0.24722 0.17671 -0.02692 -0.03439 0.01087  78  HIS A CA  
580  C C   . HIS A 84  ? 0.20750 0.23174 0.19505 -0.03180 -0.03063 0.02031  78  HIS A C   
581  O O   . HIS A 84  ? 0.21614 0.21585 0.20526 -0.02283 -0.03594 0.04331  78  HIS A O   
582  C CB  . HIS A 84  ? 0.19414 0.24082 0.17555 -0.05084 -0.03272 0.01720  78  HIS A CB  
583  C CG  . HIS A 84  ? 0.19734 0.22277 0.15753 -0.02831 -0.00912 0.01903  78  HIS A CG  
584  N ND1 . HIS A 84  ? 0.17767 0.23127 0.16610 -0.03182 -0.00083 0.03346  78  HIS A ND1 
585  C CD2 . HIS A 84  ? 0.19040 0.22192 0.16216 -0.02435 -0.01460 0.01566  78  HIS A CD2 
586  C CE1 . HIS A 84  ? 0.18628 0.22296 0.17102 -0.03040 0.00276  0.01690  78  HIS A CE1 
587  N NE2 . HIS A 84  ? 0.19676 0.21140 0.17182 -0.02799 -0.00116 0.01472  78  HIS A NE2 
588  N N   . GLU A 85  ? 0.19659 0.23314 0.23153 -0.03303 -0.00660 0.02169  79  GLU A N   
589  C CA  . GLU A 85  ? 0.16282 0.23664 0.23012 -0.05303 -0.04281 0.02463  79  GLU A CA  
590  C C   . GLU A 85  ? 0.17104 0.22953 0.22629 -0.01982 -0.03603 0.02435  79  GLU A C   
591  O O   . GLU A 85  ? 0.16019 0.22927 0.24785 -0.02307 -0.03077 0.01189  79  GLU A O   
592  C CB  . GLU A 85  ? 0.20055 0.25955 0.24551 -0.08074 -0.01367 0.04210  79  GLU A CB  
593  C CG  . GLU A 85  ? 0.22704 0.30628 0.25617 -0.09296 -0.03934 0.04060  79  GLU A CG  
594  C CD  . GLU A 85  ? 0.22618 0.33691 0.31231 -0.11284 -0.05082 0.03188  79  GLU A CD  
595  O OE1 . GLU A 85  ? 0.23889 0.35043 0.32295 -0.11391 -0.05983 0.03622  79  GLU A OE1 
596  O OE2 . GLU A 85  ? 0.24363 0.35143 0.35865 -0.10119 -0.03442 0.03067  79  GLU A OE2 
597  N N   . ASN A 86  ? 0.15487 0.21583 0.18725 -0.02320 -0.01787 0.02039  80  ASN A N   
598  C CA  . ASN A 86  ? 0.15616 0.20515 0.14959 -0.03637 -0.04352 0.01543  80  ASN A CA  
599  C C   . ASN A 86  ? 0.17219 0.19521 0.17650 -0.01026 -0.01730 0.01626  80  ASN A C   
600  O O   . ASN A 86  ? 0.17323 0.20915 0.18269 -0.00725 -0.00386 0.01320  80  ASN A O   
601  C CB  . ASN A 86  ? 0.19177 0.22724 0.16095 -0.03449 0.00773  0.02899  80  ASN A CB  
602  C CG  . ASN A 86  ? 0.16069 0.23391 0.17757 -0.01868 0.00918  0.02462  80  ASN A CG  
603  O OD1 . ASN A 86  ? 0.15899 0.23298 0.19516 0.00541  0.01992  0.03970  80  ASN A OD1 
604  N ND2 . ASN A 86  ? 0.14188 0.24316 0.20335 -0.02733 0.02483  0.01100  80  ASN A ND2 
605  N N   . ILE A 87  ? 0.16665 0.18169 0.18782 0.00813  -0.01890 0.04982  81  ILE A N   
606  C CA  . ILE A 87  ? 0.18271 0.18480 0.20143 0.00282  0.00532  0.06258  81  ILE A CA  
607  C C   . ILE A 87  ? 0.20141 0.21481 0.18811 -0.01462 -0.01198 0.05571  81  ILE A C   
608  O O   . ILE A 87  ? 0.17834 0.21685 0.21039 -0.03764 -0.03413 0.06455  81  ILE A O   
609  C CB  . ILE A 87  ? 0.18917 0.16448 0.18238 0.03047  -0.01004 0.08576  81  ILE A CB  
610  C CG1 . ILE A 87  ? 0.19788 0.16034 0.20299 0.06343  -0.02708 0.06175  81  ILE A CG1 
611  C CG2 . ILE A 87  ? 0.23154 0.17284 0.20505 -0.00804 0.03287  0.06908  81  ILE A CG2 
612  C CD1 . ILE A 87  ? 0.18418 0.17832 0.25209 0.03383  0.00398  0.05279  81  ILE A CD1 
613  N N   . ILE A 88  ? 0.21094 0.24619 0.17791 -0.00510 -0.04395 0.06332  82  ILE A N   
614  C CA  . ILE A 88  ? 0.24038 0.30734 0.19994 0.00549  -0.08232 0.05869  82  ILE A CA  
615  C C   . ILE A 88  ? 0.24793 0.34897 0.19009 -0.01167 -0.08182 0.04792  82  ILE A C   
616  O O   . ILE A 88  ? 0.29935 0.42372 0.22561 -0.00932 -0.04516 0.02021  82  ILE A O   
617  C CB  . ILE A 88  ? 0.32081 0.35262 0.26576 0.02659  -0.10164 0.07988  82  ILE A CB  
618  C CG1 . ILE A 88  ? 0.36605 0.36438 0.27246 0.05468  -0.12884 0.08562  82  ILE A CG1 
619  C CG2 . ILE A 88  ? 0.37050 0.36717 0.30500 0.00766  -0.10623 0.06208  82  ILE A CG2 
620  C CD1 . ILE A 88  ? 0.39381 0.38223 0.29146 0.02826  -0.10705 0.06633  82  ILE A CD1 
621  N N   . GLY A 89  ? 0.27253 0.31813 0.14011 -0.01174 -0.06276 0.04971  83  GLY A N   
622  C CA  . GLY A 89  ? 0.32584 0.30855 0.14034 -0.00282 -0.01549 0.06719  83  GLY A CA  
623  C C   . GLY A 89  ? 0.36527 0.29988 0.17581 -0.01034 -0.00351 0.07187  83  GLY A C   
624  O O   . GLY A 89  ? 0.40920 0.29979 0.18796 0.00741  -0.00864 0.07680  83  GLY A O   
625  N N   . ILE A 90  ? 0.34542 0.30469 0.14675 -0.04207 -0.00015 0.06097  84  ILE A N   
626  C CA  . ILE A 90  ? 0.30225 0.32932 0.16369 -0.05108 -0.06145 0.04686  84  ILE A CA  
627  C C   . ILE A 90  ? 0.31878 0.36197 0.19113 -0.08113 -0.04946 0.04066  84  ILE A C   
628  O O   . ILE A 90  ? 0.35143 0.37889 0.22352 -0.08673 -0.03446 0.03629  84  ILE A O   
629  C CB  . ILE A 90  ? 0.28183 0.33427 0.18225 -0.04529 -0.07812 0.04002  84  ILE A CB  
630  C CG1 . ILE A 90  ? 0.23792 0.33980 0.22428 -0.03426 -0.07566 0.05142  84  ILE A CG1 
631  C CG2 . ILE A 90  ? 0.28026 0.33873 0.17943 -0.06090 -0.10504 0.02852  84  ILE A CG2 
632  C CD1 . ILE A 90  ? 0.22891 0.34193 0.24375 -0.01282 -0.06223 0.07092  84  ILE A CD1 
633  N N   . ASN A 91  ? 0.28571 0.38522 0.18073 -0.08753 -0.08885 0.04389  85  ASN A N   
634  C CA  . ASN A 91  ? 0.32303 0.42029 0.21316 -0.11283 -0.05855 0.02521  85  ASN A CA  
635  C C   . ASN A 91  ? 0.32144 0.40911 0.19471 -0.13886 -0.07558 0.05120  85  ASN A C   
636  O O   . ASN A 91  ? 0.37192 0.40718 0.21275 -0.16305 -0.04067 0.05994  85  ASN A O   
637  C CB  . ASN A 91  ? 0.34416 0.46248 0.23641 -0.12071 -0.03235 0.00103  85  ASN A CB  
638  C CG  . ASN A 91  ? 0.37715 0.48623 0.25569 -0.13356 -0.00202 0.00005  85  ASN A CG  
639  O OD1 . ASN A 91  ? 0.39920 0.50680 0.24747 -0.13284 0.00948  0.01035  85  ASN A OD1 
640  N ND2 . ASN A 91  ? 0.38619 0.48703 0.26659 -0.16020 0.02263  -0.02204 85  ASN A ND2 
641  N N   . ASP A 92  ? 0.30374 0.40725 0.19436 -0.10655 -0.05614 0.06937  86  ASP A N   
642  C CA  . ASP A 92  ? 0.27506 0.40437 0.20316 -0.07953 -0.03663 0.05764  86  ASP A CA  
643  C C   . ASP A 92  ? 0.24340 0.37225 0.22563 -0.06650 -0.02684 0.07023  86  ASP A C   
644  O O   . ASP A 92  ? 0.21140 0.35904 0.21177 -0.05772 -0.04205 0.06476  86  ASP A O   
645  C CB  . ASP A 92  ? 0.28581 0.43957 0.16961 -0.05723 -0.06730 0.05669  86  ASP A CB  
646  C CG  . ASP A 92  ? 0.30009 0.47382 0.20888 -0.04526 -0.05249 0.04725  86  ASP A CG  
647  O OD1 . ASP A 92  ? 0.28116 0.47801 0.19799 -0.06803 -0.04701 0.02507  86  ASP A OD1 
648  O OD2 . ASP A 92  ? 0.29038 0.49010 0.23101 -0.02333 -0.06546 0.06886  86  ASP A OD2 
649  N N   . ILE A 93  ? 0.21544 0.35025 0.22818 -0.06171 -0.01313 0.08805  87  ILE A N   
650  C CA  . ILE A 93  ? 0.20431 0.34516 0.19307 -0.05701 -0.05669 0.06969  87  ILE A CA  
651  C C   . ILE A 93  ? 0.24780 0.34559 0.19178 -0.04283 -0.03797 0.07167  87  ILE A C   
652  O O   . ILE A 93  ? 0.26462 0.36116 0.19456 -0.04657 -0.03666 0.06985  87  ILE A O   
653  C CB  . ILE A 93  ? 0.23855 0.34672 0.21057 -0.04234 -0.01123 0.05919  87  ILE A CB  
654  C CG1 . ILE A 93  ? 0.24533 0.34175 0.21184 -0.01137 -0.02138 0.07275  87  ILE A CG1 
655  C CG2 . ILE A 93  ? 0.24068 0.33830 0.22737 -0.05136 -0.01009 0.04195  87  ILE A CG2 
656  C CD1 . ILE A 93  ? 0.29206 0.36271 0.24014 -0.00074 0.01178  0.08117  87  ILE A CD1 
657  N N   . ILE A 94  ? 0.27267 0.32673 0.18338 -0.01995 -0.01053 0.08906  88  ILE A N   
658  C CA  . ILE A 94  ? 0.29143 0.32617 0.19410 -0.01690 -0.02208 0.06063  88  ILE A CA  
659  C C   . ILE A 94  ? 0.30360 0.31700 0.17268 -0.00345 -0.01019 0.05597  88  ILE A C   
660  O O   . ILE A 94  ? 0.32059 0.32548 0.17704 -0.00127 0.02702  0.03404  88  ILE A O   
661  C CB  . ILE A 94  ? 0.30381 0.32435 0.22488 0.00960  -0.00380 0.04981  88  ILE A CB  
662  C CG1 . ILE A 94  ? 0.31384 0.34476 0.24806 0.01771  -0.00155 0.03814  88  ILE A CG1 
663  C CG2 . ILE A 94  ? 0.32306 0.32373 0.23329 0.01080  -0.00280 0.03399  88  ILE A CG2 
664  C CD1 . ILE A 94  ? 0.29767 0.35140 0.26897 0.03314  0.00393  0.05212  88  ILE A CD1 
665  N N   . ARG A 95  ? 0.28893 0.29372 0.14438 0.00256  -0.03702 0.06018  89  ARG A N   
666  C CA  . ARG A 95  ? 0.29814 0.29596 0.15337 0.00085  -0.04321 0.05749  89  ARG A CA  
667  C C   . ARG A 95  ? 0.29935 0.29937 0.15130 -0.03331 -0.03063 0.05901  89  ARG A C   
668  O O   . ARG A 95  ? 0.28045 0.30690 0.18273 -0.04117 -0.01446 0.05222  89  ARG A O   
669  C CB  . ARG A 95  ? 0.32095 0.29181 0.18149 0.00696  -0.00975 0.05149  89  ARG A CB  
670  C CG  . ARG A 95  ? 0.35563 0.29123 0.19989 0.00343  0.08113  0.02745  89  ARG A CG  
671  C CD  . ARG A 95  ? 0.38398 0.29072 0.17455 0.02092  0.07165  0.02709  89  ARG A CD  
672  N NE  . ARG A 95  ? 0.35675 0.30764 0.15961 0.01726  0.04540  0.03221  89  ARG A NE  
673  C CZ  . ARG A 95  ? 0.33210 0.32222 0.19411 0.00726  0.02042  0.02337  89  ARG A CZ  
674  N NH1 . ARG A 95  ? 0.30345 0.33774 0.18736 0.01070  0.00269  0.03747  89  ARG A NH1 
675  N NH2 . ARG A 95  ? 0.30163 0.31972 0.20487 0.01183  -0.01242 0.01389  89  ARG A NH2 
676  N N   . ALA A 96  ? 0.31938 0.31103 0.13431 -0.06147 -0.01518 0.06089  90  ALA A N   
677  C CA  . ALA A 96  ? 0.33373 0.29754 0.13344 -0.05824 -0.01083 0.04729  90  ALA A CA  
678  C C   . ALA A 96  ? 0.30894 0.28655 0.16195 -0.02687 -0.02913 0.04422  90  ALA A C   
679  O O   . ALA A 96  ? 0.30209 0.29645 0.17577 -0.02516 -0.04769 0.04575  90  ALA A O   
680  C CB  . ALA A 96  ? 0.34500 0.31727 0.15712 -0.07005 -0.00318 0.04588  90  ALA A CB  
681  N N   . PRO A 97  ? 0.27944 0.26769 0.16579 0.00117  -0.05902 0.02351  91  PRO A N   
682  C CA  . PRO A 97  ? 0.27055 0.27259 0.19382 0.00519  -0.04831 -0.00410 91  PRO A CA  
683  C C   . PRO A 97  ? 0.26688 0.28637 0.20759 0.01506  -0.03873 0.00200  91  PRO A C   
684  O O   . PRO A 97  ? 0.31243 0.28143 0.24035 0.00886  0.00673  -0.02082 91  PRO A O   
685  C CB  . PRO A 97  ? 0.29253 0.28011 0.20369 0.01512  -0.04170 0.00307  91  PRO A CB  
686  C CG  . PRO A 97  ? 0.30173 0.27702 0.18825 0.00491  -0.02975 0.00477  91  PRO A CG  
687  C CD  . PRO A 97  ? 0.29838 0.28074 0.15305 0.00548  -0.04657 0.02350  91  PRO A CD  
688  N N   . THR A 98  ? 0.24814 0.32282 0.18299 0.00770  -0.04969 0.02735  92  THR A N   
689  C CA  . THR A 98  ? 0.26702 0.34971 0.21303 0.00061  0.00942  0.03764  92  THR A CA  
690  C C   . THR A 98  ? 0.23465 0.38928 0.22272 -0.02562 0.02242  0.05362  92  THR A C   
691  O O   . THR A 98  ? 0.22511 0.38015 0.25244 -0.00574 0.03896  0.06316  92  THR A O   
692  C CB  . THR A 98  ? 0.32291 0.33515 0.21746 0.00186  0.02009  0.03326  92  THR A CB  
693  O OG1 . THR A 98  ? 0.33748 0.32525 0.22140 -0.02217 0.02503  0.04001  92  THR A OG1 
694  C CG2 . THR A 98  ? 0.35125 0.33769 0.23315 0.01414  0.03298  0.02656  92  THR A CG2 
695  N N   . ILE A 99  ? 0.23935 0.43842 0.22737 -0.04010 0.01982  0.06288  93  ILE A N   
696  C CA  . ILE A 99  ? 0.27018 0.48795 0.29885 -0.05190 0.02635  0.06324  93  ILE A CA  
697  C C   . ILE A 99  ? 0.27948 0.48932 0.28590 -0.08224 0.00670  0.07528  93  ILE A C   
698  O O   . ILE A 99  ? 0.30429 0.49356 0.28171 -0.10063 -0.00683 0.07557  93  ILE A O   
699  C CB  . ILE A 99  ? 0.28218 0.52643 0.35546 -0.04453 0.02651  0.05173  93  ILE A CB  
700  C CG1 . ILE A 99  ? 0.30669 0.55518 0.39056 -0.01831 0.05954  0.06298  93  ILE A CG1 
701  C CG2 . ILE A 99  ? 0.29644 0.53227 0.35669 -0.07276 0.02252  0.02992  93  ILE A CG2 
702  C CD1 . ILE A 99  ? 0.29993 0.57114 0.42118 0.00636  0.07056  0.07092  93  ILE A CD1 
703  N N   . GLU A 100 ? 0.27109 0.48701 0.27360 -0.07882 -0.01336 0.09439  94  GLU A N   
704  C CA  . GLU A 100 ? 0.30352 0.48050 0.26536 -0.09647 -0.02596 0.07902  94  GLU A CA  
705  C C   . GLU A 100 ? 0.36448 0.44525 0.25721 -0.13168 -0.01788 0.06394  94  GLU A C   
706  O O   . GLU A 100 ? 0.40613 0.44423 0.29242 -0.16486 -0.01836 0.06566  94  GLU A O   
707  C CB  . GLU A 100 ? 0.29955 0.50388 0.28053 -0.08494 -0.00837 0.07507  94  GLU A CB  
708  C CG  . GLU A 100 ? 0.35256 0.53325 0.33774 -0.06861 0.01541  0.06800  94  GLU A CG  
709  C CD  . GLU A 100 ? 0.37584 0.55592 0.36483 -0.05815 0.02565  0.06300  94  GLU A CD  
710  O OE1 . GLU A 100 ? 0.38988 0.57833 0.40523 -0.04430 0.02312  0.05718  94  GLU A OE1 
711  O OE2 . GLU A 100 ? 0.39135 0.55883 0.33545 -0.05231 0.02672  0.07814  94  GLU A OE2 
712  N N   . GLN A 101 ? 0.35785 0.40510 0.22071 -0.12609 -0.03235 0.06923  95  GLN A N   
713  C CA  . GLN A 101 ? 0.36189 0.37479 0.18661 -0.09787 -0.03912 0.06245  95  GLN A CA  
714  C C   . GLN A 101 ? 0.39230 0.37976 0.19142 -0.08635 -0.02688 0.05397  95  GLN A C   
715  O O   . GLN A 101 ? 0.44730 0.35034 0.20916 -0.04717 0.00194  0.04073  95  GLN A O   
716  C CB  . GLN A 101 ? 0.37037 0.35548 0.18403 -0.06236 -0.05299 0.05175  95  GLN A CB  
717  C CG  . GLN A 101 ? 0.38305 0.33807 0.17487 -0.04279 -0.08592 0.04476  95  GLN A CG  
718  C CD  . GLN A 101 ? 0.39953 0.32340 0.20772 -0.00221 -0.08680 0.06329  95  GLN A CD  
719  O OE1 . GLN A 101 ? 0.43496 0.33022 0.25039 0.03389  -0.08194 0.07114  95  GLN A OE1 
720  N NE2 . GLN A 101 ? 0.37816 0.29873 0.20160 0.01677  -0.09169 0.06600  95  GLN A NE2 
721  N N   . MET A 102 ? 0.38602 0.40050 0.18369 -0.10373 -0.02008 0.07830  96  MET A N   
722  C CA  . MET A 102 ? 0.39247 0.42620 0.16638 -0.12604 -0.03616 0.07489  96  MET A CA  
723  C C   . MET A 102 ? 0.46801 0.45111 0.19422 -0.14975 -0.02508 0.06828  96  MET A C   
724  O O   . MET A 102 ? 0.45736 0.45627 0.22327 -0.19030 -0.04555 0.05650  96  MET A O   
725  C CB  . MET A 102 ? 0.33679 0.43457 0.16263 -0.10911 -0.02641 0.09317  96  MET A CB  
726  C CG  . MET A 102 ? 0.30251 0.44703 0.17447 -0.10062 -0.00965 0.10237  96  MET A CG  
727  S SD  . MET A 102 ? 0.25866 0.46535 0.22771 -0.09866 -0.03173 0.09004  96  MET A SD  
728  C CE  . MET A 102 ? 0.21585 0.48285 0.24087 -0.07555 -0.03894 0.06015  96  MET A CE  
729  N N   . LYS A 103 ? 0.53391 0.46261 0.19560 -0.15445 -0.00803 0.04563  97  LYS A N   
730  C CA  . LYS A 103 ? 0.57066 0.47108 0.21341 -0.15854 0.01528  0.03120  97  LYS A CA  
731  C C   . LYS A 103 ? 0.55968 0.47436 0.21852 -0.15689 -0.00746 0.01186  97  LYS A C   
732  O O   . LYS A 103 ? 0.58444 0.50754 0.25779 -0.15976 -0.00801 -0.00356 97  LYS A O   
733  C CB  . LYS A 103 ? 0.58085 0.47252 0.21195 -0.16157 0.02665  0.04268  97  LYS A CB  
734  N N   . ASP A 104 ? 0.51772 0.43710 0.21398 -0.15058 -0.00750 0.02959  98  ASP A N   
735  C CA  . ASP A 104 ? 0.50429 0.41274 0.24601 -0.11848 -0.00058 0.05073  98  ASP A CA  
736  C C   . ASP A 104 ? 0.44666 0.37123 0.21620 -0.10199 -0.01803 0.04319  98  ASP A C   
737  O O   . ASP A 104 ? 0.46075 0.35730 0.19275 -0.10388 0.00155  0.03605  98  ASP A O   
738  C CB  . ASP A 104 ? 0.54766 0.42301 0.31005 -0.10822 0.01202  0.08134  98  ASP A CB  
739  C CG  . ASP A 104 ? 0.58578 0.43992 0.36200 -0.09659 -0.00497 0.10897  98  ASP A CG  
740  O OD1 . ASP A 104 ? 0.59535 0.44794 0.39323 -0.09779 -0.01463 0.10394  98  ASP A OD1 
741  O OD2 . ASP A 104 ? 0.60861 0.44336 0.38740 -0.08148 -0.00480 0.14247  98  ASP A OD2 
742  N N   . VAL A 105 ? 0.40346 0.36153 0.22272 -0.07761 -0.01452 0.03827  99  VAL A N   
743  C CA  . VAL A 105 ? 0.35681 0.34044 0.21723 -0.06037 -0.03432 0.03022  99  VAL A CA  
744  C C   . VAL A 105 ? 0.34657 0.32989 0.22752 -0.06557 -0.03716 0.02741  99  VAL A C   
745  O O   . VAL A 105 ? 0.37558 0.33503 0.26490 -0.06480 -0.02239 0.00642  99  VAL A O   
746  C CB  . VAL A 105 ? 0.37083 0.35867 0.27369 -0.03429 0.02883  0.03824  99  VAL A CB  
747  C CG1 . VAL A 105 ? 0.37913 0.36555 0.29263 -0.00868 0.02618  0.05351  99  VAL A CG1 
748  C CG2 . VAL A 105 ? 0.38136 0.37403 0.29017 -0.02173 0.05474  0.03061  99  VAL A CG2 
749  N N   . TYR A 106 ? 0.31652 0.30464 0.20696 -0.07992 -0.02329 0.03735  100 TYR A N   
750  C CA  . TYR A 106 ? 0.29885 0.29568 0.20522 -0.05274 -0.02388 0.05515  100 TYR A CA  
751  C C   . TYR A 106 ? 0.29076 0.30783 0.20175 -0.05194 -0.02215 0.07206  100 TYR A C   
752  O O   . TYR A 106 ? 0.28384 0.32180 0.21206 -0.05794 -0.03803 0.07045  100 TYR A O   
753  C CB  . TYR A 106 ? 0.28397 0.28650 0.21082 -0.02539 -0.03196 0.04830  100 TYR A CB  
754  C CG  . TYR A 106 ? 0.29172 0.26853 0.18624 -0.00047 -0.02785 0.07871  100 TYR A CG  
755  C CD1 . TYR A 106 ? 0.29584 0.26825 0.19908 0.01699  -0.02188 0.07926  100 TYR A CD1 
756  C CD2 . TYR A 106 ? 0.31441 0.27053 0.19966 -0.00262 -0.01311 0.08110  100 TYR A CD2 
757  C CE1 . TYR A 106 ? 0.32902 0.27825 0.21247 0.02598  -0.00613 0.06934  100 TYR A CE1 
758  C CE2 . TYR A 106 ? 0.32195 0.27275 0.19878 0.01637  -0.01334 0.08629  100 TYR A CE2 
759  C CZ  . TYR A 106 ? 0.35507 0.28133 0.22633 0.01316  0.00716  0.07240  100 TYR A CZ  
760  O OH  . TYR A 106 ? 0.38575 0.28399 0.26857 0.00691  0.02985  0.06428  100 TYR A OH  
761  N N   . ILE A 107 ? 0.26726 0.31063 0.19945 -0.06360 -0.02330 0.07070  101 ILE A N   
762  C CA  . ILE A 107 ? 0.23930 0.31349 0.21170 -0.05891 -0.04092 0.08025  101 ILE A CA  
763  C C   . ILE A 107 ? 0.21437 0.32565 0.20893 -0.05004 -0.03376 0.05855  101 ILE A C   
764  O O   . ILE A 107 ? 0.23375 0.33882 0.23024 -0.04186 -0.02258 0.05919  101 ILE A O   
765  C CB  . ILE A 107 ? 0.23701 0.32356 0.26460 -0.06872 -0.03918 0.08212  101 ILE A CB  
766  C CG1 . ILE A 107 ? 0.25133 0.35958 0.31354 -0.07041 -0.08049 0.08438  101 ILE A CG1 
767  C CG2 . ILE A 107 ? 0.22570 0.30034 0.24671 -0.04131 -0.04016 0.10346  101 ILE A CG2 
768  C CD1 . ILE A 107 ? 0.30531 0.38685 0.37922 -0.08414 -0.05346 0.06014  101 ILE A CD1 
769  N N   . VAL A 108 ? 0.21240 0.33111 0.17797 -0.02328 -0.03448 0.06244  102 VAL A N   
770  C CA  . VAL A 108 ? 0.21884 0.35218 0.18577 -0.02715 -0.03920 0.05022  102 VAL A CA  
771  C C   . VAL A 108 ? 0.21359 0.37297 0.17432 -0.02593 -0.03778 0.06159  102 VAL A C   
772  O O   . VAL A 108 ? 0.24289 0.36883 0.17093 -0.02592 -0.02135 0.07610  102 VAL A O   
773  C CB  . VAL A 108 ? 0.23662 0.36049 0.19073 -0.01633 -0.03940 0.05316  102 VAL A CB  
774  C CG1 . VAL A 108 ? 0.24246 0.36179 0.21860 -0.01090 -0.05443 0.03947  102 VAL A CG1 
775  C CG2 . VAL A 108 ? 0.25395 0.35676 0.17301 -0.01369 -0.04208 0.05956  102 VAL A CG2 
776  N N   . GLN A 109 ? 0.18557 0.39043 0.16417 -0.02824 -0.05364 0.07739  103 GLN A N   
777  C CA  . GLN A 109 ? 0.19432 0.40474 0.17812 -0.01425 -0.06722 0.07765  103 GLN A CA  
778  C C   . GLN A 109 ? 0.23518 0.45758 0.18479 -0.00341 -0.04820 0.09483  103 GLN A C   
779  O O   . GLN A 109 ? 0.22488 0.48772 0.18152 -0.02604 -0.06172 0.07065  103 GLN A O   
780  C CB  . GLN A 109 ? 0.17330 0.40818 0.20175 0.00653  -0.06465 0.07963  103 GLN A CB  
781  C CG  . GLN A 109 ? 0.20631 0.41782 0.22004 0.01162  -0.06557 0.05790  103 GLN A CG  
782  C CD  . GLN A 109 ? 0.23434 0.42241 0.22949 0.02486  -0.07410 0.05984  103 GLN A CD  
783  O OE1 . GLN A 109 ? 0.29374 0.43921 0.25845 0.03276  -0.01933 0.04632  103 GLN A OE1 
784  N NE2 . GLN A 109 ? 0.21826 0.38729 0.20261 0.00989  -0.08868 0.07432  103 GLN A NE2 
785  N N   . ASP A 110 ? 0.26835 0.47451 0.19821 0.00406  0.00505  0.08546  104 ASP A N   
786  C CA  . ASP A 110 ? 0.31629 0.48199 0.21619 0.00279  0.00474  0.06788  104 ASP A CA  
787  C C   . ASP A 110 ? 0.25892 0.49141 0.22146 0.02906  -0.01437 0.04993  104 ASP A C   
788  O O   . ASP A 110 ? 0.21631 0.48053 0.22212 0.02150  -0.03985 0.03432  104 ASP A O   
789  C CB  . ASP A 110 ? 0.39035 0.47461 0.22740 -0.03307 0.05547  0.05994  104 ASP A CB  
790  C CG  . ASP A 110 ? 0.44874 0.48116 0.22913 -0.05508 0.06264  0.06189  104 ASP A CG  
791  O OD1 . ASP A 110 ? 0.43659 0.48788 0.19865 -0.07903 0.06323  0.04020  104 ASP A OD1 
792  O OD2 . ASP A 110 ? 0.47250 0.47008 0.23404 -0.05458 0.06074  0.08110  104 ASP A OD2 
793  N N   . LEU A 111 ? 0.23629 0.50672 0.24063 0.04353  -0.00571 0.06364  105 LEU A N   
794  C CA  . LEU A 111 ? 0.22424 0.51721 0.25524 0.04937  -0.01188 0.07923  105 LEU A CA  
795  C C   . LEU A 111 ? 0.23081 0.51473 0.25319 0.02146  -0.00678 0.07916  105 LEU A C   
796  O O   . LEU A 111 ? 0.23354 0.52579 0.26292 -0.00405 0.01020  0.07423  105 LEU A O   
797  C CB  . LEU A 111 ? 0.23577 0.52872 0.26613 0.07535  -0.03098 0.10002  105 LEU A CB  
798  C CG  . LEU A 111 ? 0.23669 0.52764 0.30358 0.09833  -0.00228 0.11149  105 LEU A CG  
799  C CD1 . LEU A 111 ? 0.23999 0.52388 0.31548 0.11758  -0.00526 0.13786  105 LEU A CD1 
800  C CD2 . LEU A 111 ? 0.26682 0.53231 0.32632 0.10618  0.02561  0.11782  105 LEU A CD2 
801  N N   . MET A 112 ? 0.20635 0.48717 0.25888 0.05181  -0.02742 0.07495  106 MET A N   
802  C CA  . MET A 112 ? 0.17478 0.45316 0.25235 0.07343  -0.04907 0.06291  106 MET A CA  
803  C C   . MET A 112 ? 0.23032 0.45240 0.29285 0.07335  -0.00884 0.06054  106 MET A C   
804  O O   . MET A 112 ? 0.28478 0.47481 0.32846 0.10062  0.03085  0.07690  106 MET A O   
805  C CB  . MET A 112 ? 0.20328 0.42523 0.25664 0.04653  -0.02506 0.05608  106 MET A CB  
806  C CG  . MET A 112 ? 0.19286 0.40904 0.25647 0.02317  -0.00765 0.02833  106 MET A CG  
807  S SD  . MET A 112 ? 0.22037 0.39940 0.27906 -0.01883 -0.03770 -0.01696 106 MET A SD  
808  C CE  . MET A 112 ? 0.22797 0.39777 0.26359 -0.01028 -0.00698 -0.04598 106 MET A CE  
809  N N   . GLU A 113 ? 0.19524 0.43097 0.27264 0.04262  -0.04723 0.03199  107 GLU A N   
810  C CA  . GLU A 113 ? 0.20485 0.40704 0.30493 0.04392  -0.02254 0.03118  107 GLU A CA  
811  C C   . GLU A 113 ? 0.18457 0.38076 0.33889 0.04732  -0.01589 0.01673  107 GLU A C   
812  O O   . GLU A 113 ? 0.17728 0.38744 0.36952 0.05620  -0.03294 0.03694  107 GLU A O   
813  C CB  . GLU A 113 ? 0.19692 0.40749 0.29586 0.04164  -0.01904 0.05613  107 GLU A CB  
814  C CG  . GLU A 113 ? 0.21893 0.42894 0.32083 0.02148  -0.00448 0.05254  107 GLU A CG  
815  C CD  . GLU A 113 ? 0.23315 0.44993 0.34485 0.01547  -0.00546 0.04132  107 GLU A CD  
816  O OE1 . GLU A 113 ? 0.23370 0.45821 0.34854 0.00384  -0.01273 0.03739  107 GLU A OE1 
817  O OE2 . GLU A 113 ? 0.24840 0.46193 0.37556 0.01448  0.01181  0.03287  107 GLU A OE2 
818  N N   . THR A 114 ? 0.15928 0.35223 0.28866 0.06210  -0.04058 0.00155  108 THR A N   
819  C CA  . THR A 114 ? 0.13187 0.33791 0.29590 0.06339  -0.05990 -0.00131 108 THR A CA  
820  C C   . THR A 114 ? 0.15830 0.29862 0.28004 0.06353  -0.05439 0.02420  108 THR A C   
821  O O   . THR A 114 ? 0.15572 0.27010 0.25298 0.06829  -0.02104 0.01572  108 THR A O   
822  C CB  . THR A 114 ? 0.18890 0.36202 0.31689 0.05859  -0.04686 -0.01883 108 THR A CB  
823  O OG1 . THR A 114 ? 0.19650 0.37957 0.36816 0.07820  -0.03948 -0.02933 108 THR A OG1 
824  C CG2 . THR A 114 ? 0.20134 0.37332 0.27972 0.06415  -0.03143 0.01306  108 THR A CG2 
825  N N   . ASP A 115 ? 0.14629 0.29183 0.31887 0.04150  -0.07830 0.00968  109 ASP A N   
826  C CA  . ASP A 115 ? 0.16278 0.27297 0.32048 0.04077  -0.07434 0.00697  109 ASP A CA  
827  C C   . ASP A 115 ? 0.17438 0.25745 0.32184 0.04360  -0.04932 -0.00104 109 ASP A C   
828  O O   . ASP A 115 ? 0.20348 0.26353 0.33003 0.06665  -0.00048 0.01344  109 ASP A O   
829  C CB  . ASP A 115 ? 0.24525 0.26999 0.34239 0.03018  -0.02988 -0.01046 109 ASP A CB  
830  C CG  . ASP A 115 ? 0.27097 0.27070 0.35869 0.04055  -0.03984 0.01711  109 ASP A CG  
831  O OD1 . ASP A 115 ? 0.27268 0.27103 0.36059 0.05629  -0.05441 0.01079  109 ASP A OD1 
832  O OD2 . ASP A 115 ? 0.31852 0.28357 0.37907 0.00346  0.00324  0.02566  109 ASP A OD2 
833  N N   . LEU A 116 ? 0.17567 0.23257 0.29037 0.01211  -0.05455 -0.00249 110 LEU A N   
834  C CA  . LEU A 116 ? 0.18174 0.22436 0.27738 0.03114  -0.03717 0.00700  110 LEU A CA  
835  C C   . LEU A 116 ? 0.22406 0.19850 0.28736 0.03507  -0.00237 -0.00279 110 LEU A C   
836  O O   . LEU A 116 ? 0.26067 0.20099 0.31347 0.02725  0.02337  0.00457  110 LEU A O   
837  C CB  . LEU A 116 ? 0.20618 0.25193 0.27380 0.05551  -0.00141 0.04073  110 LEU A CB  
838  C CG  . LEU A 116 ? 0.16356 0.28127 0.28284 0.07483  0.01693  0.05639  110 LEU A CG  
839  C CD1 . LEU A 116 ? 0.16900 0.30227 0.29226 0.05013  0.06171  0.05662  110 LEU A CD1 
840  C CD2 . LEU A 116 ? 0.14900 0.27989 0.30337 0.09964  0.02713  0.04822  110 LEU A CD2 
841  N N   . TYR A 117 ? 0.22983 0.19714 0.29509 0.06081  0.00573  0.01209  111 TYR A N   
842  C CA  . TYR A 117 ? 0.23773 0.19574 0.31998 0.05166  0.00474  0.00474  111 TYR A CA  
843  C C   . TYR A 117 ? 0.20740 0.20480 0.32254 0.06495  -0.00669 -0.00975 111 TYR A C   
844  O O   . TYR A 117 ? 0.20781 0.21641 0.37694 0.06192  0.02312  0.00746  111 TYR A O   
845  C CB  . TYR A 117 ? 0.28234 0.20848 0.35560 0.03724  0.00846  0.00393  111 TYR A CB  
846  C CG  . TYR A 117 ? 0.34548 0.23063 0.38623 0.01485  -0.00252 0.01729  111 TYR A CG  
847  C CD1 . TYR A 117 ? 0.40180 0.24964 0.43170 -0.00061 0.02221  0.02386  111 TYR A CD1 
848  C CD2 . TYR A 117 ? 0.38933 0.24052 0.41183 0.00157  0.01573  0.01470  111 TYR A CD2 
849  C CE1 . TYR A 117 ? 0.44763 0.25800 0.45448 0.00880  0.04625  0.03715  111 TYR A CE1 
850  C CE2 . TYR A 117 ? 0.42405 0.25439 0.43300 -0.00546 0.02549  0.02763  111 TYR A CE2 
851  C CZ  . TYR A 117 ? 0.46287 0.26388 0.45386 0.00127  0.05305  0.03471  111 TYR A CZ  
852  O OH  . TYR A 117 ? 0.47858 0.26873 0.45969 -0.01026 0.06424  0.03261  111 TYR A OH  
853  N N   . LYS A 118 ? 0.22642 0.21934 0.29867 0.07924  -0.02999 -0.01462 112 LYS A N   
854  C CA  . LYS A 118 ? 0.23352 0.24512 0.31340 0.08270  -0.05479 -0.00169 112 LYS A CA  
855  C C   . LYS A 118 ? 0.24060 0.25205 0.33472 0.07357  -0.04980 -0.01406 112 LYS A C   
856  O O   . LYS A 118 ? 0.24797 0.25478 0.36523 0.07293  -0.05436 -0.02731 112 LYS A O   
857  C CB  . LYS A 118 ? 0.24353 0.26043 0.31019 0.10738  -0.07819 0.00350  112 LYS A CB  
858  C CG  . LYS A 118 ? 0.25301 0.26863 0.28849 0.10906  -0.08439 0.02690  112 LYS A CG  
859  C CD  . LYS A 118 ? 0.28764 0.28958 0.29369 0.07873  -0.07761 0.02452  112 LYS A CD  
860  C CE  . LYS A 118 ? 0.32767 0.31561 0.32504 0.05112  -0.06424 0.01773  112 LYS A CE  
861  N NZ  . LYS A 118 ? 0.32821 0.33021 0.32798 0.03768  -0.09517 0.02451  112 LYS A NZ  
862  N N   . LEU A 119 ? 0.23438 0.25025 0.34827 0.03795  -0.01748 -0.03468 113 LEU A N   
863  C CA  . LEU A 119 ? 0.21854 0.24888 0.38856 -0.00237 -0.00096 -0.02985 113 LEU A CA  
864  C C   . LEU A 119 ? 0.24511 0.24703 0.39030 -0.01774 0.01973  -0.02336 113 LEU A C   
865  O O   . LEU A 119 ? 0.27316 0.24378 0.40739 -0.02392 0.03924  -0.03507 113 LEU A O   
866  C CB  . LEU A 119 ? 0.21553 0.26570 0.44360 0.00168  0.03638  -0.02579 113 LEU A CB  
867  C CG  . LEU A 119 ? 0.19305 0.29101 0.49676 0.00379  0.00804  -0.02677 113 LEU A CG  
868  C CD1 . LEU A 119 ? 0.16926 0.31415 0.48385 -0.00308 -0.00740 -0.01185 113 LEU A CD1 
869  C CD2 . LEU A 119 ? 0.18581 0.28731 0.52573 0.00620  -0.01088 -0.01589 113 LEU A CD2 
870  N N   . LEU A 120 ? 0.19644 0.24845 0.37590 -0.04601 -0.01360 -0.02385 114 LEU A N   
871  C CA  . LEU A 120 ? 0.22183 0.27591 0.35967 -0.01204 -0.01148 -0.01650 114 LEU A CA  
872  C C   . LEU A 120 ? 0.23875 0.28414 0.35204 -0.01396 -0.02621 -0.01897 114 LEU A C   
873  O O   . LEU A 120 ? 0.25873 0.27542 0.35212 0.00895  -0.00409 -0.01794 114 LEU A O   
874  C CB  . LEU A 120 ? 0.23993 0.29862 0.35966 -0.00195 -0.00350 -0.00378 114 LEU A CB  
875  C CG  . LEU A 120 ? 0.24639 0.31709 0.38114 -0.01091 0.01110  -0.01038 114 LEU A CG  
876  C CD1 . LEU A 120 ? 0.22409 0.31264 0.38838 -0.00160 -0.03910 -0.04274 114 LEU A CD1 
877  C CD2 . LEU A 120 ? 0.28134 0.34478 0.40351 -0.02032 0.05033  0.00145  114 LEU A CD2 
878  N N   . LYS A 121 ? 0.26612 0.30956 0.37853 -0.01017 -0.00115 -0.01688 115 LYS A N   
879  C CA  . LYS A 121 ? 0.31641 0.32474 0.38489 -0.00513 0.01584  -0.01997 115 LYS A CA  
880  C C   . LYS A 121 ? 0.32964 0.33286 0.40266 0.01365  0.03071  -0.00947 115 LYS A C   
881  O O   . LYS A 121 ? 0.35461 0.35492 0.43462 0.01894  0.05255  -0.01616 115 LYS A O   
882  C CB  . LYS A 121 ? 0.34881 0.34237 0.38693 -0.00526 0.01120  -0.02917 115 LYS A CB  
883  C CG  . LYS A 121 ? 0.36829 0.35401 0.40395 0.01624  0.02047  -0.03285 115 LYS A CG  
884  C CD  . LYS A 121 ? 0.38249 0.36264 0.42379 0.04126  0.01577  -0.03133 115 LYS A CD  
885  C CE  . LYS A 121 ? 0.37430 0.36140 0.42254 0.05963  -0.00571 -0.03573 115 LYS A CE  
886  N NZ  . LYS A 121 ? 0.35575 0.36431 0.42401 0.07757  -0.02966 -0.03708 115 LYS A NZ  
887  N N   . THR A 122 ? 0.31248 0.32383 0.38769 0.01131  0.03215  0.01414  116 THR A N   
888  C CA  . THR A 122 ? 0.29639 0.32532 0.40156 0.02901  0.01840  0.03350  116 THR A CA  
889  C C   . THR A 122 ? 0.26786 0.31704 0.40691 0.05535  0.05950  0.02770  116 THR A C   
890  O O   . THR A 122 ? 0.29330 0.32738 0.43787 0.05742  0.09987  0.01058  116 THR A O   
891  C CB  . THR A 122 ? 0.30814 0.32854 0.39596 0.02363  -0.01075 0.05599  116 THR A CB  
892  O OG1 . THR A 122 ? 0.31365 0.33753 0.39730 0.01159  -0.03964 0.07442  116 THR A OG1 
893  C CG2 . THR A 122 ? 0.31866 0.33642 0.39754 0.01259  0.00010  0.05832  116 THR A CG2 
894  N N   . GLN A 123 ? 0.19495 0.29796 0.37211 0.07863  0.00514  0.04707  117 GLN A N   
895  C CA  . GLN A 123 ? 0.17618 0.31318 0.36665 0.06179  0.01941  0.03611  117 GLN A CA  
896  C C   . GLN A 123 ? 0.14899 0.31211 0.35791 0.05794  0.00388  0.02928  117 GLN A C   
897  O O   . GLN A 123 ? 0.15613 0.33487 0.37283 0.05496  0.02901  0.00276  117 GLN A O   
898  C CB  . GLN A 123 ? 0.20494 0.32686 0.36615 0.03382  0.01116  0.03785  117 GLN A CB  
899  C CG  . GLN A 123 ? 0.21311 0.34144 0.37837 0.02475  0.01834  0.04957  117 GLN A CG  
900  C CD  . GLN A 123 ? 0.22055 0.36057 0.38221 0.02540  0.00129  0.07596  117 GLN A CD  
901  O OE1 . GLN A 123 ? 0.19456 0.36466 0.37415 0.00399  -0.00546 0.06014  117 GLN A OE1 
902  N NE2 . GLN A 123 ? 0.24478 0.37818 0.39219 0.03950  -0.01659 0.09200  117 GLN A NE2 
903  N N   . HIS A 124 ? 0.16905 0.29929 0.35974 0.07031  0.01055  0.02324  118 HIS A N   
904  C CA  . HIS A 124 ? 0.23095 0.30442 0.35618 0.05916  0.02792  0.01711  118 HIS A CA  
905  C C   . HIS A 124 ? 0.19412 0.30581 0.37396 0.06699  0.02528  0.01951  118 HIS A C   
906  O O   . HIS A 124 ? 0.16949 0.31613 0.42966 0.08291  0.01212  0.02152  118 HIS A O   
907  C CB  . HIS A 124 ? 0.28049 0.31305 0.36907 0.06712  0.04677  0.02986  118 HIS A CB  
908  C CG  . HIS A 124 ? 0.33084 0.33394 0.40392 0.04525  0.07595  0.02661  118 HIS A CG  
909  N ND1 . HIS A 124 ? 0.33956 0.34299 0.41568 0.03875  0.07309  0.01818  118 HIS A ND1 
910  C CD2 . HIS A 124 ? 0.35790 0.34812 0.42115 0.02223  0.09550  0.02559  118 HIS A CD2 
911  C CE1 . HIS A 124 ? 0.34588 0.34816 0.41918 0.02809  0.07541  0.02632  118 HIS A CE1 
