data_8QR4
# 
_entry.id   8QR4 
# 
_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   8QR4         pdb_00008qr4 10.2210/pdb8qr4/pdb 
WWPDB D_1292133657 ?            ?                   
# 
_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                        8QR4 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8QR2 
_pdbx_database_related.content_type   unspecified 
# 
_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 
'(6~{S},7~{S},12~{S})-12-methyl-6,7,16,18-tetrakis(oxidanyl)-2,13-dioxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-8,14-dione' 
368.378   1   ? ? ? ? 
4 water       nat water 18.015    333 ? ? ? ? 
# 
_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 '(6~{S},7~{S},12~{S})-12-methyl-6,7,16,18-tetrakis(oxidanyl)-2,13-dioxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-8,14-dione' 
WN8 
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 
WN8 non-polymer         . 
'(6~{S},7~{S},12~{S})-12-methyl-6,7,16,18-tetrakis(oxidanyl)-2,13-dioxabicyclo[13.4.0]nonadeca-1(19),15,17-triene-8,14-dione' ? 
'C18 H24 O8'     368.378 
# 
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 336 330 330 ASP ASP A . n 
A 1 337 MET 337 331 ?   ?   ?   A . n 
A 1 338 GLU 338 332 ?   ?   ?   A . n 
A 1 339 LEU 339 333 ?   ?   ?   A . n 
A 1 340 ASP 340 334 ?   ?   ?   A . n 
A 1 341 ASP 341 335 ?   ?   ?   A . n 
A 1 342 LEU 342 336 ?   ?   ?   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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 WN8 ? ? WN8 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CME ? ? CME ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4 1   401 1   SO4 SO4 A . 
C 2 SO4 1   402 2   SO4 SO4 A . 
D 3 WN8 1   403 1   WN8 487 A . 
E 4 HOH 1   501 313 HOH HOH A . 
E 4 HOH 2   502 28  HOH HOH A . 
E 4 HOH 3   503 153 HOH HOH A . 
E 4 HOH 4   504 175 HOH HOH A . 
E 4 HOH 5   505 177 HOH HOH A . 
E 4 HOH 6   506 210 HOH HOH A . 
E 4 HOH 7   507 187 HOH HOH A . 
E 4 HOH 8   508 15  HOH HOH A . 
E 4 HOH 9   509 254 HOH HOH A . 
E 4 HOH 10  510 333 HOH HOH A . 
E 4 HOH 11  511 347 HOH HOH A . 
E 4 HOH 12  512 145 HOH HOH A . 
E 4 HOH 13  513 95  HOH HOH A . 
E 4 HOH 14  514 98  HOH HOH A . 
E 4 HOH 15  515 142 HOH HOH A . 
E 4 HOH 16  516 165 HOH HOH A . 
E 4 HOH 17  517 206 HOH HOH A . 
E 4 HOH 18  518 11  HOH HOH A . 
E 4 HOH 19  519 132 HOH HOH A . 
E 4 HOH 20  520 55  HOH HOH A . 
E 4 HOH 21  521 148 HOH HOH A . 
E 4 HOH 22  522 105 HOH HOH A . 
E 4 HOH 23  523 193 HOH HOH A . 
E 4 HOH 24  524 67  HOH HOH A . 
E 4 HOH 25  525 191 HOH HOH A . 
E 4 HOH 26  526 246 HOH HOH A . 
E 4 HOH 27  527 315 HOH HOH A . 
E 4 HOH 28  528 189 HOH HOH A . 
E 4 HOH 29  529 133 HOH HOH A . 
E 4 HOH 30  530 298 HOH HOH A . 
E 4 HOH 31  531 6   HOH HOH A . 
E 4 HOH 32  532 100 HOH HOH A . 
E 4 HOH 33  533 335 HOH HOH A . 
E 4 HOH 34  534 91  HOH HOH A . 
E 4 HOH 35  535 141 HOH HOH A . 
E 4 HOH 36  536 272 HOH HOH A . 
E 4 HOH 37  537 138 HOH HOH A . 
E 4 HOH 38  538 256 HOH HOH A . 
E 4 HOH 39  539 24  HOH HOH A . 
E 4 HOH 40  540 222 HOH HOH A . 
E 4 HOH 41  541 196 HOH HOH A . 
E 4 HOH 42  542 3   HOH HOH A . 
E 4 HOH 43  543 258 HOH HOH A . 
E 4 HOH 44  544 228 HOH HOH A . 
E 4 HOH 45  545 163 HOH HOH A . 
E 4 HOH 46  546 344 HOH HOH A . 
E 4 HOH 47  547 134 HOH HOH A . 
E 4 HOH 48  548 159 HOH HOH A . 
E 4 HOH 49  549 82  HOH HOH A . 
E 4 HOH 50  550 346 HOH HOH A . 
E 4 HOH 51  551 44  HOH HOH A . 
E 4 HOH 52  552 136 HOH HOH A . 
E 4 HOH 53  553 78  HOH HOH A . 
E 4 HOH 54  554 65  HOH HOH A . 
E 4 HOH 55  555 332 HOH HOH A . 
E 4 HOH 56  556 52  HOH HOH A . 
E 4 HOH 57  557 50  HOH HOH A . 
E 4 HOH 58  558 273 HOH HOH A . 
E 4 HOH 59  559 156 HOH HOH A . 
E 4 HOH 60  560 302 HOH HOH A . 
E 4 HOH 61  561 84  HOH HOH A . 
E 4 HOH 62  562 230 HOH HOH A . 
E 4 HOH 63  563 123 HOH HOH A . 
E 4 HOH 64  564 83  HOH HOH A . 
E 4 HOH 65  565 111 HOH HOH A . 
E 4 HOH 66  566 75  HOH HOH A . 
E 4 HOH 67  567 42  HOH HOH A . 
E 4 HOH 68  568 29  HOH HOH A . 
E 4 HOH 69  569 204 HOH HOH A . 
E 4 HOH 70  570 130 HOH HOH A . 
E 4 HOH 71  571 9   HOH HOH A . 
E 4 HOH 72  572 102 HOH HOH A . 
E 4 HOH 73  573 45  HOH HOH A . 
E 4 HOH 74  574 30  HOH HOH A . 
E 4 HOH 75  575 38  HOH HOH A . 
E 4 HOH 76  576 87  HOH HOH A . 
E 4 HOH 77  577 53  HOH HOH A . 
E 4 HOH 78  578 48  HOH HOH A . 
E 4 HOH 79  579 264 HOH HOH A . 
E 4 HOH 80  580 14  HOH HOH A . 
E 4 HOH 81  581 77  HOH HOH A . 
E 4 HOH 82  582 151 HOH HOH A . 
E 4 HOH 83  583 72  HOH HOH A . 
E 4 HOH 84  584 20  HOH HOH A . 
E 4 HOH 85  585 8   HOH HOH A . 
E 4 HOH 86  586 186 HOH HOH A . 
E 4 HOH 87  587 274 HOH HOH A . 
E 4 HOH 88  588 183 HOH HOH A . 
E 4 HOH 89  589 1   HOH HOH A . 
E 4 HOH 90  590 81  HOH HOH A . 
E 4 HOH 91  591 217 HOH HOH A . 
E 4 HOH 92  592 49  HOH HOH A . 
E 4 HOH 93  593 213 HOH HOH A . 
E 4 HOH 94  594 23  HOH HOH A . 
E 4 HOH 95  595 4   HOH HOH A . 
E 4 HOH 96  596 131 HOH HOH A . 
E 4 HOH 97  597 12  HOH HOH A . 
E 4 HOH 98  598 101 HOH HOH A . 
E 4 HOH 99  599 39  HOH HOH A . 
E 4 HOH 100 600 321 HOH HOH A . 
E 4 HOH 101 601 202 HOH HOH A . 
E 4 HOH 102 602 19  HOH HOH A . 
E 4 HOH 103 603 285 HOH HOH A . 
E 4 HOH 104 604 267 HOH HOH A . 
E 4 HOH 105 605 124 HOH HOH A . 
E 4 HOH 106 606 35  HOH HOH A . 
E 4 HOH 107 607 79  HOH HOH A . 
E 4 HOH 108 608 97  HOH HOH A . 
E 4 HOH 109 609 231 HOH HOH A . 
E 4 HOH 110 610 64  HOH HOH A . 
E 4 HOH 111 611 2   HOH HOH A . 
E 4 HOH 112 612 110 HOH HOH A . 
E 4 HOH 113 613 152 HOH HOH A . 
E 4 HOH 114 614 263 HOH HOH A . 
E 4 HOH 115 615 80  HOH HOH A . 
E 4 HOH 116 616 117 HOH HOH A . 
E 4 HOH 117 617 160 HOH HOH A . 
E 4 HOH 118 618 18  HOH HOH A . 
E 4 HOH 119 619 10  HOH HOH A . 
E 4 HOH 120 620 22  HOH HOH A . 
E 4 HOH 121 621 155 HOH HOH A . 
E 4 HOH 122 622 68  HOH HOH A . 
E 4 HOH 123 623 5   HOH HOH A . 
E 4 HOH 124 624 31  HOH HOH A . 
E 4 HOH 125 625 32  HOH HOH A . 
E 4 HOH 126 626 125 HOH HOH A . 
E 4 HOH 127 627 88  HOH HOH A . 
E 4 HOH 128 628 221 HOH HOH A . 
E 4 HOH 129 629 167 HOH HOH A . 
E 4 HOH 130 630 27  HOH HOH A . 
E 4 HOH 131 631 7   HOH HOH A . 
E 4 HOH 132 632 241 HOH HOH A . 
E 4 HOH 133 633 176 HOH HOH A . 
E 4 HOH 134 634 108 HOH HOH A . 
E 4 HOH 135 635 118 HOH HOH A . 
E 4 HOH 136 636 57  HOH HOH A . 
E 4 HOH 137 637 278 HOH HOH A . 
E 4 HOH 138 638 113 HOH HOH A . 
E 4 HOH 139 639 305 HOH HOH A . 
E 4 HOH 140 640 171 HOH HOH A . 
E 4 HOH 141 641 316 HOH HOH A . 
E 4 HOH 142 642 89  HOH HOH A . 
E 4 HOH 143 643 92  HOH HOH A . 
E 4 HOH 144 644 61  HOH HOH A . 
E 4 HOH 145 645 150 HOH HOH A . 
E 4 HOH 146 646 236 HOH HOH A . 
E 4 HOH 147 647 76  HOH HOH A . 
E 4 HOH 148 648 135 HOH HOH A . 
E 4 HOH 149 649 180 HOH HOH A . 
E 4 HOH 150 650 311 HOH HOH A . 
E 4 HOH 151 651 149 HOH HOH A . 
E 4 HOH 152 652 71  HOH HOH A . 
E 4 HOH 153 653 43  HOH HOH A . 
E 4 HOH 154 654 115 HOH HOH A . 
E 4 HOH 155 655 116 HOH HOH A . 
E 4 HOH 156 656 287 HOH HOH A . 
E 4 HOH 157 657 26  HOH HOH A . 
E 4 HOH 158 658 181 HOH HOH A . 
E 4 HOH 159 659 106 HOH HOH A . 
E 4 HOH 160 660 120 HOH HOH A . 
E 4 HOH 161 661 234 HOH HOH A . 
E 4 HOH 162 662 129 HOH HOH A . 
E 4 HOH 163 663 16  HOH HOH A . 
E 4 HOH 164 664 46  HOH HOH A . 
E 4 HOH 165 665 224 HOH HOH A . 
E 4 HOH 166 666 283 HOH HOH A . 
E 4 HOH 167 667 235 HOH HOH A . 
E 4 HOH 168 668 280 HOH HOH A . 
E 4 HOH 169 669 33  HOH HOH A . 
E 4 HOH 170 670 128 HOH HOH A . 
E 4 HOH 171 671 107 HOH HOH A . 
E 4 HOH 172 672 237 HOH HOH A . 
E 4 HOH 173 673 40  HOH HOH A . 
E 4 HOH 174 674 146 HOH HOH A . 
E 4 HOH 175 675 85  HOH HOH A . 
E 4 HOH 176 676 147 HOH HOH A . 
E 4 HOH 177 677 37  HOH HOH A . 
E 4 HOH 178 678 324 HOH HOH A . 
E 4 HOH 179 679 17  HOH HOH A . 
E 4 HOH 180 680 109 HOH HOH A . 
E 4 HOH 181 681 170 HOH HOH A . 
E 4 HOH 182 682 296 HOH HOH A . 
E 4 HOH 183 683 47  HOH HOH A . 
E 4 HOH 184 684 185 HOH HOH A . 
E 4 HOH 185 685 126 HOH HOH A . 
E 4 HOH 186 686 121 HOH HOH A . 
E 4 HOH 187 687 227 HOH HOH A . 
E 4 HOH 188 688 301 HOH HOH A . 
E 4 HOH 189 689 99  HOH HOH A . 
E 4 HOH 190 690 207 HOH HOH A . 
E 4 HOH 191 691 70  HOH HOH A . 
E 4 HOH 192 692 25  HOH HOH A . 
E 4 HOH 193 693 308 HOH HOH A . 
E 4 HOH 194 694 119 HOH HOH A . 
E 4 HOH 195 695 197 HOH HOH A . 
E 4 HOH 196 696 209 HOH HOH A . 
E 4 HOH 197 697 127 HOH HOH A . 
E 4 HOH 198 698 59  HOH HOH A . 
E 4 HOH 199 699 201 HOH HOH A . 
E 4 HOH 200 700 94  HOH HOH A . 
E 4 HOH 201 701 41  HOH HOH A . 
E 4 HOH 202 702 326 HOH HOH A . 
E 4 HOH 203 703 90  HOH HOH A . 
E 4 HOH 204 704 140 HOH HOH A . 
E 4 HOH 205 705 240 HOH HOH A . 
E 4 HOH 206 706 219 HOH HOH A . 
E 4 HOH 207 707 238 HOH HOH A . 
E 4 HOH 208 708 137 HOH HOH A . 
E 4 HOH 209 709 232 HOH HOH A . 
E 4 HOH 210 710 36  HOH HOH A . 
E 4 HOH 211 711 154 HOH HOH A . 
E 4 HOH 212 712 184 HOH HOH A . 
E 4 HOH 213 713 34  HOH HOH A . 
E 4 HOH 214 714 144 HOH HOH A . 
E 4 HOH 215 715 182 HOH HOH A . 
E 4 HOH 216 716 21  HOH HOH A . 
E 4 HOH 217 717 276 HOH HOH A . 
E 4 HOH 218 718 13  HOH HOH A . 
E 4 HOH 219 719 342 HOH HOH A . 
E 4 HOH 220 720 281 HOH HOH A . 
E 4 HOH 221 721 198 HOH HOH A . 
E 4 HOH 222 722 190 HOH HOH A . 
E 4 HOH 223 723 218 HOH HOH A . 
E 4 HOH 224 724 286 HOH HOH A . 
E 4 HOH 225 725 304 HOH HOH A . 
E 4 HOH 226 726 192 HOH HOH A . 
E 4 HOH 227 727 343 HOH HOH A . 
E 4 HOH 228 728 161 HOH HOH A . 
E 4 HOH 229 729 312 HOH HOH A . 
E 4 HOH 230 730 261 HOH HOH A . 
E 4 HOH 231 731 63  HOH HOH A . 
E 4 HOH 232 732 257 HOH HOH A . 
E 4 HOH 233 733 56  HOH HOH A . 
E 4 HOH 234 734 157 HOH HOH A . 
E 4 HOH 235 735 188 HOH HOH A . 
E 4 HOH 236 736 164 HOH HOH A . 
E 4 HOH 237 737 139 HOH HOH A . 
E 4 HOH 238 738 268 HOH HOH A . 
E 4 HOH 239 739 253 HOH HOH A . 
E 4 HOH 240 740 178 HOH HOH A . 
E 4 HOH 241 741 162 HOH HOH A . 
E 4 HOH 242 742 270 HOH HOH A . 
E 4 HOH 243 743 248 HOH HOH A . 
E 4 HOH 244 744 169 HOH HOH A . 
E 4 HOH 245 745 299 HOH HOH A . 
E 4 HOH 246 746 168 HOH HOH A . 
E 4 HOH 247 747 114 HOH HOH A . 
E 4 HOH 248 748 289 HOH HOH A . 
E 4 HOH 249 749 245 HOH HOH A . 
E 4 HOH 250 750 331 HOH HOH A . 
E 4 HOH 251 751 330 HOH HOH A . 
E 4 HOH 252 752 86  HOH HOH A . 
E 4 HOH 253 753 329 HOH HOH A . 
E 4 HOH 254 754 275 HOH HOH A . 
E 4 HOH 255 755 348 HOH HOH A . 
E 4 HOH 256 756 293 HOH HOH A . 
E 4 HOH 257 757 96  HOH HOH A . 
E 4 HOH 258 758 174 HOH HOH A . 
E 4 HOH 259 759 69  HOH HOH A . 
E 4 HOH 260 760 122 HOH HOH A . 
E 4 HOH 261 761 195 HOH HOH A . 
E 4 HOH 262 762 334 HOH HOH A . 
E 4 HOH 263 763 337 HOH HOH A . 
E 4 HOH 264 764 300 HOH HOH A . 
E 4 HOH 265 765 297 HOH HOH A . 
E 4 HOH 266 766 212 HOH HOH A . 
E 4 HOH 267 767 220 HOH HOH A . 
E 4 HOH 268 768 350 HOH HOH A . 
E 4 HOH 269 769 251 HOH HOH A . 
E 4 HOH 270 770 143 HOH HOH A . 
E 4 HOH 271 771 172 HOH HOH A . 
E 4 HOH 272 772 62  HOH HOH A . 
E 4 HOH 273 773 271 HOH HOH A . 
E 4 HOH 274 774 166 HOH HOH A . 
E 4 HOH 275 775 336 HOH HOH A . 
E 4 HOH 276 776 54  HOH HOH A . 
E 4 HOH 277 777 243 HOH HOH A . 
E 4 HOH 278 778 351 HOH HOH A . 
E 4 HOH 279 779 173 HOH HOH A . 
E 4 HOH 280 780 51  HOH HOH A . 
E 4 HOH 281 781 277 HOH HOH A . 
E 4 HOH 282 782 338 HOH HOH A . 
E 4 HOH 283 783 223 HOH HOH A . 
E 4 HOH 284 784 58  HOH HOH A . 
E 4 HOH 285 785 295 HOH HOH A . 
E 4 HOH 286 786 216 HOH HOH A . 
E 4 HOH 287 787 328 HOH HOH A . 
E 4 HOH 288 788 303 HOH HOH A . 
E 4 HOH 289 789 341 HOH HOH A . 
E 4 HOH 290 790 345 HOH HOH A . 
E 4 HOH 291 791 250 HOH HOH A . 
E 4 HOH 292 792 352 HOH HOH A . 
E 4 HOH 293 793 320 HOH HOH A . 
E 4 HOH 294 794 339 HOH HOH A . 
E 4 HOH 295 795 318 HOH HOH A . 
E 4 HOH 296 796 233 HOH HOH A . 
E 4 HOH 297 797 199 HOH HOH A . 
E 4 HOH 298 798 288 HOH HOH A . 
E 4 HOH 299 799 208 HOH HOH A . 
E 4 HOH 300 800 158 HOH HOH A . 
E 4 HOH 301 801 291 HOH HOH A . 
E 4 HOH 302 802 203 HOH HOH A . 
E 4 HOH 303 803 226 HOH HOH A . 
E 4 HOH 304 804 252 HOH HOH A . 
E 4 HOH 305 805 74  HOH HOH A . 
E 4 HOH 306 806 322 HOH HOH A . 
E 4 HOH 307 807 60  HOH HOH A . 
E 4 HOH 308 808 112 HOH HOH A . 
E 4 HOH 309 809 93  HOH HOH A . 
E 4 HOH 310 810 259 HOH HOH A . 
E 4 HOH 311 811 215 HOH HOH A . 
E 4 HOH 312 812 66  HOH HOH A . 
E 4 HOH 313 813 205 HOH HOH A . 
E 4 HOH 314 814 104 HOH HOH A . 
E 4 HOH 315 815 229 HOH HOH A . 
E 4 HOH 316 816 247 HOH HOH A . 
E 4 HOH 317 817 103 HOH HOH A . 
E 4 HOH 318 818 73  HOH HOH A . 
E 4 HOH 319 819 225 HOH HOH A . 
E 4 HOH 320 820 323 HOH HOH A . 
E 4 HOH 321 821 194 HOH HOH A . 
E 4 HOH 322 822 340 HOH HOH A . 
E 4 HOH 323 823 327 HOH HOH A . 
E 4 HOH 324 824 317 HOH HOH A . 
E 4 HOH 325 825 279 HOH HOH A . 
E 4 HOH 326 826 255 HOH HOH A . 
E 4 HOH 327 827 262 HOH HOH A . 
E 4 HOH 328 828 294 HOH HOH A . 
E 4 HOH 329 829 200 HOH HOH A . 
E 4 HOH 330 830 290 HOH HOH A . 
E 4 HOH 331 831 309 HOH HOH A . 
E 4 HOH 332 832 292 HOH HOH A . 
E 4 HOH 333 833 284 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 328 ? CG  ? A LYS 334 CG  
2  1 Y 1 A LYS 328 ? CD  ? A LYS 334 CD  
3  1 Y 1 A LYS 328 ? CE  ? A LYS 334 CE  
4  1 Y 1 A LYS 328 ? NZ  ? A LYS 334 NZ  
5  1 Y 1 A PHE 329 ? CG  ? A PHE 335 CG  
6  1 Y 1 A PHE 329 ? CD1 ? A PHE 335 CD1 
7  1 Y 1 A PHE 329 ? CD2 ? A PHE 335 CD2 
8  1 Y 1 A PHE 329 ? CE1 ? A PHE 335 CE1 
9  1 Y 1 A PHE 329 ? CE2 ? A PHE 335 CE2 
10 1 Y 1 A PHE 329 ? CZ  ? A PHE 335 CZ  
11 1 Y 1 A ASP 330 ? CG  ? A ASP 336 CG  
12 1 Y 1 A ASP 330 ? OD1 ? A ASP 336 OD1 
13 1 Y 1 A ASP 330 ? OD2 ? A ASP 336 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                   109.780 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QR4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.620 
_cell.length_a_esd                 ? 
_cell.length_b                     70.340 
_cell.length_b_esd                 ? 
_cell.length_c                     60.520 
_cell.length_c_esd                 ? 
_cell.volume                       194762.517 
_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                         8QR4 
_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                   8QR4 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.56 
_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         2021-12-11 
_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 ID14-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979288 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID14-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          20.98 
_reflns.entry_id                                       8QR4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.92 
_reflns.d_resolution_low                               30.92 
_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                                     29397 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_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                               0.83 
_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                                0.146 
_reflns.pdbx_Rpim_I_all                                0.079 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       99502 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.959 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.122 
_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                                    1.92 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6911 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1999 
_reflns_shell.percent_possible_obs                          99.9 
_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                              0.69 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.0 
_reflns_shell.pdbx_Rrim_I_all                               0.692 
_reflns_shell.pdbx_Rpim_I_all                               0.374 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.494 
_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                                  0.578 
_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                               29.22 
_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                                 8QR4 
_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                            1.92 
_refine.ls_d_res_low                             30.92 
_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                     29314 
_refine.ls_number_reflns_R_free                  1494 
_refine.ls_number_reflns_R_work                  27820 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.61 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1907 
_refine.ls_R_factor_R_free                       0.2242 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1889 
_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                 24.6989 
_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                            0.2101 
_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                       1.92 
_refine_hist.d_res_low                        30.92 
_refine_hist.number_atoms_solvent             333 
_refine_hist.number_atoms_total               3146 
_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        2777 
_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' ? 0.0066 ? 2946 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7043 ? 3993 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0445 ? 441  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0059 ? 502  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.3563 ? 410  ? 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' 1.92 1.98  . . 143 2527 99.63 . . . . 0.2709 . . . . . . . . . . . 0.3158 
'X-RAY DIFFRACTION' 1.98 2.05  . . 122 2517 99.62 . . . . 0.2265 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 2.05 2.14  . . 125 2518 99.17 . . . . 0.2169 . . . . . . . . . . . 0.2647 
'X-RAY DIFFRACTION' 2.14 2.23  . . 134 2519 99.36 . . . . 0.2223 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 2.23 2.35  . . 146 2491 99.43 . . . . 0.2390 . . . . . . . . . . . 0.2794 
'X-RAY DIFFRACTION' 2.35 2.50  . . 137 2533 99.78 . . . . 0.1935 . . . . . . . . . . . 0.2227 
'X-RAY DIFFRACTION' 2.50 2.69  . . 137 2509 99.47 . . . . 0.1837 . . . . . . . . . . . 0.2424 
'X-RAY DIFFRACTION' 2.69 2.96  . . 138 2517 99.74 . . . . 0.1877 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 2.96 3.39  . . 132 2553 99.93 . . . . 0.1733 . . . . . . . . . . . 0.2141 
'X-RAY DIFFRACTION' 3.39 4.27  . . 129 2561 99.89 . . . . 0.1562 . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 4.27 30.92 . . 151 2575 99.63 . . . . 0.1742 . . . . . . . . . . . 0.1942 
# 
_struct.entry_id                     8QR4 
_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        8QR4 
_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              8QR4 
_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 8QR4 HIS A 1 ? UNP P63086 ? ? 'expression tag' -5 1 
1 8QR4 HIS A 2 ? UNP P63086 ? ? 'expression tag' -4 2 
1 8QR4 HIS A 3 ? UNP P63086 ? ? 'expression tag' -3 3 
1 8QR4 HIS A 4 ? UNP P63086 ? ? 'expression tag' -2 4 
1 8QR4 HIS A 5 ? UNP P63086 ? ? 'expression tag' -1 5 
1 8QR4 HIS A 6 ? UNP P63086 ? ? 'expression tag' 0  6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 360   ? 
1 MORE         -23   ? 
1 'SSA (A^2)'  16380 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                monomer 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 65  ? PHE A 82  ? HIS A 59  PHE A 76  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 116 ? GLN A 123 ? LEU A 110 GLN A 117 1 ? 8  
HELX_P HELX_P3  AA3 SER A 126 ? ALA A 147 ? SER A 120 ALA A 141 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 155 ? SER A 157 ? LYS A 149 SER A 151 5 ? 3  
HELX_P HELX_P5  AA5 ASP A 179 ? ASP A 183 ? ASP A 173 ASP A 177 5 ? 5  
HELX_P HELX_P6  AA6 THR A 194 ? ARG A 198 ? THR A 188 ARG A 192 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 199 ? ASN A 205 ? ALA A 193 ASN A 199 1 ? 7  
HELX_P HELX_P8  AA8 LYS A 211 ? ASN A 228 ? LYS A 205 ASN A 222 1 ? 18 
HELX_P HELX_P9  AA9 LEU A 238 ? GLY A 249 ? LEU A 232 GLY A 243 1 ? 12 
HELX_P HELX_P10 AB1 SER A 252 ? CME A 258 ? SER A 246 CME A 252 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 261 ? LEU A 271 ? ASN A 255 LEU A 265 1 ? 11 
HELX_P HELX_P12 AB3 PRO A 278 ? PHE A 283 ? PRO A 272 PHE A 277 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 287 ? LEU A 298 ? ASP A 281 LEU A 292 1 ? 12 
HELX_P HELX_P14 AB5 GLU A 307 ? ALA A 313 ? GLU A 301 ALA A 307 1 ? 7  
HELX_P HELX_P15 AB6 HIS A 314 ? GLU A 318 ? HIS A 308 GLU A 312 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 322 ? GLU A 326 ? ASP A 316 GLU A 320 5 ? 5  
HELX_P HELX_P17 AB8 LYS A 344 ? THR A 355 ? LYS A 338 THR A 349 1 ? 12 
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 ? ? ? ? ? ? ? 1.329 ? ? 
covale2 covale both ? A CME 165 C ? ? ? 1_555 A ASP 166 N ? ? A CME 159 A ASP 160 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale3 covale both ? A ASN 257 C ? ? ? 1_555 A CME 258 N ? ? A ASN 251 A CME 252 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale4 covale both ? A CME 258 C ? ? ? 1_555 A ILE 259 N ? ? A CME 252 A ILE 253 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
# 
_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' 
# 
_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       0.22 
# 
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 ALA A 46  ? N ALA A 40  O VAL A 55  ? O VAL A 49  
AA2 3 4 N ALA A 56  ? N ALA A 50  O GLN A 109 ? O GLN A 103 
AA2 4 5 O VAL A 108 ? O VAL A 102 N ASP A 92  ? N ASP A 86  
AA3 1 2 N THR A 114 ? N THR A 108 O LEU A 161 ? O LEU A 155 
AA3 2 3 N LEU A 160 ? N LEU A 154 O LYS A 168 ? O LYS A 162 
AA4 1 2 N LEU A 150 ? N LEU A 144 O ARG A 176 ? O ARG A 170 
# 
_pdbx_entry_details.entry_id                   8QR4 
_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 ASN A 25  ? ? 56.96   73.90 
2 1 ASP A 147 ? ? -153.30 45.25 
3 1 ASP A 165 ? ? 63.51   96.43 
4 1 ASN A 199 ? ? -160.81 19.36 
5 1 LEU A 292 ? ? -94.10  43.75 
# 
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_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -13.4148395762 11.9374290509 31.2265630486 0.299507044284  ? -0.0306572231435 ? -0.055305863982   
? 0.338538565745 ? 0.0676308008733  ? 0.188731153424 ? 1.06665402299  ? -0.120652701095  ? -0.153843293898 ? 1.04954823515  ? 
-0.458415790534 ? 3.54412361146 ? -0.0563243390982 ? 0.123871655411  ? 0.218369677379  ? -0.0681432266594 ? 0.131165790676  ? 
0.0464006898014 ? -0.599479706577 ? -0.313634154154 ? -0.0393141302693 ? 
2 'X-RAY DIFFRACTION' ? refined -1.93207222969 8.0200210082  56.4603036314 0.0897687571716 ? 0.0127572019112  ? 0.0146668131049   
? 0.105600277967 ? 0.0155370449205  ? 0.113243529284 ? 1.35894352611  ? 0.674004153735   ? 0.713694594517  ? 0.970920743796 ? 
0.38282898099   ? 1.44610024684 ? -0.0400963599435 ? 0.0653175522333 ? 0.0764813846275 ? 0.0134642547166  ? 0.0461114481794 ? 
0.0140423975714 ? -0.027482847625 ? 0.0491354751113 ? -0.0134539126117 ? 
3 'X-RAY DIFFRACTION' ? refined -3.78545569403 1.92464609588 29.1223907116 0.310252433968  ? -0.0492412772385 ? -0.00228921305373 
? 0.403127905443 ? 0.00395585583629 ? 0.193477278367 ? 0.657078194456 ? -0.0125788408741 ? 0.0584854002403 ? 1.8465714944   ? 
-2.34022078152  ? 2.98695497588 ? -0.026782245231  ? 0.373610109378  ? 0.0583715715705 ? -0.435103968845  ? -0.253728620911 ? 
-0.21682306619  ? 0.351021415572  ? 0.716180452376  ? 0.259020752508   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 9   ? A 90  A 98  ? ? 
;chain 'A' and (resid    9  through   98 )
;
2 'X-RAY DIFFRACTION' 2 A 91  A 99  ? A 311 A 319 ? ? 
;chain 'A' and (resid   99  through  319 )
;
3 'X-RAY DIFFRACTION' 3 A 312 A 320 ? A 340 A 354 ? ? 
;chain 'A' and (resid  320  through  354 )
;
# 
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 832 ? 7.26 . 
2 1 O ? A HOH 833 ? 8.67 . 
# 
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 MET 331 ? A MET 337 
16 1 Y 1 A GLU 332 ? A GLU 338 
17 1 Y 1 A LEU 333 ? A LEU 339 
18 1 Y 1 A ASP 334 ? A ASP 340 
19 1 Y 1 A ASP 335 ? A ASP 341 
20 1 Y 1 A LEU 336 ? A LEU 342 
21 1 Y 1 A GLY 355 ? A GLY 361 
22 1 Y 1 A TYR 356 ? A TYR 362 
23 1 Y 1 A ARG 357 ? A ARG 363 
24 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 
WN8 C4   C N N 418 
WN8 C5   C N N 419 
WN8 C6   C N S 420 
WN8 C7   C N S 421 
WN8 C8   C N N 422 
WN8 C9   C N N 423 
WN8 C10  C N N 424 
WN8 C11  C Y N 425 
WN8 C12  C Y N 426 
WN8 C3   C N N 427 
WN8 C2   C N N 428 
WN8 C1   C N S 429 
WN8 C    C N N 430 
WN8 O    O N N 431 
WN8 C13  C Y N 432 
WN8 C14  C Y N 433 
WN8 C15  C Y N 434 
WN8 C16  C Y N 435 
WN8 C17  C N N 436 
WN8 O1   O N N 437 
WN8 O2   O N N 438 
WN8 O3   O N N 439 
WN8 O4   O N N 440 
WN8 O5   O N N 441 
WN8 O6   O N N 442 
WN8 O7   O N N 443 
WN8 H41  H N N 444 
WN8 H9   H N N 445 
WN8 H1   H N N 446 
WN8 H2   H N N 447 
WN8 H12  H N N 448 
WN8 H13  H N N 449 
WN8 H15  H N N 450 
WN8 H14  H N N 451 
WN8 H17  H N N 452 
WN8 H16  H N N 453 
WN8 H18  H N N 454 
WN8 H31  H N N 455 
WN8 H8   H N N 456 
WN8 H7   H N N 457 
WN8 H6   H N N 458 
WN8 H    H N N 459 
WN8 H4   H N N 460 
WN8 H5   H N N 461 
WN8 H3   H N N 462 
WN8 H20  H N N 463 
WN8 H10  H N N 464 
WN8 H11  H N N 465 
WN8 H19  H N N 466 
WN8 H21  H N N 467 
# 
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 
WN8 O6  C17  doub N N 401 
WN8 C17 O7   sing N N 402 
WN8 C17 C16  sing N N 403 
WN8 O7  C1   sing N N 404 
WN8 C1  C    sing N N 405 
WN8 C1  C2   sing N N 406 
WN8 C16 C15  doub Y N 407 
WN8 C16 C11  sing Y N 408 
WN8 C15 O5   sing N N 409 
WN8 C15 C14  sing Y N 410 
WN8 C14 C13  doub Y N 411 
WN8 C13 O4   sing N N 412 
WN8 C13 C12  sing Y N 413 
WN8 C12 C11  doub Y N 414 
WN8 C11 O3   sing N N 415 
WN8 O3  C10  sing N N 416 
WN8 C10 C9   sing N N 417 
WN8 C9  C8   sing N N 418 
WN8 C8  C7   sing N N 419 
WN8 C7  O2   sing N N 420 
WN8 C7  C6   sing N N 421 
WN8 C6  O1   sing N N 422 
WN8 C6  C5   sing N N 423 
WN8 C5  O    doub N N 424 
WN8 C5  C4   sing N N 425 
WN8 C4  C3   sing N N 426 
WN8 C3  C2   sing N N 427 
WN8 C4  H41  sing N N 428 
WN8 C4  H9   sing N N 429 
WN8 C6  H1   sing N N 430 
WN8 C7  H2   sing N N 431 
WN8 C8  H12  sing N N 432 
WN8 C8  H13  sing N N 433 
WN8 C9  H15  sing N N 434 
WN8 C9  H14  sing N N 435 
WN8 C10 H17  sing N N 436 
WN8 C10 H16  sing N N 437 
WN8 C12 H18  sing N N 438 
WN8 C3  H31  sing N N 439 
WN8 C3  H8   sing N N 440 
WN8 C2  H7   sing N N 441 
WN8 C2  H6   sing N N 442 
WN8 C1  H    sing N N 443 
WN8 C   H4   sing N N 444 
WN8 C   H5   sing N N 445 
WN8 C   H3   sing N N 446 
WN8 C14 H20  sing N N 447 
WN8 O1  H10  sing N N 448 
WN8 O2  H11  sing N N 449 
WN8 O4  H19  sing N N 450 
WN8 O5  H21  sing N N 451 
# 
_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                    8QR4 
_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]   0.020568 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007397 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014217 
_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]   0.017559 
_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  ? -21.64555 21.44696  20.60074 1.000 67.78019 ? 9   PRO A N   1 
ATOM   2    C CA  . PRO A 1 15  ? -21.27971 20.85361  21.89221 1.000 56.20907 ? 9   PRO A CA  1 
ATOM   3    C C   . PRO A 1 15  ? -21.79176 21.67415  23.07373 1.000 63.47074 ? 9   PRO A C   1 
ATOM   4    O O   . PRO A 1 15  ? -21.89469 22.89600  22.96761 1.000 69.38511 ? 9   PRO A O   1 
ATOM   5    C CB  . PRO A 1 15  ? -19.74530 20.84476  21.85698 1.000 53.04843 ? 9   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 15  ? -19.36863 21.82594  20.79430 1.000 54.78661 ? 9   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 15  ? -20.46323 21.76262  19.78265 1.000 57.74052 ? 9   PRO A CD  1 
ATOM   8    N N   . GLU A 1 16  ? -22.10934 21.00834  24.18370 1.000 73.93124 ? 10  GLU A N   1 
ATOM   9    C CA  . GLU A 1 16  ? -22.60747 21.70309  25.36789 1.000 68.52136 ? 10  GLU A CA  1 
ATOM   10   C C   . GLU A 1 16  ? -21.47536 22.48516  26.02230 1.000 67.71546 ? 10  GLU A C   1 
ATOM   11   O O   . GLU A 1 16  ? -20.53960 21.89800  26.57470 1.000 66.68335 ? 10  GLU A O   1 
ATOM   12   C CB  . GLU A 1 16  ? -23.22460 20.71693  26.35589 0.800 68.62259 ? 10  GLU A CB  1 
ATOM   13   C CG  . GLU A 1 16  ? -24.47565 21.25167  27.04731 0.700 68.56098 ? 10  GLU A CG  1 
ATOM   14   C CD  . GLU A 1 16  ? -25.29495 20.16910  27.72674 0.700 63.79553 ? 10  GLU A CD  1 
ATOM   15   O OE1 . GLU A 1 16  ? -25.59989 19.14754  27.07634 0.700 53.97303 ? 10  GLU A OE1 1 
ATOM   16   O OE2 . GLU A 1 16  ? -25.63766 20.34472  28.91635 0.700 48.87265 ? 10  GLU A OE2 1 
ATOM   17   N N   . MET A 1 17  ? -21.56040 23.81094  25.95805 1.000 77.29548 ? 11  MET A N   1 
ATOM   18   C CA  . MET A 1 17  ? -20.62122 24.66394  26.67025 1.000 63.40998 ? 11  MET A CA  1 
ATOM   19   C C   . MET A 1 17  ? -20.94661 24.63894  28.16005 1.000 62.10172 ? 11  MET A C   1 
ATOM   20   O O   . MET A 1 17  ? -22.11590 24.66208  28.55370 1.000 71.15191 ? 11  MET A O   1 
ATOM   21   C CB  . MET A 1 17  ? -20.70551 26.09761  26.14285 1.000 54.91413 ? 11  MET A CB  1 
ATOM   22   C CG  . MET A 1 17  ? -20.31188 26.29322  24.67453 1.000 65.95537 ? 11  MET A CG  1 
ATOM   23   S SD  . MET A 1 17  ? -18.91365 25.33140  24.06439 1.000 69.10134 ? 11  MET A SD  1 
ATOM   24   C CE  . MET A 1 17  ? -17.54161 26.27589  24.72259 1.000 64.29720 ? 11  MET A CE  1 
ATOM   25   N N   . VAL A 1 18  ? -19.90989 24.57796  28.99560 1.000 67.74787 ? 12  VAL A N   1 
ATOM   26   C CA  . VAL A 1 18  ? -20.07655 24.61181  30.44766 1.000 67.29900 ? 12  VAL A CA  1 
ATOM   27   C C   . VAL A 1 18  ? -19.04471 25.57013  31.02586 1.000 71.61045 ? 12  VAL A C   1 
ATOM   28   O O   . VAL A 1 18  ? -17.84166 25.39766  30.79938 1.000 69.81917 ? 12  VAL A O   1 
ATOM   29   C CB  . VAL A 1 18  ? -19.93233 23.22281  31.09701 1.000 65.32832 ? 12  VAL A CB  1 
ATOM   30   C CG1 . VAL A 1 18  ? -20.25611 23.30221  32.57967 1.000 61.85064 ? 12  VAL A CG1 1 
ATOM   31   C CG2 . VAL A 1 18  ? -20.84409 22.21229  30.42126 1.000 66.75959 ? 12  VAL A CG2 1 
ATOM   32   N N   . ARG A 1 19  ? -19.51273 26.57092  31.77777 1.000 73.52224 ? 13  ARG A N   1 
ATOM   33   C CA  . ARG A 1 19  ? -18.64589 27.58203  32.39016 1.000 69.67867 ? 13  ARG A CA  1 
ATOM   34   C C   . ARG A 1 19  ? -17.71511 28.22026  31.36240 1.000 78.15486 ? 13  ARG A C   1 
ATOM   35   O O   . ARG A 1 19  ? -16.55661 28.53044  31.64856 1.000 80.01141 ? 13  ARG A O   1 
ATOM   36   C CB  . ARG A 1 19  ? -17.84293 26.99502  33.55274 1.000 70.82625 ? 13  ARG A CB  1 
ATOM   37   C CG  . ARG A 1 19  ? -18.67694 26.50610  34.72296 0.900 68.55661 ? 13  ARG A CG  1 
ATOM   38   C CD  . ARG A 1 19  ? -19.34054 27.67346  35.43429 0.800 72.52539 ? 13  ARG A CD  1 
ATOM   39   N NE  . ARG A 1 19  ? -20.13819 27.23980  36.57452 0.700 68.99357 ? 13  ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 19  ? -19.64879 27.02809  37.78863 0.700 68.64231 ? 13  ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 19  ? -18.36543 27.20708  38.05718 0.700 72.50627 ? 13  ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 19  ? -20.46710 26.62800  38.75778 0.700 69.01989 ? 13  ARG A NH2 1 
ATOM   43   N N   . GLY A 1 20  ? -18.22807 28.42393  30.15251 1.000 75.08739 ? 14  GLY A N   1 
ATOM   44   C CA  . GLY A 1 20  ? -17.40494 28.96618  29.08978 1.000 78.43097 ? 14  GLY A CA  1 
ATOM   45   C C   . GLY A 1 20  ? -16.29422 28.04503  28.63971 1.000 86.59074 ? 14  GLY A C   1 
ATOM   46   O O   . GLY A 1 20  ? -15.23373 28.52010  28.22100 1.000 96.62787 ? 14  GLY A O   1 
ATOM   47   N N   . GLN A 1 21  ? -16.50307 26.73373  28.73094 1.000 77.72343 ? 15  GLN A N   1 
ATOM   48   C CA  . GLN A 1 21  ? -15.54704 25.75199  28.24438 1.000 68.86970 ? 15  GLN A CA  1 
ATOM   49   C C   . GLN A 1 21  ? -16.30217 24.63706  27.53926 1.000 63.04795 ? 15  GLN A C   1 
ATOM   50   O O   . GLN A 1 21  ? -17.42835 24.29735  27.91152 1.000 64.03368 ? 15  GLN A O   1 
ATOM   51   C CB  . GLN A 1 21  ? -14.69343 25.16394  29.37651 0.800 69.41970 ? 15  GLN A CB  1 
ATOM   52   C CG  . GLN A 1 21  ? -13.55044 26.05409  29.83339 0.700 68.77701 ? 15  GLN A CG  1 
ATOM   53   C CD  . GLN A 1 21  ? -12.61641 25.34707  30.79760 0.600 66.55026 ? 15  GLN A CD  1 
ATOM   54   O OE1 . GLN A 1 21  ? -12.67575 24.12732  30.95502 0.600 64.21784 ? 15  GLN A OE1 1 
ATOM   55   N NE2 . GLN A 1 21  ? -11.74884 26.11176  31.45037 0.600 67.96230 ? 15  GLN A NE2 1 
ATOM   56   N N   . VAL A 1 22  ? -15.67061 24.06925  26.51484 1.000 62.44406 ? 16  VAL A N   1 
ATOM   57   C CA  . VAL A 1 22  ? -16.28754 22.97723  25.77175 1.000 51.48215 ? 16  VAL A CA  1 
ATOM   58   C C   . VAL A 1 22  ? -16.28722 21.72216  26.63668 1.000 52.45052 ? 16  VAL A C   1 
ATOM   59   O O   . VAL A 1 22  ? -15.23759 21.27215  27.10953 1.000 43.98949 ? 16  VAL A O   1 
ATOM   60   C CB  . VAL A 1 22  ? -15.56842 22.74600  24.43551 1.000 62.10024 ? 16  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 22  ? -14.05681 22.71653  24.62841 1.000 69.50734 ? 16  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 22  ? -16.05344 21.45846  23.79006 1.000 58.88080 ? 16  VAL A CG2 1 
ATOM   63   N N   . PHE A 1 23  ? -17.47331 21.16823  26.87035 1.000 50.71449 ? 17  PHE A N   1 
ATOM   64   C CA  . PHE A 1 23  ? -17.65392 19.88926  27.55468 1.000 52.79840 ? 17  PHE A CA  1 
ATOM   65   C C   . PHE A 1 23  ? -18.44009 19.02195  26.57564 1.000 38.41674 ? 17  PHE A C   1 
ATOM   66   O O   . PHE A 1 23  ? -19.66969 18.94931  26.63849 1.000 47.28772 ? 17  PHE A O   1 
ATOM   67   C CB  . PHE A 1 23  ? -18.38206 20.05909  28.88889 1.000 43.19261 ? 17  PHE A CB  1 
ATOM   68   C CG  . PHE A 1 23  ? -17.92390 19.10939  29.96264 1.000 40.45182 ? 17  PHE A CG  1 
ATOM   69   C CD1 . PHE A 1 23  ? -16.79039 19.38121  30.71193 1.000 50.66697 ? 17  PHE A CD1 1 
ATOM   70   C CD2 . PHE A 1 23  ? -18.62424 17.94248  30.22008 1.000 40.25401 ? 17  PHE A CD2 1 
ATOM   71   C CE1 . PHE A 1 23  ? -16.37158 18.51055  31.70279 1.000 40.36457 ? 17  PHE A CE1 1 
ATOM   72   C CE2 . PHE A 1 23  ? -18.20861 17.06623  31.20742 1.000 37.85150 ? 17  PHE A CE2 1 
ATOM   73   C CZ  . PHE A 1 23  ? -17.08100 17.34938  31.94762 1.000 33.84593 ? 17  PHE A CZ  1 
ATOM   74   N N   . ASP A 1 24  ? -17.72191 18.37019  25.66442 1.000 42.41541 ? 18  ASP A N   1 
ATOM   75   C CA  . ASP A 1 24  ? -18.31097 17.76881  24.46770 1.000 41.66012 ? 18  ASP A CA  1 
ATOM   76   C C   . ASP A 1 24  ? -18.44404 16.26299  24.68481 1.000 40.53710 ? 18  ASP A C   1 
ATOM   77   O O   . ASP A 1 24  ? -17.57787 15.47913  24.29551 1.000 45.73019 ? 18  ASP A O   1 
ATOM   78   C CB  . ASP A 1 24  ? -17.45489 18.10087  23.25011 0.800 46.91974 ? 18  ASP A CB  1 
ATOM   79   C CG  . ASP A 1 24  ? -18.00736 17.51991  21.96995 0.800 41.94527 ? 18  ASP A CG  1 
ATOM   80   O OD1 . ASP A 1 24  ? -19.23345 17.29895  21.89830 0.600 37.32049 ? 18  ASP A OD1 1 
ATOM   81   O OD2 . ASP A 1 24  ? -17.21372 17.28844  21.03433 0.600 40.28759 ? 18  ASP A OD2 1 
ATOM   82   N N   . VAL A 1 25  ? -19.55580 15.85593  25.29924 1.000 43.86447 ? 19  VAL A N   1 
ATOM   83   C CA  . VAL A 1 25  ? -19.78116 14.46995  25.68507 1.000 40.49712 ? 19  VAL A CA  1 
ATOM   84   C C   . VAL A 1 25  ? -21.04887 13.89651  25.06517 1.000 40.60750 ? 19  VAL A C   1 
ATOM   85   O O   . VAL A 1 25  ? -21.44277 12.77817  25.39690 1.000 38.75034 ? 19  VAL A O   1 
ATOM   86   C CB  . VAL A 1 25  ? -19.81727 14.31869  27.21913 1.000 28.32916 ? 19  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 25  ? -18.51092 14.77877  27.82968 1.000 32.60971 ? 19  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 25  ? -20.97958 15.10511  27.80052 1.000 36.33063 ? 19  VAL A CG2 1 
ATOM   89   N N   . GLY A 1 26  ? -21.69655 14.63564  24.17273 1.000 39.45994 ? 20  GLY A N   1 
ATOM   90   C CA  . GLY A 1 26  ? -22.95907 14.20963  23.61128 1.000 49.22754 ? 20  GLY A CA  1 
ATOM   91   C C   . GLY A 1 26  ? -22.78497 13.19270  22.50566 1.000 53.67289 ? 20  GLY A C   1 
ATOM   92   O O   . GLY A 1 26  ? -21.67636 12.93186  22.00832 1.000 48.99583 ? 20  GLY A O   1 
ATOM   93   N N   . PRO A 1 27  ? -23.91317 12.59289  22.08629 1.000 41.12074 ? 21  PRO A N   1 
ATOM   94   C CA  . PRO A 1 27  ? -25.24444 12.87953  22.63347 1.000 37.28740 ? 21  PRO A CA  1 
ATOM   95   C C   . PRO A 1 27  ? -25.67476 11.95658  23.77578 1.000 42.83528 ? 21  PRO A C   1 
ATOM   96   O O   . PRO A 1 27  ? -26.76612 12.14471  24.31275 1.000 35.48264 ? 21  PRO A O   1 
ATOM   97   C CB  . PRO A 1 27  ? -26.16906 12.67491  21.43055 1.000 43.96904 ? 21  PRO A CB  1 
ATOM   98   C CG  . PRO A 1 27  ? -25.39950 11.81878  20.46239 1.000 41.97785 ? 21  PRO A CG  1 
ATOM   99   C CD  . PRO A 1 27  ? -23.97858 11.68556  20.92955 1.000 35.35450 ? 21  PRO A CD  1 
ATOM   100  N N   . ARG A 1 28  ? -24.84530 10.97273  24.13648 1.000 37.85019 ? 22  ARG A N   1 
ATOM   101  C CA  . ARG A 1 28  ? -25.25114 10.02221  25.16910 1.000 37.99199 ? 22  ARG A CA  1 
ATOM   102  C C   . ARG A 1 28  ? -25.44881 10.71140  26.51303 1.000 41.02035 ? 22  ARG A C   1 
ATOM   103  O O   . ARG A 1 28  ? -26.37946 10.38277  27.25792 1.000 40.97941 ? 22  ARG A O   1 
ATOM   104  C CB  . ARG A 1 28  ? -24.22312 8.89968   25.29986 1.000 34.09775 ? 22  ARG A CB  1 
ATOM   105  C CG  . ARG A 1 28  ? -24.49539 7.96836   26.47629 1.000 41.06189 ? 22  ARG A CG  1 
ATOM   106  C CD  . ARG A 1 28  ? -23.74012 6.65793   26.36319 1.000 38.24744 ? 22  ARG A CD  1 
ATOM   107  N NE  . ARG A 1 28  ? -23.68634 5.96560   27.64493 1.000 32.39128 ? 22  ARG A NE  1 
ATOM   108  C CZ  . ARG A 1 28  ? -23.02959 4.83413   27.86048 1.000 35.61993 ? 22  ARG A CZ  1 
ATOM   109  N NH1 . ARG A 1 28  ? -22.34353 4.23914   26.89851 1.000 35.03419 ? 22  ARG A NH1 1 
ATOM   110  N NH2 . ARG A 1 28  ? -23.05832 4.28788   29.07362 1.000 39.16190 ? 22  ARG A NH2 1 
ATOM   111  N N   . TYR A 1 29  ? -24.59292 11.67299  26.83762 1.000 34.40198 ? 23  TYR A N   1 
ATOM   112  C CA  . TYR A 1 29  ? -24.58618 12.31129  28.14622 1.000 36.26457 ? 23  TYR A CA  1 
ATOM   113  C C   . TYR A 1 29  ? -25.10532 13.73592  28.00548 1.000 40.98973 ? 23  TYR A C   1 
ATOM   114  O O   . TYR A 1 29  ? -24.53499 14.53902  27.25852 1.000 36.10108 ? 23  TYR A O   1 
ATOM   115  C CB  . TYR A 1 29  ? -23.18011 12.27837  28.74157 1.000 35.87557 ? 23  TYR A CB  1 
ATOM   116  C CG  . TYR A 1 29  ? -22.63680 10.87021  28.83691 1.000 30.47026 ? 23  TYR A CG  1 
ATOM   117  C CD1 . TYR A 1 29  ? -22.99154 10.03790  29.89146 1.000 30.73649 ? 23  TYR A CD1 1 
ATOM   118  C CD2 . TYR A 1 29  ? -21.79434 10.36142  27.85474 1.000 29.36732 ? 23  TYR A CD2 1 
ATOM   119  C CE1 . TYR A 1 29  ? -22.50643 8.74419   29.97857 1.000 28.29567 ? 23  TYR A CE1 1 
ATOM   120  C CE2 . TYR A 1 29  ? -21.30459 9.06959   27.93157 1.000 28.08777 ? 23  TYR A CE2 1 
ATOM   121  C CZ  . TYR A 1 29  ? -21.66337 8.26626   28.99654 1.000 34.08961 ? 23  TYR A CZ  1 
ATOM   122  O OH  . TYR A 1 29  ? -21.17862 6.98082   29.07671 1.000 30.95359 ? 23  TYR A OH  1 
ATOM   123  N N   . THR A 1 30  ? -26.19617 14.03641  28.70944 1.000 38.23860 ? 24  THR A N   1 
ATOM   124  C CA  . THR A 1 30  ? -26.88031 15.31716  28.60400 1.000 48.77527 ? 24  THR A CA  1 
ATOM   125  C C   . THR A 1 30  ? -27.21828 15.82124  30.00054 1.000 47.15760 ? 24  THR A C   1 
ATOM   126  O O   . THR A 1 30  ? -27.01807 15.12591  30.99977 1.000 48.97503 ? 24  THR A O   1 
ATOM   127  C CB  . THR A 1 30  ? -28.15727 15.20882  27.75638 1.000 50.58691 ? 24  THR A CB  1 
ATOM   128  O OG1 . THR A 1 30  ? -29.06894 14.29162  28.37479 1.000 43.06813 ? 24  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 30  ? -27.83541 14.72947  26.35107 1.000 42.02906 ? 24  THR A CG2 1 
ATOM   130  N N   . ASN A 1 31  ? -27.74071 17.04952  30.05605 1.000 48.77451 ? 25  ASN A N   1 
ATOM   131  C CA  . ASN A 1 31  ? -28.14682 17.70630  31.30026 1.000 55.54173 ? 25  ASN A CA  1 
ATOM   132  C C   . ASN A 1 31  ? -26.96821 17.78021  32.27715 1.000 53.79328 ? 25  ASN A C   1 
ATOM   133  O O   . ASN A 1 31  ? -26.89189 17.06521  33.27858 1.000 53.88019 ? 25  ASN A O   1 
ATOM   134  C CB  . ASN A 1 31  ? -29.35062 16.99034  31.92594 0.700 55.19761 ? 25  ASN A CB  1 
ATOM   135  C CG  . ASN A 1 31  ? -30.28979 17.94211  32.63893 0.600 55.63479 ? 25  ASN A CG  1 
ATOM   136  O OD1 . ASN A 1 31  ? -29.93574 19.08633  32.92273 0.600 59.18525 ? 25  ASN A OD1 1 
ATOM   137  N ND2 . ASN A 1 31  ? -31.49856 17.47396  32.92781 0.600 62.53428 ? 25  ASN A ND2 1 
ATOM   138  N N   . LEU A 1 32  ? -26.04990 18.68520  31.95099 1.000 48.65283 ? 26  LEU A N   1 
ATOM   139  C CA  . LEU A 1 32  ? -24.74564 18.75805  32.59536 1.000 49.26682 ? 26  LEU A CA  1 
ATOM   140  C C   . LEU A 1 32  ? -24.75907 19.80231  33.70455 1.000 57.92293 ? 26  LEU A C   1 
ATOM   141  O O   . LEU A 1 32  ? -25.21242 20.93273  33.49519 1.000 61.31047 ? 26  LEU A O   1 
ATOM   142  C CB  . LEU A 1 32  ? -23.65978 19.09607  31.57134 1.000 50.63701 ? 26  LEU A CB  1 
ATOM   143  C CG  . LEU A 1 32  ? -22.97257 17.95678  30.81228 1.000 50.11608 ? 26  LEU A CG  1 
ATOM   144  C CD1 . LEU A 1 32  ? -23.98113 17.04412  30.13685 1.000 51.83249 ? 26  LEU A CD1 1 
ATOM   145  C CD2 . LEU A 1 32  ? -22.01325 18.52596  29.78372 1.000 60.38676 ? 26  LEU A CD2 1 
ATOM   146  N N   . SER A 1 33  ? -24.25273 19.42225  34.87704 1.000 46.99036 ? 27  SER A N   1 
ATOM   147  C CA  . SER A 1 33  ? -24.11387 20.32483  36.01059 1.000 49.96097 ? 27  SER A CA  1 
ATOM   148  C C   . SER A 1 33  ? -22.68348 20.27274  36.52366 1.000 54.03568 ? 27  SER A C   1 
ATOM   149  O O   . SER A 1 33  ? -22.08707 19.19634  36.61789 1.000 48.91992 ? 27  SER A O   1 
ATOM   150  C CB  . SER A 1 33  ? -25.08354 19.96809  37.14630 1.000 46.24938 ? 27  SER A CB  1 
ATOM   151  O OG  . SER A 1 33  ? -26.24994 19.33934  36.64732 1.000 60.69873 ? 27  SER A OG  1 
ATOM   152  N N   . TYR A 1 34  ? -22.14235 21.43994  36.85749 1.000 52.08297 ? 28  TYR A N   1 
ATOM   153  C CA  . TYR A 1 34  ? -20.78269 21.51968  37.36901 1.000 55.11006 ? 28  TYR A CA  1 
ATOM   154  C C   . TYR A 1 34  ? -20.70969 20.95199  38.78167 1.000 60.67850 ? 28  TYR A C   1 
ATOM   155  O O   . TYR A 1 34  ? -21.60888 21.16119  39.60099 1.000 60.04701 ? 28  TYR A O   1 
ATOM   156  C CB  . TYR A 1 34  ? -20.30322 22.96999  37.35538 1.000 55.14547 ? 28  TYR A CB  1 
ATOM   157  C CG  . TYR A 1 34  ? -18.88393 23.16170  37.83327 0.700 61.35198 ? 28  TYR A CG  1 
ATOM   158  C CD1 . TYR A 1 34  ? -17.80971 22.99655  36.96870 0.700 59.64654 ? 28  TYR A CD1 1 
ATOM   159  C CD2 . TYR A 1 34  ? -18.61851 23.50755  39.15037 0.700 57.90701 ? 28  TYR A CD2 1 
ATOM   160  C CE1 . TYR A 1 34  ? -16.51332 23.17668  37.40399 0.700 55.65950 ? 28  TYR A CE1 1 
ATOM   161  C CE2 . TYR A 1 34  ? -17.32902 23.68480  39.59365 0.700 60.84789 ? 28  TYR A CE2 1 
ATOM   162  C CZ  . TYR A 1 34  ? -16.28135 23.51912  38.71817 0.700 61.77140 ? 28  TYR A CZ  1 
ATOM   163  O OH  . TYR A 1 34  ? -14.99740 23.70031  39.16598 0.700 67.82337 ? 28  TYR A OH  1 
ATOM   164  N N   . ILE A 1 35  ? -19.62564 20.22729  39.06677 1.000 60.73989 ? 29  ILE A N   1 
ATOM   165  C CA  . ILE A 1 35  ? -19.40602 19.60168  40.36541 1.000 61.20003 ? 29  ILE A CA  1 
ATOM   166  C C   . ILE A 1 35  ? -18.10084 20.07067  40.99987 1.000 67.71800 ? 29  ILE A C   1 
ATOM   167  O O   . ILE A 1 35  ? -18.06746 20.43963  42.17755 1.000 71.12099 ? 29  ILE A O   1 
ATOM   168  C CB  . ILE A 1 35  ? -19.43333 18.06063  40.26207 1.000 54.22125 ? 29  ILE A CB  1 
ATOM   169  C CG1 . ILE A 1 35  ? -20.80533 17.56896  39.81254 1.000 55.48914 ? 29  ILE A CG1 1 
ATOM   170  C CG2 . ILE A 1 35  ? -19.08234 17.44328  41.59696 1.000 70.13575 ? 29  ILE A CG2 1 
ATOM   171  C CD1 . ILE A 1 35  ? -20.93674 16.06239  39.86588 1.000 57.50529 ? 29  ILE A CD1 1 
ATOM   172  N N   . GLY A 1 36  ? -17.01016 20.05130  40.23685 1.000 61.16146 ? 30  GLY A N   1 
ATOM   173  C CA  . GLY A 1 36  ? -15.71912 20.42677  40.77766 1.000 62.91001 ? 30  GLY A CA  1 
ATOM   174  C C   . GLY A 1 36  ? -14.61735 20.48782  39.74100 1.000 62.26211 ? 30  GLY A C   1 
ATOM   175  O O   . GLY A 1 36  ? -14.87798 20.73511  38.55983 1.000 55.87330 ? 30  GLY A O   1 
ATOM   176  N N   . GLU A 1 37  ? -13.37722 20.26138  40.16962 1.000 57.99563 ? 31  GLU A N   1 
ATOM   177  C CA  . GLU A 1 37  ? -12.22239 20.32824  39.28505 1.000 60.24876 ? 31  GLU A CA  1 
ATOM   178  C C   . GLU A 1 37  ? -11.36336 19.08665  39.44853 1.000 63.76696 ? 31  GLU A C   1 
ATOM   179  O O   . GLU A 1 37  ? -11.08052 18.66222  40.57362 1.000 52.06453 ? 31  GLU A O   1 
ATOM   180  C CB  . GLU A 1 37  ? -11.37533 21.57502  39.55850 1.000 62.76911 ? 31  GLU A CB  1 
ATOM   181  C CG  . GLU A 1 37  ? -12.05580 22.87554  39.20479 1.000 60.21306 ? 31  GLU A CG  1 
ATOM   182  C CD  . GLU A 1 37  ? -12.11246 23.11089  37.70865 1.000 68.67809 ? 31  GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 37  ? -11.21586 22.61769  36.99164 1.000 67.00932 ? 31  GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 37  ? -13.05676 23.78686  37.24884 1.000 76.11900 ? 31  GLU A OE2 1 
ATOM   185  N N   . GLY A 1 38  ? -10.95606 18.51141  38.32582 1.000 58.04137 ? 32  GLY A N   1 
ATOM   186  C CA  . GLY A 1 38  ? -9.89826  17.52812  38.29791 1.000 51.04359 ? 32  GLY A CA  1 
ATOM   187  C C   . GLY A 1 38  ? -8.55611  18.20528  38.13477 1.000 49.48015 ? 32  GLY A C   1 
ATOM   188  O O   . GLY A 1 38  ? -8.40789  19.41313  38.33835 1.000 56.21430 ? 32  GLY A O   1 
ATOM   189  N N   . ALA A 1 39  ? -7.55973  17.41013  37.75080 1.000 46.95706 ? 33  ALA A N   1 
ATOM   190  C CA  . ALA A 1 39  ? -6.23314  17.97542  37.54468 1.000 52.14561 ? 33  ALA A CA  1 
ATOM   191  C C   . ALA A 1 39  ? -6.17420  18.79532  36.26235 1.000 57.66549 ? 33  ALA A C   1 
ATOM   192  O O   . ALA A 1 39  ? -5.55023  19.86323  36.23349 1.000 48.15046 ? 33  ALA A O   1 
ATOM   193  C CB  . ALA A 1 39  ? -5.18232  16.86612  37.52365 1.000 52.22736 ? 33  ALA A CB  1 
ATOM   194  N N   . TYR A 1 40  ? -6.81877  18.32066  35.18938 1.000 51.48511 ? 34  TYR A N   1 
ATOM   195  C CA  . TYR A 1 40  ? -6.61523  18.91103  33.87080 1.000 54.69119 ? 34  TYR A CA  1 
ATOM   196  C C   . TYR A 1 40  ? -7.94068  19.31896  33.24548 1.000 51.98128 ? 34  TYR A C   1 
ATOM   197  O O   . TYR A 1 40  ? -8.07670  19.35108  32.01857 1.000 43.48482 ? 34  TYR A O   1 
ATOM   198  C CB  . TYR A 1 40  ? -5.86866  17.94176  32.95992 1.000 50.84267 ? 34  TYR A CB  1 
ATOM   199  C CG  . TYR A 1 40  ? -4.62081  17.45442  33.63191 1.000 53.37938 ? 34  TYR A CG  1 
ATOM   200  C CD1 . TYR A 1 40  ? -3.78111  18.34000  34.28330 1.000 56.54220 ? 34  TYR A CD1 1 
ATOM   201  C CD2 . TYR A 1 40  ? -4.28786  16.10934  33.63004 1.000 46.64510 ? 34  TYR A CD2 1 
ATOM   202  C CE1 . TYR A 1 40  ? -2.66951  17.90574  34.94085 1.000 57.32790 ? 34  TYR A CE1 1 
ATOM   203  C CE2 . TYR A 1 40  ? -3.15203  15.66195  34.26209 1.000 53.08837 ? 34  TYR A CE2 1 
ATOM   204  C CZ  . TYR A 1 40  ? -2.34105  16.56886  34.91507 1.000 54.68220 ? 34  TYR A CZ  1 
ATOM   205  O OH  . TYR A 1 40  ? -1.19939  16.14720  35.55398 1.000 50.71836 ? 34  TYR A OH  1 
ATOM   206  N N   . GLY A 1 41  ? -8.91975  19.63305  34.07716 1.000 49.78900 ? 35  GLY A N   1 
ATOM   207  C CA  . GLY A 1 41  ? -10.23024 20.01499  33.59555 1.000 44.22356 ? 35  GLY A CA  1 
ATOM   208  C C   . GLY A 1 41  ? -11.26357 19.85494  34.68218 1.000 39.94217 ? 35  GLY A C   1 
ATOM   209  O O   . GLY A 1 41  ? -11.00581 19.30009  35.75110 1.000 47.99967 ? 35  GLY A O   1 
ATOM   210  N N   . MET A 1 42  ? -12.45753 20.35228  34.38438 1.000 41.70056 ? 36  MET A N   1 
ATOM   211  C CA  . MET A 1 42  ? -13.52575 20.35948  35.36665 1.000 44.92667 ? 36  MET A CA  1 
ATOM   212  C C   . MET A 1 42  ? -14.23443 19.00698  35.40900 1.000 37.25213 ? 36  MET A C   1 
ATOM   213  O O   . MET A 1 42  ? -14.04896 18.14216  34.54783 1.000 39.87255 ? 36  MET A O   1 
ATOM   214  C CB  . MET A 1 42  ? -14.52139 21.47740  35.06198 1.000 52.43124 ? 36  MET A CB  1 
ATOM   215  C CG  . MET A 1 42  ? -15.52468 21.14180  33.97234 0.900 49.74478 ? 36  MET A CG  1 
ATOM   216  S SD  . MET A 1 42  ? -16.61161 22.52995  33.59065 0.700 63.52989 ? 36  MET A SD  1 
ATOM   217  C CE  . MET A 1 42  ? -15.48533 23.90805  33.79065 0.650 56.71884 ? 36  MET A CE  1 
ATOM   218  N N   . VAL A 1 43  ? -15.05699 18.83300  36.43986 1.000 39.45450 ? 37  VAL A N   1 
ATOM   219  C CA  . VAL A 1 43  ? -15.85414 17.62945  36.63805 1.000 36.38719 ? 37  VAL A CA  1 
ATOM   220  C C   . VAL A 1 43  ? -17.32094 18.02990  36.60668 1.000 42.75608 ? 37  VAL A C   1 
ATOM   221  O O   . VAL A 1 43  ? -17.71541 19.00726  37.25318 1.000 49.07018 ? 37  VAL A O   1 
ATOM   222  C CB  . VAL A 1 43  ? -15.50622 16.92727  37.96341 1.000 42.31377 ? 37  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 43  ? -16.41548 15.72709  38.18807 1.000 38.42575 ? 37  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 43  ? -14.04502 16.50726  37.97404 1.000 36.28701 ? 37  VAL A CG2 1 
ATOM   225  N N   . CYS A 1 44  ? -18.12358 17.28194  35.85438 1.000 40.51444 ? 38  CYS A N   1 
ATOM   226  C CA  . CYS A 1 44  ? -19.54079 17.57118  35.70921 1.000 41.38374 ? 38  CYS A CA  1 
ATOM   227  C C   . CYS A 1 44  ? -20.36569 16.32165  35.97228 1.000 38.23799 ? 38  CYS A C   1 
ATOM   228  O O   . CYS A 1 44  ? -19.92867 15.19868  35.70685 1.000 34.42833 ? 38  CYS A O   1 
ATOM   229  C CB  . CYS A 1 44  ? -19.87456 18.10072  34.30695 1.000 43.39955 ? 38  CYS A CB  1 
ATOM   230  S SG  . CYS A 1 44  ? -19.30016 19.77458  33.95547 1.000 46.61961 ? 38  CYS A SG  1 
ATOM   231  N N   . SER A 1 45  ? -21.56337 16.53072  36.50873 1.000 37.95481 ? 39  SER A N   1 
ATOM   232  C CA  . SER A 1 45  ? -22.57640 15.49339  36.46386 1.000 36.35321 ? 39  SER A CA  1 
ATOM   233  C C   . SER A 1 45  ? -23.30861 15.56808  35.12989 1.000 35.59332 ? 39  SER A C   1 
ATOM   234  O O   . SER A 1 45  ? -23.30730 16.59749  34.45069 1.000 34.77862 ? 39  SER A O   1 
ATOM   235  C CB  . SER A 1 45  ? -23.56806 15.63090  37.61894 1.000 42.91605 ? 39  SER A CB  1 
ATOM   236  O OG  . SER A 1 45  ? -24.34354 16.80878  37.49074 1.000 39.13843 ? 39  SER A OG  1 
ATOM   237  N N   . ALA A 1 46  ? -23.92934 14.45543  34.75177 1.000 39.07939 ? 40  ALA A N   1 
ATOM   238  C CA  . ALA A 1 46  ? -24.62410 14.37508  33.47540 1.000 40.52235 ? 40  ALA A CA  1 
ATOM   239  C C   . ALA A 1 46  ? -25.56290 13.18297  33.50841 1.000 39.42792 ? 40  ALA A C   1 
ATOM   240  O O   . ALA A 1 46  ? -25.36246 12.23516  34.27034 1.000 35.38453 ? 40  ALA A O   1 
ATOM   241  C CB  . ALA A 1 46  ? -23.64453 14.25054  32.30374 1.000 32.08022 ? 40  ALA A CB  1 
ATOM   242  N N   . TYR A 1 47  ? -26.58722 13.23971  32.66395 1.000 37.00263 ? 41  TYR A N   1 
ATOM   243  C CA  . TYR A 1 47  ? -27.53923 12.14616  32.53500 1.000 39.16951 ? 41  TYR A CA  1 
ATOM   244  C C   . TYR A 1 47  ? -27.07269 11.19874  31.43638 1.000 36.69879 ? 41  TYR A C   1 
ATOM   245  O O   . TYR A 1 47  ? -26.95999 11.59685  30.27146 1.000 32.97277 ? 41  TYR A O   1 
ATOM   246  C CB  . TYR A 1 47  ? -28.94090 12.67130  32.22924 0.800 38.51701 ? 41  TYR A CB  1 
ATOM   247  C CG  . TYR A 1 47  ? -29.95800 11.56876  32.05303 0.700 40.00031 ? 41  TYR A CG  1 
ATOM   248  C CD1 . TYR A 1 47  ? -30.39452 10.82147  33.13874 0.600 39.64044 ? 41  TYR A CD1 1 
ATOM   249  C CD2 . TYR A 1 47  ? -30.47293 11.26609  30.79990 0.600 45.97819 ? 41  TYR A CD2 1 
ATOM   250  C CE1 . TYR A 1 47  ? -31.32086 9.80802   32.98296 0.600 37.76966 ? 41  TYR A CE1 1 
ATOM   251  C CE2 . TYR A 1 47  ? -31.40052 10.25439  30.63415 0.600 39.15111 ? 41  TYR A CE2 1 
ATOM   252  C CZ  . TYR A 1 47  ? -31.82037 9.52894   31.72923 0.600 42.04998 ? 41  TYR A CZ  1 
ATOM   253  O OH  . TYR A 1 47  ? -32.74251 8.52067   31.56924 0.600 46.47982 ? 41  TYR A OH  1 
ATOM   254  N N   . ASP A 1 48  ? -26.79641 9.95229   31.81242 1.000 37.36863 ? 42  ASP A N   1 
ATOM   255  C CA  . ASP A 1 48  ? -26.46008 8.90218   30.85684 1.000 33.76497 ? 42  ASP A CA  1 
ATOM   256  C C   . ASP A 1 48  ? -27.75395 8.43581   30.20199 1.000 41.62919 ? 42  ASP A C   1 
ATOM   257  O O   . ASP A 1 48  ? -28.57332 7.76600   30.83882 1.000 37.29573 ? 42  ASP A O   1 
ATOM   258  C CB  . ASP A 1 48  ? -25.74609 7.75367   31.56666 1.000 34.38584 ? 42  ASP A CB  1 
ATOM   259  C CG  . ASP A 1 48  ? -25.21698 6.69410   30.61346 1.000 37.52341 ? 42  ASP A CG  1 
ATOM   260  O OD1 . ASP A 1 48  ? -25.83398 6.44508   29.55806 1.000 40.54270 ? 42  ASP A OD1 1 
ATOM   261  O OD2 . ASP A 1 48  ? -24.17295 6.08973   30.93911 1.000 47.15109 ? 42  ASP A OD2 1 
ATOM   262  N N   . ASN A 1 49  ? -27.94128 8.78459   28.92777 1.000 41.20053 ? 43  ASN A N   1 
ATOM   263  C CA  . ASN A 1 49  ? -29.19408 8.46293   28.25501 1.000 48.83025 ? 43  ASN A CA  1 
ATOM   264  C C   . ASN A 1 49  ? -29.32104 6.98184   27.92267 1.000 46.04869 ? 43  ASN A C   1 
ATOM   265  O O   . ASN A 1 49  ? -30.42941 6.52390   27.62795 1.000 57.39048 ? 43  ASN A O   1 
ATOM   266  C CB  . ASN A 1 49  ? -29.34178 9.29974   26.98422 1.000 46.04668 ? 43  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 49  ? -29.65518 10.75292  27.28127 1.000 44.88158 ? 43  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 49  ? -30.81933 11.14158  27.37888 1.000 47.65042 ? 43  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 49  ? -28.61503 11.56465  27.42838 1.000 40.79910 ? 43  ASN A ND2 1 
ATOM   270  N N   . LEU A 1 50  ? -28.22544 6.22270   27.96636 1.000 41.86258 ? 44  LEU A N   1 
ATOM   271  C CA  . LEU A 1 50  ? -28.31802 4.78704   27.72241 1.000 44.41180 ? 44  LEU A CA  1 
ATOM   272  C C   . LEU A 1 50  ? -28.69492 4.03608   28.99546 1.000 58.18203 ? 44  LEU A C   1 
ATOM   273  O O   . LEU A 1 50  ? -29.76623 3.42494   29.07515 1.000 49.60063 ? 44  LEU A O   1 
ATOM   274  C CB  . LEU A 1 50  ? -27.00024 4.25515   27.15294 1.000 51.73821 ? 44  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 50  ? -26.87791 2.72794   27.13939 1.000 45.64705 ? 44  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 50  ? -27.67791 2.13167   25.99166 1.000 52.25498 ? 44  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 50  ? -25.42249 2.30319   27.05391 1.000 46.56412 ? 44  LEU A CD2 1 
ATOM   278  N N   . ASN A 1 51  ? -27.82796 4.07775   30.00753 1.000 44.03770 ? 45  ASN A N   1 
ATOM   279  C CA  . ASN A 1 51  ? -28.09245 3.37996   31.25985 1.000 45.82393 ? 45  ASN A CA  1 
ATOM   280  C C   . ASN A 1 51  ? -29.10843 4.09466   32.14172 1.000 47.78635 ? 45  ASN A C   1 
ATOM   281  O O   . ASN A 1 51  ? -29.39751 3.60237   33.23771 1.000 40.05890 ? 45  ASN A O   1 
ATOM   282  C CB  . ASN A 1 51  ? -26.79022 3.17378   32.03866 1.000 47.23702 ? 45  ASN A CB  1 
ATOM   283  C CG  . ASN A 1 51  ? -25.89678 2.12265   31.40990 1.000 53.91282 ? 45  ASN A CG  1 
ATOM   284  O OD1 . ASN A 1 51  ? -24.72183 2.36968   31.13625 1.000 62.29491 ? 45  ASN A OD1 1 
ATOM   285  N ND2 . ASN A 1 51  ? -26.45739 0.94409   31.16211 1.000 59.84258 ? 45  ASN A ND2 1 
ATOM   286  N N   . LYS A 1 52  ? -29.67111 5.21688   31.67973 1.000 45.94967 ? 46  LYS A N   1 
ATOM   287  C CA  . LYS A 1 52  ? -30.71487 5.95926   32.40063 1.000 43.52850 ? 46  LYS A CA  1 
ATOM   288  C C   . LYS A 1 52  ? -30.32620 6.21839   33.85600 1.000 48.44521 ? 46  LYS A C   1 
ATOM   289  O O   . LYS A 1 52  ? -31.12750 6.05726   34.77880 1.000 46.54865 ? 46  LYS A O   1 
ATOM   290  C CB  . LYS A 1 52  ? -32.07237 5.25127   32.30098 0.800 43.91406 ? 46  LYS A CB  1 
ATOM   291  C CG  . LYS A 1 52  ? -32.14650 4.15898   31.23718 0.700 48.65269 ? 46  LYS A CG  1 
ATOM   292  C CD  . LYS A 1 52  ? -33.54140 3.58281   31.09072 0.600 58.59450 ? 46  LYS A CD  1 
ATOM   293  C CE  . LYS A 1 52  ? -33.62005 2.68363   29.86625 0.600 64.13731 ? 46  LYS A CE  1 
ATOM   294  N NZ  . LYS A 1 52  ? -33.34937 1.25682   30.19808 0.600 68.84674 ? 46  LYS A NZ  1 
ATOM   295  N N   . VAL A 1 53  ? -29.07188 6.62011   34.05862 1.000 46.72858 ? 47  VAL A N   1 
ATOM   296  C CA  . VAL A 1 53  ? -28.56039 7.03089   35.36122 1.000 50.28323 ? 47  VAL A CA  1 
ATOM   297  C C   . VAL A 1 53  ? -27.74393 8.30202   35.17409 1.000 41.27393 ? 47  VAL A C   1 
ATOM   298  O O   . VAL A 1 53  ? -27.19610 8.55524   34.09815 1.000 41.18163 ? 47  VAL A O   1 
ATOM   299  C CB  . VAL A 1 53  ? -27.70004 5.93173   36.03295 1.000 42.16887 ? 47  VAL A CB  1 
ATOM   300  C CG1 . VAL A 1 53  ? -28.45134 4.61469   36.09974 1.000 51.89693 ? 47  VAL A CG1 1 
ATOM   301  C CG2 . VAL A 1 53  ? -26.39542 5.74603   35.27587 1.000 46.54027 ? 47  VAL A CG2 1 
ATOM   302  N N   . ARG A 1 54  ? -27.67299 9.11714   36.22152 1.000 46.65243 ? 48  ARG A N   1 
ATOM   303  C CA  . ARG A 1 54  ? -26.76351 10.25115  36.17886 1.000 41.19228 ? 48  ARG A CA  1 
ATOM   304  C C   . ARG A 1 54  ? -25.36617 9.80429   36.58856 1.000 37.93958 ? 48  ARG A C   1 
ATOM   305  O O   . ARG A 1 54  ? -25.19533 8.92278   37.43515 1.000 38.79628 ? 48  ARG A O   1 
ATOM   306  C CB  . ARG A 1 54  ? -27.24620 11.39608  37.07203 1.000 33.13256 ? 48  ARG A CB  1 
ATOM   307  C CG  . ARG A 1 54  ? -27.99850 12.48118  36.29974 1.000 54.61910 ? 48  ARG A CG  1 
ATOM   308  C CD  . ARG A 1 54  ? -28.44009 13.64463  37.18587 1.000 38.14335 ? 48  ARG A CD  1 
ATOM   309  N NE  . ARG A 1 54  ? -27.53238 14.78557  37.10160 1.000 42.78300 ? 48  ARG A NE  1 
ATOM   310  C CZ  . ARG A 1 54  ? -27.41299 15.58146  36.04564 1.000 44.69932 ? 48  ARG A CZ  1 
ATOM   311  N NH1 . ARG A 1 54  ? -28.14957 15.40884  34.95985 1.000 43.82521 ? 48  ARG A NH1 1 
ATOM   312  N NH2 . ARG A 1 54  ? -26.53263 16.57812  36.08011 1.000 43.38900 ? 48  ARG A NH2 1 
ATOM   313  N N   . VAL A 1 55  ? -24.35897 10.40784  35.95720 1.000 35.09666 ? 49  VAL A N   1 
ATOM   314  C CA  . VAL A 1 55  ? -22.97421 9.98400   36.10412 1.000 29.45953 ? 49  VAL A CA  1 
ATOM   315  C C   . VAL A 1 55  ? -22.09778 11.20673  36.33771 1.000 28.65207 ? 49  VAL A C   1 
ATOM   316  O O   . VAL A 1 55  ? -22.53100 12.35014  36.19818 1.000 31.54713 ? 49  VAL A O   1 
ATOM   317  C CB  . VAL A 1 55  ? -22.47339 9.19906   34.87407 1.000 36.10749 ? 49  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 55  ? -23.15038 7.83844   34.79437 1.000 35.89693 ? 49  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 55  ? -22.70597 10.00576  33.60240 1.000 27.88757 ? 49  VAL A CG2 1 
ATOM   320  N N   . ALA A 1 56  ? -20.84656 10.94218  36.70045 1.000 31.51339 ? 50  ALA A N   1 
ATOM   321  C CA  . ALA A 1 56  ? -19.82008 11.96689  36.81087 1.000 24.86832 ? 50  ALA A CA  1 
ATOM   322  C C   . ALA A 1 56  ? -18.86247 11.84763  35.63272 1.000 28.53367 ? 50  ALA A C   1 
ATOM   323  O O   . ALA A 1 56  ? -18.54624 10.73963  35.18883 1.000 31.41499 ? 50  ALA A O   1 
ATOM   324  C CB  . ALA A 1 56  ? -19.05257 11.83596  38.12954 1.000 24.21012 ? 50  ALA A CB  1 
ATOM   325  N N   . ILE A 1 57  ? -18.41314 12.99101  35.11749 1.000 26.29157 ? 51  ILE A N   1 
ATOM   326  C CA  . ILE A 1 57  ? -17.52183 13.02870  33.96188 1.000 30.70549 ? 51  ILE A CA  1 
ATOM   327  C C   . ILE A 1 57  ? -16.40029 14.02076  34.23208 1.000 27.59042 ? 51  ILE A C   1 
ATOM   328  O O   . ILE A 1 57  ? -16.65660 15.18315  34.56373 1.000 30.44164 ? 51  ILE A O   1 
ATOM   329  C CB  . ILE A 1 57  ? -18.26519 13.40151  32.66342 1.000 25.17611 ? 51  ILE A CB  1 
ATOM   330  C CG1 . ILE A 1 57  ? -19.42820 12.43920  32.41031 1.000 25.26296 ? 51  ILE A CG1 1 
ATOM   331  C CG2 . ILE A 1 57  ? -17.30705 13.40300  31.48367 1.000 24.73091 ? 51  ILE A CG2 1 
ATOM   332  C CD1 . ILE A 1 57  ? -20.19987 12.73130  31.14237 1.000 28.01693 ? 51  ILE A CD1 1 
ATOM   333  N N   . LYS A 1 58  ? -15.16088 13.56353  34.07847 1.000 23.42053 ? 52  LYS A N   1 
ATOM   334  C CA  . LYS A 1 58  ? -13.96943 14.38334  34.26532 1.000 29.95938 ? 52  LYS A CA  1 
ATOM   335  C C   . LYS A 1 58  ? -13.36119 14.68372  32.90213 1.000 25.59412 ? 52  LYS A C   1 
ATOM   336  O O   . LYS A 1 58  ? -13.01367 13.75937  32.15993 1.000 25.50971 ? 52  LYS A O   1 
ATOM   337  C CB  . LYS A 1 58  ? -12.95027 13.67084  35.15658 0.900 25.63221 ? 52  LYS A CB  1 
ATOM   338  C CG  . LYS A 1 58  ? -11.61640 14.39275  35.28905 0.700 23.01516 ? 52  LYS A CG  1 
ATOM   339  C CD  . LYS A 1 58  ? -10.75092 13.75982  36.36873 0.700 29.49112 ? 52  LYS A CD  1 
ATOM   340  C CE  . LYS A 1 58  ? -10.46406 12.29821  36.05668 0.600 27.85243 ? 52  LYS A CE  1 
ATOM   341  N NZ  . LYS A 1 58  ? -9.37383  11.74557  36.90785 0.600 26.65025 ? 52  LYS A NZ  1 
ATOM   342  N N   . LYS A 1 59  ? -13.23647 15.96732  32.57540 1.000 28.51850 ? 53  LYS A N   1 
ATOM   343  C CA  . LYS A 1 59  ? -12.57752 16.39254  31.34690 1.000 28.89016 ? 53  LYS A CA  1 
ATOM   344  C C   . LYS A 1 59  ? -11.07858 16.52059  31.58654 1.000 35.26261 ? 53  LYS A C   1 
ATOM   345  O O   . LYS A 1 59  ? -10.65237 17.09366  32.59342 1.000 36.09403 ? 53  LYS A O   1 
ATOM   346  C CB  . LYS A 1 59  ? -13.14906 17.72183  30.85408 1.000 37.42206 ? 53  LYS A CB  1 
ATOM   347  C CG  . LYS A 1 59  ? -12.25999 18.44010  29.85298 0.800 33.65817 ? 53  LYS A CG  1 
ATOM   348  C CD  . LYS A 1 59  ? -12.93144 19.67961  29.29392 0.700 36.37476 ? 53  LYS A CD  1 
ATOM   349  C CE  . LYS A 1 59  ? -12.59134 19.85960  27.82537 0.700 41.85416 ? 53  LYS A CE  1 
ATOM   350  N NZ  . LYS A 1 59  ? -12.05282 21.21520  27.53463 0.600 41.72315 ? 53  LYS A NZ  1 
ATOM   351  N N   . ILE A 1 60  ? -10.28416 15.98340  30.66318 1.000 31.43961 ? 54  ILE A N   1 
ATOM   352  C CA  . ILE A 1 60  ? -8.83023  15.97986  30.77177 1.000 29.00246 ? 54  ILE A CA  1 
ATOM   353  C C   . ILE A 1 60  ? -8.25016  16.59603  29.50638 1.000 36.45297 ? 54  ILE A C   1 
ATOM   354  O O   . ILE A 1 60  ? -8.64981  16.22958  28.39557 1.000 33.51636 ? 54  ILE A O   1 
ATOM   355  C CB  . ILE A 1 60  ? -8.27750  14.55648  30.97969 1.000 30.50443 ? 54  ILE A CB  1 
ATOM   356  C CG1 . ILE A 1 60  ? -9.09153  13.81174  32.04000 1.000 30.72293 ? 54  ILE A CG1 1 
ATOM   357  C CG2 . ILE A 1 60  ? -6.80979  14.60700  31.37277 1.000 35.31320 ? 54  ILE A CG2 1 
ATOM   358  C CD1 . ILE A 1 60  ? -8.51871  12.46384  32.41556 1.000 39.01639 ? 54  ILE A CD1 1 
ATOM   359  N N   . SER A 1 61  ? -7.30680  17.52545  29.67441 1.000 32.46451 ? 55  SER A N   1 
ATOM   360  C CA  . SER A 1 61  ? -6.63578  18.20328  28.56225 1.000 35.26246 ? 55  SER A CA  1 
ATOM   361  C C   . SER A 1 61  ? -5.13083  18.13326  28.79159 1.000 35.37368 ? 55  SER A C   1 
ATOM   362  O O   . SER A 1 61  ? -4.51180  19.11085  29.23233 1.000 39.07480 ? 55  SER A O   1 
ATOM   363  C CB  . SER A 1 61  ? -7.10688  19.65308  28.43617 1.000 34.06044 ? 55  SER A CB  1 
ATOM   364  O OG  . SER A 1 61  ? -8.51857  19.72714  28.35401 1.000 40.24030 ? 55  SER A OG  1 
ATOM   365  N N   . PRO A 1 62  ? -4.50366  16.99024  28.49267 1.000 38.09619 ? 56  PRO A N   1 
ATOM   366  C CA  . PRO A 1 62  ? -3.12368  16.77175  28.94568 1.000 34.90756 ? 56  PRO A CA  1 
ATOM   367  C C   . PRO A 1 62  ? -2.05179  16.83972  27.86517 1.000 40.13867 ? 56  PRO A C   1 
ATOM   368  O O   . PRO A 1 62  ? -0.85962  16.86455  28.18549 1.000 31.13971 ? 56  PRO A O   1 
ATOM   369  C CB  . PRO A 1 62  ? -3.20458  15.35790  29.52421 1.000 35.90073 ? 56  PRO A CB  1 
ATOM   370  C CG  . PRO A 1 62  ? -4.12815  14.66282  28.52946 1.000 36.50605 ? 56  PRO A CG  1 
ATOM   371  C CD  . PRO A 1 62  ? -5.13430  15.72353  28.07474 1.000 33.96025 ? 56  PRO A CD  1 
ATOM   372  N N   . PHE A 1 63  ? -2.44481  16.87319  26.59125 1.000 35.17049 ? 57  PHE A N   1 
ATOM   373  C CA  . PHE A 1 63  ? -1.52420  16.46879  25.53266 1.000 41.66983 ? 57  PHE A CA  1 
ATOM   374  C C   . PHE A 1 63  ? -0.42526  17.47978  25.23440 1.000 43.60364 ? 57  PHE A C   1 
ATOM   375  O O   . PHE A 1 63  ? 0.53068   17.12614  24.53596 1.000 38.60215 ? 57  PHE A O   1 
ATOM   376  C CB  . PHE A 1 63  ? -2.30630  16.15384  24.26026 1.000 35.45961 ? 57  PHE A CB  1 
ATOM   377  C CG  . PHE A 1 63  ? -3.34534  15.09583  24.45375 1.000 29.97436 ? 57  PHE A CG  1 
ATOM   378  C CD1 . PHE A 1 63  ? -2.96923  13.79479  24.74511 1.000 28.82861 ? 57  PHE A CD1 1 
ATOM   379  C CD2 . PHE A 1 63  ? -4.69258  15.39497  24.35357 1.000 37.02321 ? 57  PHE A CD2 1 
ATOM   380  C CE1 . PHE A 1 63  ? -3.91321  12.81113  24.93246 1.000 31.35007 ? 57  PHE A CE1 1 
ATOM   381  C CE2 . PHE A 1 63  ? -5.64545  14.41362  24.53835 1.000 34.71726 ? 57  PHE A CE2 1 
ATOM   382  C CZ  . PHE A 1 63  ? -5.25519  13.11936  24.82693 1.000 29.81573 ? 57  PHE A CZ  1 
ATOM   383  N N   . GLU A 1 64  ? -0.51253  18.70809  25.73801 1.000 37.36008 ? 58  GLU A N   1 
ATOM   384  C CA  . GLU A 1 64  ? 0.58215   19.63901  25.50352 1.000 50.22830 ? 58  GLU A CA  1 
ATOM   385  C C   . GLU A 1 64  ? 1.77134   19.40315  26.42428 1.000 45.95127 ? 58  GLU A C   1 
ATOM   386  O O   . GLU A 1 64  ? 2.82595   20.00991  26.20669 1.000 45.34399 ? 58  GLU A O   1 
ATOM   387  C CB  . GLU A 1 64  ? 0.10357   21.08626  25.64836 0.700 47.28671 ? 58  GLU A CB  1 
ATOM   388  C CG  . GLU A 1 64  ? -0.68952  21.59147  24.45587 0.600 41.08415 ? 58  GLU A CG  1 
ATOM   389  C CD  . GLU A 1 64  ? 0.19100   22.26336  23.42028 0.500 49.05168 ? 58  GLU A CD  1 
ATOM   390  O OE1 . GLU A 1 64  ? 0.83264   21.53796  22.63209 0.500 49.68659 ? 58  GLU A OE1 1 
ATOM   391  O OE2 . GLU A 1 64  ? 0.24418   23.51170  23.39367 0.500 51.03057 ? 58  GLU A OE2 1 
ATOM   392  N N   . HIS A 1 65  ? 1.64402   18.53082  27.42325 1.000 50.87852 ? 59  HIS A N   1 
ATOM   393  C CA  . HIS A 1 65  ? 2.69030   18.36571  28.42355 1.000 56.25900 ? 59  HIS A CA  1 
ATOM   394  C C   . HIS A 1 65  ? 2.93069   16.89886  28.74084 1.000 50.27861 ? 59  HIS A C   1 
ATOM   395  O O   . HIS A 1 65  ? 1.99068   16.14035  28.99858 1.000 43.52908 ? 59  HIS A O   1 
ATOM   396  C CB  . HIS A 1 65  ? 2.35077   19.14587  29.69564 0.900 47.08320 ? 59  HIS A CB  1 
ATOM   397  C CG  . HIS A 1 65  ? 2.38366   20.63026  29.50725 0.800 59.37211 ? 59  HIS A CG  1 
ATOM   398  N ND1 . HIS A 1 65  ? 1.52540   21.48726  30.15905 0.700 63.26330 ? 59  HIS A ND1 1 
ATOM   399  C CD2 . HIS A 1 65  ? 3.19434   21.41233  28.75607 0.700 52.30499 ? 59  HIS A CD2 1 
ATOM   400  C CE1 . HIS A 1 65  ? 1.79196   22.73128  29.80480 0.700 53.45647 ? 59  HIS A CE1 1 
ATOM   401  N NE2 . HIS A 1 65  ? 2.80179   22.71353  28.95432 0.700 56.88412 ? 59  HIS A NE2 1 
ATOM   402  N N   . GLN A 1 66  ? 4.21200   16.52696  28.72436 1.000 41.44553 ? 60  GLN A N   1 
ATOM   403  C CA  . GLN A 1 66  ? 4.63708   15.15633  28.98064 1.000 44.56658 ? 60  GLN A CA  1 
ATOM   404  C C   . GLN A 1 66  ? 4.16419   14.67603  30.34571 1.000 39.41086 ? 60  GLN A C   1 
ATOM   405  O O   . GLN A 1 66  ? 3.68869   13.54214  30.48854 1.000 36.71442 ? 60  GLN A O   1 
ATOM   406  C CB  . GLN A 1 66  ? 6.16352   15.09648  28.87352 1.000 51.58198 ? 60  GLN A CB  1 
ATOM   407  C CG  . GLN A 1 66  ? 6.87572   14.06314  29.72734 0.950 43.73390 ? 60  GLN A CG  1 
ATOM   408  C CD  . GLN A 1 66  ? 7.09136   12.76747  28.97502 0.900 54.74983 ? 60  GLN A CD  1 
ATOM   409  O OE1 . GLN A 1 66  ? 7.06721   12.74488  27.74737 0.800 50.32417 ? 60  GLN A OE1 1 
ATOM   410  N NE2 . GLN A 1 66  ? 7.33217   11.69089  29.70086 0.800 51.81484 ? 60  GLN A NE2 1 
ATOM   411  N N   . THR A 1 67  ? 4.27928   15.53607  31.36217 1.000 45.52348 ? 61  THR A N   1 
ATOM   412  C CA  . THR A 1 67  ? 3.88497   15.15001  32.71261 1.000 42.58491 ? 61  THR A CA  1 
ATOM   413  C C   . THR A 1 67  ? 2.38879   14.89602  32.79789 1.000 41.65864 ? 61  THR A C   1 
ATOM   414  O O   . THR A 1 67  ? 1.95467   13.93728  33.44792 1.000 35.44984 ? 61  THR A O   1 
ATOM   415  C CB  . THR A 1 67  ? 4.29099   16.22689  33.71616 0.700 40.66736 ? 61  THR A CB  1 
ATOM   416  O OG1 . THR A 1 67  ? 3.65835   17.46517  33.37094 0.700 48.37204 ? 61  THR A OG1 1 
ATOM   417  C CG2 . THR A 1 67  ? 5.79813   16.41623  33.70866 0.700 38.20669 ? 61  THR A CG2 1 
ATOM   418  N N   . TYR A 1 68  ? 1.57896   15.73977  32.15068 1.000 43.82895 ? 62  TYR A N   1 
ATOM   419  C CA  . TYR A 1 68  ? 0.13993   15.54243  32.25542 1.000 39.84695 ? 62  TYR A CA  1 
ATOM   420  C C   . TYR A 1 68  ? -0.26898  14.27904  31.51572 1.000 35.95062 ? 62  TYR A C   1 
ATOM   421  O O   . TYR A 1 68  ? -1.17451  13.55873  31.95115 1.000 35.43269 ? 62  TYR A O   1 
ATOM   422  C CB  . TYR A 1 68  ? -0.64335  16.73831  31.71116 0.900 37.20401 ? 62  TYR A CB  1 
ATOM   423  C CG  . TYR A 1 68  ? -0.29907  18.08191  32.31406 0.800 51.24570 ? 62  TYR A CG  1 
ATOM   424  C CD1 . TYR A 1 68  ? 0.12818   18.18799  33.63064 0.700 49.78163 ? 62  TYR A CD1 1 
ATOM   425  C CD2 . TYR A 1 68  ? -0.58571  19.25626  31.63238 0.700 50.34718 ? 62  TYR A CD2 1 
ATOM   426  C CE1 . TYR A 1 68  ? 0.39226   19.41990  34.20226 0.700 45.27900 ? 62  TYR A CE1 1 
ATOM   427  C CE2 . TYR A 1 68  ? -0.34273  20.49176  32.20450 0.700 49.41541 ? 62  TYR A CE2 1 