912  N NE2 . HIS A 124 ? 0.37555 0.35335 0.43143 0.02031  0.09677  0.02829  118 HIS A NE2 
913  N N   . LEU A 125 ? 0.18666 0.30649 0.35763 0.06082  0.04200  -0.01303 119 LEU A N   
914  C CA  . LEU A 125 ? 0.15584 0.31008 0.35802 0.06902  0.01906  -0.01799 119 LEU A CA  
915  C C   . LEU A 125 ? 0.19425 0.30890 0.36125 0.04985  0.02430  -0.03515 119 LEU A C   
916  O O   . LEU A 125 ? 0.25073 0.29848 0.34099 0.01735  0.02234  -0.02957 119 LEU A O   
917  C CB  . LEU A 125 ? 0.13829 0.33452 0.38305 0.07331  0.02643  -0.02271 119 LEU A CB  
918  C CG  . LEU A 125 ? 0.18207 0.38364 0.40527 0.09227  0.05418  -0.02660 119 LEU A CG  
919  C CD1 . LEU A 125 ? 0.16932 0.38385 0.39223 0.09620  0.05915  -0.04265 119 LEU A CD1 
920  C CD2 . LEU A 125 ? 0.25206 0.40491 0.42694 0.08542  0.07477  -0.01986 119 LEU A CD2 
921  N N   . SER A 126 ? 0.16481 0.31850 0.37051 0.05062  0.01759  -0.03159 120 SER A N   
922  C CA  . SER A 126 ? 0.17046 0.34841 0.35118 0.04395  0.02927  -0.03863 120 SER A CA  
923  C C   . SER A 126 ? 0.19442 0.35433 0.34420 0.02471  0.04821  -0.01074 120 SER A C   
924  O O   . SER A 126 ? 0.14500 0.36094 0.31665 0.01485  0.05738  -0.01015 120 SER A O   
925  C CB  . SER A 126 ? 0.16983 0.36214 0.36212 0.05171  0.04590  -0.07523 120 SER A CB  
926  O OG  . SER A 126 ? 0.15910 0.37991 0.33943 0.03817  0.02704  -0.06614 120 SER A OG  
927  N N   . ASN A 127 ? 0.23113 0.33733 0.34705 0.01759  0.06499  0.01139  121 ASN A N   
928  C CA  . ASN A 127 ? 0.21848 0.31862 0.33761 0.01747  0.03294  0.02684  121 ASN A CA  
929  C C   . ASN A 127 ? 0.18598 0.31015 0.33408 0.01328  0.05040  0.02988  121 ASN A C   
930  O O   . ASN A 127 ? 0.21014 0.28819 0.35153 0.02003  0.06453  0.05029  121 ASN A O   
931  C CB  . ASN A 127 ? 0.26255 0.31843 0.35474 0.00624  0.05122  0.01177  121 ASN A CB  
932  C CG  . ASN A 127 ? 0.25842 0.30803 0.36095 -0.00447 0.04058  0.00648  121 ASN A CG  
933  O OD1 . ASN A 127 ? 0.20724 0.30406 0.34661 -0.02183 -0.02252 0.00373  121 ASN A OD1 
934  N ND2 . ASN A 127 ? 0.29681 0.30058 0.40009 0.00966  0.08512  0.01201  121 ASN A ND2 
935  N N   . ASP A 128 ? 0.19303 0.32019 0.32943 -0.00121 0.07201  0.01271  122 ASP A N   
936  C CA  . ASP A 128 ? 0.19414 0.32750 0.33899 -0.01950 0.07952  0.04350  122 ASP A CA  
937  C C   . ASP A 128 ? 0.17330 0.32293 0.31766 -0.00670 0.07895  0.03824  122 ASP A C   
938  O O   . ASP A 128 ? 0.18907 0.32850 0.32379 -0.02221 0.04690  0.01564  122 ASP A O   
939  C CB  . ASP A 128 ? 0.19639 0.32782 0.36178 -0.01530 0.07492  0.07750  122 ASP A CB  
940  C CG  . ASP A 128 ? 0.20588 0.32147 0.35803 -0.02992 0.07310  0.11532  122 ASP A CG  
941  O OD1 . ASP A 128 ? 0.23307 0.33065 0.35009 -0.03800 0.05766  0.12665  122 ASP A OD1 
942  O OD2 . ASP A 128 ? 0.21959 0.31381 0.34880 -0.03649 0.09959  0.12079  122 ASP A OD2 
943  N N   . HIS A 129 ? 0.14173 0.30247 0.28759 0.02361  0.05800  0.04768  123 HIS A N   
944  C CA  . HIS A 129 ? 0.09303 0.29090 0.27927 0.02934  0.03458  0.03842  123 HIS A CA  
945  C C   . HIS A 129 ? 0.10788 0.26999 0.24950 0.03943  0.02010  0.04086  123 HIS A C   
946  O O   . HIS A 129 ? 0.12577 0.26996 0.23824 0.01098  0.04080  0.03933  123 HIS A O   
947  C CB  . HIS A 129 ? 0.08784 0.29109 0.29393 0.03256  0.01093  0.02869  123 HIS A CB  
948  C CG  . HIS A 129 ? 0.11835 0.32433 0.31814 0.04869  0.06032  0.01499  123 HIS A CG  
949  N ND1 . HIS A 129 ? 0.13782 0.34083 0.33466 0.05550  0.08349  0.00184  123 HIS A ND1 
950  C CD2 . HIS A 129 ? 0.14155 0.32171 0.32943 0.04596  0.06389  0.01626  123 HIS A CD2 
951  C CE1 . HIS A 129 ? 0.18593 0.34273 0.32827 0.04380  0.07142  0.00125  123 HIS A CE1 
952  N NE2 . HIS A 129 ? 0.16845 0.33101 0.31514 0.04018  0.06055  0.00927  123 HIS A NE2 
953  N N   . ILE A 130 ? 0.11684 0.27384 0.24378 0.03411  0.01006  0.01163  124 ILE A N   
954  C CA  . ILE A 130 ? 0.11181 0.26240 0.22541 0.04411  -0.00771 0.01332  124 ILE A CA  
955  C C   . ILE A 130 ? 0.13940 0.23214 0.24075 0.04186  0.01574  0.02708  124 ILE A C   
956  O O   . ILE A 130 ? 0.18603 0.23868 0.23707 0.02525  0.03248  0.03104  124 ILE A O   
957  C CB  . ILE A 130 ? 0.11890 0.27689 0.23817 0.04239  0.00318  -0.01370 124 ILE A CB  
958  C CG1 . ILE A 130 ? 0.16872 0.27414 0.23887 0.02834  0.01792  -0.04197 124 ILE A CG1 
959  C CG2 . ILE A 130 ? 0.10858 0.27378 0.26622 0.04282  -0.00149 0.00030  124 ILE A CG2 
960  C CD1 . ILE A 130 ? 0.18684 0.28422 0.25867 0.01143  0.02965  -0.05067 124 ILE A CD1 
961  N N   . CYS A 131 ? 0.15538 0.21470 0.24072 0.06331  0.04872  0.04240  125 CYS A N   
962  C CA  . CYS A 131 ? 0.19536 0.21431 0.23600 0.02970  0.06161  0.05783  125 CYS A CA  
963  C C   . CYS A 131 ? 0.17545 0.21471 0.23003 0.03366  0.04732  0.05085  125 CYS A C   
964  O O   . CYS A 131 ? 0.18868 0.19862 0.23351 0.03524  0.08016  0.05214  125 CYS A O   
965  C CB  . CYS A 131 ? 0.22446 0.22342 0.25133 0.03811  0.05345  0.08049  125 CYS A CB  
966  S SG  . CYS A 131 ? 0.30011 0.24461 0.28457 0.03175  0.08548  0.07385  125 CYS A SG  
967  N N   . TYR A 132 ? 0.17215 0.23449 0.25251 -0.02132 0.02373  0.03090  126 TYR A N   
968  C CA  . TYR A 132 ? 0.12602 0.24930 0.25458 -0.03357 -0.03560 0.04258  126 TYR A CA  
969  C C   . TYR A 132 ? 0.15762 0.23035 0.24487 -0.02622 0.02031  0.03815  126 TYR A C   
970  O O   . TYR A 132 ? 0.14969 0.22963 0.23008 -0.00581 0.00551  0.03706  126 TYR A O   
971  C CB  . TYR A 132 ? 0.14055 0.28925 0.31531 -0.05145 -0.03542 0.04409  126 TYR A CB  
972  C CG  . TYR A 132 ? 0.17278 0.31698 0.34550 -0.10189 -0.01849 0.05405  126 TYR A CG  
973  C CD1 . TYR A 132 ? 0.22278 0.34377 0.36666 -0.11626 -0.01000 0.04026  126 TYR A CD1 
974  C CD2 . TYR A 132 ? 0.21879 0.33439 0.35709 -0.12542 -0.01591 0.05501  126 TYR A CD2 
975  C CE1 . TYR A 132 ? 0.23944 0.35046 0.36836 -0.14108 -0.07622 0.03621  126 TYR A CE1 
976  C CE2 . TYR A 132 ? 0.25038 0.34422 0.35317 -0.14179 -0.06159 0.04349  126 TYR A CE2 
977  C CZ  . TYR A 132 ? 0.29520 0.36112 0.37277 -0.14629 -0.07714 0.03482  126 TYR A CZ  
978  O OH  . TYR A 132 ? 0.35515 0.38352 0.41806 -0.13536 -0.10001 0.04782  126 TYR A OH  
979  N N   . PHE A 133 ? 0.13462 0.20975 0.23324 -0.04464 0.01401  0.01676  127 PHE A N   
980  C CA  . PHE A 133 ? 0.10860 0.19838 0.25541 -0.02657 0.03736  0.01364  127 PHE A CA  
981  C C   . PHE A 133 ? 0.14716 0.19029 0.22260 -0.00138 0.01766  0.03245  127 PHE A C   
982  O O   . PHE A 133 ? 0.18128 0.19232 0.19854 -0.01052 0.03685  0.03417  127 PHE A O   
983  C CB  . PHE A 133 ? 0.12891 0.20158 0.27042 0.00792  0.01788  0.02722  127 PHE A CB  
984  C CG  . PHE A 133 ? 0.18204 0.22336 0.29963 0.02540  0.02006  0.01691  127 PHE A CG  
985  C CD1 . PHE A 133 ? 0.21067 0.24270 0.33123 0.04425  -0.01429 0.01420  127 PHE A CD1 
986  C CD2 . PHE A 133 ? 0.21527 0.22133 0.32639 0.03966  0.01432  0.02131  127 PHE A CD2 
987  C CE1 . PHE A 133 ? 0.22834 0.24462 0.33420 0.05486  -0.02876 0.00449  127 PHE A CE1 
988  C CE2 . PHE A 133 ? 0.21243 0.22590 0.32540 0.05829  -0.02149 0.00939  127 PHE A CE2 
989  C CZ  . PHE A 133 ? 0.21452 0.23779 0.31941 0.06654  -0.04324 0.01273  127 PHE A CZ  
990  N N   . LEU A 134 ? 0.16012 0.19498 0.21786 0.01858  -0.00482 0.03531  128 LEU A N   
991  C CA  . LEU A 134 ? 0.12967 0.19932 0.20193 -0.00989 -0.01942 0.02369  128 LEU A CA  
992  C C   . LEU A 134 ? 0.13586 0.19317 0.20622 -0.00708 0.00347  0.01582  128 LEU A C   
993  O O   . LEU A 134 ? 0.16987 0.19092 0.19967 0.01954  0.00655  0.02420  128 LEU A O   
994  C CB  . LEU A 134 ? 0.15162 0.19826 0.18907 -0.01138 -0.00236 0.02351  128 LEU A CB  
995  C CG  . LEU A 134 ? 0.18224 0.20456 0.17437 -0.01088 0.01585  0.02923  128 LEU A CG  
996  C CD1 . LEU A 134 ? 0.20418 0.19157 0.21134 -0.01176 0.04845  0.01848  128 LEU A CD1 
997  C CD2 . LEU A 134 ? 0.25010 0.20470 0.17520 -0.00329 0.03294  0.03335  128 LEU A CD2 
998  N N   . TYR A 135 ? 0.11084 0.17941 0.18818 -0.03133 0.00301  0.00641  129 TYR A N   
999  C CA  . TYR A 135 ? 0.13211 0.17531 0.18567 -0.03272 0.01625  0.01549  129 TYR A CA  
1000 C C   . TYR A 135 ? 0.13948 0.19184 0.18324 0.00288  0.00115  0.02766  129 TYR A C   
1001 O O   . TYR A 135 ? 0.13168 0.20596 0.19276 -0.00894 0.00397  0.03709  129 TYR A O   
1002 C CB  . TYR A 135 ? 0.15550 0.18208 0.20989 -0.05070 0.02181  -0.01299 129 TYR A CB  
1003 C CG  . TYR A 135 ? 0.17672 0.19935 0.18182 -0.04320 0.02672  -0.02383 129 TYR A CG  
1004 C CD1 . TYR A 135 ? 0.20012 0.21509 0.18377 -0.04595 0.03981  -0.00769 129 TYR A CD1 
1005 C CD2 . TYR A 135 ? 0.17448 0.21206 0.16379 -0.03756 0.05022  -0.01535 129 TYR A CD2 
1006 C CE1 . TYR A 135 ? 0.20612 0.21794 0.18247 -0.06143 0.02195  -0.00490 129 TYR A CE1 
1007 C CE2 . TYR A 135 ? 0.21909 0.20747 0.16504 -0.02942 0.02565  0.01981  129 TYR A CE2 
1008 C CZ  . TYR A 135 ? 0.21472 0.21526 0.17760 -0.04413 0.00129  0.00327  129 TYR A CZ  
1009 O OH  . TYR A 135 ? 0.21605 0.21448 0.22176 -0.04265 0.01183  0.02484  129 TYR A OH  
1010 N N   . GLN A 136 ? 0.11847 0.18648 0.15174 -0.02424 -0.05660 0.03048  130 GLN A N   
1011 C CA  . GLN A 136 ? 0.09638 0.19882 0.17127 -0.01804 -0.03613 0.02774  130 GLN A CA  
1012 C C   . GLN A 136 ? 0.12928 0.19558 0.17408 -0.01557 0.00317  0.02025  130 GLN A C   
1013 O O   . GLN A 136 ? 0.12412 0.21578 0.17356 -0.01027 0.02148  0.02934  130 GLN A O   
1014 C CB  . GLN A 136 ? 0.09312 0.20563 0.21886 -0.02192 -0.02416 0.01329  130 GLN A CB  
1015 C CG  . GLN A 136 ? 0.07603 0.21607 0.25264 -0.00270 -0.03388 0.01317  130 GLN A CG  
1016 C CD  . GLN A 136 ? 0.08808 0.22440 0.24399 0.00175  -0.03334 0.01888  130 GLN A CD  
1017 O OE1 . GLN A 136 ? 0.08821 0.22040 0.22546 0.01004  -0.03265 0.03539  130 GLN A OE1 
1018 N NE2 . GLN A 136 ? 0.11226 0.23406 0.22185 -0.02194 0.02037  0.01253  130 GLN A NE2 
1019 N N   . ILE A 137 ? 0.12218 0.15785 0.17132 -0.01358 -0.01855 0.00911  131 ILE A N   
1020 C CA  . ILE A 137 ? 0.12758 0.15130 0.18258 0.00607  -0.02394 0.01710  131 ILE A CA  
1021 C C   . ILE A 137 ? 0.12439 0.16138 0.17035 0.01590  -0.01551 0.01963  131 ILE A C   
1022 O O   . ILE A 137 ? 0.15160 0.15006 0.16693 -0.00525 -0.00301 0.02665  131 ILE A O   
1023 C CB  . ILE A 137 ? 0.13288 0.14570 0.20180 0.00597  -0.00754 0.00494  131 ILE A CB  
1024 C CG1 . ILE A 137 ? 0.11397 0.17524 0.20676 -0.01220 -0.00369 -0.00637 131 ILE A CG1 
1025 C CG2 . ILE A 137 ? 0.16369 0.14539 0.20634 0.03962  -0.02432 0.03277  131 ILE A CG2 
1026 C CD1 . ILE A 137 ? 0.09961 0.17883 0.20473 -0.01453 -0.00819 0.00488  131 ILE A CD1 
1027 N N   . LEU A 138 ? 0.15558 0.18022 0.15572 0.02007  0.00964  0.02806  132 LEU A N   
1028 C CA  . LEU A 138 ? 0.16989 0.18002 0.11960 0.00946  0.03211  0.02441  132 LEU A CA  
1029 C C   . LEU A 138 ? 0.14747 0.18169 0.14906 -0.00762 0.02047  0.01583  132 LEU A C   
1030 O O   . LEU A 138 ? 0.13117 0.18177 0.14672 -0.01231 0.00621  0.01421  132 LEU A O   
1031 C CB  . LEU A 138 ? 0.20392 0.18550 0.11312 -0.01312 0.02956  0.01547  132 LEU A CB  
1032 C CG  . LEU A 138 ? 0.18015 0.19332 0.13243 0.00611  0.03232  0.00721  132 LEU A CG  
1033 C CD1 . LEU A 138 ? 0.16875 0.20272 0.13895 -0.00272 -0.00050 0.03044  132 LEU A CD1 
1034 C CD2 . LEU A 138 ? 0.17320 0.19732 0.17232 0.01287  0.04110  -0.00983 132 LEU A CD2 
1035 N N   . ARG A 139 ? 0.11647 0.17771 0.16910 -0.02142 -0.00355 0.00178  133 ARG A N   
1036 C CA  . ARG A 139 ? 0.10628 0.18242 0.15721 -0.04942 -0.00487 0.01239  133 ARG A CA  
1037 C C   . ARG A 139 ? 0.11065 0.18417 0.16414 -0.03120 0.01584  0.03518  133 ARG A C   
1038 O O   . ARG A 139 ? 0.12638 0.19943 0.14954 -0.01952 0.01722  0.03111  133 ARG A O   
1039 C CB  . ARG A 139 ? 0.10198 0.16728 0.17829 -0.02519 0.00096  0.02485  133 ARG A CB  
1040 C CG  . ARG A 139 ? 0.09621 0.15643 0.19709 -0.04064 -0.01085 -0.01173 133 ARG A CG  
1041 C CD  . ARG A 139 ? 0.11667 0.16549 0.20396 -0.03806 -0.03994 -0.01812 133 ARG A CD  
1042 N NE  . ARG A 139 ? 0.13002 0.16225 0.20377 -0.03623 -0.03749 0.01087  133 ARG A NE  
1043 C CZ  . ARG A 139 ? 0.17441 0.17432 0.20855 -0.03948 -0.04542 0.04129  133 ARG A CZ  
1044 N NH1 . ARG A 139 ? 0.18586 0.18216 0.23745 -0.03376 -0.07124 0.04343  133 ARG A NH1 
1045 N NH2 . ARG A 139 ? 0.19353 0.18568 0.19403 -0.04391 -0.05406 0.04693  133 ARG A NH2 
1046 N N   . GLY A 140 ? 0.10714 0.17484 0.18949 -0.03412 0.00197  0.02692  134 GLY A N   
1047 C CA  . GLY A 140 ? 0.11699 0.16800 0.18605 -0.03288 0.02234  0.01151  134 GLY A CA  
1048 C C   . GLY A 140 ? 0.12677 0.16607 0.17284 -0.02085 -0.01033 0.00707  134 GLY A C   
1049 O O   . GLY A 140 ? 0.15815 0.14815 0.16239 -0.02842 -0.00266 0.02782  134 GLY A O   
1050 N N   . LEU A 141 ? 0.11229 0.18210 0.19286 -0.03537 -0.03299 0.01326  135 LEU A N   
1051 C CA  . LEU A 141 ? 0.10971 0.17717 0.19402 -0.03458 -0.04645 -0.00256 135 LEU A CA  
1052 C C   . LEU A 141 ? 0.12744 0.16483 0.18773 -0.02680 -0.00282 0.02086  135 LEU A C   
1053 O O   . LEU A 141 ? 0.16515 0.17897 0.19859 -0.03039 0.00973  0.01802  135 LEU A O   
1054 C CB  . LEU A 141 ? 0.12301 0.19209 0.17189 -0.01781 -0.04088 0.00327  135 LEU A CB  
1055 C CG  . LEU A 141 ? 0.11284 0.18631 0.13956 -0.03598 -0.01829 0.00589  135 LEU A CG  
1056 C CD1 . LEU A 141 ? 0.15095 0.20559 0.18369 -0.03343 0.03737  0.01464  135 LEU A CD1 
1057 C CD2 . LEU A 141 ? 0.17438 0.20691 0.17481 -0.03553 -0.00172 0.00748  135 LEU A CD2 
1058 N N   . LYS A 142 ? 0.17710 0.14304 0.15518 -0.00158 -0.00594 0.02516  136 LYS A N   
1059 C CA  . LYS A 142 ? 0.19533 0.13800 0.15763 -0.00278 0.02501  0.03251  136 LYS A CA  
1060 C C   . LYS A 142 ? 0.20263 0.16814 0.15917 -0.00514 0.00640  0.01209  136 LYS A C   
1061 O O   . LYS A 142 ? 0.19352 0.16670 0.17531 -0.02480 0.01299  -0.00111 136 LYS A O   
1062 C CB  . LYS A 142 ? 0.16721 0.11522 0.17878 -0.00726 0.00475  0.06082  136 LYS A CB  
1063 C CG  . LYS A 142 ? 0.19548 0.11316 0.19276 -0.01927 0.00362  0.04411  136 LYS A CG  
1064 C CD  . LYS A 142 ? 0.22610 0.09366 0.20597 -0.04330 -0.00470 0.02688  136 LYS A CD  
1065 C CE  . LYS A 142 ? 0.23180 0.10089 0.24408 -0.04847 -0.01489 0.00128  136 LYS A CE  
1066 N NZ  . LYS A 142 ? 0.25337 0.10743 0.24583 -0.05570 -0.01436 0.00083  136 LYS A NZ  
1067 N N   . TYR A 143 ? 0.19191 0.18035 0.14756 -0.00458 -0.04392 0.01338  137 TYR A N   
1068 C CA  . TYR A 143 ? 0.16211 0.19215 0.14603 -0.01172 -0.03160 0.00402  137 TYR A CA  
1069 C C   . TYR A 143 ? 0.17661 0.19076 0.18109 -0.03419 0.00523  -0.01364 137 TYR A C   
1070 O O   . TYR A 143 ? 0.19048 0.19746 0.16557 -0.06011 0.02247  -0.03709 137 TYR A O   
1071 C CB  . TYR A 143 ? 0.17355 0.18125 0.15115 0.00880  -0.02389 0.00492  137 TYR A CB  
1072 C CG  . TYR A 143 ? 0.20073 0.18712 0.16379 -0.00647 -0.02230 -0.00718 137 TYR A CG  
1073 C CD1 . TYR A 143 ? 0.22736 0.18062 0.15651 -0.01147 -0.00243 -0.00805 137 TYR A CD1 
1074 C CD2 . TYR A 143 ? 0.20204 0.18369 0.18312 0.01145  0.00215  -0.01655 137 TYR A CD2 
1075 C CE1 . TYR A 143 ? 0.24294 0.18525 0.21206 -0.00004 -0.00295 -0.02208 137 TYR A CE1 
1076 C CE2 . TYR A 143 ? 0.19642 0.20601 0.17713 0.00137  -0.02499 0.00909  137 TYR A CE2 
1077 C CZ  . TYR A 143 ? 0.23129 0.21774 0.20352 -0.00011 -0.01919 -0.00385 137 TYR A CZ  
1078 O OH  . TYR A 143 ? 0.23281 0.23239 0.19468 0.00717  -0.02693 -0.00191 137 TYR A OH  
1079 N N   . ILE A 144 ? 0.15163 0.17751 0.18367 -0.02577 -0.00503 -0.01549 138 ILE A N   
1080 C CA  . ILE A 144 ? 0.13558 0.19069 0.18442 -0.00756 -0.00416 0.00342  138 ILE A CA  
1081 C C   . ILE A 144 ? 0.12976 0.20686 0.18166 -0.00442 0.01260  0.01022  138 ILE A C   
1082 O O   . ILE A 144 ? 0.18327 0.21472 0.18161 -0.02769 0.04503  -0.00474 138 ILE A O   
1083 C CB  . ILE A 144 ? 0.09771 0.17840 0.18855 -0.00741 -0.00864 -0.00078 138 ILE A CB  
1084 C CG1 . ILE A 144 ? 0.14385 0.18785 0.14449 0.02363  -0.00854 -0.01905 138 ILE A CG1 
1085 C CG2 . ILE A 144 ? 0.11386 0.19050 0.18774 -0.04520 0.01922  0.01771  138 ILE A CG2 
1086 C CD1 . ILE A 144 ? 0.18897 0.20464 0.16148 0.04530  -0.00783 -0.01221 138 ILE A CD1 
1087 N N   . HIS A 145 ? 0.08724 0.20036 0.17419 -0.00752 -0.02176 0.00072  139 HIS A N   
1088 C CA  . HIS A 145 ? 0.09864 0.19036 0.16424 0.01520  -0.00883 -0.02248 139 HIS A CA  
1089 C C   . HIS A 145 ? 0.15817 0.19844 0.18973 0.01343  0.01405  -0.02294 139 HIS A C   
1090 O O   . HIS A 145 ? 0.19074 0.21642 0.20229 0.02422  0.00018  -0.02094 139 HIS A O   
1091 C CB  . HIS A 145 ? 0.12947 0.19847 0.15829 0.01695  -0.01254 -0.02651 139 HIS A CB  
1092 C CG  . HIS A 145 ? 0.15230 0.20836 0.16027 0.00247  -0.00559 -0.03641 139 HIS A CG  
1093 N ND1 . HIS A 145 ? 0.15937 0.20574 0.14345 0.01112  -0.01986 -0.02595 139 HIS A ND1 
1094 C CD2 . HIS A 145 ? 0.14794 0.21476 0.16102 -0.01637 -0.00139 -0.02859 139 HIS A CD2 
1095 C CE1 . HIS A 145 ? 0.15894 0.22445 0.16512 0.00436  -0.01362 -0.02041 139 HIS A CE1 
1096 N NE2 . HIS A 145 ? 0.15437 0.22793 0.13364 -0.02683 -0.01363 -0.04520 139 HIS A NE2 
1097 N N   . SER A 146 ? 0.19953 0.18787 0.17544 -0.01483 0.00014  -0.01546 140 SER A N   
1098 C CA  . SER A 146 ? 0.19619 0.17769 0.17330 -0.02347 -0.00242 -0.04841 140 SER A CA  
1099 C C   . SER A 146 ? 0.22818 0.20861 0.19292 -0.00611 0.01917  -0.02472 140 SER A C   
1100 O O   . SER A 146 ? 0.26916 0.22091 0.22708 -0.01664 0.03820  -0.05300 140 SER A O   
1101 C CB  . SER A 146 ? 0.20118 0.18489 0.16962 -0.00371 -0.01829 -0.02168 140 SER A CB  
1102 O OG  . SER A 146 ? 0.23629 0.20583 0.19342 -0.01975 -0.00962 -0.04908 140 SER A OG  
1103 N N   . ALA A 147 ? 0.20535 0.22823 0.16215 -0.03695 0.01183  0.00585  141 ALA A N   
1104 C CA  . ALA A 147 ? 0.19679 0.25946 0.16407 -0.02296 0.01550  -0.00569 141 ALA A CA  
1105 C C   . ALA A 147 ? 0.22675 0.27367 0.18415 -0.02391 0.03777  -0.02595 141 ALA A C   
1106 O O   . ALA A 147 ? 0.25074 0.29923 0.21669 -0.04683 0.06832  -0.03481 141 ALA A O   
1107 C CB  . ALA A 147 ? 0.21225 0.26590 0.16061 -0.02285 -0.00435 0.01133  141 ALA A CB  
1108 N N   . ASN A 148 ? 0.22358 0.27248 0.19104 -0.01649 0.02236  -0.04617 142 ASN A N   
1109 C CA  . ASN A 148 ? 0.22554 0.27154 0.23128 0.02385  0.06271  -0.04380 142 ASN A CA  
1110 C C   . ASN A 148 ? 0.20476 0.27804 0.21964 0.02683  0.05538  -0.03058 142 ASN A C   
1111 O O   . ASN A 148 ? 0.18334 0.29215 0.24388 0.03008  0.03140  -0.02549 142 ASN A O   
1112 C CB  . ASN A 148 ? 0.24725 0.28561 0.28233 0.02473  0.06372  -0.04855 142 ASN A CB  
1113 C CG  . ASN A 148 ? 0.28902 0.28930 0.34558 0.02582  0.08441  -0.04406 142 ASN A CG  
1114 O OD1 . ASN A 148 ? 0.29910 0.27976 0.36469 0.02662  0.05397  -0.03824 142 ASN A OD1 
1115 N ND2 . ASN A 148 ? 0.31730 0.29388 0.38429 0.03134  0.11045  -0.05967 142 ASN A ND2 
1116 N N   . VAL A 149 ? 0.17226 0.28109 0.21433 0.01342  0.02223  -0.02096 143 VAL A N   
1117 C CA  . VAL A 149 ? 0.16559 0.26607 0.18683 0.01185  -0.00081 -0.01419 143 VAL A CA  
1118 C C   . VAL A 149 ? 0.18164 0.24760 0.18675 -0.00831 0.00002  -0.02648 143 VAL A C   
1119 O O   . VAL A 149 ? 0.17564 0.23837 0.19379 0.00031  0.01889  -0.03126 143 VAL A O   
1120 C CB  . VAL A 149 ? 0.19527 0.28289 0.16684 -0.00731 0.00587  -0.02623 143 VAL A CB  
1121 C CG1 . VAL A 149 ? 0.20306 0.29843 0.18404 -0.00677 -0.00694 -0.03838 143 VAL A CG1 
1122 C CG2 . VAL A 149 ? 0.22841 0.29572 0.15401 -0.02795 0.02028  -0.04092 143 VAL A CG2 
1123 N N   . LEU A 150 ? 0.18726 0.23487 0.18196 -0.01246 -0.00657 -0.03911 144 LEU A N   
1124 C CA  . LEU A 150 ? 0.15519 0.23759 0.18117 -0.01026 -0.04404 -0.03197 144 LEU A CA  
1125 C C   . LEU A 150 ? 0.13509 0.22966 0.17018 0.01063  -0.01790 -0.00445 144 LEU A C   
1126 O O   . LEU A 150 ? 0.15699 0.24302 0.19572 0.01351  0.00592  -0.01432 144 LEU A O   
1127 C CB  . LEU A 150 ? 0.15976 0.26459 0.22870 0.00571  -0.03978 -0.00554 144 LEU A CB  
1128 C CG  . LEU A 150 ? 0.18151 0.27513 0.26095 0.00204  -0.02233 -0.00730 144 LEU A CG  
1129 C CD1 . LEU A 150 ? 0.16217 0.26606 0.26484 0.00741  -0.04606 -0.03728 144 LEU A CD1 
1130 C CD2 . LEU A 150 ? 0.23107 0.29027 0.27083 -0.00002 -0.00527 -0.01566 144 LEU A CD2 
1131 N N   . HIS A 151 ? 0.12663 0.20438 0.16895 0.01511  0.00185  0.00490  145 HIS A N   
1132 C CA  . HIS A 151 ? 0.13714 0.19783 0.17085 -0.01559 0.01844  0.00805  145 HIS A CA  
1133 C C   . HIS A 151 ? 0.16487 0.20848 0.17147 -0.02350 0.01659  -0.00483 145 HIS A C   
1134 O O   . HIS A 151 ? 0.14840 0.23159 0.16647 -0.01786 0.03593  -0.00665 145 HIS A O   
1135 C CB  . HIS A 151 ? 0.13108 0.18444 0.15597 0.00338  0.00193  0.02852  145 HIS A CB  
1136 C CG  . HIS A 151 ? 0.12674 0.17414 0.15219 -0.01284 -0.02640 0.02439  145 HIS A CG  
1137 N ND1 . HIS A 151 ? 0.13299 0.16183 0.18405 -0.00791 0.00366  0.04735  145 HIS A ND1 
1138 C CD2 . HIS A 151 ? 0.12671 0.17909 0.18246 0.01752  -0.01544 0.05106  145 HIS A CD2 
1139 C CE1 . HIS A 151 ? 0.14943 0.17377 0.20141 0.00906  0.00251  0.05084  145 HIS A CE1 
1140 N NE2 . HIS A 151 ? 0.14955 0.17747 0.20139 0.00477  0.00315  0.05487  145 HIS A NE2 
1141 N N   . ARG A 152 ? 0.16828 0.19387 0.14723 -0.00719 -0.00080 -0.01147 146 ARG A N   
1142 C CA  . ARG A 152 ? 0.16477 0.20859 0.16445 0.00641  0.02118  -0.02472 146 ARG A CA  
1143 C C   . ARG A 152 ? 0.18865 0.22498 0.21937 0.00369  0.02646  -0.00170 146 ARG A C   
1144 O O   . ARG A 152 ? 0.18945 0.25450 0.30469 0.00057  0.03671  -0.03055 146 ARG A O   
1145 C CB  . ARG A 152 ? 0.19560 0.21993 0.15440 0.02532  0.01842  -0.03601 146 ARG A CB  
1146 C CG  . ARG A 152 ? 0.21507 0.25891 0.16188 0.04589  0.01318  -0.03649 146 ARG A CG  
1147 C CD  . ARG A 152 ? 0.25183 0.28394 0.19327 0.03396  0.00905  -0.04310 146 ARG A CD  
1148 N NE  . ARG A 152 ? 0.34254 0.30884 0.23732 0.03233  0.04155  -0.04592 146 ARG A NE  
1149 C CZ  . ARG A 152 ? 0.38112 0.31844 0.23263 0.03169  0.02627  -0.05256 146 ARG A CZ  
1150 N NH1 . ARG A 152 ? 0.39855 0.32440 0.22878 0.05339  0.00513  -0.07798 146 ARG A NH1 
1151 N NH2 . ARG A 152 ? 0.35570 0.32361 0.21602 0.01024  -0.00465 -0.05248 146 ARG A NH2 
1152 N N   . ASP A 153 ? 0.15626 0.21778 0.18181 0.01878  -0.00099 0.02203  147 ASP A N   
1153 C CA  . ASP A 153 ? 0.17577 0.20396 0.19379 0.01012  -0.00058 0.03712  147 ASP A CA  
1154 C C   . ASP A 153 ? 0.16710 0.19192 0.19522 0.00288  -0.02834 0.03321  147 ASP A C   
1155 O O   . ASP A 153 ? 0.17390 0.19101 0.20402 0.01094  -0.04400 0.04814  147 ASP A O   
1156 C CB  . ASP A 153 ? 0.17660 0.20013 0.21777 0.00922  0.00314  0.03150  147 ASP A CB  
1157 C CG  . ASP A 153 ? 0.22737 0.21758 0.22906 0.00785  -0.00828 0.03941  147 ASP A CG  
1158 O OD1 . ASP A 153 ? 0.21797 0.22117 0.24121 0.00128  -0.00049 0.02007  147 ASP A OD1 
1159 O OD2 . ASP A 153 ? 0.25880 0.22568 0.24820 0.02520  -0.02314 0.01491  147 ASP A OD2 
1160 N N   . LEU A 154 ? 0.15427 0.19067 0.18922 0.01507  -0.02433 0.02748  148 LEU A N   
1161 C CA  . LEU A 154 ? 0.15267 0.17677 0.20105 -0.01527 0.02431  0.02428  148 LEU A CA  
1162 C C   . LEU A 154 ? 0.18380 0.19105 0.19614 -0.01116 0.02125  0.01752  148 LEU A C   
1163 O O   . LEU A 154 ? 0.17733 0.18494 0.18100 -0.02529 -0.00608 0.01573  148 LEU A O   
1164 C CB  . LEU A 154 ? 0.16264 0.17660 0.20099 -0.01577 0.01474  0.01314  148 LEU A CB  
1165 C CG  . LEU A 154 ? 0.13743 0.17220 0.17673 -0.00751 -0.01910 0.00206  148 LEU A CG  
1166 C CD1 . LEU A 154 ? 0.14548 0.18770 0.16939 0.02851  -0.01609 0.02372  148 LEU A CD1 
1167 C CD2 . LEU A 154 ? 0.15355 0.18695 0.17525 -0.00640 -0.03615 -0.00090 148 LEU A CD2 
1168 N N   . LYS A 155 ? 0.16651 0.19495 0.18057 0.01767  0.01781  0.00284  149 LYS A N   
1169 C CA  . LYS A 155 ? 0.12936 0.19757 0.17609 0.00178  0.00831  -0.00020 149 LYS A CA  
1170 C C   . LYS A 155 ? 0.14722 0.19853 0.18131 0.02471  -0.00558 -0.00035 149 LYS A C   
1171 O O   . LYS A 155 ? 0.15455 0.16900 0.19534 0.02633  0.00341  0.01071  149 LYS A O   
1172 C CB  . LYS A 155 ? 0.16179 0.20408 0.18765 -0.02580 -0.00490 0.02469  149 LYS A CB  
1173 C CG  . LYS A 155 ? 0.16920 0.20341 0.21106 -0.00727 0.01304  0.06267  149 LYS A CG  
1174 C CD  . LYS A 155 ? 0.17697 0.23208 0.23824 -0.01532 -0.00117 0.07281  149 LYS A CD  
1175 C CE  . LYS A 155 ? 0.18397 0.24288 0.27897 -0.04675 -0.02136 0.09561  149 LYS A CE  
1176 N NZ  . LYS A 155 ? 0.20116 0.26272 0.33397 -0.04277 -0.06172 0.09637  149 LYS A NZ  
1177 N N   . PRO A 156 ? 0.15139 0.20949 0.19956 0.02280  -0.02296 -0.00778 150 PRO A N   
1178 C CA  . PRO A 156 ? 0.14659 0.20320 0.21849 0.02279  0.00484  0.00149  150 PRO A CA  
1179 C C   . PRO A 156 ? 0.14449 0.20325 0.23615 0.02668  -0.00572 0.03007  150 PRO A C   
1180 O O   . PRO A 156 ? 0.14286 0.21662 0.24996 0.03407  0.00535  0.03084  150 PRO A O   
1181 C CB  . PRO A 156 ? 0.18487 0.21041 0.22596 0.00931  0.01014  -0.00453 150 PRO A CB  
1182 C CG  . PRO A 156 ? 0.13280 0.21725 0.20935 0.01023  0.00595  0.00133  150 PRO A CG  
1183 C CD  . PRO A 156 ? 0.15084 0.21496 0.20827 0.00887  0.02696  -0.02284 150 PRO A CD  
1184 N N   . SER A 157 ? 0.14300 0.20681 0.21254 0.03873  -0.02865 0.03926  151 SER A N   
1185 C CA  . SER A 157 ? 0.20951 0.22005 0.22246 0.02681  -0.02105 0.03270  151 SER A CA  
1186 C C   . SER A 157 ? 0.19566 0.22055 0.21129 0.01722  -0.03317 0.02370  151 SER A C   
1187 O O   . SER A 157 ? 0.21359 0.23219 0.23206 0.02412  -0.02439 0.02319  151 SER A O   
1188 C CB  . SER A 157 ? 0.22592 0.23327 0.25856 0.02515  -0.01459 0.04258  151 SER A CB  
1189 O OG  . SER A 157 ? 0.22135 0.22587 0.28729 0.02048  -0.01179 0.05474  151 SER A OG  
1190 N N   . ASN A 158 ? 0.15655 0.21827 0.23409 0.01533  -0.01851 0.03684  152 ASN A N   
1191 C CA  . ASN A 158 ? 0.13241 0.21237 0.22903 0.01574  -0.02672 0.05524  152 ASN A CA  
1192 C C   . ASN A 158 ? 0.15743 0.22482 0.26289 0.02259  -0.00808 0.04097  152 ASN A C   
1193 O O   . ASN A 158 ? 0.16112 0.21526 0.26427 0.02893  -0.00454 0.05210  152 ASN A O   
1194 C CB  . ASN A 158 ? 0.13995 0.21748 0.21327 -0.00558 -0.05451 0.05654  152 ASN A CB  
1195 C CG  . ASN A 158 ? 0.15945 0.23595 0.22161 0.00801  -0.04393 0.06843  152 ASN A CG  
1196 O OD1 . ASN A 158 ? 0.21334 0.24498 0.25259 0.01294  -0.01426 0.06011  152 ASN A OD1 
1197 N ND2 . ASN A 158 ? 0.13344 0.24678 0.24509 -0.00678 -0.05807 0.09271  152 ASN A ND2 
1198 N N   . LEU A 159 ? 0.12427 0.22316 0.24120 0.02657  -0.02025 0.02539  153 LEU A N   
1199 C CA  . LEU A 159 ? 0.11614 0.23287 0.22588 0.02689  -0.03983 0.02696  153 LEU A CA  
1200 C C   . LEU A 159 ? 0.12111 0.25295 0.23599 0.02821  -0.04253 0.02040  153 LEU A C   
1201 O O   . LEU A 159 ? 0.15323 0.27052 0.27049 0.04737  -0.03502 0.02752  153 LEU A O   
1202 C CB  . LEU A 159 ? 0.12208 0.23074 0.21042 0.04699  -0.06135 0.03192  153 LEU A CB  
1203 C CG  . LEU A 159 ? 0.11407 0.23841 0.19947 0.05567  -0.03623 0.02642  153 LEU A CG  
1204 C CD1 . LEU A 159 ? 0.10770 0.24860 0.18894 0.02654  -0.05071 0.05126  153 LEU A CD1 
1205 C CD2 . LEU A 159 ? 0.14071 0.24535 0.22848 0.09102  -0.00050 0.01111  153 LEU A CD2 
1206 N N   . LEU A 160 ? 0.10120 0.26297 0.20683 0.00760  -0.04230 0.02598  154 LEU A N   
1207 C CA  . LEU A 160 ? 0.11789 0.29043 0.19921 0.01977  -0.02684 0.04722  154 LEU A CA  
1208 C C   . LEU A 160 ? 0.14260 0.30413 0.20000 0.02621  -0.01055 0.04135  154 LEU A C   
1209 O O   . LEU A 160 ? 0.14877 0.28778 0.21130 0.04231  0.01291  0.01365  154 LEU A O   
1210 C CB  . LEU A 160 ? 0.14395 0.31326 0.20640 0.03005  -0.03273 0.06209  154 LEU A CB  
1211 C CG  . LEU A 160 ? 0.25715 0.32567 0.28279 0.03154  0.02963  0.07481  154 LEU A CG  
1212 C CD1 . LEU A 160 ? 0.27645 0.34394 0.28721 0.01614  0.03228  0.08878  154 LEU A CD1 
1213 C CD2 . LEU A 160 ? 0.32406 0.32863 0.35696 0.01875  0.09244  0.04697  154 LEU A CD2 
1214 N N   . LEU A 161 ? 0.14925 0.33624 0.20435 0.00082  -0.00091 0.03153  155 LEU A N   
1215 C CA  . LEU A 161 ? 0.16351 0.36218 0.19327 0.01257  -0.00708 0.01982  155 LEU A CA  
1216 C C   . LEU A 161 ? 0.16514 0.38373 0.21056 0.01235  0.00956  0.02195  155 LEU A C   
1217 O O   . LEU A 161 ? 0.18173 0.39181 0.23029 0.03083  -0.00308 0.03213  155 LEU A O   
1218 C CB  . LEU A 161 ? 0.18956 0.36938 0.20125 0.03613  -0.05581 0.02315  155 LEU A CB  
1219 C CG  . LEU A 161 ? 0.25212 0.38915 0.22514 0.03324  -0.08025 0.00967  155 LEU A CG  
1220 C CD1 . LEU A 161 ? 0.29108 0.40300 0.27642 0.04604  -0.09086 0.03301  155 LEU A CD1 
1221 C CD2 . LEU A 161 ? 0.23056 0.39229 0.27113 -0.02656 -0.09146 -0.01994 155 LEU A CD2 
1222 N N   . ASN A 162 ? 0.13034 0.40554 0.22623 -0.00478 -0.01085 0.01287  156 ASN A N   
1223 C CA  . ASN A 162 ? 0.11316 0.40976 0.27410 0.00779  -0.02830 0.03693  156 ASN A CA  
1224 C C   . ASN A 162 ? 0.12205 0.41128 0.30870 -0.00379 0.00126  0.04417  156 ASN A C   
1225 O O   . ASN A 162 ? 0.12419 0.39537 0.32703 -0.00495 0.00329  0.02999  156 ASN A O   
1226 C CB  . ASN A 162 ? 0.13639 0.40916 0.30300 0.00393  -0.02802 0.02309  156 ASN A CB  
1227 C CG  . ASN A 162 ? 0.17278 0.42249 0.36114 0.01440  -0.02366 -0.00325 156 ASN A CG  
1228 O OD1 . ASN A 162 ? 0.14137 0.41836 0.36780 -0.00473 -0.02373 0.00795  156 ASN A OD1 
1229 N ND2 . ASN A 162 ? 0.22290 0.43080 0.38851 0.02460  -0.02093 -0.01844 156 ASN A ND2 
1230 N N   . THR A 163 ? 0.11646 0.42031 0.35235 0.01587  0.01738  0.05658  157 THR A N   
1231 C CA  . THR A 163 ? 0.12186 0.43011 0.37073 0.01887  -0.01762 0.06295  157 THR A CA  
1232 C C   . THR A 163 ? 0.11981 0.44295 0.37147 0.00829  0.00630  0.05481  157 THR A C   
1233 O O   . THR A 163 ? 0.15377 0.44382 0.39072 -0.00620 0.07162  0.05665  157 THR A O   
1234 C CB  . THR A 163 ? 0.19601 0.50227 0.42052 -0.01679 -0.03987 0.07721  157 THR A CB  
1235 O OG1 . THR A 163 ? 0.21612 0.53554 0.46071 -0.02614 -0.03080 0.07338  157 THR A OG1 
1236 C CG2 . THR A 163 ? 0.23262 0.52127 0.45438 0.00364  -0.02321 0.08953  157 THR A CG2 
1237 N N   . THR A 164 ? 0.12420 0.43738 0.35495 0.00203  0.00290  0.04037  158 THR A N   
1238 C CA  . THR A 164 ? 0.14668 0.42977 0.36365 -0.00910 0.01227  0.01190  158 THR A CA  
1239 C C   . THR A 164 ? 0.15270 0.42570 0.33119 -0.01548 0.02663  0.00880  158 THR A C   
1240 O O   . THR A 164 ? 0.18455 0.43006 0.37276 -0.02796 0.06470  0.03125  158 THR A O   
1241 C CB  . THR A 164 ? 0.15471 0.43131 0.40363 -0.01391 0.00187  -0.01974 158 THR A CB  
1242 O OG1 . THR A 164 ? 0.13618 0.43607 0.42170 0.02068  -0.01965 -0.04721 158 THR A OG1 
1243 C CG2 . THR A 164 ? 0.19137 0.43222 0.42610 -0.03145 0.01358  -0.01525 158 THR A CG2 
1244 N N   . CME A 165 ? 0.11963 0.42433 0.27629 -0.02498 -0.00444 0.00246  159 CME A N   