ATOM   428  C CZ  . TYR A 1 68  ? 0.15081   20.56747  33.48685 0.700 51.76120 ? 62  TYR A CZ  1 
ATOM   429  O OH  . TYR A 1 68  ? 0.39720   21.79937  34.05224 0.700 52.46448 ? 62  TYR A OH  1 
ATOM   430  N N   . CYS A 1 69  ? 0.40692   13.98750  30.39927 1.000 30.80745 ? 63  CYS A N   1 
ATOM   431  C CA  . CYS A 1 69  ? 0.14004   12.75747  29.65869 1.000 35.08565 ? 63  CYS A CA  1 
ATOM   432  C C   . CYS A 1 69  ? 0.48018   11.52617  30.49084 1.000 28.15882 ? 63  CYS A C   1 
ATOM   433  O O   . CYS A 1 69  ? -0.25644  10.53293  30.46993 1.000 33.20135 ? 63  CYS A O   1 
ATOM   434  C CB  . CYS A 1 69  ? 0.93368   12.75457  28.35452 1.000 39.57094 ? 63  CYS A CB  1 
ATOM   435  S SG  . CYS A 1 69  ? 0.39496   13.96008  27.13233 1.000 39.21054 ? 63  CYS A SG  1 
ATOM   436  N N   . GLN A 1 70  ? 1.60462   11.56458  31.21615 1.000 32.62442 ? 64  GLN A N   1 
ATOM   437  C CA  . GLN A 1 70  ? 1.94266   10.46451  32.11807 1.000 32.09878 ? 64  GLN A CA  1 
ATOM   438  C C   . GLN A 1 70  ? 0.85998   10.24698  33.16549 1.000 27.70153 ? 64  GLN A C   1 
ATOM   439  O O   . GLN A 1 70  ? 0.40586   9.11681   33.37850 1.000 34.52658 ? 64  GLN A O   1 
ATOM   440  C CB  . GLN A 1 70  ? 3.28338   10.71017  32.81206 0.800 33.39554 ? 64  GLN A CB  1 
ATOM   441  C CG  . GLN A 1 70  ? 4.51586   10.23742  32.07037 0.700 34.75022 ? 64  GLN A CG  1 
ATOM   442  C CD  . GLN A 1 70  ? 5.74638   11.03955  32.43339 0.600 44.88415 ? 64  GLN A CD  1 
ATOM   443  O OE1 . GLN A 1 70  ? 5.64899   12.11947  33.01407 0.600 40.77468 ? 64  GLN A OE1 1 
ATOM   444  N NE2 . GLN A 1 70  ? 6.91618   10.46542  32.18348 0.600 49.75477 ? 64  GLN A NE2 1 
ATOM   445  N N   . ARG A 1 71  ? 0.45485   11.31808  33.85100 1.000 30.45953 ? 65  ARG A N   1 
ATOM   446  C CA  . ARG A 1 71  ? -0.56009  11.19128  34.89127 1.000 32.20850 ? 65  ARG A CA  1 
ATOM   447  C C   . ARG A 1 71  ? -1.85247  10.61457  34.33035 1.000 33.58768 ? 65  ARG A C   1 
ATOM   448  O O   . ARG A 1 71  ? -2.49705  9.77379   34.96875 1.000 30.70707 ? 65  ARG A O   1 
ATOM   449  C CB  . ARG A 1 71  ? -0.81408  12.55243  35.53816 0.900 37.34503 ? 65  ARG A CB  1 
ATOM   450  C CG  . ARG A 1 71  ? -1.87407  12.53408  36.62202 0.800 42.66291 ? 65  ARG A CG  1 
ATOM   451  C CD  . ARG A 1 71  ? -1.77275  13.74704  37.52926 0.700 39.61957 ? 65  ARG A CD  1 
ATOM   452  N NE  . ARG A 1 71  ? -2.89184  13.81750  38.46038 0.700 37.74498 ? 65  ARG A NE  1 
ATOM   453  C CZ  . ARG A 1 71  ? -2.97020  14.66671  39.47576 0.600 36.00367 ? 65  ARG A CZ  1 
ATOM   454  N NH1 . ARG A 1 71  ? -2.01507  15.55060  39.71321 0.600 40.33383 ? 65  ARG A NH1 1 
ATOM   455  N NH2 . ARG A 1 71  ? -4.03403  14.62834  40.27350 0.600 33.73182 ? 65  ARG A NH2 1 
ATOM   456  N N   . THR A 1 72  ? -2.23843  11.04803  33.12958 1.000 28.91403 ? 66  THR A N   1 
ATOM   457  C CA  . THR A 1 72  ? -3.45871  10.54867  32.50767 1.000 28.63099 ? 66  THR A CA  1 
ATOM   458  C C   . THR A 1 72  ? -3.31344  9.08416   32.11081 1.000 26.46977 ? 66  THR A C   1 
ATOM   459  O O   . THR A 1 72  ? -4.21015  8.27102   32.36272 1.000 20.05628 ? 66  THR A O   1 
ATOM   460  C CB  . THR A 1 72  ? -3.80834  11.40482  31.28832 1.000 30.73034 ? 66  THR A CB  1 
ATOM   461  O OG1 . THR A 1 72  ? -3.97712  12.76941  31.69302 1.000 33.77766 ? 66  THR A OG1 1 
ATOM   462  C CG2 . THR A 1 72  ? -5.09232  10.91275  30.64385 1.000 27.27608 ? 66  THR A CG2 1 
ATOM   463  N N   . LEU A 1 73  ? -2.18146  8.72858   31.49766 1.000 25.44367 ? 67  LEU A N   1 
ATOM   464  C CA  . LEU A 1 73  ? -1.98313  7.35886   31.03181 1.000 28.31842 ? 67  LEU A CA  1 
ATOM   465  C C   . LEU A 1 73  ? -1.98994  6.36590   32.18829 1.000 19.53707 ? 67  LEU A C   1 
ATOM   466  O O   . LEU A 1 73  ? -2.66574  5.33270   32.12615 1.000 26.30867 ? 67  LEU A O   1 
ATOM   467  C CB  . LEU A 1 73  ? -0.67330  7.25067   30.25056 1.000 29.81028 ? 67  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 73  ? -0.43937  5.88608   29.59483 1.000 31.50386 ? 67  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 73  ? -1.66538  5.43597   28.80521 1.000 31.40464 ? 67  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 73  ? 0.80711   5.90019   28.71809 1.000 26.46301 ? 67  LEU A CD2 1 
ATOM   471  N N   . ARG A 1 74  ? -1.22648  6.65040   33.24787 1.000 23.80249 ? 68  ARG A N   1 
ATOM   472  C CA  . ARG A 1 74  ? -1.11370  5.68506   34.33767 1.000 25.66829 ? 68  ARG A CA  1 
ATOM   473  C C   . ARG A 1 74  ? -2.45723  5.46847   35.02738 1.000 20.10931 ? 68  ARG A C   1 
ATOM   474  O O   . ARG A 1 74  ? -2.79880  4.33601   35.38725 1.000 21.47975 ? 68  ARG A O   1 
ATOM   475  C CB  . ARG A 1 74  ? -0.04400  6.13160   35.33836 1.000 32.47685 ? 68  ARG A CB  1 
ATOM   476  C CG  . ARG A 1 74  ? -0.41469  7.34441   36.16795 1.000 42.29608 ? 68  ARG A CG  1 
ATOM   477  C CD  . ARG A 1 74  ? 0.67998   7.71808   37.14778 1.000 46.72707 ? 68  ARG A CD  1 
ATOM   478  N NE  . ARG A 1 74  ? 1.98511   7.85390   36.51377 1.000 47.75816 ? 68  ARG A NE  1 
ATOM   479  C CZ  . ARG A 1 74  ? 2.79430   8.88767   36.69814 1.000 46.87726 ? 68  ARG A CZ  1 
ATOM   480  N NH1 . ARG A 1 74  ? 2.44290   9.91247   37.45930 1.000 56.33769 ? 68  ARG A NH1 1 
ATOM   481  N NH2 . ARG A 1 74  ? 3.98278   8.89651   36.10116 1.000 51.21073 ? 68  ARG A NH2 1 
ATOM   482  N N   . GLU A 1 75  ? -3.24481  6.53459   35.20003 1.000 25.23499 ? 69  GLU A N   1 
ATOM   483  C CA  . GLU A 1 75  ? -4.57267  6.38061   35.78834 1.000 24.72617 ? 69  GLU A CA  1 
ATOM   484  C C   . GLU A 1 75  ? -5.44656  5.46687   34.93972 1.000 24.44921 ? 69  GLU A C   1 
ATOM   485  O O   . GLU A 1 75  ? -6.11374  4.56336   35.45956 1.000 21.64236 ? 69  GLU A O   1 
ATOM   486  C CB  . GLU A 1 75  ? -5.24739  7.74075   35.95531 0.800 22.96932 ? 69  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 75  ? -6.73567  7.61554   36.25126 0.700 21.20359 ? 69  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 75  ? -7.30773  8.81667   36.96635 0.700 32.99749 ? 69  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 75  ? -7.43514  9.88279   36.32663 0.700 33.66980 ? 69  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 75  ? -7.64253  8.68976   38.16218 0.700 24.65573 ? 69  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 76  ? -5.45902  5.69236   33.62510 1.000 23.97624 ? 70  ILE A N   1 
ATOM   492  C CA  . ILE A 1 76  ? -6.29686  4.88350   32.74352 1.000 17.43309 ? 70  ILE A CA  1 
ATOM   493  C C   . ILE A 1 76  ? -5.83227  3.43275   32.75647 1.000 24.51979 ? 70  ILE A C   1 
ATOM   494  O O   . ILE A 1 76  ? -6.63957  2.50597   32.88861 1.000 26.35760 ? 70  ILE A O   1 
ATOM   495  C CB  . ILE A 1 76  ? -6.29833  5.46649   31.31868 1.000 23.29133 ? 70  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 76  ? -6.97881  6.83662   31.30597 1.000 27.22965 ? 70  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 76  ? -6.98586  4.51544   30.35147 1.000 24.36704 ? 70  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 76  ? -6.76210  7.60965   30.02397 1.000 26.81626 ? 70  ILE A CD1 1 
ATOM   499  N N   . LYS A 1 77  ? -4.51957  3.21559   32.63081 1.000 22.81307 ? 71  LYS A N   1 
ATOM   500  C CA  . LYS A 1 77  ? -3.99086  1.85444   32.63506 1.000 19.83516 ? 71  LYS A CA  1 
ATOM   501  C C   . LYS A 1 77  ? -4.36191  1.11986   33.91824 1.000 21.96886 ? 71  LYS A C   1 
ATOM   502  O O   . LYS A 1 77  ? -4.78654  -0.04107  33.87782 1.000 27.59794 ? 71  LYS A O   1 
ATOM   503  C CB  . LYS A 1 77  ? -2.47223  1.87963   32.45019 0.900 20.88836 ? 71  LYS A CB  1 
ATOM   504  C CG  . LYS A 1 77  ? -2.01659  2.25907   31.04952 0.800 38.48713 ? 71  LYS A CG  1 
ATOM   505  C CD  . LYS A 1 77  ? -0.64913  1.66890   30.73412 0.700 36.08471 ? 71  LYS A CD  1 
ATOM   506  C CE  . LYS A 1 77  ? -0.72117  0.70910   29.55746 0.600 43.12862 ? 71  LYS A CE  1 
ATOM   507  N NZ  . LYS A 1 77  ? 0.48339   0.79758   28.68675 0.600 42.74516 ? 71  LYS A NZ  1 
ATOM   508  N N   . ILE A 1 78  ? -4.23032  1.78658   35.06576 1.000 24.13132 ? 72  ILE A N   1 
ATOM   509  C CA  . ILE A 1 78  ? -4.53798  1.14005   36.33792 1.000 22.01534 ? 72  ILE A CA  1 
ATOM   510  C C   . ILE A 1 78  ? -6.03124  0.85785   36.45793 1.000 27.74789 ? 72  ILE A C   1 
ATOM   511  O O   . ILE A 1 78  ? -6.44146  -0.26606  36.77262 1.000 23.39884 ? 72  ILE A O   1 
ATOM   512  C CB  . ILE A 1 78  ? -4.03280  1.99586   37.51223 1.000 25.09129 ? 72  ILE A CB  1 
ATOM   513  C CG1 . ILE A 1 78  ? -2.50292  2.01778   37.54362 1.000 28.03531 ? 72  ILE A CG1 1 
ATOM   514  C CG2 . ILE A 1 78  ? -4.60676  1.49345   38.81988 1.000 24.65494 ? 72  ILE A CG2 1 
ATOM   515  C CD1 . ILE A 1 78  ? -1.93571  3.16110   38.34165 1.000 23.70720 ? 72  ILE A CD1 1 
ATOM   516  N N   . LEU A 1 79  ? -6.86791  1.87182   36.21888 1.000 24.12989 ? 73  LEU A N   1 
ATOM   517  C CA  . LEU A 1 79  ? -8.29421  1.71476   36.49345 1.000 26.47332 ? 73  LEU A CA  1 
ATOM   518  C C   . LEU A 1 79  ? -8.96952  0.76911   35.50982 1.000 25.56215 ? 73  LEU A C   1 
ATOM   519  O O   . LEU A 1 79  ? -9.95896  0.11899   35.86495 1.000 30.91084 ? 73  LEU A O   1 
ATOM   520  C CB  . LEU A 1 79  ? -8.99089  3.07323   36.49117 1.000 25.83929 ? 73  LEU A CB  1 
ATOM   521  C CG  . LEU A 1 79  ? -8.74403  3.90670   37.74773 1.000 22.90080 ? 73  LEU A CG  1 
ATOM   522  C CD1 . LEU A 1 79  ? -9.36490  5.28903   37.61886 1.000 26.34780 ? 73  LEU A CD1 1 
ATOM   523  C CD2 . LEU A 1 79  ? -9.25368  3.18431   38.99568 1.000 28.60060 ? 73  LEU A CD2 1 
ATOM   524  N N   . LEU A 1 80  ? -8.46186  0.67265   34.27904 1.000 25.18754 ? 74  LEU A N   1 
ATOM   525  C CA  . LEU A 1 80  ? -9.02380  -0.28922  33.33885 1.000 35.86999 ? 74  LEU A CA  1 
ATOM   526  C C   . LEU A 1 80  ? -8.72950  -1.73060  33.73308 1.000 32.03078 ? 74  LEU A C   1 
ATOM   527  O O   . LEU A 1 80  ? -9.42267  -2.63765  33.26273 1.000 31.63812 ? 74  LEU A O   1 
ATOM   528  C CB  . LEU A 1 80  ? -8.51455  -0.02217  31.92166 1.000 38.25005 ? 74  LEU A CB  1 
ATOM   529  C CG  . LEU A 1 80  ? -9.06464  1.22296   31.22281 1.000 31.23661 ? 74  LEU A CG  1 
ATOM   530  C CD1 . LEU A 1 80  ? -8.74429  1.18460   29.74002 1.000 37.44782 ? 74  LEU A CD1 1 
ATOM   531  C CD2 . LEU A 1 80  ? -10.56522 1.33625   31.43932 1.000 30.01630 ? 74  LEU A CD2 1 
ATOM   532  N N   . ARG A 1 81  ? -7.72998  -1.97102  34.58001 1.000 27.84544 ? 75  ARG A N   1 
ATOM   533  C CA  . ARG A 1 81  ? -7.50132  -3.32193  35.07442 1.000 29.48224 ? 75  ARG A CA  1 
ATOM   534  C C   . ARG A 1 81  ? -8.11134  -3.56680  36.44749 1.000 29.94803 ? 75  ARG A C   1 
ATOM   535  O O   . ARG A 1 81  ? -8.50652  -4.69980  36.74227 1.000 33.38006 ? 75  ARG A O   1 
ATOM   536  C CB  . ARG A 1 81  ? -6.00056  -3.63956  35.11852 1.000 28.98823 ? 75  ARG A CB  1 
ATOM   537  C CG  . ARG A 1 81  ? -5.72155  -5.11282  35.39843 0.800 35.87447 ? 75  ARG A CG  1 
ATOM   538  C CD  . ARG A 1 81  ? -4.25784  -5.41542  35.67687 0.800 38.16660 ? 75  ARG A CD  1 
ATOM   539  N NE  . ARG A 1 81  ? -3.39584  -5.12877  34.53714 0.700 33.93312 ? 75  ARG A NE  1 
ATOM   540  C CZ  . ARG A 1 81  ? -2.10326  -5.42178  34.48796 0.700 33.77402 ? 75  ARG A CZ  1 
ATOM   541  N NH1 . ARG A 1 81  ? -1.49553  -6.03732  35.48910 0.700 37.58353 ? 75  ARG A NH1 1 
ATOM   542  N NH2 . ARG A 1 81  ? -1.40426  -5.09370  33.40528 0.700 37.90578 ? 75  ARG A NH2 1 
ATOM   543  N N   . PHE A 1 82  ? -8.21642  -2.53635  37.28331 1.000 31.82870 ? 76  PHE A N   1 
ATOM   544  C CA  . PHE A 1 82  ? -8.79137  -2.69986  38.61221 1.000 20.38835 ? 76  PHE A CA  1 
ATOM   545  C C   . PHE A 1 82  ? -10.30007 -2.90373  38.53570 1.000 24.11508 ? 76  PHE A C   1 
ATOM   546  O O   . PHE A 1 82  ? -10.98528 -2.28703  37.71638 1.000 20.33236 ? 76  PHE A O   1 
ATOM   547  C CB  . PHE A 1 82  ? -8.49417  -1.47538  39.47966 1.000 18.83512 ? 76  PHE A CB  1 
ATOM   548  C CG  . PHE A 1 82  ? -7.10338  -1.44348  40.05234 1.000 17.99759 ? 76  PHE A CG  1 
ATOM   549  C CD1 . PHE A 1 82  ? -6.13526  -2.34591  39.64000 1.000 21.04212 ? 76  PHE A CD1 1 
ATOM   550  C CD2 . PHE A 1 82  ? -6.77070  -0.50841  41.01971 1.000 22.02485 ? 76  PHE A CD2 1 
ATOM   551  C CE1 . PHE A 1 82  ? -4.85724  -2.30897  40.17647 1.000 23.95585 ? 76  PHE A CE1 1 
ATOM   552  C CE2 . PHE A 1 82  ? -5.49718  -0.46820  41.56377 1.000 24.66007 ? 76  PHE A CE2 1 
ATOM   553  C CZ  . PHE A 1 82  ? -4.53853  -1.36867  41.14016 1.000 21.89209 ? 76  PHE A CZ  1 
ATOM   554  N N   . ARG A 1 83  ? -10.81765 -3.77103  39.40648 1.000 21.83465 ? 77  ARG A N   1 
ATOM   555  C CA  . ARG A 1 83  ? -12.25602 -3.88458  39.64574 1.000 26.22535 ? 77  ARG A CA  1 
ATOM   556  C C   . ARG A 1 83  ? -12.46063 -4.18059  41.12450 1.000 20.90565 ? 77  ARG A C   1 
ATOM   557  O O   . ARG A 1 83  ? -12.11839 -5.27223  41.58939 1.000 23.85919 ? 77  ARG A O   1 
ATOM   558  C CB  A ARG A 1 83  ? -12.89556 -4.97220  38.78118 0.500 24.47148 ? 77  ARG A CB  1 
ATOM   559  C CB  B ARG A 1 83  ? -12.88552 -4.97598  38.77775 0.500 24.46634 ? 77  ARG A CB  1 
ATOM   560  C CG  A ARG A 1 83  ? -14.40753 -5.06292  38.95975 0.500 25.70447 ? 77  ARG A CG  1 
ATOM   561  C CG  B ARG A 1 83  ? -13.32627 -4.50649  37.39741 0.500 35.01019 ? 77  ARG A CG  1 
ATOM   562  C CD  A ARG A 1 83  ? -15.03924 -6.15421  38.10690 0.500 30.95062 ? 77  ARG A CD  1 
ATOM   563  C CD  B ARG A 1 83  ? -12.62987 -5.28944  36.29455 0.500 38.95498 ? 77  ARG A CD  1 
ATOM   564  N NE  A ARG A 1 83  ? -14.78746 -7.49164  38.63111 0.500 32.66240 ? 77  ARG A NE  1 
ATOM   565  N NE  B ARG A 1 83  ? -13.08955 -4.90247  34.96548 0.500 34.30160 ? 77  ARG A NE  1 
ATOM   566  C CZ  A ARG A 1 83  ? -13.93304 -8.35743  38.10344 0.500 34.08993 ? 77  ARG A CZ  1 
ATOM   567  C CZ  B ARG A 1 83  ? -12.62830 -3.86109  34.28641 0.500 33.20361 ? 77  ARG A CZ  1 
ATOM   568  N NH1 A ARG A 1 83  ? -13.22911 -8.06320  37.02267 0.500 35.86820 ? 77  ARG A NH1 1 
ATOM   569  N NH1 B ARG A 1 83  ? -11.69058 -3.07165  34.78388 0.500 28.52997 ? 77  ARG A NH1 1 
ATOM   570  N NH2 A ARG A 1 83  ? -13.78560 -9.55111  38.67109 0.500 46.38989 ? 77  ARG A NH2 1 
ATOM   571  N NH2 B ARG A 1 83  ? -13.11869 -3.60645  33.07677 0.500 38.42698 ? 77  ARG A NH2 1 
ATOM   572  N N   . HIS A 1 84  ? -13.01460 -3.21779  41.86064 1.000 18.41115 ? 78  HIS A N   1 
ATOM   573  C CA  . HIS A 1 84  ? -13.20712 -3.37424  43.29660 1.000 18.52071 ? 78  HIS A CA  1 
ATOM   574  C C   . HIS A 1 84  ? -14.31582 -2.44208  43.76180 1.000 18.05396 ? 78  HIS A C   1 
ATOM   575  O O   . HIS A 1 84  ? -14.44091 -1.32342  43.25904 1.000 19.48094 ? 78  HIS A O   1 
ATOM   576  C CB  . HIS A 1 84  ? -11.91285 -3.08470  44.06814 1.000 17.51946 ? 78  HIS A CB  1 
ATOM   577  C CG  . HIS A 1 84  ? -11.95121 -3.51944  45.50046 1.000 20.36261 ? 78  HIS A CG  1 
ATOM   578  N ND1 . HIS A 1 84  ? -12.46843 -2.72926  46.50463 1.000 19.23956 ? 78  HIS A ND1 1 
ATOM   579  C CD2 . HIS A 1 84  ? -11.53797 -4.66254  46.09742 1.000 19.45126 ? 78  HIS A CD2 1 
ATOM   580  C CE1 . HIS A 1 84  ? -12.36740 -3.36463  47.65849 1.000 20.40474 ? 78  HIS A CE1 1 
ATOM   581  N NE2 . HIS A 1 84  ? -11.80736 -4.54052  47.43931 1.000 18.65462 ? 78  HIS A NE2 1 
ATOM   582  N N   . GLU A 1 85  ? -15.09475 -2.90629  44.74482 1.000 19.53443 ? 79  GLU A N   1 
ATOM   583  C CA  . GLU A 1 85  ? -16.24971 -2.14787  45.22152 1.000 19.12888 ? 79  GLU A CA  1 
ATOM   584  C C   . GLU A 1 85  ? -15.85930 -0.78931  45.79122 1.000 22.58132 ? 79  GLU A C   1 
ATOM   585  O O   . GLU A 1 85  ? -16.63575 0.16825   45.69167 1.000 19.19002 ? 79  GLU A O   1 
ATOM   586  C CB  . GLU A 1 85  ? -17.00489 -2.95395  46.28059 0.900 19.94214 ? 79  GLU A CB  1 
ATOM   587  C CG  . GLU A 1 85  ? -17.75024 -4.16628  45.74182 0.800 30.60360 ? 79  GLU A CG  1 
ATOM   588  C CD  . GLU A 1 85  ? -18.44673 -4.95403  46.83636 0.700 29.40191 ? 79  GLU A CD  1 
ATOM   589  O OE1 . GLU A 1 85  ? -18.16540 -4.69560  48.02640 0.700 25.40350 ? 79  GLU A OE1 1 
ATOM   590  O OE2 . GLU A 1 85  ? -19.27550 -5.83038  46.50691 0.700 29.65773 ? 79  GLU A OE2 1 
ATOM   591  N N   . ASN A 1 86  ? -14.67910 -0.68487  46.40588 1.000 20.09690 ? 80  ASN A N   1 
ATOM   592  C CA  . ASN A 1 86  ? -14.24414 0.54052   47.06281 1.000 18.41836 ? 80  ASN A CA  1 
ATOM   593  C C   . ASN A 1 86  ? -13.23883 1.32305   46.22505 1.000 18.10293 ? 80  ASN A C   1 
ATOM   594  O O   . ASN A 1 86  ? -12.46255 2.11631   46.76898 1.000 18.09960 ? 80  ASN A O   1 
ATOM   595  C CB  . ASN A 1 86  ? -13.66612 0.21488   48.44048 1.000 18.61979 ? 80  ASN A CB  1 
ATOM   596  C CG  . ASN A 1 86  ? -14.64109 -0.56496  49.30394 1.000 22.90495 ? 80  ASN A CG  1 
ATOM   597  O OD1 . ASN A 1 86  ? -14.40182 -1.72547  49.63650 1.000 19.39208 ? 80  ASN A OD1 1 
ATOM   598  N ND2 . ASN A 1 86  ? -15.75426 0.06760   49.66092 1.000 19.87753 ? 80  ASN A ND2 1 
ATOM   599  N N   . ILE A 1 87  ? -13.23745 1.10493   44.91478 1.000 17.57756 ? 81  ILE A N   1 
ATOM   600  C CA  . ILE A 1 87  ? -12.43274 1.86048   43.96610 1.000 17.22718 ? 81  ILE A CA  1 
ATOM   601  C C   . ILE A 1 87  ? -13.36182 2.26390   42.83128 1.000 18.52046 ? 81  ILE A C   1 
ATOM   602  O O   . ILE A 1 87  ? -13.99841 1.39820   42.21820 1.000 18.22889 ? 81  ILE A O   1 
ATOM   603  C CB  . ILE A 1 87  ? -11.25312 1.03502   43.42702 1.000 16.83416 ? 81  ILE A CB  1 
ATOM   604  C CG1 . ILE A 1 87  ? -10.29713 0.64967   44.55843 1.000 16.90746 ? 81  ILE A CG1 1 
ATOM   605  C CG2 . ILE A 1 87  ? -10.50951 1.80871   42.34447 1.000 17.11996 ? 81  ILE A CG2 1 
ATOM   606  C CD1 . ILE A 1 87  ? -9.21155  -0.30198  44.11501 1.000 19.99308 ? 81  ILE A CD1 1 
ATOM   607  N N   . ILE A 1 88  ? -13.45539 3.56212   42.55438 1.000 19.02902 ? 82  ILE A N   1 
ATOM   608  C CA  . ILE A 1 88  ? -14.36018 4.01886   41.50397 1.000 19.39073 ? 82  ILE A CA  1 
ATOM   609  C C   . ILE A 1 88  ? -13.74434 3.67720   40.15176 1.000 20.14301 ? 82  ILE A C   1 
ATOM   610  O O   . ILE A 1 88  ? -12.59525 4.03134   39.86536 1.000 27.13873 ? 82  ILE A O   1 
ATOM   611  C CB  . ILE A 1 88  ? -14.67745 5.51885   41.63378 1.000 19.46359 ? 82  ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 88  ? -15.76668 5.91492   40.63196 1.000 30.24530 ? 82  ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 88  ? -13.44510 6.38855   41.45642 1.000 25.40571 ? 82  ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 88  ? -16.62431 7.08228   41.08622 1.000 28.50943 ? 82  ILE A CD1 1 
ATOM   615  N N   . GLY A 1 89  ? -14.49489 2.94258   39.33289 1.000 18.78384 ? 83  GLY A N   1 
ATOM   616  C CA  . GLY A 1 89  ? -14.00112 2.48984   38.05250 1.000 26.50769 ? 83  GLY A CA  1 
ATOM   617  C C   . GLY A 1 89  ? -14.33183 3.45725   36.93426 1.000 29.42758 ? 83  GLY A C   1 
ATOM   618  O O   . GLY A 1 89  ? -14.96208 4.49554   37.12794 1.000 30.13816 ? 83  GLY A O   1 
ATOM   619  N N   . ILE A 1 90  ? -13.88786 3.09607   35.73608 1.000 25.94937 ? 84  ILE A N   1 
ATOM   620  C CA  . ILE A 1 90  ? -14.15870 3.86938   34.53087 1.000 23.30710 ? 84  ILE A CA  1 
ATOM   621  C C   . ILE A 1 90  ? -15.30481 3.19983   33.78581 1.000 22.67954 ? 84  ILE A C   1 
ATOM   622  O O   . ILE A 1 90  ? -15.18154 2.05143   33.34309 1.000 28.46357 ? 84  ILE A O   1 
ATOM   623  C CB  . ILE A 1 90  ? -12.91060 3.98386   33.64231 1.000 26.47192 ? 84  ILE A CB  1 
ATOM   624  C CG1 . ILE A 1 90  ? -11.82731 4.80605   34.34453 1.000 20.97775 ? 84  ILE A CG1 1 
ATOM   625  C CG2 . ILE A 1 90  ? -13.27025 4.60665   32.30246 1.000 26.13292 ? 84  ILE A CG2 1 
ATOM   626  C CD1 . ILE A 1 90  ? -10.48285 4.75595   33.65434 1.000 24.51848 ? 84  ILE A CD1 1 
ATOM   627  N N   . ASN A 1 91  ? -16.42488 3.91505   33.65342 1.000 23.85832 ? 85  ASN A N   1 
ATOM   628  C CA  . ASN A 1 91  ? -17.57317 3.38505   32.92613 1.000 23.49874 ? 85  ASN A CA  1 
ATOM   629  C C   . ASN A 1 91  ? -17.41959 3.55141   31.42114 1.000 29.26310 ? 85  ASN A C   1 
ATOM   630  O O   . ASN A 1 91  ? -17.91781 2.72017   30.65354 1.000 24.96742 ? 85  ASN A O   1 
ATOM   631  C CB  . ASN A 1 91  ? -18.85628 4.08353   33.37911 0.800 21.15518 ? 85  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 91  ? -19.13549 3.89429   34.85352 0.700 28.64831 ? 85  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 91  ? -18.46517 3.11434   35.52759 0.700 24.17725 ? 85  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 91  ? -20.13092 4.61094   35.36414 0.700 27.16065 ? 85  ASN A ND2 1 
ATOM   635  N N   . ASP A 1 92  ? -16.73715 4.60745   30.98785 1.000 25.96505 ? 86  ASP A N   1 
ATOM   636  C CA  . ASP A 1 92  ? -16.70324 5.00259   29.58851 1.000 29.66998 ? 86  ASP A CA  1 
ATOM   637  C C   . ASP A 1 92  ? -15.62496 6.06176   29.42581 1.000 30.37492 ? 86  ASP A C   1 
ATOM   638  O O   . ASP A 1 92  ? -15.32806 6.80418   30.36527 1.000 24.67355 ? 86  ASP A O   1 
ATOM   639  C CB  . ASP A 1 92  ? -18.06920 5.54416   29.14411 1.000 24.30060 ? 86  ASP A CB  1 
ATOM   640  C CG  . ASP A 1 92  ? -18.14762 5.81007   27.65241 1.000 33.03015 ? 86  ASP A CG  1 
ATOM   641  O OD1 . ASP A 1 92  ? -17.26893 5.33878   26.90016 1.000 26.56624 ? 86  ASP A OD1 1 
ATOM   642  O OD2 . ASP A 1 92  ? -19.10395 6.49369   27.23265 1.000 26.50849 ? 86  ASP A OD2 1 
ATOM   643  N N   . ILE A 1 93  ? -15.03611 6.11782   28.23486 1.000 22.12988 ? 87  ILE A N   1 
ATOM   644  C CA  . ILE A 1 93  ? -14.06258 7.14735   27.89250 1.000 24.17255 ? 87  ILE A CA  1 
ATOM   645  C C   . ILE A 1 93  ? -14.46690 7.76378   26.56268 1.000 23.21317 ? 87  ILE A C   1 
ATOM   646  O O   . ILE A 1 93  ? -14.71259 7.04310   25.59008 1.000 24.44920 ? 87  ILE A O   1 
ATOM   647  C CB  . ILE A 1 93  ? -12.62640 6.59314   27.82089 1.000 26.26126 ? 87  ILE A CB  1 
ATOM   648  C CG1 . ILE A 1 93  ? -12.20885 6.01836   29.17458 1.000 21.72833 ? 87  ILE A CG1 1 
ATOM   649  C CG2 . ILE A 1 93  ? -11.66119 7.68242   27.39260 1.000 27.70016 ? 87  ILE A CG2 1 
ATOM   650  C CD1 . ILE A 1 93  ? -10.80581 5.44701   29.19729 1.000 24.52496 ? 87  ILE A CD1 1 
ATOM   651  N N   . ILE A 1 94  ? -14.52982 9.09246   26.52200 1.000 24.98284 ? 88  ILE A N   1 
ATOM   652  C CA  . ILE A 1 94  ? -14.96929 9.84034   25.35013 1.000 26.42158 ? 88  ILE A CA  1 
ATOM   653  C C   . ILE A 1 94  ? -13.78671 10.61891  24.79420 1.000 22.91858 ? 88  ILE A C   1 
ATOM   654  O O   . ILE A 1 94  ? -13.12904 11.36782  25.52688 1.000 27.21566 ? 88  ILE A O   1 
ATOM   655  C CB  . ILE A 1 94  ? -16.12969 10.79010  25.69264 1.000 24.39709 ? 88  ILE A CB  1 
ATOM   656  C CG1 . ILE A 1 94  ? -17.29355 10.01109  26.31068 1.000 24.62260 ? 88  ILE A CG1 1 
ATOM   657  C CG2 . ILE A 1 94  ? -16.57495 11.56166  24.45425 1.000 27.93170 ? 88  ILE A CG2 1 
ATOM   658  C CD1 . ILE A 1 94  ? -18.17682 10.84751  27.21292 1.000 29.69780 ? 88  ILE A CD1 1 
ATOM   659  N N   . ARG A 1 95  ? -13.52816 10.45185  23.49933 1.000 23.22633 ? 89  ARG A N   1 
ATOM   660  C CA  . ARG A 1 95  ? -12.50944 11.22579  22.80264 1.000 23.68869 ? 89  ARG A CA  1 
ATOM   661  C C   . ARG A 1 95  ? -12.76941 11.11912  21.30538 1.000 24.43470 ? 89  ARG A C   1 
ATOM   662  O O   . ARG A 1 95  ? -13.57386 10.30141  20.85068 1.000 24.74721 ? 89  ARG A O   1 
ATOM   663  C CB  . ARG A 1 95  ? -11.09465 10.75649  23.16753 1.000 26.60575 ? 89  ARG A CB  1 
ATOM   664  C CG  . ARG A 1 95  ? -10.86356 9.26122   23.03436 1.000 30.28009 ? 89  ARG A CG  1 
ATOM   665  C CD  . ARG A 1 95  ? -10.14382 8.94534   21.74131 1.000 27.81955 ? 89  ARG A CD  1 
ATOM   666  N NE  . ARG A 1 95  ? -9.62184  7.58589   21.69664 1.000 25.49834 ? 89  ARG A NE  1 
ATOM   667  C CZ  . ARG A 1 95  ? -9.77393  6.76400   20.66690 1.000 27.94770 ? 89  ARG A CZ  1 
ATOM   668  N NH1 . ARG A 1 95  ? -10.46795 7.11762   19.59718 1.000 23.50526 ? 89  ARG A NH1 1 
ATOM   669  N NH2 . ARG A 1 95  ? -9.21798  5.55682   20.71203 1.000 29.24936 ? 89  ARG A NH2 1 
ATOM   670  N N   . ALA A 1 96  ? -12.07667 11.96937  20.54288 1.000 25.50759 ? 90  ALA A N   1 
ATOM   671  C CA  . ALA A 1 96  ? -12.26703 12.03095  19.10231 1.000 27.87057 ? 90  ALA A CA  1 
ATOM   672  C C   . ALA A 1 96  ? -11.85359 10.71242  18.44753 1.000 25.55543 ? 90  ALA A C   1 
ATOM   673  O O   . ALA A 1 96  ? -11.09637 9.93183   19.02686 1.000 24.61109 ? 90  ALA A O   1 
ATOM   674  C CB  . ALA A 1 96  ? -11.46524 13.19333  18.51548 1.000 27.06683 ? 90  ALA A CB  1 
ATOM   675  N N   . PRO A 1 97  ? -12.35235 10.43482  17.23728 1.000 26.30736 ? 91  PRO A N   1 
ATOM   676  C CA  . PRO A 1 97  ? -12.02732 9.15103   16.59313 1.000 26.94548 ? 91  PRO A CA  1 
ATOM   677  C C   . PRO A 1 97  ? -10.59752 9.05149   16.08809 1.000 26.01876 ? 91  PRO A C   1 
ATOM   678  O O   . PRO A 1 97  ? -10.14231 7.93717   15.80381 1.000 29.95964 ? 91  PRO A O   1 
ATOM   679  C CB  . PRO A 1 97  ? -13.02435 9.07985   15.42769 1.000 27.12747 ? 91  PRO A CB  1 
ATOM   680  C CG  . PRO A 1 97  ? -13.36864 10.50612  15.14997 1.000 28.13322 ? 91  PRO A CG  1 
ATOM   681  C CD  . PRO A 1 97  ? -13.39775 11.16203  16.49734 1.000 27.55634 ? 91  PRO A CD  1 
ATOM   682  N N   . THR A 1 98  ? -9.88093  10.16312  15.94683 1.000 26.54467 ? 92  THR A N   1 
ATOM   683  C CA  . THR A 1 98  ? -8.53008  10.14804  15.40377 1.000 26.83629 ? 92  THR A CA  1 
ATOM   684  C C   . THR A 1 98  ? -7.58612  10.88902  16.33811 1.000 30.39940 ? 92  THR A C   1 
ATOM   685  O O   . THR A 1 98  ? -7.99974  11.75689  17.11145 1.000 26.61284 ? 92  THR A O   1 
ATOM   686  C CB  . THR A 1 98  ? -8.47058  10.78403  14.01208 1.000 28.19680 ? 92  THR A CB  1 
ATOM   687  O OG1 . THR A 1 98  ? -8.85681  12.16247  14.09660 1.000 28.96972 ? 92  THR A OG1 1 
ATOM   688  C CG2 . THR A 1 98  ? -9.40814  10.05767  13.06476 1.000 30.27634 ? 92  THR A CG2 1 
ATOM   689  N N   . ILE A 1 99  ? -6.30001  10.53430  16.25272 1.000 31.40784 ? 93  ILE A N   1 
ATOM   690  C CA  . ILE A 1 99  ? -5.29339  11.21336  17.06293 1.000 32.07806 ? 93  ILE A CA  1 
ATOM   691  C C   . ILE A 1 99  ? -5.19140  12.67629  16.65202 1.000 37.43777 ? 93  ILE A C   1 
ATOM   692  O O   . ILE A 1 99  ? -5.01158  13.56185  17.49975 1.000 32.36187 ? 93  ILE A O   1 
ATOM   693  C CB  A ILE A 1 99  ? -3.94106  10.47457  16.97693 0.350 34.40265 ? 93  ILE A CB  1 
ATOM   694  C CB  B ILE A 1 99  ? -3.93123  10.50361  16.93799 0.650 34.46001 ? 93  ILE A CB  1 
ATOM   695  C CG1 A ILE A 1 99  ? -3.11777  10.70661  18.24276 0.350 31.50967 ? 93  ILE A CG1 1 
ATOM   696  C CG1 B ILE A 1 99  ? -4.00612  9.08156   17.48843 0.650 38.48816 ? 93  ILE A CG1 1 
ATOM   697  C CG2 A ILE A 1 99  ? -3.14095  10.87337  15.74357 0.350 31.97763 ? 93  ILE A CG2 1 
ATOM   698  C CG2 B ILE A 1 99  ? -2.84922  11.28741  17.66368 0.650 29.59908 ? 93  ILE A CG2 1 
ATOM   699  C CD1 A ILE A 1 99  ? -1.97735  9.73466   18.38979 0.350 35.47343 ? 93  ILE A CD1 1 
ATOM   700  C CD1 B ILE A 1 99  ? -2.66426  8.38060   17.56400 0.650 36.17756 ? 93  ILE A CD1 1 
ATOM   701  N N   . GLU A 1 100 ? -5.34167  12.95587  15.34959 1.000 30.34002 ? 94  GLU A N   1 
ATOM   702  C CA  . GLU A 1 100 ? -5.29824  14.33222  14.86403 1.000 38.22926 ? 94  GLU A CA  1 
ATOM   703  C C   . GLU A 1 100 ? -6.32194  15.19187  15.58476 1.000 31.41304 ? 94  GLU A C   1 
ATOM   704  O O   . GLU A 1 100 ? -6.03571  16.32998  15.97166 1.000 32.65411 ? 94  GLU A O   1 
ATOM   705  C CB  . GLU A 1 100 ? -5.58090  14.38597  13.35602 1.000 31.43111 ? 94  GLU A CB  1 
ATOM   706  C CG  . GLU A 1 100 ? -4.43735  14.04172  12.40994 0.700 38.75522 ? 94  GLU A CG  1 
ATOM   707  C CD  . GLU A 1 100 ? -4.12133  12.55980  12.36476 0.700 34.54884 ? 94  GLU A CD  1 
ATOM   708  O OE1 . GLU A 1 100 ? -3.21378  12.17299  11.59748 0.700 37.98332 ? 94  GLU A OE1 1 
ATOM   709  O OE2 . GLU A 1 100 ? -4.78861  11.77962  13.07526 0.700 29.95348 ? 94  GLU A OE2 1 
ATOM   710  N N   . GLN A 1 101 ? -7.52392  14.65454  15.77537 1.000 35.17283 ? 95  GLN A N   1 
ATOM   711  C CA  . GLN A 1 101 ? -8.66818  15.41918  16.24232 1.000 30.00956 ? 95  GLN A CA  1 
ATOM   712  C C   . GLN A 1 101 ? -8.85640  15.37051  17.75007 1.000 29.02991 ? 95  GLN A C   1 
ATOM   713  O O   . GLN A 1 101 ? -9.69084  16.11797  18.27228 1.000 35.91489 ? 95  GLN A O   1 
ATOM   714  C CB  . GLN A 1 101 ? -9.94207  14.90281  15.56624 1.000 30.07641 ? 95  GLN A CB  1 
ATOM   715  C CG  . GLN A 1 101 ? -10.05137 15.24654  14.09162 1.000 31.42182 ? 95  GLN A CG  1 
ATOM   716  C CD  . GLN A 1 101 ? -11.22637 14.55618  13.42659 1.000 31.52148 ? 95  GLN A CD  1 
ATOM   717  O OE1 . GLN A 1 101 ? -12.11092 15.20686  12.86577 1.000 32.70940 ? 95  GLN A OE1 1 
ATOM   718  N NE2 . GLN A 1 101 ? -11.24494 13.23182  13.49136 1.000 30.45693 ? 95  GLN A NE2 1 
ATOM   719  N N   . MET A 1 102 ? -8.12693  14.51655  18.46602 1.000 28.58564 ? 96  MET A N   1 
ATOM   720  C CA  . MET A 1 102 ? -8.37409  14.34082  19.89304 1.000 32.30333 ? 96  MET A CA  1 
ATOM   721  C C   . MET A 1 102 ? -7.57354  15.39167  20.65288 1.000 36.68699 ? 96  MET A C   1 
ATOM   722  O O   . MET A 1 102 ? -6.33839  15.34749  20.69168 1.000 33.35989 ? 96  MET A O   1 
ATOM   723  C CB  . MET A 1 102 ? -8.05374  12.91772  20.35243 1.000 27.78222 ? 96  MET A CB  1 
ATOM   724  C CG  . MET A 1 102 ? -7.79061  12.77982  21.84941 1.000 28.40484 ? 96  MET A CG  1 
ATOM   725  S SD  . MET A 1 102 ? -7.17513  11.15644  22.36010 1.000 27.71828 ? 96  MET A SD  1 
ATOM   726  C CE  . MET A 1 102 ? -5.48315  11.21199  21.79115 1.000 24.40233 ? 96  MET A CE  1 
ATOM   727  N N   . LYS A 1 103 ? -8.29183  16.35915  21.21848 1.000 30.55646 ? 97  LYS A N   1 
ATOM   728  C CA  . LYS A 1 103 ? -7.74324  17.41156  22.05933 1.000 39.72216 ? 97  LYS A CA  1 
ATOM   729  C C   . LYS A 1 103 ? -8.03350  17.19860  23.53279 1.000 39.56056 ? 97  LYS A C   1 
ATOM   730  O O   . LYS A 1 103 ? -7.24010  17.61849  24.37720 1.000 39.20893 ? 97  LYS A O   1 
ATOM   731  C CB  . LYS A 1 103 ? -8.31987  18.76868  21.63756 0.800 41.91261 ? 97  LYS A CB  1 
ATOM   732  C CG  . LYS A 1 103 ? -7.35567  19.93261  21.67479 0.700 48.46460 ? 97  LYS A CG  1 
ATOM   733  C CD  . LYS A 1 103 ? -7.73900  20.96435  20.62467 0.600 48.40548 ? 97  LYS A CD  1 
ATOM   734  C CE  . LYS A 1 103 ? -9.19282  21.39260  20.78243 0.500 45.45564 ? 97  LYS A CE  1 
ATOM   735  N NZ  . LYS A 1 103 ? -9.37052  22.44475  21.82149 0.500 40.21607 ? 97  LYS A NZ  1 
ATOM   736  N N   . ASP A 1 104 ? -9.15058  16.55139  23.85082 1.000 33.62677 ? 98  ASP A N   1 
ATOM   737  C CA  . ASP A 1 104 ? -9.58430  16.32767  25.21897 1.000 42.54901 ? 98  ASP A CA  1 
ATOM   738  C C   . ASP A 1 104 ? -9.98935  14.87061  25.38145 1.000 34.69637 ? 98  ASP A C   1 
ATOM   739  O O   . ASP A 1 104 ? -10.28785 14.17388  24.40771 1.000 33.02537 ? 98  ASP A O   1 
ATOM   740  C CB  . ASP A 1 104 ? -10.76246 17.23963  25.59016 1.000 41.12310 ? 98  ASP A CB  1 
ATOM   741  C CG  . ASP A 1 104 ? -10.47044 18.70303  25.33433 1.000 43.80741 ? 98  ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 104 ? -9.40055  19.18060  25.76631 1.000 44.72083 ? 98  ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 104 ? -11.30839 19.37299  24.69437 1.000 44.22713 ? 98  ASP A OD2 1 
ATOM   744  N N   . VAL A 1 105 ? -9.99186  14.41588  26.63085 1.000 28.43475 ? 99  VAL A N   1 
ATOM   745  C CA  . VAL A 1 105 ? -10.44171 13.07763  26.99198 1.000 26.44427 ? 99  VAL A CA  1 
ATOM   746  C C   . VAL A 1 105 ? -11.40446 13.21086  28.16196 1.000 29.07565 ? 99  VAL A C   1 
ATOM   747  O O   . VAL A 1 105 ? -11.12157 13.93669  29.12228 1.000 29.25702 ? 99  VAL A O   1 
ATOM   748  C CB  . VAL A 1 105 ? -9.26466  12.15229  27.36079 1.000 38.02694 ? 99  VAL A CB  1 
ATOM   749  C CG1 . VAL A 1 105 ? -9.77150  10.77615  27.76364 1.000 36.70528 ? 99  VAL A CG1 1 
ATOM   750  C CG2 . VAL A 1 105 ? -8.28926  12.03935  26.20094 1.000 39.55530 ? 99  VAL A CG2 1 
ATOM   751  N N   . TYR A 1 106 ? -12.53575 12.51709  28.08532 1.000 26.57325 ? 100 TYR A N   1 
ATOM   752  C CA  . TYR A 1 106 ? -13.53524 12.53600  29.14550 1.000 30.53359 ? 100 TYR A CA  1 
ATOM   753  C C   . TYR A 1 106 ? -13.65473 11.15310  29.76931 1.000 28.07309 ? 100 TYR A C   1 
ATOM   754  O O   . TYR A 1 106 ? -13.83111 10.15859  29.05801 1.000 24.50470 ? 100 TYR A O   1 
ATOM   755  C CB  . TYR A 1 106 ? -14.89509 12.99697  28.61668 1.000 25.21823 ? 100 TYR A CB  1 
ATOM   756  C CG  . TYR A 1 106 ? -14.87592 14.37596  27.99839 1.000 31.95416 ? 100 TYR A CG  1 
ATOM   757  C CD1 . TYR A 1 106 ? -14.46984 14.56570  26.68283 1.000 32.82950 ? 100 TYR A CD1 1 
ATOM   758  C CD2 . TYR A 1 106 ? -15.24497 15.49290  28.73790 1.000 27.34929 ? 100 TYR A CD2 1 
ATOM   759  C CE1 . TYR A 1 106 ? -14.44902 15.82700  26.11513 1.000 39.32028 ? 100 TYR A CE1 1 
ATOM   760  C CE2 . TYR A 1 106 ? -15.22751 16.75719  28.17860 1.000 33.17313 ? 100 TYR A CE2 1 
ATOM   761  C CZ  . TYR A 1 106 ? -14.82770 16.91858  26.86821 1.000 41.36852 ? 100 TYR A CZ  1 
ATOM   762  O OH  . TYR A 1 106 ? -14.80875 18.17546  26.30904 1.000 40.93755 ? 100 TYR A OH  1 
ATOM   763  N N   . ILE A 1 107 ? -13.56235 11.09907  31.09539 1.000 21.59240 ? 101 ILE A N   1 
ATOM   764  C CA  . ILE A 1 107 ? -13.66152 9.86230   31.85993 1.000 26.91421 ? 101 ILE A CA  1 
ATOM   765  C C   . ILE A 1 107 ? -15.01561 9.85081   32.55154 1.000 24.25606 ? 101 ILE A C   1 
ATOM   766  O O   . ILE A 1 107 ? -15.31782 10.74673  33.34967 1.000 24.51925 ? 101 ILE A O   1 
ATOM   767  C CB  . ILE A 1 107 ? -12.52330 9.73623   32.88570 1.000 22.19245 ? 101 ILE A CB  1 
ATOM   768  C CG1 . ILE A 1 107 ? -11.16259 9.90217   32.20481 1.000 33.88320 ? 101 ILE A CG1 1 
ATOM   769  C CG2 . ILE A 1 107 ? -12.60996 8.40817   33.61422 1.000 21.36511 ? 101 ILE A CG2 1 
ATOM   770  C CD1 . ILE A 1 107 ? -10.90254 8.89753   31.10718 1.000 28.26640 ? 101 ILE A CD1 1 
ATOM   771  N N   . VAL A 1 108 ? -15.82560 8.83825   32.25236 1.000 27.84625 ? 102 VAL A N   1 
ATOM   772  C CA  . VAL A 1 108 ? -17.15409 8.68418   32.83470 1.000 22.39844 ? 102 VAL A CA  1 
ATOM   773  C C   . VAL A 1 108 ? -17.06670 7.69263   33.98351 1.000 21.51003 ? 102 VAL A C   1 
ATOM   774  O O   . VAL A 1 108 ? -16.54622 6.58223   33.81659 1.000 21.67169 ? 102 VAL A O   1 
ATOM   775  C CB  . VAL A 1 108 ? -18.17322 8.21455   31.78294 1.000 25.83461 ? 102 VAL A CB  1 
ATOM   776  C CG1 . VAL A 1 108 ? -19.56670 8.13786   32.39304 1.000 30.11022 ? 102 VAL A CG1 1 
ATOM   777  C CG2 . VAL A 1 108 ? -18.15857 9.14395   30.58099 1.000 28.37076 ? 102 VAL A CG2 1 
ATOM   778  N N   . GLN A 1 109 ? -17.57628 8.08893   35.14979 1.000 21.85676 ? 103 GLN A N   1 
ATOM   779  C CA  . GLN A 1 109 ? -17.52493 7.26288   36.34696 1.000 23.07485 ? 103 GLN A CA  1 
ATOM   780  C C   . GLN A 1 109 ? -18.85796 7.36294   37.07909 1.000 28.34836 ? 103 GLN A C   1 
ATOM   781  O O   . GLN A 1 109 ? -19.70916 8.19632   36.75437 1.000 26.20265 ? 103 GLN A O   1 
ATOM   782  C CB  . GLN A 1 109 ? -16.35771 7.68018   37.25435 1.000 22.54657 ? 103 GLN A CB  1 
ATOM   783  C CG  . GLN A 1 109 ? -15.00610 7.69178   36.53984 0.800 21.93571 ? 103 GLN A CG  1 
ATOM   784  C CD  . GLN A 1 109 ? -13.85645 8.11874   37.42948 0.700 24.63265 ? 103 GLN A CD  1 
ATOM   785  O OE1 . GLN A 1 109 ? -13.67924 9.30286   37.70800 0.700 18.85082 ? 103 GLN A OE1 1 
ATOM   786  N NE2 . GLN A 1 109 ? -13.05933 7.15208   37.87075 0.700 20.69123 ? 103 GLN A NE2 1 
ATOM   787  N N   . ASP A 1 110 ? -19.03937 6.48913   38.06994 1.000 28.77986 ? 104 ASP A N   1 
ATOM   788  C CA  . ASP A 1 110 ? -20.25746 6.50637   38.87161 1.000 29.45576 ? 104 ASP A CA  1 
ATOM   789  C C   . ASP A 1 110 ? -20.43443 7.86497   39.53904 1.000 36.20140 ? 104 ASP A C   1 
ATOM   790  O O   . ASP A 1 110 ? -19.46144 8.51176   39.93572 1.000 26.00102 ? 104 ASP A O   1 
ATOM   791  C CB  . ASP A 1 110 ? -20.21064 5.40988   39.93760 1.000 33.76437 ? 104 ASP A CB  1 
ATOM   792  C CG  . ASP A 1 110 ? -20.34526 4.01623   39.35579 1.000 37.95996 ? 104 ASP A CG  1 
ATOM   793  O OD1 . ASP A 1 110 ? -20.83474 3.88450   38.21452 0.780 32.18023 ? 104 ASP A OD1 1 
ATOM   794  O OD2 . ASP A 1 110 ? -19.95803 3.04887   40.04600 0.680 27.13248 ? 104 ASP A OD2 1 
ATOM   795  N N   . LEU A 1 111 ? -21.68400 8.30418   39.65744 1.000 21.57057 ? 105 LEU A N   1 
ATOM   796  C CA  . LEU A 1 111 ? -21.98732 9.55615   40.33835 1.000 29.92146 ? 105 LEU A CA  1 
ATOM   797  C C   . LEU A 1 111 ? -22.20275 9.27789   41.82172 1.000 32.09542 ? 105 LEU A C   1 
ATOM   798  O O   . LEU A 1 111 ? -23.11518 8.53264   42.19633 1.000 28.93528 ? 105 LEU A O   1 
ATOM   799  C CB  . LEU A 1 111 ? -23.21389 10.23490  39.73316 1.000 31.50305 ? 105 LEU A CB  1 
ATOM   800  C CG  . LEU A 1 111 ? -23.64923 11.51255  40.45442 1.000 32.20307 ? 105 LEU A CG  1 
ATOM   801  C CD1 . LEU A 1 111 ? -22.61479 12.61060  40.27203 1.000 25.05747 ? 105 LEU A CD1 1 
ATOM   802  C CD2 . LEU A 1 111 ? -25.01321 11.97816  39.96979 1.000 38.94795 ? 105 LEU A CD2 1 
ATOM   803  N N   . MET A 1 112 ? -21.35963 9.86787   42.65867 1.000 26.14982 ? 106 MET A N   1 
ATOM   804  C CA  . MET A 1 112 ? -21.46038 9.72769   44.10191 1.000 20.90435 ? 106 MET A CA  1 
ATOM   805  C C   . MET A 1 112 ? -22.10360 10.97967  44.69033 1.000 33.33866 ? 106 MET A C   1 
ATOM   806  O O   . MET A 1 112 ? -22.27316 11.99551  44.01275 1.000 39.11823 ? 106 MET A O   1 
ATOM   807  C CB  . MET A 1 112 ? -20.07389 9.47682   44.70067 1.000 19.91202 ? 106 MET A CB  1 
ATOM   808  C CG  . MET A 1 112 ? -19.36232 8.29012   44.06570 1.000 19.69871 ? 106 MET A CG  1 
ATOM   809  S SD  . MET A 1 112 ? -20.06112 6.69249   44.52452 1.000 23.44248 ? 106 MET A SD  1 
ATOM   810  C CE  . MET A 1 112 ? -19.35176 6.48176   46.16130 1.000 23.10204 ? 106 MET A CE  1 
ATOM   811  N N   . GLU A 1 113 ? -22.47441 10.89925  45.96987 1.000 24.52270 ? 107 GLU A N   1 
ATOM   812  C CA  . GLU A 1 113 ? -23.19448 12.01812  46.57098 1.000 22.35316 ? 107 GLU A CA  1 
ATOM   813  C C   . GLU A 1 113 ? -22.25600 13.11793  47.04950 1.000 27.80813 ? 107 GLU A C   1 
ATOM   814  O O   . GLU A 1 113 ? -22.55777 14.30468  46.87949 1.000 27.70717 ? 107 GLU A O   1 
ATOM   815  C CB  . GLU A 1 113 ? -24.07688 11.53960  47.72570 0.800 21.05176 ? 107 GLU A CB  1 
ATOM   816  C CG  . GLU A 1 113 ? -24.98961 12.64152  48.25084 0.700 30.80625 ? 107 GLU A CG  1 
ATOM   817  C CD  . GLU A 1 113 ? -25.76406 12.24313  49.48945 0.500 34.19279 ? 107 GLU A CD  1 
ATOM   818  O OE1 . GLU A 1 113 ? -26.75105 11.49474  49.35412 0.500 29.51809 ? 107 GLU A OE1 1 
ATOM   819  O OE2 . GLU A 1 113 ? -25.38383 12.67280  50.59864 0.500 33.91201 ? 107 GLU A OE2 1 
ATOM   820  N N   . THR A 1 114 ? -21.12371 12.75498  47.64458 1.000 21.15613 ? 108 THR A N   1 
ATOM   821  C CA  . THR A 1 114 ? -20.20967 13.74525  48.19475 1.000 19.40769 ? 108 THR A CA  1 
ATOM   822  C C   . THR A 1 114 ? -18.83193 13.10887  48.33254 1.000 19.30215 ? 108 THR A C   1 
ATOM   823  O O   . THR A 1 114 ? -18.62183 11.94293  47.98658 1.000 20.14066 ? 108 THR A O   1 
ATOM   824  C CB  . THR A 1 114 ? -20.72269 14.27880  49.53974 1.000 22.80465 ? 108 THR A CB  1 
ATOM   825  O OG1 . THR A 1 114 ? -19.89887 15.36492  49.97837 1.000 30.18395 ? 108 THR A OG1 1 
ATOM   826  C CG2 . THR A 1 114 ? -20.70381 13.18154  50.59323 1.000 18.50965 ? 108 THR A CG2 1 
ATOM   827  N N   . ASP A 1 115 ? -17.88678 13.89459  48.82960 1.000 21.49743 ? 109 ASP A N   1 
ATOM   828  C CA  . ASP A 1 115 ? -16.56124 13.40570  49.16588 1.000 22.63203 ? 109 ASP A CA  1 
ATOM   829  C C   . ASP A 1 115 ? -16.29648 13.67945  50.63992 1.000 22.46264 ? 109 ASP A C   1 
ATOM   830  O O   . ASP A 1 115 ? -16.99747 14.46911  51.27811 1.000 22.88676 ? 109 ASP A O   1 
ATOM   831  C CB  . ASP A 1 115 ? -15.48434 14.04391  48.27175 1.000 23.83923 ? 109 ASP A CB  1 
ATOM   832  C CG  . ASP A 1 115 ? -15.37396 15.54469  48.45960 1.000 29.03731 ? 109 ASP A CG  1 
ATOM   833  O OD1 . ASP A 1 115 ? -14.87728 15.98326  49.51497 1.000 23.42841 ? 109 ASP A OD1 1 
ATOM   834  O OD2 . ASP A 1 115 ? -15.78361 16.28880  47.54503 1.000 32.38974 ? 109 ASP A OD2 1 
ATOM   835  N N   . LEU A 1 116 ? -15.28328 13.00216  51.18553 1.000 20.80446 ? 110 LEU A N   1 
ATOM   836  C CA  . LEU A 1 116 ? -15.04571 13.09196  52.62272 1.000 19.11068 ? 110 LEU A CA  1 
ATOM   837  C C   . LEU A 1 116 ? -14.54357 14.47397  53.02669 1.000 21.00055 ? 110 LEU A C   1 
ATOM   838  O O   . LEU A 1 116 ? -14.80999 14.92105  54.14782 1.000 23.17487 ? 110 LEU A O   1 
ATOM   839  C CB  . LEU A 1 116 ? -14.06462 12.00664  53.06651 1.000 19.21462 ? 110 LEU A CB  1 
ATOM   840  C CG  . LEU A 1 116 ? -13.83517 11.87426  54.57351 1.000 21.48663 ? 110 LEU A CG  1 
ATOM   841  C CD1 . LEU A 1 116 ? -15.15598 11.63656  55.29808 1.000 19.68300 ? 110 LEU A CD1 1 
ATOM   842  C CD2 . LEU A 1 116 ? -12.84536 10.75809  54.87601 1.000 17.32879 ? 110 LEU A CD2 1 
ATOM   843  N N   . TYR A 1 117 ? -13.83112 15.16765  52.13533 1.000 22.34665 ? 111 TYR A N   1 
ATOM   844  C CA  . TYR A 1 117 ? -13.43245 16.54483  52.41522 1.000 22.50463 ? 111 TYR A CA  1 
ATOM   845  C C   . TYR A 1 117 ? -14.65134 17.42300  52.67505 1.000 22.64006 ? 111 TYR A C   1 
ATOM   846  O O   . TYR A 1 117 ? -14.74965 18.08035  53.71693 1.000 23.81794 ? 111 TYR A O   1 
ATOM   847  C CB  . TYR A 1 117 ? -12.60563 17.10430  51.25577 1.000 24.34976 ? 111 TYR A CB  1 
ATOM   848  C CG  . TYR A 1 117 ? -12.18184 18.54345  51.44824 1.000 21.69267 ? 111 TYR A CG  1 
ATOM   849  C CD1 . TYR A 1 117 ? -12.79585 19.56741  50.73693 1.000 33.78465 ? 111 TYR A CD1 1 
ATOM   850  C CD2 . TYR A 1 117 ? -11.16392 18.87789  52.33246 1.000 30.11774 ? 111 TYR A CD2 1 
ATOM   851  C CE1 . TYR A 1 117 ? -12.41455 20.88570  50.90816 1.000 28.98368 ? 111 TYR A CE1 1 
ATOM   852  C CE2 . TYR A 1 117 ? -10.77412 20.19178  52.50846 1.000 32.37418 ? 111 TYR A CE2 1 
ATOM   853  C CZ  . TYR A 1 117 ? -11.40185 21.19129  51.79410 1.000 34.54433 ? 111 TYR A CZ  1 
ATOM   854  O OH  . TYR A 1 117 ? -11.01806 22.50191  51.96569 0.490 36.97410 ? 111 TYR A OH  1 
ATOM   855  N N   . LYS A 1 118 ? -15.59551 17.44279  51.73006 1.000 19.55256 ? 112 LYS A N   1 
ATOM   856  C CA  . LYS A 1 118 ? -16.80493 18.24556  51.89862 1.000 24.45113 ? 112 LYS A CA  1 
ATOM   857  C C   . LYS A 1 118 ? -17.60848 17.79363  53.11142 1.000 24.41323 ? 112 LYS A C   1 
ATOM   858  O O   . LYS A 1 118 ? -18.13306 18.62392  53.86373 1.000 25.83962 ? 112 LYS A O   1 
ATOM   859  C CB  . LYS A 1 118 ? -17.66466 18.16940  50.63592 0.900 23.20930 ? 112 LYS A CB  1 
ATOM   860  C CG  . LYS A 1 118 ? -17.02862 18.78445  49.40357 0.600 26.75320 ? 112 LYS A CG  1 
ATOM   861  C CD  . LYS A 1 118 ? -16.68633 20.24561  49.63602 0.500 31.57465 ? 112 LYS A CD  1 
ATOM   862  C CE  . LYS A 1 118 ? -16.93315 21.06954  48.38263 0.500 34.88793 ? 112 LYS A CE  1 
ATOM   863  N NZ  . LYS A 1 118 ? -17.24442 22.48955  48.70360 0.500 34.70065 ? 112 LYS A NZ  1 
ATOM   864  N N   . LEU A 1 119 ? -17.72665 16.47944  53.30729 1.000 19.23879 ? 113 LEU A N   1 
ATOM   865  C CA  . LEU A 1 119 ? -18.45860 15.95288  54.45570 1.000 25.79754 ? 113 LEU A CA  1 
ATOM   866  C C   . LEU A 1 119 ? -17.87070 16.46104  55.76814 1.000 25.58933 ? 113 LEU A C   1 
ATOM   867  O O   . LEU A 1 119 ? -18.60160 16.91248  56.65713 1.000 32.20666 ? 113 LEU A O   1 
ATOM   868  C CB  . LEU A 1 119 ? -18.44367 14.42493  54.41372 1.000 25.53980 ? 113 LEU A CB  1 
ATOM   869  C CG  . LEU A 1 119 ? -19.60740 13.63225  55.00488 1.000 35.86964 ? 113 LEU A CG  1 
ATOM   870  C CD1 . LEU A 1 119 ? -20.92326 14.01611  54.35477 1.000 24.55586 ? 113 LEU A CD1 1 
ATOM   871  C CD2 . LEU A 1 119 ? -19.33546 12.14613  54.83401 1.000 33.78361 ? 113 LEU A CD2 1 
ATOM   872  N N   . LEU A 1 120 ? -16.54406 16.40131  55.90349 1.000 21.28459 ? 114 LEU A N   1 
ATOM   873  C CA  . LEU A 1 120 ? -15.89847 16.77160  57.15848 1.000 21.99830 ? 114 LEU A CA  1 
ATOM   874  C C   . LEU A 1 120 ? -16.02116 18.25838  57.47491 1.000 21.27103 ? 114 LEU A C   1 
ATOM   875  O O   . LEU A 1 120 ? -15.87558 18.64201  58.64095 1.000 25.99068 ? 114 LEU A O   1 
ATOM   876  C CB  . LEU A 1 120 ? -14.42595 16.36256  57.12007 1.000 18.61190 ? 114 LEU A CB  1 
ATOM   877  C CG  . LEU A 1 120 ? -14.16347 14.86331  57.27878 1.000 25.59444 ? 114 LEU A CG  1 
ATOM   878  C CD1 . LEU A 1 120 ? -12.67984 14.54855  57.16245 1.000 28.25290 ? 114 LEU A CD1 1 
ATOM   879  C CD2 . LEU A 1 120 ? -14.71703 14.36832  58.60662 1.000 30.07450 ? 114 LEU A CD2 1 
ATOM   880  N N   . LYS A 1 121 ? -16.28477 19.10410  56.47497 1.000 22.06832 ? 115 LYS A N   1 
ATOM   881  C CA  . LYS A 1 121 ? -16.42702 20.53122  56.74836 1.000 27.22667 ? 115 LYS A CA  1 
ATOM   882  C C   . LYS A 1 121 ? -17.66796 20.84487  57.57699 1.000 34.94243 ? 115 LYS A C   1 
ATOM   883  O O   . LYS A 1 121 ? -17.68567 21.85248  58.29249 1.000 31.93946 ? 115 LYS A O   1 
ATOM   884  C CB  . LYS A 1 121 ? -16.46016 21.33007  55.44269 0.800 27.16315 ? 115 LYS A CB  1 
ATOM   885  C CG  . LYS A 1 121 ? -15.32997 21.02923  54.47790 0.700 28.57401 ? 115 LYS A CG  1 
ATOM   886  C CD  . LYS A 1 121 ? -14.21103 22.05941  54.60435 0.600 33.31461 ? 115 LYS A CD  1 
ATOM   887  C CE  . LYS A 1 121 ? -13.15411 21.63454  55.61294 0.500 27.31801 ? 115 LYS A CE  1 
ATOM   888  N NZ  . LYS A 1 121 ? -11.88445 22.39596  55.45790 0.500 19.96894 ? 115 LYS A NZ  1 
ATOM   889  N N   . THR A 1 122 ? -18.71213 20.01489  57.50002 1.000 29.86956 ? 116 THR A N   1 
ATOM   890  C CA  . THR A 1 122 ? -19.97950 20.34699  58.14045 1.000 25.95185 ? 116 THR A CA  1 
ATOM   891  C C   . THR A 1 122 ? -20.59390 19.24381  58.99294 1.000 30.71984 ? 116 THR A C   1 
ATOM   892  O O   . THR A 1 122 ? -21.50754 19.54281  59.76999 1.000 37.67155 ? 116 THR A O   1 
ATOM   893  C CB  . THR A 1 122 ? -21.02183 20.76754  57.08999 0.800 34.34343 ? 116 THR A CB  1 
ATOM   894  O OG1 . THR A 1 122 ? -21.21063 19.70354  56.14796 0.800 32.36804 ? 116 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 122 ? -20.58140 22.03175  56.36080 0.800 36.94854 ? 116 THR A CG2 1 
ATOM   896  N N   . GLN A 1 123 ? -20.14415 17.99635  58.88353 1.000 26.90606 ? 117 GLN A N   1 
ATOM   897  C CA  . GLN A 1 123 ? -20.81258 16.87882  59.53798 1.000 30.52122 ? 117 GLN A CA  1 
ATOM   898  C C   . GLN A 1 123 ? -19.90070 16.21819  60.56154 1.000 27.62326 ? 117 GLN A C   1 
ATOM   899  O O   . GLN A 1 123 ? -18.77692 15.82068  60.23794 1.000 23.78212 ? 117 GLN A O   1 
ATOM   900  C CB  . GLN A 1 123 ? -21.28482 15.84323  58.51257 1.000 27.67075 ? 117 GLN A CB  1 
ATOM   901  C CG  . GLN A 1 123 ? -22.14401 16.42195  57.40377 1.000 22.89428 ? 117 GLN A CG  1 
ATOM   902  C CD  . GLN A 1 123 ? -23.45241 16.97802  57.92253 1.000 34.35105 ? 117 GLN A CD  1 
ATOM   903  O OE1 . GLN A 1 123 ? -24.02966 16.45062  58.87452 1.000 25.80331 ? 117 GLN A OE1 1 
ATOM   904  N NE2 . GLN A 1 123 ? -23.92753 18.05031  57.30216 1.000 32.38816 ? 117 GLN A NE2 1 
ATOM   905  N N   . HIS A 1 124 ? -20.39533 16.09901  61.79144 1.000 22.77168 ? 118 HIS A N   1 
ATOM   906  C CA  . HIS A 1 124 ? -19.75504 15.26476  62.79844 1.000 28.31993 ? 118 HIS A CA  1 
ATOM   907  C C   . HIS A 1 124 ? -20.06376 13.80088  62.51031 1.000 26.22810 ? 118 HIS A C   1 
ATOM   908  O O   . HIS A 1 124 ? -21.21780 13.43789  62.25973 1.000 27.50360 ? 118 HIS A O   1 
ATOM   909  C CB  . HIS A 1 124 ? -20.23664 15.66151  64.19634 1.000 31.44052 ? 118 HIS A CB  1 
ATOM   910  C CG  . HIS A 1 124 ? -19.97863 14.63016  65.25337 0.600 37.64311 ? 118 HIS A CG  1 
ATOM   911  N ND1 . HIS A 1 124 ? -20.75054 13.49617  65.39605 0.600 34.26173 ? 118 HIS A ND1 1 
ATOM   912  C CD2 . HIS A 1 124 ? -19.03300 14.56392  66.22080 0.600 36.27898 ? 118 HIS A CD2 1 
ATOM   913  C CE1 . HIS A 1 124 ? -20.29313 12.77768  66.40599 0.600 36.77758 ? 118 HIS A CE1 1 
ATOM   914  N NE2 . HIS A 1 124 ? -19.25033 13.40264  66.92254 0.600 43.07737 ? 118 HIS A NE2 1 
ATOM   915  N N   . LEU A 1 125 ? -19.03284 12.96221  62.53673 1.000 24.20273 ? 119 LEU A N   1 
ATOM   916  C CA  . LEU A 1 125 ? -19.19481 11.54273  62.25605 1.000 21.65260 ? 119 LEU A CA  1 
ATOM   917  C C   . LEU A 1 125 ? -19.44634 10.78411  63.55161 1.000 30.34936 ? 119 LEU A C   1 
ATOM   918  O O   . LEU A 1 125 ? -18.73970 10.98646  64.54465 1.000 28.27535 ? 119 LEU A O   1 
ATOM   919  C CB  . LEU A 1 125 ? -17.95976 10.97040  61.55512 1.000 19.95172 ? 119 LEU A CB  1 
ATOM   920  C CG  . LEU A 1 125 ? -17.79114 11.11648  60.03693 1.000 28.97448 ? 119 LEU A CG  1 
ATOM   921  C CD1 . LEU A 1 125 ? -18.00668 12.54739  59.55767 1.000 33.37737 ? 119 LEU A CD1 1 
ATOM   922  C CD2 . LEU A 1 125 ? -16.43250 10.59068  59.58919 1.000 23.57146 ? 119 LEU A CD2 1 
ATOM   923  N N   . SER A 1 126 ? -20.45888 9.92225   63.54145 1.000 29.08634 ? 120 SER A N   1 
ATOM   924  C CA  . SER A 1 126 ? -20.61618 8.96388   64.62151 1.000 28.93087 ? 120 SER A CA  1 
ATOM   925  C C   . SER A 1 126 ? -19.48161 7.94508   64.56948 1.000 21.17197 ? 120 SER A C   1 
ATOM   926  O O   . SER A 1 126 ? -18.84301 7.74440   63.53304 1.000 21.54135 ? 120 SER A O   1 
ATOM   927  C CB  . SER A 1 126 ? -21.96765 8.25680   64.52036 1.000 26.70548 ? 120 SER A CB  1 
ATOM   928  O OG  . SER A 1 126 ? -21.93691 7.24895   63.52194 1.000 21.52944 ? 120 SER A OG  1 
ATOM   929  N N   . ASN A 1 127 ? -19.21956 7.30631   65.71227 1.000 29.30364 ? 121 ASN A N   1 
ATOM   930  C CA  . ASN A 1 127 ? -18.17796 6.28432   65.74266 1.000 26.97902 ? 121 ASN A CA  1 
ATOM   931  C C   . ASN A 1 127 ? -18.48141 5.16179   64.75937 1.000 27.50224 ? 121 ASN A C   1 
ATOM   932  O O   . ASN A 1 127 ? -17.56552 4.58999   64.15744 1.000 23.27145 ? 121 ASN A O   1 
ATOM   933  C CB  . ASN A 1 127 ? -18.01369 5.72268   67.15316 1.000 26.94601 ? 121 ASN A CB  1 
ATOM   934  C CG  . ASN A 1 127 ? -16.91034 4.68312   67.23249 0.800 34.49708 ? 121 ASN A CG  1 
ATOM   935  O OD1 . ASN A 1 127 ? -15.80197 4.89960   66.73831 0.800 22.09305 ? 121 ASN A OD1 1 
ATOM   936  N ND2 . ASN A 1 127 ? -17.21292 3.54167   67.83863 0.800 29.74356 ? 121 ASN A ND2 1 
ATOM   937  N N   . ASP A 1 128 ? -19.76489 4.83748   64.57608 1.000 25.29190 ? 122 ASP A N   1 
ATOM   938  C CA  . ASP A 1 128 ? -20.13211 3.80570   63.61279 1.000 21.87517 ? 122 ASP A CA  1 
ATOM   939  C C   . ASP A 1 128 ? -19.76814 4.22197   62.19222 1.000 20.86030 ? 122 ASP A C   1 
ATOM   940  O O   . ASP A 1 128 ? -19.31929 3.39222   61.39146 1.000 22.43771 ? 122 ASP A O   1 
ATOM   941  C CB  . ASP A 1 128 ? -21.62535 3.49267   63.72056 1.000 26.16840 ? 122 ASP A CB  1 
ATOM   942  C CG  . ASP A 1 128 ? -21.95688 2.64666   64.93527 0.700 22.78637 ? 122 ASP A CG  1 
ATOM   943  O OD1 . ASP A 1 128 ? -21.10914 1.81926   65.33015 0.500 25.52271 ? 122 ASP A OD1 1 
ATOM   944  O OD2 . ASP A 1 128 ? -23.06340 2.80670   65.49218 0.500 25.07553 ? 122 ASP A OD2 1 
ATOM   945  N N   . HIS A 1 129 ? -19.95079 5.50394   61.85901 1.000 18.65547 ? 123 HIS A N   1 
ATOM   946  C CA  . HIS A 1 129 ? -19.56254 5.97670   60.53189 1.000 19.63545 ? 123 HIS A CA  1 
ATOM   947  C C   . HIS A 1 129 ? -18.04886 5.95776   60.36112 1.000 17.70142 ? 123 HIS A C   1 
ATOM   948  O O   . HIS A 1 129 ? -17.54309 5.53108   59.31748 1.000 15.43329 ? 123 HIS A O   1 
ATOM   949  C CB  . HIS A 1 129 ? -20.10833 7.38425   60.28179 1.000 18.41113 ? 123 HIS A CB  1 
ATOM   950  C CG  . HIS A 1 129 ? -21.55897 7.41451   59.91226 1.000 24.01760 ? 123 HIS A CG  1 
ATOM   951  N ND1 . HIS A 1 129 ? -22.56723 7.45026   60.85086 1.000 21.55153 ? 123 HIS A ND1 1 
ATOM   952  C CD2 . HIS A 1 129 ? -22.17021 7.40265   58.70360 1.000 24.55224 ? 123 HIS A CD2 1 
ATOM   953  C CE1 . HIS A 1 129 ? -23.73667 7.46768   60.23627 1.000 25.18293 ? 123 HIS A CE1 1 
ATOM   954  N NE2 . HIS A 1 129 ? -23.52369 7.43930   58.93294 1.000 22.24577 ? 123 HIS A NE2 1 
ATOM   955  N N   . ILE A 1 130 ? -17.31095 6.41498   61.37538 1.000 17.32042 ? 124 ILE A N   1 
ATOM   956  C CA  . ILE A 1 130 ? -15.85176 6.38486   61.30668 1.000 13.30684 ? 124 ILE A CA  1 
ATOM   957  C C   . ILE A 1 130 ? -15.35962 4.95884   61.09503 1.000 16.97720 ? 124 ILE A C   1 
ATOM   958  O O   . ILE A 1 130 ? -14.45451 4.70787   60.28955 1.000 18.67073 ? 124 ILE A O   1 
ATOM   959  C CB  . ILE A 1 130 ? -15.24908 7.00378   62.58130 1.000 13.55159 ? 124 ILE A CB  1 
ATOM   960  C CG1 . ILE A 1 130 ? -15.63033 8.47964   62.69643 1.000 14.86766 ? 124 ILE A CG1 1 
ATOM   961  C CG2 . ILE A 1 130 ? -13.73927 6.85274   62.58128 1.000 13.19690 ? 124 ILE A CG2 1 
ATOM   962  C CD1 . ILE A 1 130 ? -15.14234 9.13470   63.97264 1.000 20.48211 ? 124 ILE A CD1 1 
ATOM   963  N N   . CYS A 1 131 ? -15.95385 4.00314   61.81180 1.000 17.30702 ? 125 CYS A N   1 
ATOM   964  C CA  . CYS A 1 131 ? -15.53943 2.60961   61.69829 1.000 16.23771 ? 125 CYS A CA  1 
ATOM   965  C C   . CYS A 1 131 ? -15.82972 2.05398   60.30753 1.000 19.86971 ? 125 CYS A C   1 
ATOM   966  O O   . CYS A 1 131 ? -14.98397 1.37470   59.71380 1.000 17.01584 ? 125 CYS A O   1 
ATOM   967  C CB  . CYS A 1 131 ? -16.24303 1.78494   62.77724 1.000 19.28824 ? 125 CYS A CB  1 
ATOM   968  S SG  . CYS A 1 131 ? -15.73817 0.06299   62.89686 1.000 24.55865 ? 125 CYS A SG  1 
ATOM   969  N N   . TYR A 1 132 ? -17.01620 2.34032   59.76782 1.000 17.28647 ? 126 TYR A N   1 
ATOM   970  C CA  . TYR A 1 132 ? -17.37404 1.83100   58.44827 1.000 19.87994 ? 126 TYR A CA  1 
ATOM   971  C C   . TYR A 1 132 ? -16.55020 2.50249   57.35435 1.000 13.76772 ? 126 TYR A C   1 
ATOM   972  O O   . TYR A 1 132 ? -16.10608 1.83807   56.40976 1.000 11.59398 ? 126 TYR A O   1 
ATOM   973  C CB  . TYR A 1 132 ? -18.87476 2.02690   58.21801 1.000 22.77431 ? 126 TYR A CB  1 
ATOM   974  C CG  . TYR A 1 132 ? -19.40726 1.47695   56.91328 0.700 17.20124 ? 126 TYR A CG  1 
ATOM   975  C CD1 . TYR A 1 132 ? -19.03030 0.22043   56.45709 0.700 19.73790 ? 126 TYR A CD1 1 
ATOM   976  C CD2 . TYR A 1 132 ? -20.32047 2.20171   56.15748 0.700 15.59483 ? 126 TYR A CD2 1 
ATOM   977  C CE1 . TYR A 1 132 ? -19.52804 -0.28712  55.26706 0.700 22.79384 ? 126 TYR A CE1 1 
ATOM   978  C CE2 . TYR A 1 132 ? -20.82589 1.70154   54.96998 0.700 14.99223 ? 126 TYR A CE2 1 
ATOM   979  C CZ  . TYR A 1 132 ? -20.42570 0.45842   54.52916 0.700 17.35458 ? 126 TYR A CZ  1 
ATOM   980  O OH  . TYR A 1 132 ? -20.92520 -0.03978  53.34672 0.700 29.11180 ? 126 TYR A OH  1 
ATOM   981  N N   . PHE A 1 133 ? -16.32993 3.81653   57.46802 1.000 15.33747 ? 127 PHE A N   1 
ATOM   982  C CA  . PHE A 1 133 ? -15.50502 4.52188   56.49031 1.000 14.48125 ? 127 PHE A CA  1 
ATOM   983  C C   . PHE A 1 133 ? -14.08649 3.97163   56.47850 1.000 16.17213 ? 127 PHE A C   1 
ATOM   984  O O   . PHE A 1 133 ? -13.52703 3.68128   55.41400 1.000 14.63998 ? 127 PHE A O   1 
ATOM   985  C CB  . PHE A 1 133 ? -15.48123 6.02128   56.79379 1.000 17.91658 ? 127 PHE A CB  1 
ATOM   986  C CG  . PHE A 1 133 ? -16.77847 6.72831   56.51512 1.000 25.24314 ? 127 PHE A CG  1 
ATOM   987  C CD1 . PHE A 1 133 ? -17.81728 6.08789   55.85949 1.000 18.11532 ? 127 PHE A CD1 1 
ATOM   988  C CD2 . PHE A 1 133 ? -16.95020 8.04467   56.90571 1.000 23.62734 ? 127 PHE A CD2 1 
ATOM   989  C CE1 . PHE A 1 133 ? -19.00727 6.74991   55.60798 1.000 27.89511 ? 127 PHE A CE1 1 
ATOM   990  C CE2 . PHE A 1 133 ? -18.13264 8.70962   56.65723 1.000 20.98020 ? 127 PHE A CE2 1 
ATOM   991  C CZ  . PHE A 1 133 ? -19.16299 8.06209   56.00712 1.000 20.26563 ? 127 PHE A CZ  1 
ATOM   992  N N   . LEU A 1 134 ? -13.48433 3.83137   57.66322 1.000 18.06573 ? 128 LEU A N   1 
ATOM   993  C CA  . LEU A 1 134 ? -12.11856 3.32510   57.74968 1.000 13.40100 ? 128 LEU A CA  1 
ATOM   994  C C   . LEU A 1 134 ? -12.00889 1.91652   57.18115 1.000 14.84123 ? 128 LEU A C   1 
ATOM   995  O O   . LEU A 1 134 ? -11.05184 1.60175   56.46560 1.000 10.71041 ? 128 LEU A O   1 
ATOM   996  C CB  . LEU A 1 134 ? -11.64391 3.34704   59.20191 1.000 13.98565 ? 128 LEU A CB  1 
ATOM   997  C CG  . LEU A 1 134 ? -10.22605 2.81888   59.42190 1.000 12.52587 ? 128 LEU A CG  1 
ATOM   998  C CD1 . LEU A 1 134 ? -9.20905  3.68879   58.69813 1.000 19.92319 ? 128 LEU A CD1 1 
ATOM   999  C CD2 . LEU A 1 134 ? -9.90871  2.72346   60.91300 1.000 14.97347 ? 128 LEU A CD2 1 
ATOM   1000 N N   . TYR A 1 135 ? -12.97458 1.05083   57.49635 1.000 12.59954 ? 129 TYR A N   1 
ATOM   1001 C CA  . TYR A 1 135 ? -12.94193 -0.30575  56.96198 1.000 14.83005 ? 129 TYR A CA  1 
ATOM   1002 C C   . TYR A 1 135 ? -12.94717 -0.30386  55.43734 1.000 15.94603 ? 129 TYR A C   1 
ATOM   1003 O O   . TYR A 1 135 ? -12.21634 -1.07703  54.80646 1.000 13.65985 ? 129 TYR A O   1 
ATOM   1004 C CB  . TYR A 1 135 ? -14.12186 -1.11632  57.49507 1.000 16.14018 ? 129 TYR A CB  1 
ATOM   1005 C CG  . TYR A 1 135 ? -14.24079 -2.46733  56.82881 1.000 18.13579 ? 129 TYR A CG  1 
ATOM   1006 C CD1 . TYR A 1 135 ? -13.38290 -3.50224  57.16661 1.000 13.65292 ? 129 TYR A CD1 1 
ATOM   1007 C CD2 . TYR A 1 135 ? -15.18981 -2.69592  55.84040 1.000 17.14742 ? 129 TYR A CD2 1 
ATOM   1008 C CE1 . TYR A 1 135 ? -13.47391 -4.73493  56.55448 1.000 13.65717 ? 129 TYR A CE1 1 
ATOM   1009 C CE2 . TYR A 1 135 ? -15.28953 -3.92663  55.21805 1.000 20.98496 ? 129 TYR A CE2 1 
ATOM   1010 C CZ  . TYR A 1 135 ? -14.42755 -4.94146  55.57880 1.000 16.72011 ? 129 TYR A CZ  1 
ATOM   1011 O OH  . TYR A 1 135 ? -14.51546 -6.16834  54.96880 1.000 15.42286 ? 129 TYR A OH  1 
ATOM   1012 N N   . GLN A 1 136 ? -13.76071 0.56003   54.82424 1.000 16.13978 ? 130 GLN A N   1 
ATOM   1013 C CA  . GLN A 1 136 ? -13.85429 0.56148   53.36617 1.000 15.19741 ? 130 GLN A CA  1 
ATOM   1014 C C   . GLN A 1 136 ? -12.58288 1.10246   52.72442 1.000 13.60621 ? 130 GLN A C   1 
ATOM   1015 O O   . GLN A 1 136 ? -12.14963 0.59913   51.68071 1.000 14.47999 ? 130 GLN A O   1 
ATOM   1016 C CB  . GLN A 1 136 ? -15.06448 1.37450   52.91348 1.000 11.54960 ? 130 GLN A CB  1 
ATOM   1017 C CG  . GLN A 1 136 ? -16.39302 0.79509   53.34308 0.900 10.77834 ? 130 GLN A CG  1 
ATOM   1018 C CD  . GLN A 1 136 ? -17.55582 1.65243   52.89420 0.900 18.12211 ? 130 GLN A CD  1 
ATOM   1019 O OE1 . GLN A 1 136 ? -18.02860 1.53032   51.76428 0.800 15.23886 ? 130 GLN A OE1 1 
ATOM   1020 N NE2 . GLN A 1 136 ? -18.00952 2.54098   53.76883 0.800 13.22194 ? 130 GLN A NE2 1 
ATOM   1021 N N   . ILE A 1 137 ? -11.98542 2.13923   53.31873 1.000 11.07917 ? 131 ILE A N   1 
ATOM   1022 C CA  . ILE A 1 137 ? -10.70151 2.64372   52.83005 1.000 11.60539 ? 131 ILE A CA  1 
ATOM   1023 C C   . ILE A 1 137 ? -9.66579  1.52792   52.81622 1.000 15.03951 ? 131 ILE A C   1 
ATOM   1024 O O   . ILE A 1 137 ? -8.98238  1.30095   51.81013 1.000 14.15618 ? 131 ILE A O   1 
ATOM   1025 C CB  . ILE A 1 137 ? -10.22239 3.83126   53.68636 1.000 13.95095 ? 131 ILE A CB  1 
ATOM   1026 C CG1 . ILE A 1 137 ? -11.16911 5.02088   53.54494 1.000 13.62751 ? 131 ILE A CG1 1 
ATOM   1027 C CG2 . ILE A 1 137 ? -8.80711  4.23767   53.29344 1.000 13.05033 ? 131 ILE A CG2 1 
ATOM   1028 C CD1 . ILE A 1 137 ? -11.09163 5.99286   54.71306 1.000 11.86910 ? 131 ILE A CD1 1 
ATOM   1029 N N   . LEU A 1 138 ? -9.53402  0.81551   53.93849 1.000 11.07451 ? 132 LEU A N   1 
ATOM   1030 C CA  . LEU A 1 138 ? -8.53106  -0.24171  54.04052 1.000 15.40216 ? 132 LEU A CA  1 
ATOM   1031 C C   . LEU A 1 138 ? -8.86158  -1.41738  53.12976 1.000 14.51640 ? 132 LEU A C   1 
ATOM   1032 O O   . LEU A 1 138 ? -7.95698  -2.05200  52.57242 1.000 11.77414 ? 132 LEU A O   1 
ATOM   1033 C CB  . LEU A 1 138 ? -8.41004  -0.70736  55.49164 1.000 10.80289 ? 132 LEU A CB  1 
ATOM   1034 C CG  . LEU A 1 138 ? -7.86841  0.33197   56.47271 1.000 16.56834 ? 132 LEU A CG  1 
ATOM   1035 C CD1 . LEU A 1 138 ? -8.07597  -0.12772  57.90708 1.000 17.99234 ? 132 LEU A CD1 1 
ATOM   1036 C CD2 . LEU A 1 138 ? -6.38802  0.59517   56.20321 1.000 16.27655 ? 132 LEU A CD2 1 
ATOM   1037 N N   . ARG A 1 139 ? -10.14848 -1.73046  52.97606 1.000 14.45619 ? 133 ARG A N   1 
ATOM   1038 C CA  . ARG A 1 139 ? -10.54767 -2.79372  52.05923 1.000 14.06341 ? 133 ARG A CA  1 
ATOM   1039 C C   . ARG A 1 139 ? -10.15534 -2.44168  50.62880 1.000 11.09784 ? 133 ARG A C   1 
ATOM   1040 O O   . ARG A 1 139 ? -9.58810  -3.26774  49.90497 1.000 13.71332 ? 133 ARG A O   1 
ATOM   1041 C CB  . ARG A 1 139 ? -12.05441 -3.03904  52.18012 1.000 14.39330 ? 133 ARG A CB  1 
ATOM   1042 C CG  . ARG A 1 139 ? -12.59698 -4.22831  51.39470 1.000 12.25157 ? 133 ARG A CG  1 
ATOM   1043 C CD  . ARG A 1 139 ? -14.07528 -4.43203  51.71979 1.000 17.04397 ? 133 ARG A CD  1 
ATOM   1044 N NE  . ARG A 1 139 ? -14.66654 -5.56905  51.02370 1.000 16.31807 ? 133 ARG A NE  1 
ATOM   1045 C CZ  . ARG A 1 139 ? -15.45369 -5.47357  49.96021 1.000 24.57187 ? 133 ARG A CZ  1 
ATOM   1046 N NH1 . ARG A 1 139 ? -15.75215 -4.30265  49.42389 1.000 21.83684 ? 133 ARG A NH1 1 
ATOM   1047 N NH2 . ARG A 1 139 ? -15.95651 -6.58141  49.42297 1.000 19.54814 ? 133 ARG A NH2 1 
ATOM   1048 N N   . GLY A 1 140 ? -10.42973 -1.20472  50.21096 1.000 14.39358 ? 134 GLY A N   1 
ATOM   1049 C CA  . GLY A 1 140 ? -9.96129  -0.75973  48.90898 1.000 10.09469 ? 134 GLY A CA  1 
ATOM   1050 C C   . GLY A 1 140 ? -8.44684  -0.72787  48.82372 1.000 12.02298 ? 134 GLY A C   1 
ATOM   1051 O O   . GLY A 1 140 ? -7.86203  -1.12592  47.81404 1.000 14.34854 ? 134 GLY A O   1 
ATOM   1052 N N   . LEU A 1 141 ? -7.78932  -0.26756  49.88883 1.000 12.44562 ? 135 LEU A N   1 
ATOM   1053 C CA  . LEU A 1 141 ? -6.33095  -0.20231  49.87396 1.000 17.73750 ? 135 LEU A CA  1 
ATOM   1054 C C   . LEU A 1 141 ? -5.70586  -1.59119  49.79654 1.000 11.40107 ? 135 LEU A C   1 
ATOM   1055 O O   . LEU A 1 141 ? -4.65927  -1.76969  49.16216 1.000 14.45887 ? 135 LEU A O   1 
ATOM   1056 C CB  . LEU A 1 141 ? -5.82401  0.54362   51.10664 1.000 11.31040 ? 135 LEU A CB  1 
ATOM   1057 C CG  . LEU A 1 141 ? -4.34519  0.93363   51.07176 1.000 10.41678 ? 135 LEU A CG  1 
ATOM   1058 C CD1 . LEU A 1 141 ? -4.06345  1.86639   49.90304 1.000 13.99389 ? 135 LEU A CD1 1 
ATOM   1059 C CD2 . LEU A 1 141 ? -3.91466  1.56878   52.38876 1.000 16.26929 ? 135 LEU A CD2 1 
ATOM   1060 N N   . LYS A 1 142 ? -6.31836  -2.58549  50.44696 1.000 12.81462 ? 136 LYS A N   1 
ATOM   1061 C CA  . LYS A 1 142 ? -5.77082  -3.93975  50.40210 1.000 12.95733 ? 136 LYS A CA  1 
ATOM   1062 C C   . LYS A 1 142 ? -5.68955  -4.44171  48.96567 1.000 13.39154 ? 136 LYS A C   1 
ATOM   1063 O O   . LYS A 1 142 ? -4.67519  -5.01068  48.54399 1.000 13.54379 ? 136 LYS A O   1 
ATOM   1064 C CB  . LYS A 1 142 ? -6.61900  -4.88885  51.25452 1.000 10.32013 ? 136 LYS A CB  1 
ATOM   1065 C CG  . LYS A 1 142 ? -6.22151  -6.35344  51.10337 1.000 12.29296 ? 136 LYS A CG  1 
ATOM   1066 C CD  . LYS A 1 142 ? -7.14810  -7.30994  51.84671 1.000 13.12297 ? 136 LYS A CD  1 
ATOM   1067 C CE  . LYS A 1 142 ? -6.70034  -8.75683  51.64163 1.000 15.72500 ? 136 LYS A CE  1 
ATOM   1068 N NZ  . LYS A 1 142 ? -7.72366  -9.75981  52.06106 1.000 15.30020 ? 136 LYS A NZ  1 
ATOM   1069 N N   . TYR A 1 143 ? -6.75305  -4.22380  48.19549 1.000 12.56346 ? 137 TYR A N   1 
ATOM   1070 C CA  . TYR A 1 143 ? -6.74904  -4.60380  46.78726 1.000 11.06343 ? 137 TYR A CA  1 
ATOM   1071 C C   . TYR A 1 143 ? -5.65667  -3.86527  46.02176 1.000 16.14560 ? 137 TYR A C   1 
ATOM   1072 O O   . TYR A 1 143 ? -4.90975  -4.47003  45.24289 1.000 15.79924 ? 137 TYR A O   1 
ATOM   1073 C CB  . TYR A 1 143 ? -8.12623  -4.32153  46.18699 1.000 13.32263 ? 137 TYR A CB  1 
ATOM   1074 C CG  . TYR A 1 143 ? -8.26649  -4.66866  44.72525 1.000 16.72580 ? 137 TYR A CG  1 
ATOM   1075 C CD1 . TYR A 1 143 ? -8.64478  -5.94330  44.32863 1.000 20.84762 ? 137 TYR A CD1 1 
ATOM   1076 C CD2 . TYR A 1 143 ? -8.03374  -3.71804  43.74170 1.000 20.88282 ? 137 TYR A CD2 1 
ATOM   1077 C CE1 . TYR A 1 143 ? -8.78472  -6.26231  42.98959 1.000 14.14360 ? 137 TYR A CE1 1 
ATOM   1078 C CE2 . TYR A 1 143 ? -8.16883  -4.02843  42.39950 1.000 20.38707 ? 137 TYR A CE2 1 
ATOM   1079 C CZ  . TYR A 1 143 ? -8.54283  -5.30177  42.02956 1.000 17.59199 ? 137 TYR A CZ  1 
ATOM   1080 O OH  . TYR A 1 143 ? -8.67980  -5.61515  40.69475 1.000 22.50319 ? 137 TYR A OH  1 
ATOM   1081 N N   . ILE A 1 144 ? -5.54930  -2.55125  46.23522 1.000 15.92690 ? 138 ILE A N   1 
ATOM   1082 C CA  . ILE A 1 144 ? -4.54863  -1.75255  45.52861 1.000 15.70171 ? 138 ILE A CA  1 
ATOM   1083 C C   . ILE A 1 144 ? -3.15130  -2.28446  45.81239 1.000 15.79470 ? 138 ILE A C   1 
ATOM   1084 O O   . ILE A 1 144 ? -2.37079  -2.56563  44.89425 1.000 17.35135 ? 138 ILE A O   1 
ATOM   1085 C CB  . ILE A 1 144 ? -4.66565  -0.27092  45.92844 1.000 10.39627 ? 138 ILE A CB  1 
ATOM   1086 C CG1 . ILE A 1 144 ? -6.00344  0.30968   45.47822 1.000 14.61169 ? 138 ILE A CG1 1 
ATOM   1087 C CG2 . ILE A 1 144 ? -3.52264  0.53406   45.31931 1.000 13.23728 ? 138 ILE A CG2 1 
ATOM   1088 C CD1 . ILE A 1 144 ? -6.32247  1.64199   46.12412 1.000 14.17263 ? 138 ILE A CD1 1 
ATOM   1089 N N   . HIS A 1 145 ? -2.81938  -2.43279  47.09598 1.000 12.15929 ? 139 HIS A N   1 
ATOM   1090 C CA  . HIS A 1 145 ? -1.49261  -2.90005  47.47604 1.000 14.20198 ? 139 HIS A CA  1 
ATOM   1091 C C   . HIS A 1 145 ? -1.24607  -4.32980  47.01474 1.000 15.08353 ? 139 HIS A C   1 
ATOM   1092 O O   . HIS A 1 145 ? -0.10425  -4.69777  46.71434 1.000 16.63994 ? 139 HIS A O   1 
ATOM   1093 C CB  . HIS A 1 145 ? -1.32476  -2.77823  48.99163 1.000 14.40504 ? 139 HIS A CB  1 
ATOM   1094 C CG  . HIS A 1 145 ? -1.08626  -1.37588  49.45594 1.000 14.09334 ? 139 HIS A CG  1 
ATOM   1095 N ND1 . HIS A 1 145 ? -0.83936  -1.05827  50.77413 1.000 13.95240 ? 139 HIS A ND1 1 
ATOM   1096 C CD2 . HIS A 1 145 ? -1.04776  -0.20646  48.77307 1.000 15.89955 ? 139 HIS A CD2 1 
ATOM   1097 C CE1 . HIS A 1 145 ? -0.65970  0.24636   50.88362 1.000 18.94852 ? 139 HIS A CE1 1 
ATOM   1098 N NE2 . HIS A 1 145 ? -0.78160  0.78660   49.68390 1.000 15.01365 ? 139 HIS A NE2 1 
ATOM   1099 N N   . SER A 1 146 ? -2.29904  -5.14583  46.93747 1.000 14.56476 ? 140 SER A N   1 
ATOM   1100 C CA  . SER A 1 146 ? -2.14502  -6.49794  46.41982 1.000 16.02663 ? 140 SER A CA  1 
ATOM   1101 C C   . SER A 1 146 ? -1.78037  -6.50395  44.94182 1.000 18.23921 ? 140 SER A C   1 
ATOM   1102 O O   . SER A 1 146 ? -1.26986  -7.51283  44.44411 1.000 16.23901 ? 140 SER A O   1 
ATOM   1103 C CB  . SER A 1 146 ? -3.42633  -7.29757  46.64631 1.000 20.48528 ? 140 SER A CB  1 
ATOM   1104 O OG  . SER A 1 146 ? -4.45461  -6.87792  45.76066 1.000 17.61363 ? 140 SER A OG  1 
ATOM   1105 N N   . ALA A 1 147 ? -2.02812  -5.40476  44.23466 1.000 20.83672 ? 141 ALA A N   1 
ATOM   1106 C CA  . ALA A 1 147 ? -1.64335  -5.26654  42.83911 1.000 21.59147 ? 141 ALA A CA  1 
ATOM   1107 C C   . ALA A 1 147 ? -0.24937  -4.68202  42.67738 1.000 22.28397 ? 141 ALA A C   1 
ATOM   1108 O O   . ALA A 1 147 ? 0.14102   -4.34845  41.55331 1.000 22.48128 ? 141 ALA A O   1 
ATOM   1109 C CB  . ALA A 1 147 ? -2.66072  -4.39760  42.09308 1.000 17.78630 ? 141 ALA A CB  1 
ATOM   1110 N N   . ASN A 1 148 ? 0.50361   -4.55885  43.77380 1.000 19.04176 ? 142 ASN A N   1 
ATOM   1111 C CA  . ASN A 1 148 ? 1.83101   -3.94358  43.77725 1.000 17.40396 ? 142 ASN A CA  1 
ATOM   1112 C C   . ASN A 1 148 ? 1.76494   -2.47385  43.37240 1.000 20.41205 ? 142 ASN A C   1 
ATOM   1113 O O   . ASN A 1 148 ? 2.71387   -1.93078  42.80363 1.000 20.43557 ? 142 ASN A O   1 
ATOM   1114 C CB  . ASN A 1 148 ? 2.80953   -4.70950  42.87889 1.000 21.72473 ? 142 ASN A CB  1 
ATOM   1115 C CG  . ASN A 1 148 ? 4.25433   -4.55384  43.32026 0.800 27.06340 ? 142 ASN A CG  1 
ATOM   1116 O OD1 . ASN A 1 148 ? 4.54651   -4.48410  44.51424 0.800 23.10669 ? 142 ASN A OD1 1 
ATOM   1117 N ND2 . ASN A 1 148 ? 5.16581   -4.49701  42.35499 0.800 31.71561 ? 142 ASN A ND2 1 
ATOM   1118 N N   . VAL A 1 149 ? 0.64864   -1.81614  43.67762 1.000 14.26803 ? 143 VAL A N   1 
ATOM   1119 C CA  . VAL A 1 149 ? 0.42125   -0.42026  43.32226 1.000 19.86509 ? 143 VAL A CA  1 
ATOM   1120 C C   . VAL A 1 149 ? 0.31784   0.41202   44.59406 1.000 16.13075 ? 143 VAL A C   1 
ATOM   1121 O O   . VAL A 1 149 ? -0.22823  -0.04146  45.60677 1.000 14.87115 ? 143 VAL A O   1 
ATOM   1122 C CB  . VAL A 1 149 ? -0.84699  -0.26943  42.45778 1.000 15.85325 ? 143 VAL A CB  1 
ATOM   1123 C CG1 . VAL A 1 149 ? -1.19396  1.19926   42.24809 1.000 17.90105 ? 143 VAL A CG1 1 
ATOM   1124 C CG2 . VAL A 1 149 ? -0.65506  -0.97038  41.12505 1.000 16.58100 ? 143 VAL A CG2 1 
ATOM   1125 N N   . LEU A 1 150 ? 0.85063   1.62902   44.53803 1.000 17.04128 ? 144 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 150 ? 0.70902   2.61961   45.59450 1.000 12.95612 ? 144 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 150 ? -0.17449  3.74984   45.09079 1.000 14.75312 ? 144 LEU A C   1 
ATOM   1128 O O   . LEU A 1 150 ? 0.03314   4.24302   43.97976 1.000 17.42901 ? 144 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 150 ? 2.07127   3.17892   45.98825 1.000 14.59527 ? 144 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 150 ? 3.18888   2.15882   46.14305 1.000 23.74758 ? 144 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 150 ? 4.45482   2.89717   46.44727 1.000 19.55046 ? 144 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 150 ? 2.86371   1.17539   47.24193 1.000 22.67414 ? 144 LEU A CD2 1 