1245 C CA  . CME A 165 ? 0.18000 0.42672 0.25925 0.02828  0.03030  0.02094  159 CME A CA  
1246 C CB  . CME A 165 ? 0.25492 0.48368 0.27563 0.06298  0.05750  -0.00006 159 CME A CB  
1247 S SG  . CME A 165 ? 0.28438 0.54624 0.30137 0.11184  0.04535  -0.00540 159 CME A SG  
1248 S SD  . CME A 165 ? 0.36852 0.54187 0.33747 0.16141  -0.02638 -0.02629 159 CME A SD  
1249 C CE  . CME A 165 ? 0.35656 0.53014 0.27255 0.17065  -0.00640 -0.01766 159 CME A CE  
1250 C CZ  . CME A 165 ? 0.34129 0.51774 0.23527 0.18452  0.02765  -0.02801 159 CME A CZ  
1251 O OH  . CME A 165 ? 0.36893 0.50708 0.19972 0.20019  0.04564  -0.01722 159 CME A OH  
1252 C C   . CME A 165 ? 0.15685 0.37201 0.24801 0.00975  0.03113  0.02914  159 CME A C   
1253 O O   . CME A 165 ? 0.15371 0.35394 0.24192 0.00674  0.03672  0.02015  159 CME A O   
1254 N N   . ASP A 166 ? 0.12735 0.33921 0.28225 0.00477  0.02824  -0.00286 160 ASP A N   
1255 C CA  . ASP A 166 ? 0.12575 0.31429 0.29990 -0.00708 0.01851  -0.01052 160 ASP A CA  
1256 C C   . ASP A 166 ? 0.10808 0.30491 0.25333 -0.00425 0.00596  -0.00205 160 ASP A C   
1257 O O   . ASP A 166 ? 0.11270 0.32232 0.24034 0.01001  0.00164  0.00591  160 ASP A O   
1258 C CB  . ASP A 166 ? 0.10781 0.31374 0.36772 -0.03331 -0.03793 -0.02514 160 ASP A CB  
1259 C CG  . ASP A 166 ? 0.14638 0.32480 0.44937 -0.04340 -0.04085 -0.01622 160 ASP A CG  
1260 O OD1 . ASP A 166 ? 0.15090 0.32062 0.50919 -0.04107 -0.04457 0.01089  160 ASP A OD1 
1261 O OD2 . ASP A 166 ? 0.17899 0.33976 0.49229 -0.04903 -0.01443 -0.03210 160 ASP A OD2 
1262 N N   . LEU A 167 ? 0.12407 0.29109 0.21531 -0.01878 0.00608  0.01716  161 LEU A N   
1263 C CA  . LEU A 167 ? 0.12683 0.26085 0.18847 -0.01975 -0.00194 0.03513  161 LEU A CA  
1264 C C   . LEU A 167 ? 0.14276 0.26365 0.20158 -0.02510 0.00605  0.05246  161 LEU A C   
1265 O O   . LEU A 167 ? 0.17199 0.27264 0.21779 -0.00679 0.02156  0.07507  161 LEU A O   
1266 C CB  . LEU A 167 ? 0.12123 0.25700 0.19022 -0.04075 -0.02126 0.02452  161 LEU A CB  
1267 C CG  . LEU A 167 ? 0.12929 0.26200 0.21504 -0.03939 -0.00958 0.04389  161 LEU A CG  
1268 C CD1 . LEU A 167 ? 0.14054 0.27643 0.21422 -0.02308 -0.03334 0.03345  161 LEU A CD1 
1269 C CD2 . LEU A 167 ? 0.13335 0.26548 0.23417 -0.02817 0.02486  0.07563  161 LEU A CD2 
1270 N N   . LYS A 168 ? 0.12019 0.25494 0.16719 -0.03789 0.01270  0.04506  162 LYS A N   
1271 C CA  . LYS A 168 ? 0.12483 0.26010 0.16894 -0.03109 -0.02554 0.02173  162 LYS A CA  
1272 C C   . LYS A 168 ? 0.12767 0.25268 0.18984 -0.02027 -0.01392 0.02419  162 LYS A C   
1273 O O   . LYS A 168 ? 0.15054 0.25231 0.19688 0.00777  0.01076  0.01711  162 LYS A O   
1274 C CB  . LYS A 168 ? 0.13852 0.28056 0.20159 -0.03987 -0.05430 0.01487  162 LYS A CB  
1275 C CG  . LYS A 168 ? 0.13243 0.30097 0.23604 -0.04793 -0.04643 0.00618  162 LYS A CG  
1276 C CD  . LYS A 168 ? 0.16292 0.33198 0.27897 -0.04874 -0.03098 -0.00524 162 LYS A CD  
1277 C CE  . LYS A 168 ? 0.21371 0.34475 0.33469 -0.04117 -0.00510 -0.00190 162 LYS A CE  
1278 N NZ  . LYS A 168 ? 0.24536 0.36484 0.36460 -0.01894 -0.02257 -0.00898 162 LYS A NZ  
1279 N N   . ILE A 169 ? 0.09888 0.24725 0.18742 -0.03089 -0.03763 0.01723  163 ILE A N   
1280 C CA  . ILE A 169 ? 0.08987 0.24703 0.17483 -0.01686 -0.03017 0.05189  163 ILE A CA  
1281 C C   . ILE A 169 ? 0.12810 0.24815 0.17434 -0.01484 -0.02140 0.04688  163 ILE A C   
1282 O O   . ILE A 169 ? 0.15381 0.24005 0.17514 -0.01291 -0.02573 0.00546  163 ILE A O   
1283 C CB  . ILE A 169 ? 0.10506 0.24148 0.16153 0.00258  0.00222  0.05879  163 ILE A CB  
1284 C CG1 . ILE A 169 ? 0.09589 0.22464 0.14157 0.01143  -0.02234 0.06928  163 ILE A CG1 
1285 C CG2 . ILE A 169 ? 0.12710 0.24988 0.19452 -0.02051 -0.00450 0.04470  163 ILE A CG2 
1286 C CD1 . ILE A 169 ? 0.13520 0.22870 0.17992 0.03662  -0.00177 0.08831  163 ILE A CD1 
1287 N N   . CYS A 170 ? 0.15166 0.24978 0.16407 -0.00583 -0.00611 0.10176  164 CYS A N   
1288 C CA  . CYS A 170 ? 0.14145 0.29048 0.18262 -0.02141 -0.00530 0.08404  164 CYS A CA  
1289 C C   . CYS A 170 ? 0.14141 0.27169 0.19064 0.00062  0.00111  0.06430  164 CYS A C   
1290 O O   . CYS A 170 ? 0.15457 0.25563 0.16598 0.01496  -0.01516 0.03618  164 CYS A O   
1291 C CB  . CYS A 170 ? 0.15619 0.33346 0.18281 -0.00095 -0.04176 0.11105  164 CYS A CB  
1292 S SG  . CYS A 170 ? 0.22476 0.39636 0.26843 0.00968  0.00549  0.11008  164 CYS A SG  
1293 N N   . ASP A 171 ? 0.17660 0.27937 0.23292 -0.01083 0.05307  0.06863  165 ASP A N   
1294 C CA  . ASP A 171 ? 0.19188 0.31273 0.26457 -0.01124 0.01587  0.08023  165 ASP A CA  
1295 C C   . ASP A 171 ? 0.21435 0.35351 0.25240 0.00582  0.01184  0.10547  165 ASP A C   
1296 O O   . ASP A 171 ? 0.24743 0.37844 0.26034 0.01080  0.01239  0.10667  165 ASP A O   
1297 C CB  . ASP A 171 ? 0.22321 0.31589 0.28526 -0.02704 0.01328  0.08846  165 ASP A CB  
1298 C CG  . ASP A 171 ? 0.27662 0.32435 0.32558 -0.05255 0.02165  0.08881  165 ASP A CG  
1299 O OD1 . ASP A 171 ? 0.27857 0.33603 0.32192 -0.05101 0.01217  0.11713  165 ASP A OD1 
1300 O OD2 . ASP A 171 ? 0.31179 0.32257 0.34666 -0.09141 0.00383  0.07594  165 ASP A OD2 
1301 N N   . PHE A 172 ? 0.20758 0.36402 0.24106 0.00401  0.02944  0.13598  166 PHE A N   
1302 C CA  . PHE A 172 ? 0.19728 0.36491 0.23986 0.00686  0.01849  0.15363  166 PHE A CA  
1303 C C   . PHE A 172 ? 0.24264 0.39340 0.26691 0.02349  0.04835  0.14705  166 PHE A C   
1304 O O   . PHE A 172 ? 0.23888 0.41143 0.21945 0.03781  0.06053  0.13475  166 PHE A O   
1305 C CB  . PHE A 172 ? 0.19110 0.35392 0.23735 0.00040  0.00317  0.12956  166 PHE A CB  
1306 C CG  . PHE A 172 ? 0.17186 0.32388 0.20006 -0.02967 -0.01488 0.08743  166 PHE A CG  
1307 C CD1 . PHE A 172 ? 0.19304 0.31522 0.21314 -0.02433 -0.00618 0.08275  166 PHE A CD1 
1308 C CD2 . PHE A 172 ? 0.17782 0.30452 0.18850 -0.04927 -0.02141 0.03605  166 PHE A CD2 
1309 C CE1 . PHE A 172 ? 0.18470 0.29390 0.20322 -0.04076 -0.00351 0.04662  166 PHE A CE1 
1310 C CE2 . PHE A 172 ? 0.13938 0.29818 0.18259 -0.06568 -0.01538 0.02038  166 PHE A CE2 
1311 C CZ  . PHE A 172 ? 0.16043 0.29389 0.18521 -0.04310 -0.03266 0.02345  166 PHE A CZ  
1312 N N   . GLY A 173 ? 0.25638 0.38487 0.30706 0.00371  0.07299  0.16510  167 GLY A N   
1313 C CA  . GLY A 173 ? 0.24906 0.38252 0.29356 0.00362  0.05916  0.16658  167 GLY A CA  
1314 C C   . GLY A 173 ? 0.26021 0.37448 0.29980 0.00537  0.05506  0.14049  167 GLY A C   
1315 O O   . GLY A 173 ? 0.25665 0.41339 0.33209 0.00811  0.04809  0.14271  167 GLY A O   
1316 N N   . LEU A 174 ? 0.27831 0.31820 0.24850 0.03901  0.04733  0.12282  168 LEU A N   
1317 C CA  . LEU A 174 ? 0.33847 0.29371 0.24111 0.01042  0.06920  0.06476  168 LEU A CA  
1318 C C   . LEU A 174 ? 0.28266 0.30093 0.20407 -0.03133 0.04735  0.04566  168 LEU A C   
1319 O O   . LEU A 174 ? 0.27049 0.30267 0.18803 -0.06074 0.03612  0.00324  168 LEU A O   
1320 C CB  . LEU A 174 ? 0.41568 0.27288 0.22830 0.03168  0.09571  0.04503  168 LEU A CB  
1321 C CG  . LEU A 174 ? 0.48075 0.25435 0.24212 0.01352  0.13369  0.01685  168 LEU A CG  
1322 C CD1 . LEU A 174 ? 0.51426 0.24741 0.25427 0.00473  0.14708  0.01759  168 LEU A CD1 
1323 C CD2 . LEU A 174 ? 0.49091 0.25073 0.25767 0.01132  0.13267  0.00650  168 LEU A CD2 
1324 N N   . ALA A 175 ? 0.22337 0.29977 0.17747 -0.05492 0.02287  0.03200  169 ALA A N   
1325 C CA  . ALA A 175 ? 0.17782 0.31286 0.19421 -0.06305 0.02083  0.03058  169 ALA A CA  
1326 C C   . ALA A 175 ? 0.19134 0.31842 0.22653 -0.03582 0.03153  0.02988  169 ALA A C   
1327 O O   . ALA A 175 ? 0.20104 0.33841 0.22779 0.00369  0.05609  0.06362  169 ALA A O   
1328 C CB  . ALA A 175 ? 0.22237 0.32540 0.18571 -0.06623 0.00534  0.03368  169 ALA A CB  
1329 N N   . ARG A 176 ? 0.17666 0.30076 0.23890 -0.03819 0.01895  0.00942  170 ARG A N   
1330 C CA  . ARG A 176 ? 0.18591 0.29676 0.26430 -0.03059 0.02770  -0.01409 170 ARG A CA  
1331 C C   . ARG A 176 ? 0.19708 0.29006 0.23716 -0.01910 0.03489  -0.05077 170 ARG A C   
1332 O O   . ARG A 176 ? 0.21405 0.28732 0.22675 0.00423  0.04670  -0.07729 170 ARG A O   
1333 C CB  . ARG A 176 ? 0.20457 0.31089 0.29883 -0.03358 0.03488  0.01279  170 ARG A CB  
1334 C CG  . ARG A 176 ? 0.24729 0.32601 0.31546 -0.03084 0.05749  0.03846  170 ARG A CG  
1335 C CD  . ARG A 176 ? 0.30232 0.34709 0.34196 -0.02650 0.07185  0.05777  170 ARG A CD  
1336 N NE  . ARG A 176 ? 0.34774 0.37227 0.34242 -0.01053 0.07371  0.06202  170 ARG A NE  
1337 C CZ  . ARG A 176 ? 0.34048 0.38631 0.34988 -0.02314 0.07502  0.06600  170 ARG A CZ  
1338 N NH1 . ARG A 176 ? 0.29592 0.39143 0.33233 -0.02018 0.06525  0.06577  170 ARG A NH1 
1339 N NH2 . ARG A 176 ? 0.31529 0.38309 0.34815 -0.05153 0.06788  0.06609  170 ARG A NH2 
1340 N N   . VAL A 177 ? 0.21512 0.30005 0.23371 -0.02270 0.05535  -0.06700 171 VAL A N   
1341 C CA  . VAL A 177 ? 0.21801 0.30607 0.23922 -0.03711 0.06068  -0.09599 171 VAL A CA  
1342 C C   . VAL A 177 ? 0.21013 0.31989 0.26597 -0.04202 0.04724  -0.09007 171 VAL A C   
1343 O O   . VAL A 177 ? 0.21384 0.32876 0.30146 -0.04239 0.06540  -0.09158 171 VAL A O   
1344 C CB  . VAL A 177 ? 0.24057 0.32882 0.24570 -0.01930 0.06978  -0.07982 171 VAL A CB  
1345 C CG1 . VAL A 177 ? 0.25634 0.32245 0.23922 -0.00627 0.05581  -0.08244 171 VAL A CG1 
1346 C CG2 . VAL A 177 ? 0.27105 0.33802 0.25593 -0.03777 0.07944  -0.07631 171 VAL A CG2 
1347 N N   . ALA A 178 ? 0.21821 0.32430 0.25509 -0.03587 0.01527  -0.09004 172 ALA A N   
1348 C CA  . ALA A 178 ? 0.22487 0.35538 0.29731 -0.01749 0.05681  -0.07049 172 ALA A CA  
1349 C C   . ALA A 178 ? 0.22565 0.36549 0.34031 -0.01121 0.03701  -0.08389 172 ALA A C   
1350 O O   . ALA A 178 ? 0.21004 0.36908 0.34381 -0.01539 0.01379  -0.10770 172 ALA A O   
1351 C CB  . ALA A 178 ? 0.22592 0.36671 0.30031 -0.01934 0.10879  -0.06200 172 ALA A CB  
1352 N N   . ASP A 179 ? 0.19465 0.36119 0.37140 -0.01611 0.02546  -0.08892 173 ASP A N   
1353 C CA  . ASP A 179 ? 0.19787 0.38824 0.41042 -0.01167 0.01724  -0.10057 173 ASP A CA  
1354 C C   . ASP A 179 ? 0.20739 0.37872 0.42378 0.00889  0.00670  -0.10524 173 ASP A C   
1355 O O   . ASP A 179 ? 0.20065 0.37807 0.41616 0.04901  0.01220  -0.10325 173 ASP A O   
1356 C CB  . ASP A 179 ? 0.22462 0.40567 0.45867 -0.03772 0.04136  -0.11376 173 ASP A CB  
1357 C CG  . ASP A 179 ? 0.23895 0.43504 0.50651 -0.04244 0.04434  -0.10618 173 ASP A CG  
1358 O OD1 . ASP A 179 ? 0.23079 0.43697 0.53943 -0.02255 0.05897  -0.11181 173 ASP A OD1 
1359 O OD2 . ASP A 179 ? 0.26035 0.45971 0.50350 -0.04138 0.04112  -0.10401 173 ASP A OD2 
1360 N N   . PRO A 180 ? 0.24000 0.37918 0.43888 -0.00429 -0.03931 -0.10234 174 PRO A N   
1361 C CA  . PRO A 180 ? 0.25137 0.38615 0.47002 -0.00407 -0.05902 -0.10545 174 PRO A CA  
1362 C C   . PRO A 180 ? 0.26642 0.39126 0.50074 0.02618  -0.07522 -0.12014 174 PRO A C   
1363 O O   . PRO A 180 ? 0.27441 0.39173 0.50508 0.04262  -0.11103 -0.11681 174 PRO A O   
1364 C CB  . PRO A 180 ? 0.26786 0.37508 0.44608 -0.03225 -0.06854 -0.10486 174 PRO A CB  
1365 C CG  . PRO A 180 ? 0.26424 0.37712 0.43918 -0.04265 -0.07246 -0.10934 174 PRO A CG  
1366 C CD  . PRO A 180 ? 0.24321 0.37800 0.43092 -0.02778 -0.07429 -0.09556 174 PRO A CD  
1367 N N   . ASP A 181 ? 0.27852 0.39408 0.54376 0.04336  -0.03617 -0.14377 175 ASP A N   
1368 C CA  . ASP A 181 ? 0.30616 0.40371 0.55057 0.05984  -0.02273 -0.17350 175 ASP A CA  
1369 C C   . ASP A 181 ? 0.27640 0.42047 0.53041 0.04290  -0.02855 -0.20155 175 ASP A C   
1370 O O   . ASP A 181 ? 0.29148 0.44626 0.55954 0.04207  -0.04040 -0.18527 175 ASP A O   
1371 C CB  . ASP A 181 ? 0.37090 0.40211 0.58839 0.07242  -0.00698 -0.16422 175 ASP A CB  
1372 C CG  . ASP A 181 ? 0.44228 0.41021 0.61152 0.08598  0.00630  -0.16053 175 ASP A CG  
1373 O OD1 . ASP A 181 ? 0.48125 0.41274 0.63197 0.07950  0.01820  -0.16326 175 ASP A OD1 
1374 O OD2 . ASP A 181 ? 0.46066 0.41212 0.60462 0.09263  -0.00257 -0.15701 175 ASP A OD2 
1375 N N   . HIS A 182 ? 0.27061 0.41572 0.49556 0.02283  -0.01115 -0.21856 176 HIS A N   
1376 C CA  . HIS A 182 ? 0.28076 0.42061 0.50952 0.00665  0.02024  -0.20345 176 HIS A CA  
1377 C C   . HIS A 182 ? 0.26855 0.39201 0.47327 0.01979  0.04049  -0.15241 176 HIS A C   
1378 O O   . HIS A 182 ? 0.30638 0.41598 0.47514 -0.00059 0.08566  -0.12602 176 HIS A O   
1379 C CB  A HIS A 182 ? 0.29673 0.42763 0.53799 -0.01435 0.04434  -0.22040 176 HIS A CB  
1380 C CB  B HIS A 182 ? 0.30230 0.44565 0.54218 0.00228  0.01764  -0.20367 176 HIS A CB  
1381 C CG  A HIS A 182 ? 0.31253 0.43564 0.55913 -0.03069 0.05872  -0.23786 176 HIS A CG  
1382 C CG  B HIS A 182 ? 0.32274 0.47123 0.56594 0.00257  0.00101  -0.20416 176 HIS A CG  
1383 N ND1 A HIS A 182 ? 0.30156 0.43336 0.55934 -0.04023 0.05009  -0.24640 176 HIS A ND1 
1384 N ND1 B HIS A 182 ? 0.33006 0.48053 0.57557 0.00286  -0.00588 -0.20453 176 HIS A ND1 
1385 C CD2 A HIS A 182 ? 0.33277 0.43840 0.57218 -0.03911 0.07359  -0.24835 176 HIS A CD2 
1386 C CD2 B HIS A 182 ? 0.32240 0.48194 0.56806 0.00079  -0.01959 -0.20592 176 HIS A CD2 
1387 C CE1 A HIS A 182 ? 0.31945 0.43613 0.56572 -0.05693 0.06057  -0.25401 176 HIS A CE1 
1388 C CE1 B HIS A 182 ? 0.33403 0.48929 0.58078 0.00276  -0.00915 -0.20441 176 HIS A CE1 
1389 N NE2 A HIS A 182 ? 0.34796 0.44495 0.58040 -0.04481 0.08163  -0.24743 176 HIS A NE2 
1390 N NE2 B HIS A 182 ? 0.32619 0.49052 0.57609 0.00209  -0.01762 -0.20689 176 HIS A NE2 
1391 N N   . ASP A 183 ? 0.21571 0.35255 0.41042 0.02511  0.02345  -0.14760 177 ASP A N   
1392 C CA  . ASP A 183 ? 0.19041 0.34730 0.39042 0.02329  0.00715  -0.12204 177 ASP A CA  
1393 C C   . ASP A 183 ? 0.19173 0.34424 0.35168 0.03450  0.01719  -0.10954 177 ASP A C   
1394 O O   . ASP A 183 ? 0.19753 0.32782 0.30735 0.02251  0.00365  -0.11892 177 ASP A O   
1395 C CB  . ASP A 183 ? 0.22916 0.33968 0.39896 0.00920  0.01749  -0.11703 177 ASP A CB  
1396 C CG  . ASP A 183 ? 0.23639 0.33537 0.40719 -0.00052 -0.00937 -0.10478 177 ASP A CG  
1397 O OD1 . ASP A 183 ? 0.22226 0.34035 0.41366 0.02232  -0.04420 -0.11623 177 ASP A OD1 
1398 O OD2 . ASP A 183 ? 0.25741 0.33711 0.42558 -0.00900 0.00284  -0.08998 177 ASP A OD2 
1399 N N   . HIS A 184 ? 0.16500 0.34873 0.36425 0.03502  -0.01116 -0.08739 178 HIS A N   
1400 C CA  . HIS A 184 ? 0.19963 0.33739 0.34617 0.02455  0.00200  -0.09567 178 HIS A CA  
1401 C C   . HIS A 184 ? 0.22202 0.32981 0.32005 0.00900  0.03067  -0.08783 178 HIS A C   
1402 O O   . HIS A 184 ? 0.24199 0.34468 0.32624 -0.01476 0.06632  -0.10900 178 HIS A O   
1403 C CB  . HIS A 184 ? 0.25089 0.36587 0.37317 0.02194  0.00524  -0.06619 178 HIS A CB  
1404 C CG  . HIS A 184 ? 0.32485 0.40106 0.41711 0.00645  0.04370  -0.05474 178 HIS A CG  
1405 N ND1 . HIS A 184 ? 0.34817 0.41679 0.43696 -0.01814 0.05041  -0.05116 178 HIS A ND1 
1406 C CD2 . HIS A 184 ? 0.38216 0.41623 0.44264 -0.00064 0.07654  -0.04491 178 HIS A CD2 
1407 C CE1 . HIS A 184 ? 0.38838 0.42417 0.45011 -0.01782 0.07759  -0.05063 178 HIS A CE1 
1408 N NE2 . HIS A 184 ? 0.40608 0.42046 0.45114 -0.01401 0.09255  -0.05501 178 HIS A NE2 
1409 N N   . THR A 185 ? 0.19775 0.30084 0.30886 -0.00909 0.00482  -0.07270 179 THR A N   
1410 C CA  . THR A 185 ? 0.23082 0.30845 0.31631 -0.01136 0.02138  -0.04878 179 THR A CA  
1411 C C   . THR A 185 ? 0.23521 0.30032 0.31871 0.00219  0.03014  -0.05224 179 THR A C   
1412 O O   . THR A 185 ? 0.22947 0.29477 0.30715 -0.00830 0.05058  -0.05670 179 THR A O   
1413 C CB  . THR A 185 ? 0.24559 0.32240 0.32028 -0.04873 0.03682  -0.03541 179 THR A CB  
1414 O OG1 . THR A 185 ? 0.31144 0.32274 0.32266 -0.07849 0.05404  -0.03956 179 THR A OG1 
1415 C CG2 . THR A 185 ? 0.18672 0.33004 0.32886 -0.03140 0.02704  -0.01172 179 THR A CG2 
1416 N N   . GLY A 186 ? 0.23999 0.31328 0.33098 -0.02423 0.01783  -0.06729 180 GLY A N   
1417 C CA  . GLY A 186 ? 0.25399 0.31965 0.32674 -0.01996 0.01567  -0.06701 180 GLY A CA  
1418 C C   . GLY A 186 ? 0.24217 0.31333 0.31486 -0.02851 0.01615  -0.05359 180 GLY A C   
1419 O O   . GLY A 186 ? 0.23078 0.31444 0.32457 0.00219  -0.01045 -0.04490 180 GLY A O   
1420 N N   . PHE A 187 ? 0.25782 0.30877 0.29574 -0.04055 0.02928  -0.03911 181 PHE A N   
1421 C CA  . PHE A 187 ? 0.25907 0.30569 0.27205 -0.05373 0.00684  -0.03321 181 PHE A CA  
1422 C C   . PHE A 187 ? 0.28878 0.34089 0.26501 -0.07890 -0.02629 -0.00044 181 PHE A C   
1423 O O   . PHE A 187 ? 0.32525 0.37045 0.28893 -0.10035 0.01813  0.01667  181 PHE A O   
1424 C CB  . PHE A 187 ? 0.21230 0.28828 0.25293 -0.03008 -0.03207 -0.04963 181 PHE A CB  
1425 C CG  . PHE A 187 ? 0.24155 0.27761 0.27440 -0.00557 0.00917  -0.00973 181 PHE A CG  
1426 C CD1 . PHE A 187 ? 0.22555 0.26501 0.28432 0.01178  -0.00361 0.01577  181 PHE A CD1 
1427 C CD2 . PHE A 187 ? 0.25091 0.27244 0.27377 -0.00043 0.01732  -0.01168 181 PHE A CD2 
1428 C CE1 . PHE A 187 ? 0.25249 0.25477 0.26734 0.00721  -0.01093 0.02076  181 PHE A CE1 
1429 C CE2 . PHE A 187 ? 0.26306 0.27059 0.27719 0.01383  -0.00088 0.00691  181 PHE A CE2 
1430 C CZ  . PHE A 187 ? 0.25579 0.26590 0.27180 0.01762  -0.02403 0.02818  181 PHE A CZ  
1431 N N   . LEU A 188 ? 0.32957 0.34617 0.26881 -0.07593 -0.02664 0.01208  182 LEU A N   
1432 C CA  . LEU A 188 ? 0.37161 0.35516 0.28187 -0.06275 -0.04681 0.01392  182 LEU A CA  
1433 C C   . LEU A 188 ? 0.34027 0.38431 0.29622 -0.06833 -0.03633 0.01830  182 LEU A C   
1434 O O   . LEU A 188 ? 0.35797 0.41768 0.30720 -0.06105 -0.04872 0.04003  182 LEU A O   
1435 C CB  . LEU A 188 ? 0.46856 0.34531 0.28989 -0.04383 -0.04738 0.02159  182 LEU A CB  
1436 C CG  . LEU A 188 ? 0.52782 0.33060 0.30914 -0.02776 -0.05905 0.01969  182 LEU A CG  
1437 C CD1 . LEU A 188 ? 0.54975 0.32546 0.31754 -0.03907 -0.07269 0.01982  182 LEU A CD1 
1438 C CD2 . LEU A 188 ? 0.54506 0.31747 0.29930 0.00591  -0.04168 0.02163  182 LEU A CD2 
1439 N N   A THR A 189 ? 0.28122 0.36795 0.24803 -0.08308 -0.05803 0.00001  183 THR A N   
1440 N N   B THR A 189 ? 0.34637 0.39888 0.31502 -0.05876 -0.03752 -0.00190 183 THR A N   
1441 C CA  A THR A 189 ? 0.24260 0.35107 0.23365 -0.08512 -0.05288 0.00639  183 THR A CA  
1442 C CA  B THR A 189 ? 0.36251 0.41723 0.35425 -0.03491 -0.04562 0.00515  183 THR A CA  
1443 C C   A THR A 189 ? 0.20958 0.34224 0.22639 -0.08482 -0.07740 0.02103  183 THR A C   
1444 C C   B THR A 189 ? 0.34668 0.39954 0.36249 -0.02762 -0.05896 0.02476  183 THR A C   
1445 O O   A THR A 189 ? 0.18539 0.33293 0.22878 -0.09376 -0.08039 0.02509  183 THR A O   
1446 O O   B THR A 189 ? 0.34491 0.40436 0.35952 -0.02692 -0.08355 0.04476  183 THR A O   
1447 C CB  A THR A 189 ? 0.20892 0.33779 0.23166 -0.09334 -0.04498 -0.01108 183 THR A CB  
1448 C CB  B THR A 189 ? 0.38976 0.44751 0.38728 -0.01674 -0.01374 -0.01539 183 THR A CB  
1449 O OG1 A THR A 189 ? 0.17615 0.34345 0.25785 -0.10713 -0.04263 -0.00964 183 THR A OG1 
1450 O OG1 B THR A 189 ? 0.40898 0.46249 0.41408 -0.00553 0.00597  -0.03056 183 THR A OG1 
1451 C CG2 A THR A 189 ? 0.18205 0.33073 0.20523 -0.09297 -0.06818 -0.01355 183 THR A CG2 
1452 C CG2 B THR A 189 ? 0.40327 0.45892 0.40372 -0.02110 -0.00295 -0.00783 183 THR A CG2 
1453 N N   A GLU A 190 ? 0.20107 0.34102 0.23676 -0.08837 -0.07667 0.03152  184 GLU A N   
1454 N N   B GLU A 190 ? 0.32131 0.37693 0.37239 -0.02966 -0.04893 0.02673  184 GLU A N   
1455 C CA  A GLU A 190 ? 0.19451 0.34268 0.25086 -0.09424 -0.04105 0.03553  184 GLU A CA  
1456 C CA  B GLU A 190 ? 0.30480 0.37116 0.38658 -0.03122 -0.05505 0.02814  184 GLU A CA  
1457 C C   A GLU A 190 ? 0.17738 0.33684 0.25153 -0.08392 -0.01497 0.02346  184 GLU A C   
1458 C C   B GLU A 190 ? 0.32594 0.37091 0.39082 -0.01560 -0.05882 0.04154  184 GLU A C   
1459 O O   A GLU A 190 ? 0.18588 0.34398 0.26745 -0.08757 0.02149  0.02503  184 GLU A O   
1460 O O   B GLU A 190 ? 0.32178 0.37625 0.39021 0.00136  -0.08255 0.06878  184 GLU A O   
1461 C CB  A GLU A 190 ? 0.25090 0.35478 0.26472 -0.10324 -0.01514 0.04696  184 GLU A CB  
1462 C CB  B GLU A 190 ? 0.29135 0.37009 0.41705 -0.03570 -0.03270 -0.00435 184 GLU A CB  
1463 C CG  A GLU A 190 ? 0.29334 0.37149 0.29518 -0.10899 0.00148  0.04754  184 GLU A CG  
1464 C CG  B GLU A 190 ? 0.31209 0.37564 0.41591 -0.03243 -0.03495 -0.00477 184 GLU A CG  
1465 C CD  A GLU A 190 ? 0.35457 0.38935 0.31770 -0.10291 0.03049  0.05245  184 GLU A CD  
1466 C CD  B GLU A 190 ? 0.30824 0.38653 0.42002 -0.01650 -0.00711 -0.00505 184 GLU A CD  
1467 O OE1 A GLU A 190 ? 0.37686 0.39878 0.30205 -0.09184 0.03848  0.06292  184 GLU A OE1 
1468 O OE1 B GLU A 190 ? 0.27445 0.37590 0.40444 -0.00072 -0.00898 0.00586  184 GLU A OE1 
1469 O OE2 A GLU A 190 ? 0.38660 0.40570 0.34846 -0.08844 0.05491  0.05615  184 GLU A OE2 
1470 O OE2 B GLU A 190 ? 0.34595 0.40653 0.44430 -0.02317 0.00804  -0.01409 184 GLU A OE2 
1471 N N   A TYR A 191 ? 0.15966 0.33365 0.23593 -0.06689 -0.04390 0.01398  185 TYR A N   
1472 N N   B TYR A 191 ? 0.33686 0.36982 0.39170 -0.02422 -0.06326 0.02281  185 TYR A N   
1473 C CA  A TYR A 191 ? 0.16126 0.32262 0.24385 -0.05617 -0.04625 0.02589  185 TYR A CA  
1474 C CA  B TYR A 191 ? 0.36793 0.37791 0.40751 -0.01637 -0.03530 0.00215  185 TYR A CA  
1475 C C   A TYR A 191 ? 0.18845 0.32644 0.26939 -0.03895 -0.03270 0.03685  185 TYR A C   
1476 C C   B TYR A 191 ? 0.34315 0.35936 0.38992 -0.01488 -0.02576 -0.01378 185 TYR A C   
1477 O O   A TYR A 191 ? 0.21987 0.32928 0.28500 -0.01922 -0.01613 0.03065  185 TYR A O   
1478 O O   B TYR A 191 ? 0.35262 0.35500 0.39736 -0.01044 -0.00994 -0.01562 185 TYR A O   
1479 C CB  A TYR A 191 ? 0.13569 0.31212 0.22418 -0.06260 -0.06930 0.02093  185 TYR A CB  
1480 C CB  B TYR A 191 ? 0.42599 0.40518 0.42472 -0.00228 -0.02423 -0.00974 185 TYR A CB  
1481 C CG  A TYR A 191 ? 0.12406 0.30121 0.22032 -0.06464 -0.05715 0.03671  185 TYR A CG  
1482 C CG  B TYR A 191 ? 0.47286 0.43251 0.43863 0.00923  -0.01446 -0.03003 185 TYR A CG  
1483 C CD1 A TYR A 191 ? 0.11558 0.29633 0.21629 -0.05515 -0.05454 0.03877  185 TYR A CD1 
1484 C CD1 B TYR A 191 ? 0.49710 0.44290 0.44321 0.01480  -0.01192 -0.03892 185 TYR A CD1 
1485 C CD2 A TYR A 191 ? 0.13388 0.28888 0.19939 -0.06668 -0.06460 0.03012  185 TYR A CD2 
1486 C CD2 B TYR A 191 ? 0.48921 0.44447 0.44716 0.00972  -0.01343 -0.04243 185 TYR A CD2 
1487 C CE1 A TYR A 191 ? 0.13420 0.30901 0.20843 -0.04230 -0.04092 0.04870  185 TYR A CE1 
1488 C CE1 B TYR A 191 ? 0.49926 0.45054 0.44206 0.01115  -0.02642 -0.05163 185 TYR A CE1 
1489 C CE2 A TYR A 191 ? 0.15180 0.30838 0.21257 -0.06038 -0.02974 0.05479  185 TYR A CE2 
1490 C CE2 B TYR A 191 ? 0.49773 0.44873 0.43693 0.01723  -0.02132 -0.05292 185 TYR A CE2 
1491 C CZ  A TYR A 191 ? 0.14664 0.31029 0.18690 -0.04848 -0.03136 0.05955  185 TYR A CZ  
1492 C CZ  B TYR A 191 ? 0.50627 0.45355 0.44094 0.01612  -0.02751 -0.05745 185 TYR A CZ  
1493 O OH  A TYR A 191 ? 0.17613 0.31997 0.17012 -0.01986 -0.01099 0.07661  185 TYR A OH  
1494 O OH  B TYR A 191 ? 0.50434 0.45094 0.43021 0.01726  -0.05038 -0.05253 185 TYR A OH  
1495 N N   A VAL A 192 ? 0.17910 0.32450 0.27500 -0.04381 -0.04164 0.04794  186 VAL A N   
1496 N N   B VAL A 192 ? 0.30252 0.34278 0.36070 -0.02381 -0.03695 -0.03598 186 VAL A N   
1497 C CA  A VAL A 192 ? 0.17032 0.32416 0.28071 -0.04796 -0.04849 0.03499  186 VAL A CA  
1498 C CA  B VAL A 192 ? 0.25098 0.33115 0.34434 -0.02477 -0.04315 -0.04555 186 VAL A CA  
1499 C C   A VAL A 192 ? 0.13863 0.30108 0.28602 -0.04374 -0.05833 0.03863  186 VAL A C   
1500 C C   B VAL A 192 ? 0.24900 0.31442 0.34565 -0.01329 -0.02672 -0.03496 186 VAL A C   
1501 O O   A VAL A 192 ? 0.15158 0.30842 0.29526 -0.06859 -0.05298 0.04549  186 VAL A O   
1502 O O   B VAL A 192 ? 0.26576 0.31468 0.34824 -0.01875 0.00633  -0.05343 186 VAL A O   
1503 C CB  A VAL A 192 ? 0.18287 0.34080 0.28622 -0.04862 -0.05187 0.02180  186 VAL A CB  
1504 C CB  B VAL A 192 ? 0.23529 0.33776 0.35815 -0.03502 -0.04143 -0.06081 186 VAL A CB  
1505 C CG1 A VAL A 192 ? 0.18108 0.34249 0.29120 -0.04480 -0.05444 0.02846  186 VAL A CG1 
1506 C CG1 B VAL A 192 ? 0.21911 0.34432 0.36416 -0.03771 -0.04714 -0.05459 186 VAL A CG1 
1507 C CG2 A VAL A 192 ? 0.25195 0.35508 0.31421 -0.02691 -0.00142 0.01529  186 VAL A CG2 
1508 C CG2 B VAL A 192 ? 0.24556 0.34363 0.36934 -0.01211 -0.02853 -0.05244 186 VAL A CG2 
1509 N N   A ALA A 193 ? 0.15253 0.27897 0.28974 -0.00779 -0.06066 0.03759  187 ALA A N   
1510 N N   B ALA A 193 ? 0.23759 0.28972 0.33999 0.01273  -0.04092 0.00071  187 ALA A N   
1511 C CA  A ALA A 193 ? 0.14658 0.26078 0.29544 0.00706  -0.05998 0.04998  187 ALA A CA  
1512 C CA  B ALA A 193 ? 0.23293 0.26192 0.34113 0.02373  -0.07727 0.01561  187 ALA A CA  
1513 C C   A ALA A 193 ? 0.17821 0.25900 0.32457 0.01210  -0.03611 0.02245  187 ALA A C   
1514 C C   B ALA A 193 ? 0.21813 0.25555 0.35670 0.03696  -0.05691 -0.01171 187 ALA A C   
1515 O O   A ALA A 193 ? 0.21205 0.25042 0.32715 0.03132  0.01221  0.05456  187 ALA A O   
1516 O O   B ALA A 193 ? 0.24100 0.22783 0.37143 0.04274  0.00823  0.00200  187 ALA A O   
1517 C CB  A ALA A 193 ? 0.15050 0.24545 0.28297 0.00748  -0.04984 0.07276  187 ALA A CB  
1518 C CB  B ALA A 193 ? 0.22916 0.24819 0.33851 0.02527  -0.13614 0.02655  187 ALA A CB  
1519 N N   . THR A 194 ? 0.20341 0.27040 0.37998 0.00084  -0.04718 -0.03492 188 THR A N   
1520 C CA  . THR A 194 ? 0.21384 0.24267 0.31905 -0.01844 -0.05617 -0.02744 188 THR A CA  
1521 C C   . THR A 194 ? 0.25923 0.23825 0.31047 -0.04820 -0.09075 -0.00533 188 THR A C   
1522 O O   . THR A 194 ? 0.30315 0.26630 0.28311 -0.04381 -0.09728 0.00941  188 THR A O   
1523 C CB  . THR A 194 ? 0.18113 0.22473 0.26916 -0.01614 -0.06415 -0.01876 188 THR A CB  
1524 O OG1 . THR A 194 ? 0.20303 0.22694 0.23485 -0.03500 -0.03952 0.00326  188 THR A OG1 
1525 C CG2 . THR A 194 ? 0.16578 0.21780 0.30667 0.00803  -0.02652 -0.00281 188 THR A CG2 
1526 N N   . ARG A 195 ? 0.25696 0.20282 0.29811 -0.06163 -0.11833 -0.00085 189 ARG A N   
1527 C CA  . ARG A 195 ? 0.29437 0.18016 0.28389 -0.08301 -0.12793 0.03396  189 ARG A CA  
1528 C C   . ARG A 195 ? 0.25417 0.18487 0.28331 -0.04633 -0.13841 0.06581  189 ARG A C   
1529 O O   . ARG A 195 ? 0.29266 0.21338 0.28043 -0.03097 -0.10453 0.07547  189 ARG A O   
1530 C CB  A ARG A 195 ? 0.31740 0.17461 0.26129 -0.10428 -0.12660 0.05230  189 ARG A CB  
1531 C CB  B ARG A 195 ? 0.32355 0.19030 0.31893 -0.08875 -0.12259 0.04240  189 ARG A CB  
1532 C CG  A ARG A 195 ? 0.33650 0.18653 0.23639 -0.11798 -0.11900 0.05202  189 ARG A CG  
1533 C CG  B ARG A 195 ? 0.33381 0.20810 0.34212 -0.09302 -0.13316 0.03737  189 ARG A CG  
1534 C CD  A ARG A 195 ? 0.36180 0.18844 0.21156 -0.12628 -0.10284 0.04290  189 ARG A CD  
1535 C CD  B ARG A 195 ? 0.35314 0.22631 0.38103 -0.08691 -0.10818 0.02177  189 ARG A CD  
1536 N NE  A ARG A 195 ? 0.38906 0.20620 0.22210 -0.13624 -0.11999 0.05280  189 ARG A NE  
1537 N NE  B ARG A 195 ? 0.39061 0.24010 0.42011 -0.10555 -0.05661 0.00170  189 ARG A NE  
1538 C CZ  A ARG A 195 ? 0.38958 0.20682 0.24559 -0.13775 -0.10941 0.06742  189 ARG A CZ  
1539 C CZ  B ARG A 195 ? 0.41509 0.24779 0.46556 -0.10037 -0.01883 -0.00662 189 ARG A CZ  
1540 N NH1 A ARG A 195 ? 0.41149 0.20834 0.28703 -0.14224 -0.08955 0.05880  189 ARG A NH1 
1541 N NH1 B ARG A 195 ? 0.41153 0.24572 0.47100 -0.10935 -0.01580 -0.02079 189 ARG A NH1 
1542 N NH2 A ARG A 195 ? 0.39660 0.22049 0.27236 -0.14180 -0.13252 0.08041  189 ARG A NH2 
1543 N NH2 B ARG A 195 ? 0.41688 0.24816 0.48149 -0.08690 -0.01999 -0.00497 189 ARG A NH2 
1544 N N   . TRP A 196 ? 0.26917 0.18163 0.29501 -0.04137 -0.10046 0.04539  190 TRP A N   
1545 C CA  . TRP A 196 ? 0.23476 0.17118 0.31226 -0.01530 -0.10303 0.02728  190 TRP A CA  
1546 C C   . TRP A 196 ? 0.20449 0.16572 0.27939 0.00171  -0.08258 0.01140  190 TRP A C   
1547 O O   . TRP A 196 ? 0.19749 0.15299 0.24864 0.00926  -0.06161 -0.00493 190 TRP A O   
1548 C CB  . TRP A 196 ? 0.24005 0.17225 0.34768 -0.01303 -0.11991 0.00003  190 TRP A CB  
1549 C CG  . TRP A 196 ? 0.25840 0.19309 0.37804 -0.00146 -0.14082 0.01150  190 TRP A CG  
1550 C CD1 . TRP A 196 ? 0.30011 0.20484 0.39812 0.01515  -0.13555 0.00196  190 TRP A CD1 
1551 C CD2 . TRP A 196 ? 0.28720 0.21384 0.42194 0.01004  -0.11387 0.02691  190 TRP A CD2 
1552 N NE1 . TRP A 196 ? 0.30299 0.22516 0.42890 0.01410  -0.13183 0.01536  190 TRP A NE1 
1553 C CE2 . TRP A 196 ? 0.29347 0.23040 0.44231 0.02228  -0.12804 0.01927  190 TRP A CE2 
1554 C CE3 . TRP A 196 ? 0.30274 0.22667 0.45919 0.01781  -0.07691 0.03823  190 TRP A CE3 
1555 C CZ2 . TRP A 196 ? 0.28284 0.25469 0.47698 0.02841  -0.11017 0.01538  190 TRP A CZ2 
1556 C CZ3 . TRP A 196 ? 0.31496 0.23476 0.49016 0.02947  -0.05200 0.03262  190 TRP A CZ3 
1557 C CH2 . TRP A 196 ? 0.30305 0.24440 0.49877 0.02615  -0.06784 0.01122  190 TRP A CH2 
1558 N N   . TYR A 197 ? 0.19324 0.16696 0.25933 0.00858  -0.05175 0.01086  191 TYR A N   
1559 C CA  . TYR A 197 ? 0.16871 0.17723 0.23779 -0.01969 -0.04197 0.00299  191 TYR A CA  
1560 C C   . TYR A 197 ? 0.18328 0.18706 0.23076 -0.02618 -0.02783 0.02127  191 TYR A C   
1561 O O   . TYR A 197 ? 0.19269 0.17626 0.21744 -0.04393 -0.00224 0.00061  191 TYR A O   
1562 C CB  . TYR A 197 ? 0.16245 0.17885 0.21300 -0.03041 -0.05178 -0.00298 191 TYR A CB  
1563 C CG  . TYR A 197 ? 0.20304 0.19184 0.24079 -0.00720 -0.02694 0.01873  191 TYR A CG  
1564 C CD1 . TYR A 197 ? 0.19860 0.20578 0.26216 0.00408  -0.01640 0.02155  191 TYR A CD1 
1565 C CD2 . TYR A 197 ? 0.20796 0.20044 0.22990 0.00312  -0.07656 0.01304  191 TYR A CD2 
1566 C CE1 . TYR A 197 ? 0.16125 0.19956 0.23977 0.01340  -0.05551 0.01818  191 TYR A CE1 
1567 C CE2 . TYR A 197 ? 0.20071 0.21522 0.25999 -0.00256 -0.06156 0.01793  191 TYR A CE2 
1568 C CZ  . TYR A 197 ? 0.18677 0.20319 0.24869 0.01835  -0.05048 0.01836  191 TYR A CZ  
1569 O OH  . TYR A 197 ? 0.23109 0.19251 0.26692 0.02477  -0.03444 0.01008  191 TYR A OH  
1570 N N   . ARG A 198 ? 0.18913 0.21078 0.22888 -0.04119 -0.04327 0.04398  192 ARG A N   
1571 C CA  . ARG A 198 ? 0.20799 0.22678 0.22816 -0.04537 -0.00941 0.02296  192 ARG A CA  
1572 C C   . ARG A 198 ? 0.15865 0.23454 0.21000 -0.03492 -0.01129 0.01125  192 ARG A C   
1573 O O   . ARG A 198 ? 0.14828 0.26287 0.21901 -0.03585 -0.00078 -0.01826 192 ARG A O   
1574 C CB  . ARG A 198 ? 0.28994 0.21850 0.25013 -0.07441 0.03636  0.01731  192 ARG A CB  
1575 C CG  . ARG A 198 ? 0.29392 0.22029 0.25323 -0.08717 0.03511  0.00419  192 ARG A CG  
1576 C CD  . ARG A 198 ? 0.27052 0.20930 0.23677 -0.07277 0.01655  0.00208  192 ARG A CD  
1577 N NE  . ARG A 198 ? 0.22600 0.22114 0.20456 -0.04678 -0.02789 0.00317  192 ARG A NE  