ATOM   1133 N N   . HIS A 1 151 ? -1.14421  4.17113   45.90660 1.000 13.01179 ? 145 HIS A N   1 
ATOM   1134 C CA  . HIS A 1 151 ? -2.00501  5.28000   45.50227 1.000 14.98093 ? 145 HIS A CA  1 
ATOM   1135 C C   . HIS A 1 151 ? -1.24700  6.60269   45.54882 1.000 15.59535 ? 145 HIS A C   1 
ATOM   1136 O O   . HIS A 1 151 ? -1.24309  7.36532   44.57346 1.000 15.30651 ? 145 HIS A O   1 
ATOM   1137 C CB  . HIS A 1 151 ? -3.24976  5.33471   46.39069 1.000 11.15951 ? 145 HIS A CB  1 
ATOM   1138 C CG  . HIS A 1 151 ? -4.23752  6.38053   45.97617 1.000 18.74699 ? 145 HIS A CG  1 
ATOM   1139 N ND1 . HIS A 1 151 ? -4.09454  7.71149   46.30554 1.000 14.84468 ? 145 HIS A ND1 1 
ATOM   1140 C CD2 . HIS A 1 151 ? -5.38617  6.29049   45.26181 1.000 15.79817 ? 145 HIS A CD2 1 
ATOM   1141 C CE1 . HIS A 1 151 ? -5.10699  8.39751   45.80625 1.000 17.28846 ? 145 HIS A CE1 1 
ATOM   1142 N NE2 . HIS A 1 151 ? -5.90749  7.55845   45.17187 1.000 15.64140 ? 145 HIS A NE2 1 
ATOM   1143 N N   . ARG A 1 152 ? -0.62216  6.89766   46.68909 1.000 12.77049 ? 146 ARG A N   1 
ATOM   1144 C CA  . ARG A 1 152 ? 0.31426   7.99973   46.90930 1.000 13.04840 ? 146 ARG A CA  1 
ATOM   1145 C C   . ARG A 1 152 ? -0.33509  9.37688   46.95065 1.000 19.43928 ? 146 ARG A C   1 
ATOM   1146 O O   . ARG A 1 152 ? 0.38236   10.37773  46.91421 1.000 17.15281 ? 146 ARG A O   1 
ATOM   1147 C CB  . ARG A 1 152 ? 1.44137   8.00819   45.86679 0.900 16.00260 ? 146 ARG A CB  1 
ATOM   1148 C CG  . ARG A 1 152 ? 2.20997   6.69985   45.79546 0.800 21.41684 ? 146 ARG A CG  1 
ATOM   1149 C CD  . ARG A 1 152 ? 3.22329   6.67165   44.65902 0.800 26.03277 ? 146 ARG A CD  1 
ATOM   1150 N NE  . ARG A 1 152 ? 4.42412   7.44983   44.93743 0.700 26.35474 ? 146 ARG A NE  1 
ATOM   1151 C CZ  . ARG A 1 152 ? 4.81462   8.50630   44.23738 0.600 29.12760 ? 146 ARG A CZ  1 
ATOM   1152 N NH1 . ARG A 1 152 ? 4.10197   8.96532   43.22217 0.600 30.39222 ? 146 ARG A NH1 1 
ATOM   1153 N NH2 . ARG A 1 152 ? 5.95166   9.11523   44.56140 0.600 22.80510 ? 146 ARG A NH2 1 
ATOM   1154 N N   . ASP A 1 153 ? -1.65923  9.47081   47.03109 1.000 14.82700 ? 147 ASP A N   1 
ATOM   1155 C CA  . ASP A 1 153 ? -2.29150  10.76544  47.27448 1.000 14.84344 ? 147 ASP A CA  1 
ATOM   1156 C C   . ASP A 1 153 ? -3.63635  10.55637  47.96080 1.000 16.12674 ? 147 ASP A C   1 
ATOM   1157 O O   . ASP A 1 153 ? -4.64773  11.15714  47.59831 1.000 16.22375 ? 147 ASP A O   1 
ATOM   1158 C CB  . ASP A 1 153 ? -2.44024  11.56961  45.98285 1.000 17.68816 ? 147 ASP A CB  1 
ATOM   1159 C CG  . ASP A 1 153 ? -2.63237  13.05357  46.24261 1.000 20.57138 ? 147 ASP A CG  1 
ATOM   1160 O OD1 . ASP A 1 153 ? -2.27540  13.51639  47.34847 1.000 18.98470 ? 147 ASP A OD1 1 
ATOM   1161 O OD2 . ASP A 1 153 ? -3.13453  13.75806  45.34195 1.000 21.16808 ? 147 ASP A OD2 1 
ATOM   1162 N N   . LEU A 1 154 ? -3.65905  9.69045   48.96683 1.000 13.98294 ? 148 LEU A N   1 
ATOM   1163 C CA  . LEU A 1 154 ? -4.88010  9.47675   49.72894 1.000 11.41323 ? 148 LEU A CA  1 
ATOM   1164 C C   . LEU A 1 154 ? -5.15120  10.66624  50.64022 1.000 18.88459 ? 148 LEU A C   1 
ATOM   1165 O O   . LEU A 1 154 ? -4.27295  11.11278  51.38599 1.000 14.04738 ? 148 LEU A O   1 
ATOM   1166 C CB  . LEU A 1 154 ? -4.79058  8.18704   50.54056 1.000 11.82888 ? 148 LEU A CB  1 
ATOM   1167 C CG  . LEU A 1 154 ? -4.69271  6.91191   49.70020 1.000 11.26356 ? 148 LEU A CG  1 
ATOM   1168 C CD1 . LEU A 1 154 ? -4.29220  5.72126   50.55964 1.000 10.06194 ? 148 LEU A CD1 1 
ATOM   1169 C CD2 . LEU A 1 154 ? -6.02587  6.64736   48.98385 1.000 12.31074 ? 148 LEU A CD2 1 
ATOM   1170 N N   . LYS A 1 155 ? -6.37162  11.17800  50.56637 1.000 11.91563 ? 149 LYS A N   1 
ATOM   1171 C CA  . LYS A 1 155 ? -6.81427  12.33250  51.33361 1.000 13.16434 ? 149 LYS A CA  1 
ATOM   1172 C C   . LYS A 1 155 ? -8.33924  12.37990  51.26452 1.000 17.62034 ? 149 LYS A C   1 
ATOM   1173 O O   . LYS A 1 155 ? -8.93579  11.71509  50.41185 1.000 15.88243 ? 149 LYS A O   1 
ATOM   1174 C CB  . LYS A 1 155 ? -6.19791  13.63421  50.79475 1.000 10.62954 ? 149 LYS A CB  1 
ATOM   1175 C CG  . LYS A 1 155 ? -6.35157  13.83434  49.30199 1.000 19.87441 ? 149 LYS A CG  1 
ATOM   1176 C CD  . LYS A 1 155 ? -5.61483  15.07729  48.84244 1.000 14.98219 ? 149 LYS A CD  1 
ATOM   1177 C CE  . LYS A 1 155 ? -5.76740  15.28806  47.34782 1.000 21.25389 ? 149 LYS A CE  1 
ATOM   1178 N NZ  . LYS A 1 155 ? -5.12081  16.55248  46.90121 1.000 22.78457 ? 149 LYS A NZ  1 
ATOM   1179 N N   . PRO A 1 156 ? -8.98827  13.13307  52.16307 1.000 15.47110 ? 150 PRO A N   1 
ATOM   1180 C CA  . PRO A 1 156 ? -10.46234 13.11753  52.18051 1.000 13.58674 ? 150 PRO A CA  1 
ATOM   1181 C C   . PRO A 1 156 ? -11.10130 13.47887  50.84988 1.000 16.49773 ? 150 PRO A C   1 
ATOM   1182 O O   . PRO A 1 156 ? -12.13644 12.90107  50.49699 1.000 18.38195 ? 150 PRO A O   1 
ATOM   1183 C CB  . PRO A 1 156 ? -10.79729 14.13775  53.27482 1.000 11.50943 ? 150 PRO A CB  1 
ATOM   1184 C CG  . PRO A 1 156 ? -9.64810  14.01664  54.22954 1.000 12.28023 ? 150 PRO A CG  1 
ATOM   1185 C CD  . PRO A 1 156 ? -8.43939  13.83141  53.34333 1.000 15.40526 ? 150 PRO A CD  1 
ATOM   1186 N N   . SER A 1 157 ? -10.51460 14.40941  50.09106 1.000 14.53628 ? 151 SER A N   1 
ATOM   1187 C CA  . SER A 1 157 ? -11.12244 14.80452  48.82445 1.000 20.26626 ? 151 SER A CA  1 
ATOM   1188 C C   . SER A 1 157 ? -11.05757 13.70106  47.77684 1.000 21.53484 ? 151 SER A C   1 
ATOM   1189 O O   . SER A 1 157 ? -11.78328 13.76996  46.77867 1.000 19.21770 ? 151 SER A O   1 
ATOM   1190 C CB  . SER A 1 157 ? -10.45925 16.07055  48.27912 1.000 17.76782 ? 151 SER A CB  1 
ATOM   1191 O OG  . SER A 1 157 ? -9.14052  15.80195  47.84377 1.000 24.75579 ? 151 SER A OG  1 
ATOM   1192 N N   . ASN A 1 158 ? -10.21472 12.69141  47.97543 1.000 16.37866 ? 152 ASN A N   1 
ATOM   1193 C CA  . ASN A 1 158 ? -10.13703 11.55981  47.06624 1.000 17.00953 ? 152 ASN A CA  1 
ATOM   1194 C C   . ASN A 1 158 ? -10.95959 10.37021  47.54429 1.000 22.23523 ? 152 ASN A C   1 
ATOM   1195 O O   . ASN A 1 158 ? -10.80751 9.26380   47.01394 1.000 15.26157 ? 152 ASN A O   1 
ATOM   1196 C CB  . ASN A 1 158 ? -8.67814  11.15114  46.84749 1.000 16.66940 ? 152 ASN A CB  1 
ATOM   1197 C CG  . ASN A 1 158 ? -7.99568  12.00691  45.79898 0.800 19.97577 ? 152 ASN A CG  1 
ATOM   1198 O OD1 . ASN A 1 158 ? -8.65949  12.60345  44.95296 0.800 14.67151 ? 152 ASN A OD1 1 
ATOM   1199 N ND2 . ASN A 1 158 ? -6.66865  12.07315  45.84765 0.800 14.26014 ? 152 ASN A ND2 1 
ATOM   1200 N N   . LEU A 1 159 ? -11.83762 10.57835  48.51987 1.000 16.53759 ? 153 LEU A N   1 
ATOM   1201 C CA  . LEU A 1 159 ? -12.69309 9.53192   49.06565 1.000 12.00231 ? 153 LEU A CA  1 
ATOM   1202 C C   . LEU A 1 159 ? -14.13790 9.94680   48.82389 1.000 14.19267 ? 153 LEU A C   1 
ATOM   1203 O O   . LEU A 1 159 ? -14.61764 10.91327  49.42524 1.000 15.99014 ? 153 LEU A O   1 
ATOM   1204 C CB  . LEU A 1 159 ? -12.41423 9.32571   50.55347 1.000 15.36876 ? 153 LEU A CB  1 
ATOM   1205 C CG  . LEU A 1 159 ? -10.96551 8.96958   50.89554 1.000 11.59044 ? 153 LEU A CG  1 
ATOM   1206 C CD1 . LEU A 1 159 ? -10.78398 8.84327   52.40205 1.000 9.63842  ? 153 LEU A CD1 1 
ATOM   1207 C CD2 . LEU A 1 159 ? -10.55180 7.68194   50.18042 1.000 9.70465  ? 153 LEU A CD2 1 
ATOM   1208 N N   . LEU A 1 160 ? -14.82094 9.22905   47.93942 1.000 12.24796 ? 154 LEU A N   1 
ATOM   1209 C CA  . LEU A 1 160 ? -16.18780 9.54673   47.55376 1.000 14.93304 ? 154 LEU A CA  1 
ATOM   1210 C C   . LEU A 1 160 ? -17.17517 8.68684   48.33014 1.000 12.75620 ? 154 LEU A C   1 
ATOM   1211 O O   . LEU A 1 160 ? -16.90064 7.52596   48.64123 1.000 16.52043 ? 154 LEU A O   1 
ATOM   1212 C CB  . LEU A 1 160 ? -16.38832 9.33342   46.05243 1.000 13.60783 ? 154 LEU A CB  1 
ATOM   1213 C CG  . LEU A 1 160 ? -15.38071 10.02102  45.12725 1.000 16.11979 ? 154 LEU A CG  1 
ATOM   1214 C CD1 . LEU A 1 160 ? -15.77758 9.84130   43.67057 1.000 21.31883 ? 154 LEU A CD1 1 
ATOM   1215 C CD2 . LEU A 1 160 ? -15.26589 11.50421  45.46891 1.000 26.63816 ? 154 LEU A CD2 1 
ATOM   1216 N N   . LEU A 1 161 ? -18.33862 9.26856   48.62804 1.000 18.09549 ? 155 LEU A N   1 
ATOM   1217 C CA  . LEU A 1 161 ? -19.39743 8.59334   49.36447 1.000 16.51342 ? 155 LEU A CA  1 
ATOM   1218 C C   . LEU A 1 161 ? -20.70606 8.72785   48.60065 1.000 16.93610 ? 155 LEU A C   1 
ATOM   1219 O O   . LEU A 1 161 ? -21.03090 9.80966   48.10281 1.000 17.21543 ? 155 LEU A O   1 
ATOM   1220 C CB  . LEU A 1 161 ? -19.57944 9.17651   50.78146 1.000 20.19930 ? 155 LEU A CB  1 
ATOM   1221 C CG  . LEU A 1 161 ? -18.48944 9.03963   51.85458 1.000 19.79233 ? 155 LEU A CG  1 
ATOM   1222 C CD1 . LEU A 1 161 ? -18.03652 7.59619   52.01576 1.000 15.98972 ? 155 LEU A CD1 1 
ATOM   1223 C CD2 . LEU A 1 161 ? -17.31175 9.95889   51.58726 1.000 20.78061 ? 155 LEU A CD2 1 
ATOM   1224 N N   . ASN A 1 162 ? -21.45661 7.63216   48.50645 1.000 18.58579 ? 156 ASN A N   1 
ATOM   1225 C CA  . ASN A 1 162 ? -22.79903 7.70361   47.94727 1.000 18.84154 ? 156 ASN A CA  1 
ATOM   1226 C C   . ASN A 1 162 ? -23.79531 7.96421   49.07622 1.000 21.53649 ? 156 ASN A C   1 
ATOM   1227 O O   . ASN A 1 162 ? -23.41496 8.16695   50.23361 1.000 21.57686 ? 156 ASN A O   1 
ATOM   1228 C CB  . ASN A 1 162 ? -23.12590 6.44744   47.13520 1.000 18.78295 ? 156 ASN A CB  1 
ATOM   1229 C CG  . ASN A 1 162 ? -23.21893 5.18465   47.98028 1.000 23.34960 ? 156 ASN A CG  1 
ATOM   1230 O OD1 . ASN A 1 162 ? -23.25629 5.22621   49.20949 1.000 28.39131 ? 156 ASN A OD1 1 
ATOM   1231 N ND2 . ASN A 1 162 ? -23.28827 4.04323   47.30482 1.000 33.36873 ? 156 ASN A ND2 1 
ATOM   1232 N N   . THR A 1 163 ? -25.08977 7.95088   48.74819 1.000 18.89500 ? 157 THR A N   1 
ATOM   1233 C CA  . THR A 1 163 ? -26.11320 8.31927   49.71746 1.000 25.14460 ? 157 THR A CA  1 
ATOM   1234 C C   . THR A 1 163 ? -26.24624 7.30761   50.84941 1.000 27.92436 ? 157 THR A C   1 
ATOM   1235 O O   . THR A 1 163 ? -26.77083 7.65545   51.91322 1.000 25.42391 ? 157 THR A O   1 
ATOM   1236 C CB  . THR A 1 163 ? -27.46135 8.50057   49.00834 1.000 25.40041 ? 157 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 163 ? -28.28308 9.38860   49.77230 1.000 38.64324 ? 157 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 163 ? -28.17765 7.16816   48.83596 1.000 28.97932 ? 157 THR A CG2 1 
ATOM   1239 N N   . THR A 1 164 ? -25.78331 6.07745   50.65297 1.000 20.11938 ? 158 THR A N   1 
ATOM   1240 C CA  . THR A 1 164 ? -25.83944 5.06831   51.70124 1.000 16.84014 ? 158 THR A CA  1 
ATOM   1241 C C   . THR A 1 164 ? -24.45741 4.87891   52.32349 1.000 27.72413 ? 158 THR A C   1 
ATOM   1242 O O   . THR A 1 164 ? -24.13633 3.81173   52.84707 1.000 26.22420 ? 158 THR A O   1 
ATOM   1243 C CB  . THR A 1 164 ? -26.35657 3.72601   51.16835 1.000 20.75041 ? 158 THR A CB  1 
ATOM   1244 O OG1 . THR A 1 164 ? -25.72314 3.43049   49.91954 1.000 22.97134 ? 158 THR A OG1 1 
ATOM   1245 C CG2 . THR A 1 164 ? -27.86471 3.78604   50.96128 1.000 30.65645 ? 158 THR A CG2 1 
HETATM 1246 N N   . CME A 1 165 ? -23.64733 5.92926   52.24373 1.000 19.24014 ? 159 CME A N   1 
HETATM 1247 C CA  . CME A 1 165 ? -22.24664 5.98257   52.94365 1.000 21.41558 ? 159 CME A CA  1 
HETATM 1248 C CB  . CME A 1 165 ? -22.39896 5.87417   54.41952 1.000 23.65866 ? 159 CME A CB  1 
HETATM 1249 S SG  . CME A 1 165 ? -23.26583 7.32080   55.12054 0.800 22.24743 ? 159 CME A SG  1 
HETATM 1250 S SD  . CME A 1 165 ? -22.18228 8.88858   54.55123 0.800 28.64160 ? 159 CME A SD  1 
HETATM 1251 C CE  . CME A 1 165 ? -23.05605 9.58917   53.05937 0.800 27.71163 ? 159 CME A CE  1 
HETATM 1252 C CZ  . CME A 1 165 ? -24.26748 10.17617  53.30846 0.800 28.71560 ? 159 CME A CZ  1 
HETATM 1253 O OH  . CME A 1 165 ? -24.12812 11.16327  54.29708 0.800 25.89076 ? 159 CME A OH  1 
HETATM 1254 C C   . CME A 1 165 ? -21.25135 4.79483   52.39294 1.000 24.30342 ? 159 CME A C   1 
HETATM 1255 O O   . CME A 1 165 ? -20.29608 4.42910   53.06628 1.000 20.56313 ? 159 CME A O   1 
ATOM   1256 N N   . ASP A 1 166 ? -21.52651 4.26567   51.20448 1.000 20.35242 ? 160 ASP A N   1 
ATOM   1257 C CA  . ASP A 1 166 ? -20.54090 3.41035   50.54461 1.000 20.33613 ? 160 ASP A CA  1 
ATOM   1258 C C   . ASP A 1 166 ? -19.40334 4.29420   50.04529 1.000 17.03887 ? 160 ASP A C   1 
ATOM   1259 O O   . ASP A 1 166 ? -19.64269 5.37951   49.51625 1.000 14.94681 ? 160 ASP A O   1 
ATOM   1260 C CB  . ASP A 1 166 ? -21.15730 2.61400   49.39167 0.700 20.49730 ? 160 ASP A CB  1 
ATOM   1261 C CG  . ASP A 1 166 ? -22.32470 1.75266   49.83177 0.700 21.29868 ? 160 ASP A CG  1 
ATOM   1262 O OD1 . ASP A 1 166 ? -22.09093 0.72824   50.50652 0.700 27.21404 ? 160 ASP A OD1 1 
ATOM   1263 O OD2 . ASP A 1 166 ? -23.47545 2.09154   49.49185 0.700 28.31358 ? 160 ASP A OD2 1 
ATOM   1264 N N   . LEU A 1 167 ? -18.16805 3.82946   50.21426 1.000 16.25077 ? 161 LEU A N   1 
ATOM   1265 C CA  . LEU A 1 167 ? -16.98380 4.63153   49.94752 1.000 11.25593 ? 161 LEU A CA  1 
ATOM   1266 C C   . LEU A 1 167 ? -16.21178 4.05981   48.76448 1.000 13.92039 ? 161 LEU A C   1 
ATOM   1267 O O   . LEU A 1 167 ? -16.09462 2.83857   48.61710 1.000 15.97804 ? 161 LEU A O   1 
ATOM   1268 C CB  . LEU A 1 167 ? -16.09094 4.69364   51.19655 1.000 14.29174 ? 161 LEU A CB  1 
ATOM   1269 C CG  . LEU A 1 167 ? -14.80728 5.52742   51.20664 1.000 17.41567 ? 161 LEU A CG  1 
ATOM   1270 C CD1 . LEU A 1 167 ? -14.50843 5.96410   52.63116 1.000 17.93016 ? 161 LEU A CD1 1 
ATOM   1271 C CD2 . LEU A 1 167 ? -13.62075 4.74366   50.65355 1.000 17.85149 ? 161 LEU A CD2 1 
ATOM   1272 N N   . LYS A 1 168 ? -15.69007 4.94949   47.91922 1.000 14.26325 ? 162 LYS A N   1 
ATOM   1273 C CA  . LYS A 1 168 ? -14.85576 4.55583   46.79176 1.000 15.75773 ? 162 LYS A CA  1 
ATOM   1274 C C   . LYS A 1 168 ? -13.64438 5.47258   46.69209 1.000 17.54662 ? 162 LYS A C   1 
ATOM   1275 O O   . LYS A 1 168 ? -13.75067 6.68650   46.89393 1.000 14.50978 ? 162 LYS A O   1 
ATOM   1276 C CB  . LYS A 1 168 ? -15.63411 4.57935   45.46691 1.000 12.09976 ? 162 LYS A CB  1 
ATOM   1277 C CG  . LYS A 1 168 ? -16.80339 3.60731   45.39161 1.000 14.21905 ? 162 LYS A CG  1 
ATOM   1278 C CD  . LYS A 1 168 ? -17.51077 3.72436   44.04422 1.000 19.98339 ? 162 LYS A CD  1 
ATOM   1279 C CE  . LYS A 1 168 ? -18.78745 2.89675   43.98317 1.000 29.40835 ? 162 LYS A CE  1 
ATOM   1280 N NZ  . LYS A 1 168 ? -18.53293 1.44457   44.18610 1.000 27.06608 ? 162 LYS A NZ  1 
ATOM   1281 N N   . ILE A 1 169 ? -12.49833 4.88075   46.36288 1.000 12.47842 ? 163 ILE A N   1 
ATOM   1282 C CA  . ILE A 1 169 ? -11.23450 5.60147   46.24948 1.000 13.12865 ? 163 ILE A CA  1 
ATOM   1283 C C   . ILE A 1 169 ? -11.08881 6.11286   44.82337 1.000 11.80105 ? 163 ILE A C   1 
ATOM   1284 O O   . ILE A 1 169 ? -11.28089 5.35950   43.86210 1.000 15.15088 ? 163 ILE A O   1 
ATOM   1285 C CB  . ILE A 1 169 ? -10.05428 4.69348   46.63232 1.000 18.44869 ? 163 ILE A CB  1 
ATOM   1286 C CG1 . ILE A 1 169 ? -10.14862 4.29537   48.10471 1.000 12.36438 ? 163 ILE A CG1 1 
ATOM   1287 C CG2 . ILE A 1 169 ? -8.72582  5.38692   46.34753 1.000 17.91121 ? 163 ILE A CG2 1 
ATOM   1288 C CD1 . ILE A 1 169 ? -9.19355  3.18615   48.49651 1.000 13.54887 ? 163 ILE A CD1 1 
ATOM   1289 N N   . CYS A 1 170 ? -10.72982 7.38610   44.68459 1.000 13.97326 ? 164 CYS A N   1 
ATOM   1290 C CA  A CYS A 1 170 ? -10.64753 8.08900   43.41049 0.800 16.82471 ? 164 CYS A CA  1 
ATOM   1291 C CA  B CYS A 1 170 ? -10.61718 7.99988   43.37534 0.200 16.75008 ? 164 CYS A CA  1 
ATOM   1292 C C   . CYS A 1 170 ? -9.23483  8.61246   43.17451 1.000 23.01918 ? 164 CYS A C   1 
ATOM   1293 O O   . CYS A 1 170 ? -8.43216  8.73811   44.10553 1.000 16.31682 ? 164 CYS A O   1 
ATOM   1294 C CB  A CYS A 1 170 ? -11.63667 9.26745   43.36553 0.800 18.21396 ? 164 CYS A CB  1 
ATOM   1295 C CB  B CYS A 1 170 ? -11.72393 9.03878   43.18732 0.200 18.89838 ? 164 CYS A CB  1 
ATOM   1296 S SG  A CYS A 1 170 ? -11.90896 10.02380  41.72639 0.800 19.87081 ? 164 CYS A SG  1 
ATOM   1297 S SG  B CYS A 1 170 ? -11.55432 10.47509  44.23240 0.200 21.50676 ? 164 CYS A SG  1 
ATOM   1298 N N   . ASP A 1 171 ? -8.95965  8.94828   41.91191 1.000 18.35910 ? 165 ASP A N   1 
ATOM   1299 C CA  . ASP A 1 171 ? -7.71702  9.55596   41.43883 1.000 20.16996 ? 165 ASP A CA  1 
ATOM   1300 C C   . ASP A 1 171 ? -6.49452  8.66497   41.62593 1.000 20.67966 ? 165 ASP A C   1 
ATOM   1301 O O   . ASP A 1 171 ? -5.87590  8.65083   42.69556 1.000 21.89416 ? 165 ASP A O   1 
ATOM   1302 C CB  . ASP A 1 171 ? -7.47767  10.90685  42.11503 1.000 19.87160 ? 165 ASP A CB  1 
ATOM   1303 C CG  . ASP A 1 171 ? -6.39292  11.71836  41.42284 0.800 19.19197 ? 165 ASP A CG  1 
ATOM   1304 O OD1 . ASP A 1 171 ? -5.87814  11.26647  40.37840 0.600 15.82144 ? 165 ASP A OD1 1 
ATOM   1305 O OD2 . ASP A 1 171 ? -6.05578  12.81093  41.92056 0.600 22.02183 ? 165 ASP A OD2 1 
ATOM   1306 N N   . PHE A 1 172 ? -6.11947  7.94210   40.57189 1.000 20.15173 ? 166 PHE A N   1 
ATOM   1307 C CA  . PHE A 1 172 ? -4.88426  7.17083   40.55578 1.000 19.15084 ? 166 PHE A CA  1 
ATOM   1308 C C   . PHE A 1 172 ? -3.82498  7.81117   39.66903 1.000 18.55293 ? 166 PHE A C   1 
ATOM   1309 O O   . PHE A 1 172 ? -2.92507  7.12087   39.17971 1.000 27.79939 ? 166 PHE A O   1 
ATOM   1310 C CB  . PHE A 1 172 ? -5.16462  5.73553   40.11739 1.000 18.14202 ? 166 PHE A CB  1 
ATOM   1311 C CG  . PHE A 1 172 ? -5.80429  4.90290   41.18791 1.000 21.10328 ? 166 PHE A CG  1 
ATOM   1312 C CD1 . PHE A 1 172 ? -7.15212  5.04364   41.47416 1.000 20.95025 ? 166 PHE A CD1 1 
ATOM   1313 C CD2 . PHE A 1 172 ? -5.05522  4.00246   41.92765 1.000 20.96332 ? 166 PHE A CD2 1 
ATOM   1314 C CE1 . PHE A 1 172 ? -7.74598  4.29100   42.46581 1.000 24.63660 ? 166 PHE A CE1 1 
ATOM   1315 C CE2 . PHE A 1 172 ? -5.64425  3.24449   42.92059 1.000 15.21537 ? 166 PHE A CE2 1 
ATOM   1316 C CZ  . PHE A 1 172 ? -6.98941  3.39036   43.19076 1.000 16.18487 ? 166 PHE A CZ  1 
ATOM   1317 N N   . GLY A 1 173 ? -3.91036  9.12617   39.46177 1.000 21.95521 ? 167 GLY A N   1 
ATOM   1318 C CA  . GLY A 1 173 ? -2.96728  9.80972   38.59704 1.000 26.86280 ? 167 GLY A CA  1 
ATOM   1319 C C   . GLY A 1 173 ? -1.58563  9.97237   39.19078 1.000 32.27129 ? 167 GLY A C   1 
ATOM   1320 O O   . GLY A 1 173 ? -0.62837  10.19866  38.44473 1.000 31.65086 ? 167 GLY A O   1 
ATOM   1321 N N   . LEU A 1 174 ? -1.46137  9.88140   40.51352 1.000 25.59928 ? 168 LEU A N   1 
ATOM   1322 C CA  . LEU A 1 174 ? -0.16855  9.92359   41.18218 1.000 28.44818 ? 168 LEU A CA  1 
ATOM   1323 C C   . LEU A 1 174 ? 0.33455   8.53800   41.56024 1.000 23.88226 ? 168 LEU A C   1 
ATOM   1324 O O   . LEU A 1 174 ? 1.37627   8.42630   42.21380 1.000 21.89821 ? 168 LEU A O   1 
ATOM   1325 C CB  . LEU A 1 174 ? -0.23255  10.80425  42.43732 0.800 22.97302 ? 168 LEU A CB  1 
ATOM   1326 C CG  . LEU A 1 174 ? -0.72625  12.25564  42.35585 0.600 30.87305 ? 168 LEU A CG  1 
ATOM   1327 C CD1 . LEU A 1 174 ? -0.01405  13.00793  41.23862 0.600 34.14544 ? 168 LEU A CD1 1 
ATOM   1328 C CD2 . LEU A 1 174 ? -2.25037  12.36960  42.23092 0.600 33.18178 ? 168 LEU A CD2 1 
ATOM   1329 N N   . ALA A 1 175 ? -0.37782  7.48713   41.16544 1.000 19.07498 ? 169 ALA A N   1 
ATOM   1330 C CA  . ALA A 1 175 ? -0.03104  6.13707   41.57229 1.000 22.24953 ? 169 ALA A CA  1 
ATOM   1331 C C   . ALA A 1 175 ? 1.27797   5.68165   40.93050 1.000 22.65433 ? 169 ALA A C   1 
ATOM   1332 O O   . ALA A 1 175 ? 1.69484   6.17165   39.87762 1.000 21.80077 ? 169 ALA A O   1 
ATOM   1333 C CB  . ALA A 1 175 ? -1.15481  5.16810   41.21191 1.000 21.02726 ? 169 ALA A CB  1 
ATOM   1334 N N   . ARG A 1 176 ? 1.92713   4.72239   41.59061 1.000 20.47642 ? 170 ARG A N   1 
ATOM   1335 C CA  . ARG A 1 176 ? 3.17302   4.13367   41.11723 1.000 24.72899 ? 170 ARG A CA  1 
ATOM   1336 C C   . ARG A 1 176 ? 3.19250   2.65417   41.47558 1.000 21.98845 ? 170 ARG A C   1 
ATOM   1337 O O   . ARG A 1 176 ? 2.52475   2.21018   42.41367 1.000 18.30884 ? 170 ARG A O   1 
ATOM   1338 C CB  . ARG A 1 176 ? 4.40974   4.81387   41.73147 1.000 28.36409 ? 170 ARG A CB  1 
ATOM   1339 C CG  . ARG A 1 176 ? 4.61717   6.27466   41.35972 0.900 29.06975 ? 170 ARG A CG  1 
ATOM   1340 C CD  . ARG A 1 176 ? 5.00322   6.44510   39.89711 0.800 43.10401 ? 170 ARG A CD  1 
ATOM   1341 N NE  . ARG A 1 176 ? 5.53963   7.77372   39.61614 0.800 44.51352 ? 170 ARG A NE  1 
ATOM   1342 C CZ  . ARG A 1 176 ? 4.85903   8.90841   39.72237 0.700 43.33448 ? 170 ARG A CZ  1 
ATOM   1343 N NH1 . ARG A 1 176 ? 3.57568   8.92139   40.04507 0.600 36.00105 ? 170 ARG A NH1 1 
ATOM   1344 N NH2 . ARG A 1 176 ? 5.47979   10.06069  39.48739 0.500 44.00541 ? 170 ARG A NH2 1 
ATOM   1345 N N   . VAL A 1 177 ? 3.97434   1.88966   40.71582 1.000 27.66243 ? 171 VAL A N   1 
ATOM   1346 C CA  . VAL A 1 177 ? 4.27011   0.51767   41.10535 1.000 22.63546 ? 171 VAL A CA  1 
ATOM   1347 C C   . VAL A 1 177 ? 5.25515   0.53857   42.26454 1.000 22.78907 ? 171 VAL A C   1 
ATOM   1348 O O   . VAL A 1 177 ? 6.23652   1.29365   42.25111 1.000 26.05129 ? 171 VAL A O   1 
ATOM   1349 C CB  . VAL A 1 177 ? 4.82339   -0.27746  39.91412 1.000 27.42729 ? 171 VAL A CB  1 
ATOM   1350 C CG1 . VAL A 1 177 ? 5.28985   -1.65414  40.36266 1.000 26.39760 ? 171 VAL A CG1 1 
ATOM   1351 C CG2 . VAL A 1 177 ? 3.76840   -0.39571  38.82173 1.000 25.88237 ? 171 VAL A CG2 1 
ATOM   1352 N N   . ALA A 1 178 ? 4.98984   -0.27851  43.28151 1.000 20.86180 ? 172 ALA A N   1 
ATOM   1353 C CA  . ALA A 1 178 ? 5.86055   -0.32020  44.44868 1.000 20.37769 ? 172 ALA A CA  1 
ATOM   1354 C C   . ALA A 1 178 ? 7.27731   -0.71345  44.04769 1.000 22.98734 ? 172 ALA A C   1 
ATOM   1355 O O   . ALA A 1 178 ? 7.48371   -1.56061  43.17527 1.000 24.68506 ? 172 ALA A O   1 
ATOM   1356 C CB  . ALA A 1 178 ? 5.31060   -1.30137  45.48324 1.000 21.40984 ? 172 ALA A CB  1 
ATOM   1357 N N   . ASP A 1 179 ? 8.25995   -0.08121  44.69095 1.000 25.17445 ? 173 ASP A N   1 
ATOM   1358 C CA  . ASP A 1 179 ? 9.67283   -0.31818  44.39234 1.000 24.47660 ? 173 ASP A CA  1 
ATOM   1359 C C   . ASP A 1 179 ? 10.47600  -0.10997  45.66843 1.000 28.51998 ? 173 ASP A C   1 
ATOM   1360 O O   . ASP A 1 179 ? 11.25319  0.84388   45.79009 1.000 30.32540 ? 173 ASP A O   1 
ATOM   1361 C CB  . ASP A 1 179 ? 10.14754  0.61261   43.27798 1.000 29.67337 ? 173 ASP A CB  1 
ATOM   1362 C CG  . ASP A 1 179 ? 11.48022  0.19869   42.69461 1.000 35.84006 ? 173 ASP A CG  1 
ATOM   1363 O OD1 . ASP A 1 179 ? 12.07639  -0.78570  43.18146 1.000 29.54940 ? 173 ASP A OD1 1 
ATOM   1364 O OD2 . ASP A 1 179 ? 11.92883  0.86221   41.73825 1.000 35.82168 ? 173 ASP A OD2 1 
ATOM   1365 N N   . PRO A 1 180 ? 10.31092  -0.99944  46.65334 1.000 34.70731 ? 174 PRO A N   1 
ATOM   1366 C CA  . PRO A 1 180 ? 10.91859  -0.75173  47.97166 1.000 29.60585 ? 174 PRO A CA  1 
ATOM   1367 C C   . PRO A 1 180 ? 12.43565  -0.80368  47.97199 1.000 33.77176 ? 174 PRO A C   1 
ATOM   1368 O O   . PRO A 1 180 ? 13.05358  -0.21217  48.86604 1.000 35.92279 ? 174 PRO A O   1 
ATOM   1369 C CB  . PRO A 1 180 ? 10.32527  -1.86257  48.84800 1.000 30.03315 ? 174 PRO A CB  1 
ATOM   1370 C CG  . PRO A 1 180 ? 9.96852   -2.95003  47.88624 1.000 35.24354 ? 174 PRO A CG  1 
ATOM   1371 C CD  . PRO A 1 180 ? 9.56890   -2.27235  46.60961 1.000 34.69434 ? 174 PRO A CD  1 
ATOM   1372 N N   . ASP A 1 181 ? 13.05822  -1.48592  47.01016 1.000 34.12200 ? 175 ASP A N   1 
ATOM   1373 C CA  . ASP A 1 181 ? 14.51384  -1.55844  46.97872 1.000 36.27687 ? 175 ASP A CA  1 
ATOM   1374 C C   . ASP A 1 181 ? 15.15950  -0.28198  46.45575 1.000 36.70808 ? 175 ASP A C   1 
ATOM   1375 O O   . ASP A 1 181 ? 16.36556  -0.09419  46.64667 1.000 38.30896 ? 175 ASP A O   1 
ATOM   1376 C CB  . ASP A 1 181 ? 14.96652  -2.75076  46.13167 0.800 43.90379 ? 175 ASP A CB  1 
ATOM   1377 C CG  . ASP A 1 181 ? 14.49615  -4.07604  46.69583 0.800 40.55597 ? 175 ASP A CG  1 
ATOM   1378 O OD1 . ASP A 1 181 ? 14.32864  -4.17093  47.93037 0.700 41.09901 ? 175 ASP A OD1 1 
ATOM   1379 O OD2 . ASP A 1 181 ? 14.29548  -5.02259  45.90739 0.700 43.00479 ? 175 ASP A OD2 1 
ATOM   1380 N N   . HIS A 1 182 ? 14.39648  0.59366   45.79874 1.000 33.94130 ? 176 HIS A N   1 
ATOM   1381 C CA  . HIS A 1 182 ? 14.91760  1.85732   45.28788 1.000 39.88261 ? 176 HIS A CA  1 
ATOM   1382 C C   . HIS A 1 182 ? 14.22649  3.04672   45.94924 1.000 32.85064 ? 176 HIS A C   1 
ATOM   1383 O O   . HIS A 1 182 ? 14.02041  4.08070   45.31184 1.000 33.16841 ? 176 HIS A O   1 
ATOM   1384 C CB  A HIS A 1 182 ? 14.77609  1.92481   43.76831 0.500 37.94991 ? 176 HIS A CB  1 
ATOM   1385 C CB  B HIS A 1 182 ? 14.76497  1.95777   43.76803 0.500 37.95203 ? 176 HIS A CB  1 
ATOM   1386 C CG  A HIS A 1 182 ? 15.58980  0.89886   43.04338 0.500 44.95558 ? 176 HIS A CG  1 
ATOM   1387 C CG  B HIS A 1 182 ? 15.14122  0.71614   43.01774 0.500 43.28642 ? 176 HIS A CG  1 
ATOM   1388 N ND1 A HIS A 1 182 ? 15.14004  -0.38495  42.82014 0.500 43.17352 ? 176 HIS A ND1 1 
ATOM   1389 N ND1 B HIS A 1 182 ? 15.90593  -0.29350  43.56205 0.500 48.17050 ? 176 HIS A ND1 1 
ATOM   1390 C CD2 A HIS A 1 182 ? 16.82958  0.96285   42.50202 0.500 43.20608 ? 176 HIS A CD2 1 
ATOM   1391 C CD2 B HIS A 1 182 ? 14.85904  0.33006   41.75081 0.500 44.25055 ? 176 HIS A CD2 1 
ATOM   1392 C CE1 A HIS A 1 182 ? 16.06471  -1.06515  42.16596 0.500 49.06985 ? 176 HIS A CE1 1 
ATOM   1393 C CE1 B HIS A 1 182 ? 16.07163  -1.25049  42.66641 0.500 48.39810 ? 176 HIS A CE1 1 
ATOM   1394 N NE2 A HIS A 1 182 ? 17.09987  -0.27056  41.96101 0.500 41.93830 ? 176 HIS A NE2 1 
ATOM   1395 N NE2 B HIS A 1 182 ? 15.44620  -0.89640  41.55843 0.500 51.14910 ? 176 HIS A NE2 1 
ATOM   1396 N N   . ASP A 1 183 ? 13.86694  2.92099   47.22658 1.000 24.15525 ? 177 ASP A N   1 
ATOM   1397 C CA  . ASP A 1 183 ? 13.07475  3.94839   47.89178 1.000 26.62853 ? 177 ASP A CA  1 
ATOM   1398 C C   . ASP A 1 183 ? 13.91980  4.98699   48.62372 1.000 32.10967 ? 177 ASP A C   1 
ATOM   1399 O O   . ASP A 1 183 ? 13.41802  6.07963   48.91471 1.000 24.26185 ? 177 ASP A O   1 
ATOM   1400 C CB  . ASP A 1 183 ? 12.09918  3.29646   48.87932 1.000 31.88174 ? 177 ASP A CB  1 
ATOM   1401 C CG  . ASP A 1 183 ? 11.19380  4.30377   49.55973 1.000 30.25876 ? 177 ASP A CG  1 
ATOM   1402 O OD1 . ASP A 1 183 ? 10.34748  4.90130   48.86484 1.000 28.52893 ? 177 ASP A OD1 1 
ATOM   1403 O OD2 . ASP A 1 183 ? 11.33120  4.50482   50.78396 1.000 25.68452 ? 177 ASP A OD2 1 
ATOM   1404 N N   . HIS A 1 184 ? 15.18269  4.68715   48.91693 1.000 27.47899 ? 178 HIS A N   1 
ATOM   1405 C CA  . HIS A 1 184 ? 16.02004  5.60403   49.68285 1.000 26.50408 ? 178 HIS A CA  1 
ATOM   1406 C C   . HIS A 1 184 ? 16.46924  6.78980   48.83666 1.000 24.48328 ? 178 HIS A C   1 
ATOM   1407 O O   . HIS A 1 184 ? 16.83404  6.63986   47.66630 1.000 29.63165 ? 178 HIS A O   1 
ATOM   1408 C CB  . HIS A 1 184 ? 17.24510  4.87749   50.24466 0.900 29.11301 ? 178 HIS A CB  1 
ATOM   1409 C CG  . HIS A 1 184 ? 16.92085  3.61270   50.97845 0.700 36.12569 ? 178 HIS A CG  1 
ATOM   1410 N ND1 . HIS A 1 184 ? 17.02421  3.50368   52.34857 0.700 48.04444 ? 178 HIS A ND1 1 
ATOM   1411 C CD2 . HIS A 1 184 ? 16.49973  2.40408   50.53637 0.700 48.08036 ? 178 HIS A CD2 1 
ATOM   1412 C CE1 . HIS A 1 184 ? 16.67972  2.28352   52.71895 0.700 46.84257 ? 178 HIS A CE1 1 
ATOM   1413 N NE2 . HIS A 1 184 ? 16.35729  1.59618   51.63821 0.700 48.97098 ? 178 HIS A NE2 1 
ATOM   1414 N N   . THR A 1 185 ? 16.44461  7.97298   49.44422 1.000 24.58712 ? 179 THR A N   1 
ATOM   1415 C CA  . THR A 1 185 ? 16.92073  9.19771   48.81189 1.000 24.92047 ? 179 THR A CA  1 
ATOM   1416 C C   . THR A 1 185 ? 17.43311  10.13186  49.90509 1.000 24.64228 ? 179 THR A C   1 
ATOM   1417 O O   . THR A 1 185 ? 17.51373  9.75725   51.07907 1.000 24.76019 ? 179 THR A O   1 
ATOM   1418 C CB  . THR A 1 185 ? 15.81804  9.84914   47.96608 1.000 28.58960 ? 179 THR A CB  1 
ATOM   1419 O OG1 . THR A 1 185 ? 16.38675  10.89280  47.16473 1.000 31.09057 ? 179 THR A OG1 1 
ATOM   1420 C CG2 . THR A 1 185 ? 14.73194  10.43484  48.85951 1.000 25.73995 ? 179 THR A CG2 1 
ATOM   1421 N N   . GLY A 1 186 ? 17.77743  11.36089  49.51539 1.000 24.69370 ? 180 GLY A N   1 
ATOM   1422 C CA  . GLY A 1 186 ? 18.38309  12.30839  50.42458 1.000 27.43466 ? 180 GLY A CA  1 
ATOM   1423 C C   . GLY A 1 186 ? 17.37346  13.09557  51.24271 1.000 39.09013 ? 180 GLY A C   1 
ATOM   1424 O O   . GLY A 1 186 ? 16.16041  12.89793  51.16714 1.000 26.72475 ? 180 GLY A O   1 
ATOM   1425 N N   . PHE A 1 187 ? 17.91259  14.02641  52.02713 1.000 28.81024 ? 181 PHE A N   1 
ATOM   1426 C CA  . PHE A 1 187 ? 17.13225  14.81964  52.96778 1.000 33.46350 ? 181 PHE A CA  1 
ATOM   1427 C C   . PHE A 1 187 ? 16.47743  16.00102  52.25882 1.000 26.78723 ? 181 PHE A C   1 
ATOM   1428 O O   . PHE A 1 187 ? 17.13166  16.71863  51.49409 1.000 28.03724 ? 181 PHE A O   1 
ATOM   1429 C CB  . PHE A 1 187 ? 18.04716  15.29499  54.10024 1.000 19.12494 ? 181 PHE A CB  1 
ATOM   1430 C CG  . PHE A 1 187 ? 17.36630  16.13213  55.14899 1.000 23.70622 ? 181 PHE A CG  1 
ATOM   1431 C CD1 . PHE A 1 187 ? 16.23781  15.67823  55.80835 1.000 23.01250 ? 181 PHE A CD1 1 
ATOM   1432 C CD2 . PHE A 1 187 ? 17.89988  17.36068  55.51479 1.000 29.52993 ? 181 PHE A CD2 1 
ATOM   1433 C CE1 . PHE A 1 187 ? 15.63506  16.44849  56.78521 1.000 23.19894 ? 181 PHE A CE1 1 
ATOM   1434 C CE2 . PHE A 1 187 ? 17.30341  18.13280  56.49319 1.000 25.76124 ? 181 PHE A CE2 1 
ATOM   1435 C CZ  . PHE A 1 187 ? 16.16816  17.67530  57.12817 1.000 24.46957 ? 181 PHE A CZ  1 
ATOM   1436 N N   . LEU A 1 188 ? 15.17605  16.18308  52.50130 1.000 27.25206 ? 182 LEU A N   1 
ATOM   1437 C CA  . LEU A 1 188 ? 14.41849  17.32515  51.98334 1.000 27.30237 ? 182 LEU A CA  1 
ATOM   1438 C C   . LEU A 1 188 ? 14.37825  17.33770  50.45574 1.000 40.30428 ? 182 LEU A C   1 
ATOM   1439 O O   . LEU A 1 188 ? 14.43054  18.39597  49.82497 1.000 27.98535 ? 182 LEU A O   1 
ATOM   1440 C CB  . LEU A 1 188 ? 14.98059  18.64339  52.52401 1.000 40.35831 ? 182 LEU A CB  1 
ATOM   1441 C CG  . LEU A 1 188 ? 14.87474  18.85041  54.03778 1.000 32.12532 ? 182 LEU A CG  1 
ATOM   1442 C CD1 . LEU A 1 188 ? 15.21552  20.28276  54.41625 1.000 29.67561 ? 182 LEU A CD1 1 
ATOM   1443 C CD2 . LEU A 1 188 ? 13.47675  18.48929  54.52257 1.000 25.40640 ? 182 LEU A CD2 1 
ATOM   1444 N N   . THR A 1 189 ? 14.27435  16.15645  49.85251 1.000 26.65412 ? 183 THR A N   1 
ATOM   1445 C CA  . THR A 1 189 ? 14.13394  16.05315  48.40604 1.000 36.23379 ? 183 THR A CA  1 
ATOM   1446 C C   . THR A 1 189 ? 12.66980  16.16721  47.99818 1.000 33.42892 ? 183 THR A C   1 
ATOM   1447 O O   . THR A 1 189 ? 11.77183  15.69471  48.70308 1.000 30.52977 ? 183 THR A O   1 
ATOM   1448 C CB  . THR A 1 189 ? 14.72836  14.74376  47.87997 1.000 29.77512 ? 183 THR A CB  1 
ATOM   1449 O OG1 . THR A 1 189 ? 13.87304  13.64752  48.22826 1.000 60.56151 ? 183 THR A OG1 1 
ATOM   1450 C CG2 . THR A 1 189 ? 16.12529  14.51970  48.42823 1.000 41.39155 ? 183 THR A CG2 1 
ATOM   1451 N N   . GLU A 1 190 ? 12.45032  16.79169  46.83977 1.000 30.34271 ? 184 GLU A N   1 
ATOM   1452 C CA  . GLU A 1 190 ? 11.14108  17.20624  46.34409 1.000 57.95023 ? 184 GLU A CA  1 
ATOM   1453 C C   . GLU A 1 190 ? 10.11203  16.08266  46.36656 1.000 56.03624 ? 184 GLU A C   1 
ATOM   1454 O O   . GLU A 1 190 ? 10.47035  14.89992  46.35333 1.000 55.29607 ? 184 GLU A O   1 
ATOM   1455 C CB  . GLU A 1 190 ? 11.28241  17.74773  44.91831 1.000 50.54406 ? 184 GLU A CB  1 
ATOM   1456 C CG  . GLU A 1 190 ? 12.19831  18.96171  44.78803 1.000 58.27752 ? 184 GLU A CG  1 
ATOM   1457 C CD  . GLU A 1 190 ? 13.65723  18.58517  44.56404 0.700 63.47913 ? 184 GLU A CD  1 
ATOM   1458 O OE1 . GLU A 1 190 ? 14.08075  17.50526  45.03160 0.700 52.29919 ? 184 GLU A OE1 1 
ATOM   1459 O OE2 . GLU A 1 190 ? 14.38045  19.37157  43.91593 0.700 63.42746 ? 184 GLU A OE2 1 
ATOM   1460 N N   . TYR A 1 191 ? 8.83080   16.44313  46.38958 1.000 54.29164 ? 185 TYR A N   1 
ATOM   1461 C CA  . TYR A 1 191 ? 7.77540   15.44197  46.39482 1.000 56.57793 ? 185 TYR A CA  1 
ATOM   1462 C C   . TYR A 1 191 ? 6.48395   16.05162  45.86891 1.000 56.09470 ? 185 TYR A C   1 
ATOM   1463 O O   . TYR A 1 191 ? 6.33233   17.27398  45.80297 1.000 48.45717 ? 185 TYR A O   1 
ATOM   1464 C CB  . TYR A 1 191 ? 7.56967   14.85589  47.79016 1.000 44.72870 ? 185 TYR A CB  1 
ATOM   1465 C CG  . TYR A 1 191 ? 6.87628   13.52225  47.74892 1.000 50.01892 ? 185 TYR A CG  1 
ATOM   1466 C CD1 . TYR A 1 191 ? 7.51899   12.40304  47.23814 1.000 54.31448 ? 185 TYR A CD1 1 
ATOM   1467 C CD2 . TYR A 1 191 ? 5.57924   13.37961  48.21094 1.000 49.44801 ? 185 TYR A CD2 1 
ATOM   1468 C CE1 . TYR A 1 191 ? 6.88668   11.17849  47.19059 1.000 31.27017 ? 185 TYR A CE1 1 
ATOM   1469 C CE2 . TYR A 1 191 ? 4.94479   12.15971  48.17312 1.000 43.98417 ? 185 TYR A CE2 1 
ATOM   1470 C CZ  . TYR A 1 191 ? 5.59900   11.06328  47.66075 1.000 35.82347 ? 185 TYR A CZ  1 
ATOM   1471 O OH  . TYR A 1 191 ? 4.95997   9.84601   47.62174 1.000 45.61243 ? 185 TYR A OH  1 
ATOM   1472 N N   . VAL A 1 192 ? 5.54608   15.17131  45.51400 1.000 47.17645 ? 186 VAL A N   1 
ATOM   1473 C CA  . VAL A 1 192 ? 4.35634   15.56257  44.77599 1.000 55.68653 ? 186 VAL A CA  1 
ATOM   1474 C C   . VAL A 1 192 ? 3.07457   15.46518  45.60259 1.000 39.89222 ? 186 VAL A C   1 
ATOM   1475 O O   . VAL A 1 192 ? 2.17254   16.28963  45.41305 1.000 48.62056 ? 186 VAL A O   1 
ATOM   1476 C CB  . VAL A 1 192 ? 4.23089   14.72680  43.48383 1.000 50.17481 ? 186 VAL A CB  1 
ATOM   1477 C CG1 . VAL A 1 192 ? 3.22214   15.35654  42.53153 1.000 54.44908 ? 186 VAL A CG1 1 
ATOM   1478 C CG2 . VAL A 1 192 ? 5.58510   14.58088  42.80986 1.000 57.06340 ? 186 VAL A CG2 1 
ATOM   1479 N N   . ALA A 1 193 ? 2.96087   14.49246  46.50708 1.000 49.42435 ? 187 ALA A N   1 
ATOM   1480 C CA  . ALA A 1 193 ? 1.69171   14.23549  47.17688 1.000 43.41339 ? 187 ALA A CA  1 
ATOM   1481 C C   . ALA A 1 193 ? 1.31982   15.37883  48.11872 1.000 26.65899 ? 187 ALA A C   1 
ATOM   1482 O O   . ALA A 1 193 ? 2.10988   16.28565  48.39518 1.000 41.69354 ? 187 ALA A O   1 
ATOM   1483 C CB  . ALA A 1 193 ? 1.73994   12.92353  47.95533 1.000 24.00974 ? 187 ALA A CB  1 
ATOM   1484 N N   . THR A 1 194 ? 0.09102   15.30650  48.63078 1.000 35.25394 ? 188 THR A N   1 
ATOM   1485 C CA  . THR A 1 194 ? -0.48648  16.41301  49.38271 1.000 23.65375 ? 188 THR A CA  1 
ATOM   1486 C C   . THR A 1 194 ? 0.14759   16.51262  50.76658 1.000 25.31343 ? 188 THR A C   1 
ATOM   1487 O O   . THR A 1 194 ? 0.23958   15.52096  51.49652 1.000 20.41635 ? 188 THR A O   1 
ATOM   1488 C CB  . THR A 1 194 ? -1.99934  16.24769  49.49042 1.000 20.22711 ? 188 THR A CB  1 
ATOM   1489 O OG1 . THR A 1 194 ? -2.54523  16.04365  48.17780 1.000 16.82802 ? 188 THR A OG1 1 
ATOM   1490 C CG2 . THR A 1 194 ? -2.61375  17.50157  50.08144 1.000 14.62013 ? 188 THR A CG2 1 
ATOM   1491 N N   . ARG A 1 195 ? 0.52664   17.73888  51.13319 1.000 20.11754 ? 189 ARG A N   1 
ATOM   1492 C CA  A ARG A 1 195 ? 1.37797   17.98564  52.29536 0.500 20.26093 ? 189 ARG A CA  1 
ATOM   1493 C CA  B ARG A 1 195 ? 1.38833   17.96152  52.29033 0.500 20.25509 ? 189 ARG A CA  1 
ATOM   1494 C C   . ARG A 1 195 ? 0.83098   17.34215  53.56704 1.000 21.09551 ? 189 ARG A C   1 
ATOM   1495 O O   . ARG A 1 195 ? 1.51704   16.56204  54.23704 1.000 20.11703 ? 189 ARG A O   1 
ATOM   1496 C CB  A ARG A 1 195 ? 1.52850   19.49685  52.48512 0.500 24.10273 ? 189 ARG A CB  1 
ATOM   1497 C CB  B ARG A 1 195 ? 1.61485   19.45550  52.48909 0.500 24.14572 ? 189 ARG A CB  1 
ATOM   1498 C CG  A ARG A 1 195 ? 2.40551   19.91971  53.64761 0.500 22.13174 ? 189 ARG A CG  1 
ATOM   1499 C CG  B ARG A 1 195 ? 2.62654   19.74851  53.57289 0.500 21.88384 ? 189 ARG A CG  1 
ATOM   1500 C CD  A ARG A 1 195 ? 2.24845   21.41094  53.91172 0.500 22.26350 ? 189 ARG A CD  1 
ATOM   1501 C CD  B ARG A 1 195 ? 2.85020   21.22647  53.70286 0.500 24.01608 ? 189 ARG A CD  1 
ATOM   1502 N NE  A ARG A 1 195 ? 1.97634   22.16025  52.68963 0.500 20.94047 ? 189 ARG A NE  1 
ATOM   1503 N NE  B ARG A 1 195 ? 3.22651   21.82181  52.42676 0.500 27.54951 ? 189 ARG A NE  1 
ATOM   1504 C CZ  A ARG A 1 195 ? 1.03070   23.08290  52.56898 0.500 28.08521 ? 189 ARG A CZ  1 
ATOM   1505 C CZ  B ARG A 1 195 ? 2.58549   22.83013  51.85341 0.500 27.79489 ? 189 ARG A CZ  1 
ATOM   1506 N NH1 A ARG A 1 195 ? 0.25557   23.41619  53.58806 0.500 26.06581 ? 189 ARG A NH1 1 
ATOM   1507 N NH1 B ARG A 1 195 ? 1.53295   23.39295  52.42441 0.500 28.16582 ? 189 ARG A NH1 1 
ATOM   1508 N NH2 A ARG A 1 195 ? 0.85641   23.68504  51.39503 0.500 25.90332 ? 189 ARG A NH2 1 
ATOM   1509 N NH2 B ARG A 1 195 ? 3.02007   23.29480  50.68500 0.500 29.84238 ? 189 ARG A NH2 1 
ATOM   1510 N N   . TRP A 1 196 ? -0.40745  17.68902  53.93236 1.000 19.72894 ? 190 TRP A N   1 
ATOM   1511 C CA  . TRP A 1 196 ? -0.93543  17.28405  55.23472 1.000 17.64848 ? 190 TRP A CA  1 
ATOM   1512 C C   . TRP A 1 196 ? -0.99700  15.77495  55.41897 1.000 21.93749 ? 190 TRP A C   1 
ATOM   1513 O O   . TRP A 1 196 ? -1.12591  15.30565  56.55638 1.000 18.62218 ? 190 TRP A O   1 
ATOM   1514 C CB  . TRP A 1 196 ? -2.32778  17.87506  55.45815 1.000 19.92451 ? 190 TRP A CB  1 
ATOM   1515 C CG  . TRP A 1 196 ? -2.36365  19.37351  55.48777 1.000 21.37134 ? 190 TRP A CG  1 
ATOM   1516 C CD1 . TRP A 1 196 ? -1.30012  20.21987  55.59664 1.000 22.88843 ? 190 TRP A CD1 1 
ATOM   1517 C CD2 . TRP A 1 196 ? -3.53207  20.19989  55.44084 1.000 24.60607 ? 190 TRP A CD2 1 
ATOM   1518 N NE1 . TRP A 1 196 ? -1.73359  21.52562  55.60690 1.000 27.32369 ? 190 TRP A NE1 1 
ATOM   1519 C CE2 . TRP A 1 196 ? -3.10050  21.53889  55.51292 1.000 29.72389 ? 190 TRP A CE2 1 
ATOM   1520 C CE3 . TRP A 1 196 ? -4.90180  19.93675  55.33580 1.000 26.38366 ? 190 TRP A CE3 1 
ATOM   1521 C CZ2 . TRP A 1 196 ? -3.98869  22.61218  55.48377 1.000 28.76066 ? 190 TRP A CZ2 1 
ATOM   1522 C CZ3 . TRP A 1 196 ? -5.78211  21.00360  55.30767 1.000 26.04270 ? 190 TRP A CZ3 1 
ATOM   1523 C CH2 . TRP A 1 196 ? -5.32258  22.32411  55.38157 1.000 25.75493 ? 190 TRP A CH2 1 
ATOM   1524 N N   . TYR A 1 197 ? -0.90103  15.00667  54.33930 1.000 14.74731 ? 191 TYR A N   1 
ATOM   1525 C CA  . TYR A 1 197 ? -1.04178  13.55953  54.39710 1.000 16.02918 ? 191 TYR A CA  1 
ATOM   1526 C C   . TYR A 1 197 ? 0.27186   12.86441  54.07608 1.000 19.49284 ? 191 TYR A C   1 
ATOM   1527 O O   . TYR A 1 197 ? 0.29323   11.64985  53.85167 1.000 19.71943 ? 191 TYR A O   1 
ATOM   1528 C CB  . TYR A 1 197 ? -2.17519  13.14029  53.45553 1.000 16.15406 ? 191 TYR A CB  1 
ATOM   1529 C CG  . TYR A 1 197 ? -3.41784  13.92541  53.80982 1.000 19.15640 ? 191 TYR A CG  1 
ATOM   1530 C CD1 . TYR A 1 197 ? -4.22799  13.54068  54.87083 1.000 22.21298 ? 191 TYR A CD1 1 
ATOM   1531 C CD2 . TYR A 1 197 ? -3.72554  15.10713  53.14808 1.000 14.91942 ? 191 TYR A CD2 1 
ATOM   1532 C CE1 . TYR A 1 197 ? -5.33796  14.28597  55.22829 1.000 16.59574 ? 191 TYR A CE1 1 
ATOM   1533 C CE2 . TYR A 1 197 ? -4.83040  15.86012  53.49998 1.000 18.89133 ? 191 TYR A CE2 1 
ATOM   1534 C CZ  . TYR A 1 197 ? -5.63251  15.44368  54.54012 1.000 15.81098 ? 191 TYR A CZ  1 
ATOM   1535 O OH  . TYR A 1 197 ? -6.73334  16.18719  54.89458 1.000 18.97683 ? 191 TYR A OH  1 
ATOM   1536 N N   . ARG A 1 198 ? 1.36950   13.61913  54.09875 1.000 17.73749 ? 192 ARG A N   1 
ATOM   1537 C CA  . ARG A 1 198 ? 2.69772   13.13718  53.75309 1.000 16.77378 ? 192 ARG A CA  1 
ATOM   1538 C C   . ARG A 1 198 ? 3.35874   12.50255  54.97158 1.000 18.82893 ? 192 ARG A C   1 
ATOM   1539 O O   . ARG A 1 198 ? 3.41317   13.11135  56.04392 1.000 16.74913 ? 192 ARG A O   1 
ATOM   1540 C CB  . ARG A 1 198 ? 3.53260   14.31671  53.25888 1.000 21.02148 ? 192 ARG A CB  1 
ATOM   1541 C CG  . ARG A 1 198 ? 4.25070   14.14727  51.95032 1.000 32.65767 ? 192 ARG A CG  1 
ATOM   1542 C CD  . ARG A 1 198 ? 4.88296   15.48070  51.59075 1.000 22.24745 ? 192 ARG A CD  1 
ATOM   1543 N NE  . ARG A 1 198 ? 4.18472   16.12367  50.48397 1.000 20.81117 ? 192 ARG A NE  1 
ATOM   1544 C CZ  . ARG A 1 198 ? 4.30351   17.40531  50.16642 1.000 30.16588 ? 192 ARG A CZ  1 
ATOM   1545 N NH1 . ARG A 1 198 ? 5.04294   18.23055  50.88895 1.000 28.03132 ? 192 ARG A NH1 1 
ATOM   1546 N NH2 . ARG A 1 198 ? 3.65911   17.87251  49.10037 1.000 33.00822 ? 192 ARG A NH2 1 
ATOM   1547 N N   . ALA A 1 199 ? 3.86649   11.28679  54.80220 1.000 13.64703 ? 193 ALA A N   1 
ATOM   1548 C CA  . ALA A 1 199 ? 4.54431   10.59883  55.88516 1.000 16.00386 ? 193 ALA A CA  1 
ATOM   1549 C C   . ALA A 1 199 ? 5.87289   11.28673  56.20289 1.000 15.15989 ? 193 ALA A C   1 
ATOM   1550 O O   . ALA A 1 199 ? 6.49672   11.88592  55.32195 1.000 15.44117 ? 193 ALA A O   1 
ATOM   1551 C CB  . ALA A 1 199 ? 4.78248   9.13773   55.51246 1.000 17.03557 ? 193 ALA A CB  1 
ATOM   1552 N N   . PRO A 1 200 ? 6.32853   11.21453  57.45797 1.000 19.64706 ? 194 PRO A N   1 
ATOM   1553 C CA  . PRO A 1 200 ? 7.55710   11.93879  57.82535 1.000 14.47195 ? 194 PRO A CA  1 
ATOM   1554 C C   . PRO A 1 200 ? 8.77058   11.51779  57.02018 1.000 19.14111 ? 194 PRO A C   1 
ATOM   1555 O O   . PRO A 1 200 ? 9.62193   12.36472  56.72216 1.000 15.61907 ? 194 PRO A O   1 
ATOM   1556 C CB  . PRO A 1 200 ? 7.72505   11.61429  59.31657 1.000 15.30337 ? 194 PRO A CB  1 
ATOM   1557 C CG  . PRO A 1 200 ? 6.96010   10.34997  59.52641 1.000 12.06408 ? 194 PRO A CG  1 
ATOM   1558 C CD  . PRO A 1 200 ? 5.80299   10.41038  58.57483 1.000 17.31292 ? 194 PRO A CD  1 
ATOM   1559 N N   . GLU A 1 201 ? 8.87024   10.24157  56.63430 1.000 14.40590 ? 195 GLU A N   1 
ATOM   1560 C CA  . GLU A 1 201 ? 10.05330  9.79032   55.90743 1.000 16.65641 ? 195 GLU A CA  1 
ATOM   1561 C C   . GLU A 1 201 ? 10.16617  10.42170  54.52534 1.000 15.84643 ? 195 GLU A C   1 
ATOM   1562 O O   . GLU A 1 201 ? 11.25679  10.41120  53.94143 1.000 17.08793 ? 195 GLU A O   1 
ATOM   1563 C CB  . GLU A 1 201 ? 10.06224  8.26472   55.79178 1.000 17.44812 ? 195 GLU A CB  1 
ATOM   1564 C CG  . GLU A 1 201 ? 8.90719   7.66371   55.00462 1.000 20.10096 ? 195 GLU A CG  1 
ATOM   1565 C CD  . GLU A 1 201 ? 7.70128   7.33883   55.87326 1.000 17.81748 ? 195 GLU A CD  1 
ATOM   1566 O OE1 . GLU A 1 201 ? 7.63771   7.80860   57.03127 1.000 14.86351 ? 195 GLU A OE1 1 
ATOM   1567 O OE2 . GLU A 1 201 ? 6.82123   6.59315   55.39979 1.000 18.59685 ? 195 GLU A OE2 1 
ATOM   1568 N N   . ILE A 1 202 ? 9.07022   10.96830  53.99170 1.000 20.34808 ? 196 ILE A N   1 
ATOM   1569 C CA  . ILE A 1 202 ? 9.14258   11.69665  52.72928 1.000 16.15174 ? 196 ILE A CA  1 
ATOM   1570 C C   . ILE A 1 202 ? 10.07122  12.89661  52.86196 1.000 22.40705 ? 196 ILE A C   1 
ATOM   1571 O O   . ILE A 1 202 ? 10.86956  13.18380  51.96155 1.000 22.63081 ? 196 ILE A O   1 
ATOM   1572 C CB  . ILE A 1 202 ? 7.73315   12.11715  52.26933 1.000 16.48424 ? 196 ILE A CB  1 
ATOM   1573 C CG1 . ILE A 1 202 ? 6.86748   10.88842  51.97773 1.000 20.55872 ? 196 ILE A CG1 1 
ATOM   1574 C CG2 . ILE A 1 202 ? 7.81695   13.01330  51.03908 1.000 19.55803 ? 196 ILE A CG2 1 
ATOM   1575 C CD1 . ILE A 1 202 ? 7.35314   10.05773  50.80602 1.000 19.09662 ? 196 ILE A CD1 1 
ATOM   1576 N N   . MET A 1 203 ? 9.99115   13.61091  53.98559 1.000 18.36760 ? 197 MET A N   1 
ATOM   1577 C CA  . MET A 1 203 ? 10.86968  14.75033  54.20201 1.000 25.85406 ? 197 MET A CA  1 
ATOM   1578 C C   . MET A 1 203 ? 12.29492  14.33913  54.55152 1.000 28.19878 ? 197 MET A C   1 
ATOM   1579 O O   . MET A 1 203 ? 13.19598  15.18445  54.51082 1.000 28.03976 ? 197 MET A O   1 
ATOM   1580 C CB  . MET A 1 203 ? 10.34778  15.65248  55.32743 1.000 20.57973 ? 197 MET A CB  1 
ATOM   1581 C CG  . MET A 1 203 ? 9.06464   16.43107  55.04786 1.000 23.53423 ? 197 MET A CG  1 
ATOM   1582 S SD  . MET A 1 203 ? 7.70140   15.45698  54.38696 1.000 23.27256 ? 197 MET A SD  1 
ATOM   1583 C CE  . MET A 1 203 ? 6.90884   14.96492  55.91153 1.000 24.18446 ? 197 MET A CE  1 
ATOM   1584 N N   . LEU A 1 204 ? 12.51972  13.07287  54.89712 1.000 19.00880 ? 198 LEU A N   1 
ATOM   1585 C CA  . LEU A 1 204 ? 13.78574  12.62876  55.46567 1.000 21.09672 ? 198 LEU A CA  1 
ATOM   1586 C C   . LEU A 1 204 ? 14.61555  11.81055  54.48510 1.000 20.32843 ? 198 LEU A C   1 
ATOM   1587 O O   . LEU A 1 204 ? 15.76592  12.16410  54.20595 1.000 24.92650 ? 198 LEU A O   1 
ATOM   1588 C CB  . LEU A 1 204 ? 13.52411  11.81856  56.74461 1.000 19.20073 ? 198 LEU A CB  1 
ATOM   1589 C CG  . LEU A 1 204 ? 12.95099  12.58503  57.93951 1.000 22.92395 ? 198 LEU A CG  1 
ATOM   1590 C CD1 . LEU A 1 204 ? 12.51192  11.62348  59.03443 1.000 19.37199 ? 198 LEU A CD1 1 
ATOM   1591 C CD2 . LEU A 1 204 ? 13.96971  13.58573  58.47935 1.000 17.43415 ? 198 LEU A CD2 1 
ATOM   1592 N N   . ASN A 1 205 ? 14.06312  10.71521  53.94880 1.000 19.41685 ? 199 ASN A N   1 
ATOM   1593 C CA  . ASN A 1 205 ? 14.91261  9.80534   53.17211 1.000 21.95399 ? 199 ASN A CA  1 
ATOM   1594 C C   . ASN A 1 205 ? 14.13781  8.87597   52.24396 1.000 28.45670 ? 199 ASN A C   1 
ATOM   1595 O O   . ASN A 1 205 ? 14.70737  7.85711   51.84061 1.000 17.87206 ? 199 ASN A O   1 
ATOM   1596 C CB  . ASN A 1 205 ? 15.77423  8.96394   54.12599 1.000 15.53321 ? 199 ASN A CB  1 
ATOM   1597 C CG  . ASN A 1 205 ? 14.94106  8.01719   54.98350 0.800 19.77189 ? 199 ASN A CG  1 
ATOM   1598 O OD1 . ASN A 1 205 ? 13.71040  8.10538   55.01650 0.800 16.88078 ? 199 ASN A OD1 1 
ATOM   1599 N ND2 . ASN A 1 205 ? 15.60913  7.10468   55.67695 0.800 18.80082 ? 199 ASN A ND2 1 
ATOM   1600 N N   . SER A 1 206 ? 12.88698  9.16276   51.88792 1.000 18.37644 ? 200 SER A N   1 
ATOM   1601 C CA  . SER A 1 206 ? 12.07759  8.21286   51.13961 1.000 18.49026 ? 200 SER A CA  1 
ATOM   1602 C C   . SER A 1 206 ? 11.50626  8.85914   49.88487 1.000 26.14771 ? 200 SER A C   1 
ATOM   1603 O O   . SER A 1 206 ? 11.04325  10.00365  49.91878 1.000 17.77002 ? 200 SER A O   1 
ATOM   1604 C CB  . SER A 1 206 ? 10.93947  7.66463   52.00718 1.000 21.14444 ? 200 SER A CB  1 
ATOM   1605 O OG  . SER A 1 206 ? 10.02385  6.91320   51.23259 1.000 20.31587 ? 200 SER A OG  1 
ATOM   1606 N N   . LYS A 1 207 ? 11.54023  8.11587   48.77676 1.000 22.91527 ? 201 LYS A N   1 
ATOM   1607 C CA  . LYS A 1 207 ? 10.90065  8.55416   47.54195 1.000 22.71670 ? 201 LYS A CA  1 
ATOM   1608 C C   . LYS A 1 207 ? 9.40823   8.25623   47.50937 1.000 23.11498 ? 201 LYS A C   1 
ATOM   1609 O O   . LYS A 1 207 ? 8.74076   8.63440   46.54063 1.000 27.48068 ? 201 LYS A O   1 
ATOM   1610 C CB  . LYS A 1 207 ? 11.55264  7.89677   46.32278 1.000 23.81353 ? 201 LYS A CB  1 
ATOM   1611 C CG  . LYS A 1 207 ? 13.06391  7.99067   46.23849 1.000 27.82186 ? 201 LYS A CG  1 
ATOM   1612 C CD  . LYS A 1 207 ? 13.54530  7.17242   45.04801 1.000 29.63968 ? 201 LYS A CD  1 
ATOM   1613 C CE  . LYS A 1 207 ? 14.87029  7.66739   44.49646 0.600 36.90274 ? 201 LYS A CE  1 
ATOM   1614 N NZ  . LYS A 1 207 ? 15.90806  6.60101   44.48723 0.400 31.35334 ? 201 LYS A NZ  1 
ATOM   1615 N N   . GLY A 1 208 ? 8.87375   7.58019   48.52198 1.000 21.85541 ? 202 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 208 ? 7.47131   7.21341   48.50987 1.000 23.89413 ? 202 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 208 ? 7.14214   6.01899   47.64399 1.000 24.14947 ? 202 GLY A C   1 
ATOM   1618 O O   . GLY A 1 208 ? 6.04515   5.95534   47.07982 1.000 23.04305 ? 202 GLY A O   1 
ATOM   1619 N N   . TYR A 1 209 ? 8.06180   5.06336   47.52314 1.000 17.95858 ? 203 TYR A N   1 
ATOM   1620 C CA  . TYR A 1 209 ? 7.86552   3.87936   46.69674 1.000 18.97456 ? 203 TYR A CA  1 
ATOM   1621 C C   . TYR A 1 209 ? 7.50702   2.63607   47.50335 1.000 21.90801 ? 203 TYR A C   1 
ATOM   1622 O O   . TYR A 1 209 ? 7.56571   1.52673   46.96264 1.000 21.70739 ? 203 TYR A O   1 
ATOM   1623 C CB  . TYR A 1 209 ? 9.11317   3.58848   45.85634 1.000 26.72028 ? 203 TYR A CB  1 
ATOM   1624 C CG  . TYR A 1 209 ? 9.48900   4.64487   44.83751 0.900 24.00850 ? 203 TYR A CG  1 
ATOM   1625 C CD1 . TYR A 1 209 ? 8.64853   5.71378   44.55653 0.700 28.46183 ? 203 TYR A CD1 1 
ATOM   1626 C CD2 . TYR A 1 209 ? 10.68542  4.55432   44.13918 0.700 33.71192 ? 203 TYR A CD2 1 
ATOM   1627 C CE1 . TYR A 1 209 ? 8.99812   6.66955   43.61993 0.700 20.64746 ? 203 TYR A CE1 1 
ATOM   1628 C CE2 . TYR A 1 209 ? 11.03936  5.50064   43.20314 0.700 38.33820 ? 203 TYR A CE2 1 
ATOM   1629 C CZ  . TYR A 1 209 ? 10.19397  6.55619   42.94659 0.700 36.53876 ? 203 TYR A CZ  1 
ATOM   1630 O OH  . TYR A 1 209 ? 10.54982  7.50089   42.01170 0.700 37.67422 ? 203 TYR A OH  1 
ATOM   1631 N N   . THR A 1 210 ? 7.12374   2.78629   48.76940 1.000 20.20929 ? 204 THR A N   1 
ATOM   1632 C CA  . THR A 1 210 ? 6.76104   1.65190   49.60690 1.000 20.37429 ? 204 THR A CA  1 
ATOM   1633 C C   . THR A 1 210 ? 5.32096   1.78589   50.07948 1.000 19.69058 ? 204 THR A C   1 
ATOM   1634 O O   . THR A 1 210 ? 4.79330   2.88962   50.20131 1.000 17.42218 ? 204 THR A O   1 
ATOM   1635 C CB  . THR A 1 210 ? 7.68492   1.53135   50.82196 1.000 20.61608 ? 204 THR A CB  1 
ATOM   1636 O OG1 . THR A 1 210 ? 7.35624   2.55462   51.76616 1.000 29.60181 ? 204 THR A OG1 1 
ATOM   1637 C CG2 . THR A 1 210 ? 9.14483   1.66808   50.40315 1.000 25.69732 ? 204 THR A CG2 1 
ATOM   1638 N N   . LYS A 1 211 ? 4.69591   0.64667   50.37383 1.000 15.42012 ? 205 LYS A N   1 
ATOM   1639 C CA  . LYS A 1 211 ? 3.28011   0.64526   50.72639 1.000 15.19014 ? 205 LYS A CA  1 
ATOM   1640 C C   . LYS A 1 211 ? 2.99698   1.44788   51.98929 1.000 20.04776 ? 205 LYS A C   1 
ATOM   1641 O O   . LYS A 1 211 ? 1.86758   1.90898   52.17980 1.000 13.66733 ? 205 LYS A O   1 
ATOM   1642 C CB  . LYS A 1 211 ? 2.80311   -0.79901  50.87713 1.000 22.77777 ? 205 LYS A CB  1 
ATOM   1643 C CG  . LYS A 1 211 ? 2.79305   -1.54930  49.54834 1.000 14.66220 ? 205 LYS A CG  1 
ATOM   1644 C CD  . LYS A 1 211 ? 2.53799   -3.03867  49.70508 1.000 16.90624 ? 205 LYS A CD  1 
ATOM   1645 C CE  . LYS A 1 211 ? 2.59001   -3.72680  48.34678 1.000 17.75590 ? 205 LYS A CE  1 
ATOM   1646 N NZ  . LYS A 1 211 ? 2.27486   -5.17621  48.42962 1.000 19.28429 ? 205 LYS A NZ  1 
ATOM   1647 N N   . SER A 1 212 ? 4.00577   1.65709   52.83746 1.000 15.13110 ? 206 SER A N   1 
ATOM   1648 C CA  . SER A 1 212 ? 3.78365   2.33817   54.10358 1.000 12.14930 ? 206 SER A CA  1 
ATOM   1649 C C   . SER A 1 212 ? 3.42813   3.81360   53.93969 1.000 12.18118 ? 206 SER A C   1 
ATOM   1650 O O   . SER A 1 212 ? 2.90043   4.40760   54.88603 1.000 14.47754 ? 206 SER A O   1 
ATOM   1651 C CB  . SER A 1 212 ? 5.02196   2.19348   54.99493 1.000 20.06165 ? 206 SER A CB  1 
ATOM   1652 O OG  . SER A 1 212 ? 6.20656   2.50248   54.28286 1.000 17.67458 ? 206 SER A OG  1 
ATOM   1653 N N   . ILE A 1 213 ? 3.70230   4.43280   52.78418 1.000 11.03674 ? 207 ILE A N   1 
ATOM   1654 C CA  . ILE A 1 213 ? 3.33733   5.84349   52.66743 1.000 12.52929 ? 207 ILE A CA  1 
ATOM   1655 C C   . ILE A 1 213 ? 1.82467   5.98288   52.58556 1.000 13.63511 ? 207 ILE A C   1 
ATOM   1656 O O   . ILE A 1 213 ? 1.26531   7.00682   52.99721 1.000 13.79887 ? 207 ILE A O   1 
ATOM   1657 C CB  . ILE A 1 213 ? 4.02181   6.54370   51.47165 1.000 19.66154 ? 207 ILE A CB  1 
ATOM   1658 C CG1 . ILE A 1 213 ? 4.05379   5.68110   50.21086 1.000 25.70135 ? 207 ILE A CG1 1 
ATOM   1659 C CG2 . ILE A 1 213 ? 5.44716   6.96118   51.83667 1.000 27.51719 ? 207 ILE A CG2 1 
ATOM   1660 C CD1 . ILE A 1 213 ? 2.78007   5.65742   49.39835 1.000 25.97313 ? 207 ILE A CD1 1 
ATOM   1661 N N   . ASP A 1 214 ? 1.14045   4.96157   52.06369 1.000 10.57400 ? 208 ASP A N   1 
ATOM   1662 C CA  . ASP A 1 214 ? -0.31689  5.00496   51.98704 1.000 12.09180 ? 208 ASP A CA  1 
ATOM   1663 C C   . ASP A 1 214 ? -0.93957  4.83161   53.36381 1.000 14.15602 ? 208 ASP A C   1 
ATOM   1664 O O   . ASP A 1 214 ? -1.94946  5.47038   53.68020 1.000 13.15025 ? 208 ASP A O   1 
ATOM   1665 C CB  . ASP A 1 214 ? -0.83257  3.92087   51.04190 1.000 9.28290  ? 208 ASP A CB  1 
ATOM   1666 C CG  . ASP A 1 214 ? -0.78272  4.33498   49.58502 1.000 12.36558 ? 208 ASP A CG  1 
ATOM   1667 O OD1 . ASP A 1 214 ? -0.80464  5.55290   49.29612 1.000 14.60126 ? 208 ASP A OD1 1 
ATOM   1668 O OD2 . ASP A 1 214 ? -0.73289  3.43190   48.72564 1.000 15.10700 ? 208 ASP A OD2 1 
ATOM   1669 N N   . ILE A 1 215 ? -0.35561  3.96069   54.19148 1.000 14.64427 ? 209 ILE A N   1 
ATOM   1670 C CA  . ILE A 1 215 ? -0.90974  3.70903   55.51722 1.000 17.98883 ? 209 ILE A CA  1 
ATOM   1671 C C   . ILE A 1 215 ? -0.85917  4.97295   56.36629 1.000 14.64843 ? 209 ILE A C   1 
ATOM   1672 O O   . ILE A 1 215 ? -1.79474  5.26673   57.12066 1.000 11.63913 ? 209 ILE A O   1 
ATOM   1673 C CB  . ILE A 1 215 ? -0.17178  2.53801   56.19121 1.000 18.63659 ? 209 ILE A CB  1 
ATOM   1674 C CG1 . ILE A 1 215 ? -0.47997  1.22575   55.46600 1.000 15.43401 ? 209 ILE A CG1 1 
ATOM   1675 C CG2 . ILE A 1 215 ? -0.56090  2.44000   57.65031 1.000 10.25689 ? 209 ILE A CG2 1 
ATOM   1676 C CD1 . ILE A 1 215 ? -1.94451  0.82551   55.51552 1.000 17.54440 ? 209 ILE A CD1 1 
ATOM   1677 N N   . TRP A 1 216 ? 0.22738   5.74385   56.25424 1.000 17.55325 ? 210 TRP A N   1 
ATOM   1678 C CA  . TRP A 1 216 ? 0.30676   7.01086   56.97749 1.000 15.78943 ? 210 TRP A CA  1 
ATOM   1679 C C   . TRP A 1 216 ? -0.83191  7.94032   56.58551 1.000 14.12588 ? 210 TRP A C   1 
ATOM   1680 O O   . TRP A 1 216 ? -1.43691  8.59153   57.44627 1.000 15.08713 ? 210 TRP A O   1 
ATOM   1681 C CB  . TRP A 1 216 ? 1.64642   7.70042   56.71834 1.000 14.59982 ? 210 TRP A CB  1 
ATOM   1682 C CG  . TRP A 1 216 ? 1.74815   9.01704   57.43192 1.000 16.43696 ? 210 TRP A CG  1 
ATOM   1683 C CD1 . TRP A 1 216 ? 1.32982   10.23267  56.97104 1.000 14.26877 ? 210 TRP A CD1 1 
ATOM   1684 C CD2 . TRP A 1 216 ? 2.29928   9.25153   58.73484 1.000 12.47903 ? 210 TRP A CD2 1 
ATOM   1685 N NE1 . TRP A 1 216 ? 1.58159   11.20626  57.90578 1.000 17.50093 ? 210 TRP A NE1 1 
ATOM   1686 C CE2 . TRP A 1 216 ? 2.17881   10.63101  58.99643 1.000 13.63982 ? 210 TRP A CE2 1 
ATOM   1687 C CE3 . TRP A 1 216 ? 2.88398   8.42964   59.70362 1.000 12.95813 ? 210 TRP A CE3 1 
ATOM   1688 C CZ2 . TRP A 1 216 ? 2.61904   11.20711  60.18764 1.000 14.73126 ? 210 TRP A CZ2 1 
ATOM   1689 C CZ3 . TRP A 1 216 ? 3.32141   9.00419   60.88882 1.000 11.82680 ? 210 TRP A CZ3 1 
ATOM   1690 C CH2 . TRP A 1 216 ? 3.18490   10.37876  61.11854 1.000 15.24105 ? 210 TRP A CH2 1 
ATOM   1691 N N   . SER A 1 217 ? -1.12195  8.03271   55.28460 1.000 15.25002 ? 211 SER A N   1 
ATOM   1692 C CA  . SER A 1 217 ? -2.20417  8.89613   54.83024 1.000 14.91856 ? 211 SER A CA  1 
ATOM   1693 C C   . SER A 1 217 ? -3.53342  8.45997   55.43286 1.000 11.88295 ? 211 SER A C   1 
ATOM   1694 O O   . SER A 1 217 ? -4.32836  9.29712   55.87359 1.000 15.38734 ? 211 SER A O   1 
ATOM   1695 C CB  . SER A 1 217 ? -2.27471  8.89075   53.30002 1.000 14.82261 ? 211 SER A CB  1 
ATOM   1696 O OG  . SER A 1 217 ? -1.08439  9.40403   52.72257 1.000 16.35260 ? 211 SER A OG  1 
ATOM   1697 N N   . VAL A 1 218 ? -3.78279  7.14891   55.47353 1.000 10.73351 ? 212 VAL A N   1 
ATOM   1698 C CA  . VAL A 1 218 ? -5.01434  6.64095   56.07139 1.000 8.20387  ? 212 VAL A CA  1 
ATOM   1699 C C   . VAL A 1 218 ? -5.06483  6.98720   57.55310 1.000 14.19560 ? 212 VAL A C   1 
ATOM   1700 O O   . VAL A 1 218 ? -6.11884  7.35613   58.08507 1.000 12.87470 ? 212 VAL A O   1 
ATOM   1701 C CB  . VAL A 1 218 ? -5.13097  5.12429   55.83378 1.000 10.99217 ? 212 VAL A CB  1 
ATOM   1702 C CG1 . VAL A 1 218 ? -6.38097  4.57603   56.49821 1.000 15.96192 ? 212 VAL A CG1 1 
ATOM   1703 C CG2 . VAL A 1 218 ? -5.13195  4.82108   54.33484 1.000 11.26184 ? 212 VAL A CG2 1 
ATOM   1704 N N   . GLY A 1 219 ? -3.92485  6.87986   58.24201 1.000 9.85556  ? 213 GLY A N   1 
ATOM   1705 C CA  . GLY A 1 219 ? -3.86906  7.31582   59.62751 1.000 13.27811 ? 213 GLY A CA  1 
ATOM   1706 C C   . GLY A 1 219 ? -4.24900  8.77421   59.78847 1.000 13.61757 ? 213 GLY A C   1 
ATOM   1707 O O   . GLY A 1 219 ? -5.02064  9.13010   60.68141 1.000 13.34292 ? 213 GLY A O   1 
ATOM   1708 N N   . CYS A 1 220 ? -3.72569  9.63594   58.91184 1.000 11.76057 ? 214 CYS A N   1 
ATOM   1709 C CA  . CYS A 1 220 ? -4.09881  11.04524  58.94413 1.000 12.28817 ? 214 CYS A CA  1 
ATOM   1710 C C   . CYS A 1 220 ? -5.59129  11.23061  58.69338 1.000 12.54366 ? 214 CYS A C   1 
ATOM   1711 O O   . CYS A 1 220 ? -6.21460  12.12726  59.27482 1.000 12.66584 ? 214 CYS A O   1 
ATOM   1712 C CB  . CYS A 1 220 ? -3.28580  11.82436  57.90919 1.000 8.81760  ? 214 CYS A CB  1 
ATOM   1713 S SG  . CYS A 1 220 ? -1.48803  11.90565  58.22208 1.000 13.95361 ? 214 CYS A SG  1 
ATOM   1714 N N   . ILE A 1 221 ? -6.17997  10.39247  57.83935 1.000 13.32248 ? 215 ILE A N   1 
ATOM   1715 C CA  . ILE A 1 221 ? -7.60239  10.51846  57.53347 1.000 9.11835  ? 215 ILE A CA  1 
ATOM   1716 C C   . ILE A 1 221 ? -8.44571  10.07339  58.72163 1.000 9.90849  ? 215 ILE A C   1 
ATOM   1717 O O   . ILE A 1 221 ? -9.45797  10.70433  59.05365 1.000 12.94903 ? 215 ILE A O   1 
ATOM   1718 C CB  . ILE A 1 221 ? -7.93656  9.72321   56.25784 1.000 11.12413 ? 215 ILE A CB  1 
ATOM   1719 C CG1 . ILE A 1 221 ? -7.23883  10.34790  55.04813 1.000 14.05105 ? 215 ILE A CG1 1 
ATOM   1720 C CG2 . ILE A 1 221 ? -9.44674  9.64844   56.03914 1.000 11.63688 ? 215 ILE A CG2 1 
ATOM   1721 C CD1 . ILE A 1 221 ? -7.14216  9.42252   53.85092 1.000 17.26207 ? 215 ILE A CD1 1 
ATOM   1722 N N   . LEU A 1 222 ? -8.03767  8.99154   59.38946 1.000 17.26299 ? 216 LEU A N   1 
ATOM   1723 C CA  . LEU A 1 222 ? -8.74921  8.53898   60.58280 1.000 19.75262 ? 216 LEU A CA  1 
ATOM   1724 C C   . LEU A 1 222 ? -8.75538  9.61518   61.66197 1.000 19.40924 ? 216 LEU A C   1 
ATOM   1725 O O   . LEU A 1 222 ? -9.79497  9.89613   62.27048 1.000 15.82511 ? 216 LEU A O   1 
ATOM   1726 C CB  . LEU A 1 222 ? -8.11680  7.25358   61.12056 1.000 17.08995 ? 216 LEU A CB  1 
ATOM   1727 C CG  . LEU A 1 222 ? -8.64990  6.81434   62.49037 1.000 17.49949 ? 216 LEU A CG  1 
ATOM   1728 C CD1 . LEU A 1 222 ? -10.15537 6.57145   62.43850 1.000 14.08050 ? 216 LEU A CD1 1 
ATOM   1729 C CD2 . LEU A 1 222 ? -7.91320  5.58794   63.01368 1.000 13.80558 ? 216 LEU A CD2 1 
ATOM   1730 N N   . ALA A 1 223 ? -7.59319  10.22064  61.92199 1.000 19.35573 ? 217 ALA A N   1 
ATOM   1731 C CA  . ALA A 1 223 ? -7.52546  11.29720  62.90478 1.000 17.53542 ? 217 ALA A CA  1 
ATOM   1732 C C   . ALA A 1 223 ? -8.43735  12.44990  62.51367 1.000 16.42960 ? 217 ALA A C   1 
ATOM   1733 O O   . ALA A 1 223 ? -9.10995  13.04115  63.36793 1.000 18.19382 ? 217 ALA A O   1 
ATOM   1734 C CB  . ALA A 1 223 ? -6.08282  11.78166  63.05636 1.000 21.35034 ? 217 ALA A CB  1 
ATOM   1735 N N   . GLU A 1 224 ? -8.49208  12.76588  61.21925 1.000 17.48252 ? 218 GLU A N   1 
ATOM   1736 C CA  . GLU A 1 224 ? -9.31406  13.87621  60.76325 1.000 18.09039 ? 218 GLU A CA  1 
ATOM   1737 C C   . GLU A 1 224 ? -10.80047 13.54943  60.86777 1.000 16.76959 ? 218 GLU A C   1 
ATOM   1738 O O   . GLU A 1 224 ? -11.61091 14.45032  61.10457 1.000 17.56847 ? 218 GLU A O   1 
ATOM   1739 C CB  . GLU A 1 224 ? -8.92145  14.24618  59.33232 1.000 21.17413 ? 218 GLU A CB  1 
ATOM   1740 C CG  . GLU A 1 224 ? -9.58974  15.48990  58.77458 1.000 25.80941 ? 218 GLU A CG  1 
ATOM   1741 C CD  . GLU A 1 224 ? -8.84513  16.04003  57.56891 1.000 22.59477 ? 218 GLU A CD  1 
ATOM   1742 O OE1 . GLU A 1 224 ? -7.72900  15.55186  57.28906 1.000 20.81129 ? 218 GLU A OE1 1 
ATOM   1743 O OE2 . GLU A 1 224 ? -9.36667  16.96014  56.90611 1.000 17.30709 ? 218 GLU A OE2 1 
ATOM   1744 N N   . MET A 1 225 ? -11.17860 12.27372  60.71772 1.000 16.52743 ? 219 MET A N   1 
ATOM   1745 C CA  . MET A 1 225 ? -12.57147 11.89671  60.95267 1.000 18.02241 ? 219 MET A CA  1 
ATOM   1746 C C   . MET A 1 225 ? -12.93643 11.98154  62.42915 1.000 24.48604 ? 219 MET A C   1 
ATOM   1747 O O   . MET A 1 225 ? -14.11146 12.17315  62.76600 1.000 21.87425 ? 219 MET A O   1 
ATOM   1748 C CB  . MET A 1 225 ? -12.85530 10.48180  60.43732 1.000 14.72142 ? 219 MET A CB  1 
ATOM   1749 C CG  . MET A 1 225 ? -12.64519 10.26637  58.94461 1.000 18.69025 ? 219 MET A CG  1 
ATOM   1750 S SD  . MET A 1 225 ? -13.34135 8.68746   58.39134 1.000 19.99089 ? 219 MET A SD  1 
ATOM   1751 C CE  . MET A 1 225 ? -11.98231 7.56870   58.72547 1.000 21.72744 ? 219 MET A CE  1 
ATOM   1752 N N   . LEU A 1 226 ? -11.95510 11.83716  63.32298 1.000 15.30292 ? 220 LEU A N   1 
ATOM   1753 C CA  . LEU A 1 226 ? -12.25998 11.85422  64.74965 1.000 20.93194 ? 220 LEU A CA  1 
ATOM   1754 C C   . LEU A 1 226 ? -12.57191 13.25781  65.25258 1.000 26.44803 ? 220 LEU A C   1 
ATOM   1755 O O   . LEU A 1 226 ? -13.29300 13.40911  66.24504 1.000 24.51347 ? 220 LEU A O   1 
ATOM   1756 C CB  . LEU A 1 226 ? -11.09886 11.26048  65.54896 1.000 15.86458 ? 220 LEU A CB  1 
ATOM   1757 C CG  . LEU A 1 226 ? -10.81988 9.76813   65.37283 1.000 21.17141 ? 220 LEU A CG  1 
ATOM   1758 C CD1 . LEU A 1 226 ? -9.45113  9.41174   65.93866 1.000 24.39713 ? 220 LEU A CD1 1 
ATOM   1759 C CD2 . LEU A 1 226 ? -11.91016 8.94129   66.03295 1.000 17.21257 ? 220 LEU A CD2 1 
ATOM   1760 N N   . SER A 1 227 ? -12.05162 14.29195  64.58852 1.000 19.68620 ? 221 SER A N   1 
ATOM   1761 C CA  . SER A 1 227 ? -12.16238 15.65370  65.09291 1.000 25.72324 ? 221 SER A CA  1 
ATOM   1762 C C   . SER A 1 227 ? -12.57041 16.68582  64.04869 1.000 21.02603 ? 221 SER A C   1 
ATOM   1763 O O   . SER A 1 227 ? -12.72967 17.86001  64.40233 1.000 26.83491 ? 221 SER A O   1 
ATOM   1764 C CB  . SER A 1 227 ? -10.83175 16.08826  65.72483 1.000 25.88924 ? 221 SER A CB  1 
ATOM   1765 O OG  . SER A 1 227 ? -9.80947  16.12466  64.74673 1.000 21.45937 ? 221 SER A OG  1 
ATOM   1766 N N   . ASN A 1 228 ? -12.74079 16.29265  62.78570 1.000 18.07986 ? 222 ASN A N   1 
ATOM   1767 C CA  . ASN A 1 228 ? -13.11196 17.19667  61.69308 1.000 18.32156 ? 222 ASN A CA  1 
ATOM   1768 C C   . ASN A 1 228 ? -12.06403 18.27596  61.43698 1.000 28.00735 ? 222 ASN A C   1 
ATOM   1769 O O   . ASN A 1 228 ? -12.39368 19.35001  60.92756 1.000 30.44544 ? 222 ASN A O   1 
ATOM   1770 C CB  . ASN A 1 228 ? -14.47861 17.84977  61.93606 1.000 25.02526 ? 222 ASN A CB  1 
ATOM   1771 C CG  . ASN A 1 228 ? -15.60545 16.84215  61.97675 1.000 27.99221 ? 222 ASN A CG  1 
ATOM   1772 O OD1 . ASN A 1 228 ? -15.79366 16.15006  62.97500 1.000 27.25792 ? 222 ASN A OD1 1 
ATOM   1773 N ND2 . ASN A 1 228 ? -16.36914 16.75910  60.88998 1.000 21.61212 ? 222 ASN A ND2 1 
ATOM   1774 N N   . ARG A 1 229 ? -10.80614 18.01692  61.78223 1.000 21.47068 ? 223 ARG A N   1 
ATOM   1775 C CA  . ARG A 1 229 ? -9.72557  18.93054  61.45429 1.000 21.95727 ? 223 ARG A CA  1 
ATOM   1776 C C   . ARG A 1 229 ? -8.47360  18.12066  61.15742 1.000 21.97988 ? 223 ARG A C   1 
ATOM   1777 O O   . ARG A 1 229 ? -8.28296  17.03756  61.72411 1.000 18.64177 ? 223 ARG A O   1 
ATOM   1778 C CB  . ARG A 1 229 ? -9.45699  19.93759  62.58746 0.800 24.46954 ? 223 ARG A CB  1 
ATOM   1779 C CG  . ARG A 1 229 ? -8.46059  19.50084  63.65019 0.700 32.83329 ? 223 ARG A CG  1 
ATOM   1780 C CD  . ARG A 1 229 ? -8.08697  20.69173  64.53023 0.600 39.32050 ? 223 ARG A CD  1 
ATOM   1781 N NE  . ARG A 1 229 ? -6.67638  20.70824  64.90550 0.600 40.08535 ? 223 ARG A NE  1 
ATOM   1782 C CZ  . ARG A 1 229 ? -5.69478  21.13952  64.12445 0.600 35.74759 ? 223 ARG A CZ  1 
ATOM   1783 N NH1 . ARG A 1 229 ? -5.92733  21.56762  62.89468 0.600 35.21718 ? 223 ARG A NH1 1 
ATOM   1784 N NH2 . ARG A 1 229 ? -4.44915  21.14484  64.59109 0.600 30.39151 ? 223 ARG A NH2 1 
ATOM   1785 N N   . PRO A 1 230 ? -7.62595  18.59803  60.24680 1.000 17.77607 ? 224 PRO A N   1 
ATOM   1786 C CA  . PRO A 1 230 ? -6.39093  17.86696  59.93858 1.000 19.19849 ? 224 PRO A CA  1 
ATOM   1787 C C   . PRO A 1 230 ? -5.48143  17.79805  61.15576 1.000 20.08612 ? 224 PRO A C   1 
ATOM   1788 O O   . PRO A 1 230 ? -5.29921  18.78161  61.87511 1.000 21.27260 ? 224 PRO A O   1 
ATOM   1789 C CB  . PRO A 1 230 ? -5.76077  18.68925  58.80671 1.000 23.05918 ? 224 PRO A CB  1 
ATOM   1790 C CG  . PRO A 1 230 ? -6.39448  20.04152  58.90905 1.000 26.97868 ? 224 PRO A CG  1 
ATOM   1791 C CD  . PRO A 1 230 ? -7.78928  19.78860  59.39768 1.000 23.41326 ? 224 PRO A CD  1 
ATOM   1792 N N   . ILE A 1 231 ? -4.90595  16.61754  61.37978 1.000 14.82589 ? 225 ILE A N   1 
ATOM   1793 C CA  . ILE A 1 231 ? -4.09961  16.41643  62.57726 1.000 17.58775 ? 225 ILE A CA  1 
ATOM   1794 C C   . ILE A 1 231 ? -2.72093  17.06338  62.42286 1.000 18.57937 ? 225 ILE A C   1 
ATOM   1795 O O   . ILE A 1 231 ? -2.15275  17.55956  63.40389 1.000 19.77145 ? 225 ILE A O   1 
ATOM   1796 C CB  A ILE A 1 231 ? -3.99505  14.91480  62.89907 0.440 20.51411 ? 225 ILE A CB  1 
ATOM   1797 C CB  B ILE A 1 231 ? -3.99751  14.91333  62.89922 0.560 20.52958 ? 225 ILE A CB  1 
ATOM   1798 C CG1 A ILE A 1 231 ? -3.12240  14.68345  64.13478 0.440 18.55286 ? 225 ILE A CG1 1 
ATOM   1799 C CG1 B ILE A 1 231 ? -3.13974  14.67785  64.14627 0.560 18.52723 ? 225 ILE A CG1 1 
ATOM   1800 C CG2 A ILE A 1 231 ? -3.46028  14.13863  61.70107 0.440 16.86972 ? 225 ILE A CG2 1 
ATOM   1801 C CG2 B ILE A 1 231 ? -3.44760  14.13743  61.70722 0.560 16.59644 ? 225 ILE A CG2 1 
ATOM   1802 C CD1 A ILE A 1 231 ? -2.99137  13.23212  64.51445 0.440 18.28627 ? 225 ILE A CD1 1 
ATOM   1803 C CD1 B ILE A 1 231 ? -3.82538  15.06489  65.43868 0.560 19.29215 ? 225 ILE A CD1 1 
ATOM   1804 N N   . PHE A 1 232 ? -2.17889  17.11006  61.20577 1.000 17.38844 ? 226 PHE A N   1 
ATOM   1805 C CA  . PHE A 1 232 ? -0.86261  17.69336  60.93670 1.000 17.70397 ? 226 PHE A CA  1 
ATOM   1806 C C   . PHE A 1 232 ? -0.99789  18.77626  59.87014 1.000 20.75015 ? 226 PHE A C   1 
ATOM   1807 O O   . PHE A 1 232 ? -0.58995  18.58565  58.71812 1.000 21.06119 ? 226 PHE A O   1 
ATOM   1808 C CB  . PHE A 1 232 ? 0.13294   16.62371  60.48457 1.000 16.89773 ? 226 PHE A CB  1 
ATOM   1809 C CG  . PHE A 1 232 ? 0.25530   15.45654  61.42244 1.000 17.82077 ? 226 PHE A CG  1 
ATOM   1810 C CD1 . PHE A 1 232 ? 0.58434   15.64376  62.75795 1.000 15.55044 ? 226 PHE A CD1 1 
ATOM   1811 C CD2 . PHE A 1 232 ? 0.06710   14.16448  60.95921 1.000 15.27197 ? 226 PHE A CD2 1 
ATOM   1812 C CE1 . PHE A 1 232 ? 0.70277   14.56423  63.61437 1.000 19.35803 ? 226 PHE A CE1 1 
ATOM   1813 C CE2 . PHE A 1 232 ? 0.18584   13.07989  61.80970 1.000 17.50396 ? 226 PHE A CE2 1 
ATOM   1814 C CZ  . PHE A 1 232 ? 0.50505   13.27923  63.13971 1.000 16.74565 ? 226 PHE A CZ  1 
ATOM   1815 N N   . PRO A 1 233 ? -1.55893  19.93704  60.22214 1.000 22.89799 ? 227 PRO A N   1 
ATOM   1816 C CA  . PRO A 1 233 ? -1.80522  20.97548  59.19793 1.000 25.46968 ? 227 PRO A CA  1 
ATOM   1817 C C   . PRO A 1 233 ? -0.57729  21.83333  58.91312 1.000 22.27262 ? 227 PRO A C   1 
ATOM   1818 O O   . PRO A 1 233 ? -0.51785  23.03003  59.21764 1.000 25.16245 ? 227 PRO A O   1 
ATOM   1819 C CB  . PRO A 1 233 ? -2.94941  21.77733  59.82373 1.000 31.32962 ? 227 PRO A CB  1 
ATOM   1820 C CG  . PRO A 1 233 ? -2.63270  21.73164  61.29247 1.000 25.01287 ? 227 PRO A CG  1 
ATOM   1821 C CD  . PRO A 1 233 ? -2.04726  20.35427  61.54976 1.000 25.27413 ? 227 PRO A CD  1 
ATOM   1822 N N   . GLY A 1 234 ? 0.43279   21.21573  58.30612 1.000 23.38830 ? 228 GLY A N   1 
ATOM   1823 C CA  . GLY A 1 234 ? 1.62429   21.96164  57.93984 1.000 23.09368 ? 228 GLY A CA  1 
ATOM   1824 C C   . GLY A 1 234 ? 1.28991   23.08285  56.97197 1.000 34.37970 ? 228 GLY A C   1 
ATOM   1825 O O   . GLY A 1 234 ? 0.50168   22.91554  56.03806 1.000 27.17106 ? 228 GLY A O   1 
ATOM   1826 N N   . LYS A 1 235 ? 1.88941   24.24122  57.20932 1.000 27.50932 ? 229 LYS A N   1 
ATOM   1827 C CA  . LYS A 1 235 ? 1.55910   25.44490  56.46402 1.000 36.40882 ? 229 LYS A CA  1 
ATOM   1828 C C   . LYS A 1 235 ? 2.48192   25.66550  55.27003 1.000 33.82510 ? 229 LYS A C   1 
ATOM   1829 O O   . LYS A 1 235 ? 2.25062   26.59181  54.48496 1.000 33.30771 ? 229 LYS A O   1 
ATOM   1830 C CB  . LYS A 1 235 ? 1.55623   26.63254  57.43612 1.000 31.68956 ? 229 LYS A CB  1 
ATOM   1831 C CG  . LYS A 1 235 ? 0.14863   26.87473  57.99020 0.800 39.13576 ? 229 LYS A CG  1 
ATOM   1832 C CD  . LYS A 1 235 ? 0.07852   27.62903  59.31927 0.600 40.60364 ? 229 LYS A CD  1 
ATOM   1833 C CE  . LYS A 1 235 ? 0.39104   29.09637  59.21680 0.600 42.82696 ? 229 LYS A CE  1 
ATOM   1834 N NZ  . LYS A 1 235 ? 1.84348   29.28539  59.34815 0.600 40.92574 ? 229 LYS A NZ  1 
ATOM   1835 N N   . HIS A 1 236 ? 3.48813   24.80910  55.10431 0.800 28.18101 ? 230 HIS A N   1 
ATOM   1836 C CA  . HIS A 1 236 ? 4.36550   24.75573  53.93939 0.800 31.85500 ? 230 HIS A CA  1 
ATOM   1837 C C   . HIS A 1 236 ? 5.20817   23.49358  54.07376 0.800 26.27832 ? 230 HIS A C   1 