1578 C CZ  . ARG A 198 ? 0.31105 0.21947 0.19164 -0.04221 -0.04566 0.00802  192 ARG A CZ  
1579 N NH1 . ARG A 198 ? 0.37001 0.20949 0.17431 -0.05764 -0.04854 0.00309  192 ARG A NH1 
1580 N NH2 . ARG A 198 ? 0.34601 0.23198 0.19240 -0.02835 -0.03087 -0.00634 192 ARG A NH2 
1581 N N   . ALA A 199 ? 0.14008 0.20742 0.19298 -0.01647 -0.02363 0.00219  193 ALA A N   
1582 C CA  . ALA A 199 ? 0.14313 0.21009 0.19517 -0.02212 -0.02119 -0.01266 193 ALA A CA  
1583 C C   . ALA A 199 ? 0.13950 0.23957 0.17984 -0.01443 -0.00468 -0.00981 193 ALA A C   
1584 O O   . ALA A 199 ? 0.18097 0.24721 0.19875 -0.01604 0.02887  -0.02019 193 ALA A O   
1585 C CB  . ALA A 199 ? 0.16039 0.21073 0.22865 -0.01799 -0.00315 -0.02742 193 ALA A CB  
1586 N N   . PRO A 200 ? 0.13364 0.25304 0.16223 -0.01851 0.01582  -0.01787 194 PRO A N   
1587 C CA  . PRO A 200 ? 0.11147 0.26343 0.16307 -0.00597 -0.00891 -0.01151 194 PRO A CA  
1588 C C   . PRO A 200 ? 0.13134 0.26404 0.18177 -0.03056 0.03103  -0.01013 194 PRO A C   
1589 O O   . PRO A 200 ? 0.11466 0.26697 0.19534 -0.03571 0.02060  0.00706  194 PRO A O   
1590 C CB  . PRO A 200 ? 0.16055 0.28005 0.18083 -0.05023 0.02351  -0.02537 194 PRO A CB  
1591 C CG  . PRO A 200 ? 0.17761 0.27397 0.16271 -0.05598 -0.00140 -0.04292 194 PRO A CG  
1592 C CD  . PRO A 200 ? 0.13139 0.27310 0.14212 -0.02804 -0.01115 -0.00624 194 PRO A CD  
1593 N N   . GLU A 201 ? 0.15460 0.26551 0.16701 -0.02526 0.03297  -0.04102 195 GLU A N   
1594 C CA  . GLU A 201 ? 0.18478 0.27559 0.18446 -0.03407 0.02731  -0.01593 195 GLU A CA  
1595 C C   . GLU A 201 ? 0.20822 0.29033 0.18712 -0.04884 0.01981  -0.02181 195 GLU A C   
1596 O O   . GLU A 201 ? 0.17793 0.29726 0.19246 -0.06783 0.03029  -0.00416 195 GLU A O   
1597 C CB  . GLU A 201 ? 0.14733 0.26084 0.18529 -0.03508 -0.01351 -0.01150 195 GLU A CB  
1598 C CG  . GLU A 201 ? 0.13883 0.27234 0.17784 -0.03696 -0.02663 0.01037  195 GLU A CG  
1599 C CD  . GLU A 201 ? 0.16082 0.28705 0.18041 -0.02969 0.01507  0.00371  195 GLU A CD  
1600 O OE1 . GLU A 201 ? 0.17540 0.28216 0.18418 -0.05458 0.00488  -0.02610 195 GLU A OE1 
1601 O OE2 . GLU A 201 ? 0.15479 0.30394 0.17895 -0.01348 0.02630  0.01675  195 GLU A OE2 
1602 N N   . ILE A 202 ? 0.17709 0.28451 0.17624 -0.02689 0.00177  -0.02644 196 ILE A N   
1603 C CA  . ILE A 202 ? 0.15399 0.29939 0.18043 -0.02803 -0.00590 -0.00739 196 ILE A CA  
1604 C C   . ILE A 202 ? 0.17911 0.30635 0.19707 -0.03421 0.00396  -0.00359 196 ILE A C   
1605 O O   . ILE A 202 ? 0.17830 0.32729 0.23192 -0.04122 0.00658  0.00487  196 ILE A O   
1606 C CB  . ILE A 202 ? 0.16583 0.29734 0.19369 -0.01352 0.01696  -0.01175 196 ILE A CB  
1607 C CG1 . ILE A 202 ? 0.14405 0.30140 0.19524 -0.00563 0.02552  -0.04108 196 ILE A CG1 
1608 C CG2 . ILE A 202 ? 0.20200 0.30622 0.22574 -0.02495 0.06334  -0.00084 196 ILE A CG2 
1609 C CD1 . ILE A 202 ? 0.16287 0.31312 0.23336 0.02108  0.00856  -0.06017 196 ILE A CD1 
1610 N N   . MET A 203 ? 0.19391 0.29050 0.22620 -0.02443 -0.01653 -0.01947 197 MET A N   
1611 C CA  . MET A 203 ? 0.17350 0.30850 0.24864 -0.00686 0.00256  -0.01786 197 MET A CA  
1612 C C   . MET A 203 ? 0.16977 0.32008 0.25798 -0.01617 -0.00558 -0.01612 197 MET A C   
1613 O O   . MET A 203 ? 0.15458 0.34661 0.29746 -0.02895 -0.02414 0.01464  197 MET A O   
1614 C CB  . MET A 203 ? 0.19980 0.29922 0.25791 0.01435  -0.00654 -0.01630 197 MET A CB  
1615 C CG  . MET A 203 ? 0.18400 0.31360 0.24087 -0.02633 -0.03201 -0.01867 197 MET A CG  
1616 S SD  . MET A 203 ? 0.23969 0.33554 0.24205 -0.01772 -0.00096 -0.03413 197 MET A SD  
1617 C CE  . MET A 203 ? 0.26808 0.32734 0.23873 -0.00412 0.05053  -0.03413 197 MET A CE  
1618 N N   . LEU A 204 ? 0.15537 0.30842 0.22154 -0.00452 0.01438  -0.00623 198 LEU A N   
1619 C CA  . LEU A 204 ? 0.13173 0.32069 0.20418 -0.03488 0.02425  -0.02457 198 LEU A CA  
1620 C C   . LEU A 204 ? 0.12667 0.36228 0.19815 -0.04370 -0.00983 -0.04145 198 LEU A C   
1621 O O   . LEU A 204 ? 0.14883 0.39316 0.20646 -0.04920 -0.02580 -0.02874 198 LEU A O   
1622 C CB  . LEU A 204 ? 0.17614 0.32520 0.19850 -0.01508 0.00297  -0.01216 198 LEU A CB  
1623 C CG  . LEU A 204 ? 0.18698 0.32600 0.19873 -0.03424 0.01584  -0.01374 198 LEU A CG  
1624 C CD1 . LEU A 204 ? 0.17596 0.33026 0.18362 -0.04877 0.02942  -0.00741 198 LEU A CD1 
1625 C CD2 . LEU A 204 ? 0.20730 0.33242 0.19994 -0.03671 0.00634  -0.03252 198 LEU A CD2 
1626 N N   . ASN A 205 ? 0.13336 0.35809 0.19467 -0.02736 -0.00625 -0.05267 199 ASN A N   
1627 C CA  . ASN A 205 ? 0.16726 0.34497 0.21868 0.00342  -0.00456 -0.04140 199 ASN A CA  
1628 C C   . ASN A 205 ? 0.13945 0.33765 0.24439 0.00028  -0.01310 -0.04823 199 ASN A C   
1629 O O   . ASN A 205 ? 0.13774 0.32593 0.26030 0.00347  -0.00034 -0.07118 199 ASN A O   
1630 C CB  . ASN A 205 ? 0.19354 0.34789 0.20548 0.00326  -0.00308 -0.02184 199 ASN A CB  
1631 C CG  . ASN A 205 ? 0.20030 0.34627 0.18915 0.00399  -0.00648 -0.01377 199 ASN A CG  
1632 O OD1 . ASN A 205 ? 0.23151 0.35081 0.20709 0.01487  0.00162  0.01187  199 ASN A OD1 
1633 N ND2 . ASN A 205 ? 0.21015 0.34612 0.19114 -0.01506 0.00388  -0.02664 199 ASN A ND2 
1634 N N   . SER A 206 ? 0.11936 0.33986 0.23246 0.00350  -0.04049 -0.04975 200 SER A N   
1635 C CA  . SER A 206 ? 0.15141 0.34785 0.23369 -0.01403 -0.01078 -0.06058 200 SER A CA  
1636 C C   . SER A 206 ? 0.16317 0.36247 0.24467 -0.01403 -0.00200 -0.05911 200 SER A C   
1637 O O   . SER A 206 ? 0.13355 0.37049 0.25775 -0.00107 -0.00213 -0.05697 200 SER A O   
1638 C CB  . SER A 206 ? 0.16437 0.33147 0.22514 -0.02395 -0.00554 -0.06726 200 SER A CB  
1639 O OG  . SER A 206 ? 0.18443 0.32536 0.21832 0.01145  -0.01736 -0.05131 200 SER A OG  
1640 N N   . LYS A 207 ? 0.16272 0.37038 0.22305 -0.02520 -0.02039 -0.07435 201 LYS A N   
1641 C CA  . LYS A 207 ? 0.17654 0.37987 0.23067 -0.03888 -0.00129 -0.07178 201 LYS A CA  
1642 C C   . LYS A 207 ? 0.20286 0.37204 0.23510 -0.00252 -0.01875 -0.05471 201 LYS A C   
1643 O O   . LYS A 207 ? 0.21667 0.36600 0.27491 0.01030  -0.02374 -0.05768 201 LYS A O   
1644 C CB  . LYS A 207 ? 0.18101 0.40524 0.21871 -0.06660 0.00962  -0.09354 201 LYS A CB  
1645 C CG  . LYS A 207 ? 0.24325 0.43712 0.25170 -0.06104 0.03036  -0.09561 201 LYS A CG  
1646 C CD  . LYS A 207 ? 0.33169 0.45679 0.30669 -0.04857 0.08228  -0.09650 201 LYS A CD  
1647 C CE  . LYS A 207 ? 0.37343 0.46135 0.33314 -0.04589 0.11019  -0.09039 201 LYS A CE  
1648 N NZ  . LYS A 207 ? 0.39785 0.46860 0.35193 -0.03953 0.12084  -0.08982 201 LYS A NZ  
1649 N N   . GLY A 208 ? 0.17686 0.35860 0.21292 0.01823  -0.03182 -0.04030 202 GLY A N   
1650 C CA  . GLY A 208 ? 0.21480 0.35926 0.22846 0.01466  0.00237  -0.05817 202 GLY A CA  
1651 C C   . GLY A 208 ? 0.18999 0.35912 0.19630 0.01611  0.00610  -0.05811 202 GLY A C   
1652 O O   . GLY A 208 ? 0.19219 0.36884 0.22443 0.03497  -0.03169 -0.04350 202 GLY A O   
1653 N N   . TYR A 209 ? 0.15980 0.34785 0.17985 0.01264  0.04737  -0.06116 203 TYR A N   
1654 C CA  . TYR A 209 ? 0.14876 0.34345 0.18082 -0.01122 0.06106  -0.05979 203 TYR A CA  
1655 C C   . TYR A 209 ? 0.16705 0.34917 0.20503 -0.01605 0.04037  -0.06053 203 TYR A C   
1656 O O   . TYR A 209 ? 0.18577 0.33649 0.22289 -0.01681 0.02379  -0.05403 203 TYR A O   
1657 C CB  . TYR A 209 ? 0.16276 0.33629 0.19022 0.00001  0.08336  -0.04211 203 TYR A CB  
1658 C CG  . TYR A 209 ? 0.22294 0.36544 0.18277 -0.02263 0.09206  -0.06071 203 TYR A CG  
1659 C CD1 . TYR A 209 ? 0.26819 0.37455 0.18252 -0.04271 0.08183  -0.05856 203 TYR A CD1 
1660 C CD2 . TYR A 209 ? 0.26438 0.37482 0.20152 -0.03841 0.10943  -0.04621 203 TYR A CD2 
1661 C CE1 . TYR A 209 ? 0.28936 0.37861 0.21791 -0.06253 0.07669  -0.06392 203 TYR A CE1 
1662 C CE2 . TYR A 209 ? 0.31630 0.38605 0.25162 -0.05519 0.09770  -0.03811 203 TYR A CE2 
1663 C CZ  . TYR A 209 ? 0.33213 0.39206 0.25588 -0.07251 0.08853  -0.04434 203 TYR A CZ  
1664 O OH  . TYR A 209 ? 0.38336 0.40873 0.28883 -0.08276 0.11603  -0.05112 203 TYR A OH  
1665 N N   . THR A 210 ? 0.15178 0.35592 0.20591 -0.02107 0.03510  -0.05696 204 THR A N   
1666 C CA  . THR A 210 ? 0.17555 0.35649 0.25535 -0.00174 0.01286  -0.03047 204 THR A CA  
1667 C C   . THR A 210 ? 0.17713 0.31563 0.24120 -0.00391 0.02656  -0.02868 204 THR A C   
1668 O O   . THR A 210 ? 0.19740 0.30437 0.21767 0.00244  0.01570  -0.01468 204 THR A O   
1669 C CB  . THR A 210 ? 0.20414 0.39989 0.31365 0.01492  0.00127  -0.01526 204 THR A CB  
1670 O OG1 . THR A 210 ? 0.25309 0.42208 0.32767 0.00563  -0.03088 -0.01332 204 THR A OG1 
1671 C CG2 . THR A 210 ? 0.18736 0.41770 0.32562 0.03169  -0.02408 0.00880  204 THR A CG2 
1672 N N   . LYS A 211 ? 0.12366 0.27521 0.22265 -0.01905 -0.00672 -0.04579 205 LYS A N   
1673 C CA  . LYS A 211 ? 0.12829 0.25324 0.21034 -0.01318 -0.02246 -0.05617 205 LYS A CA  
1674 C C   . LYS A 211 ? 0.11519 0.25663 0.18159 0.01010  -0.01116 -0.02865 205 LYS A C   
1675 O O   . LYS A 211 ? 0.11260 0.24143 0.20106 0.01384  0.01122  -0.02740 205 LYS A O   
1676 C CB  . LYS A 211 ? 0.17767 0.24504 0.20775 -0.00491 -0.02095 -0.06729 205 LYS A CB  
1677 C CG  . LYS A 211 ? 0.19796 0.24374 0.19213 0.02241  -0.02195 -0.06532 205 LYS A CG  
1678 C CD  . LYS A 211 ? 0.21319 0.24499 0.20218 0.04704  -0.02294 -0.05095 205 LYS A CD  
1679 C CE  . LYS A 211 ? 0.23043 0.25087 0.22940 0.04239  0.00306  -0.05643 205 LYS A CE  
1680 N NZ  . LYS A 211 ? 0.22865 0.25872 0.23009 0.04569  0.00035  -0.04424 205 LYS A NZ  
1681 N N   . SER A 212 ? 0.15305 0.26295 0.17093 0.00575  -0.02113 -0.03452 206 SER A N   
1682 C CA  . SER A 212 ? 0.13374 0.25620 0.18123 0.01769  -0.01444 -0.02000 206 SER A CA  
1683 C C   . SER A 212 ? 0.13248 0.26231 0.18657 -0.00091 -0.02416 0.00900  206 SER A C   
1684 O O   . SER A 212 ? 0.14382 0.26042 0.18535 -0.00474 -0.01707 0.01063  206 SER A O   
1685 C CB  . SER A 212 ? 0.17209 0.26903 0.21186 0.00722  0.02515  -0.02988 206 SER A CB  
1686 O OG  . SER A 212 ? 0.17775 0.29185 0.22208 0.00563  -0.02452 -0.03941 206 SER A OG  
1687 N N   . ILE A 213 ? 0.15467 0.25880 0.20701 -0.00962 -0.02505 0.04158  207 ILE A N   
1688 C CA  . ILE A 213 ? 0.12720 0.26417 0.21374 -0.03855 -0.01473 0.04801  207 ILE A CA  
1689 C C   . ILE A 213 ? 0.10134 0.24914 0.20221 -0.03753 -0.01242 0.02311  207 ILE A C   
1690 O O   . ILE A 213 ? 0.14056 0.25436 0.20783 -0.02774 -0.00706 0.02384  207 ILE A O   
1691 C CB  . ILE A 213 ? 0.20118 0.28652 0.24133 -0.08704 0.01439  0.01922  207 ILE A CB  
1692 C CG1 . ILE A 213 ? 0.28022 0.32701 0.31089 -0.10232 0.03289  -0.02020 207 ILE A CG1 
1693 C CG2 . ILE A 213 ? 0.21770 0.29403 0.26379 -0.06582 0.05439  0.02841  207 ILE A CG2 
1694 C CD1 . ILE A 213 ? 0.27598 0.34717 0.33491 -0.13739 -0.00256 -0.04085 207 ILE A CD1 
1695 N N   . ASP A 214 ? 0.08655 0.21844 0.18939 -0.03317 -0.01654 -0.00070 208 ASP A N   
1696 C CA  . ASP A 214 ? 0.07049 0.19905 0.17333 -0.04529 -0.00703 0.00005  208 ASP A CA  
1697 C C   . ASP A 214 ? 0.13708 0.19076 0.15144 -0.01268 -0.00185 0.01102  208 ASP A C   
1698 O O   . ASP A 214 ? 0.15296 0.20523 0.14730 -0.02099 -0.00235 0.03104  208 ASP A O   
1699 C CB  . ASP A 214 ? 0.08653 0.18923 0.14279 -0.00823 -0.01142 -0.00351 208 ASP A CB  
1700 C CG  . ASP A 214 ? 0.12988 0.18865 0.17147 0.01022  0.00013  -0.00435 208 ASP A CG  
1701 O OD1 . ASP A 214 ? 0.14286 0.19640 0.17280 0.00723  0.01564  0.01944  208 ASP A OD1 
1702 O OD2 . ASP A 214 ? 0.15311 0.19161 0.16389 0.00774  -0.02009 -0.01475 208 ASP A OD2 
1703 N N   . ILE A 215 ? 0.14746 0.17276 0.12999 0.00240  0.00408  0.00970  209 ILE A N   
1704 C CA  . ILE A 215 ? 0.13018 0.15110 0.15137 -0.01914 0.00280  0.00933  209 ILE A CA  
1705 C C   . ILE A 215 ? 0.13027 0.16699 0.17300 -0.00769 0.00348  -0.00831 209 ILE A C   
1706 O O   . ILE A 215 ? 0.12119 0.17151 0.18950 0.01783  -0.00373 -0.00084 209 ILE A O   
1707 C CB  . ILE A 215 ? 0.12430 0.16509 0.16264 -0.01900 0.01188  -0.00693 209 ILE A CB  
1708 C CG1 . ILE A 215 ? 0.11081 0.16622 0.16177 -0.02282 -0.02368 -0.00060 209 ILE A CG1 
1709 C CG2 . ILE A 215 ? 0.12857 0.16005 0.15580 -0.01992 0.03489  -0.01193 209 ILE A CG2 
1710 C CD1 . ILE A 215 ? 0.12072 0.19584 0.18802 -0.02266 -0.03225 -0.00656 209 ILE A CD1 
1711 N N   . TRP A 216 ? 0.11273 0.16347 0.17758 0.00239  -0.02268 -0.00097 210 TRP A N   
1712 C CA  . TRP A 216 ? 0.11545 0.18192 0.19216 -0.00372 -0.02132 -0.00948 210 TRP A CA  
1713 C C   . TRP A 216 ? 0.14868 0.18998 0.17356 -0.00211 0.00238  0.00381  210 TRP A C   
1714 O O   . TRP A 216 ? 0.13641 0.19759 0.16937 -0.00406 0.01988  0.01689  210 TRP A O   
1715 C CB  . TRP A 216 ? 0.11379 0.17369 0.18482 -0.02455 -0.01160 -0.02806 210 TRP A CB  
1716 C CG  . TRP A 216 ? 0.11992 0.17765 0.17047 -0.00884 -0.00836 -0.00527 210 TRP A CG  
1717 C CD1 . TRP A 216 ? 0.15617 0.18156 0.18663 -0.00793 0.02868  -0.01449 210 TRP A CD1 
1718 C CD2 . TRP A 216 ? 0.12645 0.18683 0.13916 -0.00213 -0.02089 -0.02106 210 TRP A CD2 
1719 N NE1 . TRP A 216 ? 0.15403 0.20118 0.15939 -0.00202 0.00527  -0.00986 210 TRP A NE1 
1720 C CE2 . TRP A 216 ? 0.13176 0.20906 0.15084 -0.00185 -0.03743 -0.01269 210 TRP A CE2 
1721 C CE3 . TRP A 216 ? 0.14746 0.21680 0.14776 -0.02531 0.01140  -0.03011 210 TRP A CE3 
1722 C CZ2 . TRP A 216 ? 0.12980 0.22676 0.16067 0.00952  -0.01034 -0.00390 210 TRP A CZ2 
1723 C CZ3 . TRP A 216 ? 0.17345 0.22314 0.17408 -0.03134 0.04840  -0.05605 210 TRP A CZ3 
1724 C CH2 . TRP A 216 ? 0.16053 0.22179 0.19193 0.00247  0.02084  -0.01062 210 TRP A CH2 
1725 N N   . SER A 217 ? 0.15452 0.17924 0.15977 -0.02386 -0.03111 0.00824  211 SER A N   
1726 C CA  . SER A 217 ? 0.13413 0.19722 0.13914 -0.01365 -0.03017 -0.00063 211 SER A CA  
1727 C C   . SER A 217 ? 0.15565 0.19605 0.16178 -0.03147 -0.00205 0.01848  211 SER A C   
1728 O O   . SER A 217 ? 0.15940 0.20612 0.16750 -0.02782 -0.00970 0.01076  211 SER A O   
1729 C CB  . SER A 217 ? 0.12029 0.20113 0.14527 -0.02581 -0.00242 0.01267  211 SER A CB  
1730 O OG  . SER A 217 ? 0.15195 0.19937 0.18330 -0.02056 0.02081  0.00702  211 SER A OG  
1731 N N   . VAL A 218 ? 0.13714 0.18131 0.16829 -0.05386 -0.01744 0.01326  212 VAL A N   
1732 C CA  . VAL A 218 ? 0.12669 0.19134 0.16907 -0.05556 -0.01880 -0.00111 212 VAL A CA  
1733 C C   . VAL A 218 ? 0.10558 0.19023 0.14126 -0.01981 -0.00513 0.00830  212 VAL A C   
1734 O O   . VAL A 218 ? 0.12963 0.21000 0.16405 -0.00006 0.01735  0.01818  212 VAL A O   
1735 C CB  . VAL A 218 ? 0.14743 0.20106 0.16069 -0.05397 -0.01051 -0.00243 212 VAL A CB  
1736 C CG1 . VAL A 218 ? 0.17110 0.21176 0.18881 -0.06396 0.03114  0.01049  212 VAL A CG1 
1737 C CG2 . VAL A 218 ? 0.20405 0.20760 0.15350 -0.03822 0.00375  -0.01680 212 VAL A CG2 
1738 N N   . GLY A 219 ? 0.12545 0.17866 0.11226 -0.02654 -0.01849 -0.01173 213 GLY A N   
1739 C CA  . GLY A 219 ? 0.15774 0.17113 0.12665 -0.01797 0.02877  -0.00578 213 GLY A CA  
1740 C C   . GLY A 219 ? 0.16173 0.18682 0.15435 -0.01504 0.01777  0.01207  213 GLY A C   
1741 O O   . GLY A 219 ? 0.18561 0.20554 0.15271 -0.01610 0.03692  0.01712  213 GLY A O   
1742 N N   . CYS A 220 ? 0.12752 0.16908 0.16998 -0.03438 -0.00613 0.02268  214 CYS A N   
1743 C CA  . CYS A 220 ? 0.10519 0.17296 0.19333 -0.01196 0.01660  0.02942  214 CYS A CA  
1744 C C   . CYS A 220 ? 0.12513 0.19211 0.21208 -0.01945 0.03026  0.01370  214 CYS A C   
1745 O O   . CYS A 220 ? 0.13845 0.20156 0.21560 0.00414  0.00910  0.00807  214 CYS A O   
1746 C CB  . CYS A 220 ? 0.06981 0.18746 0.19530 -0.01373 0.02960  0.00609  214 CYS A CB  
1747 S SG  . CYS A 220 ? 0.12824 0.19943 0.20210 0.00566  0.01867  0.00002  214 CYS A SG  
1748 N N   . ILE A 221 ? 0.11517 0.20344 0.18894 -0.01481 -0.00363 0.02071  215 ILE A N   
1749 C CA  . ILE A 221 ? 0.08580 0.20188 0.19083 -0.02305 -0.01518 0.00256  215 ILE A CA  
1750 C C   . ILE A 221 ? 0.13191 0.19847 0.17808 0.00680  0.00007  0.01927  215 ILE A C   
1751 O O   . ILE A 221 ? 0.15721 0.20300 0.19600 0.02701  0.01536  0.02740  215 ILE A O   
1752 C CB  . ILE A 221 ? 0.09458 0.20411 0.16355 -0.01451 -0.03456 0.01096  215 ILE A CB  
1753 C CG1 . ILE A 221 ? 0.13564 0.18511 0.17623 0.00824  0.01347  -0.00881 215 ILE A CG1 
1754 C CG2 . ILE A 221 ? 0.12033 0.22908 0.20748 -0.02006 -0.01995 -0.01684 215 ILE A CG2 
1755 C CD1 . ILE A 221 ? 0.17922 0.19077 0.15494 0.02964  0.02179  -0.01594 215 ILE A CD1 
1756 N N   . LEU A 222 ? 0.13451 0.18870 0.18588 -0.00520 0.03373  0.01351  216 LEU A N   
1757 C CA  . LEU A 222 ? 0.13847 0.17875 0.17793 -0.01668 0.03102  0.00785  216 LEU A CA  
1758 C C   . LEU A 222 ? 0.14187 0.19778 0.20594 -0.00518 0.03009  -0.01289 216 LEU A C   
1759 O O   . LEU A 222 ? 0.14202 0.19745 0.20384 0.00691  0.00901  -0.01735 216 LEU A O   
1760 C CB  . LEU A 222 ? 0.13452 0.20197 0.18936 -0.00073 0.01712  0.05508  216 LEU A CB  
1761 C CG  . LEU A 222 ? 0.12312 0.19932 0.16618 -0.01444 -0.00096 0.04010  216 LEU A CG  
1762 C CD1 . LEU A 222 ? 0.13273 0.20212 0.17948 -0.05925 0.00071  0.01239  216 LEU A CD1 
1763 C CD2 . LEU A 222 ? 0.17841 0.18385 0.18505 0.00892  0.03019  0.04969  216 LEU A CD2 
1764 N N   . ALA A 223 ? 0.14553 0.21140 0.20593 -0.01636 0.01027  -0.01155 217 ALA A N   
1765 C CA  . ALA A 223 ? 0.16084 0.22034 0.19918 -0.02365 0.00908  -0.02018 217 ALA A CA  
1766 C C   . ALA A 223 ? 0.16861 0.23231 0.23157 0.02023  0.04783  -0.01616 217 ALA A C   
1767 O O   . ALA A 223 ? 0.16637 0.24426 0.23782 0.03471  0.02664  -0.01176 217 ALA A O   
1768 C CB  . ALA A 223 ? 0.19182 0.22074 0.18355 -0.07018 0.04029  -0.03998 217 ALA A CB  
1769 N N   . GLU A 224 ? 0.17177 0.22945 0.23906 0.01703  0.05176  -0.00880 218 GLU A N   
1770 C CA  . GLU A 224 ? 0.16384 0.23079 0.23003 0.01584  0.02146  0.02251  218 GLU A CA  
1771 C C   . GLU A 224 ? 0.17204 0.25498 0.25213 0.01622  0.00818  0.00068  218 GLU A C   
1772 O O   . GLU A 224 ? 0.22830 0.27429 0.28014 0.01964  0.01740  0.02645  218 GLU A O   
1773 C CB  . GLU A 224 ? 0.17306 0.20654 0.23212 0.04527  0.01027  0.04570  218 GLU A CB  
1774 C CG  . GLU A 224 ? 0.17809 0.21338 0.27266 0.02991  0.01285  0.04879  218 GLU A CG  
1775 C CD  . GLU A 224 ? 0.21159 0.22133 0.30842 0.02015  -0.01955 0.03795  218 GLU A CD  
1776 O OE1 . GLU A 224 ? 0.20599 0.20599 0.33896 0.01018  -0.02980 0.01646  218 GLU A OE1 
1777 O OE2 . GLU A 224 ? 0.21749 0.24018 0.35198 0.02321  -0.02979 0.05196  218 GLU A OE2 
1778 N N   . MET A 225 ? 0.14305 0.24924 0.26280 -0.00775 -0.00290 -0.00129 219 MET A N   
1779 C CA  . MET A 225 ? 0.14826 0.25898 0.25033 -0.01240 0.02056  -0.03106 219 MET A CA  
1780 C C   . MET A 225 ? 0.19607 0.26817 0.25860 0.02974  0.06602  -0.01333 219 MET A C   
1781 O O   . MET A 225 ? 0.23551 0.27756 0.25897 0.05450  0.04067  -0.00944 219 MET A O   
1782 C CB  . MET A 225 ? 0.16819 0.26029 0.27651 -0.00260 0.05226  -0.01165 219 MET A CB  
1783 C CG  . MET A 225 ? 0.12030 0.24533 0.26557 0.02314  0.03734  0.00036  219 MET A CG  
1784 S SD  . MET A 225 ? 0.15145 0.25263 0.28456 0.01729  0.00603  0.00396  219 MET A SD  
1785 C CE  . MET A 225 ? 0.14373 0.26281 0.27506 0.03077  0.02517  -0.01386 219 MET A CE  
1786 N N   . LEU A 226 ? 0.21113 0.25838 0.24115 0.04255  0.07775  0.00332  220 LEU A N   
1787 C CA  . LEU A 226 ? 0.23439 0.26708 0.26532 0.03242  0.08035  0.01256  220 LEU A CA  
1788 C C   . LEU A 226 ? 0.25230 0.27965 0.30710 0.03103  0.08741  -0.01620 220 LEU A C   
1789 O O   . LEU A 226 ? 0.30823 0.30371 0.34105 0.00603  0.13943  -0.02608 220 LEU A O   
1790 C CB  . LEU A 226 ? 0.22376 0.27669 0.26835 0.03001  0.03991  0.02942  220 LEU A CB  
1791 C CG  . LEU A 226 ? 0.21214 0.29386 0.26966 0.00975  0.03505  0.02384  220 LEU A CG  
1792 C CD1 . LEU A 226 ? 0.20693 0.30683 0.26259 -0.00456 -0.00087 0.04887  220 LEU A CD1 
1793 C CD2 . LEU A 226 ? 0.20135 0.30768 0.28134 0.01540  0.01070  0.01483  220 LEU A CD2 
1794 N N   . SER A 227 ? 0.23686 0.26111 0.32372 0.02708  0.02896  -0.04331 221 SER A N   
1795 C CA  . SER A 227 ? 0.26328 0.27480 0.37229 0.03499  0.02664  -0.06217 221 SER A CA  
1796 C C   . SER A 227 ? 0.26530 0.26166 0.39429 0.06434  0.00801  -0.06147 221 SER A C   
1797 O O   . SER A 227 ? 0.28427 0.25002 0.41132 0.09120  0.01375  -0.06912 221 SER A O   
1798 C CB  . SER A 227 ? 0.25215 0.30624 0.40119 0.03022  0.01313  -0.05496 221 SER A CB  
1799 O OG  . SER A 227 ? 0.25116 0.32209 0.41756 0.00191  0.00702  -0.05541 221 SER A OG  
1800 N N   . ASN A 228 ? 0.20881 0.26676 0.40585 0.06140  -0.01836 -0.03301 222 ASN A N   
1801 C CA  . ASN A 228 ? 0.18726 0.26259 0.42159 0.07482  -0.05126 0.02212  222 ASN A CA  
1802 C C   . ASN A 228 ? 0.23339 0.29740 0.45683 0.05660  -0.05031 0.04719  222 ASN A C   
1803 O O   . ASN A 228 ? 0.28337 0.33095 0.49664 0.01358  -0.03683 0.07311  222 ASN A O   
1804 C CB  . ASN A 228 ? 0.21036 0.26572 0.42293 0.06390  -0.02922 0.00925  222 ASN A CB  
1805 C CG  . ASN A 228 ? 0.21146 0.26720 0.43463 0.08327  -0.00603 0.01316  222 ASN A CG  
1806 O OD1 . ASN A 228 ? 0.22432 0.25611 0.44315 0.07425  0.01227  -0.00527 222 ASN A OD1 
1807 N ND2 . ASN A 228 ? 0.20805 0.28040 0.43040 0.08557  -0.00437 0.02953  222 ASN A ND2 
1808 N N   . ARG A 229 ? 0.21411 0.28681 0.42546 0.05457  -0.05182 0.02045  223 ARG A N   
1809 C CA  . ARG A 229 ? 0.23196 0.27061 0.41749 0.04625  -0.02770 0.00058  223 ARG A CA  
1810 C C   . ARG A 229 ? 0.20096 0.23794 0.39117 0.05000  -0.02797 0.00524  223 ARG A C   
1811 O O   . ARG A 229 ? 0.18091 0.22501 0.38056 0.02972  -0.01709 0.00687  223 ARG A O   
1812 C CB  . ARG A 229 ? 0.28730 0.28051 0.41814 0.04195  -0.01764 -0.00370 223 ARG A CB  
1813 C CG  . ARG A 229 ? 0.34621 0.30414 0.42061 0.01951  -0.02966 -0.02550 223 ARG A CG  
1814 C CD  . ARG A 229 ? 0.40058 0.31357 0.42996 0.01703  -0.01630 -0.02310 223 ARG A CD  
1815 N NE  . ARG A 229 ? 0.44115 0.31567 0.42652 0.02205  -0.00245 -0.01028 223 ARG A NE  
1816 C CZ  . ARG A 229 ? 0.45155 0.30502 0.43169 0.02845  -0.00095 -0.00184 223 ARG A CZ  
1817 N NH1 . ARG A 229 ? 0.46231 0.30253 0.42892 0.01807  0.00923  -0.00765 223 ARG A NH1 
1818 N NH2 . ARG A 229 ? 0.44391 0.29367 0.42656 0.04564  -0.01748 0.00514  223 ARG A NH2 
1819 N N   . PRO A 230 ? 0.21159 0.22004 0.36733 0.05882  -0.01419 0.03850  224 PRO A N   
1820 C CA  . PRO A 230 ? 0.21196 0.23029 0.35552 0.05036  -0.01658 0.02490  224 PRO A CA  
1821 C C   . PRO A 230 ? 0.22209 0.22184 0.33093 0.03840  -0.01314 -0.01471 224 PRO A C   
1822 O O   . PRO A 230 ? 0.21948 0.22494 0.36766 0.03379  -0.02151 -0.05712 224 PRO A O   
1823 C CB  . PRO A 230 ? 0.22596 0.22557 0.36947 0.05969  -0.00824 0.05324  224 PRO A CB  
1824 C CG  . PRO A 230 ? 0.25488 0.25426 0.40373 0.04933  0.02075  0.04690  224 PRO A CG  
1825 C CD  . PRO A 230 ? 0.23399 0.25232 0.39546 0.04682  -0.01196 0.04390  224 PRO A CD  
1826 N N   . ILE A 231 ? 0.21482 0.23526 0.29780 0.00675  -0.00759 0.00087  225 ILE A N   
1827 C CA  . ILE A 231 ? 0.17483 0.21467 0.28529 0.00616  -0.02622 -0.00248 225 ILE A CA  
1828 C C   . ILE A 231 ? 0.18749 0.22005 0.28860 -0.01675 -0.00527 -0.03304 225 ILE A C   
1829 O O   . ILE A 231 ? 0.17606 0.23442 0.29101 -0.02081 -0.00831 -0.05148 225 ILE A O   
1830 C CB  . ILE A 231 ? 0.19584 0.18751 0.28301 -0.00725 -0.01048 -0.01508 225 ILE A CB  
1831 C CG1 . ILE A 231 ? 0.23033 0.19609 0.28517 -0.00288 -0.05577 0.01389  225 ILE A CG1 
1832 C CG2 . ILE A 231 ? 0.18430 0.16030 0.30290 -0.00904 0.02543  -0.01593 225 ILE A CG2 
1833 C CD1 . ILE A 231 ? 0.25711 0.21564 0.30764 -0.01536 -0.02365 0.00981  225 ILE A CD1 
1834 N N   . PHE A 232 ? 0.16275 0.21352 0.28256 -0.02634 0.00101  -0.01070 226 PHE A N   
1835 C CA  . PHE A 232 ? 0.16761 0.20706 0.28271 -0.03374 -0.01901 0.01168  226 PHE A CA  
1836 C C   . PHE A 232 ? 0.21507 0.22814 0.35746 -0.02578 -0.01615 0.03599  226 PHE A C   
1837 O O   . PHE A 232 ? 0.18937 0.24398 0.34286 -0.03481 -0.02706 0.07185  226 PHE A O   
1838 C CB  . PHE A 232 ? 0.18221 0.21917 0.24023 -0.02887 -0.00716 0.01070  226 PHE A CB  
1839 C CG  . PHE A 232 ? 0.18210 0.22190 0.22524 -0.00822 0.01220  -0.00241 226 PHE A CG  
1840 C CD1 . PHE A 232 ? 0.18834 0.23221 0.20086 -0.00110 -0.00608 -0.00586 226 PHE A CD1 
1841 C CD2 . PHE A 232 ? 0.15448 0.22640 0.20207 -0.00778 -0.00014 -0.02465 226 PHE A CD2 
1842 C CE1 . PHE A 232 ? 0.17470 0.22998 0.19326 -0.00866 -0.00525 -0.02613 226 PHE A CE1 
1843 C CE2 . PHE A 232 ? 0.14793 0.22380 0.18861 0.00220  -0.00102 -0.03003 226 PHE A CE2 
1844 C CZ  . PHE A 232 ? 0.14619 0.23205 0.17642 -0.01324 -0.01837 -0.05264 226 PHE A CZ  
1845 N N   . PRO A 233 ? 0.27845 0.21922 0.42377 -0.05384 -0.01897 0.02241  227 PRO A N   
1846 C CA  . PRO A 233 ? 0.29356 0.22552 0.45143 -0.04923 -0.03503 0.03415  227 PRO A CA  
1847 C C   . PRO A 233 ? 0.29373 0.22977 0.47349 -0.07188 -0.07486 0.03891  227 PRO A C   
1848 O O   . PRO A 233 ? 0.27644 0.25301 0.51338 -0.06142 -0.09444 0.04175  227 PRO A O   
1849 C CB  . PRO A 233 ? 0.33099 0.24275 0.47036 -0.03904 0.01220  0.04512  227 PRO A CB  
1850 C CG  . PRO A 233 ? 0.33402 0.23432 0.46461 -0.02839 0.04856  0.03589  227 PRO A CG  
1851 C CD  . PRO A 233 ? 0.29661 0.22671 0.44180 -0.03350 0.00836  0.03170  227 PRO A CD  
1852 N N   . GLY A 234 ? 0.30728 0.21836 0.44043 -0.09827 -0.10698 0.04429  228 GLY A N   
1853 C CA  . GLY A 234 ? 0.35862 0.22988 0.42334 -0.11905 -0.12568 0.06132  228 GLY A CA  
1854 C C   . GLY A 234 ? 0.44614 0.25980 0.41846 -0.14321 -0.12727 0.07159  228 GLY A C   
1855 O O   . GLY A 234 ? 0.45852 0.27550 0.41985 -0.14668 -0.14380 0.07762  228 GLY A O   
1856 N N   . LYS A 235 ? 0.51502 0.26501 0.41128 -0.14083 -0.11646 0.09168  229 LYS A N   
1857 C CA  . LYS A 235 ? 0.58258 0.29472 0.42436 -0.14052 -0.09967 0.08004  229 LYS A CA  
1858 C C   . LYS A 235 ? 0.62827 0.30697 0.41162 -0.18036 -0.07075 0.04992  229 LYS A C   
1859 O O   . LYS A 235 ? 0.67349 0.32835 0.43013 -0.15525 -0.07336 0.06866  229 LYS A O   
1860 C CB  . LYS A 235 ? 0.59080 0.30336 0.43594 -0.09279 -0.10205 0.09913  229 LYS A CB  
1861 C CG  . LYS A 235 ? 0.60251 0.31013 0.44979 -0.05931 -0.08746 0.11449  229 LYS A CG  
1862 C CD  . LYS A 235 ? 0.61417 0.31044 0.45817 -0.03361 -0.07608 0.11927  229 LYS A CD  
1863 C CE  . LYS A 235 ? 0.62223 0.31673 0.46192 -0.01104 -0.07561 0.12836  229 LYS A CE  
1864 N NZ  . LYS A 235 ? 0.63120 0.32127 0.46866 0.00632  -0.06883 0.12178  229 LYS A NZ  
1865 N N   . HIS A 236 ? 0.62248 0.29944 0.39286 -0.21902 -0.04370 -0.00733 230 HIS A N   
1866 C CA  . HIS A 236 ? 0.63230 0.33098 0.38726 -0.24068 0.01589  -0.04152 230 HIS A CA  
1867 C C   . HIS A 236 ? 0.63683 0.36208 0.37019 -0.23519 0.06372  -0.06956 230 HIS A C   
1868 O O   . HIS A 236 ? 0.61114 0.35438 0.33164 -0.24365 0.02273  -0.06591 230 HIS A O   
1869 C CB  . HIS A 236 ? 0.64358 0.32929 0.39328 -0.24156 0.03352  -0.03956 230 HIS A CB  
1870 C CG  . HIS A 236 ? 0.61952 0.33802 0.40312 -0.24687 0.04394  -0.03652 230 HIS A CG  
1871 N ND1 . HIS A 236 ? 0.58252 0.34173 0.40867 -0.24638 0.04051  -0.03638 230 HIS A ND1 
1872 C CD2 . HIS A 236 ? 0.59629 0.34016 0.39094 -0.24570 0.06341  -0.03158 230 HIS A CD2 
1873 C CE1 . HIS A 236 ? 0.56568 0.34703 0.38741 -0.24680 0.04618  -0.04452 230 HIS A CE1 
1874 N NE2 . HIS A 236 ? 0.57840 0.34900 0.38125 -0.24842 0.06996  -0.04226 230 HIS A NE2 
1875 N N   . TYR A 237 ? 0.64813 0.40900 0.38264 -0.21344 0.13791  -0.07551 231 TYR A N   
1876 C CA  . TYR A 237 ? 0.61212 0.43529 0.37668 -0.20656 0.14230  -0.10983 231 TYR A CA  
1877 C C   . TYR A 237 ? 0.50346 0.44090 0.37646 -0.20184 0.07548  -0.13188 231 TYR A C   
1878 O O   . TYR A 237 ? 0.45123 0.42165 0.32710 -0.20365 0.03564  -0.14800 231 TYR A O   
1879 C CB  . TYR A 237 ? 0.66080 0.45836 0.39331 -0.21524 0.18702  -0.10542 231 TYR A CB  
1880 C CG  . TYR A 237 ? 0.69214 0.48237 0.37447 -0.21577 0.19750  -0.11096 231 TYR A CG  
1881 C CD1 . TYR A 237 ? 0.68245 0.49430 0.37227 -0.23313 0.19233  -0.12985 231 TYR A CD1 
1882 C CD2 . TYR A 237 ? 0.70887 0.48812 0.35455 -0.21659 0.20843  -0.10590 231 TYR A CD2 
1883 C CE1 . TYR A 237 ? 0.69486 0.49955 0.36533 -0.24138 0.19771  -0.13424 231 TYR A CE1 
1884 C CE2 . TYR A 237 ? 0.70668 0.49799 0.34866 -0.22673 0.20402  -0.09369 231 TYR A CE2 
1885 C CZ  . TYR A 237 ? 0.69058 0.50389 0.34548 -0.24682 0.20553  -0.11411 231 TYR A CZ  
1886 O OH  . TYR A 237 ? 0.65503 0.50489 0.33458 -0.24470 0.20561  -0.09924 231 TYR A OH  
1887 N N   . LEU A 238 ? 0.47459 0.45127 0.40830 -0.17709 0.09092  -0.12720 232 LEU A N   
1888 C CA  . LEU A 238 ? 0.40865 0.46504 0.38301 -0.15746 0.03040  -0.08614 232 LEU A CA  
1889 C C   . LEU A 238 ? 0.39038 0.47485 0.38456 -0.12055 0.02719  -0.05979 232 LEU A C   
1890 O O   . LEU A 238 ? 0.38254 0.52020 0.37473 -0.11571 -0.03130 -0.08570 232 LEU A O   
1891 C CB  . LEU A 238 ? 0.40739 0.45224 0.39407 -0.16166 0.02838  -0.08665 232 LEU A CB  
1892 C CG  . LEU A 238 ? 0.41017 0.43293 0.39742 -0.18371 0.03192  -0.07765 232 LEU A CG  
1893 C CD1 . LEU A 238 ? 0.40467 0.43669 0.42320 -0.17868 0.05898  -0.06455 232 LEU A CD1 
1894 C CD2 . LEU A 238 ? 0.45192 0.43993 0.40140 -0.17660 0.04578  -0.08932 232 LEU A CD2 
1895 N N   . ASP A 239 ? 0.37265 0.43566 0.37412 -0.11846 0.03717  -0.03965 233 ASP A N   
1896 C CA  . ASP A 239 ? 0.31150 0.38799 0.33303 -0.10992 0.01933  -0.02059 233 ASP A CA  
1897 C C   . ASP A 239 ? 0.24343 0.36224 0.30750 -0.09717 -0.00454 0.00119  233 ASP A C   
1898 O O   . ASP A 239 ? 0.22746 0.37049 0.28684 -0.06933 -0.01436 0.02314  233 ASP A O   
1899 C CB  . ASP A 239 ? 0.33115 0.36477 0.32729 -0.10208 -0.00382 -0.01289 233 ASP A CB  
1900 C CG  . ASP A 239 ? 0.33223 0.35871 0.34452 -0.08353 -0.02812 0.00495  233 ASP A CG  
1901 O OD1 . ASP A 239 ? 0.33150 0.37226 0.34445 -0.05876 -0.03990 -0.01115 233 ASP A OD1 
1902 O OD2 . ASP A 239 ? 0.36543 0.34710 0.34843 -0.05605 -0.03836 0.03249  233 ASP A OD2 
1903 N N   . GLN A 240 ? 0.20173 0.32328 0.30298 -0.11952 -0.03195 -0.00705 234 GLN A N   
1904 C CA  . GLN A 240 ? 0.19232 0.30468 0.27856 -0.08075 -0.05447 0.02880  234 GLN A CA  
1905 C C   . GLN A 240 ? 0.17386 0.33981 0.29009 -0.08062 -0.04414 0.05393  234 GLN A C   
1906 O O   . GLN A 240 ? 0.20779 0.35677 0.29181 -0.07779 -0.02514 0.06256  234 GLN A O   
1907 C CB  . GLN A 240 ? 0.20958 0.25997 0.26721 -0.05498 -0.06133 0.04377  234 GLN A CB  
1908 C CG  . GLN A 240 ? 0.21168 0.22949 0.27941 -0.07209 -0.03236 0.04215  234 GLN A CG  
1909 C CD  . GLN A 240 ? 0.22645 0.22697 0.27773 -0.07210 -0.04788 0.05978  234 GLN A CD  
1910 O OE1 . GLN A 240 ? 0.23957 0.23359 0.29446 -0.05692 -0.02662 0.05756  234 GLN A OE1 
1911 N NE2 . GLN A 240 ? 0.24695 0.23078 0.24552 -0.08591 -0.06296 0.03053  234 GLN A NE2 
1912 N N   . LEU A 241 ? 0.15663 0.36123 0.30926 -0.06922 -0.04767 0.05556  235 LEU A N   
1913 C CA  . LEU A 241 ? 0.14246 0.37903 0.34028 -0.05696 -0.06055 0.06451  235 LEU A CA  
1914 C C   . LEU A 241 ? 0.18088 0.38123 0.34398 -0.05266 -0.03662 0.04426  235 LEU A C   
1915 O O   . LEU A 241 ? 0.17951 0.40689 0.32946 -0.02542 -0.03177 0.05728  235 LEU A O   
1916 C CB  . LEU A 241 ? 0.15956 0.39893 0.37594 -0.05780 -0.06303 0.07281  235 LEU A CB  
1917 C CG  . LEU A 241 ? 0.16051 0.40792 0.38700 -0.08317 -0.04739 0.05519  235 LEU A CG  
1918 C CD1 . LEU A 241 ? 0.19052 0.41676 0.38393 -0.09133 -0.04900 0.03112  235 LEU A CD1 
1919 C CD2 . LEU A 241 ? 0.13747 0.41291 0.37899 -0.06644 -0.04122 0.05469  235 LEU A CD2 
1920 N N   . ASN A 242 ? 0.22334 0.36460 0.35740 -0.08284 0.00830  -0.00147 236 ASN A N   
1921 C CA  . ASN A 242 ? 0.25442 0.34996 0.32023 -0.07036 -0.00265 -0.01262 236 ASN A CA  
1922 C C   . ASN A 242 ? 0.27314 0.32484 0.29128 -0.06531 -0.01691 -0.00534 236 ASN A C   
1923 O O   . ASN A 242 ? 0.29280 0.33148 0.27030 -0.07666 -0.02677 0.00025  236 ASN A O   
1924 C CB  . ASN A 242 ? 0.22263 0.35153 0.32588 -0.06402 -0.02390 -0.04065 236 ASN A CB  
1925 C CG  . ASN A 242 ? 0.21593 0.36792 0.33581 -0.03202 -0.02836 -0.03236 236 ASN A CG  
1926 O OD1 . ASN A 242 ? 0.20825 0.37627 0.35326 -0.02380 -0.07562 -0.02084 236 ASN A OD1 
1927 N ND2 . ASN A 242 ? 0.17471 0.36259 0.30522 -0.04024 -0.04307 -0.04515 236 ASN A ND2 
1928 N N   . HIS A 243 ? 0.26449 0.27879 0.27708 -0.04853 -0.02868 -0.00538 237 HIS A N   
1929 C CA  . HIS A 243 ? 0.24576 0.24735 0.27871 -0.03429 -0.03357 0.01532  237 HIS A CA  
1930 C C   . HIS A 243 ? 0.25449 0.23300 0.28217 -0.04113 0.01525  -0.00860 237 HIS A C   
1931 O O   . HIS A 243 ? 0.26034 0.22491 0.25402 -0.05063 0.00480  -0.00405 237 HIS A O   
1932 C CB  . HIS A 243 ? 0.27094 0.24920 0.26564 -0.02580 -0.07817 0.02086  237 HIS A CB  
1933 C CG  . HIS A 243 ? 0.30412 0.26450 0.32537 0.01582  -0.04148 0.03210  237 HIS A CG  
1934 N ND1 . HIS A 243 ? 0.34538 0.28035 0.37356 0.01740  -0.03225 0.03983  237 HIS A ND1 
1935 C CD2 . HIS A 243 ? 0.31638 0.26507 0.37147 0.02626  -0.03311 0.02507  237 HIS A CD2 
1936 C CE1 . HIS A 243 ? 0.36478 0.28519 0.40082 0.02479  -0.00652 0.04344  237 HIS A CE1 
1937 N NE2 . HIS A 243 ? 0.35095 0.28870 0.40451 0.03202  -0.01173 0.03839  237 HIS A NE2 
1938 N N   . ILE A 244 ? 0.20085 0.23406 0.27313 -0.01839 0.00225  -0.02149 238 ILE A N   
1939 C CA  . ILE A 244 ? 0.19956 0.25106 0.23961 -0.00145 -0.02121 -0.02401 238 ILE A CA  
1940 C C   . ILE A 244 ? 0.19597 0.26697 0.23591 -0.00793 -0.03876 -0.02397 238 ILE A C   
1941 O O   . ILE A 244 ? 0.19507 0.27591 0.23352 -0.02648 -0.02969 -0.03779 238 ILE A O   
1942 C CB  . ILE A 244 ? 0.16476 0.24729 0.22767 0.01874  -0.04097 -0.01005 238 ILE A CB  
1943 C CG1 . ILE A 244 ? 0.13495 0.25830 0.24305 -0.03102 -0.03045 -0.05334 238 ILE A CG1 
1944 C CG2 . ILE A 244 ? 0.13391 0.23468 0.23016 0.01353  -0.06180 -0.02925 238 ILE A CG2 
1945 C CD1 . ILE A 244 ? 0.11573 0.27255 0.24783 -0.01263 0.00136  -0.05814 238 ILE A CD1 
1946 N N   . LEU A 245 ? 0.18851 0.26639 0.22494 -0.03032 -0.06849 -0.03224 239 LEU A N   
1947 C CA  . LEU A 245 ? 0.19864 0.27656 0.21847 -0.02007 -0.07183 -0.02171 239 LEU A CA  
1948 C C   . LEU A 245 ? 0.22723 0.27656 0.21636 -0.02835 -0.04748 -0.04339 239 LEU A C   
1949 O O   . LEU A 245 ? 0.27080 0.29884 0.20477 -0.02079 -0.05000 -0.04747 239 LEU A O   
1950 C CB  . LEU A 245 ? 0.20215 0.27754 0.24844 -0.01506 -0.05790 -0.02282 239 LEU A CB  
1951 C CG  . LEU A 245 ? 0.20380 0.27132 0.29497 0.00752  -0.04427 -0.03037 239 LEU A CG  
1952 C CD1 . LEU A 245 ? 0.19491 0.28624 0.30930 -0.00020 -0.02385 -0.06578 239 LEU A CD1 
1953 C CD2 . LEU A 245 ? 0.27078 0.28130 0.30705 0.00907  -0.02132 -0.01595 239 LEU A CD2 
1954 N N   . GLY A 246 ? 0.22663 0.27777 0.22151 -0.01425 -0.03058 -0.06165 240 GLY A N   
1955 C CA  . GLY A 246 ? 0.23966 0.28018 0.22239 -0.00294 -0.00950 -0.06570 240 GLY A CA  
1956 C C   . GLY A 246 ? 0.24996 0.28304 0.22976 0.01184  -0.00426 -0.07727 240 GLY A C   
1957 O O   . GLY A 246 ? 0.27989 0.29063 0.25255 -0.00868 0.02482  -0.07696 240 GLY A O   
1958 N N   . ILE A 247 ? 0.22428 0.28575 0.24678 0.02112  -0.02871 -0.07325 241 ILE A N   
1959 C CA  . ILE A 247 ? 0.19817 0.28746 0.25471 0.01253  -0.01475 -0.07774 241 ILE A CA  
1960 C C   . ILE A 247 ? 0.18528 0.30480 0.25245 0.01207  0.00211  -0.06949 241 ILE A C   
1961 O O   . ILE A 247 ? 0.19830 0.32367 0.27571 0.01841  0.01515  -0.05933 241 ILE A O   
1962 C CB  . ILE A 247 ? 0.18043 0.28230 0.29334 0.01467  -0.03279 -0.07310 241 ILE A CB  
1963 C CG1 . ILE A 247 ? 0.23968 0.30338 0.31498 -0.01165 -0.05228 -0.05964 241 ILE A CG1 
1964 C CG2 . ILE A 247 ? 0.16388 0.27927 0.31742 0.01062  -0.01983 -0.08204 241 ILE A CG2 
1965 C CD1 . ILE A 247 ? 0.28820 0.32501 0.34094 0.01225  -0.02810 -0.04547 241 ILE A CD1 
1966 N N   . LEU A 248 ? 0.19350 0.30142 0.24131 0.00396  0.01735  -0.07267 242 LEU A N   
1967 C CA  . LEU A 248 ? 0.17724 0.31610 0.22377 0.01176  0.00706  -0.06737 242 LEU A CA  
1968 C C   . LEU A 248 ? 0.20723 0.33275 0.20288 0.02508  0.00148  -0.03990 242 LEU A C   
1969 O O   . LEU A 248 ? 0.22161 0.33141 0.23292 0.02849  0.01418  -0.01671 242 LEU A O   
1970 C CB  A LEU A 248 ? 0.15682 0.30877 0.21990 0.00549  0.01844  -0.07326 242 LEU A CB  
1971 C CB  B LEU A 248 ? 0.18327 0.30494 0.21272 0.00649  0.03422  -0.07020 242 LEU A CB  
1972 C CG  A LEU A 248 ? 0.11273 0.30723 0.24054 -0.00277 0.00824  -0.07152 242 LEU A CG  
1973 C CG  B LEU A 248 ? 0.16938 0.30158 0.22876 -0.00278 0.04264  -0.06588 242 LEU A CG  
1974 C CD1 A LEU A 248 ? 0.09358 0.31347 0.24406 0.00778  -0.00207 -0.05387 242 LEU A CD1 
1975 C CD1 B LEU A 248 ? 0.17309 0.29522 0.22776 -0.02362 0.05308  -0.07292 242 LEU A CD1 
1976 C CD2 A LEU A 248 ? 0.10952 0.30425 0.24386 -0.02942 0.01118  -0.08806 242 LEU A CD2 
1977 C CD2 B LEU A 248 ? 0.17154 0.30777 0.25097 -0.00128 0.05006  -0.06289 242 LEU A CD2 
1978 N N   . GLY A 249 ? 0.21757 0.33241 0.17842 0.02651  -0.01537 -0.03985 243 GLY A N   
1979 C CA  . GLY A 249 ? 0.18284 0.33227 0.20066 0.04875  -0.04208 -0.02572 243 GLY A CA  
1980 C C   . GLY A 249 ? 0.19250 0.32460 0.19663 0.03644  -0.03428 -0.00738 243 GLY A C   
1981 O O   . GLY A 249 ? 0.22046 0.32802 0.19202 0.02993  -0.02072 -0.02239 243 GLY A O   
1982 N N   . SER A 250 ? 0.16190 0.30928 0.22947 0.02758  -0.04611 -0.00826 244 SER A N   
1983 C CA  . SER A 250 ? 0.20148 0.28452 0.23911 0.01743  -0.02236 -0.01320 244 SER A CA  
1984 C C   . SER A 250 ? 0.22279 0.28266 0.21391 0.01983  -0.01484 -0.01772 244 SER A C   
1985 O O   . SER A 250 ? 0.23060 0.27476 0.21288 0.00285  -0.00023 -0.00383 244 SER A O   
1986 C CB  . SER A 250 ? 0.19805 0.26586 0.24297 -0.00697 -0.01781 -0.04595 244 SER A CB  
1987 O OG  . SER A 250 ? 0.23131 0.27513 0.29656 -0.02233 0.05358  -0.05650 244 SER A OG  
1988 N N   . PRO A 251 ? 0.22093 0.28164 0.18419 0.04251  -0.02266 -0.00699 245 PRO A N   
1989 C CA  . PRO A 251 ? 0.24523 0.26567 0.16707 0.05927  -0.02032 0.00473  245 PRO A CA  
1990 C C   . PRO A 251 ? 0.24338 0.26403 0.17726 0.01415  -0.00099 -0.00151 245 PRO A C   
1991 O O   . PRO A 251 ? 0.22393 0.26648 0.18189 0.00630  -0.00292 0.00591  245 PRO A O   
1992 C CB  . PRO A 251 ? 0.29729 0.27485 0.17543 0.09795  0.00125  0.02046  245 PRO A CB  
1993 C CG  . PRO A 251 ? 0.33894 0.27986 0.19238 0.04991  0.03627  -0.00727 245 PRO A CG  
1994 C CD  . PRO A 251 ? 0.26436 0.28174 0.17692 0.04795  0.02745  -0.01804 245 PRO A CD  
1995 N N   . SER A 252 ? 0.22300 0.24249 0.17220 -0.00780 -0.00315 -0.00423 246 SER A N   
1996 C CA  . SER A 252 ? 0.21024 0.24949 0.18289 0.00031  -0.02729 0.00316  246 SER A CA  
1997 C C   . SER A 252 ? 0.22033 0.25556 0.21568 0.01934  -0.03966 -0.00312 246 SER A C   
1998 O O   . SER A 252 ? 0.22177 0.24880 0.21653 0.02312  -0.02943 -0.01262 246 SER A O   
1999 C CB  . SER A 252 ? 0.22485 0.26184 0.16941 0.00359  -0.03877 -0.01392 246 SER A CB  
2000 O OG  . SER A 252 ? 0.23004 0.28105 0.22167 -0.01000 -0.02173 -0.02865 246 SER A OG  
2001 N N   . GLN A 253 ? 0.21304 0.26958 0.25863 0.05758  -0.05204 0.00258  247 GLN A N   
2002 C CA  . GLN A 253 ? 0.19735 0.31691 0.27824 0.05123  -0.07552 -0.01568 247 GLN A CA  
2003 C C   . GLN A 253 ? 0.20369 0.30684 0.28415 0.04863  -0.03879 -0.01930 247 GLN A C   
2004 O O   . GLN A 253 ? 0.18026 0.31042 0.30385 0.04587  -0.01847 -0.01509 247 GLN A O   
2005 C CB  . GLN A 253 ? 0.21692 0.37030 0.32050 0.05485  -0.07312 -0.02379 247 GLN A CB  
2006 C CG  . GLN A 253 ? 0.23567 0.41958 0.36241 0.05170  -0.06232 -0.03018 247 GLN A CG  
2007 C CD  A GLN A 253 ? 0.26292 0.44719 0.40228 0.05615  -0.05610 -0.02238 247 GLN A CD  
2008 C CD  B GLN A 253 ? 0.23405 0.42516 0.36833 0.04268  -0.04480 -0.04090 247 GLN A CD  
2009 O OE1 A GLN A 253 ? 0.28837 0.46083 0.41712 0.06748  -0.06331 -0.02371 247 GLN A OE1 
2010 O OE1 B GLN A 253 ? 0.22420 0.42619 0.36716 0.03831  -0.05140 -0.04444 247 GLN A OE1 
2011 N NE2 A GLN A 253 ? 0.28044 0.45617 0.42780 0.04942  -0.02832 -0.03234 247 GLN A NE2 
2012 N NE2 B GLN A 253 ? 0.22897 0.42703 0.37747 0.04620  -0.02161 -0.04776 247 GLN A NE2 
2013 N N   . GLU A 254 ? 0.22056 0.30127 0.25876 0.01757  -0.05347 -0.04391 248 GLU A N   
2014 C CA  . GLU A 254 ? 0.24482 0.30239 0.26952 0.01177  -0.03805 -0.03860 248 GLU A CA  
2015 C C   . GLU A 254 ? 0.23812 0.30331 0.24643 -0.00373 -0.00985 -0.04441 248 GLU A C   
2016 O O   . GLU A 254 ? 0.27472 0.31840 0.24942 0.00524  -0.00481 -0.04967 248 GLU A O   
2017 C CB  . GLU A 254 ? 0.27708 0.29975 0.28392 -0.01255 -0.04697 -0.03892 248 GLU A CB  
2018 C CG  . GLU A 254 ? 0.29984 0.31070 0.32857 -0.01017 -0.05821 -0.00634 248 GLU A CG  
2019 C CD  . GLU A 254 ? 0.33830 0.32413 0.36519 -0.00161 -0.06454 0.02818  248 GLU A CD  
2020 O OE1 . GLU A 254 ? 0.36203 0.32424 0.39045 0.02546  -0.05744 0.04179  248 GLU A OE1 
2021 O OE2 . GLU A 254 ? 0.33074 0.32690 0.37591 -0.02899 -0.07598 0.04280  248 GLU A OE2 
2022 N N   . ASP A 255 ? 0.19112 0.30715 0.22427 0.00596  -0.03940 -0.00922 249 ASP A N   
2023 C CA  . ASP A 255 ? 0.20594 0.32243 0.22778 0.00720  -0.02106 -0.01960 249 ASP A CA  
2024 C C   . ASP A 255 ? 0.19557 0.31862 0.22745 -0.00177 -0.02748 -0.01601 249 ASP A C   
2025 O O   . ASP A 255 ? 0.21847 0.32419 0.22882 -0.02939 -0.01101 -0.00270 249 ASP A O   
2026 C CB  . ASP A 255 ? 0.19377 0.32959 0.21458 0.03014  0.00232  -0.01006 249 ASP A CB  
2027 C CG  . ASP A 255 ? 0.19723 0.32926 0.19384 0.04073  -0.02420 -0.00053 249 ASP A CG  
2028 O OD1 . ASP A 255 ? 0.19021 0.32466 0.16464 0.03504  -0.04528 -0.00460 249 ASP A OD1 
2029 O OD2 . ASP A 255 ? 0.21282 0.33581 0.22987 0.03463  -0.01917 -0.00618 249 ASP A OD2 
2030 N N   . LEU A 256 ? 0.17975 0.32659 0.22867 0.01063  -0.05096 -0.01705 250 LEU A N   
2031 C CA  . LEU A 256 ? 0.22202 0.35623 0.26830 0.02482  0.00317  -0.01019 250 LEU A CA  
2032 C C   . LEU A 256 ? 0.21068 0.38934 0.29561 0.00674  0.02162  -0.01183 250 LEU A C   
2033 O O   . LEU A 256 ? 0.21896 0.40741 0.29152 -0.01573 0.05291  -0.00211 250 LEU A O   
2034 C CB  . LEU A 256 ? 0.25095 0.35941 0.25935 0.03277  -0.01514 -0.00440 250 LEU A CB  
2035 C CG  . LEU A 256 ? 0.28339 0.37300 0.24087 0.04682  -0.04223 0.01436  250 LEU A CG  
2036 C CD1 . LEU A 256 ? 0.26793 0.38380 0.27051 0.03069  -0.07278 -0.02254 250 LEU A CD1 
2037 C CD2 . LEU A 256 ? 0.32960 0.37772 0.27702 0.04459  0.03042  0.02538  250 LEU A CD2 
2038 N N   . ASN A 257 ? 0.20530 0.40255 0.32824 0.04824  0.02276  -0.01273 251 ASN A N   
2039 C CA  . ASN A 257 ? 0.23092 0.42164 0.35317 0.06972  0.02665  -0.01629 251 ASN A CA  
2040 C C   . ASN A 257 ? 0.24619 0.42403 0.37617 0.08069  0.03860  -0.03222 251 ASN A C   
2041 O O   . ASN A 257 ? 0.27423 0.43968 0.39957 0.10521  0.06225  -0.04409 251 ASN A O   
2042 C CB  . ASN A 257 ? 0.27079 0.44016 0.35624 0.05497  0.02280  -0.00942 251 ASN A CB  
2043 C CG  . ASN A 257 ? 0.30545 0.46269 0.37420 0.05562  0.01765  0.01683  251 ASN A CG  
2044 O OD1 . ASN A 257 ? 0.31859 0.47806 0.37882 0.02981  0.00481  0.02423  251 ASN A OD1 
2045 N ND2 . ASN A 257 ? 0.32670 0.47331 0.38031 0.07884  0.04367  0.02446  251 ASN A ND2 
2046 N N   . CME A 258 ? 0.25471 0.41306 0.36735 0.05995  0.02548  -0.03357 252 CME A N   
2047 C CA  . CME A 258 ? 0.27393 0.40614 0.36148 0.01641  0.03099  -0.06704 252 CME A CA  
2048 C CB  . CME A 258 ? 0.29276 0.40754 0.40881 0.03320  0.03785  -0.07995 252 CME A CB  
2049 S SG  . CME A 258 ? 0.29029 0.41610 0.45890 0.02561  0.02052  -0.07572 252 CME A SG  
2050 S SD  . CME A 258 ? 0.42675 0.46242 0.52164 0.01572  0.04381  -0.05935 252 CME A SD  
2051 C CE  . CME A 258 ? 0.42785 0.46065 0.50476 0.01680  0.02337  -0.04904 252 CME A CE  
2052 C CZ  . CME A 258 ? 0.40938 0.45743 0.50418 0.02210  0.01296  -0.04151 252 CME A CZ  
2053 O OH  . CME A 258 ? 0.42675 0.45573 0.53750 0.02452  0.07042  -0.04216 252 CME A OH  
2054 C C   . CME A 258 ? 0.29350 0.42288 0.35240 -0.01105 0.05721  -0.06340 252 CME A C   
2055 O O   . CME A 258 ? 0.35830 0.43737 0.35289 -0.02080 0.04456  -0.05304 252 CME A O   
2056 N N   . ILE A 259 ? 0.19136 0.42279 0.34761 -0.02616 0.03947  -0.03211 253 ILE A N   
2057 C CA  . ILE A 259 ? 0.15794 0.43507 0.32874 -0.00662 -0.00119 -0.01087 253 ILE A CA  
2058 C C   . ILE A 259 ? 0.16453 0.46485 0.33109 -0.02105 0.02825  -0.01781 253 ILE A C   
2059 O O   . ILE A 259 ? 0.17289 0.48409 0.32856 -0.02556 0.03494  0.00626  253 ILE A O   
2060 C CB  . ILE A 259 ? 0.14679 0.40872 0.32081 -0.01259 0.01572  0.01699  253 ILE A CB  
2061 C CG1 . ILE A 259 ? 0.15042 0.38770 0.32064 0.02815  0.01671  0.04002  253 ILE A CG1 
2062 C CG2 . ILE A 259 ? 0.13575 0.40930 0.29994 -0.04319 0.00757  0.03118  253 ILE A CG2 
2063 C CD1 . ILE A 259 ? 0.17632 0.38733 0.31667 0.02241  0.06050  0.03418  253 ILE A CD1 
2064 N N   . ILE A 260 ? 0.15034 0.47908 0.32898 0.00046  0.01452  -0.01446 254 ILE A N   
2065 C CA  . ILE A 260 ? 0.15827 0.47832 0.33458 0.02743  -0.00467 -0.01273 254 ILE A CA  
2066 C C   . ILE A 260 ? 0.16449 0.44828 0.29795 0.04293  0.00236  -0.00824 254 ILE A C   
2067 O O   . ILE A 260 ? 0.16181 0.45322 0.33333 0.03386  0.02724  -0.00376 254 ILE A O   
2068 C CB  . ILE A 260 ? 0.21705 0.50959 0.38748 0.04232  -0.00690 -0.02273 254 ILE A CB  
2069 C CG1 . ILE A 260 ? 0.26774 0.52843 0.40991 0.05805  0.01278  -0.01721 254 ILE A CG1 
2070 C CG2 . ILE A 260 ? 0.24718 0.52097 0.42701 0.05184  0.01314  -0.02251 254 ILE A CG2 
2071 C CD1 . ILE A 260 ? 0.28842 0.54312 0.41671 0.05939  -0.00383 0.00236  254 ILE A CD1 
2072 N N   . ASN A 261 ? 0.22259 0.42088 0.26910 0.02755  0.00247  -0.00348 255 ASN A N   
2073 C CA  A ASN A 261 ? 0.23764 0.39866 0.24783 0.01352  -0.02193 -0.01076 255 ASN A CA  
2074 C CA  B ASN A 261 ? 0.25852 0.42199 0.25118 0.02933  -0.00441 -0.00247 255 ASN A CA  
2075 C C   . ASN A 261 ? 0.24230 0.41497 0.23973 0.02305  -0.01832 -0.01486 255 ASN A C   
2076 O O   . ASN A 261 ? 0.23050 0.41167 0.23826 0.03310  -0.02577 -0.02002 255 ASN A O   
2077 C CB  A ASN A 261 ? 0.24782 0.36633 0.25829 -0.02041 -0.04279 -0.01165 255 ASN A CB  
2078 C CB  B ASN A 261 ? 0.30686 0.43568 0.26846 0.02730  0.00764  0.01193  255 ASN A CB  
2079 C CG  A ASN A 261 ? 0.23863 0.33675 0.25482 -0.05139 -0.06930 -0.01612 255 ASN A CG  
2080 C CG  B ASN A 261 ? 0.33301 0.45200 0.27995 0.03342  0.01650  0.02459  255 ASN A CG  
2081 O OD1 A ASN A 261 ? 0.21649 0.31612 0.25105 -0.06074 -0.09957 -0.02513 255 ASN A OD1 
2082 O OD1 B ASN A 261 ? 0.33500 0.46048 0.29024 0.03399  0.00523  0.02802  255 ASN A OD1 
2083 N ND2 A ASN A 261 ? 0.23869 0.32365 0.25204 -0.05975 -0.07895 -0.02117 255 ASN A ND2 
2084 N ND2 B ASN A 261 ? 0.34582 0.45285 0.27387 0.04775  0.03640  0.02612  255 ASN A ND2 
2085 N N   . LEU A 262 ? 0.25328 0.43232 0.22726 0.01122  -0.00411 -0.03630 256 LEU A N   
2086 C CA  . LEU A 262 ? 0.22903 0.45757 0.25846 -0.01415 -0.00266 -0.02574 256 LEU A CA  
2087 C C   . LEU A 262 ? 0.17970 0.45467 0.22763 -0.02984 -0.01431 -0.03588 256 LEU A C   
2088 O O   . LEU A 262 ? 0.17936 0.47785 0.21902 -0.02663 -0.00852 -0.03571 256 LEU A O   
2089 C CB  . LEU A 262 ? 0.25746 0.48189 0.30380 -0.01476 0.00030  -0.00844 256 LEU A CB  
2090 C CG  . LEU A 262 ? 0.25102 0.49281 0.34322 -0.01702 0.01184  -0.00626 256 LEU A CG  
2091 C CD1 . LEU A 262 ? 0.28978 0.50154 0.38791 -0.03617 0.03148  -0.00212 256 LEU A CD1 
2092 C CD2 . LEU A 262 ? 0.23158 0.48347 0.29955 -0.00830 -0.02715 -0.02523 256 LEU A CD2 
2093 N N   . LYS A 263 ? 0.16350 0.43390 0.23921 -0.03514 -0.01074 -0.01623 257 LYS A N   
2094 C CA  . LYS A 263 ? 0.17650 0.42624 0.24166 -0.03920 -0.00283 0.00618  257 LYS A CA  
2095 C C   . LYS A 263 ? 0.16278 0.39438 0.22364 -0.02521 -0.01073 0.01800  257 LYS A C   
2096 O O   . LYS A 263 ? 0.14638 0.40959 0.24574 -0.02029 0.00038  0.01150  257 LYS A O   
2097 C CB  . LYS A 263 ? 0.22997 0.44461 0.25014 -0.06483 0.04632  0.00525  257 LYS A CB  
2098 C CG  . LYS A 263 ? 0.30757 0.45682 0.26308 -0.06822 0.06953  0.01276  257 LYS A CG  
2099 C CD  . LYS A 263 ? 0.34486 0.45934 0.26025 -0.06806 0.09155  0.01629  257 LYS A CD  
2100 C CE  . LYS A 263 ? 0.35870 0.45220 0.25657 -0.07244 0.09422  0.02190  257 LYS A CE  
2101 N NZ  . LYS A 263 ? 0.37379 0.44879 0.26256 -0.06432 0.09545  0.03939  257 LYS A NZ  
2102 N N   . ALA A 264 ? 0.15548 0.35232 0.20876 -0.03711 -0.02938 0.01280  258 ALA A N   
2103 C CA  . ALA A 264 ? 0.17592 0.32219 0.20221 -0.03538 -0.02339 0.02144  258 ALA A CA  
2104 C C   . ALA A 264 ? 0.17680 0.31275 0.21167 -0.01949 -0.00811 0.02005  258 ALA A C   
2105 O O   . ALA A 264 ? 0.13862 0.30601 0.22881 0.00881  0.00285  0.03268  258 ALA A O   
2106 C CB  . ALA A 264 ? 0.19462 0.31698 0.18170 -0.01964 -0.03504 0.01085  258 ALA A CB  
2107 N N   . ARG A 265 ? 0.18507 0.30581 0.18706 0.00023  -0.01536 0.03022  259 ARG A N   
2108 C CA  . ARG A 265 ? 0.21180 0.28033 0.18499 0.06019  0.00096  0.05780  259 ARG A CA  
2109 C C   . ARG A 265 ? 0.17772 0.26735 0.18954 0.03968  0.00055  0.04222  259 ARG A C   
2110 O O   . ARG A 265 ? 0.16999 0.25640 0.20683 0.03406  0.01912  0.03393  259 ARG A O   
2111 C CB  . ARG A 265 ? 0.24476 0.28055 0.18162 0.07205  -0.00666 0.04937  259 ARG A CB  
2112 C CG  . ARG A 265 ? 0.24091 0.29391 0.21211 0.07542  -0.02932 0.03333  259 ARG A CG  
2113 C CD  . ARG A 265 ? 0.20940 0.30914 0.23199 0.04806  -0.06660 0.00463  259 ARG A CD  
2114 N NE  . ARG A 265 ? 0.20720 0.31916 0.26389 0.01625  -0.03338 -0.00079 259 ARG A NE  
2115 C CZ  . ARG A 265 ? 0.21997 0.31789 0.27449 -0.02783 -0.01994 -0.00501 259 ARG A CZ  
2116 N NH1 . ARG A 265 ? 0.23199 0.31796 0.28507 -0.03281 -0.02188 0.01318  259 ARG A NH1 
2117 N NH2 . ARG A 265 ? 0.20512 0.32163 0.26749 -0.06554 -0.04024 -0.04491 259 ARG A NH2 
2118 N N   . ASN A 266 ? 0.18007 0.27714 0.20769 0.04274  -0.00149 0.01337  260 ASN A N   
2119 C CA  . ASN A 266 ? 0.14954 0.28288 0.21780 0.03872  -0.00502 0.01839  260 ASN A CA  
2120 C C   . ASN A 266 ? 0.16000 0.26467 0.20971 0.02312  0.00619  0.00580  260 ASN A C   
2121 O O   . ASN A 266 ? 0.17498 0.27021 0.20735 0.03618  0.01634  -0.00789 260 ASN A O   
2122 C CB  . ASN A 266 ? 0.12866 0.31672 0.22256 0.06271  -0.01169 0.02052  260 ASN A CB  
2123 C CG  . ASN A 266 ? 0.15377 0.32312 0.25892 0.05463  0.02965  0.01066  260 ASN A CG  
2124 O OD1 . ASN A 266 ? 0.17583 0.36171 0.27006 0.04497  0.03048  0.01430  260 ASN A OD1 
2125 N ND2 . ASN A 266 ? 0.12472 0.30233 0.26547 0.04716  0.02712  -0.02828 260 ASN A ND2 
2126 N N   . TYR A 267 ? 0.14515 0.24658 0.21117 0.04424  -0.00713 0.03389  261 TYR A N   
2127 C CA  . TYR A 267 ? 0.16002 0.25651 0.19177 0.04926  -0.00435 0.02744  261 TYR A CA  
2128 C C   . TYR A 267 ? 0.14565 0.24879 0.21504 0.03747  0.00965  0.02201  261 TYR A C   
2129 O O   . TYR A 267 ? 0.15667 0.24748 0.22660 0.04417  -0.00432 0.01620  261 TYR A O   
2130 C CB  . TYR A 267 ? 0.18049 0.24977 0.18346 0.04285  -0.02769 0.01785  261 TYR A CB  
2131 C CG  . TYR A 267 ? 0.19294 0.24145 0.18655 0.04046  -0.01765 0.01232  261 TYR A CG  
2132 C CD1 . TYR A 267 ? 0.19399 0.25387 0.22189 0.04824  -0.01899 0.02457  261 TYR A CD1 
2133 C CD2 . TYR A 267 ? 0.19970 0.22804 0.19719 0.04578  -0.01344 0.01060  261 TYR A CD2 
2134 C CE1 . TYR A 267 ? 0.21015 0.26130 0.23771 0.04768  -0.01278 0.03288  261 TYR A CE1 
2135 C CE2 . TYR A 267 ? 0.20327 0.23599 0.21597 0.03581  -0.01447 0.02280  261 TYR A CE2 
2136 C CZ  . TYR A 267 ? 0.19527 0.24760 0.23744 0.03594  -0.01088 0.03774  261 TYR A CZ  
2137 O OH  . TYR A 267 ? 0.21283 0.25170 0.26556 0.03205  0.01308  0.02604  261 TYR A OH  
2138 N N   . LEU A 268 ? 0.11913 0.24672 0.19207 0.02400  -0.01557 0.00512  262 LEU A N   
2139 C CA  . LEU A 268 ? 0.14302 0.22784 0.17527 0.00007  0.01286  -0.01720 262 LEU A CA  
2140 C C   . LEU A 268 ? 0.13550 0.21428 0.18083 0.02107  -0.01258 -0.01744 262 LEU A C   
2141 O O   . LEU A 268 ? 0.16568 0.23380 0.15945 0.01973  -0.00909 -0.02515 262 LEU A O   
2142 C CB  . LEU A 268 ? 0.15435 0.23498 0.17055 -0.00881 -0.00398 -0.05302 262 LEU A CB  
2143 C CG  . LEU A 268 ? 0.16520 0.25287 0.19706 -0.01690 -0.00098 -0.06638 262 LEU A CG  
2144 C CD1 . LEU A 268 ? 0.20806 0.26568 0.19230 -0.02528 -0.04210 -0.05575 262 LEU A CD1 
2145 C CD2 . LEU A 268 ? 0.17465 0.28240 0.22634 -0.00918 0.02535  -0.05176 262 LEU A CD2 
2146 N N   . LEU A 269 ? 0.14203 0.19939 0.19292 0.01748  -0.02193 0.00687  263 LEU A N   
2147 C CA  . LEU A 269 ? 0.14139 0.20457 0.20698 0.03942  -0.03220 -0.00128 263 LEU A CA  
2148 C C   . LEU A 269 ? 0.17294 0.23530 0.21493 0.03773  -0.01991 -0.01141 263 LEU A C   
2149 O O   . LEU A 269 ? 0.20173 0.25878 0.21920 0.02247  -0.00028 -0.02759 263 LEU A O   
2150 C CB  . LEU A 269 ? 0.15007 0.21340 0.21146 0.04481  -0.02475 0.00675  263 LEU A CB  
2151 C CG  . LEU A 269 ? 0.15106 0.20780 0.22920 0.04945  0.04772  0.02940  263 LEU A CG  
2152 C CD1 . LEU A 269 ? 0.15520 0.23587 0.26234 0.05971  0.08319  0.04426  263 LEU A CD1 
2153 C CD2 . LEU A 269 ? 0.19305 0.22742 0.22333 0.03781  0.03887  0.02536  263 LEU A CD2 
2154 N N   . SER A 270 ? 0.16815 0.22401 0.24035 0.04662  0.00383  0.02159  264 SER A N   
2155 C CA  . SER A 270 ? 0.21504 0.20703 0.22759 0.03029  -0.00259 0.00929  264 SER A CA  
2156 C C   . SER A 270 ? 0.21179 0.21749 0.24364 0.01707  -0.01133 -0.00288 264 SER A C   
2157 O O   . SER A 270 ? 0.23842 0.21719 0.26909 0.00237  0.00013  -0.02635 264 SER A O   
2158 C CB  . SER A 270 ? 0.25001 0.21857 0.23860 0.02854  0.01336  0.01834  264 SER A CB  
2159 O OG  . SER A 270 ? 0.27128 0.20596 0.24537 0.02733  0.02354  0.04634  264 SER A OG  
2160 N N   . LEU A 271 ? 0.17623 0.22080 0.23749 0.02876  -0.01196 0.01024  265 LEU A N   
2161 C CA  . LEU A 271 ? 0.22144 0.24044 0.20711 0.04345  0.00097  0.00431  265 LEU A CA  
2162 C C   . LEU A 271 ? 0.23309 0.23610 0.19902 0.05434  -0.00985 0.02263  265 LEU A C   
2163 O O   . LEU A 271 ? 0.23662 0.24634 0.20793 0.03742  -0.03284 0.04229  265 LEU A O   
2164 C CB  . LEU A 271 ? 0.18848 0.23454 0.18467 0.04640  -0.01702 -0.00010 265 LEU A CB  
2165 C CG  . LEU A 271 ? 0.23635 0.22859 0.19575 0.03292  -0.02377 -0.00105 265 LEU A CG  
2166 C CD1 . LEU A 271 ? 0.20981 0.24302 0.23226 0.02198  0.01787  0.01227  265 LEU A CD1 
2167 C CD2 . LEU A 271 ? 0.27805 0.22219 0.21718 0.01260  -0.00554 -0.03451 265 LEU A CD2 
2168 N N   . PRO A 272 ? 0.26950 0.23269 0.18280 0.05192  0.01413  -0.00422 266 PRO A N   
2169 C CA  . PRO A 272 ? 0.27132 0.24472 0.17451 0.03505  0.03905  -0.02045 266 PRO A CA  
2170 C C   . PRO A 272 ? 0.27000 0.28589 0.19144 -0.01182 0.04070  -0.00942 266 PRO A C   
2171 O O   . PRO A 272 ? 0.28920 0.29990 0.23635 -0.02614 0.04831  -0.01922 266 PRO A O   
2172 C CB  . PRO A 272 ? 0.32390 0.23815 0.20550 0.06959  0.06173  -0.00145 266 PRO A CB  
2173 C CG  . PRO A 272 ? 0.34912 0.24046 0.21757 0.07022  0.09506  -0.02085 266 PRO A CG  
2174 C CD  . PRO A 272 ? 0.29082 0.23295 0.17607 0.07371  0.03514  -0.01568 266 PRO A CD  
2175 N N   . HIS A 273 ? 0.25357 0.30246 0.18390 -0.04618 0.03630  0.01998  267 HIS A N   
2176 C CA  . HIS A 273 ? 0.29367 0.30578 0.17878 -0.05473 0.02994  0.01174  267 HIS A CA  
2177 C C   . HIS A 273 ? 0.27194 0.31783 0.22661 -0.04145 0.03803  -0.03320 267 HIS A C   
2178 O O   . HIS A 273 ? 0.31310 0.33198 0.26194 -0.04663 0.06790  -0.05425 267 HIS A O   
2179 C CB  . HIS A 273 ? 0.32522 0.29684 0.15289 -0.08237 0.04033  0.02151  267 HIS A CB  
2180 C CG  . HIS A 273 ? 0.34351 0.28228 0.17185 -0.10797 0.04224  0.01873  267 HIS A CG  
2181 N ND1 . HIS A 273 ? 0.34342 0.27452 0.17451 -0.08789 0.02782  0.03145  267 HIS A ND1 
2182 C CD2 . HIS A 273 ? 0.37493 0.28295 0.21437 -0.12657 0.07445  -0.00686 267 HIS A CD2 
2183 C CE1 . HIS A 273 ? 0.33781 0.26671 0.17735 -0.12202 0.03615  0.00880  267 HIS A CE1 
2184 N NE2 . HIS A 273 ? 0.37324 0.27871 0.21918 -0.14046 0.05630  0.00073  267 HIS A NE2 
2185 N N   . LYS A 274 ? 0.21304 0.32497 0.23033 -0.04587 0.00781  -0.03393 268 LYS A N   
2186 C CA  . LYS A 274 ? 0.23502 0.34090 0.25945 -0.02990 0.03284  -0.02943 268 LYS A CA  
2187 C C   . LYS A 274 ? 0.26741 0.36223 0.25575 -0.04122 0.05627  -0.04408 268 LYS A C   
2188 O O   . LYS A 274 ? 0.27542 0.35705 0.23554 -0.04610 0.03207  -0.04688 268 LYS A O   
2189 C CB  . LYS A 274 ? 0.22925 0.34029 0.25899 -0.02145 -0.01678 -0.01308 268 LYS A CB  
2190 C CG  . LYS A 274 ? 0.26295 0.35014 0.26675 -0.02684 -0.01479 -0.00907 268 LYS A CG  
2191 C CD  . LYS A 274 ? 0.26725 0.35681 0.28130 -0.04500 -0.02284 -0.00418 268 LYS A CD  
2192 C CE  . LYS A 274 ? 0.28668 0.35716 0.28581 -0.05608 -0.03347 -0.01505 268 LYS A CE  
2193 N NZ  . LYS A 274 ? 0.29262 0.35397 0.27240 -0.06877 -0.05088 -0.02761 268 LYS A NZ  
2194 N N   . ASN A 275 ? 0.27711 0.38216 0.24551 -0.06082 0.06634  -0.06134 269 ASN A N   
2195 C CA  . ASN A 275 ? 0.29630 0.40539 0.24731 -0.06848 0.05744  -0.06580 269 ASN A CA  
2196 C C   . ASN A 275 ? 0.26214 0.39306 0.25045 -0.06344 0.01640  -0.05568 269 ASN A C   
2197 O O   . ASN A 275 ? 0.27611 0.38575 0.28645 -0.04929 0.05297  -0.07273 269 ASN A O   
2198 C CB  . ASN A 275 ? 0.30279 0.42507 0.25209 -0.06703 0.06551  -0.07597 269 ASN A CB  
2199 C CG  . ASN A 275 ? 0.33482 0.43663 0.25531 -0.04168 0.06058  -0.07197 269 ASN A CG  
2200 O OD1 . ASN A 275 ? 0.38600 0.44577 0.28073 -0.03488 0.06245  -0.05818 269 ASN A OD1 
2201 N ND2 . ASN A 275 ? 0.29025 0.43750 0.27182 -0.01816 0.07673  -0.06879 269 ASN A ND2 
2202 N N   . LYS A 276 ? 0.25391 0.38638 0.26174 -0.06558 -0.00871 -0.03662 270 LYS A N   
2203 C CA  . LYS A 276 ? 0.24274 0.38833 0.28476 -0.05433 -0.00666 -0.03603 270 LYS A CA  
2204 C C   . LYS A 276 ? 0.21048 0.40194 0.27547 -0.01480 -0.00405 -0.01747 270 LYS A C   
2205 O O   . LYS A 276 ? 0.21940 0.41896 0.29529 0.01295  0.02394  -0.00033 270 LYS A O   
2206 C CB  . LYS A 276 ? 0.27582 0.38900 0.33856 -0.07803 -0.00357 -0.04295 270 LYS A CB  
2207 C CG  . LYS A 276 ? 0.32208 0.39853 0.39540 -0.08338 -0.00602 -0.06589 270 LYS A CG  
2208 C CD  . LYS A 276 ? 0.36426 0.41197 0.42555 -0.09322 -0.02982 -0.08851 270 LYS A CD  
2209 C CE  . LYS A 276 ? 0.39795 0.43359 0.45049 -0.07357 -0.05077 -0.08316 270 LYS A CE  
2210 N NZ  . LYS A 276 ? 0.40603 0.43373 0.45134 -0.06348 -0.07046 -0.09730 270 LYS A NZ  
2211 N N   . VAL A 277 ? 0.19379 0.40354 0.26629 0.01677  0.00423  0.00578  271 VAL A N   
2212 C CA  . VAL A 277 ? 0.19404 0.41922 0.25555 0.00713  0.00015  -0.00112 271 VAL A CA  
2213 C C   . VAL A 277 ? 0.22561 0.42277 0.22670 0.00436  -0.01639 -0.02508 271 VAL A C   
2214 O O   . VAL A 277 ? 0.24287 0.43218 0.23111 0.01534  -0.00606 -0.02735 271 VAL A O   
2215 C CB  . VAL A 277 ? 0.20736 0.42845 0.28205 0.00622  0.02345  0.00133  271 VAL A CB  
2216 C CG1 . VAL A 277 ? 0.22897 0.42440 0.29294 0.04078  0.05664  0.01252  271 VAL A CG1 
2217 C CG2 . VAL A 277 ? 0.25010 0.42933 0.28091 0.00668  0.04038  0.00026  271 VAL A CG2 
2218 N N   . PRO A 278 ? 0.25987 0.42503 0.20407 -0.02585 -0.00685 -0.03512 272 PRO A N   
2219 C CA  . PRO A 278 ? 0.26805 0.41102 0.20536 -0.04024 -0.00652 -0.05491 272 PRO A CA  
2220 C C   . PRO A 278 ? 0.25480 0.39124 0.22178 -0.03615 -0.01920 -0.06898 272 PRO A C   
2221 O O   . PRO A 278 ? 0.27003 0.39326 0.24778 -0.03620 0.00580  -0.07910 272 PRO A O   
2222 C CB  . PRO A 278 ? 0.29136 0.42778 0.23443 -0.04928 0.03099  -0.04181 272 PRO A CB  
2223 C CG  . PRO A 278 ? 0.29786 0.43280 0.23945 -0.06086 0.03309  -0.03775 272 PRO A CG  
2224 C CD  . PRO A 278 ? 0.29763 0.43319 0.20010 -0.05703 0.02114  -0.03531 272 PRO A CD  
2225 N N   . TRP A 279 ? 0.24354 0.37845 0.21892 -0.01510 -0.03509 -0.07605 273 TRP A N   
2226 C CA  . TRP A 279 ? 0.24217 0.37687 0.22088 -0.02284 -0.02662 -0.07501 273 TRP A CA  
2227 C C   . TRP A 279 ? 0.25773 0.41196 0.24238 -0.04786 0.01469  -0.06812 273 TRP A C   
2228 O O   . TRP A 279 ? 0.27547 0.40531 0.24131 -0.04987 0.03521  -0.07798 273 TRP A O   
2229 C CB  . TRP A 279 ? 0.27446 0.36211 0.23144 -0.03397 0.02501  -0.08258 273 TRP A CB  
2230 C CG  . TRP A 279 ? 0.25161 0.33878 0.23395 -0.04855 0.01785  -0.07086 273 TRP A CG  
2231 C CD1 . TRP A 279 ? 0.25740 0.32823 0.22919 -0.06062 0.00389  -0.06502 273 TRP A CD1 
2232 C CD2 . TRP A 279 ? 0.25568 0.32818 0.20386 -0.04686 0.02056  -0.05320 273 TRP A CD2 
2233 N NE1 . TRP A 279 ? 0.24916 0.33173 0.24357 -0.04002 0.01404  -0.05148 273 TRP A NE1 
2234 C CE2 . TRP A 279 ? 0.25131 0.32545 0.21357 -0.04341 0.02196  -0.04791 273 TRP A CE2 
2235 C CE3 . TRP A 279 ? 0.25365 0.33935 0.18874 -0.04765 0.00410  -0.05297 273 TRP A CE3 
2236 C CZ2 . TRP A 279 ? 0.26051 0.32633 0.20980 -0.02893 0.02198  -0.05699 273 TRP A CZ2 
2237 C CZ3 . TRP A 279 ? 0.25150 0.34535 0.21067 -0.04042 -0.00332 -0.05349 273 TRP A CZ3 
2238 C CH2 . TRP A 279 ? 0.26190 0.33544 0.21418 -0.04033 0.02587  -0.06427 273 TRP A CH2 
2239 N N   . ASN A 280 ? 0.24680 0.44518 0.27025 -0.06726 0.02054  -0.06545 274 ASN A N   
2240 C CA  . ASN A 280 ? 0.26456 0.46761 0.29133 -0.04272 0.02391  -0.06255 274 ASN A CA  
2241 C C   . ASN A 280 ? 0.25312 0.46614 0.30961 -0.02190 0.01387  -0.08050 274 ASN A C   
2242 O O   . ASN A 280 ? 0.24507 0.46119 0.33022 -0.03601 0.02332  -0.09351 274 ASN A O   
2243 C CB  . ASN A 280 ? 0.32804 0.50969 0.31337 -0.05321 0.06904  -0.04395 274 ASN A CB  