ATOM   1838 O O   . HIS A 1 236 ? 5.18424   22.82875  55.11265 0.800 31.46346 ? 230 HIS A O   1 
ATOM   1839 C CB  . HIS A 1 236 ? 5.23938   26.00465  53.81803 0.800 35.77648 ? 230 HIS A CB  1 
ATOM   1840 C CG  . HIS A 1 236 ? 5.94637   26.37010  55.08336 0.800 28.79061 ? 230 HIS A CG  1 
ATOM   1841 N ND1 . HIS A 1 236 ? 7.11461   25.76119  55.48806 0.800 22.00770 ? 230 HIS A ND1 1 
ATOM   1842 C CD2 . HIS A 1 236 ? 5.65006   27.28740  56.03391 0.800 22.08978 ? 230 HIS A CD2 1 
ATOM   1843 C CE1 . HIS A 1 236 ? 7.50544   26.28502  56.63634 0.800 25.93845 ? 230 HIS A CE1 1 
ATOM   1844 N NE2 . HIS A 1 236 ? 6.63404   27.21332  56.98918 0.800 22.39908 ? 230 HIS A NE2 1 
ATOM   1845 N N   . TYR A 1 237 ? 5.94068   23.16154  53.00063 0.800 30.70287 ? 231 TYR A N   1 
ATOM   1846 C CA  . TYR A 1 237 ? 6.70613   21.91295  52.93933 0.800 32.52116 ? 231 TYR A CA  1 
ATOM   1847 C C   . TYR A 1 237 ? 7.49047   21.63545  54.21163 0.800 27.77841 ? 231 TYR A C   1 
ATOM   1848 O O   . TYR A 1 237 ? 7.46366   20.52305  54.75135 0.800 27.92871 ? 231 TYR A O   1 
ATOM   1849 C CB  . TYR A 1 237 ? 7.67479   21.93991  51.75250 0.800 35.30903 ? 231 TYR A CB  1 
ATOM   1850 C CG  . TYR A 1 237 ? 8.50261   20.67386  51.61506 0.800 35.31339 ? 231 TYR A CG  1 
ATOM   1851 C CD1 . TYR A 1 237 ? 8.01042   19.56268  50.93862 0.800 35.44699 ? 231 TYR A CD1 1 
ATOM   1852 C CD2 . TYR A 1 237 ? 9.77699   20.59146  52.16369 0.800 32.72209 ? 231 TYR A CD2 1 
ATOM   1853 C CE1 . TYR A 1 237 ? 8.76450   18.40497  50.81651 0.800 27.22352 ? 231 TYR A CE1 1 
ATOM   1854 C CE2 . TYR A 1 237 ? 10.53518  19.44021  52.04755 0.800 34.30979 ? 231 TYR A CE2 1 
ATOM   1855 C CZ  . TYR A 1 237 ? 10.02598  18.35129  51.37268 0.800 34.56181 ? 231 TYR A CZ  1 
ATOM   1856 O OH  . TYR A 1 237 ? 10.78337  17.20652  51.25693 0.800 32.44726 ? 231 TYR A OH  1 
ATOM   1857 N N   . LEU A 1 238 ? 8.21168   22.64321  54.69071 0.800 36.74546 ? 232 LEU A N   1 
ATOM   1858 C CA  . LEU A 1 238 ? 9.11644   22.45683  55.81406 1.000 32.89252 ? 232 LEU A CA  1 
ATOM   1859 C C   . LEU A 1 238 ? 8.36055   22.35838  57.13135 0.800 19.87811 ? 232 LEU A C   1 
ATOM   1860 O O   . LEU A 1 238 ? 8.81162   21.67045  58.05331 0.800 28.68379 ? 232 LEU A O   1 
ATOM   1861 C CB  . LEU A 1 238 ? 10.11474  23.61313  55.84120 1.000 34.42796 ? 232 LEU A CB  1 
ATOM   1862 C CG  . LEU A 1 238 ? 10.78693  23.81167  54.47717 1.000 25.28325 ? 232 LEU A CG  1 
ATOM   1863 C CD1 . LEU A 1 238 ? 11.11993  25.27848  54.23556 1.000 32.98242 ? 232 LEU A CD1 1 
ATOM   1864 C CD2 . LEU A 1 238 ? 12.02979  22.94150  54.32600 1.000 35.28963 ? 232 LEU A CD2 1 
ATOM   1865 N N   . ASP A 1 239 ? 7.19938   23.01051  57.21925 1.000 31.85512 ? 233 ASP A N   1 
ATOM   1866 C CA  . ASP A 1 239 ? 6.41817   23.01144  58.45075 1.000 23.82669 ? 233 ASP A CA  1 
ATOM   1867 C C   . ASP A 1 239 ? 5.81971   21.64109  58.75531 1.000 25.31074 ? 233 ASP A C   1 
ATOM   1868 O O   . ASP A 1 239 ? 5.52270   21.34824  59.91803 1.000 23.87710 ? 233 ASP A O   1 
ATOM   1869 C CB  . ASP A 1 239 ? 5.31062   24.06375  58.34977 1.000 26.89364 ? 233 ASP A CB  1 
ATOM   1870 C CG  . ASP A 1 239 ? 4.71175   24.41815  59.69472 1.000 28.91325 ? 233 ASP A CG  1 
ATOM   1871 O OD1 . ASP A 1 239 ? 5.47582   24.57671  60.66763 1.000 26.92114 ? 233 ASP A OD1 1 
ATOM   1872 O OD2 . ASP A 1 239 ? 3.47258   24.54579  59.77539 1.000 27.10990 ? 233 ASP A OD2 1 
ATOM   1873 N N   . GLN A 1 240 ? 5.63128   20.79583  57.73647 1.000 21.67242 ? 234 GLN A N   1 
ATOM   1874 C CA  . GLN A 1 240 ? 4.91294   19.53708  57.93313 1.000 20.93866 ? 234 GLN A CA  1 
ATOM   1875 C C   . GLN A 1 240 ? 5.57240   18.67227  59.00222 1.000 28.10900 ? 234 GLN A C   1 
ATOM   1876 O O   . GLN A 1 240 ? 4.90204   18.18139  59.91826 1.000 21.21581 ? 234 GLN A O   1 
ATOM   1877 C CB  . GLN A 1 240 ? 4.80768   18.77344  56.61005 1.000 20.70845 ? 234 GLN A CB  1 
ATOM   1878 C CG  . GLN A 1 240 ? 3.84467   17.58522  56.66116 1.000 21.79863 ? 234 GLN A CG  1 
ATOM   1879 C CD  . GLN A 1 240 ? 2.42769   17.97404  57.06204 1.000 15.46081 ? 234 GLN A CD  1 
ATOM   1880 O OE1 . GLN A 1 240 ? 1.99682   19.10889  56.85983 1.000 21.14826 ? 234 GLN A OE1 1 
ATOM   1881 N NE2 . GLN A 1 240 ? 1.70375   17.03103  57.65100 1.000 18.51467 ? 234 GLN A NE2 1 
ATOM   1882 N N   . LEU A 1 241 ? 6.89005   18.47713  58.90642 1.000 23.81691 ? 235 LEU A N   1 
ATOM   1883 C CA  . LEU A 1 241 ? 7.57990   17.63496  59.88106 0.850 20.62333 ? 235 LEU A CA  1 
ATOM   1884 C C   . LEU A 1 241 ? 7.48468   18.21161  61.29050 1.000 17.95458 ? 235 LEU A C   1 
ATOM   1885 O O   . LEU A 1 241 ? 7.43960   17.45247  62.26685 1.000 20.30250 ? 235 LEU A O   1 
ATOM   1886 C CB  . LEU A 1 241 ? 9.03987   17.44485  59.46297 1.000 19.98800 ? 235 LEU A CB  1 
ATOM   1887 C CG  . LEU A 1 241 ? 9.91815   16.44825  60.22703 1.000 26.32326 ? 235 LEU A CG  1 
ATOM   1888 C CD1 . LEU A 1 241 ? 9.36937   15.02740  60.14656 1.000 20.82267 ? 235 LEU A CD1 1 
ATOM   1889 C CD2 . LEU A 1 241 ? 11.33881  16.49735  59.68706 1.000 27.67197 ? 235 LEU A CD2 1 
ATOM   1890 N N   . ASN A 1 242 ? 7.43354   19.54223  61.41738 1.000 22.38664 ? 236 ASN A N   1 
ATOM   1891 C CA  . ASN A 1 242 ? 7.23150   20.16504  62.72517 1.000 25.94323 ? 236 ASN A CA  1 
ATOM   1892 C C   . ASN A 1 242 ? 5.96385   19.64349  63.39203 1.000 21.96815 ? 236 ASN A C   1 
ATOM   1893 O O   . ASN A 1 242 ? 5.96065   19.30989  64.58301 1.000 21.56560 ? 236 ASN A O   1 
ATOM   1894 C CB  . ASN A 1 242 ? 7.15387   21.69069  62.58754 0.800 17.87087 ? 236 ASN A CB  1 
ATOM   1895 C CG  . ASN A 1 242 ? 8.45969   22.31279  62.13210 0.700 30.42875 ? 236 ASN A CG  1 
ATOM   1896 O OD1 . ASN A 1 242 ? 9.53305   21.74822  62.33183 0.700 23.19057 ? 236 ASN A OD1 1 
ATOM   1897 N ND2 . ASN A 1 242 ? 8.37223   23.49355  61.52332 0.700 16.53044 ? 236 ASN A ND2 1 
ATOM   1898 N N   . HIS A 1 243 ? 4.87042   19.57030  62.63122 1.000 17.60379 ? 237 HIS A N   1 
ATOM   1899 C CA  . HIS A 1 243 ? 3.59235   19.16787  63.20849 1.000 17.48622 ? 237 HIS A CA  1 
ATOM   1900 C C   . HIS A 1 243 ? 3.59620   17.69710  63.60123 1.000 15.68327 ? 237 HIS A C   1 
ATOM   1901 O O   . HIS A 1 243 ? 3.04818   17.32741  64.64723 1.000 19.82560 ? 237 HIS A O   1 
ATOM   1902 C CB  . HIS A 1 243 ? 2.46221   19.45890  62.22121 1.000 15.70499 ? 237 HIS A CB  1 
ATOM   1903 C CG  . HIS A 1 243 ? 2.15542   20.91542  62.07382 1.000 19.18464 ? 237 HIS A CG  1 
ATOM   1904 N ND1 . HIS A 1 243 ? 1.03438   21.49792  62.62314 1.000 28.82292 ? 237 HIS A ND1 1 
ATOM   1905 C CD2 . HIS A 1 243 ? 2.82936   21.91028  61.44950 1.000 24.35013 ? 237 HIS A CD2 1 
ATOM   1906 C CE1 . HIS A 1 243 ? 1.02806   22.78816  62.33986 1.000 36.23004 ? 237 HIS A CE1 1 
ATOM   1907 N NE2 . HIS A 1 243 ? 2.10711   23.06430  61.62962 1.000 23.27462 ? 237 HIS A NE2 1 
ATOM   1908 N N   . ILE A 1 244 ? 4.21223   16.84520  62.78057 1.000 11.92042 ? 238 ILE A N   1 
ATOM   1909 C CA  . ILE A 1 244 ? 4.23034   15.41414  63.07034 1.000 15.08835 ? 238 ILE A CA  1 
ATOM   1910 C C   . ILE A 1 244 ? 5.01129   15.14229  64.34925 1.000 19.12195 ? 238 ILE A C   1 
ATOM   1911 O O   . ILE A 1 244 ? 4.54098   14.43627  65.24989 1.000 16.80081 ? 238 ILE A O   1 
ATOM   1912 C CB  . ILE A 1 244 ? 4.80624   14.63579  61.87420 1.000 14.10336 ? 238 ILE A CB  1 
ATOM   1913 C CG1 . ILE A 1 244 ? 3.85153   14.73296  60.67775 1.000 18.70216 ? 238 ILE A CG1 1 
ATOM   1914 C CG2 . ILE A 1 244 ? 5.06372   13.18462  62.25045 1.000 13.24313 ? 238 ILE A CG2 1 
ATOM   1915 C CD1 . ILE A 1 244 ? 4.46187   14.27214  59.36882 1.000 18.81393 ? 238 ILE A CD1 1 
ATOM   1916 N N   . LEU A 1 245 ? 6.21789   15.70268  64.44958 1.000 17.64476 ? 239 LEU A N   1 
ATOM   1917 C CA  . LEU A 1 245 ? 7.01954   15.50322  65.65133 1.000 22.90759 ? 239 LEU A CA  1 
ATOM   1918 C C   . LEU A 1 245 ? 6.40503   16.19674  66.86014 1.000 19.17494 ? 239 LEU A C   1 
ATOM   1919 O O   . LEU A 1 245 ? 6.60768   15.75299  67.99637 1.000 18.32417 ? 239 LEU A O   1 
ATOM   1920 C CB  . LEU A 1 245 ? 8.44363   16.00071  65.41486 1.000 15.67406 ? 239 LEU A CB  1 
ATOM   1921 C CG  . LEU A 1 245 ? 9.17083   15.29347  64.27058 1.000 27.69818 ? 239 LEU A CG  1 
ATOM   1922 C CD1 . LEU A 1 245 ? 10.53408  15.91906  64.02294 1.000 22.76062 ? 239 LEU A CD1 1 
ATOM   1923 C CD2 . LEU A 1 245 ? 9.29850   13.80582  64.56596 1.000 20.33073 ? 239 LEU A CD2 1 
ATOM   1924 N N   . GLY A 1 246 ? 5.65379   17.27734  66.64008 1.000 15.42159 ? 240 GLY A N   1 
ATOM   1925 C CA  . GLY A 1 246 ? 4.98242   17.95175  67.73742 1.000 18.17657 ? 240 GLY A CA  1 
ATOM   1926 C C   . GLY A 1 246 ? 3.96757   17.08908  68.45841 1.000 25.06565 ? 240 GLY A C   1 
ATOM   1927 O O   . GLY A 1 246 ? 3.63324   17.37384  69.61405 1.000 20.24285 ? 240 GLY A O   1 
ATOM   1928 N N   . ILE A 1 247 ? 3.47721   16.03541  67.81058 1.000 21.82342 ? 241 ILE A N   1 
ATOM   1929 C CA  . ILE A 1 247 ? 2.49780   15.12863  68.39470 1.000 14.92643 ? 241 ILE A CA  1 
ATOM   1930 C C   . ILE A 1 247 ? 3.11425   13.76811  68.70842 1.000 16.44512 ? 241 ILE A C   1 
ATOM   1931 O O   . ILE A 1 247 ? 2.92105   13.22700  69.79788 1.000 17.93224 ? 241 ILE A O   1 
ATOM   1932 C CB  . ILE A 1 247 ? 1.26246   14.98374  67.47593 1.000 14.30353 ? 241 ILE A CB  1 
ATOM   1933 C CG1 . ILE A 1 247 ? 0.33016   16.18511  67.65674 1.000 22.92829 ? 241 ILE A CG1 1 
ATOM   1934 C CG2 . ILE A 1 247 ? 0.53176   13.67345  67.75216 1.000 14.55975 ? 241 ILE A CG2 1 
ATOM   1935 C CD1 . ILE A 1 247 ? -0.55173  16.46427  66.45883 1.000 24.39265 ? 241 ILE A CD1 1 
ATOM   1936 N N   . LEU A 1 248 ? 3.86356   13.19749  67.76031 1.000 15.15006 ? 242 LEU A N   1 
ATOM   1937 C CA  . LEU A 1 248 ? 4.48888   11.90048  68.00305 1.000 20.83877 ? 242 LEU A CA  1 
ATOM   1938 C C   . LEU A 1 248 ? 5.61177   11.98205  69.02842 1.000 22.71477 ? 242 LEU A C   1 
ATOM   1939 O O   . LEU A 1 248 ? 5.93222   10.96970  69.66196 1.000 17.94044 ? 242 LEU A O   1 
ATOM   1940 C CB  A LEU A 1 248 ? 5.03442   11.31131  66.69766 0.500 18.33965 ? 242 LEU A CB  1 
ATOM   1941 C CB  B LEU A 1 248 ? 5.03572   11.31699  66.69917 0.500 18.33987 ? 242 LEU A CB  1 
ATOM   1942 C CG  A LEU A 1 248 ? 4.09927   10.57238  65.73164 0.500 15.43210 ? 242 LEU A CG  1 
ATOM   1943 C CG  B LEU A 1 248 ? 4.05426   10.68168  65.71331 0.500 15.46717 ? 242 LEU A CG  1 
ATOM   1944 C CD1 A LEU A 1 248 ? 2.83968   11.37076  65.40182 0.500 17.04522 ? 242 LEU A CD1 1 
ATOM   1945 C CD1 B LEU A 1 248 ? 4.74015   9.55422   64.95608 0.500 14.79576 ? 242 LEU A CD1 1 
ATOM   1946 C CD2 A LEU A 1 248 ? 4.84547   10.19241  64.45749 0.500 13.19498 ? 242 LEU A CD2 1 
ATOM   1947 C CD2 B LEU A 1 248 ? 2.79689   10.18076  66.41681 0.500 17.97802 ? 242 LEU A CD2 1 
ATOM   1948 N N   . GLY A 1 249 ? 6.21680   13.15081  69.20131 1.000 19.85848 ? 243 GLY A N   1 
ATOM   1949 C CA  . GLY A 1 249 ? 7.37845   13.27229  70.05474 1.000 18.15408 ? 243 GLY A CA  1 
ATOM   1950 C C   . GLY A 1 249 ? 8.65025   12.92156  69.30894 1.000 24.49751 ? 243 GLY A C   1 
ATOM   1951 O O   . GLY A 1 249 ? 8.64427   12.53548  68.13774 1.000 16.68455 ? 243 GLY A O   1 
ATOM   1952 N N   . SER A 1 250 ? 9.76760   13.06152  70.01483 1.000 18.04154 ? 244 SER A N   1 
ATOM   1953 C CA  . SER A 1 250 ? 11.06512  12.80274  69.41094 1.000 14.17295 ? 244 SER A CA  1 
ATOM   1954 C C   . SER A 1 250 ? 11.19071  11.32521  69.04817 1.000 18.57281 ? 244 SER A C   1 
ATOM   1955 O O   . SER A 1 250 ? 10.73984  10.45877  69.80691 1.000 17.19546 ? 244 SER A O   1 
ATOM   1956 C CB  . SER A 1 250 ? 12.18921  13.20328  70.37010 1.000 13.90577 ? 244 SER A CB  1 
ATOM   1957 O OG  . SER A 1 250 ? 12.08177  14.56746  70.73400 1.000 21.51058 ? 244 SER A OG  1 
ATOM   1958 N N   . PRO A 1 251 ? 11.77894  11.00136  67.89773 1.000 20.87069 ? 245 PRO A N   1 
ATOM   1959 C CA  . PRO A 1 251 ? 11.99888  9.59011   67.56004 1.000 20.15868 ? 245 PRO A CA  1 
ATOM   1960 C C   . PRO A 1 251 ? 12.94984  8.92381   68.54280 1.000 21.28732 ? 245 PRO A C   1 
ATOM   1961 O O   . PRO A 1 251 ? 13.85842  9.55295   69.09103 1.000 19.33824 ? 245 PRO A O   1 
ATOM   1962 C CB  . PRO A 1 251 ? 12.60825  9.64092   66.15322 1.000 16.29319 ? 245 PRO A CB  1 
ATOM   1963 C CG  . PRO A 1 251 ? 12.35010  11.00843  65.63738 1.000 26.77946 ? 245 PRO A CG  1 
ATOM   1964 C CD  . PRO A 1 251 ? 12.10412  11.91809  66.79045 1.000 17.23857 ? 245 PRO A CD  1 
ATOM   1965 N N   . SER A 1 252 ? 12.73619  7.62699   68.75074 1.000 15.62429 ? 246 SER A N   1 
ATOM   1966 C CA  . SER A 1 252 ? 13.61739  6.85041   69.60541 1.000 24.21255 ? 246 SER A CA  1 
ATOM   1967 C C   . SER A 1 252 ? 14.98794  6.69271   68.94924 1.000 27.15974 ? 246 SER A C   1 
ATOM   1968 O O   . SER A 1 252 ? 15.17853  6.96964   67.76050 1.000 19.57593 ? 246 SER A O   1 
ATOM   1969 C CB  . SER A 1 252 ? 13.01233  5.47699   69.89336 1.000 25.04611 ? 246 SER A CB  1 
ATOM   1970 O OG  . SER A 1 252 ? 12.94288  4.69679   68.71095 1.000 20.01987 ? 246 SER A OG  1 
ATOM   1971 N N   . GLN A 1 253 ? 15.95691  6.24156   69.74979 1.000 25.16712 ? 247 GLN A N   1 
ATOM   1972 C CA  . GLN A 1 253 ? 17.28231  5.95476   69.21051 1.000 25.28613 ? 247 GLN A CA  1 
ATOM   1973 C C   . GLN A 1 253 ? 17.21750  4.86054   68.15390 1.000 25.01201 ? 247 GLN A C   1 
ATOM   1974 O O   . GLN A 1 253 ? 17.90214  4.93498   67.12638 1.000 20.66953 ? 247 GLN A O   1 
ATOM   1975 C CB  . GLN A 1 253 ? 18.23321  5.54755   70.33675 1.000 25.86238 ? 247 GLN A CB  1 
ATOM   1976 C CG  . GLN A 1 253 ? 19.63629  5.21011   69.86402 1.000 31.94666 ? 247 GLN A CG  1 
ATOM   1977 C CD  A GLN A 1 253 ? 20.59981  4.98090   71.01231 0.600 34.00097 ? 247 GLN A CD  1 
ATOM   1978 C CD  B GLN A 1 253 ? 20.33161  6.39548   69.22142 0.400 26.04063 ? 247 GLN A CD  1 
ATOM   1979 O OE1 A GLN A 1 253 ? 20.32476  4.19959   71.92429 0.600 36.90694 ? 247 GLN A OE1 1 
ATOM   1980 O OE1 B GLN A 1 253 ? 20.48463  6.45473   68.00204 0.400 29.73250 ? 247 GLN A OE1 1 
ATOM   1981 N NE2 A GLN A 1 253 ? 21.73976  5.65844   70.97031 0.600 32.41530 ? 247 GLN A NE2 1 
ATOM   1982 N NE2 B GLN A 1 253 ? 20.75484  7.34887   70.04271 0.400 24.73438 ? 247 GLN A NE2 1 
ATOM   1983 N N   . GLU A 1 254 ? 16.39524  3.83613   68.39133 1.000 20.40173 ? 248 GLU A N   1 
ATOM   1984 C CA  . GLU A 1 254 ? 16.27570  2.73847   67.43810 1.000 22.24055 ? 248 GLU A CA  1 
ATOM   1985 C C   . GLU A 1 254 ? 15.72875  3.22240   66.10164 1.000 27.99372 ? 248 GLU A C   1 
ATOM   1986 O O   . GLU A 1 254 ? 16.21550  2.81584   65.04018 1.000 25.34382 ? 248 GLU A O   1 
ATOM   1987 C CB  . GLU A 1 254 ? 15.38367  1.63980   68.01465 1.000 32.44256 ? 248 GLU A CB  1 
ATOM   1988 C CG  A GLU A 1 254 ? 15.31265  0.38790   67.15454 0.500 35.31120 ? 248 GLU A CG  1 
ATOM   1989 C CG  B GLU A 1 254 ? 15.19231  0.44499   67.09496 0.500 35.27374 ? 248 GLU A CG  1 
ATOM   1990 C CD  A GLU A 1 254 ? 14.67247  -0.78189  67.87633 0.500 37.92987 ? 248 GLU A CD  1 
ATOM   1991 C CD  B GLU A 1 254 ? 14.05304  -0.45346  67.53671 0.500 40.24822 ? 248 GLU A CD  1 
ATOM   1992 O OE1 A GLU A 1 254 ? 15.39765  -1.52314  68.56995 0.500 29.25820 ? 248 GLU A OE1 1 
ATOM   1993 O OE1 B GLU A 1 254 ? 13.21896  -0.00212  68.35056 0.500 43.73275 ? 248 GLU A OE1 1 
ATOM   1994 O OE2 A GLU A 1 254 ? 13.44272  -0.96152  67.74738 0.500 42.56987 ? 248 GLU A OE2 1 
ATOM   1995 O OE2 B GLU A 1 254 ? 13.98779  -1.60874  67.06605 0.500 39.34823 ? 248 GLU A OE2 1 
ATOM   1996 N N   . ASP A 1 255 ? 14.71795  4.09398   66.13186 1.000 22.23835 ? 249 ASP A N   1 
ATOM   1997 C CA  . ASP A 1 255 ? 14.16430  4.61439   64.88788 1.000 24.57943 ? 249 ASP A CA  1 
ATOM   1998 C C   . ASP A 1 255 ? 15.13181  5.56369   64.19263 1.000 26.93763 ? 249 ASP A C   1 
ATOM   1999 O O   . ASP A 1 255 ? 15.14236  5.63709   62.95822 1.000 22.83194 ? 249 ASP A O   1 
ATOM   2000 C CB  . ASP A 1 255 ? 12.82654  5.30563   65.15650 1.000 14.31849 ? 249 ASP A CB  1 
ATOM   2001 C CG  . ASP A 1 255 ? 11.73946  4.32721   65.55324 0.800 15.84769 ? 249 ASP A CG  1 
ATOM   2002 O OD1 . ASP A 1 255 ? 11.96474  3.10666   65.41727 0.800 16.19709 ? 249 ASP A OD1 1 
ATOM   2003 O OD2 . ASP A 1 255 ? 10.66178  4.77542   65.99944 0.800 17.43521 ? 249 ASP A OD2 1 
ATOM   2004 N N   . LEU A 1 256 ? 15.94885  6.29374   64.95541 1.000 18.90120 ? 250 LEU A N   1 
ATOM   2005 C CA  . LEU A 1 256 ? 16.95571  7.14822   64.33232 1.000 26.80580 ? 250 LEU A CA  1 
ATOM   2006 C C   . LEU A 1 256 ? 18.04098  6.32190   63.65524 1.000 26.25124 ? 250 LEU A C   1 
ATOM   2007 O O   . LEU A 1 256 ? 18.48481  6.65826   62.55085 1.000 26.48955 ? 250 LEU A O   1 
ATOM   2008 C CB  . LEU A 1 256 ? 17.56977  8.09128   65.36578 1.000 27.31847 ? 250 LEU A CB  1 
ATOM   2009 C CG  . LEU A 1 256 ? 16.68535  9.27454   65.75487 1.000 34.58087 ? 250 LEU A CG  1 
ATOM   2010 C CD1 . LEU A 1 256 ? 17.38776  10.15488  66.75851 1.000 29.55328 ? 250 LEU A CD1 1 
ATOM   2011 C CD2 . LEU A 1 256 ? 16.30572  10.07277  64.52162 1.000 25.03520 ? 250 LEU A CD2 1 
ATOM   2012 N N   . ASN A 1 257 ? 18.47319  5.23796   64.29378 1.000 25.63079 ? 251 ASN A N   1 
ATOM   2013 C CA  . ASN A 1 257 ? 19.49856  4.36409   63.72971 1.000 30.98241 ? 251 ASN A CA  1 
ATOM   2014 C C   . ASN A 1 257 ? 19.04925  3.74983   62.40622 1.000 35.57889 ? 251 ASN A C   1 
ATOM   2015 O O   . ASN A 1 257 ? 19.87683  3.35382   61.58345 1.000 33.73019 ? 251 ASN A O   1 
ATOM   2016 C CB  . ASN A 1 257 ? 19.86543  3.25856   64.72228 1.000 28.51653 ? 251 ASN A CB  1 
ATOM   2017 C CG  . ASN A 1 257 ? 20.60431  3.78768   65.93586 0.900 41.62205 ? 251 ASN A CG  1 
ATOM   2018 O OD1 . ASN A 1 257 ? 21.26100  4.82630   65.87075 0.900 36.63934 ? 251 ASN A OD1 1 
ATOM   2019 N ND2 . ASN A 1 257 ? 20.50258  3.07267   67.05193 0.900 30.87724 ? 251 ASN A ND2 1 
HETATM 2020 N N   . CME A 1 258 ? 17.73741  3.67442   62.20573 1.000 31.35876 ? 252 CME A N   1 
HETATM 2021 C CA  . CME A 1 258 ? 17.18741  3.15070   60.97349 1.000 34.62972 ? 252 CME A CA  1 
HETATM 2022 C CB  . CME A 1 258 ? 15.65175  2.76553   61.15257 1.000 31.81716 ? 252 CME A CB  1 
HETATM 2023 S SG  . CME A 1 258 ? 15.45184  1.19263   62.05843 0.700 30.22410 ? 252 CME A SG  1 
HETATM 2024 S SD  . CME A 1 258 ? 16.81428  -0.07565  61.16704 0.700 57.38710 ? 252 CME A SD  1 
HETATM 2025 C CE  . CME A 1 258 ? 15.84267  -1.26121  60.31519 0.700 52.64994 ? 252 CME A CE  1 
HETATM 2026 C CZ  . CME A 1 258 ? 14.93984  -0.73321  59.33987 0.500 42.97856 ? 252 CME A CZ  1 
HETATM 2027 O OH  . CME A 1 258 ? 13.91822  -1.63686  59.11001 0.500 50.32881 ? 252 CME A OH  1 
HETATM 2028 C C   . CME A 1 258 ? 17.35430  4.25217   59.81911 1.000 30.16664 ? 252 CME A C   1 
HETATM 2029 O O   . CME A 1 258 ? 17.27978  3.94229   58.65400 1.000 33.73735 ? 252 CME A O   1 
ATOM   2030 N N   . ILE A 1 259 ? 17.55844  5.50375   60.21874 1.000 26.28075 ? 253 ILE A N   1 
ATOM   2031 C CA  . ILE A 1 259 ? 17.81928  6.57397   59.26387 1.000 26.83419 ? 253 ILE A CA  1 
ATOM   2032 C C   . ILE A 1 259 ? 19.32871  6.73104   59.11190 1.000 31.42030 ? 253 ILE A C   1 
ATOM   2033 O O   . ILE A 1 259 ? 19.98648  7.42224   59.89330 1.000 23.98873 ? 253 ILE A O   1 
ATOM   2034 C CB  . ILE A 1 259 ? 17.16155  7.89072   59.69019 1.000 23.23644 ? 253 ILE A CB  1 
ATOM   2035 C CG1 . ILE A 1 259 ? 15.64752  7.70999   59.82964 1.000 22.30628 ? 253 ILE A CG1 1 
ATOM   2036 C CG2 . ILE A 1 259 ? 17.46688  8.98441   58.67739 1.000 16.82931 ? 253 ILE A CG2 1 
ATOM   2037 C CD1 . ILE A 1 259 ? 14.97079  8.85111   60.54516 1.000 22.80920 ? 253 ILE A CD1 1 
ATOM   2038 N N   . ILE A 1 260 ? 19.87686  6.06954   58.09409 1.000 24.87098 ? 254 ILE A N   1 
ATOM   2039 C CA  . ILE A 1 260 ? 21.32099  6.06447   57.90955 1.000 30.37811 ? 254 ILE A CA  1 
ATOM   2040 C C   . ILE A 1 260 ? 21.81786  7.29067   57.15294 1.000 27.14050 ? 254 ILE A C   1 
ATOM   2041 O O   . ILE A 1 260 ? 23.00441  7.62649   57.25462 1.000 28.45783 ? 254 ILE A O   1 
ATOM   2042 C CB  . ILE A 1 260 ? 21.73712  4.75150   57.22631 1.000 37.51001 ? 254 ILE A CB  1 
ATOM   2043 C CG1 . ILE A 1 260 ? 21.37224  4.76594   55.74341 0.700 29.29071 ? 254 ILE A CG1 1 
ATOM   2044 C CG2 . ILE A 1 260 ? 21.08918  3.56354   57.92501 0.700 34.49818 ? 254 ILE A CG2 1 
ATOM   2045 C CD1 . ILE A 1 260 ? 22.10925  3.72511   54.94650 0.700 35.28662 ? 254 ILE A CD1 1 
ATOM   2046 N N   . ASN A 1 261 ? 20.94904  7.98291   56.41556 1.000 23.45857 ? 255 ASN A N   1 
ATOM   2047 C CA  . ASN A 1 261 ? 21.34925  9.23381   55.78064 1.000 26.17877 ? 255 ASN A CA  1 
ATOM   2048 C C   . ASN A 1 261 ? 21.71200  10.26660  56.84254 1.000 23.93546 ? 255 ASN A C   1 
ATOM   2049 O O   . ASN A 1 261 ? 20.93298  10.52932  57.76288 1.000 25.28686 ? 255 ASN A O   1 
ATOM   2050 C CB  . ASN A 1 261 ? 20.22591  9.76003   54.88646 1.000 27.26151 ? 255 ASN A CB  1 
ATOM   2051 C CG  . ASN A 1 261 ? 20.64875  10.96718  54.07180 1.000 31.19379 ? 255 ASN A CG  1 
ATOM   2052 O OD1 . ASN A 1 261 ? 20.55203  12.10544  54.53089 1.000 30.05267 ? 255 ASN A OD1 1 
ATOM   2053 N ND2 . ASN A 1 261 ? 21.11963  10.72371  52.85333 1.000 33.16560 ? 255 ASN A ND2 1 
ATOM   2054 N N   . LEU A 1 262 ? 22.89894  10.86185  56.70586 1.000 24.44987 ? 256 LEU A N   1 
ATOM   2055 C CA  . LEU A 1 262 ? 23.44316  11.67330  57.79109 1.000 26.01368 ? 256 LEU A CA  1 
ATOM   2056 C C   . LEU A 1 262 ? 22.73051  13.01490  57.91342 1.000 26.32033 ? 256 LEU A C   1 
ATOM   2057 O O   . LEU A 1 262 ? 22.48916  13.49013  59.02835 1.000 20.03792 ? 256 LEU A O   1 
ATOM   2058 C CB  A LEU A 1 262 ? 24.94387  11.88564  57.59729 0.500 24.13931 ? 256 LEU A CB  1 
ATOM   2059 C CB  B LEU A 1 262 ? 24.94199  11.87405  57.58054 0.500 24.14082 ? 256 LEU A CB  1 
ATOM   2060 C CG  A LEU A 1 262 ? 25.83302  10.74311  58.08467 0.500 22.99429 ? 256 LEU A CG  1 
ATOM   2061 C CG  B LEU A 1 262 ? 25.74838  12.18654  58.83759 0.500 22.58266 ? 256 LEU A CG  1 
ATOM   2062 C CD1 A LEU A 1 262 ? 27.19975  10.79861  57.43114 0.500 26.88585 ? 256 LEU A CD1 1 
ATOM   2063 C CD1 B LEU A 1 262 ? 25.46555  11.16214  59.92365 0.500 27.85444 ? 256 LEU A CD1 1 
ATOM   2064 C CD2 A LEU A 1 262 ? 25.95779  10.79124  59.59737 0.500 28.98021 ? 256 LEU A CD2 1 
ATOM   2065 C CD2 B LEU A 1 262 ? 27.22431  12.21710  58.50431 0.500 30.40751 ? 256 LEU A CD2 1 
ATOM   2066 N N   . LYS A 1 263 ? 22.39353  13.65002  56.78903 1.000 25.16947 ? 257 LYS A N   1 
ATOM   2067 C CA  . LYS A 1 263 ? 21.71396  14.93928  56.87149 1.000 28.54575 ? 257 LYS A CA  1 
ATOM   2068 C C   . LYS A 1 263 ? 20.35328  14.80127  57.54234 1.000 19.86691 ? 257 LYS A C   1 
ATOM   2069 O O   . LYS A 1 263 ? 19.96482  15.64988  58.35314 1.000 18.76102 ? 257 LYS A O   1 
ATOM   2070 C CB  . LYS A 1 263 ? 21.57530  15.55873  55.48079 1.000 28.27984 ? 257 LYS A CB  1 
ATOM   2071 C CG  . LYS A 1 263 ? 22.90535  15.91160  54.84183 0.900 29.08362 ? 257 LYS A CG  1 
ATOM   2072 C CD  . LYS A 1 263 ? 22.74265  16.90823  53.70424 0.900 38.01422 ? 257 LYS A CD  1 
ATOM   2073 C CE  . LYS A 1 263 ? 23.92949  17.86216  53.64867 0.600 41.93945 ? 257 LYS A CE  1 
ATOM   2074 N NZ  . LYS A 1 263 ? 23.89306  18.74363  52.44910 0.600 34.32335 ? 257 LYS A NZ  1 
ATOM   2075 N N   . ALA A 1 264 ? 19.62358  13.72926  57.23035 1.000 17.52697 ? 258 ALA A N   1 
ATOM   2076 C CA  . ALA A 1 264 ? 18.31761  13.51796  57.84402 1.000 17.59118 ? 258 ALA A CA  1 
ATOM   2077 C C   . ALA A 1 264 ? 18.45115  13.18926  59.32685 1.000 19.10117 ? 258 ALA A C   1 
ATOM   2078 O O   . ALA A 1 264 ? 17.73571  13.75237  60.16379 1.000 18.93975 ? 258 ALA A O   1 
ATOM   2079 C CB  . ALA A 1 264 ? 17.56762  12.40779  57.10889 1.000 17.77639 ? 258 ALA A CB  1 
ATOM   2080 N N   . ARG A 1 265 ? 19.35979  12.27220  59.67210 1.000 16.60124 ? 259 ARG A N   1 
ATOM   2081 C CA  . ARG A 1 265 ? 19.53029  11.90033  61.07517 1.000 18.05201 ? 259 ARG A CA  1 
ATOM   2082 C C   . ARG A 1 265 ? 20.02234  13.07607  61.90939 1.000 16.78533 ? 259 ARG A C   1 
ATOM   2083 O O   . ARG A 1 265 ? 19.52653  13.30883  63.01813 1.000 17.99948 ? 259 ARG A O   1 
ATOM   2084 C CB  . ARG A 1 265 ? 20.49824  10.72454  61.20824 0.900 25.17200 ? 259 ARG A CB  1 
ATOM   2085 C CG  . ARG A 1 265 ? 20.52727  10.13700  62.61443 0.800 28.62493 ? 259 ARG A CG  1 
ATOM   2086 C CD  . ARG A 1 265 ? 21.67542  9.16408   62.81136 0.800 26.29697 ? 259 ARG A CD  1 
ATOM   2087 N NE  . ARG A 1 265 ? 21.51069  7.93303   62.04777 0.800 27.08378 ? 259 ARG A NE  1 
ATOM   2088 C CZ  . ARG A 1 265 ? 22.27832  6.86200   62.19309 0.700 30.91732 ? 259 ARG A CZ  1 
ATOM   2089 N NH1 . ARG A 1 265 ? 23.27338  6.83933   63.06609 0.700 31.92239 ? 259 ARG A NH1 1 
ATOM   2090 N NH2 . ARG A 1 265 ? 22.04239  5.78772   61.44531 0.700 28.17671 ? 259 ARG A NH2 1 
ATOM   2091 N N   . ASN A 1 266 ? 21.00274  13.82416  61.39955 1.000 17.67608 ? 260 ASN A N   1 
ATOM   2092 C CA  . ASN A 1 266 ? 21.54482  14.93999  62.16684 1.000 18.10266 ? 260 ASN A CA  1 
ATOM   2093 C C   . ASN A 1 266 ? 20.53395  16.06739  62.33553 1.000 18.96067 ? 260 ASN A C   1 
ATOM   2094 O O   . ASN A 1 266 ? 20.58191  16.79089  63.33913 1.000 19.79912 ? 260 ASN A O   1 
ATOM   2095 C CB  . ASN A 1 266 ? 22.82004  15.46526  61.51358 1.000 19.33257 ? 260 ASN A CB  1 
ATOM   2096 C CG  . ASN A 1 266 ? 24.01877  14.58787  61.80351 1.000 31.10667 ? 260 ASN A CG  1 
ATOM   2097 O OD1 . ASN A 1 266 ? 24.01381  13.81250  62.76021 1.000 27.51564 ? 260 ASN A OD1 1 
ATOM   2098 N ND2 . ASN A 1 266 ? 25.05507  14.70959  60.98531 1.000 23.89025 ? 260 ASN A ND2 1 
ATOM   2099 N N   . TYR A 1 267 ? 19.62712  16.24893  61.37461 1.000 16.97207 ? 261 TYR A N   1 
ATOM   2100 C CA  . TYR A 1 267 ? 18.54863  17.20889  61.58181 1.000 19.83972 ? 261 TYR A CA  1 
ATOM   2101 C C   . TYR A 1 267 ? 17.70482  16.82071  62.78684 1.000 15.62520 ? 261 TYR A C   1 
ATOM   2102 O O   . TYR A 1 267 ? 17.43074  17.64807  63.66330 1.000 17.95113 ? 261 TYR A O   1 
ATOM   2103 C CB  . TYR A 1 267 ? 17.66217  17.32757  60.33784 1.000 16.06529 ? 261 TYR A CB  1 
ATOM   2104 C CG  . TYR A 1 267 ? 16.46118  18.19598  60.63300 1.000 15.53651 ? 261 TYR A CG  1 
ATOM   2105 C CD1 . TYR A 1 267 ? 16.58809  19.57625  60.70933 1.000 17.17667 ? 261 TYR A CD1 1 
ATOM   2106 C CD2 . TYR A 1 267 ? 15.21494  17.63617  60.88464 1.000 19.13532 ? 261 TYR A CD2 1 
ATOM   2107 C CE1 . TYR A 1 267 ? 15.50815  20.37599  61.00612 1.000 21.83422 ? 261 TYR A CE1 1 
ATOM   2108 C CE2 . TYR A 1 267 ? 14.12377  18.43112  61.18409 1.000 14.28285 ? 261 TYR A CE2 1 
ATOM   2109 C CZ  . TYR A 1 267 ? 14.27936  19.80127  61.24187 1.000 18.23697 ? 261 TYR A CZ  1 
ATOM   2110 O OH  . TYR A 1 267 ? 13.20303  20.60390  61.53801 1.000 24.53752 ? 261 TYR A OH  1 
ATOM   2111 N N   . LEU A 1 268 ? 17.28688  15.55679  62.84551 1.000 15.08909 ? 262 LEU A N   1 
ATOM   2112 C CA  . LEU A 1 268 ? 16.45448  15.10106  63.95132 1.000 15.77745 ? 262 LEU A CA  1 
ATOM   2113 C C   . LEU A 1 268 ? 17.21008  15.16233  65.27276 1.000 14.90585 ? 262 LEU A C   1 
ATOM   2114 O O   . LEU A 1 268 ? 16.62841  15.47471  66.31779 1.000 15.93214 ? 262 LEU A O   1 
ATOM   2115 C CB  . LEU A 1 268 ? 15.96038  13.68535  63.66504 1.000 13.97090 ? 262 LEU A CB  1 
ATOM   2116 C CG  . LEU A 1 268 ? 15.02558  13.60478  62.45605 1.000 25.68242 ? 262 LEU A CG  1 
ATOM   2117 C CD1 . LEU A 1 268 ? 14.84132  12.16132  62.00924 1.000 19.02675 ? 262 LEU A CD1 1 
ATOM   2118 C CD2 . LEU A 1 268 ? 13.68050  14.26374  62.76673 1.000 17.27845 ? 262 LEU A CD2 1 
ATOM   2119 N N   . LEU A 1 269 ? 18.51258  14.88123  65.24116 1.000 15.67689 ? 263 LEU A N   1 
ATOM   2120 C CA  . LEU A 1 269 ? 19.32847  14.95781  66.44629 1.000 16.98219 ? 263 LEU A CA  1 
ATOM   2121 C C   . LEU A 1 269 ? 19.49105  16.38622  66.94549 1.000 20.42832 ? 263 LEU A C   1 
ATOM   2122 O O   . LEU A 1 269 ? 19.72443  16.58853  68.14244 1.000 19.18755 ? 263 LEU A O   1 
ATOM   2123 C CB  . LEU A 1 269 ? 20.69880  14.33931  66.18426 1.000 17.14002 ? 263 LEU A CB  1 
ATOM   2124 C CG  . LEU A 1 269 ? 20.74053  12.81447  66.09077 1.000 20.32191 ? 263 LEU A CG  1 
ATOM   2125 C CD1 . LEU A 1 269 ? 22.14862  12.32872  65.76231 1.000 27.00327 ? 263 LEU A CD1 1 
ATOM   2126 C CD2 . LEU A 1 269 ? 20.24740  12.20402  67.39333 1.000 24.55261 ? 263 LEU A CD2 1 
ATOM   2127 N N   . SER A 1 270 ? 19.36783  17.37718  66.06074 1.000 17.74892 ? 264 SER A N   1 
ATOM   2128 C CA  . SER A 1 270 ? 19.54846  18.77446  66.43317 1.000 20.44683 ? 264 SER A CA  1 
ATOM   2129 C C   . SER A 1 270 ? 18.33189  19.36927  67.12913 1.000 16.99242 ? 264 SER A C   1 
ATOM   2130 O O   . SER A 1 270 ? 18.44202  20.45423  67.70985 1.000 24.81015 ? 264 SER A O   1 
ATOM   2131 C CB  . SER A 1 270 ? 19.88192  19.60539  65.18966 1.000 17.64797 ? 264 SER A CB  1 
ATOM   2132 O OG  . SER A 1 270 ? 18.72392  19.81599  64.39567 1.000 25.55138 ? 264 SER A OG  1 
ATOM   2133 N N   . LEU A 1 271 ? 17.19268  18.69308  67.09165 1.000 19.44977 ? 265 LEU A N   1 
ATOM   2134 C CA  . LEU A 1 271 ? 15.97157  19.22218  67.67012 1.000 17.42143 ? 265 LEU A CA  1 
ATOM   2135 C C   . LEU A 1 271 ? 15.94154  18.98018  69.17837 1.000 30.45033 ? 265 LEU A C   1 
ATOM   2136 O O   . LEU A 1 271 ? 16.45157  17.96638  69.66174 1.000 20.49010 ? 265 LEU A O   1 
ATOM   2137 C CB  . LEU A 1 271 ? 14.75738  18.56438  67.02212 1.000 18.30890 ? 265 LEU A CB  1 
ATOM   2138 C CG  . LEU A 1 271 ? 14.61069  18.74834  65.50900 1.000 20.77323 ? 265 LEU A CG  1 
ATOM   2139 C CD1 . LEU A 1 271 ? 13.41530  17.96376  64.98288 1.000 15.71989 ? 265 LEU A CD1 1 
ATOM   2140 C CD2 . LEU A 1 271 ? 14.48748  20.22210  65.14853 1.000 21.70687 ? 265 LEU A CD2 1 
ATOM   2141 N N   . PRO A 1 272 ? 15.35335  19.89622  69.94303 1.000 26.68461 ? 266 PRO A N   1 
ATOM   2142 C CA  . PRO A 1 272 ? 15.15513  19.64067  71.37222 1.000 28.50108 ? 266 PRO A CA  1 
ATOM   2143 C C   . PRO A 1 272 ? 14.15081  18.51895  71.57593 1.000 24.06483 ? 266 PRO A C   1 
ATOM   2144 O O   . PRO A 1 272 ? 13.37201  18.17247  70.68395 1.000 19.66675 ? 266 PRO A O   1 
ATOM   2145 C CB  . PRO A 1 272 ? 14.61761  20.97365  71.91155 1.000 28.73622 ? 266 PRO A CB  1 
ATOM   2146 C CG  . PRO A 1 272 ? 14.85419  21.97861  70.81372 1.000 31.58747 ? 266 PRO A CG  1 
ATOM   2147 C CD  . PRO A 1 272 ? 14.81470  21.20300  69.53933 1.000 27.00891 ? 266 PRO A CD  1 
ATOM   2148 N N   . HIS A 1 273 ? 14.17734  17.94041  72.77300 1.000 21.62658 ? 267 HIS A N   1 
ATOM   2149 C CA  . HIS A 1 273 ? 13.25998  16.84741  73.06013 1.000 27.46397 ? 267 HIS A CA  1 
ATOM   2150 C C   . HIS A 1 273 ? 11.81441  17.32403  73.02921 1.000 25.32654 ? 267 HIS A C   1 
ATOM   2151 O O   . HIS A 1 273 ? 11.47609  18.38061  73.56885 1.000 29.19468 ? 267 HIS A O   1 
ATOM   2152 C CB  . HIS A 1 273 ? 13.55460  16.21773  74.41833 1.000 34.07101 ? 267 HIS A CB  1 
ATOM   2153 C CG  . HIS A 1 273 ? 12.62090  15.09967  74.75956 1.000 33.02727 ? 267 HIS A CG  1 
ATOM   2154 N ND1 . HIS A 1 273 ? 12.77908  13.82177  74.26773 1.000 35.89086 ? 267 HIS A ND1 1 
ATOM   2155 C CD2 . HIS A 1 273 ? 11.49561  15.07659  75.51236 1.000 37.84590 ? 267 HIS A CD2 1 
ATOM   2156 C CE1 . HIS A 1 273 ? 11.80214  13.05531  74.71801 1.000 30.26652 ? 267 HIS A CE1 1 
ATOM   2157 N NE2 . HIS A 1 273 ? 11.00994  13.79225  75.47573 1.000 37.98477 ? 267 HIS A NE2 1 
ATOM   2158 N N   . LYS A 1 274 ? 10.96244  16.53026  72.38875 1.000 20.83662 ? 268 LYS A N   1 
ATOM   2159 C CA  . LYS A 1 274 ? 9.52276   16.73458  72.39306 1.000 26.91129 ? 268 LYS A CA  1 
ATOM   2160 C C   . LYS A 1 274 ? 8.85549   15.49111  72.95874 1.000 25.47707 ? 268 LYS A C   1 
ATOM   2161 O O   . LYS A 1 274 ? 9.22089   14.36572  72.60325 1.000 22.46777 ? 268 LYS A O   1 
ATOM   2162 C CB  . LYS A 1 274 ? 8.97749   17.00461  70.98614 1.000 27.20816 ? 268 LYS A CB  1 
ATOM   2163 C CG  . LYS A 1 274 ? 9.72240   18.05397  70.17791 1.000 26.62995 ? 268 LYS A CG  1 
ATOM   2164 C CD  . LYS A 1 274 ? 9.31742   17.95878  68.70686 1.000 27.68866 ? 268 LYS A CD  1 
ATOM   2165 C CE  . LYS A 1 274 ? 10.20389  18.80707  67.80120 1.000 25.56574 ? 268 LYS A CE  1 
ATOM   2166 N NZ  . LYS A 1 274 ? 9.92846   20.26439  67.95031 1.000 30.08809 ? 268 LYS A NZ  1 
ATOM   2167 N N   . ASN A 1 275 ? 7.87905   15.69491  73.83666 1.000 26.52637 ? 269 ASN A N   1 
ATOM   2168 C CA  . ASN A 1 275 ? 7.13028   14.58055  74.39432 1.000 29.97645 ? 269 ASN A CA  1 
ATOM   2169 C C   . ASN A 1 275 ? 5.98956   14.17824  73.46927 1.000 24.08092 ? 269 ASN A C   1 
ATOM   2170 O O   . ASN A 1 275 ? 5.43283   14.99993  72.73529 1.000 27.42544 ? 269 ASN A O   1 
ATOM   2171 C CB  . ASN A 1 275 ? 6.57552   14.93293  75.77614 0.800 31.59459 ? 269 ASN A CB  1 
ATOM   2172 C CG  . ASN A 1 275 ? 7.60690   15.59075  76.66661 0.600 30.76346 ? 269 ASN A CG  1 
ATOM   2173 O OD1 . ASN A 1 275 ? 8.59192   14.96544  77.05659 0.600 36.80354 ? 269 ASN A OD1 1 
ATOM   2174 N ND2 . ASN A 1 275 ? 7.38437   16.85698  76.99841 0.600 33.42026 ? 269 ASN A ND2 1 
ATOM   2175 N N   . LYS A 1 276 ? 5.66622   12.88790  73.49642 1.000 20.49351 ? 270 LYS A N   1 
ATOM   2176 C CA  . LYS A 1 276 ? 4.48902   12.38618  72.80460 1.000 20.51174 ? 270 LYS A CA  1 
ATOM   2177 C C   . LYS A 1 276 ? 3.23140   12.98040  73.42527 1.000 28.35225 ? 270 LYS A C   1 
ATOM   2178 O O   . LYS A 1 276 ? 3.11846   13.09493  74.64794 1.000 20.82368 ? 270 LYS A O   1 
ATOM   2179 C CB  . LYS A 1 276 ? 4.44982   10.85746  72.88627 1.000 23.19861 ? 270 LYS A CB  1 
ATOM   2180 C CG  A LYS A 1 276 ? 3.35220   10.19190  72.06634 0.590 23.67834 ? 270 LYS A CG  1 
ATOM   2181 C CG  B LYS A 1 276 ? 3.20891   10.22013  72.27647 0.410 23.63829 ? 270 LYS A CG  1 
ATOM   2182 C CD  A LYS A 1 276 ? 3.49506   8.67627   72.11673 0.590 23.10886 ? 270 LYS A CD  1 
ATOM   2183 C CD  B LYS A 1 276 ? 3.01736   8.80201   72.79093 0.410 23.73127 ? 270 LYS A CD  1 
ATOM   2184 C CE  A LYS A 1 276 ? 2.44989   7.97227   71.26335 0.590 29.92989 ? 270 LYS A CE  1 
ATOM   2185 C CE  B LYS A 1 276 ? 1.96935   8.04969   71.98531 0.410 32.61226 ? 270 LYS A CE  1 
ATOM   2186 N NZ  A LYS A 1 276 ? 2.39083   8.50715   69.87567 0.590 26.60135 ? 270 LYS A NZ  1 
ATOM   2187 N NZ  B LYS A 1 276 ? 0.68377   8.79826   71.89751 0.410 29.54125 ? 270 LYS A NZ  1 
ATOM   2188 N N   . VAL A 1 277 ? 2.29157   13.38138  72.57775 1.000 20.09124 ? 271 VAL A N   1 
ATOM   2189 C CA  . VAL A 1 277 ? 0.98240   13.84666  73.02363 1.000 23.19338 ? 271 VAL A CA  1 
ATOM   2190 C C   . VAL A 1 277 ? 0.04401   12.64341  73.02638 1.000 21.06224 ? 271 VAL A C   1 