2244 C CG  . ASN A 280 ? 0.40704 0.54431 0.34098 -0.05671 0.11352  -0.01334 274 ASN A CG  
2245 O OD1 . ASN A 280 ? 0.45677 0.55263 0.32834 -0.06203 0.11495  -0.01172 274 ASN A OD1 
2246 N ND2 . ASN A 280 ? 0.46431 0.56165 0.37131 -0.04586 0.12410  0.01562  274 ASN A ND2 
2247 N N   . ARG A 281 ? 0.25396 0.46121 0.31048 -0.00857 -0.00099 -0.09523 275 ARG A N   
2248 C CA  . ARG A 281 ? 0.27890 0.46714 0.34191 -0.00702 -0.01079 -0.12266 275 ARG A CA  
2249 C C   . ARG A 281 ? 0.27631 0.44588 0.35451 -0.01449 0.03285  -0.13519 275 ARG A C   
2250 O O   . ARG A 281 ? 0.29001 0.44981 0.36621 -0.01126 0.05138  -0.15817 275 ARG A O   
2251 C CB  . ARG A 281 ? 0.28805 0.48714 0.38216 -0.01082 -0.02338 -0.12975 275 ARG A CB  
2252 C CG  . ARG A 281 ? 0.32917 0.51685 0.41910 -0.00530 -0.02659 -0.12796 275 ARG A CG  
2253 C CD  . ARG A 281 ? 0.36079 0.53878 0.46092 -0.01304 -0.02510 -0.13315 275 ARG A CD  
2254 N NE  . ARG A 281 ? 0.38327 0.55299 0.49513 0.00078  -0.01541 -0.12694 275 ARG A NE  
2255 C CZ  . ARG A 281 ? 0.37479 0.55618 0.51042 0.00599  -0.03786 -0.12456 275 ARG A CZ  
2256 N NH1 . ARG A 281 ? 0.38459 0.56288 0.51071 0.00645  -0.04598 -0.12472 275 ARG A NH1 
2257 N NH2 . ARG A 281 ? 0.36731 0.55387 0.52437 0.01696  -0.03203 -0.12100 275 ARG A NH2 
2258 N N   . LEU A 282 ? 0.24448 0.42654 0.33931 -0.03712 0.04116  -0.12440 276 LEU A N   
2259 C CA  . LEU A 282 ? 0.28592 0.40238 0.36473 -0.03155 0.04455  -0.10474 276 LEU A CA  
2260 C C   . LEU A 282 ? 0.31423 0.38874 0.34756 -0.03033 0.02162  -0.09614 276 LEU A C   
2261 O O   . LEU A 282 ? 0.35812 0.37558 0.37818 -0.01463 0.03534  -0.07508 276 LEU A O   
2262 C CB  . LEU A 282 ? 0.34097 0.40094 0.40054 -0.01656 0.05978  -0.08798 276 LEU A CB  
2263 C CG  . LEU A 282 ? 0.40190 0.39662 0.44826 -0.02649 0.08828  -0.07935 276 LEU A CG  
2264 C CD1 . LEU A 282 ? 0.43184 0.40140 0.47511 -0.02795 0.12166  -0.08054 276 LEU A CD1 
2265 C CD2 . LEU A 282 ? 0.43033 0.38678 0.45125 -0.03708 0.09568  -0.07200 276 LEU A CD2 
2266 N N   . PHE A 283 ? 0.26460 0.38186 0.30261 -0.06588 -0.00640 -0.10578 277 PHE A N   
2267 C CA  . PHE A 283 ? 0.23854 0.37753 0.30152 -0.03563 0.00528  -0.09448 277 PHE A CA  
2268 C C   . PHE A 283 ? 0.24904 0.38854 0.31574 -0.02236 0.00933  -0.11207 277 PHE A C   
2269 O O   . PHE A 283 ? 0.25272 0.38549 0.32134 -0.01864 0.02437  -0.10514 277 PHE A O   
2270 C CB  . PHE A 283 ? 0.24014 0.37030 0.25382 -0.03488 -0.00058 -0.07235 277 PHE A CB  
2271 C CG  . PHE A 283 ? 0.25563 0.35952 0.24938 -0.00652 0.01342  -0.04045 277 PHE A CG  
2272 C CD1 . PHE A 283 ? 0.27629 0.36546 0.26962 0.00833  0.02565  -0.02178 277 PHE A CD1 
2273 C CD2 . PHE A 283 ? 0.24691 0.33525 0.23560 0.01808  0.03565  -0.05673 277 PHE A CD2 
2274 C CE1 . PHE A 283 ? 0.26494 0.35723 0.26811 0.02195  0.02232  -0.02167 277 PHE A CE1 
2275 C CE2 . PHE A 283 ? 0.26703 0.33352 0.22949 0.01221  0.00379  -0.05279 277 PHE A CE2 
2276 C CZ  . PHE A 283 ? 0.25670 0.34581 0.23521 0.01304  -0.02480 -0.04373 277 PHE A CZ  
2277 N N   . PRO A 284 ? 0.25991 0.40489 0.35933 -0.02351 0.00941  -0.13962 278 PRO A N   
2278 C CA  . PRO A 284 ? 0.27556 0.42865 0.36745 -0.00681 0.04564  -0.14281 278 PRO A CA  
2279 C C   . PRO A 284 ? 0.27224 0.45924 0.38881 0.00884  0.05857  -0.11671 278 PRO A C   
2280 O O   . PRO A 284 ? 0.29487 0.48425 0.39905 0.00489  0.09475  -0.09977 278 PRO A O   
2281 C CB  . PRO A 284 ? 0.31473 0.42321 0.38415 -0.00427 0.06502  -0.14404 278 PRO A CB  
2282 C CG  . PRO A 284 ? 0.31853 0.42057 0.37578 -0.00608 0.07633  -0.14122 278 PRO A CG  
2283 C CD  . PRO A 284 ? 0.30205 0.41120 0.38875 0.00348  0.05808  -0.13061 278 PRO A CD  
2284 N N   . ASN A 285 ? 0.24372 0.46255 0.37245 0.01535  0.00585  -0.12210 279 ASN A N   
2285 C CA  . ASN A 285 ? 0.26516 0.47002 0.40963 0.01570  0.02455  -0.11524 279 ASN A CA  
2286 C C   . ASN A 285 ? 0.25397 0.45844 0.37938 0.01590  0.04269  -0.12339 279 ASN A C   
2287 O O   . ASN A 285 ? 0.28744 0.45179 0.40010 -0.00148 0.06718  -0.13872 279 ASN A O   
2288 C CB  . ASN A 285 ? 0.29285 0.49614 0.43707 0.01525  0.00814  -0.08903 279 ASN A CB  
2289 C CG  . ASN A 285 ? 0.36800 0.52419 0.46182 0.02991  0.03015  -0.06308 279 ASN A CG  
2290 O OD1 . ASN A 285 ? 0.40686 0.53450 0.46103 0.03033  0.03796  -0.05913 279 ASN A OD1 
2291 N ND2 . ASN A 285 ? 0.35687 0.53384 0.46482 0.04372  0.01787  -0.05655 279 ASN A ND2 
2292 N N   . ALA A 286 ? 0.22939 0.44813 0.33439 0.04630  0.05827  -0.09225 280 ALA A N   
2293 C CA  . ALA A 286 ? 0.22190 0.44688 0.29692 0.01923  0.07835  -0.07733 280 ALA A CA  
2294 C C   . ALA A 286 ? 0.23891 0.44124 0.27465 -0.00274 0.07664  -0.06348 280 ALA A C   
2295 O O   . ALA A 286 ? 0.25221 0.44958 0.25505 -0.02710 0.07877  -0.06590 280 ALA A O   
2296 C CB  . ALA A 286 ? 0.18662 0.45002 0.29402 0.03341  0.05485  -0.08030 280 ALA A CB  
2297 N N   . ASP A 287 ? 0.22168 0.41960 0.27471 -0.01537 0.05604  -0.05190 281 ASP A N   
2298 C CA  . ASP A 287 ? 0.22631 0.41129 0.24929 -0.03296 0.05186  -0.03632 281 ASP A CA  
2299 C C   . ASP A 287 ? 0.24133 0.39778 0.20204 -0.03648 0.05719  -0.02488 281 ASP A C   
2300 O O   . ASP A 287 ? 0.24673 0.38756 0.19313 -0.04692 0.06822  -0.04276 281 ASP A O   
2301 C CB  . ASP A 287 ? 0.17885 0.41615 0.27200 -0.04591 0.00368  -0.05156 281 ASP A CB  
2302 C CG  . ASP A 287 ? 0.18731 0.42628 0.33823 -0.05791 0.00532  -0.05472 281 ASP A CG  
2303 O OD1 . ASP A 287 ? 0.21521 0.43233 0.34548 -0.07558 -0.00196 -0.06090 281 ASP A OD1 
2304 O OD2 . ASP A 287 ? 0.22851 0.43710 0.39845 -0.05183 0.02530  -0.04087 281 ASP A OD2 
2305 N N   . SER A 288 ? 0.26187 0.39662 0.21364 -0.02043 0.06501  0.00905  282 SER A N   
2306 C CA  . SER A 288 ? 0.27357 0.39824 0.18967 -0.04045 0.05677  0.01457  282 SER A CA  
2307 C C   . SER A 288 ? 0.24406 0.37026 0.17123 -0.04210 0.05203  0.02083  282 SER A C   
2308 O O   . SER A 288 ? 0.24012 0.36982 0.17165 -0.04249 0.04023  0.03414  282 SER A O   
2309 C CB  . SER A 288 ? 0.33617 0.42613 0.22238 -0.05931 0.06778  0.01360  282 SER A CB  
2310 O OG  . SER A 288 ? 0.38002 0.46038 0.25134 -0.03796 0.07432  0.01849  282 SER A OG  
2311 N N   . LYS A 289 ? 0.23091 0.34885 0.17806 -0.03992 0.06153  0.02142  283 LYS A N   
2312 C CA  . LYS A 289 ? 0.24684 0.31558 0.18502 -0.04713 0.05025  0.01585  283 LYS A CA  
2313 C C   . LYS A 289 ? 0.22742 0.29547 0.18515 -0.02737 0.04621  0.01661  283 LYS A C   
2314 O O   . LYS A 289 ? 0.23919 0.29021 0.18146 -0.03332 0.04825  -0.00494 283 LYS A O   
2315 C CB  . LYS A 289 ? 0.25851 0.31378 0.17822 -0.08275 0.01904  -0.00141 283 LYS A CB  
2316 C CG  . LYS A 289 ? 0.30185 0.32474 0.21501 -0.09571 0.02403  -0.00128 283 LYS A CG  
2317 C CD  . LYS A 289 ? 0.34795 0.34105 0.26074 -0.10499 0.05150  0.01489  283 LYS A CD  
2318 C CE  . LYS A 289 ? 0.38021 0.35519 0.29152 -0.11473 0.06165  0.03756  283 LYS A CE  
2319 N NZ  . LYS A 289 ? 0.41682 0.37560 0.30204 -0.10855 0.08497  0.03779  283 LYS A NZ  
2320 N N   . ALA A 290 ? 0.18312 0.27890 0.19410 -0.03869 0.00674  0.02581  284 ALA A N   
2321 C CA  . ALA A 290 ? 0.16828 0.27499 0.18923 -0.02385 0.01504  0.03970  284 ALA A CA  
2322 C C   . ALA A 290 ? 0.19128 0.26619 0.17739 -0.02663 0.01634  0.02939  284 ALA A C   
2323 O O   . ALA A 290 ? 0.19803 0.25333 0.18900 -0.00452 0.03235  0.03836  284 ALA A O   
2324 C CB  . ALA A 290 ? 0.15262 0.26266 0.20175 -0.00567 0.01362  0.04763  284 ALA A CB  
2325 N N   . LEU A 291 ? 0.19922 0.27109 0.17160 -0.04521 0.00544  -0.01487 285 LEU A N   
2326 C CA  . LEU A 291 ? 0.18535 0.28271 0.15817 -0.03286 -0.00109 -0.02183 285 LEU A CA  
2327 C C   . LEU A 291 ? 0.20211 0.27583 0.17275 -0.02416 0.01684  -0.00620 285 LEU A C   
2328 O O   . LEU A 291 ? 0.19268 0.28417 0.20940 -0.03153 0.03341  0.00390  285 LEU A O   
2329 C CB  . LEU A 291 ? 0.19692 0.30208 0.17398 -0.03116 0.02047  -0.01784 285 LEU A CB  
2330 C CG  . LEU A 291 ? 0.21189 0.30527 0.18447 -0.03381 0.05453  -0.01562 285 LEU A CG  
2331 C CD1 . LEU A 291 ? 0.20651 0.30405 0.18784 -0.04503 0.06453  -0.04676 285 LEU A CD1 
2332 C CD2 . LEU A 291 ? 0.20901 0.31001 0.21423 -0.03897 0.04411  0.00367  285 LEU A CD2 
2333 N N   . ASP A 292 ? 0.20939 0.26132 0.17618 0.00673  0.02828  -0.00436 286 ASP A N   
2334 C CA  . ASP A 292 ? 0.22440 0.26801 0.17104 0.02371  0.03107  0.01755  286 ASP A CA  
2335 C C   . ASP A 292 ? 0.20159 0.26266 0.16946 0.00974  0.02887  0.00416  286 ASP A C   
2336 O O   . ASP A 292 ? 0.18267 0.29616 0.17558 0.00261  0.01224  -0.01625 286 ASP A O   
2337 C CB  . ASP A 292 ? 0.27680 0.28815 0.19955 0.02394  0.03526  0.02207  286 ASP A CB  
2338 C CG  . ASP A 292 ? 0.31227 0.31741 0.19708 0.02184  -0.03905 0.01137  286 ASP A CG  
2339 O OD1 . ASP A 292 ? 0.34663 0.34487 0.24781 0.04228  -0.06086 0.00470  286 ASP A OD1 
2340 O OD2 . ASP A 292 ? 0.31715 0.32410 0.18901 0.00369  -0.03796 0.00664  286 ASP A OD2 
2341 N N   . LEU A 293 ? 0.20505 0.23088 0.14585 -0.02459 0.01991  -0.00078 287 LEU A N   
2342 C CA  . LEU A 293 ? 0.19174 0.21269 0.13966 -0.02506 0.00193  -0.01114 287 LEU A CA  
2343 C C   . LEU A 293 ? 0.18429 0.21373 0.17956 0.01575  0.02206  -0.00410 287 LEU A C   
2344 O O   . LEU A 293 ? 0.19098 0.22014 0.19195 0.02819  0.01631  -0.00663 287 LEU A O   
2345 C CB  . LEU A 293 ? 0.21455 0.20497 0.15226 -0.01678 0.02157  0.00824  287 LEU A CB  
2346 C CG  . LEU A 293 ? 0.22064 0.18871 0.16276 -0.01251 0.04522  0.00304  287 LEU A CG  
2347 C CD1 . LEU A 293 ? 0.19115 0.18750 0.19015 -0.00728 0.05779  0.00743  287 LEU A CD1 
2348 C CD2 . LEU A 293 ? 0.25170 0.19668 0.15295 -0.01815 0.01871  -0.00997 287 LEU A CD2 
2349 N N   . LEU A 294 ? 0.17018 0.19380 0.19215 0.01210  0.01198  -0.00032 288 LEU A N   
2350 C CA  . LEU A 294 ? 0.14892 0.18611 0.17755 0.02074  0.00500  0.00842  288 LEU A CA  
2351 C C   . LEU A 294 ? 0.14856 0.20257 0.16362 0.00091  0.00406  0.01975  288 LEU A C   
2352 O O   . LEU A 294 ? 0.17012 0.22948 0.17020 -0.00052 0.02388  0.01452  288 LEU A O   
2353 C CB  . LEU A 294 ? 0.17742 0.18365 0.18136 0.02967  0.03003  0.00310  288 LEU A CB  
2354 C CG  . LEU A 294 ? 0.19657 0.19366 0.13947 0.01307  0.03498  -0.00015 288 LEU A CG  
2355 C CD1 . LEU A 294 ? 0.20446 0.19770 0.12415 0.01044  0.00498  0.03298  288 LEU A CD1 
2356 C CD2 . LEU A 294 ? 0.20466 0.20828 0.16671 0.03062  0.05302  -0.03803 288 LEU A CD2 
2357 N N   . ASP A 295 ? 0.13984 0.19583 0.15744 0.00861  -0.01578 0.00086  289 ASP A N   
2358 C CA  . ASP A 295 ? 0.15411 0.23358 0.15409 0.04427  -0.01665 0.00685  289 ASP A CA  
2359 C C   . ASP A 295 ? 0.19705 0.22764 0.18639 0.02981  0.00372  -0.01243 289 ASP A C   
2360 O O   . ASP A 295 ? 0.16288 0.22810 0.19991 0.03288  0.01700  -0.02940 289 ASP A O   
2361 C CB  . ASP A 295 ? 0.19511 0.28365 0.19027 0.08875  -0.03193 0.02200  289 ASP A CB  
2362 C CG  . ASP A 295 ? 0.25397 0.31713 0.24460 0.08883  -0.01971 0.00631  289 ASP A CG  
2363 O OD1 . ASP A 295 ? 0.25805 0.33015 0.28698 0.05087  -0.02484 -0.03233 289 ASP A OD1 
2364 O OD2 . ASP A 295 ? 0.31678 0.35421 0.27515 0.11691  0.01769  0.02468  289 ASP A OD2 
2365 N N   . LYS A 296 ? 0.20976 0.20825 0.17067 0.02298  -0.02177 -0.00747 290 LYS A N   
2366 C CA  . LYS A 296 ? 0.21879 0.21504 0.17192 0.00704  -0.01015 0.02373  290 LYS A CA  
2367 C C   . LYS A 296 ? 0.20222 0.23653 0.17935 0.00762  -0.00345 0.01313  290 LYS A C   
2368 O O   . LYS A 296 ? 0.20134 0.26820 0.19118 -0.00033 -0.00993 -0.01803 290 LYS A O   
2369 C CB  . LYS A 296 ? 0.25535 0.20214 0.17727 0.00904  -0.00064 0.05139  290 LYS A CB  
2370 C CG  . LYS A 296 ? 0.28275 0.22919 0.18576 0.00884  0.02070  0.05353  290 LYS A CG  
2371 C CD  A LYS A 296 ? 0.28381 0.23826 0.18371 0.00101  0.02397  0.07979  290 LYS A CD  
2372 C CD  B LYS A 296 ? 0.31530 0.25166 0.23538 0.01657  0.03913  0.06919  290 LYS A CD  
2373 C CE  A LYS A 296 ? 0.28496 0.24149 0.16869 -0.01031 0.03916  0.09426  290 LYS A CE  
2374 C CE  B LYS A 296 ? 0.35099 0.27473 0.27477 0.01253  0.07598  0.06943  290 LYS A CE  
2375 N NZ  A LYS A 296 ? 0.27721 0.25150 0.13659 -0.01685 0.00348  0.08551  290 LYS A NZ  
2376 N NZ  B LYS A 296 ? 0.37404 0.29311 0.30077 0.02266  0.07826  0.06108  290 LYS A NZ  
2377 N N   . MET A 297 ? 0.17162 0.22812 0.14677 0.01110  -0.03404 0.05273  291 MET A N   
2378 C CA  . MET A 297 ? 0.14161 0.22967 0.12122 -0.00571 -0.00930 0.01707  291 MET A CA  
2379 C C   . MET A 297 ? 0.12174 0.22513 0.14333 -0.01260 0.02060  -0.00168 291 MET A C   
2380 O O   . MET A 297 ? 0.15616 0.21989 0.18036 -0.02611 0.05656  -0.03062 291 MET A O   
2381 C CB  A MET A 297 ? 0.12326 0.23270 0.14312 -0.01420 -0.00732 0.01969  291 MET A CB  
2382 C CB  B MET A 297 ? 0.12629 0.22910 0.12862 0.00032  -0.00204 0.02100  291 MET A CB  
2383 C CG  A MET A 297 ? 0.13514 0.25231 0.18673 -0.01047 -0.02290 0.01193  291 MET A CG  
2384 C CG  B MET A 297 ? 0.13483 0.24265 0.15302 0.01617  -0.01951 0.01602  291 MET A CG  
2385 S SD  A MET A 297 ? 0.15844 0.26982 0.23027 -0.00355 -0.00526 0.00168  291 MET A SD  
2386 S SD  B MET A 297 ? 0.14547 0.25106 0.17493 0.03035  -0.01379 0.01063  291 MET A SD  
2387 C CE  A MET A 297 ? 0.14956 0.26717 0.22948 -0.02953 0.01993  -0.00429 291 MET A CE  
2388 C CE  B MET A 297 ? 0.16725 0.25168 0.17478 -0.00164 -0.02205 -0.00515 291 MET A CE  
2389 N N   . LEU A 298 ? 0.12688 0.22496 0.16696 -0.00987 -0.01586 -0.00609 292 LEU A N   
2390 C CA  . LEU A 298 ? 0.15845 0.21828 0.16447 0.02392  -0.01956 -0.00359 292 LEU A CA  
2391 C C   . LEU A 298 ? 0.19118 0.24307 0.21068 0.03981  -0.00865 -0.00267 292 LEU A C   
2392 O O   . LEU A 298 ? 0.21726 0.26679 0.27239 0.05818  -0.07609 -0.01844 292 LEU A O   
2393 C CB  . LEU A 298 ? 0.15458 0.21776 0.14922 0.02156  -0.00200 -0.00658 292 LEU A CB  
2394 C CG  . LEU A 298 ? 0.14707 0.21246 0.14173 0.03663  0.01583  -0.00797 292 LEU A CG  
2395 C CD1 . LEU A 298 ? 0.18501 0.21226 0.15154 0.02744  0.02400  -0.02534 292 LEU A CD1 
2396 C CD2 . LEU A 298 ? 0.12816 0.22835 0.14438 0.02132  0.00261  -0.00709 292 LEU A CD2 
2397 N N   . THR A 299 ? 0.15465 0.24715 0.20624 0.04833  0.00251  0.01257  293 THR A N   
2398 C CA  A THR A 299 ? 0.16743 0.24948 0.18027 0.05676  -0.02317 0.00849  293 THR A CA  
2399 C CA  B THR A 299 ? 0.20069 0.25968 0.21042 0.04185  0.00341  0.00909  293 THR A CA  
2400 C C   . THR A 299 ? 0.15341 0.26368 0.18129 0.04169  -0.04163 -0.00635 293 THR A C   
2401 O O   . THR A 299 ? 0.17995 0.27321 0.17313 0.01441  -0.03054 0.01165  293 THR A O   
2402 C CB  A THR A 299 ? 0.15935 0.24235 0.15653 0.05460  -0.02984 -0.00487 293 THR A CB  
2403 C CB  B THR A 299 ? 0.26392 0.27397 0.25324 0.01495  0.05840  -0.00254 293 THR A CB  
2404 O OG1 A THR A 299 ? 0.15838 0.25566 0.18054 0.06821  -0.03848 0.02088  293 THR A OG1 
2405 O OG1 B THR A 299 ? 0.29869 0.27295 0.29580 -0.00956 0.07814  0.00116  293 THR A OG1 
2406 C CG2 A THR A 299 ? 0.13169 0.20530 0.14050 0.05673  -0.06046 -0.00149 293 THR A CG2 
2407 C CG2 B THR A 299 ? 0.27267 0.28609 0.26580 0.02713  0.04823  0.00599  293 THR A CG2 
2408 N N   . PHE A 300 ? 0.12136 0.27357 0.21189 0.02161  -0.05447 -0.01977 294 PHE A N   
2409 C CA  . PHE A 300 ? 0.13228 0.30896 0.20338 0.00753  -0.01458 -0.04075 294 PHE A CA  
2410 C C   . PHE A 300 ? 0.14311 0.31479 0.19606 0.02541  0.00449  -0.04070 294 PHE A C   
2411 O O   . PHE A 300 ? 0.18045 0.32076 0.19479 0.04473  0.00983  -0.03444 294 PHE A O   
2412 C CB  . PHE A 300 ? 0.14513 0.33012 0.19883 -0.02942 -0.01072 -0.02683 294 PHE A CB  
2413 C CG  . PHE A 300 ? 0.21950 0.36317 0.19220 -0.05694 -0.03111 -0.00318 294 PHE A CG  
2414 C CD1 . PHE A 300 ? 0.24941 0.37037 0.17936 -0.07932 -0.04685 0.00339  294 PHE A CD1 
2415 C CD2 . PHE A 300 ? 0.24537 0.37829 0.19723 -0.05792 -0.02853 0.00451  294 PHE A CD2 
2416 C CE1 . PHE A 300 ? 0.26616 0.38478 0.18668 -0.07112 -0.01785 0.01702  294 PHE A CE1 
2417 C CE2 . PHE A 300 ? 0.26343 0.38794 0.18247 -0.06223 -0.05753 0.03050  294 PHE A CE2 
2418 C CZ  . PHE A 300 ? 0.28080 0.38792 0.17742 -0.06864 -0.04239 0.03277  294 PHE A CZ  
2419 N N   . ASN A 301 ? 0.12283 0.31872 0.20312 0.04184  0.00781  -0.02376 295 ASN A N   
2420 C CA  . ASN A 301 ? 0.16327 0.33137 0.18786 0.03828  -0.02004 -0.02794 295 ASN A CA  
2421 C C   . ASN A 301 ? 0.15367 0.33645 0.18770 0.00777  -0.00259 -0.02996 295 ASN A C   
2422 O O   . ASN A 301 ? 0.14795 0.32756 0.21620 0.00320  0.02194  -0.01365 295 ASN A O   
2423 C CB  . ASN A 301 ? 0.18167 0.35350 0.23091 0.07166  -0.03411 -0.03834 295 ASN A CB  
2424 C CG  . ASN A 301 ? 0.20200 0.38394 0.25650 0.09176  -0.03070 -0.04168 295 ASN A CG  
2425 O OD1 . ASN A 301 ? 0.22228 0.40595 0.28471 0.09221  -0.04083 -0.07251 295 ASN A OD1 
2426 N ND2 . ASN A 301 ? 0.19047 0.38821 0.25343 0.11523  -0.04140 -0.02670 295 ASN A ND2 
2427 N N   . PRO A 302 ? 0.13923 0.33812 0.15353 -0.00562 -0.00186 -0.06495 296 PRO A N   
2428 C CA  . PRO A 302 ? 0.16579 0.34750 0.13645 0.00631  0.00491  -0.05287 296 PRO A CA  
2429 C C   . PRO A 302 ? 0.16872 0.34906 0.17097 0.03396  -0.02574 -0.05275 296 PRO A C   
2430 O O   . PRO A 302 ? 0.16733 0.36436 0.24843 0.04331  -0.03407 -0.01736 296 PRO A O   
2431 C CB  . PRO A 302 ? 0.17645 0.35339 0.16414 -0.01537 0.01725  -0.04121 296 PRO A CB  
2432 C CG  . PRO A 302 ? 0.13517 0.35715 0.16061 0.00208  -0.00582 -0.04380 296 PRO A CG  
2433 C CD  . PRO A 302 ? 0.14059 0.35246 0.17107 0.00747  0.04672  -0.06948 296 PRO A CD  
2434 N N   . HIS A 303 ? 0.16657 0.34551 0.20717 0.06150  -0.01891 -0.04586 297 HIS A N   
2435 C CA  . HIS A 303 ? 0.18770 0.34044 0.25020 0.09249  -0.02143 -0.01937 297 HIS A CA  
2436 C C   . HIS A 303 ? 0.25179 0.31075 0.27451 0.07884  -0.00996 0.00423  297 HIS A C   
2437 O O   . HIS A 303 ? 0.32509 0.30072 0.32892 0.07418  0.03650  -0.00853 297 HIS A O   
2438 C CB  . HIS A 303 ? 0.20006 0.38425 0.28851 0.08015  -0.00618 -0.02730 297 HIS A CB  
2439 C CG  . HIS A 303 ? 0.23513 0.41800 0.33882 0.07006  0.03959  -0.02272 297 HIS A CG  
2440 N ND1 . HIS A 303 ? 0.27247 0.44162 0.37027 0.07758  0.08837  -0.01786 297 HIS A ND1 
2441 C CD2 . HIS A 303 ? 0.25055 0.43593 0.35641 0.05991  0.06205  -0.01334 297 HIS A CD2 
2442 C CE1 . HIS A 303 ? 0.27392 0.45026 0.37494 0.06417  0.10445  -0.02343 297 HIS A CE1 
2443 N NE2 . HIS A 303 ? 0.27287 0.45127 0.37801 0.05475  0.09818  -0.02341 297 HIS A NE2 
2444 N N   . LYS A 304 ? 0.21131 0.29885 0.21987 0.07343  -0.03728 0.02604  298 LYS A N   
2445 C CA  . LYS A 304 ? 0.18496 0.30677 0.24033 0.04751  -0.05073 0.00772  298 LYS A CA  
2446 C C   . LYS A 304 ? 0.16660 0.27017 0.24506 0.04657  -0.04013 0.02074  298 LYS A C   
2447 O O   . LYS A 304 ? 0.16385 0.27187 0.27785 0.06886  -0.03007 0.03565  298 LYS A O   
2448 C CB  . LYS A 304 ? 0.18584 0.35055 0.24389 0.03087  -0.09279 0.00871  298 LYS A CB  
2449 C CG  . LYS A 304 ? 0.21537 0.39003 0.26512 0.00631  -0.08687 0.00017  298 LYS A CG  
2450 C CD  . LYS A 304 ? 0.20985 0.40545 0.26244 -0.00909 -0.11984 -0.00925 298 LYS A CD  
2451 C CE  . LYS A 304 ? 0.22758 0.40148 0.26896 -0.02869 -0.13803 -0.02902 298 LYS A CE  
2452 N NZ  . LYS A 304 ? 0.23595 0.40741 0.29767 -0.05238 -0.14054 -0.04474 298 LYS A NZ  
2453 N N   . ARG A 305 ? 0.17402 0.23829 0.24048 0.05000  -0.03050 0.03101  299 ARG A N   
2454 C CA  . ARG A 305 ? 0.14635 0.21198 0.18789 0.04416  -0.06163 0.04923  299 ARG A CA  
2455 C C   . ARG A 305 ? 0.16866 0.18862 0.22376 0.01645  -0.02895 0.03321  299 ARG A C   
2456 O O   . ARG A 305 ? 0.21646 0.19969 0.25012 -0.01712 -0.02033 -0.00642 299 ARG A O   
2457 C CB  . ARG A 305 ? 0.11839 0.20362 0.20768 0.05085  -0.03248 0.05470  299 ARG A CB  
2458 C CG  . ARG A 305 ? 0.10268 0.21232 0.21115 0.03131  -0.00446 0.04976  299 ARG A CG  
2459 C CD  . ARG A 305 ? 0.11865 0.22438 0.15601 -0.00155 0.00060  0.03901  299 ARG A CD  
2460 N NE  . ARG A 305 ? 0.12701 0.22808 0.15355 -0.02375 -0.00422 0.00874  299 ARG A NE  
2461 C CZ  . ARG A 305 ? 0.13921 0.23223 0.14080 -0.01743 0.00529  -0.00190 299 ARG A CZ  
2462 N NH1 . ARG A 305 ? 0.15503 0.25231 0.13972 -0.00391 -0.00315 -0.02781 299 ARG A NH1 
2463 N NH2 . ARG A 305 ? 0.12748 0.23030 0.15616 -0.02458 0.01391  -0.02236 299 ARG A NH2 
2464 N N   . ILE A 306 ? 0.15054 0.17376 0.19748 0.00123  -0.01863 0.04559  300 ILE A N   
2465 C CA  . ILE A 306 ? 0.17186 0.18046 0.19269 0.00190  -0.00891 0.01136  300 ILE A CA  
2466 C C   . ILE A 306 ? 0.20005 0.17802 0.19162 0.01655  0.01493  -0.00461 300 ILE A C   
2467 O O   . ILE A 306 ? 0.19612 0.19360 0.19562 0.03139  0.01770  -0.00861 300 ILE A O   
2468 C CB  . ILE A 306 ? 0.16540 0.19207 0.20707 -0.00191 -0.00193 0.02718  300 ILE A CB  
2469 C CG1 . ILE A 306 ? 0.17531 0.21031 0.20207 -0.00918 -0.00347 0.02458  300 ILE A CG1 
2470 C CG2 . ILE A 306 ? 0.17844 0.19397 0.23044 0.00651  0.01673  0.00099  300 ILE A CG2 
2471 C CD1 . ILE A 306 ? 0.22022 0.22062 0.22479 -0.00305 0.01698  -0.00168 300 ILE A CD1 
2472 N N   . GLU A 307 ? 0.17432 0.16893 0.17052 0.03740  -0.01378 -0.02230 301 GLU A N   
2473 C CA  . GLU A 307 ? 0.15814 0.17172 0.17758 0.05068  -0.02576 -0.01553 301 GLU A CA  
2474 C C   . GLU A 307 ? 0.19580 0.17253 0.17671 0.03091  -0.01483 0.00235  301 GLU A C   
2475 O O   . GLU A 307 ? 0.22592 0.18478 0.17554 0.03209  -0.00261 0.03370  301 GLU A O   
2476 C CB  . GLU A 307 ? 0.17539 0.20238 0.23066 0.02673  -0.02031 -0.00982 301 GLU A CB  
2477 C CG  . GLU A 307 ? 0.20795 0.23309 0.26729 0.00167  0.01956  -0.02933 301 GLU A CG  
2478 C CD  . GLU A 307 ? 0.25964 0.23439 0.30765 -0.00748 0.05772  -0.05799 301 GLU A CD  
2479 O OE1 . GLU A 307 ? 0.28436 0.21454 0.30724 -0.00407 0.07178  -0.06519 301 GLU A OE1 
2480 O OE2 . GLU A 307 ? 0.28420 0.25385 0.33751 0.00217  0.08455  -0.07558 301 GLU A OE2 
2481 N N   . VAL A 308 ? 0.19077 0.16474 0.18389 0.03647  -0.04507 -0.02106 302 VAL A N   
2482 C CA  . VAL A 308 ? 0.17376 0.15886 0.19632 0.04116  -0.03752 -0.01735 302 VAL A CA  
2483 C C   . VAL A 308 ? 0.19618 0.16646 0.20475 0.03415  -0.01363 -0.01479 302 VAL A C   
2484 O O   . VAL A 308 ? 0.21308 0.16961 0.21442 0.03032  0.03036  -0.00885 302 VAL A O   
2485 C CB  . VAL A 308 ? 0.14541 0.16775 0.19563 0.04134  -0.05663 -0.02967 302 VAL A CB  
2486 C CG1 . VAL A 308 ? 0.18245 0.16348 0.18552 0.02970  -0.03941 -0.05229 302 VAL A CG1 
2487 C CG2 . VAL A 308 ? 0.16793 0.18806 0.21955 0.03502  -0.04220 0.00838  302 VAL A CG2 
2488 N N   . GLU A 309 ? 0.21387 0.15246 0.21601 0.01608  -0.01088 -0.02205 303 GLU A N   
2489 C CA  A GLU A 309 ? 0.24533 0.18316 0.22209 0.03719  0.00090  -0.00954 303 GLU A CA  
2490 C CA  B GLU A 309 ? 0.23792 0.17978 0.23405 0.02407  0.01552  -0.01357 303 GLU A CA  
2491 C C   . GLU A 309 ? 0.23079 0.18570 0.20958 0.02199  -0.01525 0.01460  303 GLU A C   
2492 O O   . GLU A 309 ? 0.22644 0.20050 0.22633 0.03221  -0.01182 0.03255  303 GLU A O   
2493 C CB  A GLU A 309 ? 0.29484 0.19750 0.23003 0.06018  -0.00013 -0.00800 303 GLU A CB  
2494 C CB  B GLU A 309 ? 0.27531 0.18716 0.26734 0.02190  0.04116  -0.01991 303 GLU A CB  
2495 C CG  A GLU A 309 ? 0.32304 0.22424 0.21510 0.08143  -0.01621 -0.00325 303 GLU A CG  
2496 C CG  B GLU A 309 ? 0.29274 0.21085 0.28404 0.01769  0.05152  -0.02605 303 GLU A CG  
2497 C CD  A GLU A 309 ? 0.36758 0.24618 0.22656 0.08214  -0.00666 0.01695  303 GLU A CD  
2498 C CD  B GLU A 309 ? 0.32388 0.22599 0.31787 0.00482  0.08206  -0.01087 303 GLU A CD  
2499 O OE1 A GLU A 309 ? 0.37835 0.24150 0.21982 0.10679  0.01031  0.05441  303 GLU A OE1 
2500 O OE1 B GLU A 309 ? 0.35478 0.23999 0.35399 0.02081  0.11509  0.00875  303 GLU A OE1 
2501 O OE2 A GLU A 309 ? 0.39272 0.25387 0.25172 0.05983  -0.02023 0.01102  303 GLU A OE2 
2502 O OE2 B GLU A 309 ? 0.34141 0.23439 0.33397 -0.02057 0.10957  -0.02202 303 GLU A OE2 
2503 N N   . GLN A 310 ? 0.21772 0.18045 0.19188 0.01455  -0.04079 0.02168  304 GLN A N   
2504 C CA  . GLN A 310 ? 0.23504 0.19757 0.20309 0.00962  -0.03170 0.02750  304 GLN A CA  
2505 C C   . GLN A 310 ? 0.25796 0.19476 0.19455 0.00662  0.02052  0.02875  304 GLN A C   
2506 O O   . GLN A 310 ? 0.24836 0.20858 0.22258 -0.01834 0.00786  0.03508  304 GLN A O   
2507 C CB  . GLN A 310 ? 0.25052 0.20230 0.24724 0.00046  -0.01357 -0.00043 304 GLN A CB  
2508 C CG  . GLN A 310 ? 0.23308 0.19850 0.25388 0.01253  0.00115  0.01959  304 GLN A CG  
2509 C CD  . GLN A 310 ? 0.20666 0.18469 0.22470 0.01785  -0.02230 0.03260  304 GLN A CD  
2510 O OE1 . GLN A 310 ? 0.19364 0.18728 0.22338 0.04125  -0.03372 0.05831  304 GLN A OE1 
2511 N NE2 . GLN A 310 ? 0.23564 0.18827 0.22290 0.01161  -0.00022 0.02993  304 GLN A NE2 
2512 N N   . ALA A 311 ? 0.24308 0.16442 0.18545 0.01823  0.00973  0.01486  305 ALA A N   
2513 C CA  . ALA A 311 ? 0.18441 0.16487 0.18371 0.01110  0.00037  0.03259  305 ALA A CA  
2514 C C   . ALA A 311 ? 0.20873 0.18898 0.16071 0.00485  -0.01268 0.02811  305 ALA A C   
2515 O O   . ALA A 311 ? 0.22385 0.19807 0.14354 -0.00325 0.01657  0.03207  305 ALA A O   
2516 C CB  . ALA A 311 ? 0.18503 0.16559 0.16589 0.00179  -0.00684 0.02453  305 ALA A CB  
2517 N N   . LEU A 312 ? 0.19981 0.18308 0.17192 -0.01469 -0.03197 0.03908  306 LEU A N   
2518 C CA  . LEU A 312 ? 0.18698 0.20186 0.16585 -0.02402 -0.00567 0.02781  306 LEU A CA  
2519 C C   . LEU A 312 ? 0.20798 0.19174 0.18896 -0.03502 -0.00018 0.02846  306 LEU A C   
2520 O O   . LEU A 312 ? 0.23656 0.19639 0.19946 -0.02628 0.01009  -0.00889 306 LEU A O   
2521 C CB  . LEU A 312 ? 0.19649 0.20284 0.16279 -0.01502 0.00770  0.02584  306 LEU A CB  
2522 C CG  . LEU A 312 ? 0.15908 0.20798 0.16041 0.00481  0.02481  0.00644  306 LEU A CG  
2523 C CD1 . LEU A 312 ? 0.12850 0.21405 0.13821 0.01048  0.03619  -0.02951 306 LEU A CD1 
2524 C CD2 . LEU A 312 ? 0.15844 0.22031 0.22065 0.00951  0.02254  0.02946  306 LEU A CD2 
2525 N N   . ALA A 313 ? 0.25476 0.19367 0.17119 -0.03694 -0.00613 0.03542  307 ALA A N   
2526 C CA  . ALA A 313 ? 0.25419 0.19485 0.18650 -0.02070 -0.02555 0.02921  307 ALA A CA  
2527 C C   . ALA A 313 ? 0.26857 0.21566 0.20707 -0.03713 -0.01510 0.02730  307 ALA A C   
2528 O O   . ALA A 313 ? 0.26603 0.23875 0.23094 -0.03449 0.00849  0.04516  307 ALA A O   
2529 C CB  . ALA A 313 ? 0.27339 0.19718 0.19215 -0.01163 -0.04568 0.00919  307 ALA A CB  
2530 N N   . HIS A 314 ? 0.27604 0.20965 0.20100 -0.05754 -0.01487 -0.00416 308 HIS A N   
2531 C CA  . HIS A 314 ? 0.27205 0.21288 0.16872 -0.03763 0.00430  0.02540  308 HIS A CA  
2532 C C   . HIS A 314 ? 0.29950 0.24480 0.17925 -0.03381 0.01038  0.04487  308 HIS A C   
2533 O O   . HIS A 314 ? 0.29510 0.26502 0.20736 -0.03415 0.00447  0.03456  308 HIS A O   
2534 C CB  . HIS A 314 ? 0.26227 0.22096 0.17485 -0.04111 -0.00076 0.01565  308 HIS A CB  
2535 C CG  . HIS A 314 ? 0.27352 0.22952 0.16041 -0.00585 0.01926  0.00897  308 HIS A CG  
2536 N ND1 . HIS A 314 ? 0.28060 0.22507 0.16694 -0.00173 -0.00095 0.00519  308 HIS A ND1 
2537 C CD2 . HIS A 314 ? 0.28191 0.24079 0.14676 -0.00399 0.00772  -0.00608 308 HIS A CD2 
2538 C CE1 . HIS A 314 ? 0.28440 0.23200 0.17679 0.00952  -0.00777 0.02307  308 HIS A CE1 
2539 N NE2 . HIS A 314 ? 0.25921 0.24423 0.16798 0.02907  0.02320  0.01471  308 HIS A NE2 
2540 N N   . PRO A 315 ? 0.31421 0.24769 0.17897 -0.00812 0.01294  0.06263  309 PRO A N   
2541 C CA  . PRO A 315 ? 0.32281 0.24944 0.17548 -0.00534 0.03012  0.08049  309 PRO A CA  
2542 C C   . PRO A 315 ? 0.29670 0.23418 0.19307 -0.01141 0.03020  0.06248  309 PRO A C   
2543 O O   . PRO A 315 ? 0.29555 0.23310 0.20466 -0.00975 0.02883  0.05841  309 PRO A O   
2544 C CB  . PRO A 315 ? 0.34487 0.26931 0.19520 -0.00209 0.05155  0.06989  309 PRO A CB  
2545 C CG  . PRO A 315 ? 0.34466 0.25547 0.19390 0.01312  0.03740  0.08961  309 PRO A CG  
2546 C CD  . PRO A 315 ? 0.32583 0.25222 0.17241 0.02257  0.02077  0.07996  309 PRO A CD  
2547 N N   . TYR A 316 ? 0.30834 0.21576 0.18550 -0.00975 0.04462  0.02437  310 TYR A N   
2548 C CA  . TYR A 316 ? 0.27459 0.20092 0.16336 -0.02862 0.00906  0.00924  310 TYR A CA  
2549 C C   . TYR A 316 ? 0.27325 0.19878 0.17257 -0.03858 0.03127  0.00855  310 TYR A C   
2550 O O   . TYR A 316 ? 0.29452 0.19851 0.19384 0.01895  0.03005  0.01233  310 TYR A O   
2551 C CB  . TYR A 316 ? 0.27574 0.20713 0.16761 -0.02794 0.01808  0.00526  310 TYR A CB  
2552 C CG  . TYR A 316 ? 0.27502 0.22451 0.18473 -0.01760 0.00953  0.01296  310 TYR A CG  
2553 C CD1 . TYR A 316 ? 0.27026 0.22668 0.20077 0.00547  0.02059  0.01214  310 TYR A CD1 
2554 C CD2 . TYR A 316 ? 0.26402 0.22789 0.17880 -0.02252 -0.03653 0.00881  310 TYR A CD2 
2555 C CE1 . TYR A 316 ? 0.26449 0.21778 0.21809 0.00204  0.01402  0.01867  310 TYR A CE1 
2556 C CE2 . TYR A 316 ? 0.27682 0.22231 0.22353 -0.00393 0.00420  0.00614  310 TYR A CE2 
2557 C CZ  . TYR A 316 ? 0.29496 0.22112 0.24034 0.01774  0.00978  0.02629  310 TYR A CZ  
2558 O OH  . TYR A 316 ? 0.32581 0.23701 0.27214 0.02061  0.01356  0.04315  310 TYR A OH  
2559 N N   . LEU A 317 ? 0.26029 0.18996 0.15836 -0.04722 0.05876  0.00526  311 LEU A N   
2560 C CA  . LEU A 317 ? 0.26180 0.19665 0.19066 -0.06186 0.08168  0.01647  311 LEU A CA  
2561 C C   . LEU A 317 ? 0.28334 0.22609 0.20118 -0.06347 0.07537  0.00675  311 LEU A C   
2562 O O   . LEU A 317 ? 0.27731 0.22958 0.21087 -0.08072 0.05703  -0.04640 311 LEU A O   
2563 C CB  . LEU A 317 ? 0.26303 0.18492 0.19183 -0.02518 0.07107  0.05718  311 LEU A CB  
2564 C CG  . LEU A 317 ? 0.21852 0.18707 0.19379 -0.01944 0.03790  0.06987  311 LEU A CG  
2565 C CD1 . LEU A 317 ? 0.23388 0.20566 0.21415 -0.02570 0.01832  0.05948  311 LEU A CD1 
2566 C CD2 . LEU A 317 ? 0.19842 0.20764 0.20842 -0.00927 -0.00228 0.06468  311 LEU A CD2 
2567 N N   . GLU A 318 ? 0.30644 0.24254 0.19513 -0.06383 0.07607  0.03294  312 GLU A N   
2568 C CA  . GLU A 318 ? 0.30914 0.25060 0.21192 -0.07331 0.04021  0.05452  312 GLU A CA  
2569 C C   . GLU A 318 ? 0.31880 0.26833 0.23231 -0.08031 0.06118  0.03432  312 GLU A C   
2570 O O   . GLU A 318 ? 0.32946 0.28239 0.26152 -0.11265 0.03844  0.01973  312 GLU A O   
2571 C CB  . GLU A 318 ? 0.36678 0.25151 0.22108 -0.07860 0.02502  0.07702  312 GLU A CB  
2572 C CG  . GLU A 318 ? 0.43810 0.27269 0.25489 -0.08059 0.04097  0.07035  312 GLU A CG  
2573 C CD  . GLU A 318 ? 0.48613 0.28600 0.27668 -0.07396 0.04897  0.07272  312 GLU A CD  
2574 O OE1 . GLU A 318 ? 0.51242 0.28866 0.27652 -0.06603 0.06095  0.05704  312 GLU A OE1 
2575 O OE2 . GLU A 318 ? 0.51171 0.31037 0.31142 -0.05820 0.06091  0.07444  312 GLU A OE2 
2576 N N   . GLN A 319 ? 0.27564 0.28166 0.21955 -0.05217 0.04357  0.02644  313 GLN A N   
2577 C CA  . GLN A 319 ? 0.27640 0.29008 0.24920 -0.04925 0.06974  -0.01682 313 GLN A CA  
2578 C C   . GLN A 319 ? 0.27955 0.27397 0.25866 -0.06059 0.07217  -0.01563 313 GLN A C   
2579 O O   . GLN A 319 ? 0.29954 0.27950 0.30605 -0.07865 0.10596  -0.02167 313 GLN A O   
2580 C CB  . GLN A 319 ? 0.25609 0.30908 0.26096 -0.01836 0.08815  -0.04557 313 GLN A CB  
2581 C CG  . GLN A 319 ? 0.28729 0.32925 0.30022 -0.01275 0.11176  -0.04364 313 GLN A CG  
2582 C CD  . GLN A 319 ? 0.28824 0.33675 0.32804 0.00128  0.12928  -0.04688 313 GLN A CD  
2583 O OE1 . GLN A 319 ? 0.27252 0.32975 0.33945 0.00403  0.11758  -0.03315 313 GLN A OE1 
2584 N NE2 . GLN A 319 ? 0.31399 0.34889 0.35416 -0.00755 0.12833  -0.05733 313 GLN A NE2 
2585 N N   . TYR A 320 ? 0.25878 0.25173 0.26471 -0.04799 0.07517  0.01229  314 TYR A N   
2586 C CA  . TYR A 320 ? 0.25312 0.23900 0.25792 -0.04640 0.05974  0.03316  314 TYR A CA  
2587 C C   . TYR A 320 ? 0.28152 0.23785 0.24386 -0.05377 0.05516  0.02368  314 TYR A C   
2588 O O   . TYR A 320 ? 0.30871 0.25504 0.25565 -0.07507 0.06032  0.01700  314 TYR A O   
2589 C CB  . TYR A 320 ? 0.22518 0.23769 0.29363 -0.05913 0.06541  0.03694  314 TYR A CB  
2590 C CG  . TYR A 320 ? 0.23473 0.25152 0.35447 -0.05639 0.05646  0.01590  314 TYR A CG  
2591 C CD1 . TYR A 320 ? 0.24729 0.27446 0.40619 -0.01396 0.04825  0.01522  314 TYR A CD1 
2592 C CD2 . TYR A 320 ? 0.23537 0.24906 0.39498 -0.07797 0.07557  0.00729  314 TYR A CD2 
2593 C CE1 . TYR A 320 ? 0.24977 0.27564 0.42545 -0.00138 0.05113  0.01672  314 TYR A CE1 
2594 C CE2 . TYR A 320 ? 0.23266 0.25399 0.42284 -0.04391 0.06528  0.01385  314 TYR A CE2 
2595 C CZ  . TYR A 320 ? 0.24357 0.27164 0.43552 -0.00974 0.06715  0.02005  314 TYR A CZ  
2596 O OH  . TYR A 320 ? 0.29874 0.29657 0.47115 -0.00691 0.08354  0.04338  314 TYR A OH  
2597 N N   . TYR A 321 ? 0.25109 0.22800 0.22297 -0.03083 0.02321  0.04693  315 TYR A N   
2598 C CA  . TYR A 321 ? 0.26167 0.22206 0.22075 -0.04866 0.01157  0.03408  315 TYR A CA  
2599 C C   . TYR A 321 ? 0.30262 0.22497 0.23521 -0.05233 0.02475  0.01218  315 TYR A C   
2600 O O   . TYR A 321 ? 0.36978 0.22952 0.24644 -0.07399 0.03399  -0.00313 315 TYR A O   
2601 C CB  . TYR A 321 ? 0.27259 0.23603 0.22052 -0.04296 0.02149  0.05948  315 TYR A CB  
2602 C CG  . TYR A 321 ? 0.29362 0.22956 0.24822 -0.04000 -0.01578 0.06461  315 TYR A CG  
2603 C CD1 . TYR A 321 ? 0.28807 0.22472 0.25573 -0.05872 -0.01931 0.02750  315 TYR A CD1 
2604 C CD2 . TYR A 321 ? 0.31754 0.22991 0.26457 -0.02975 -0.00664 0.07770  315 TYR A CD2 
2605 C CE1 . TYR A 321 ? 0.29059 0.20600 0.26739 -0.03624 -0.04563 0.03028  315 TYR A CE1 
2606 C CE2 . TYR A 321 ? 0.30404 0.21895 0.28697 -0.02650 -0.02794 0.06604  315 TYR A CE2 
2607 C CZ  . TYR A 321 ? 0.31542 0.21810 0.29593 -0.01788 -0.04328 0.03885  315 TYR A CZ  
2608 O OH  . TYR A 321 ? 0.32829 0.21379 0.33513 -0.00405 -0.07536 0.04641  315 TYR A OH  
2609 N N   . ASP A 322 ? 0.27987 0.21530 0.20906 -0.02890 0.02389  0.00539  316 ASP A N   
2610 C CA  . ASP A 322 ? 0.27611 0.23226 0.25959 -0.05162 0.03520  -0.02206 316 ASP A CA  
2611 C C   . ASP A 322 ? 0.28249 0.23256 0.24829 -0.01780 0.01659  -0.02108 316 ASP A C   
2612 O O   . ASP A 322 ? 0.29480 0.20550 0.24515 0.00419  -0.01047 -0.02303 316 ASP A O   
2613 C CB  . ASP A 322 ? 0.26727 0.24064 0.26967 -0.07032 0.03968  -0.04718 316 ASP A CB  
2614 C CG  . ASP A 322 ? 0.27228 0.25066 0.28721 -0.10384 0.07130  -0.06288 316 ASP A CG  
2615 O OD1 . ASP A 322 ? 0.29385 0.23057 0.29051 -0.09971 0.10448  -0.07010 316 ASP A OD1 
2616 O OD2 . ASP A 322 ? 0.23554 0.26975 0.29569 -0.13509 0.07412  -0.07970 316 ASP A OD2 
2617 N N   . PRO A 323 ? 0.24786 0.24912 0.25366 0.01095  -0.00970 0.01606  317 PRO A N   
2618 C CA  . PRO A 323 ? 0.23935 0.25547 0.26848 0.03173  -0.02858 0.01885  317 PRO A CA  
2619 C C   . PRO A 323 ? 0.24774 0.24311 0.29271 0.03811  -0.01813 0.01758  317 PRO A C   
2620 O O   . PRO A 323 ? 0.27529 0.25095 0.30897 0.03650  0.00926  0.00552  317 PRO A O   
2621 C CB  . PRO A 323 ? 0.25657 0.29304 0.27791 0.02570  -0.02138 0.02453  317 PRO A CB  
2622 C CG  . PRO A 323 ? 0.25394 0.29301 0.27286 0.02416  -0.00955 0.03610  317 PRO A CG  
2623 C CD  . PRO A 323 ? 0.22071 0.27619 0.24884 0.02542  -0.03683 0.04968  317 PRO A CD  
2624 N N   . SER A 324 ? 0.26174 0.21691 0.31159 0.03383  -0.01183 0.02442  318 SER A N   
2625 C CA  . SER A 324 ? 0.27721 0.22536 0.29225 0.01414  0.01342  0.00835  318 SER A CA  
2626 C C   . SER A 324 ? 0.27016 0.23109 0.28911 0.00049  0.02198  0.00300  318 SER A C   
2627 O O   . SER A 324 ? 0.28291 0.24928 0.29771 0.00182  0.01691  -0.02178 318 SER A O   
2628 C CB  . SER A 324 ? 0.25571 0.25403 0.32536 -0.00050 0.02418  -0.02240 318 SER A CB  
2629 O OG  . SER A 324 ? 0.34117 0.28851 0.36211 0.02859  0.01189  -0.01903 318 SER A OG  
2630 N N   . ASP A 325 ? 0.22241 0.20792 0.27315 -0.01401 0.02181  0.01544  319 ASP A N   
2631 C CA  . ASP A 325 ? 0.21124 0.21557 0.28002 -0.02851 0.02197  0.02019  319 ASP A CA  
2632 C C   . ASP A 325 ? 0.19413 0.19636 0.24764 -0.02645 0.01091  0.03673  319 ASP A C   
2633 O O   . ASP A 325 ? 0.19335 0.20497 0.25319 -0.01865 0.00643  0.03307  319 ASP A O   
2634 C CB  . ASP A 325 ? 0.20606 0.24197 0.32594 -0.02423 0.05110  0.02711  319 ASP A CB  
2635 C CG  . ASP A 325 ? 0.21861 0.27870 0.36774 -0.01787 0.03538  0.00207  319 ASP A CG  
2636 O OD1 . ASP A 325 ? 0.24672 0.29668 0.38735 -0.02231 0.02171  -0.02666 319 ASP A OD1 
2637 O OD2 . ASP A 325 ? 0.20824 0.28480 0.38689 0.01090  0.00473  0.01690  319 ASP A OD2 
2638 N N   . GLU A 326 ? 0.20027 0.18364 0.23054 -0.02559 -0.00251 0.01280  320 GLU A N   
2639 C CA  . GLU A 326 ? 0.20711 0.20904 0.20416 -0.02865 -0.00302 0.01183  320 GLU A CA  
2640 C C   . GLU A 326 ? 0.23145 0.20863 0.20935 -0.01981 0.01238  0.02255  320 GLU A C   
2641 O O   . GLU A 326 ? 0.21390 0.21836 0.21752 -0.03177 0.01447  0.02995  320 GLU A O   
2642 C CB  . GLU A 326 ? 0.23040 0.22407 0.21140 -0.01075 -0.00735 0.01135  320 GLU A CB  
2643 C CG  . GLU A 326 ? 0.23326 0.23515 0.19790 0.01195  0.00037  -0.00583 320 GLU A CG  
2644 C CD  . GLU A 326 ? 0.24935 0.23065 0.21440 0.00784  0.00989  0.00254  320 GLU A CD  
2645 O OE1 . GLU A 326 ? 0.27173 0.24533 0.21842 0.00888  0.00114  0.00229  320 GLU A OE1 
2646 O OE2 . GLU A 326 ? 0.23004 0.22381 0.22682 0.00218  0.01142  0.01077  320 GLU A OE2 
2647 N N   . PRO A 327 ? 0.23432 0.20772 0.19855 -0.00295 -0.03535 0.02613  321 PRO A N   
2648 C CA  . PRO A 327 ? 0.24095 0.21586 0.19702 -0.02538 -0.01867 -0.00210 321 PRO A CA  
2649 C C   . PRO A 327 ? 0.26217 0.20601 0.21478 -0.02932 0.02481  -0.01845 321 PRO A C   
2650 O O   . PRO A 327 ? 0.29468 0.19751 0.20834 -0.03289 0.03335  -0.00892 321 PRO A O   
2651 C CB  . PRO A 327 ? 0.28023 0.22495 0.19344 0.00353  -0.02665 0.00009  321 PRO A CB  
2652 C CG  . PRO A 327 ? 0.27437 0.23798 0.20826 0.00075  -0.02035 0.01956  321 PRO A CG  
2653 C CD  . PRO A 327 ? 0.24489 0.22480 0.18591 0.01007  -0.03243 0.03638  321 PRO A CD  
2654 N N   . ILE A 328 ? 0.24776 0.20569 0.22434 -0.03161 0.03161  -0.02525 322 ILE A N   
2655 C CA  . ILE A 328 ? 0.23460 0.20793 0.21109 -0.01134 -0.00551 -0.02096 322 ILE A CA  
2656 C C   . ILE A 328 ? 0.25071 0.21551 0.19746 -0.02694 -0.00585 -0.02716 322 ILE A C   
2657 O O   . ILE A 328 ? 0.26337 0.22112 0.21202 -0.01366 0.02569  -0.01728 322 ILE A O   
2658 C CB  . ILE A 328 ? 0.25712 0.21511 0.21623 -0.00673 -0.01989 -0.00812 322 ILE A CB  
2659 C CG1 . ILE A 328 ? 0.25293 0.21972 0.24899 -0.00251 -0.01401 -0.01651 322 ILE A CG1 
2660 C CG2 . ILE A 328 ? 0.27279 0.22575 0.19591 0.00446  -0.01408 -0.01588 322 ILE A CG2 
2661 C CD1 . ILE A 328 ? 0.27995 0.22683 0.26499 -0.01749 -0.00915 -0.01179 322 ILE A CD1 
2662 N N   . ALA A 329 ? 0.24488 0.21969 0.18608 -0.05277 -0.00724 -0.02495 323 ALA A N   
2663 C CA  . ALA A 329 ? 0.29064 0.22655 0.20700 -0.03974 0.00767  -0.03083 323 ALA A CA  
2664 C C   . ALA A 329 ? 0.36930 0.25977 0.25386 -0.03888 0.02905  -0.04221 323 ALA A C   
2665 O O   . ALA A 329 ? 0.37157 0.27678 0.26747 -0.02744 0.04925  -0.05084 323 ALA A O   
2666 C CB  . ALA A 329 ? 0.27744 0.21600 0.21193 -0.03593 -0.01503 -0.01050 323 ALA A CB  
2667 N N   . GLU A 330 ? 0.43404 0.28569 0.25336 -0.04464 0.04077  -0.07483 324 GLU A N   
2668 C CA  . GLU A 330 ? 0.51144 0.33836 0.31605 -0.04495 0.05541  -0.08548 324 GLU A CA  
2669 C C   . GLU A 330 ? 0.55019 0.37326 0.36425 -0.05276 0.09307  -0.09455 324 GLU A C   
2670 O O   . GLU A 330 ? 0.56824 0.38119 0.38358 -0.03248 0.09060  -0.09337 324 GLU A O   
2671 C CB  . GLU A 330 ? 0.54698 0.35939 0.33533 -0.03832 0.02634  -0.09530 324 GLU A CB  
2672 C CG  . GLU A 330 ? 0.59268 0.38369 0.38009 -0.03195 0.02184  -0.09104 324 GLU A CG  
2673 C CD  . GLU A 330 ? 0.62609 0.39938 0.41196 -0.03776 0.01447  -0.09543 324 GLU A CD  
2674 O OE1 . GLU A 330 ? 0.65202 0.41077 0.44159 -0.04016 0.04504  -0.10091 324 GLU A OE1 
2675 O OE2 . GLU A 330 ? 0.63336 0.41373 0.42334 -0.03758 -0.00224 -0.09211 324 GLU A OE2 
2676 N N   . ALA A 331 ? 0.55015 0.38961 0.37466 -0.09538 0.12614  -0.10880 325 ALA A N   
2677 C CA  . ALA A 331 ? 0.54517 0.41591 0.38047 -0.10995 0.10153  -0.09741 325 ALA A CA  
2678 C C   . ALA A 331 ? 0.53188 0.42286 0.36589 -0.09826 0.07470  -0.06671 325 ALA A C   
2679 O O   . ALA A 331 ? 0.54708 0.44205 0.36662 -0.08902 0.06371  -0.05925 325 ALA A O   
2680 C CB  . ALA A 331 ? 0.54895 0.41702 0.40119 -0.12013 0.11084  -0.10862 325 ALA A CB  
2681 N N   . PRO A 332 ? 0.50006 0.41801 0.30980 -0.09101 0.04013  -0.04545 326 PRO A N   
2682 C CA  . PRO A 332 ? 0.49293 0.41323 0.30574 -0.06391 0.05101  -0.04487 326 PRO A CA  
2683 C C   . PRO A 332 ? 0.43581 0.40981 0.27098 -0.01284 0.06527  -0.06546 326 PRO A C   
2684 O O   . PRO A 332 ? 0.46267 0.40524 0.26019 0.00031  0.05681  -0.07341 326 PRO A O   
2685 C CB  . PRO A 332 ? 0.48970 0.41038 0.32809 -0.06742 0.01393  -0.02104 326 PRO A CB  
2686 C CG  . PRO A 332 ? 0.50129 0.41387 0.34342 -0.07246 0.01521  -0.02957 326 PRO A CG  
2687 C CD  . PRO A 332 ? 0.49573 0.41561 0.32995 -0.08110 0.01920  -0.04237 326 PRO A CD  
2688 N N   . PHE A 333 ? 0.37034 0.41748 0.26284 0.00661  0.03122  -0.07245 327 PHE A N   
2689 C CA  . PHE A 333 ? 0.41339 0.44914 0.26141 0.03539  0.04135  -0.07128 327 PHE A CA  
2690 C C   . PHE A 333 ? 0.43755 0.50480 0.29886 0.02639  0.07439  -0.09654 327 PHE A C   
2691 O O   . PHE A 333 ? 0.45038 0.50929 0.32950 0.02588  0.08200  -0.10396 327 PHE A O   
2692 C CB  . PHE A 333 ? 0.44005 0.44077 0.24616 0.02494  -0.00267 -0.06095 327 PHE A CB  
2693 C CG  . PHE A 333 ? 0.44080 0.42115 0.25311 0.03019  -0.03605 -0.06680 327 PHE A CG  
2694 C CD1 . PHE A 333 ? 0.44730 0.42467 0.26715 0.03133  -0.06083 -0.05955 327 PHE A CD1 
2695 C CD2 . PHE A 333 ? 0.43870 0.40372 0.25369 0.02206  -0.04152 -0.07820 327 PHE A CD2 
2696 C CE1 . PHE A 333 ? 0.45494 0.42300 0.25883 0.03670  -0.06087 -0.05168 327 PHE A CE1 
2697 C CE2 . PHE A 333 ? 0.44976 0.40371 0.24073 0.01650  -0.05815 -0.07825 327 PHE A CE2 
2698 C CZ  . PHE A 333 ? 0.45572 0.41271 0.26109 0.02960  -0.04707 -0.06027 327 PHE A CZ  
2699 N N   . LYS A 334 ? 0.44849 0.53287 0.31417 0.03463  0.09955  -0.10615 328 LYS A N   
2700 C CA  . LYS A 334 ? 0.47189 0.55929 0.33589 0.03494  0.12147  -0.10827 328 LYS A CA  
2701 C C   . LYS A 334 ? 0.49760 0.58068 0.35718 0.03342  0.13576  -0.09662 328 LYS A C   
2702 O O   . LYS A 334 ? 0.51044 0.59028 0.38480 0.03865  0.12486  -0.08350 328 LYS A O   
2703 C CB  . LYS A 334 ? 0.46683 0.56147 0.33386 0.03255  0.13070  -0.12010 328 LYS A CB  
2704 N N   . PHE A 335 ? 0.50393 0.59040 0.35172 0.02944  0.16506  -0.09626 329 PHE A N   
2705 C CA  . PHE A 335 ? 0.49879 0.59576 0.35843 0.02714  0.18216  -0.09660 329 PHE A CA  
2706 C C   . PHE A 335 ? 0.49959 0.60136 0.35309 0.02785  0.19508  -0.10055 329 PHE A C   
2707 O O   . PHE A 335 ? 0.50811 0.60533 0.35056 0.02263  0.20913  -0.11304 329 PHE A O   
2708 C CB  . PHE A 335 ? 0.49236 0.59503 0.36146 0.02177  0.17642  -0.09022 329 PHE A CB  
2709 N N   . ASP A 340 ? 0.75790 0.89920 0.81590 0.04683  0.02486  0.09455  334 ASP A N   
2710 C CA  . ASP A 340 ? 0.75209 0.89770 0.81507 0.04416  0.02404  0.08930  334 ASP A CA  
2711 C C   . ASP A 340 ? 0.73886 0.89525 0.81505 0.04153  0.01930  0.08821  334 ASP A C   
2712 O O   . ASP A 340 ? 0.73064 0.89734 0.81312 0.04901  0.00512  0.08797  334 ASP A O   
2713 C CB  . ASP A 340 ? 0.74634 0.89587 0.80913 0.04772  0.01385  0.08471  334 ASP A CB  
2714 N N   . ASP A 341 ? 0.72764 0.88886 0.81019 0.03389  0.02265  0.08639  335 ASP A N   
2715 C CA  . ASP A 341 ? 0.69806 0.88393 0.79530 0.03049  0.01673  0.07945  335 ASP A CA  
2716 C C   . ASP A 341 ? 0.64357 0.88386 0.77682 0.03065  0.00292  0.07473  335 ASP A C   
2717 O O   . ASP A 341 ? 0.61853 0.88719 0.78206 0.04218  -0.01292 0.07537  335 ASP A O   
2718 C CB  . ASP A 341 ? 0.69170 0.87834 0.79235 0.02883  0.00130  0.07469  335 ASP A CB  
2719 N N   . LEU A 342 ? 0.58808 0.87748 0.73383 0.01993  -0.02642 0.06726  336 LEU A N   
2720 C CA  . LEU A 342 ? 0.53239 0.86613 0.70335 -0.00049 -0.03202 0.05695  336 LEU A CA  
2721 C C   . LEU A 342 ? 0.46168 0.85992 0.65110 -0.03202 -0.07530 0.04854  336 LEU A C   
2722 O O   . LEU A 342 ? 0.42893 0.86697 0.61765 -0.03378 -0.14654 0.04442  336 LEU A O   
2723 C CB  . LEU A 342 ? 0.54039 0.86103 0.71016 0.00213  -0.03019 0.04680  336 LEU A CB  
2724 C CG  . LEU A 342 ? 0.55370 0.85887 0.72102 0.00649  -0.02789 0.04144  336 LEU A CG  
2725 C CD1 . LEU A 342 ? 0.56567 0.85872 0.74143 0.00737  -0.00126 0.03430  336 LEU A CD1 
2726 C CD2 . LEU A 342 ? 0.56479 0.86070 0.72703 0.00708  -0.02501 0.04080  336 LEU A CD2 
2727 N N   . PRO A 343 ? 0.44315 0.84726 0.63389 -0.06003 -0.04830 0.04108  337 PRO A N   
2728 C CA  . PRO A 343 ? 0.41815 0.83160 0.60758 -0.08550 -0.03809 0.04247  337 PRO A CA  
2729 C C   . PRO A 343 ? 0.40000 0.81501 0.56426 -0.11166 -0.01980 0.04971  337 PRO A C   
2730 O O   . PRO A 343 ? 0.34744 0.81533 0.56276 -0.12199 -0.04323 0.05061  337 PRO A O   
2731 C CB  . PRO A 343 ? 0.44889 0.83617 0.62555 -0.07342 -0.01661 0.04261  337 PRO A CB  
2732 C CG  . PRO A 343 ? 0.47049 0.84255 0.64107 -0.06798 -0.00144 0.04258  337 PRO A CG  
2733 C CD  . PRO A 343 ? 0.46765 0.84642 0.64064 -0.06658 -0.02106 0.04097  337 PRO A CD  
2734 N N   . LYS A 344 ? 0.39907 0.79589 0.51877 -0.13579 -0.00063 0.05646  338 LYS A N   
2735 C CA  . LYS A 344 ? 0.41696 0.78487 0.49331 -0.15692 0.03876  0.06001  338 LYS A CA  
2736 C C   . LYS A 344 ? 0.37735 0.77755 0.45631 -0.16720 0.02859  0.05155  338 LYS A C   
2737 O O   . LYS A 344 ? 0.33976 0.78303 0.45137 -0.17780 0.00496  0.04267  338 LYS A O   
2738 C CB  . LYS A 344 ? 0.47782 0.77886 0.50469 -0.16148 0.09740  0.08099  338 LYS A CB  
2739 C CG  . LYS A 344 ? 0.52853 0.78065 0.51860 -0.15817 0.14245  0.10162  338 LYS A CG  
2740 C CD  . LYS A 344 ? 0.56447 0.78581 0.51721 -0.15920 0.16600  0.11216  338 LYS A CD  
2741 C CE  . LYS A 344 ? 0.58655 0.79347 0.50897 -0.16023 0.19262  0.11905  338 LYS A CE  
2742 N NZ  . LYS A 344 ? 0.58674 0.80198 0.51049 -0.15208 0.22784  0.12130  338 LYS A NZ  
2743 N N   . GLU A 345 ? 0.37114 0.76231 0.42254 -0.17141 0.04408  0.05416  339 GLU A N   
2744 C CA  . GLU A 345 ? 0.38066 0.75412 0.43097 -0.16279 0.08702  0.06364  339 GLU A CA  
2745 C C   . GLU A 345 ? 0.35676 0.75793 0.42970 -0.12788 0.09206  0.07025  339 GLU A C   
2746 O O   . GLU A 345 ? 0.31087 0.75955 0.43532 -0.12643 0.07187  0.06545  339 GLU A O   
2747 C CB  . GLU A 345 ? 0.41241 0.74421 0.41446 -0.19082 0.10912  0.06584  339 GLU A CB  
2748 C CG  . GLU A 345 ? 0.42834 0.72284 0.39362 -0.20965 0.12730  0.06416  339 GLU A CG  
2749 C CD  . GLU A 345 ? 0.43903 0.70255 0.38319 -0.21081 0.13368  0.05372  339 GLU A CD  
2750 O OE1 . GLU A 345 ? 0.43562 0.67882 0.36488 -0.19511 0.13767  0.05341  339 GLU A OE1 
2751 O OE2 . GLU A 345 ? 0.46768 0.71874 0.39404 -0.22454 0.14496  0.04268  339 GLU A OE2 
2752 N N   . LYS A 346 ? 0.35072 0.75757 0.39982 -0.09717 0.08611  0.09129  340 LYS A N   
2753 C CA  A LYS A 346 ? 0.34872 0.75376 0.39164 -0.08314 0.09524  0.09957  340 LYS A CA  
2754 C CA  B LYS A 346 ? 0.34857 0.76152 0.40112 -0.08293 0.09093  0.10014  340 LYS A CA  
2755 C C   . LYS A 346 ? 0.33124 0.76626 0.39409 -0.07663 0.06646  0.10380  340 LYS A C   
2756 O O   . LYS A 346 ? 0.33790 0.77412 0.40399 -0.07112 0.03264  0.08767  340 LYS A O   
2757 C CB  A LYS A 346 ? 0.36203 0.73779 0.38916 -0.07087 0.11944  0.10616  340 LYS A CB  
2758 C CB  B LYS A 346 ? 0.36166 0.76097 0.41530 -0.06998 0.10860  0.10879  340 LYS A CB  
2759 C CG  A LYS A 346 ? 0.38023 0.72583 0.39721 -0.06647 0.12826  0.10641  340 LYS A CG  
2760 C CG  B LYS A 346 ? 0.37847 0.76392 0.43506 -0.06501 0.11292  0.11321  340 LYS A CG  
2761 C CD  A LYS A 346 ? 0.39990 0.71758 0.39194 -0.05412 0.13489  0.10959  340 LYS A CD  
2762 C CD  B LYS A 346 ? 0.39682 0.76535 0.45318 -0.06085 0.11449  0.12218  340 LYS A CD  
2763 C CE  A LYS A 346 ? 0.42494 0.71360 0.39530 -0.04247 0.13610  0.10979  340 LYS A CE  
2764 C CE  B LYS A 346 ? 0.40945 0.76327 0.46373 -0.05756 0.12096  0.13099  340 LYS A CE  
2765 N NZ  A LYS A 346 ? 0.44615 0.71086 0.39869 -0.03564 0.14624  0.11043  340 LYS A NZ  
2766 N NZ  B LYS A 346 ? 0.41830 0.76418 0.47491 -0.05193 0.12501  0.13439  340 LYS A NZ  
2767 N N   . LEU A 347 ? 0.29265 0.77732 0.38377 -0.05880 0.02945  0.10892  341 LEU A N   
2768 C CA  . LEU A 347 ? 0.24761 0.79115 0.36329 -0.05213 -0.00822 0.11405  341 LEU A CA  
2769 C C   . LEU A 347 ? 0.25090 0.79814 0.33358 -0.05716 -0.02189 0.11150  341 LEU A C   
2770 O O   . LEU A 347 ? 0.26533 0.80459 0.31115 -0.03999 0.03582  0.11934  341 LEU A O   
2771 C CB  . LEU A 347 ? 0.21941 0.79120 0.37549 -0.06321 -0.02387 0.10347  341 LEU A CB  
2772 C CG  . LEU A 347 ? 0.21435 0.79218 0.39500 -0.04853 -0.01503 0.10883  341 LEU A CG  
2773 C CD1 . LEU A 347 ? 0.20944 0.78183 0.39426 -0.04741 -0.02702 0.09579  341 LEU A CD1 
2774 C CD2 . LEU A 347 ? 0.23822 0.79432 0.40774 -0.04355 0.00787  0.10964  341 LEU A CD2 
2775 N N   . LYS A 348 ? 0.25848 0.80206 0.33660 -0.06189 -0.05943 0.10243  342 LYS A N   
2776 C CA  . LYS A 348 ? 0.28089 0.78652 0.32617 -0.07529 -0.09370 0.09987  342 LYS A CA  
2777 C C   . LYS A 348 ? 0.28826 0.79932 0.33536 -0.03822 -0.04235 0.09882  342 LYS A C   
2778 O O   . LYS A 348 ? 0.27713 0.80043 0.29613 -0.02570 -0.05678 0.11690  342 LYS A O   
2779 C CB  . LYS A 348 ? 0.30177 0.78556 0.32418 -0.11985 -0.09959 0.09663  342 LYS A CB  
2780 C CG  . LYS A 348 ? 0.32355 0.77150 0.31352 -0.12838 -0.10714 0.10679  342 LYS A CG  
2781 C CD  . LYS A 348 ? 0.34608 0.75950 0.30167 -0.14984 -0.09952 0.09584  342 LYS A CD  
2782 C CE  . LYS A 348 ? 0.37681 0.74555 0.28502 -0.16414 -0.09784 0.09244  342 LYS A CE  
2783 N NZ  . LYS A 348 ? 0.39773 0.73899 0.27711 -0.17528 -0.08491 0.08086  342 LYS A NZ  
2784 N N   . GLU A 349 ? 0.28054 0.80483 0.37346 -0.02349 -0.01228 0.07993  343 GLU A N   
2785 C CA  . GLU A 349 ? 0.29382 0.80396 0.38887 0.00503  0.02536  0.06085  343 GLU A CA  
2786 C C   . GLU A 349 ? 0.25546 0.78996 0.37637 0.04022  0.00033  0.07306  343 GLU A C   
2787 O O   . GLU A 349 ? 0.21855 0.79418 0.38708 0.06414  0.02327  0.08212  343 GLU A O   
2788 C CB  . GLU A 349 ? 0.34858 0.81537 0.44404 0.00382  0.06566  0.03460  343 GLU A CB  
2789 C CG  . GLU A 349 ? 0.39005 0.82533 0.47843 0.00909  0.10471  0.01831  343 GLU A CG  
2790 C CD  . GLU A 349 ? 0.42343 0.83078 0.50615 0.00410  0.12891  0.00479  343 GLU A CD  
2791 O OE1 . GLU A 349 ? 0.42130 0.83500 0.50028 0.00493  0.11192  -0.00193 343 GLU A OE1 
2792 O OE2 . GLU A 349 ? 0.44990 0.83180 0.53808 0.00625  0.16260  0.00131  343 GLU A OE2 
2793 N N   . LEU A 350 ? 0.24036 0.77484 0.35453 0.05747  -0.00741 0.08114  344 LEU A N   
2794 C CA  . LEU A 350 ? 0.23702 0.74680 0.33230 0.05909  -0.00951 0.08812  344 LEU A CA  
2795 C C   . LEU A 350 ? 0.24743 0.70266 0.29594 0.07004  -0.00548 0.10303  344 LEU A C   
2796 O O   . LEU A 350 ? 0.31287 0.69947 0.29949 0.10414  0.01508  0.11864  344 LEU A O   
2797 C CB  . LEU A 350 ? 0.22800 0.75938 0.35008 0.05672  0.00194  0.08404  344 LEU A CB  
2798 C CG  . LEU A 350 ? 0.26761 0.77026 0.37957 0.05269  0.04192  0.05503  344 LEU A CG  
2799 C CD1 . LEU A 350 ? 0.26735 0.77499 0.38383 0.03979  0.03509  0.04373  344 LEU A CD1 
2800 C CD2 . LEU A 350 ? 0.28797 0.77285 0.39775 0.05194  0.05273  0.04591  344 LEU A CD2 
2801 N N   . ILE A 351 ? 0.23904 0.66710 0.26962 0.04243  -0.00006 0.09441  345 ILE A N   
2802 C CA  . ILE A 351 ? 0.21469 0.62300 0.23858 0.01695  -0.00047 0.09206  345 ILE A CA  
2803 C C   . ILE A 351 ? 0.22001 0.58519 0.25037 0.01374  0.01415  0.07572  345 ILE A C   
2804 O O   . ILE A 351 ? 0.21210 0.56351 0.25565 0.03566  0.00199  0.09544  345 ILE A O   
2805 C CB  . ILE A 351 ? 0.22912 0.61645 0.21164 -0.01929 0.00141  0.08022  345 ILE A CB  
2806 C CG1 . ILE A 351 ? 0.27162 0.61842 0.22164 -0.05046 0.00139  0.08199  345 ILE A CG1 
2807 C CG2 . ILE A 351 ? 0.20794 0.60564 0.20507 -0.02497 -0.00393 0.08336  345 ILE A CG2 
2808 C CD1 . ILE A 351 ? 0.29150 0.61876 0.21062 -0.07193 0.01072  0.07613  345 ILE A CD1 
2809 N N   . PHE A 352 ? 0.23441 0.57035 0.24814 0.00870  0.00414  0.05952  346 PHE A N   
2810 C CA  . PHE A 352 ? 0.24759 0.55034 0.21987 0.01800  -0.01206 0.05079  346 PHE A CA  
2811 C C   . PHE A 352 ? 0.25380 0.53684 0.24417 0.04081  -0.03609 0.04090  346 PHE A C   
2812 O O   . PHE A 352 ? 0.26995 0.53472 0.25826 0.03337  -0.00085 0.04533  346 PHE A O   
2813 C CB  . PHE A 352 ? 0.24436 0.54854 0.23972 0.01534  0.00417  0.04888  346 PHE A CB  
2814 C CG  . PHE A 352 ? 0.22829 0.53404 0.22726 0.03842  -0.02538 0.05546  346 PHE A CG  
2815 C CD1 . PHE A 352 ? 0.23526 0.52913 0.23552 0.03899  -0.00347 0.05653  346 PHE A CD1 
2816 C CD2 . PHE A 352 ? 0.23690 0.53648 0.23047 0.05219  -0.02508 0.06797  346 PHE A CD2 
2817 C CE1 . PHE A 352 ? 0.25471 0.52494 0.24329 0.04932  0.01375  0.05986  346 PHE A CE1 
2818 C CE2 . PHE A 352 ? 0.26243 0.53062 0.22537 0.06046  0.00538  0.09295  346 PHE A CE2 
2819 C CZ  . PHE A 352 ? 0.25692 0.52773 0.24717 0.04975  0.02488  0.07968  346 PHE A CZ  
2820 N N   . GLU A 353 ? 0.27657 0.52149 0.27848 0.09009  -0.03671 0.02642  347 GLU A N   
2821 C CA  . GLU A 353 ? 0.31638 0.51527 0.33573 0.11865  -0.01937 0.02137  347 GLU A CA  
2822 C C   . GLU A 353 ? 0.32114 0.48451 0.33010 0.10979  -0.04770 0.02596  347 GLU A C   
2823 O O   . GLU A 353 ? 0.35675 0.48329 0.34089 0.11413  -0.02069 0.02094  347 GLU A O   
2824 C CB  . GLU A 353 ? 0.35671 0.53356 0.37994 0.13872  -0.00770 0.02405  347 GLU A CB  
2825 C CG  . GLU A 353 ? 0.41535 0.54742 0.42354 0.14582  0.02957  0.01684  347 GLU A CG  
2826 C CD  . GLU A 353 ? 0.47741 0.55733 0.43299 0.14626  0.05897  0.02141  347 GLU A CD  
2827 O OE1 . GLU A 353 ? 0.50402 0.56547 0.42995 0.14640  0.06270  0.01953  347 GLU A OE1 
2828 O OE2 . GLU A 353 ? 0.51740 0.55993 0.43585 0.14225  0.07574  0.02218  347 GLU A OE2 
2829 N N   . GLU A 354 ? 0.32208 0.46303 0.32340 0.09026  -0.05226 0.03641  348 GLU A N   
2830 C CA  . GLU A 354 ? 0.33079 0.43292 0.34688 0.06038  -0.04338 0.02371  348 GLU A CA  
2831 C C   . GLU A 354 ? 0.32888 0.39591 0.33329 0.06898  -0.02881 0.03838  348 GLU A C   
2832 O O   . GLU A 354 ? 0.35455 0.38762 0.35241 0.08173  -0.04133 0.05399  348 GLU A O   
2833 C CB  . GLU A 354 ? 0.35384 0.44287 0.38203 0.04001  -0.05832 0.01382  348 GLU A CB  
2834 C CG  . GLU A 354 ? 0.42651 0.45487 0.42586 0.01266  -0.03918 -0.00652 348 GLU A CG  
2835 C CD  . GLU A 354 ? 0.46390 0.46260 0.44758 0.00820  -0.03236 -0.01272 348 GLU A CD  
2836 O OE1 . GLU A 354 ? 0.48943 0.46794 0.46086 -0.00615 -0.02125 -0.02500 348 GLU A OE1 
2837 O OE2 . GLU A 354 ? 0.48462 0.47189 0.46265 0.01323  -0.03847 -0.00603 348 GLU A OE2 
2838 N N   . THR A 355 ? 0.27410 0.36304 0.30156 0.06889  -0.04034 0.04788  349 THR A N   
2839 C CA  . THR A 355 ? 0.25765 0.35123 0.31129 0.02287  -0.02520 0.03738  349 THR A CA  
2840 C C   . THR A 355 ? 0.28102 0.34427 0.34171 0.00912  -0.02281 0.03073  349 THR A C   
2841 O O   . THR A 355 ? 0.24462 0.34191 0.36927 -0.03310 -0.04174 0.00161  349 THR A O   
2842 C CB  . THR A 355 ? 0.25175 0.35626 0.27689 0.00983  -0.02387 0.05559  349 THR A CB  
2843 O OG1 . THR A 355 ? 0.26531 0.36011 0.27637 -0.00195 -0.00173 0.05190  349 THR A OG1 
2844 C CG2 . THR A 355 ? 0.24073 0.36146 0.26102 0.00087  -0.03265 0.05638  349 THR A CG2 
2845 N N   . ALA A 356 ? 0.33899 0.34400 0.33888 0.00292  -0.01351 0.02227  350 ALA A N   
2846 C CA  . ALA A 356 ? 0.37868 0.35330 0.35335 0.00169  -0.00425 0.01109  350 ALA A CA  
2847 C C   . ALA A 356 ? 0.43541 0.36011 0.35766 -0.01445 -0.00198 0.00938  350 ALA A C   
2848 O O   . ALA A 356 ? 0.42535 0.36373 0.34396 -0.05102 -0.01998 -0.04379 350 ALA A O   
2849 C CB  . ALA A 356 ? 0.34828 0.35683 0.35953 0.03261  0.00830  0.00965  350 ALA A CB  
2850 N N   . ARG A 357 ? 0.47224 0.36034 0.36219 -0.02270 -0.00047 0.03019  351 ARG A N   
2851 C CA  . ARG A 357 ? 0.49528 0.35342 0.36256 -0.02757 0.00564  0.04739  351 ARG A CA  
2852 C C   . ARG A 357 ? 0.46854 0.35237 0.36981 -0.05474 -0.00745 0.03716  351 ARG A C   
2853 O O   . ARG A 357 ? 0.48755 0.35398 0.38377 -0.07055 -0.00408 0.03118  351 ARG A O   
2854 C CB  . ARG A 357 ? 0.54047 0.34077 0.33816 -0.02704 0.01305  0.06272  351 ARG A CB  
2855 C CG  . ARG A 357 ? 0.56520 0.34294 0.31875 -0.02362 -0.01488 0.06900  351 ARG A CG  
2856 C CD  . ARG A 357 ? 0.59375 0.35247 0.32362 -0.02279 -0.01441 0.05405  351 ARG A CD  
2857 N NE  . ARG A 357 ? 0.61598 0.35829 0.30900 -0.02952 -0.03372 0.03885  351 ARG A NE  
2858 C CZ  . ARG A 357 ? 0.63587 0.35778 0.31698 -0.04342 -0.01868 0.02712  351 ARG A CZ  
2859 N NH1 . ARG A 357 ? 0.64627 0.36313 0.33565 -0.05187 -0.01302 0.00796  351 ARG A NH1 
2860 N NH2 . ARG A 357 ? 0.63125 0.35085 0.30243 -0.04154 -0.03086 0.02499  351 ARG A NH2 
2861 N N   . PHE A 358 ? 0.41945 0.33524 0.33003 -0.05007 -0.04498 0.03812  352 PHE A N   
2862 C CA  . PHE A 358 ? 0.39245 0.34372 0.28827 -0.06198 -0.09690 0.02967  352 PHE A CA  
2863 C C   . PHE A 358 ? 0.39713 0.36707 0.27404 -0.06261 -0.09180 0.01288  352 PHE A C   
2864 O O   . PHE A 358 ? 0.39717 0.36935 0.28465 -0.05883 -0.06997 0.00513  352 PHE A O   
2865 C CB  . PHE A 358 ? 0.37572 0.33011 0.27196 -0.06233 -0.12794 0.02649  352 PHE A CB  
2866 C CG  . PHE A 358 ? 0.37847 0.33245 0.30125 -0.05004 -0.13350 0.05855  352 PHE A CG  
2867 C CD1 . PHE A 358 ? 0.38900 0.33656 0.31305 -0.05408 -0.13110 0.07629  352 PHE A CD1 
2868 C CD2 . PHE A 358 ? 0.39546 0.33929 0.32094 -0.04448 -0.11464 0.07764  352 PHE A CD2 
2869 C CE1 . PHE A 358 ? 0.40108 0.34601 0.34515 -0.05258 -0.11328 0.08200  352 PHE A CE1 
2870 C CE2 . PHE A 358 ? 0.40238 0.34103 0.36206 -0.05074 -0.08958 0.07859  352 PHE A CE2 
2871 C CZ  . PHE A 358 ? 0.40218 0.34436 0.37273 -0.04892 -0.09168 0.08613  352 PHE A CZ  
2872 N N   . GLN A 359 ? 0.39196 0.38234 0.26386 -0.06975 -0.09708 0.00814  353 GLN A N   
2873 C CA  . GLN A 359 ? 0.43319 0.40192 0.30349 -0.08153 -0.07669 0.00101  353 GLN A CA  
2874 C C   . GLN A 359 ? 0.48703 0.42111 0.39539 -0.11348 -0.07471 -0.00156 353 GLN A C   
2875 O O   . GLN A 359 ? 0.52208 0.41960 0.44607 -0.14017 -0.05648 -0.02093 353 GLN A O   
2876 C CB  . GLN A 359 ? 0.41425 0.39372 0.24973 -0.05499 -0.04706 0.00016  353 GLN A CB  
2877 C CG  . GLN A 359 ? 0.37216 0.38180 0.21044 -0.03770 -0.04922 -0.00230 353 GLN A CG  
2878 C CD  . GLN A 359 ? 0.36757 0.38755 0.19662 -0.00483 -0.03247 -0.00223 353 GLN A CD  
2879 O OE1 . GLN A 359 ? 0.37437 0.40265 0.23534 0.00733  -0.03074 0.01015  353 GLN A OE1 
2880 N NE2 . GLN A 359 ? 0.34764 0.37566 0.14018 0.02745  -0.04460 0.00062  353 GLN A NE2 
2881 N N   . PRO A 360 ? 0.48547 0.44261 0.40523 -0.11041 -0.10740 -0.01082 354 PRO A N   
2882 C CA  . PRO A 360 ? 0.51294 0.45342 0.41560 -0.09502 -0.09900 -0.02354 354 PRO A CA  
2883 C C   . PRO A 360 ? 0.53325 0.45662 0.41607 -0.09904 -0.09068 -0.04892 354 PRO A C   
2884 O O   . PRO A 360 ? 0.55656 0.45388 0.42461 -0.11077 -0.06299 -0.07010 354 PRO A O   
2885 C CB  . PRO A 360 ? 0.51125 0.45569 0.41500 -0.08998 -0.10449 -0.01040 354 PRO A CB  
2886 C CG  . PRO A 360 ? 0.50362 0.45587 0.41404 -0.09404 -0.09852 -0.00724 354 PRO A CG  
2887 C CD  . PRO A 360 ? 0.48403 0.45065 0.40118 -0.09748 -0.11722 -0.00805 354 PRO A CD  
2888 S S   A SO4 B .   ? 0.20591 0.21672 0.18135 -0.02257 -0.03003 0.04444  401 SO4 A S   
2889 S S   B SO4 B .   ? 0.29282 0.32651 0.30526 -0.06896 0.02667  0.06430  401 SO4 A S   
2890 O O1  A SO4 B .   ? 0.22453 0.20594 0.17928 -0.01727 -0.02825 0.05075  401 SO4 A O1  
2891 O O1  B SO4 B .   ? 0.27734 0.32385 0.28720 -0.06659 -0.02809 0.04524  401 SO4 A O1  
2892 O O2  A SO4 B .   ? 0.19883 0.21608 0.19090 -0.01293 -0.00598 0.05767  401 SO4 A O2  
2893 O O2  B SO4 B .   ? 0.28919 0.31248 0.28473 -0.08073 0.01333  0.07922  401 SO4 A O2  
2894 O O3  A SO4 B .   ? 0.20845 0.21014 0.19125 -0.02794 -0.02873 0.04895  401 SO4 A O3  
2895 O O3  B SO4 B .   ? 0.30802 0.32125 0.29647 -0.06085 0.00757  0.07975  401 SO4 A O3  
2896 O O4  A SO4 B .   ? 0.18926 0.21959 0.19686 -0.00417 -0.03218 0.04850  401 SO4 A O4  
2897 O O4  B SO4 B .   ? 0.29211 0.33714 0.30423 -0.07056 0.00309  0.04414  401 SO4 A O4  
2898 S S   . SO4 C .   ? 0.92450 0.93107 0.89785 -0.02081 -0.03464 -0.00013 402 SO4 A S   
2899 O O1  . SO4 C .   ? 0.94282 0.93504 0.88888 -0.03773 -0.04001 -0.00368 402 SO4 A O1  
2900 O O2  . SO4 C .   ? 0.89988 0.93536 0.91646 -0.01958 -0.01788 -0.01771 402 SO4 A O2  
2901 O O3  . SO4 C .   ? 0.93256 0.93527 0.87693 0.01124  -0.03412 0.02420  402 SO4 A O3  
2902 O O4  . SO4 C .   ? 0.91586 0.93100 0.94708 -0.02270 0.00558  -0.00458 402 SO4 A O4  
2903 C C1  . WN2 D .   ? 0.23569 0.37524 0.26481 0.04658  -0.03687 0.09931  403 WN2 A C1  
2904 C C2  . WN2 D .   ? 0.24069 0.37926 0.24315 0.04192  -0.07757 0.10455  403 WN2 A C2  
2905 C C3  . WN2 D .   ? 0.24266 0.37394 0.23082 0.01553  -0.09854 0.10131  403 WN2 A C3  
2906 C C4  . WN2 D .   ? 0.26117 0.38377 0.25881 0.00186  -0.06715 0.09939  403 WN2 A C4  
2907 C C5  . WN2 D .   ? 0.31139 0.37656 0.27282 -0.00563 -0.10484 0.07469  403 WN2 A C5  
2908 C C6  . WN2 D .   ? 0.37381 0.38106 0.32177 -0.01421 -0.07553 0.06911  403 WN2 A C6  
2909 C C7  . WN2 D .   ? 0.40982 0.36519 0.32867 -0.02588 -0.05655 0.08296  403 WN2 A C7  
2910 C C8  . WN2 D .   ? 0.45559 0.36130 0.34192 -0.03855 -0.02500 0.05195  403 WN2 A C8  
2911 C C9  . WN2 D .   ? 0.45066 0.36312 0.33152 -0.04289 -0.02586 0.04870  403 WN2 A C9  
2912 C C10 . WN2 D .   ? 0.46356 0.38536 0.34661 -0.04183 0.00603  0.04610  403 WN2 A C10 
2913 C C11 . WN2 D .   ? 0.46191 0.39761 0.35455 -0.02622 0.01217  0.03722  403 WN2 A C11 
2914 O O1  . WN2 D .   ? 0.40288 0.38858 0.35329 0.01546  -0.04890 0.08795  403 WN2 A O1  
2915 O O2  . WN2 D .   ? 0.41949 0.37121 0.32454 -0.03995 -0.05840 0.10280  403 WN2 A O2  
2916 O O3  . WN2 D .   ? 0.47835 0.35762 0.35729 -0.02352 -0.00864 0.04465  403 WN2 A O3  
2917 C C12 . WN2 D .   ? 0.44606 0.40263 0.36164 0.00708  0.03811  0.04467  403 WN2 A C12 
2918 C C13 . WN2 D .   ? 0.41289 0.41174 0.34597 0.04673  0.04056  0.05818  403 WN2 A C13 
2919 O O4  . WN2 D .   ? 0.45413 0.45075 0.38869 0.09216  0.02386  0.05666  403 WN2 A O4  
2920 O O5  . WN2 D .   ? 0.33758 0.40130 0.29270 0.08421  0.00875  0.09603  403 WN2 A O5  
2921 C C14 . WN2 D .   ? 0.40766 0.42342 0.31855 0.07049  0.00567  0.07836  403 WN2 A C14 
2922 C C15 . WN2 D .   ? 0.41883 0.43129 0.34439 0.08515  0.01926  0.06455  403 WN2 A C15 
2923 C C16 . WN2 D .   ? 0.38568 0.41588 0.34222 0.07466  0.02656  0.05713  403 WN2 A C16 
2924 C C17 . WN2 D .   ? 0.34124 0.39926 0.31751 0.07787  0.01477  0.06999  403 WN2 A C17 
2925 C C18 . WN2 D .   ? 0.36457 0.39583 0.32476 0.05715  0.03065  0.05965  403 WN2 A C18 
2926 C C19 . WN2 D .   ? 0.28483 0.38585 0.29247 0.05717  -0.00799 0.07670  403 WN2 A C19 
2927 O O6  . WN2 D .   ? 0.26194 0.37986 0.26857 0.05536  -0.00681 0.08470  403 WN2 A O6  
2928 O O7  . WN2 D .   ? 0.28541 0.38220 0.27176 0.03982  -0.03987 0.08276  403 WN2 A O7  
2929 O O   . HOH E .   ? 0.56672 0.76500 0.67064 0.08153  0.25322  -0.00981 501 HOH A O   
2930 O O   . HOH E .   ? 0.26035 0.62229 0.61432 -0.08700 0.06019  -0.27905 502 HOH A O   
2931 O O   . HOH E .   ? 1.00563 0.67293 0.50988 -0.09435 0.04681  0.29901  503 HOH A O   
2932 O O   . HOH E .   ? 0.41981 0.41815 0.49214 0.03129  -0.12994 0.06312  504 HOH A O   
2933 O O   . HOH E .   ? 0.68979 0.61062 0.65449 0.36044  0.19602  0.15961  505 HOH A O   
2934 O O   . HOH E .   ? 0.50863 0.74317 0.70827 0.14972  0.15858  -0.28449 506 HOH A O   
2935 O O   . HOH E .   ? 0.36408 0.52113 0.82888 0.08439  -0.08024 -0.35291 507 HOH A O   
2936 O O   . HOH E .   ? 0.38347 0.63665 0.82479 0.22136  0.08316  0.19653  508 HOH A O   
2937 O O   . HOH E .   ? 0.83544 0.90894 0.39463 -0.26254 -0.17393 0.20527  509 HOH A O   
2938 O O   . HOH E .   ? 0.32072 0.41569 0.57205 -0.01918 0.15849  0.02443  510 HOH A O   
2939 O O   . HOH E .   ? 0.51111 0.53304 0.67677 0.23394  0.28824  0.25785  511 HOH A O   
2940 O O   . HOH E .   ? 0.59741 0.48699 0.35710 0.10184  0.04215  0.16437  512 HOH A O   
2941 O O   . HOH E .   ? 0.48582 0.37634 0.47000 0.00621  -0.19261 -0.15855 513 HOH A O   
2942 O O   . HOH E .   ? 0.45980 0.38444 0.33504 0.04711  0.01760  0.05582  514 HOH A O   
2943 O O   . HOH E .   ? 0.52877 0.53034 0.84155 0.06129  -0.34991 -0.19937 515 HOH A O   
2944 O O   . HOH E .   ? 0.60447 0.72506 0.63671 0.21385  -0.26940 0.12394  516 HOH A O   
2945 O O   . HOH E .   ? 0.53909 0.66190 0.39889 0.32729  -0.00369 0.05091  517 HOH A O   
2946 O O   . HOH E .   ? 0.55769 0.73299 0.52116 -0.11763 -0.25709 0.02901  518 HOH A O   
2947 O O   . HOH E .   ? 0.54914 0.48377 0.31506 -0.15558 -0.07508 0.04319  519 HOH A O   
2948 O O   . HOH E .   ? 0.42507 0.50083 0.84940 0.06675  0.28447  0.06008  520 HOH A O   
2949 O O   . HOH E .   ? 0.31018 0.38870 0.28162 0.10580  0.05884  0.03922  521 HOH A O   
2950 O O   . HOH E .   ? 0.43284 0.77503 0.54223 -0.22671 -0.09813 0.08092  522 HOH A O   
2951 O O   . HOH E .   ? 0.58129 0.57786 0.67649 -0.21607 -0.13544 0.32706  523 HOH A O   
2952 O O   . HOH E .   ? 0.50057 0.40469 0.41330 0.01306  -0.06719 -0.04131 524 HOH A O   
2953 O O   . HOH E .   ? 0.81300 0.78081 0.30851 -0.14990 0.13793  -0.14056 525 HOH A O   
2954 O O   . HOH E .   ? 0.17490 0.28843 0.22015 0.04856  -0.00705 -0.02905 526 HOH A O   
2955 O O   . HOH E .   ? 0.23151 0.32008 0.74726 -0.05133 -0.08427 -0.04190 527 HOH A O   
2956 O O   . HOH E .   ? 0.91417 0.48145 0.84127 -0.00467 0.28908  -0.20301 528 HOH A O   
2957 O O   . HOH E .   ? 0.30551 1.03386 0.74099 -0.07410 -0.12003 0.10351  529 HOH A O   
2958 O O   . HOH E .   ? 0.46688 0.26036 0.25235 -0.07064 -0.07997 0.06726  530 HOH A O   
2959 O O   . HOH E .   ? 0.24679 0.28663 0.27664 -0.00762 -0.04867 -0.03089 531 HOH A O   
2960 O O   . HOH E .   ? 0.49160 0.49991 1.04812 -0.16164 -0.21666 0.22614  532 HOH A O   
2961 O O   . HOH E .   ? 0.50922 0.68354 0.39699 -0.03329 0.16301  0.14493  533 HOH A O   
2962 O O   . HOH E .   ? 0.20499 0.41151 0.47518 0.10432  0.02500  -0.11702 534 HOH A O   
2963 O O   . HOH E .   ? 0.32932 0.81444 0.75803 -0.08507 -0.12130 0.37001  535 HOH A O   
2964 O O   . HOH E .   ? 0.71717 0.49187 0.26528 -0.22101 -0.02725 -0.02732 536 HOH A O   
2965 O O   . HOH E .   ? 0.50432 0.81511 0.79385 -0.01605 0.05980  -0.25657 537 HOH A O   
2966 O O   . HOH E .   ? 0.36175 0.22620 0.48471 -0.00254 0.01983  -0.04750 538 HOH A O   
2967 O O   . HOH E .   ? 0.41385 0.72529 1.17668 -0.09382 0.25078  0.03696  539 HOH A O   
2968 O O   . HOH E .   ? 0.66545 0.44465 0.82666 -0.08855 -0.12490 -0.11810 540 HOH A O   
2969 O O   . HOH E .   ? 0.35702 0.32464 0.36717 0.03660  -0.00707 0.06344  541 HOH A O   
2970 O O   . HOH E .   ? 0.36693 0.44286 0.33684 0.08157  0.00937  0.05789  542 HOH A O   
2971 O O   . HOH E .   ? 0.46278 0.39091 0.45269 -0.04288 0.01673  -0.00923 543 HOH A O   
2972 O O   . HOH E .   ? 0.43182 0.28586 0.23863 -0.05586 -0.02181 0.05822  544 HOH A O   
2973 O O   . HOH E .   ? 0.27000 0.26497 0.30471 0.01178  -0.05064 0.04793  545 HOH A O   
2974 O O   . HOH E .   ? 0.50548 0.29994 0.27804 0.03801  0.00582  -0.02462 546 HOH A O   
2975 O O   . HOH E .   ? 0.53794 0.22497 0.36402 0.01310  0.19071  0.07376  547 HOH A O   
2976 O O   . HOH E .   ? 0.91617 0.95968 0.27560 -0.00104 0.10587  0.04891  548 HOH A O   
2977 O O   . HOH E .   ? 0.55273 0.45006 0.45902 -0.00620 -0.07712 0.14555  549 HOH A O   
2978 O O   . HOH E .   ? 0.69778 0.79744 0.75927 0.03362  0.14870  0.44420  550 HOH A O   
2979 O O   . HOH E .   ? 0.28187 0.34363 0.20331 -0.04525 0.02561  -0.03340 551 HOH A O   
2980 O O   . HOH E .   ? 0.76243 0.50135 0.59013 0.32430  -0.03292 -0.13857 552 HOH A O   
2981 O O   . HOH E .   ? 0.50406 0.22894 0.35501 0.10818  -0.17223 -0.01623 553 HOH A O   
2982 O O   . HOH E .   ? 0.36665 0.36955 0.38540 -0.04572 0.02677  0.21071  554 HOH A O   
2983 O O   . HOH E .   ? 0.70376 0.26226 0.64507 -0.04160 -0.15474 0.02284  555 HOH A O   
2984 O O   . HOH E .   ? 0.21147 0.38561 0.42354 0.00852  -0.04028 -0.01482 556 HOH A O   
2985 O O   . HOH E .   ? 0.36022 0.35564 0.59357 0.02027  -0.08308 0.13890  557 HOH A O   
2986 O O   . HOH E .   ? 0.35956 0.52096 0.37589 -0.07317 0.03709  -0.02596 558 HOH A O   
2987 O O   . HOH E .   ? 0.27958 0.21764 0.21138 -0.06789 0.01102  0.01319  559 HOH A O   
2988 O O   . HOH E .   ? 0.62275 0.64205 0.48430 -0.28309 -0.11834 -0.00299 560 HOH A O   
2989 O O   . HOH E .   ? 0.66997 0.66008 0.51330 -0.12224 -0.03459 -0.17241 561 HOH A O   
2990 O O   . HOH E .   ? 0.46551 0.62279 0.36421 0.03639  -0.11794 0.03457  562 HOH A O   
2991 O O   . HOH E .   ? 0.55713 0.32351 0.32559 -0.00649 -0.14111 0.13850  563 HOH A O   
2992 O O   . HOH E .   ? 0.38580 0.35033 0.30089 -0.07024 0.02767  0.01956  564 HOH A O   
2993 O O   . HOH E .   ? 0.43716 0.59771 0.88011 -0.09656 -0.24071 0.35503  565 HOH A O   
2994 O O   . HOH E .   ? 0.41864 0.42490 0.39865 -0.06105 -0.00026 0.10800  566 HOH A O   
2995 O O   . HOH E .   ? 0.40251 0.39971 0.34746 0.08363  0.06628  -0.06118 567 HOH A O   
2996 O O   . HOH E .   ? 0.40995 0.61496 0.33493 0.07834  0.06326  -0.00222 568 HOH A O   
2997 O O   . HOH E .   ? 0.36772 0.49923 0.82286 -0.01057 0.03355  0.35461  569 HOH A O   
2998 O O   . HOH E .   ? 0.63494 0.61682 0.65403 0.11927  0.05387  -0.34680 570 HOH A O   
2999 O O   . HOH E .   ? 0.28516 0.33257 0.38283 -0.03687 0.17028  -0.03810 571 HOH A O   
3000 O O   . HOH E .   ? 0.48225 0.57073 0.63938 0.00621  0.17649  0.19275  572 HOH A O   
3001 O O   . HOH E .   ? 0.33966 0.47049 0.23719 -0.06436 0.05158  -0.01252 573 HOH A O   
3002 O O   . HOH E .   ? 0.24462 0.35232 0.28191 0.04322  -0.03650 -0.07776 574 HOH A O   
3003 O O   . HOH E .   ? 0.38181 0.25822 0.37735 0.03263  0.09252  0.00879  575 HOH A O   
3004 O O   . HOH E .   ? 0.41469 0.43690 0.37175 -0.01033 -0.11933 -0.00036 576 HOH A O   
3005 O O   . HOH E .   ? 0.46263 0.45450 0.64340 0.11405  0.01671  0.07697  577 HOH A O   
3006 O O   . HOH E .   ? 0.24680 0.63389 0.25935 -0.05056 0.00927  -0.09136 578 HOH A O   
3007 O O   . HOH E .   ? 0.66482 0.57410 0.93023 -0.04372 -0.06984 -0.11121 579 HOH A O   
3008 O O   . HOH E .   ? 0.73347 0.25493 0.62848 -0.00039 -0.26669 -0.06025 580 HOH A O   
3009 O O   . HOH E .   ? 0.27492 0.37483 0.41464 -0.05414 -0.02114 0.02198  581 HOH A O   
3010 O O   . HOH E .   ? 0.40332 0.64317 0.24826 -0.07143 -0.08410 0.13148  582 HOH A O   
3011 O O   . HOH E .   ? 0.43677 0.44437 0.34444 0.05321  0.04629  -0.01288 583 HOH A O   
3012 O O   . HOH E .   ? 0.59185 0.78286 0.58403 0.28565  0.16964  0.25259  584 HOH A O   
3013 O O   . HOH E .   ? 0.15818 0.27648 0.24398 0.00531  -0.01913 0.05137  585 HOH A O   
3014 O O   . HOH E .   ? 0.31849 0.32021 0.21523 0.02380  -0.04418 -0.03264 586 HOH A O   
3015 O O   . HOH E .   ? 0.47465 0.34745 0.17985 -0.06447 -0.07002 0.03748  587 HOH A O   
3016 O O   . HOH E .   ? 0.53309 0.59585 0.31215 -0.09209 -0.03452 0.01390  588 HOH A O   
3017 O O   . HOH E .   ? 0.21746 0.19266 0.19275 0.00944  -0.00441 0.00374  589 HOH A O   
3018 O O   . HOH E .   ? 0.36642 0.57800 0.49819 -0.01972 0.07170  -0.14277 590 HOH A O   
3019 O O   . HOH E .   ? 0.41292 0.47258 0.37628 -0.09254 0.05708  0.01005  591 HOH A O   
3020 O O   . HOH E .   ? 0.78078 0.32912 0.36879 0.03153  0.16113  0.10101  592 HOH A O   
3021 O O   . HOH E .   ? 0.15374 0.20136 0.20194 0.00285  0.01521  0.00381  593 HOH A O   
3022 O O   . HOH E .   ? 0.33012 0.54710 0.28203 -0.08020 -0.06956 -0.09605 594 HOH A O   
3023 O O   . HOH E .   ? 0.40865 0.84637 0.53497 -0.10587 -0.14917 -0.03402 595 HOH A O   
3024 O O   . HOH E .   ? 0.68583 0.52481 0.50765 -0.30782 -0.23241 0.21810  596 HOH A O   
3025 O O   . HOH E .   ? 0.44911 0.29949 0.85893 0.03910  0.01773  -0.11123 597 HOH A O   
3026 O O   . HOH E .   ? 0.27253 0.80044 0.41175 -0.04197 -0.08405 0.20905  598 HOH A O   
3027 O O   . HOH E .   ? 0.93882 0.67600 0.34326 0.06293  0.04902  0.20674  599 HOH A O   
3028 O O   . HOH E .   ? 0.62089 0.47288 0.58190 -0.06447 -0.08559 0.05967  600 HOH A O   
3029 O O   . HOH E .   ? 0.25384 0.48470 0.26631 0.13006  0.05252  0.02810  601 HOH A O   
3030 O O   . HOH E .   ? 0.76835 0.53808 0.41777 0.18779  0.04519  -0.07109 602 HOH A O   
3031 O O   . HOH E .   ? 0.23263 0.58880 0.32038 0.12125  0.06883  0.22768  603 HOH A O   
3032 O O   . HOH E .   ? 0.35362 0.26397 0.34940 0.04646  0.01873  -0.05612 604 HOH A O   
3033 O O   . HOH E .   ? 0.29612 0.23486 0.24603 -0.02581 -0.02931 0.00215  605 HOH A O   
3034 O O   . HOH E .   ? 0.25420 0.25044 0.39680 -0.02835 -0.00032 -0.01264 606 HOH A O   
3035 O O   . HOH E .   ? 0.15432 0.23167 0.20290 0.00153  -0.01413 -0.01298 607 HOH A O   
3036 O O   . HOH E .   ? 0.27149 0.75995 0.68230 0.03518  0.07951  -0.23642 608 HOH A O   
3037 O O   . HOH E .   ? 0.52687 0.98210 0.29608 0.21382  -0.08002 -0.03274 609 HOH A O   
3038 O O   . HOH E .   ? 0.26759 0.60675 0.99773 0.03487  0.08977  0.01892  610 HOH A O   
3039 O O   . HOH E .   ? 0.96549 0.52428 0.73945 -0.14776 -0.12052 0.08981  611 HOH A O   
3040 O O   . HOH E .   ? 0.26343 0.38178 0.31885 0.04748  0.07590  -0.01053 612 HOH A O   
3041 O O   . HOH E .   ? 0.48939 0.23469 0.28150 -0.08347 -0.06045 0.01891  613 HOH A O   
3042 O O   . HOH E .   ? 0.49200 0.61955 0.62033 -0.13794 -0.13777 0.05503  614 HOH A O   
3043 O O   . HOH E .   ? 0.24400 0.28677 0.16705 -0.00491 0.01535  -0.02333 615 HOH A O   
3044 O O   . HOH E .   ? 0.81407 0.53859 0.28093 -0.08098 -0.13161 0.05439  616 HOH A O   
3045 O O   . HOH E .   ? 0.33643 0.47946 0.59432 0.02133  -0.02255 -0.08943 617 HOH A O   
3046 O O   . HOH E .   ? 0.18327 0.16397 0.29072 -0.00320 -0.03510 0.02351  618 HOH A O   
3047 O O   . HOH E .   ? 1.04968 0.52184 0.41535 -0.21416 -0.17596 -0.07117 619 HOH A O   
3048 O O   . HOH E .   ? 0.69823 0.64577 0.32102 -0.26285 0.04683  0.11775  620 HOH A O   
3049 O O   . HOH E .   ? 0.27887 0.38665 0.18624 0.00838  -0.00166 -0.02029 621 HOH A O   
3050 O O   . HOH E .   ? 0.27242 0.48975 0.56685 -0.05209 0.02516  0.03711  622 HOH A O   
3051 O O   . HOH E .   ? 0.58585 0.50522 0.55958 -0.24412 0.08467  0.03539  623 HOH A O   
3052 O O   . HOH E .   ? 0.50441 0.74998 0.89114 -0.13355 -0.25181 -0.04859 624 HOH A O   
3053 O O   . HOH E .   ? 0.42664 0.41867 0.52393 0.18086  0.02363  -0.07998 625 HOH A O   
3054 O O   . HOH E .   ? 0.87306 0.52086 0.32687 0.19123  -0.03957 0.00508  626 HOH A O   
3055 O O   . HOH E .   ? 0.97250 0.38133 0.43667 -0.10771 0.03778  0.06711  627 HOH A O   
3056 O O   . HOH E .   ? 0.74972 0.60933 0.71476 -0.23840 0.34525  -0.31989 628 HOH A O   
3057 O O   . HOH E .   ? 0.42785 0.84108 0.44150 0.12916  -0.05391 0.25999  629 HOH A O   
3058 O O   . HOH E .   ? 0.20574 0.44020 0.42327 -0.05651 -0.03637 0.04603  630 HOH A O   
3059 O O   . HOH E .   ? 0.24911 0.29106 0.85400 0.03180  0.09622  0.18176  631 HOH A O   
3060 O O   . HOH E .   ? 0.37450 0.23643 0.31653 -0.03608 0.00876  0.02108  632 HOH A O   
3061 O O   . HOH E .   ? 0.32176 0.25104 0.26270 -0.11039 0.00484  -0.01182 633 HOH A O   
3062 O O   . HOH E .   ? 1.04166 0.38397 0.47254 -0.20682 -0.18799 -0.02189 634 HOH A O   
3063 O O   . HOH E .   ? 0.37282 0.40725 0.58414 0.17063  -0.16203 -0.08863 635 HOH A O   
3064 O O   . HOH E .   ? 0.36459 0.45374 0.57092 0.06262  0.15132  0.01293  636 HOH A O   
3065 O O   . HOH E .   ? 0.74394 0.39917 0.50617 -0.06530 -0.02223 0.04561  637 HOH A O   
3066 O O   . HOH E .   ? 0.41814 0.74845 0.61927 -0.19881 0.03225  0.25117  638 HOH A O   
3067 O O   . HOH E .   ? 0.14840 0.24661 0.20429 -0.03177 -0.00655 0.00959  639 HOH A O   
3068 O O   . HOH E .   ? 0.18950 0.25896 0.25385 0.01551  -0.02992 0.05733  640 HOH A O   
3069 O O   . HOH E .   ? 0.20853 0.27481 0.18807 0.03147  0.04578  0.02880  641 HOH A O   
3070 O O   . HOH E .   ? 0.49428 0.31768 0.47115 -0.03278 0.07076  0.05519  642 HOH A O   
3071 O O   . HOH E .   ? 0.22668 0.22756 0.25199 0.00731  -0.00348 0.04281  643 HOH A O   
3072 O O   . HOH E .   ? 0.35615 0.27833 0.30198 -0.09054 -0.03090 -0.00889 644 HOH A O   
3073 O O   . HOH E .   ? 0.43640 0.77528 0.41358 -0.24540 -0.07172 -0.02680 645 HOH A O   
3074 O O   . HOH E .   ? 0.68958 0.30963 0.43730 -0.15567 -0.01909 0.07604  646 HOH A O   
3075 O O   . HOH E .   ? 0.53679 0.95897 0.48679 0.19138  -0.22468 -0.12901 647 HOH A O   
3076 O O   . HOH E .   ? 0.52606 0.48745 0.57794 -0.14802 0.08096  0.17239  648 HOH A O   
3077 O O   . HOH E .   ? 0.31163 0.82773 0.34577 -0.01983 0.08155  -0.05567 649 HOH A O   
3078 O O   . HOH E .   ? 0.63709 0.29939 0.78599 0.01034  -0.26689 0.12203  650 HOH A O   
3079 O O   . HOH E .   ? 0.35594 0.39418 0.26305 0.06951  0.01915  0.03727  651 HOH A O   
3080 O O   . HOH E .   ? 0.13838 0.22912 0.17194 0.04901  0.00891  0.03169  652 HOH A O   
3081 O O   . HOH E .   ? 0.20557 0.31295 0.46119 -0.07055 -0.06073 0.04406  653 HOH A O   
3082 O O   . HOH E .   ? 0.28072 0.21953 0.38178 0.03907  -0.02635 0.00379  654 HOH A O   
3083 O O   . HOH E .   ? 0.29968 0.33332 0.40481 0.16793  0.01931  -0.08239 655 HOH A O   
3084 O O   . HOH E .   ? 0.27910 0.26854 0.51593 -0.07948 -0.04427 0.15561  656 HOH A O   
3085 O O   . HOH E .   ? 0.35925 0.46215 0.21439 0.02433  0.04386  -0.02014 657 HOH A O   
3086 O O   . HOH E .   ? 0.32595 0.58234 0.45167 0.03141  0.07976  -0.08759 658 HOH A O   
3087 O O   . HOH E .   ? 0.65098 0.48868 0.44638 -0.08608 -0.08822 -0.04993 659 HOH A O   
3088 O O   . HOH E .   ? 0.59497 0.75854 0.72746 0.04929  0.28925  0.06439  660 HOH A O   
3089 O O   . HOH E .   ? 0.20067 0.26541 0.32983 0.03158  0.00531  -0.05719 661 HOH A O   
3090 O O   . HOH E .   ? 0.24002 0.79631 0.35705 -0.10248 -0.02114 0.17846  662 HOH A O   
3091 O O   . HOH E .   ? 0.20726 0.47252 0.41566 -0.07386 -0.00592 -0.09707 663 HOH A O   
3092 O O   . HOH E .   ? 0.57112 0.82165 0.62417 0.18227  -0.23471 0.13901  664 HOH A O   
3093 O O   . HOH E .   ? 0.25746 0.60468 0.50966 0.02994  0.12464  0.20345  665 HOH A O   
3094 O O   . HOH E .   ? 0.43272 0.24903 0.50900 0.03225  0.03660  0.04537  666 HOH A O   
3095 O O   . HOH E .   ? 0.33068 0.17657 0.26946 0.01175  -0.05501 0.01767  667 HOH A O   
3096 O O   . HOH E .   ? 0.19899 0.16565 0.27686 0.01736  -0.02839 0.01085  668 HOH A O   
3097 O O   . HOH E .   ? 0.37445 0.37887 0.28767 -0.01138 -0.03120 -0.06513 669 HOH A O   
3098 O O   . HOH E .   ? 0.19463 0.48411 0.27338 0.01859  0.00699  -0.01217 670 HOH A O   
3099 O O   . HOH E .   ? 0.60006 0.55024 0.45438 -0.11948 0.17430  -0.25940 671 HOH A O   
3100 O O   . HOH E .   ? 0.36736 0.80493 0.37140 -0.03961 0.13720  -0.09246 672 HOH A O   
3101 O O   . HOH E .   ? 0.37236 0.44700 0.28414 -0.06037 -0.04893 0.06206  673 HOH A O   
3102 O O   . HOH E .   ? 0.50661 0.76036 0.35474 -0.01716 -0.02938 0.01123  674 HOH A O   
3103 O O   . HOH E .   ? 0.22767 0.36104 0.42172 -0.07090 -0.10945 0.06164  675 HOH A O   
3104 O O   . HOH E .   ? 0.41672 0.37458 0.51875 0.01525  0.00628  -0.05177 676 HOH A O   
3105 O O   . HOH E .   ? 0.40661 0.38934 0.25507 0.07877  -0.06695 0.00761  677 HOH A O   
3106 O O   . HOH E .   ? 0.29505 0.75430 0.66597 0.06634  -0.11308 -0.30837 678 HOH A O   
3107 O O   . HOH E .   ? 0.21563 0.44616 0.36802 0.04601  -0.01784 0.01219  679 HOH A O   
3108 O O   . HOH E .   ? 0.56198 0.92597 0.42080 0.05060  -0.09180 0.15294  680 HOH A O   
3109 O O   . HOH E .   ? 0.41377 0.69377 0.31697 -0.17625 0.03042  0.06039  681 HOH A O   
3110 O O   . HOH E .   ? 0.44764 0.46878 0.86348 -0.17662 -0.11070 0.22782  682 HOH A O   
3111 O O   . HOH E .   ? 0.28364 0.37461 0.22956 0.02218  -0.05007 0.01029  683 HOH A O   
3112 O O   . HOH E .   ? 0.27115 0.41393 0.31759 0.02118  -0.01595 -0.10027 684 HOH A O   
3113 O O   . HOH E .   ? 0.31534 0.67415 0.98701 0.03686  -0.12163 -0.27949 685 HOH A O   
3114 O O   . HOH E .   ? 0.46522 0.57653 0.31470 0.02190  0.14424  0.02308  686 HOH A O   
3115 O O   . HOH E .   ? 0.59303 0.42672 0.32126 0.06889  0.15049  0.01866  687 HOH A O   
3116 O O   . HOH E .   ? 0.16736 0.55169 0.31808 -0.07978 0.00309  -0.06801 688 HOH A O   
3117 O O   . HOH E .   ? 0.41520 0.65467 1.00560 0.15020  -0.04839 -0.11148 689 HOH A O   
3118 O O   . HOH E .   ? 0.56823 0.36800 0.42642 -0.06385 -0.06009 -0.04529 690 HOH A O   
3119 O O   . HOH E .   ? 0.76667 0.35537 0.29971 0.16581  0.07457  0.10685  691 HOH A O   
3120 O O   . HOH E .   ? 0.26162 0.43999 0.56631 -0.03580 -0.02842 0.01397  692 HOH A O   
3121 O O   . HOH E .   ? 0.80467 0.89926 0.38708 0.49994  -0.12651 -0.14141 693 HOH A O   
3122 O O   . HOH E .   ? 0.46710 1.05809 0.46870 0.13036  0.01149  -0.01747 694 HOH A O   
3123 O O   . HOH E .   ? 0.26923 0.37835 0.40168 0.03719  0.04390  0.17484  695 HOH A O   
3124 O O   . HOH E .   ? 0.57196 0.35144 0.45849 0.00941  -0.22161 -0.02921 696 HOH A O   
3125 O O   . HOH E .   ? 0.60789 0.77569 0.62570 -0.08119 -0.23645 0.26218  697 HOH A O   
3126 O O   . HOH E .   ? 0.55455 0.65842 0.92304 -0.32601 -0.12684 0.10981  698 HOH A O   
3127 O O   . HOH E .   ? 0.39565 0.45852 0.24806 0.23871  0.11586  0.13217  699 HOH A O   
3128 O O   . HOH E .   ? 0.59634 0.32819 0.42020 -0.06140 0.14586  0.05043  700 HOH A O   
3129 O O   . HOH E .   ? 0.17489 0.33426 0.44153 0.06039  -0.03024 -0.13413 701 HOH A O   
3130 O O   . HOH E .   ? 0.93683 0.70183 0.46498 -0.26215 0.23920  -0.22894 702 HOH A O   
3131 O O   . HOH E .   ? 0.72132 0.57077 0.65384 -0.24633 0.23081  -0.08582 703 HOH A O   
3132 O O   . HOH E .   ? 0.90844 0.45050 0.65421 -0.33253 0.06670  -0.04307 704 HOH A O   
3133 O O   . HOH E .   ? 0.52895 0.56555 0.82213 -0.12663 -0.11836 -0.12663 705 HOH A O   
3134 O O   . HOH E .   ? 0.27648 0.64226 0.36634 0.12570  0.03320  0.07033  706 HOH A O   
3135 O O   . HOH E .   ? 0.50234 0.39889 0.32802 0.10249  0.06371  -0.07708 707 HOH A O   
3136 O O   . HOH E .   ? 0.80383 0.33805 0.34200 -0.24191 0.02983  0.01795  708 HOH A O   
3137 O O   . HOH E .   ? 0.40670 0.70734 0.60740 -0.13490 -0.02486 -0.05709 709 HOH A O   
3138 O O   . HOH E .   ? 0.61944 0.57798 0.37544 0.15367  -0.03561 -0.04699 710 HOH A O   
3139 O O   . HOH E .   ? 0.48892 0.93412 0.69418 -0.06560 0.32489  -0.01814 711 HOH A O   
3140 O O   . HOH E .   ? 0.90270 0.37607 0.60132 -0.09502 0.42077  -0.06267 712 HOH A O   
3141 O O   . HOH E .   ? 0.50550 0.65377 0.78860 -0.11857 -0.24819 -0.14054 713 HOH A O   
3142 O O   . HOH E .   ? 0.38317 0.94543 0.40855 0.25009  -0.10148 -0.19616 714 HOH A O   
3143 O O   . HOH E .   ? 0.80004 0.78700 0.51794 0.06864  -0.23365 0.27005  715 HOH A O   
3144 O O   . HOH E .   ? 0.34200 0.66050 0.97522 -0.09821 -0.08286 0.09784  716 HOH A O   
3145 O O   . HOH E .   ? 0.37917 1.06131 0.37075 0.22993  0.03199  -0.05010 717 HOH A O   
3146 O O   . HOH E .   ? 0.19755 0.56770 0.38062 -0.07492 0.02257  0.01899  718 HOH A O   
3147 O O   . HOH E .   ? 0.30723 0.43838 0.40609 -0.02984 -0.11718 -0.00544 719 HOH A O   
3148 O O   . HOH E .   ? 0.45395 1.07093 0.40105 -0.13918 -0.00934 -0.25293 720 HOH A O   
3149 O O   . HOH E .   ? 0.59764 0.68292 0.43064 -0.34988 0.19741  -0.18708 721 HOH A O   
3150 O O   . HOH E .   ? 0.50715 0.55651 0.34724 -0.01577 0.04718  0.16120  722 HOH A O   
3151 O O   . HOH E .   ? 0.41877 0.78553 0.72567 0.21878  0.01547  0.07126  723 HOH A O   
3152 O O   . HOH E .   ? 0.73728 0.77588 0.50336 -0.03578 0.07240  0.25494  724 HOH A O   
3153 O O   . HOH E .   ? 0.54090 1.03200 0.61620 0.02520  -0.02468 0.31772  725 HOH A O   
3154 O O   . HOH E .   ? 0.64166 0.46172 0.34456 0.13377  0.03292  0.09768  726 HOH A O   
3155 O O   . HOH E .   ? 0.55932 0.59397 0.54355 0.15257  0.05711  0.22959  727 HOH A O   
3156 O O   . HOH E .   ? 0.86556 0.49373 0.40356 -0.18493 0.11727  -0.09077 728 HOH A O   
3157 O O   . HOH E .   ? 0.46684 0.32834 0.73913 0.06717  -0.05347 0.00388  729 HOH A O   
3158 O O   . HOH E .   ? 0.47077 0.82940 0.61884 -0.08643 -0.01925 0.20614  730 HOH A O   
3159 O O   . HOH E .   ? 0.34837 0.46469 0.39685 -0.03511 -0.05715 0.05424  731 HOH A O   
3160 O O   . HOH E .   ? 0.70989 0.48668 0.79720 -0.24490 0.40233  -0.24935 732 HOH A O   
3161 O O   . HOH E .   ? 0.88762 0.59193 0.47879 -0.27630 -0.05626 0.09511  733 HOH A O   
3162 O O   . HOH E .   ? 0.46004 1.24643 0.39076 0.05550  0.07899  0.02663  734 HOH A O   
3163 O O   . HOH E .   ? 0.40550 0.63385 0.68132 0.11978  -0.14629 0.14169  735 HOH A O   
3164 O O   . HOH E .   ? 0.56730 0.62445 0.37092 -0.32378 -0.17764 0.15830  736 HOH A O   
3165 O O   . HOH E .   ? 0.56397 0.50916 0.37526 0.22941  0.10204  -0.05805 737 HOH A O   
3166 O O   . HOH E .   ? 0.60863 0.74345 0.48678 0.12556  0.16316  0.22116  738 HOH A O   
3167 O O   . HOH E .   ? 0.58831 0.59099 0.80658 0.25141  -0.00476 -0.14397 739 HOH A O   
3168 O O   . HOH E .   ? 0.84888 0.56785 0.66105 -0.12663 -0.12663 -0.12663 740 HOH A O   
3169 O O   . HOH E .   ? 0.44848 0.71530 0.61516 -0.00062 0.03492  0.00738  741 HOH A O   
3170 O O   . HOH E .   ? 0.53414 1.18354 0.53704 0.08351  -0.11642 0.01983  742 HOH A O   
3171 O O   . HOH E .   ? 0.80291 0.53311 0.78724 -0.23425 -0.16307 -0.04146 743 HOH A O   
3172 O O   . HOH E .   ? 0.18108 0.46034 0.17731 0.03762  0.00800  -0.00663 744 HOH A O   
3173 O O   . HOH E .   ? 0.55329 0.86379 0.84012 -0.16604 -0.17673 -0.13225 745 HOH A O   
3174 O O   . HOH E .   ? 0.34283 0.69828 0.27215 0.06003  -0.11985 0.01321  746 HOH A O   
3175 O O   . HOH E .   ? 0.22559 0.60069 0.38345 -0.07092 0.07926  0.04290  747 HOH A O   
3176 O O   . HOH E .   ? 0.24845 0.23682 0.26433 0.00843  0.00374  -0.02538 748 HOH A O   
3177 O O   . HOH E .   ? 0.32162 0.43277 0.59350 0.04985  0.01826  0.01720  749 HOH A O   
3178 O O   . HOH E .   ? 0.83867 0.46726 0.86957 -0.24743 0.34184  -0.16099 750 HOH A O   
3179 O O   . HOH E .   ? 0.31735 0.42460 0.35175 -0.02787 -0.04654 -0.02266 751 HOH A O   
3180 O O   . HOH E .   ? 0.34636 0.74419 0.45889 0.07742  0.15342  -0.00278 752 HOH A O   
3181 O O   . HOH E .   ? 0.60859 0.71716 0.51038 -0.31327 -0.22780 0.08896  753 HOH A O   
3182 O O   . HOH E .   ? 0.73542 0.54207 0.41489 0.11501  -0.05226 0.10147  754 HOH A O   
3183 O O   . HOH E .   ? 0.89208 0.61002 0.54234 -0.14944 0.33741  0.06725  755 HOH A O   
3184 O O   . HOH E .   ? 0.48535 0.31056 0.33709 0.03510  0.13406  0.15484  756 HOH A O   
3185 O O   . HOH E .   ? 0.66455 0.59874 0.77654 -0.27253 -0.11049 0.00598  757 HOH A O   
3186 O O   . HOH E .   ? 0.71914 0.90555 0.86902 -0.15879 0.29918  0.21580  758 HOH A O   
3187 O O   . HOH E .   ? 0.48651 0.43233 0.46689 -0.03756 0.05862  -0.03542 759 HOH A O   
3188 O O   . HOH E .   ? 0.54865 0.93900 0.74737 0.35035  -0.08457 -0.28751 760 HOH A O   
3189 O O   . HOH E .   ? 0.40596 0.36685 0.86209 0.14362  -0.12533 -0.15130 761 HOH A O   
3190 O O   . HOH E .   ? 0.62395 0.83044 0.66703 -0.10634 0.17676  0.34158  762 HOH A O   
3191 O O   . HOH E .   ? 0.68453 0.68028 0.78334 -0.05682 -0.40578 0.19426  763 HOH A O   
3192 O O   . HOH E .   ? 0.54905 0.79585 0.48396 -0.29111 -0.19197 0.07443  764 HOH A O   
3193 O O   . HOH E .   ? 0.63066 0.79237 0.67415 -0.02467 -0.12663 0.24775  765 HOH A O   
3194 O O   . HOH E .   ? 0.52358 0.55828 0.59201 0.13255  0.23381  0.14074  766 HOH A O   
3195 O O   . HOH E .   ? 0.89788 0.60908 0.98524 0.23441  0.15396  0.19611  767 HOH A O   
3196 O O   . HOH E .   ? 0.63455 0.58501 0.52327 0.06391  0.19907  0.22078  768 HOH A O   
3197 O O   . HOH E .   ? 0.84875 0.70339 0.66500 0.07837  -0.19183 -0.10021 769 HOH A O   
3198 O O   . HOH E .   ? 1.07591 0.51115 0.36087 -0.20784 0.02273  0.04057  770 HOH A O   
3199 O O   . HOH E .   ? 0.50590 0.49843 0.23608 -0.04221 -0.00762 0.00871  771 HOH A O   
3200 O O   . HOH E .   ? 0.63465 0.78768 0.75361 -0.00422 -0.15248 0.19944  772 HOH A O   
3201 O O   . HOH E .   ? 0.61596 0.66121 0.68816 -0.04773 0.05764  0.09898  773 HOH A O   
3202 O O   . HOH E .   ? 0.44919 0.53686 0.47745 -0.09340 -0.01748 0.02149  774 HOH A O   
3203 O O   . HOH E .   ? 0.72163 0.73572 0.51106 -0.10898 -0.01062 -0.14822 775 HOH A O   
3204 O O   . HOH E .   ? 0.45750 0.62566 0.77285 -0.23193 -0.04139 -0.05009 776 HOH A O   
3205 O O   . HOH E .   ? 0.44760 0.99548 0.54983 -0.16683 0.15240  -0.03274 777 HOH A O   
3206 O O   . HOH E .   ? 0.75798 0.55668 0.67881 0.25102  -0.34124 -0.14621 778 HOH A O   
3207 O O   . HOH E .   ? 0.90015 0.52384 0.64639 0.04664  0.34045  0.11211  779 HOH A O   
3208 O O   . HOH E .   ? 0.21288 0.49580 0.38953 -0.05284 -0.02112 0.05966  780 HOH A O   
3209 O O   . HOH E .   ? 0.34579 0.43312 0.65325 -0.00280 0.07024  -0.07280 781 HOH A O   
3210 O O   . HOH E .   ? 0.87480 0.77687 0.38456 0.18863  0.19498  0.09459  782 HOH A O   
3211 O O   . HOH E .   ? 0.79963 0.59135 0.83417 -0.12264 0.00149  0.27265  783 HOH A O   
3212 O O   . HOH E .   ? 0.52531 0.62187 0.24969 0.08476  0.09953  0.05484  784 HOH A O   
3213 O O   . HOH E .   ? 0.48063 0.61613 0.76943 0.15252  0.17282  0.28358  785 HOH A O   
3214 O O   . HOH E .   ? 0.34797 0.48781 0.53005 0.01449  -0.01860 -0.00581 786 HOH A O   
3215 O O   . HOH E .   ? 0.56995 0.68392 0.62656 0.28438  0.03764  0.25230  787 HOH A O   
3216 O O   . HOH E .   ? 0.26887 0.43123 0.22827 0.02083  -0.03651 -0.07263 788 HOH A O   
3217 O O   . HOH E .   ? 0.52663 0.73949 0.50731 0.19517  0.22184  0.09905  789 HOH A O   
3218 O O   . HOH E .   ? 0.77876 0.41583 0.71276 0.01893  0.08351  -0.03411 790 HOH A O   
3219 O O   . HOH E .   ? 0.76579 0.30838 0.76118 0.03926  -0.06702 -0.03400 791 HOH A O   
3220 O O   . HOH E .   ? 0.53689 0.47100 0.36163 -0.17437 0.00300  0.00160  792 HOH A O   
3221 O O   . HOH E .   ? 0.30974 0.57234 0.69775 -0.00387 -0.02317 -0.18468 793 HOH A O   
3222 O O   . HOH E .   ? 0.48826 0.36590 0.41832 -0.15072 0.02376  0.17700  794 HOH A O   
3223 O O   . HOH E .   ? 0.54490 0.63529 0.58342 0.09812  -0.12647 0.05300  795 HOH A O   
3224 O O   . HOH E .   ? 0.42286 0.40559 0.50489 -0.03324 -0.07987 -0.02623 796 HOH A O   
3225 O O   . HOH E .   ? 0.67594 0.51725 0.78853 -0.12663 -0.04170 -0.03409 797 HOH A O   
3226 O O   . HOH E .   ? 0.75176 0.43734 0.33058 -0.06058 -0.03986 0.06292  798 HOH A O   
3227 O O   . HOH E .   ? 0.60866 0.69084 0.82502 0.33183  -0.12553 0.02701  799 HOH A O   
3228 O O   . HOH E .   ? 0.53196 0.80313 0.72930 0.19979  -0.05082 -0.39767 800 HOH A O   
3229 O O   . HOH E .   ? 0.79767 0.87767 0.34489 0.31933  0.09033  0.03233  801 HOH A O   
3230 O O   . HOH E .   ? 0.53644 0.52365 0.64629 0.15346  -0.22204 -0.00314 802 HOH A O   
3231 O O   . HOH E .   ? 0.82199 0.54339 0.31153 -0.04074 0.00536  -0.00397 803 HOH A O   
3232 O O   . HOH E .   ? 0.50051 0.73966 0.53877 0.05400  -0.02600 -0.06555 804 HOH A O   
3233 O O   . HOH E .   ? 0.63227 0.63205 0.76840 0.07327  -0.08958 0.19290  805 HOH A O   
3234 O O   . HOH E .   ? 0.49998 0.51560 0.46217 0.04878  0.13056  -0.11949 806 HOH A O   
3235 O O   . HOH E .   ? 0.47245 0.92967 1.09965 0.15590  -0.14976 0.15890  807 HOH A O   
3236 O O   . HOH E .   ? 0.65769 0.53409 0.56026 0.20277  -0.06701 0.10395  808 HOH A O   
3237 O O   . HOH E .   ? 0.54610 0.41701 0.49339 -0.01739 0.02530  -0.04821 809 HOH A O   
3238 O O   . HOH E .   ? 0.51135 0.61658 0.78650 -0.09858 0.08679  0.08498  810 HOH A O   
3239 O O   . HOH E .   ? 0.55186 0.64020 0.83640 -0.16125 0.27654  0.10496  811 HOH A O   
3240 O O   . HOH E .   ? 0.38244 0.76738 0.67629 0.04903  -0.21202 0.08194  812 HOH A O   
3241 O O   . HOH E .   ? 0.83711 0.51015 0.62030 0.06800  -0.11685 -0.14415 813 HOH A O   
3242 O O   . HOH E .   ? 0.77840 0.67575 0.68973 0.08644  -0.13513 0.13068  814 HOH A O   
# 