ATOM   2191 O O   . VAL A 1 277 ? -0.12510  12.00779  71.97411 1.000 25.45303 ? 271 VAL A O   1 
ATOM   2192 C CB  . VAL A 1 277 ? 0.44123   14.96411  72.12408 1.000 27.19874 ? 271 VAL A CB  1 
ATOM   2193 C CG1 . VAL A 1 277 ? -0.98154  15.32160  72.52251 1.000 25.47456 ? 271 VAL A CG1 1 
ATOM   2194 C CG2 . VAL A 1 277 ? 1.34229   16.18836  72.19504 1.000 21.98426 ? 271 VAL A CG2 1 
ATOM   2195 N N   . PRO A 1 278 ? -0.55645  12.28875  74.16204 1.000 23.31424 ? 272 PRO A N   1 
ATOM   2196 C CA  . PRO A 1 278 ? -1.42550  11.10474  74.19985 1.000 22.42767 ? 272 PRO A CA  1 
ATOM   2197 C C   . PRO A 1 278 ? -2.62132  11.27834  73.27578 1.000 19.28174 ? 272 PRO A C   1 
ATOM   2198 O O   . PRO A 1 278 ? -3.25370  12.33651  73.24569 1.000 19.41361 ? 272 PRO A O   1 
ATOM   2199 C CB  . PRO A 1 278 ? -1.85552  11.02425  75.67023 1.000 25.62907 ? 272 PRO A CB  1 
ATOM   2200 C CG  . PRO A 1 278 ? -0.85038  11.83599  76.41542 1.000 28.28260 ? 272 PRO A CG  1 
ATOM   2201 C CD  . PRO A 1 278 ? -0.43787  12.93036  75.48181 1.000 24.95388 ? 272 PRO A CD  1 
ATOM   2202 N N   . TRP A 1 279 ? -2.92174  10.22582  72.50994 1.000 19.99463 ? 273 TRP A N   1 
ATOM   2203 C CA  . TRP A 1 279 ? -4.04523  10.29259  71.57909 1.000 18.95808 ? 273 TRP A CA  1 
ATOM   2204 C C   . TRP A 1 279 ? -5.34483  10.59176  72.31191 1.000 18.66354 ? 273 TRP A C   1 
ATOM   2205 O O   . TRP A 1 279 ? -6.17940  11.36399  71.82584 1.000 28.04554 ? 273 TRP A O   1 
ATOM   2206 C CB  . TRP A 1 279 ? -4.17134  8.98327   70.79870 1.000 21.44559 ? 273 TRP A CB  1 
ATOM   2207 C CG  . TRP A 1 279 ? -2.99523  8.65676   69.92887 1.000 21.36850 ? 273 TRP A CG  1 
ATOM   2208 C CD1 . TRP A 1 279 ? -2.14860  7.59365   70.05875 1.000 22.66983 ? 273 TRP A CD1 1 
ATOM   2209 C CD2 . TRP A 1 279 ? -2.53340  9.40238   68.79436 1.000 15.84246 ? 273 TRP A CD2 1 
ATOM   2210 N NE1 . TRP A 1 279 ? -1.19074  7.62977   69.07069 1.000 17.91903 ? 273 TRP A NE1 1 
ATOM   2211 C CE2 . TRP A 1 279 ? -1.40487  8.73058   68.28293 1.000 18.55015 ? 273 TRP A CE2 1 
ATOM   2212 C CE3 . TRP A 1 279 ? -2.96581  10.57148  68.16165 1.000 14.72606 ? 273 TRP A CE3 1 
ATOM   2213 C CZ2 . TRP A 1 279 ? -0.70354  9.18996   67.16706 1.000 15.48709 ? 273 TRP A CZ2 1 
ATOM   2214 C CZ3 . TRP A 1 279 ? -2.26740  11.02646  67.05706 1.000 22.58588 ? 273 TRP A CZ3 1 
ATOM   2215 C CH2 . TRP A 1 279 ? -1.14918  10.33730  66.57088 1.000 16.89335 ? 273 TRP A CH2 1 
ATOM   2216 N N   . ASN A 1 280 ? -5.52783  9.99995   73.49353 1.000 24.14931 ? 274 ASN A N   1 
ATOM   2217 C CA  . ASN A 1 280 ? -6.77559  10.17398  74.22626 1.000 20.60810 ? 274 ASN A CA  1 
ATOM   2218 C C   . ASN A 1 280 ? -6.93667  11.57274  74.80878 1.000 32.94062 ? 274 ASN A C   1 
ATOM   2219 O O   . ASN A 1 280 ? -8.03201  11.90917  75.26557 1.000 31.69440 ? 274 ASN A O   1 
ATOM   2220 C CB  . ASN A 1 280 ? -6.88698  9.13517   75.34254 0.800 26.78829 ? 274 ASN A CB  1 
ATOM   2221 C CG  . ASN A 1 280 ? -6.12441  9.53065   76.58513 0.700 25.03449 ? 274 ASN A CG  1 
ATOM   2222 O OD1 . ASN A 1 280 ? -4.96042  9.92320   76.51725 0.600 25.78838 ? 274 ASN A OD1 1 
ATOM   2223 N ND2 . ASN A 1 280 ? -6.78524  9.44281   77.73329 0.600 30.90847 ? 274 ASN A ND2 1 
ATOM   2224 N N   . ARG A 1 281 ? -5.88492  12.38702  74.82679 1.000 29.04317 ? 275 ARG A N   1 
ATOM   2225 C CA  . ARG A 1 281 ? -6.05238  13.79912  75.14870 1.000 34.87531 ? 275 ARG A CA  1 
ATOM   2226 C C   . ARG A 1 281 ? -6.34831  14.64401  73.92066 1.000 31.13818 ? 275 ARG A C   1 
ATOM   2227 O O   . ARG A 1 281 ? -7.05164  15.65860  74.02212 1.000 30.66338 ? 275 ARG A O   1 
ATOM   2228 C CB  . ARG A 1 281 ? -4.80766  14.35350  75.82484 1.000 31.80714 ? 275 ARG A CB  1 
ATOM   2229 C CG  . ARG A 1 281 ? -4.34496  13.62705  77.05839 0.800 29.72194 ? 275 ARG A CG  1 
ATOM   2230 C CD  . ARG A 1 281 ? -3.63554  14.63194  77.95578 0.700 45.08110 ? 275 ARG A CD  1 
ATOM   2231 N NE  . ARG A 1 281 ? -2.60066  15.34945  77.21222 0.700 49.11662 ? 275 ARG A NE  1 
ATOM   2232 C CZ  . ARG A 1 281 ? -1.39891  15.65426  77.68629 0.700 47.76160 ? 275 ARG A CZ  1 
ATOM   2233 N NH1 . ARG A 1 281 ? -1.00665  15.24943  78.88461 0.700 34.49549 ? 275 ARG A NH1 1 
ATOM   2234 N NH2 . ARG A 1 281 ? -0.56394  16.36939  76.93202 0.700 42.52736 ? 275 ARG A NH2 1 
ATOM   2235 N N   . LEU A 1 282 ? -5.79577  14.26627  72.76697 1.000 24.22400 ? 276 LEU A N   1 
ATOM   2236 C CA  . LEU A 1 282 ? -6.16448  14.93198  71.52599 1.000 23.34597 ? 276 LEU A CA  1 
ATOM   2237 C C   . LEU A 1 282 ? -7.59193  14.59543  71.12599 1.000 24.54359 ? 276 LEU A C   1 
ATOM   2238 O O   . LEU A 1 282 ? -8.28650  15.43530  70.54379 1.000 31.18664 ? 276 LEU A O   1 
ATOM   2239 C CB  . LEU A 1 282 ? -5.20501  14.53631  70.40529 1.000 29.80167 ? 276 LEU A CB  1 
ATOM   2240 C CG  . LEU A 1 282 ? -3.84062  15.22184  70.32306 1.000 27.56859 ? 276 LEU A CG  1 
ATOM   2241 C CD1 . LEU A 1 282 ? -3.01741  14.61337  69.19650 1.000 31.96534 ? 276 LEU A CD1 1 
ATOM   2242 C CD2 . LEU A 1 282 ? -3.99184  16.72195  70.12702 1.000 31.98559 ? 276 LEU A CD2 1 
ATOM   2243 N N   . PHE A 1 283 ? -8.04145  13.37826  71.42552 1.000 28.75371 ? 277 PHE A N   1 
ATOM   2244 C CA  . PHE A 1 283 ? -9.35444  12.88396  71.01400 1.000 29.44080 ? 277 PHE A CA  1 
ATOM   2245 C C   . PHE A 1 283 ? -10.03887 12.24224  72.21532 1.000 22.60802 ? 277 PHE A C   1 
ATOM   2246 O O   . PHE A 1 283 ? -10.16807 11.01465  72.29027 1.000 25.64207 ? 277 PHE A O   1 
ATOM   2247 C CB  . PHE A 1 283 ? -9.22200  11.88112  69.86699 1.000 23.93592 ? 277 PHE A CB  1 
ATOM   2248 C CG  . PHE A 1 283 ? -8.38402  12.37181  68.71820 1.000 24.37299 ? 277 PHE A CG  1 
ATOM   2249 C CD1 . PHE A 1 283 ? -8.85266  13.36277  67.86997 1.000 26.55996 ? 277 PHE A CD1 1 
ATOM   2250 C CD2 . PHE A 1 283 ? -7.13197  11.82792  68.47762 1.000 19.07422 ? 277 PHE A CD2 1 
ATOM   2251 C CE1 . PHE A 1 283 ? -8.08277  13.80958  66.80916 1.000 28.57271 ? 277 PHE A CE1 1 
ATOM   2252 C CE2 . PHE A 1 283 ? -6.35640  12.26933  67.41689 1.000 21.78996 ? 277 PHE A CE2 1 
ATOM   2253 C CZ  . PHE A 1 283 ? -6.83100  13.26034  66.58327 1.000 21.56596 ? 277 PHE A CZ  1 
ATOM   2254 N N   . PRO A 1 284 ? -10.49870 13.04909  73.17668 1.000 29.38737 ? 278 PRO A N   1 
ATOM   2255 C CA  . PRO A 1 284 ? -11.08107 12.46908  74.40036 1.000 26.33243 ? 278 PRO A CA  1 
ATOM   2256 C C   . PRO A 1 284 ? -12.37988 11.71307  74.16848 1.000 34.92465 ? 278 PRO A C   1 
ATOM   2257 O O   . PRO A 1 284 ? -12.76214 10.90269  75.02197 1.000 34.24111 ? 278 PRO A O   1 
ATOM   2258 C CB  . PRO A 1 284 ? -11.30403 13.69147  75.30174 1.000 30.13101 ? 278 PRO A CB  1 
ATOM   2259 C CG  . PRO A 1 284 ? -11.36822 14.85275  74.37029 1.000 25.37532 ? 278 PRO A CG  1 
ATOM   2260 C CD  . PRO A 1 284 ? -10.49191 14.52190  73.20070 1.000 28.17736 ? 278 PRO A CD  1 
ATOM   2261 N N   . ASN A 1 285 ? -13.06755 11.94603  73.05187 1.000 29.07203 ? 279 ASN A N   1 
ATOM   2262 C CA  . ASN A 1 285 ? -14.31477 11.25646  72.74965 1.000 37.26658 ? 279 ASN A CA  1 
ATOM   2263 C C   . ASN A 1 285 ? -14.11811 9.99458   71.92173 1.000 36.46160 ? 279 ASN A C   1 
ATOM   2264 O O   . ASN A 1 285 ? -15.07738 9.23610   71.74102 1.000 28.25904 ? 279 ASN A O   1 
ATOM   2265 C CB  . ASN A 1 285 ? -15.26915 12.19511  72.00130 0.800 34.32765 ? 279 ASN A CB  1 
ATOM   2266 C CG  . ASN A 1 285 ? -15.88503 13.24183  72.90328 0.700 39.05999 ? 279 ASN A CG  1 
ATOM   2267 O OD1 . ASN A 1 285 ? -15.42735 14.38378  72.95128 0.600 42.34192 ? 279 ASN A OD1 1 
ATOM   2268 N ND2 . ASN A 1 285 ? -16.93974 12.86244  73.61457 0.600 44.26649 ? 279 ASN A ND2 1 
ATOM   2269 N N   . ALA A 1 286 ? -12.91212 9.75004   71.41992 1.000 19.49520 ? 280 ALA A N   1 
ATOM   2270 C CA  . ALA A 1 286 ? -12.70835 8.66966   70.46787 1.000 30.65573 ? 280 ALA A CA  1 
ATOM   2271 C C   . ALA A 1 286 ? -12.75383 7.30747   71.15057 1.000 22.35757 ? 280 ALA A C   1 
ATOM   2272 O O   . ALA A 1 286 ? -12.38596 7.15531   72.31839 1.000 23.32994 ? 280 ALA A O   1 
ATOM   2273 C CB  . ALA A 1 286 ? -11.37256 8.84248   69.74447 1.000 27.59561 ? 280 ALA A CB  1 
ATOM   2274 N N   . ASP A 1 287 ? -13.22162 6.31370   70.39743 1.000 25.85960 ? 281 ASP A N   1 
ATOM   2275 C CA  . ASP A 1 287 ? -13.15241 4.92417   70.82845 1.000 23.97111 ? 281 ASP A CA  1 
ATOM   2276 C C   . ASP A 1 287 ? -11.70468 4.54896   71.12405 1.000 22.13971 ? 281 ASP A C   1 
ATOM   2277 O O   . ASP A 1 287 ? -10.80015 4.87787   70.35241 1.000 23.24637 ? 281 ASP A O   1 
ATOM   2278 C CB  . ASP A 1 287 ? -13.72988 4.02251   69.73253 0.800 23.84360 ? 281 ASP A CB  1 
ATOM   2279 C CG  . ASP A 1 287 ? -13.85415 2.57264   70.15891 0.700 23.37435 ? 281 ASP A CG  1 
ATOM   2280 O OD1 . ASP A 1 287 ? -12.82358 1.94026   70.46090 0.700 31.31675 ? 281 ASP A OD1 1 
ATOM   2281 O OD2 . ASP A 1 287 ? -14.99015 2.05768   70.17704 0.700 24.39013 ? 281 ASP A OD2 1 
ATOM   2282 N N   . SER A 1 288 ? -11.48235 3.86232   72.25011 1.000 19.79983 ? 282 SER A N   1 
ATOM   2283 C CA  . SER A 1 288 ? -10.11809 3.48947   72.61582 1.000 22.77341 ? 282 SER A CA  1 
ATOM   2284 C C   . SER A 1 288 ? -9.50720  2.52672   71.60352 1.000 20.82083 ? 282 SER A C   1 
ATOM   2285 O O   . SER A 1 288 ? -8.29345  2.56351   71.36655 1.000 21.90324 ? 282 SER A O   1 
ATOM   2286 C CB  . SER A 1 288 ? -10.08795 2.87876   74.01883 1.000 22.86128 ? 282 SER A CB  1 
ATOM   2287 O OG  . SER A 1 288 ? -10.81919 1.66449   74.07174 1.000 29.47429 ? 282 SER A OG  1 
ATOM   2288 N N   . LYS A 1 289 ? -10.32167 1.66240   70.99510 1.000 17.58638 ? 283 LYS A N   1 
ATOM   2289 C CA  . LYS A 1 289 ? -9.79376  0.77255   69.96495 1.000 21.19421 ? 283 LYS A CA  1 
ATOM   2290 C C   . LYS A 1 289 ? -9.42665  1.54458   68.70268 1.000 20.06097 ? 283 LYS A C   1 
ATOM   2291 O O   . LYS A 1 289 ? -8.46322  1.18987   68.01467 1.000 20.34389 ? 283 LYS A O   1 
ATOM   2292 C CB  . LYS A 1 289 ? -10.80245 -0.33126  69.64878 1.000 25.11698 ? 283 LYS A CB  1 
ATOM   2293 C CG  . LYS A 1 289 ? -11.17810 -1.17877  70.85214 1.000 29.98714 ? 283 LYS A CG  1 
ATOM   2294 C CD  . LYS A 1 289 ? -12.11880 -2.31058  70.47636 1.000 23.45390 ? 283 LYS A CD  1 
ATOM   2295 C CE  . LYS A 1 289 ? -12.46922 -3.15533  71.69347 0.800 27.01483 ? 283 LYS A CE  1 
ATOM   2296 N NZ  . LYS A 1 289 ? -13.43901 -4.23921  71.36916 0.700 37.70440 ? 283 LYS A NZ  1 
ATOM   2297 N N   . ALA A 1 290 ? -10.18377 2.59923   68.37873 1.000 19.54039 ? 284 ALA A N   1 
ATOM   2298 C CA  . ALA A 1 290 ? -9.81972  3.44862   67.24701 1.000 23.89164 ? 284 ALA A CA  1 
ATOM   2299 C C   . ALA A 1 290 ? -8.47782  4.13034   67.48092 1.000 19.67751 ? 284 ALA A C   1 
ATOM   2300 O O   . ALA A 1 290 ? -7.65298  4.22798   66.56373 1.000 15.94397 ? 284 ALA A O   1 
ATOM   2301 C CB  . ALA A 1 290 ? -10.90743 4.49364   66.99155 1.000 16.57327 ? 284 ALA A CB  1 
ATOM   2302 N N   . LEU A 1 291 ? -8.23977  4.60464   68.70706 1.000 21.04609 ? 285 LEU A N   1 
ATOM   2303 C CA  . LEU A 1 291 ? -6.98110  5.27652   69.01385 1.000 18.55254 ? 285 LEU A CA  1 
ATOM   2304 C C   . LEU A 1 291 ? -5.80383  4.31049   68.99227 1.000 18.30781 ? 285 LEU A C   1 
ATOM   2305 O O   . LEU A 1 291 ? -4.69143  4.70021   68.62009 1.000 20.69579 ? 285 LEU A O   1 
ATOM   2306 C CB  . LEU A 1 291 ? -7.08172  5.96603   70.37254 1.000 18.77925 ? 285 LEU A CB  1 
ATOM   2307 C CG  . LEU A 1 291 ? -8.08851  7.11567   70.40597 1.000 20.83137 ? 285 LEU A CG  1 
ATOM   2308 C CD1 . LEU A 1 291 ? -8.00029  7.85835   71.72623 1.000 24.79518 ? 285 LEU A CD1 1 
ATOM   2309 C CD2 . LEU A 1 291 ? -7.85836  8.05709   69.23274 1.000 22.26892 ? 285 LEU A CD2 1 
ATOM   2310 N N   . ASP A 1 292 ? -6.02412  3.05550   69.38775 1.000 20.03117 ? 286 ASP A N   1 
ATOM   2311 C CA  . ASP A 1 292 ? -4.96284  2.05991   69.29553 1.000 21.07157 ? 286 ASP A CA  1 
ATOM   2312 C C   . ASP A 1 292 ? -4.57225  1.81197   67.84444 1.000 22.95169 ? 286 ASP A C   1 
ATOM   2313 O O   . ASP A 1 292 ? -3.38331  1.71501   67.51880 1.000 14.74398 ? 286 ASP A O   1 
ATOM   2314 C CB  . ASP A 1 292 ? -5.40746  0.76014   69.96406 1.000 23.15289 ? 286 ASP A CB  1 
ATOM   2315 C CG  . ASP A 1 292 ? -4.30075  -0.27039  70.02385 1.000 24.19146 ? 286 ASP A CG  1 
ATOM   2316 O OD1 . ASP A 1 292 ? -3.44303  -0.17599  70.92789 1.000 29.24192 ? 286 ASP A OD1 1 
ATOM   2317 O OD2 . ASP A 1 292 ? -4.28916  -1.17621  69.16454 1.000 21.15524 ? 286 ASP A OD2 1 
ATOM   2318 N N   . LEU A 1 293 ? -5.56152  1.71199   66.95472 1.000 13.20528 ? 287 LEU A N   1 
ATOM   2319 C CA  . LEU A 1 293 ? -5.25692  1.54255   65.53989 1.000 13.17195 ? 287 LEU A CA  1 
ATOM   2320 C C   . LEU A 1 293 ? -4.62198  2.80134   64.96324 1.000 13.13944 ? 287 LEU A C   1 
ATOM   2321 O O   . LEU A 1 293 ? -3.67033  2.71855   64.17771 1.000 18.39597 ? 287 LEU A O   1 
ATOM   2322 C CB  . LEU A 1 293 ? -6.52909  1.17374   64.77620 1.000 10.52059 ? 287 LEU A CB  1 
ATOM   2323 C CG  . LEU A 1 293 ? -6.40544  0.95622   63.26672 1.000 15.68360 ? 287 LEU A CG  1 
ATOM   2324 C CD1 . LEU A 1 293 ? -5.21367  0.07447   62.93295 1.000 14.37928 ? 287 LEU A CD1 1 
ATOM   2325 C CD2 . LEU A 1 293 ? -7.69021  0.35976   62.71008 1.000 18.38963 ? 287 LEU A CD2 1 
ATOM   2326 N N   . LEU A 1 294 ? -5.13333  3.97422   65.34543 1.000 14.21146 ? 288 LEU A N   1 
ATOM   2327 C CA  . LEU A 1 294 ? -4.54087  5.23325   64.90376 1.000 9.73974  ? 288 LEU A CA  1 
ATOM   2328 C C   . LEU A 1 294 ? -3.04955  5.27481   65.21256 1.000 16.28349 ? 288 LEU A C   1 
ATOM   2329 O O   . LEU A 1 294 ? -2.22934  5.61807   64.35146 1.000 13.93832 ? 288 LEU A O   1 
ATOM   2330 C CB  . LEU A 1 294 ? -5.25923  6.40599   65.57674 1.000 12.11096 ? 288 LEU A CB  1 
ATOM   2331 C CG  . LEU A 1 294 ? -4.75644  7.80777   65.22255 1.000 17.01798 ? 288 LEU A CG  1 
ATOM   2332 C CD1 . LEU A 1 294 ? -4.95836  8.09002   63.74029 1.000 14.06850 ? 288 LEU A CD1 1 
ATOM   2333 C CD2 . LEU A 1 294 ? -5.44141  8.87048   66.07926 1.000 19.28432 ? 288 LEU A CD2 1 
ATOM   2334 N N   . ASP A 1 295 ? -2.68550  4.90954   66.44502 1.000 17.10185 ? 289 ASP A N   1 
ATOM   2335 C CA  . ASP A 1 295 ? -1.28490  4.91174   66.85461 1.000 15.05002 ? 289 ASP A CA  1 
ATOM   2336 C C   . ASP A 1 295 ? -0.44491  4.00074   65.97221 1.000 17.99458 ? 289 ASP A C   1 
ATOM   2337 O O   . ASP A 1 295 ? 0.69270   4.33768   65.62210 1.000 16.24979 ? 289 ASP A O   1 
ATOM   2338 C CB  . ASP A 1 295 ? -1.17162  4.48383   68.31891 1.000 17.71572 ? 289 ASP A CB  1 
ATOM   2339 C CG  . ASP A 1 295 ? 0.26098   4.46826   68.80910 1.000 22.01228 ? 289 ASP A CG  1 
ATOM   2340 O OD1 . ASP A 1 295 ? 0.86017   5.55531   68.91674 1.000 18.89763 ? 289 ASP A OD1 1 
ATOM   2341 O OD2 . ASP A 1 295 ? 0.78661   3.36936   69.08285 1.000 22.30627 ? 289 ASP A OD2 1 
ATOM   2342 N N   . LYS A 1 296 ? -0.99286  2.84522   65.59383 1.000 16.17087 ? 290 LYS A N   1 
ATOM   2343 C CA  . LYS A 1 296 ? -0.22800  1.89160   64.80100 1.000 19.70033 ? 290 LYS A CA  1 
ATOM   2344 C C   . LYS A 1 296 ? -0.07836  2.35024   63.35432 1.000 15.15464 ? 290 LYS A C   1 
ATOM   2345 O O   . LYS A 1 296 ? 0.92211   2.02235   62.70601 1.000 15.37875 ? 290 LYS A O   1 
ATOM   2346 C CB  . LYS A 1 296 ? -0.88442  0.51222   64.89108 1.000 17.74514 ? 290 LYS A CB  1 
ATOM   2347 C CG  . LYS A 1 296 ? -0.65217  -0.14653  66.25342 1.000 19.88598 ? 290 LYS A CG  1 
ATOM   2348 C CD  A LYS A 1 296 ? -1.33414  -1.50413  66.33897 0.500 18.54134 ? 290 LYS A CD  1 
ATOM   2349 C CD  B LYS A 1 296 ? -1.56138  -1.33976  66.50723 0.500 18.38439 ? 290 LYS A CD  1 
ATOM   2350 C CE  A LYS A 1 296 ? -0.90803  -2.26599  67.58690 0.500 25.94159 ? 290 LYS A CE  1 
ATOM   2351 C CE  B LYS A 1 296 ? -1.27826  -1.93107  67.88490 0.500 25.37438 ? 290 LYS A CE  1 
ATOM   2352 N NZ  A LYS A 1 296 ? -1.13081  -1.47892  68.83177 0.500 24.97082 ? 290 LYS A NZ  1 
ATOM   2353 N NZ  B LYS A 1 296 ? -2.00563  -3.20413  68.14459 0.500 24.60145 ? 290 LYS A NZ  1 
ATOM   2354 N N   . MET A 1 297 ? -1.03862  3.12429   62.83859 1.000 14.98413 ? 291 MET A N   1 
ATOM   2355 C CA  . MET A 1 297 ? -0.91111  3.66083   61.48503 1.000 17.53235 ? 291 MET A CA  1 
ATOM   2356 C C   . MET A 1 297 ? 0.00041   4.88197   61.44379 1.000 13.95497 ? 291 MET A C   1 
ATOM   2357 O O   . MET A 1 297 ? 0.72390   5.08475   60.46349 1.000 15.70804 ? 291 MET A O   1 
ATOM   2358 C CB  A MET A 1 297 ? -2.28777  4.00975   60.91219 0.550 11.81571 ? 291 MET A CB  1 
ATOM   2359 C CB  B MET A 1 297 ? -2.28839  4.01977   60.92775 0.450 12.35559 ? 291 MET A CB  1 
ATOM   2360 C CG  A MET A 1 297 ? -3.08556  2.80816   60.42154 0.550 11.54967 ? 291 MET A CG  1 
ATOM   2361 C CG  B MET A 1 297 ? -3.32275  2.92221   61.06489 0.450 12.24330 ? 291 MET A CG  1 
ATOM   2362 S SD  A MET A 1 297 ? -4.63403  3.25141   59.59981 0.550 12.36319 ? 291 MET A SD  1 
ATOM   2363 S SD  B MET A 1 297 ? -4.95363  3.44585   60.50322 0.450 17.62820 ? 291 MET A SD  1 
ATOM   2364 C CE  A MET A 1 297 ? -5.40820  4.23094   60.87713 0.550 14.95665 ? 291 MET A CE  1 
ATOM   2365 C CE  B MET A 1 297 ? -5.50509  1.95864   59.67833 0.450 11.92183 ? 291 MET A CE  1 
ATOM   2366 N N   . LEU A 1 298 ? -0.03001  5.71531   62.48078 1.000 14.23469 ? 292 LEU A N   1 
ATOM   2367 C CA  . LEU A 1 298 ? 0.83007   6.89305   62.55565 1.000 12.56713 ? 292 LEU A CA  1 
ATOM   2368 C C   . LEU A 1 298 ? 2.10995   6.59450   63.31986 1.000 20.14725 ? 292 LEU A C   1 
ATOM   2369 O O   . LEU A 1 298 ? 2.54851   7.37577   64.16802 1.000 17.20982 ? 292 LEU A O   1 
ATOM   2370 C CB  . LEU A 1 298 ? 0.07777   8.06494   63.17681 1.000 12.37349 ? 292 LEU A CB  1 
ATOM   2371 C CG  . LEU A 1 298 ? -1.08612  8.57893   62.32262 1.000 14.41087 ? 292 LEU A CG  1 
ATOM   2372 C CD1 . LEU A 1 298 ? -1.81846  9.71797   63.02586 1.000 14.99786 ? 292 LEU A CD1 1 
ATOM   2373 C CD2 . LEU A 1 298 ? -0.60169  9.00656   60.93478 1.000 12.50453 ? 292 LEU A CD2 1 
ATOM   2374 N N   . THR A 1 299 ? 2.71097   5.44565   63.03482 1.000 16.63999 ? 293 THR A N   1 
ATOM   2375 C CA  . THR A 1 299 ? 3.98642   5.07115   63.62038 1.000 18.83709 ? 293 THR A CA  1 
ATOM   2376 C C   . THR A 1 299 ? 5.10966   5.73993   62.83856 1.000 25.68031 ? 293 THR A C   1 
ATOM   2377 O O   . THR A 1 299 ? 5.10947   5.71654   61.60328 1.000 12.82592 ? 293 THR A O   1 
ATOM   2378 C CB  . THR A 1 299 ? 4.13365   3.55077   63.59758 1.000 19.00161 ? 293 THR A CB  1 
ATOM   2379 O OG1 . THR A 1 299 ? 3.30414   2.98039   64.61946 1.000 22.45088 ? 293 THR A OG1 1 
ATOM   2380 C CG2 . THR A 1 299 ? 5.57576   3.13620   63.82562 1.000 15.33689 ? 293 THR A CG2 1 
ATOM   2381 N N   . PHE A 1 300 ? 6.05565   6.35217   63.55962 1.000 17.37085 ? 294 PHE A N   1 
ATOM   2382 C CA  . PHE A 1 300 ? 7.11400   7.12025   62.90645 1.000 15.98711 ? 294 PHE A CA  1 
ATOM   2383 C C   . PHE A 1 300 ? 7.93096   6.24583   61.96253 1.000 16.49573 ? 294 PHE A C   1 
ATOM   2384 O O   . PHE A 1 300 ? 8.16941   6.61307   60.80513 1.000 17.95122 ? 294 PHE A O   1 
ATOM   2385 C CB  . PHE A 1 300 ? 8.02296   7.76430   63.95799 1.000 13.33590 ? 294 PHE A CB  1 
ATOM   2386 C CG  . PHE A 1 300 ? 9.16826   8.54200   63.37223 1.000 15.53051 ? 294 PHE A CG  1 
ATOM   2387 C CD1 . PHE A 1 300 ? 8.99306   9.85317   62.96061 1.000 16.69268 ? 294 PHE A CD1 1 
ATOM   2388 C CD2 . PHE A 1 300 ? 10.41622  7.95827   63.21990 1.000 23.14310 ? 294 PHE A CD2 1 
ATOM   2389 C CE1 . PHE A 1 300 ? 10.04230  10.56990  62.41430 1.000 22.52095 ? 294 PHE A CE1 1 
ATOM   2390 C CE2 . PHE A 1 300 ? 11.46911  8.67066   62.67272 1.000 24.15870 ? 294 PHE A CE2 1 
ATOM   2391 C CZ  . PHE A 1 300 ? 11.28040  9.97834   62.27064 1.000 19.63447 ? 294 PHE A CZ  1 
ATOM   2392 N N   . ASN A 1 301 ? 8.36908   5.08753   62.44257 1.000 18.05825 ? 295 ASN A N   1 
ATOM   2393 C CA  . ASN A 1 301 ? 9.22933   4.20649   61.65947 1.000 17.74288 ? 295 ASN A CA  1 
ATOM   2394 C C   . ASN A 1 301 ? 8.38297   3.44526   60.64651 1.000 17.62053 ? 295 ASN A C   1 
ATOM   2395 O O   . ASN A 1 301 ? 7.52907   2.64667   61.04834 1.000 18.77480 ? 295 ASN A O   1 
ATOM   2396 C CB  . ASN A 1 301 ? 9.96203   3.23654   62.58250 1.000 19.12666 ? 295 ASN A CB  1 
ATOM   2397 C CG  . ASN A 1 301 ? 10.99976  2.38958   61.85981 1.000 27.71809 ? 295 ASN A CG  1 
ATOM   2398 O OD1 . ASN A 1 301 ? 10.79558  1.93956   60.73312 1.000 22.68814 ? 295 ASN A OD1 1 
ATOM   2399 N ND2 . ASN A 1 301 ? 12.13356  2.17470   62.51821 1.000 28.48527 ? 295 ASN A ND2 1 
ATOM   2400 N N   . PRO A 1 302 ? 8.58835   3.64731   59.34012 1.000 19.44993 ? 296 PRO A N   1 
ATOM   2401 C CA  . PRO A 1 302 ? 7.72959   2.96999   58.35159 1.000 17.84279 ? 296 PRO A CA  1 
ATOM   2402 C C   . PRO A 1 302 ? 7.83794   1.45690   58.39100 1.000 21.73592 ? 296 PRO A C   1 
ATOM   2403 O O   . PRO A 1 302 ? 6.87186   0.76601   58.04566 1.000 19.49992 ? 296 PRO A O   1 
ATOM   2404 C CB  . PRO A 1 302 ? 8.22558   3.53295   57.01123 1.000 23.01294 ? 296 PRO A CB  1 
ATOM   2405 C CG  . PRO A 1 302 ? 9.61342   4.02764   57.29229 1.000 22.88071 ? 296 PRO A CG  1 
ATOM   2406 C CD  . PRO A 1 302 ? 9.57460   4.53361   58.70277 1.000 17.98235 ? 296 PRO A CD  1 
ATOM   2407 N N   . HIS A 1 303 ? 8.98777   0.91579   58.79776 1.000 18.09489 ? 297 HIS A N   1 
ATOM   2408 C CA  . HIS A 1 303 ? 9.12609   -0.53375  58.88658 1.000 15.86516 ? 297 HIS A CA  1 
ATOM   2409 C C   . HIS A 1 303 ? 8.31913   -1.11035  60.04385 1.000 17.23207 ? 297 HIS A C   1 
ATOM   2410 O O   . HIS A 1 303 ? 7.94701   -2.28808  60.01030 1.000 26.22868 ? 297 HIS A O   1 
ATOM   2411 C CB  . HIS A 1 303 ? 10.60094  -0.90664  59.02180 0.800 25.17744 ? 297 HIS A CB  1 
ATOM   2412 C CG  . HIS A 1 303 ? 11.45287  -0.40099  57.90007 0.600 26.53810 ? 297 HIS A CG  1 
ATOM   2413 N ND1 . HIS A 1 303 ? 12.26209  0.70799   58.02150 0.600 35.86079 ? 297 HIS A ND1 1 
ATOM   2414 C CD2 . HIS A 1 303 ? 11.62519  -0.85604  56.63647 0.600 27.08382 ? 297 HIS A CD2 1 
ATOM   2415 C CE1 . HIS A 1 303 ? 12.89379  0.91636   56.88016 0.600 32.12244 ? 297 HIS A CE1 1 
ATOM   2416 N NE2 . HIS A 1 303 ? 12.52524  -0.01897  56.02333 0.600 29.66538 ? 297 HIS A NE2 1 
ATOM   2417 N N   . LYS A 1 304 ? 8.04781   -0.30911  61.07232 1.000 18.52663 ? 298 LYS A N   1 
ATOM   2418 C CA  . LYS A 1 304 ? 7.18584   -0.72309  62.17152 1.000 22.28964 ? 298 LYS A CA  1 
ATOM   2419 C C   . LYS A 1 304 ? 5.72555   -0.36131  61.94290 1.000 18.28210 ? 298 LYS A C   1 
ATOM   2420 O O   . LYS A 1 304 ? 4.86177   -0.83935  62.68648 1.000 18.02152 ? 298 LYS A O   1 
ATOM   2421 C CB  . LYS A 1 304 ? 7.65373   -0.08903  63.48276 1.000 17.44853 ? 298 LYS A CB  1 
ATOM   2422 C CG  . LYS A 1 304 ? 9.07382   -0.44822  63.88064 1.000 27.59457 ? 298 LYS A CG  1 
ATOM   2423 C CD  . LYS A 1 304 ? 9.48816   0.32086   65.12322 0.800 18.43103 ? 298 LYS A CD  1 
ATOM   2424 C CE  . LYS A 1 304 ? 10.85977  -0.10664  65.61507 0.700 21.35838 ? 298 LYS A CE  1 
ATOM   2425 N NZ  . LYS A 1 304 ? 11.36069  0.82011   66.66682 0.700 27.93422 ? 298 LYS A NZ  1 
ATOM   2426 N N   . ARG A 1 305 ? 5.44063   0.47331   60.94651 1.000 19.76320 ? 299 ARG A N   1 
ATOM   2427 C CA  . ARG A 1 305 ? 4.07548   0.89834   60.67234 1.000 18.71957 ? 299 ARG A CA  1 
ATOM   2428 C C   . ARG A 1 305 ? 3.20947   -0.29346  60.28332 1.000 15.95431 ? 299 ARG A C   1 
ATOM   2429 O O   . ARG A 1 305 ? 3.63966   -1.18339  59.54475 1.000 17.44128 ? 299 ARG A O   1 
ATOM   2430 C CB  . ARG A 1 305 ? 4.07477   1.94858   59.55929 1.000 16.79793 ? 299 ARG A CB  1 
ATOM   2431 C CG  . ARG A 1 305 ? 2.83904   2.83268   59.51624 1.000 16.32177 ? 299 ARG A CG  1 
ATOM   2432 C CD  . ARG A 1 305 ? 3.03542   3.99793   58.55453 1.000 17.21383 ? 299 ARG A CD  1 
ATOM   2433 N NE  . ARG A 1 305 ? 4.14181   4.85110   58.96845 1.000 15.72509 ? 299 ARG A NE  1 
ATOM   2434 C CZ  . ARG A 1 305 ? 4.93092   5.51592   58.13620 1.000 17.81800 ? 299 ARG A CZ  1 
ATOM   2435 N NH1 . ARG A 1 305 ? 4.75552   5.46055   56.82580 1.000 16.13059 ? 299 ARG A NH1 1 
ATOM   2436 N NH2 . ARG A 1 305 ? 5.92873   6.24447   58.63136 1.000 12.17883 ? 299 ARG A NH2 1 
ATOM   2437 N N   . ILE A 1 306 ? 1.97601   -0.30452  60.79342 1.000 18.22768 ? 300 ILE A N   1 
ATOM   2438 C CA  . ILE A 1 306 ? 1.06996   -1.41077  60.52750 1.000 14.17364 ? 300 ILE A CA  1 
ATOM   2439 C C   . ILE A 1 306 ? 0.76824   -1.49197  59.03139 1.000 13.84941 ? 300 ILE A C   1 
ATOM   2440 O O   . ILE A 1 306 ? 0.70968   -0.47653  58.32662 1.000 16.74579 ? 300 ILE A O   1 
ATOM   2441 C CB  . ILE A 1 306 ? -0.21638  -1.24510  61.35726 1.000 15.04364 ? 300 ILE A CB  1 
ATOM   2442 C CG1 . ILE A 1 306 ? -1.08067  -2.50070  61.29234 1.000 17.07821 ? 300 ILE A CG1 1 
ATOM   2443 C CG2 . ILE A 1 306 ? -1.00335  -0.03387  60.89920 1.000 11.28878 ? 300 ILE A CG2 1 
ATOM   2444 C CD1 . ILE A 1 306 ? -2.27515  -2.46030  62.21740 1.000 18.06342 ? 300 ILE A CD1 1 
ATOM   2445 N N   . GLU A 1 307 ? 0.60300   -2.71550  58.53539 1.000 18.04683 ? 301 GLU A N   1 
ATOM   2446 C CA  . GLU A 1 307 ? 0.26213   -2.91802  57.13620 1.000 15.75827 ? 301 GLU A CA  1 
ATOM   2447 C C   . GLU A 1 307 ? -1.24926  -3.04121  56.96626 1.000 12.19702 ? 301 GLU A C   1 
ATOM   2448 O O   . GLU A 1 307 ? -1.99914  -3.19029  57.93112 1.000 12.62064 ? 301 GLU A O   1 
ATOM   2449 C CB  . GLU A 1 307 ? 0.97039   -4.15040  56.58451 1.000 14.40116 ? 301 GLU A CB  1 
ATOM   2450 C CG  . GLU A 1 307 ? 2.46929   -3.97307  56.54380 1.000 20.37919 ? 301 GLU A CG  1 
ATOM   2451 C CD  . GLU A 1 307 ? 3.15256   -4.97463  55.65240 0.900 26.79948 ? 301 GLU A CD  1 
ATOM   2452 O OE1 . GLU A 1 307 ? 2.52577   -5.99062  55.28676 0.700 27.63338 ? 301 GLU A OE1 1 
ATOM   2453 O OE2 . GLU A 1 307 ? 4.32133   -4.72839  55.30097 0.700 25.36092 ? 301 GLU A OE2 1 
ATOM   2454 N N   . VAL A 1 308 ? -1.69367  -2.99131  55.70776 1.000 16.93229 ? 302 VAL A N   1 
ATOM   2455 C CA  . VAL A 1 308 ? -3.12710  -2.89518  55.43896 1.000 11.30764 ? 302 VAL A CA  1 
ATOM   2456 C C   . VAL A 1 308 ? -3.86078  -4.14263  55.92231 1.000 13.98829 ? 302 VAL A C   1 
ATOM   2457 O O   . VAL A 1 308 ? -4.94215  -4.04867  56.51904 1.000 16.79045 ? 302 VAL A O   1 
ATOM   2458 C CB  . VAL A 1 308 ? -3.37719  -2.60930  53.94283 1.000 15.15709 ? 302 VAL A CB  1 
ATOM   2459 C CG1 . VAL A 1 308 ? -2.89330  -3.75952  53.05813 1.000 13.68959 ? 302 VAL A CG1 1 
ATOM   2460 C CG2 . VAL A 1 308 ? -4.85615  -2.32499  53.70690 1.000 18.45950 ? 302 VAL A CG2 1 
ATOM   2461 N N   . GLU A 1 309 ? -3.28756  -5.32735  55.69418 1.000 12.75506 ? 303 GLU A N   1 
ATOM   2462 C CA  . GLU A 1 309 ? -3.97013  -6.54464  56.11877 1.000 15.91393 ? 303 GLU A CA  1 
ATOM   2463 C C   . GLU A 1 309 ? -3.98018  -6.68712  57.63571 1.000 18.21752 ? 303 GLU A C   1 
ATOM   2464 O O   . GLU A 1 309 ? -4.92923  -7.25227  58.19290 1.000 15.41463 ? 303 GLU A O   1 
ATOM   2465 C CB  . GLU A 1 309 ? -3.34383  -7.77293  55.45159 0.800 17.81280 ? 303 GLU A CB  1 
ATOM   2466 C CG  . GLU A 1 309 ? -3.69695  -7.89335  53.96551 0.700 15.90199 ? 303 GLU A CG  1 
ATOM   2467 C CD  . GLU A 1 309 ? -2.94306  -9.00136  53.24901 0.600 19.45531 ? 303 GLU A CD  1 
ATOM   2468 O OE1 . GLU A 1 309 ? -2.05125  -9.61931  53.86465 0.600 23.54283 ? 303 GLU A OE1 1 
ATOM   2469 O OE2 . GLU A 1 309 ? -3.25063  -9.25819  52.06558 0.600 26.81360 ? 303 GLU A OE2 1 
ATOM   2470 N N   . GLN A 1 310 ? -2.95473  -6.17586  58.32433 1.000 16.18979 ? 304 GLN A N   1 
ATOM   2471 C CA  . GLN A 1 310 ? -3.01580  -6.13530  59.78409 1.000 15.42439 ? 304 GLN A CA  1 
ATOM   2472 C C   . GLN A 1 310 ? -4.06415  -5.14365  60.26734 1.000 16.10149 ? 304 GLN A C   1 
ATOM   2473 O O   . GLN A 1 310 ? -4.77036  -5.40708  61.24872 1.000 13.99921 ? 304 GLN A O   1 
ATOM   2474 C CB  . GLN A 1 310 ? -1.66435  -5.75621  60.38366 1.000 17.88752 ? 304 GLN A CB  1 
ATOM   2475 C CG  . GLN A 1 310 ? -0.49839  -6.63431  60.04473 0.900 21.23546 ? 304 GLN A CG  1 
ATOM   2476 C CD  . GLN A 1 310 ? 0.79183   -6.06356  60.60144 0.700 17.49896 ? 304 GLN A CD  1 
ATOM   2477 O OE1 . GLN A 1 310 ? 1.33698   -5.09832  60.06837 0.700 16.77470 ? 304 GLN A OE1 1 
ATOM   2478 N NE2 . GLN A 1 310 ? 1.26746   -6.63736  61.70149 0.700 23.49222 ? 304 GLN A NE2 1 
ATOM   2479 N N   . ALA A 1 311 ? -4.15037  -3.98127  59.61567 1.000 14.02704 ? 305 ALA A N   1 
ATOM   2480 C CA  . ALA A 1 311 ? -5.12155  -2.97310  60.02597 1.000 16.50921 ? 305 ALA A CA  1 
ATOM   2481 C C   . ALA A 1 311 ? -6.54194  -3.51272  59.93666 1.000 18.45602 ? 305 ALA A C   1 
ATOM   2482 O O   . ALA A 1 311 ? -7.36148  -3.27931  60.83290 1.000 15.65274 ? 305 ALA A O   1 
ATOM   2483 C CB  . ALA A 1 311 ? -4.96587  -1.71634  59.16746 1.000 13.35701 ? 305 ALA A CB  1 
ATOM   2484 N N   . LEU A 1 312 ? -6.84588  -4.25221  58.86745 1.000 16.58479 ? 306 LEU A N   1 
ATOM   2485 C CA  . LEU A 1 312 ? -8.18109  -4.81711  58.71364 1.000 16.21254 ? 306 LEU A CA  1 
ATOM   2486 C C   . LEU A 1 312 ? -8.51520  -5.77825  59.84781 1.000 15.08131 ? 306 LEU A C   1 
ATOM   2487 O O   . LEU A 1 312 ? -9.67439  -5.86182  60.26815 1.000 17.05229 ? 306 LEU A O   1 
ATOM   2488 C CB  . LEU A 1 312 ? -8.29401  -5.51942  57.36005 1.000 15.68768 ? 306 LEU A CB  1 
ATOM   2489 C CG  . LEU A 1 312 ? -8.52494  -4.59147  56.16347 1.000 18.00453 ? 306 LEU A CG  1 
ATOM   2490 C CD1 . LEU A 1 312 ? -8.16391  -5.28269  54.85035 1.000 14.81473 ? 306 LEU A CD1 1 
ATOM   2491 C CD2 . LEU A 1 312 ? -9.96480  -4.08642  56.13090 1.000 15.06408 ? 306 LEU A CD2 1 
ATOM   2492 N N   . ALA A 1 313 ? -7.51707  -6.49087  60.36981 1.000 19.27173 ? 307 ALA A N   1 
ATOM   2493 C CA  . ALA A 1 313 ? -7.72242  -7.43557  61.45987 1.000 17.63950 ? 307 ALA A CA  1 
ATOM   2494 C C   . ALA A 1 313 ? -7.67408  -6.78078  62.83836 1.000 20.52940 ? 307 ALA A C   1 
ATOM   2495 O O   . ALA A 1 313 ? -7.72204  -7.49473  63.84662 1.000 18.00648 ? 307 ALA A O   1 
ATOM   2496 C CB  . ALA A 1 313 ? -6.68480  -8.55953  61.38183 1.000 23.53177 ? 307 ALA A CB  1 
ATOM   2497 N N   . HIS A 1 314 ? -7.58455  -5.45671  62.91228 1.000 17.23360 ? 308 HIS A N   1 
ATOM   2498 C CA  . HIS A 1 314 ? -7.52687  -4.79494  64.20884 1.000 18.44257 ? 308 HIS A CA  1 
ATOM   2499 C C   . HIS A 1 314 ? -8.88670  -4.88983  64.90229 1.000 21.22473 ? 308 HIS A C   1 
ATOM   2500 O O   . HIS A 1 314 ? -9.92636  -4.84475  64.23577 1.000 17.55431 ? 308 HIS A O   1 
ATOM   2501 C CB  . HIS A 1 314 ? -7.11426  -3.33075  64.04437 1.000 19.72369 ? 308 HIS A CB  1 
ATOM   2502 C CG  . HIS A 1 314 ? -6.78432  -2.64490  65.33432 1.000 22.53936 ? 308 HIS A CG  1 
ATOM   2503 N ND1 . HIS A 1 314 ? -7.74643  -2.08214  66.14486 1.000 19.13150 ? 308 HIS A ND1 1 
ATOM   2504 C CD2 . HIS A 1 314 ? -5.59884  -2.43453  65.95547 1.000 17.19305 ? 308 HIS A CD2 1 
ATOM   2505 C CE1 . HIS A 1 314 ? -7.16887  -1.55730  67.21163 1.000 20.89657 ? 308 HIS A CE1 1 
ATOM   2506 N NE2 . HIS A 1 314 ? -5.86590  -1.75635  67.12022 1.000 18.33464 ? 308 HIS A NE2 1 
ATOM   2507 N N   . PRO A 1 315 ? -8.91279  -5.03192  66.23278 1.000 19.34340 ? 309 PRO A N   1 
ATOM   2508 C CA  . PRO A 1 315 ? -10.20183 -5.16000  66.93812 1.000 18.72620 ? 309 PRO A CA  1 
ATOM   2509 C C   . PRO A 1 315 ? -11.16909 -4.01449  66.68978 1.000 20.37766 ? 309 PRO A C   1 
ATOM   2510 O O   . PRO A 1 315 ? -12.38285 -4.21421  66.82737 1.000 19.18552 ? 309 PRO A O   1 
ATOM   2511 C CB  . PRO A 1 315 ? -9.78535  -5.22363  68.41308 1.000 23.78801 ? 309 PRO A CB  1 
ATOM   2512 C CG  . PRO A 1 315 ? -8.41342  -5.81976  68.37795 1.000 24.79147 ? 309 PRO A CG  1 
ATOM   2513 C CD  . PRO A 1 315 ? -7.76796  -5.25874  67.13366 1.000 19.09312 ? 309 PRO A CD  1 
ATOM   2514 N N   . TYR A 1 316 ? -10.68040 -2.82265  66.33361 1.000 18.15921 ? 310 TYR A N   1 
ATOM   2515 C CA  . TYR A 1 316 ? -11.58896 -1.72175  66.02957 1.000 22.64318 ? 310 TYR A CA  1 
ATOM   2516 C C   . TYR A 1 316 ? -12.52330 -2.06651  64.87787 1.000 21.66670 ? 310 TYR A C   1 
ATOM   2517 O O   . TYR A 1 316 ? -13.66400 -1.58871  64.83643 1.000 20.40859 ? 310 TYR A O   1 
ATOM   2518 C CB  . TYR A 1 316 ? -10.79696 -0.45657  65.69720 1.000 16.31713 ? 310 TYR A CB  1 
ATOM   2519 C CG  . TYR A 1 316 ? -11.67940 0.73827   65.41660 1.000 19.70661 ? 310 TYR A CG  1 
ATOM   2520 C CD1 . TYR A 1 316 ? -12.61239 1.16875   66.35182 1.000 22.84371 ? 310 TYR A CD1 1 
ATOM   2521 C CD2 . TYR A 1 316 ? -11.59283 1.42535   64.21215 1.000 20.64460 ? 310 TYR A CD2 1 
ATOM   2522 C CE1 . TYR A 1 316 ? -13.42737 2.25521   66.10129 1.000 23.19132 ? 310 TYR A CE1 1 
ATOM   2523 C CE2 . TYR A 1 316 ? -12.40583 2.51698   63.95140 1.000 20.95952 ? 310 TYR A CE2 1 
ATOM   2524 C CZ  . TYR A 1 316 ? -13.32077 2.92582   64.90024 1.000 25.75778 ? 310 TYR A CZ  1 
ATOM   2525 O OH  . TYR A 1 316 ? -14.13208 4.00878   64.64700 1.000 22.23907 ? 310 TYR A OH  1 
ATOM   2526 N N   . LEU A 1 317 ? -12.06402 -2.90142  63.94543 1.000 18.44035 ? 311 LEU A N   1 
ATOM   2527 C CA  . LEU A 1 317 ? -12.80296 -3.23382  62.73641 1.000 21.56778 ? 311 LEU A CA  1 
ATOM   2528 C C   . LEU A 1 317 ? -13.44566 -4.61532  62.80607 1.000 18.97855 ? 311 LEU A C   1 
ATOM   2529 O O   . LEU A 1 317 ? -13.82170 -5.17120  61.76654 1.000 19.93691 ? 311 LEU A O   1 
ATOM   2530 C CB  . LEU A 1 317 ? -11.87220 -3.14453  61.52764 1.000 18.55205 ? 311 LEU A CB  1 
ATOM   2531 C CG  . LEU A 1 317 ? -11.27182 -1.76084  61.26683 1.000 15.66365 ? 311 LEU A CG  1 
ATOM   2532 C CD1 . LEU A 1 317 ? -10.38600 -1.79494  60.03716 1.000 19.00563 ? 311 LEU A CD1 1 
ATOM   2533 C CD2 . LEU A 1 317 ? -12.36575 -0.70536  61.12161 1.000 17.12528 ? 311 LEU A CD2 1 
ATOM   2534 N N   . GLU A 1 318 ? -13.59259 -5.16969  64.01252 1.000 15.83573 ? 312 GLU A N   1 
ATOM   2535 C CA  . GLU A 1 318 ? -14.03231 -6.55569  64.16059 1.000 20.22533 ? 312 GLU A CA  1 
ATOM   2536 C C   . GLU A 1 318 ? -15.44502 -6.77389  63.63450 1.000 25.78783 ? 312 GLU A C   1 
ATOM   2537 O O   . GLU A 1 318 ? -15.77809 -7.88243  63.19736 1.000 22.21593 ? 312 GLU A O   1 
ATOM   2538 C CB  . GLU A 1 318 ? -13.94747 -6.97415  65.62810 1.000 21.78732 ? 312 GLU A CB  1 
ATOM   2539 C CG  . GLU A 1 318 ? -14.00901 -8.47542  65.85178 0.800 36.21986 ? 312 GLU A CG  1 
ATOM   2540 C CD  . GLU A 1 318 ? -14.17692 -8.83603  67.31311 0.600 34.49506 ? 312 GLU A CD  1 
ATOM   2541 O OE1 . GLU A 1 318 ? -13.74134 -8.04325  68.17428 0.600 24.68704 ? 312 GLU A OE1 1 
ATOM   2542 O OE2 . GLU A 1 318 ? -14.75031 -9.90885  67.59989 0.600 41.53079 ? 312 GLU A OE2 1 
ATOM   2543 N N   . GLN A 1 319 ? -16.29004 -5.74201  63.67516 1.000 23.83959 ? 313 GLN A N   1 
ATOM   2544 C CA  . GLN A 1 319 ? -17.65911 -5.88241  63.18904 1.000 28.26397 ? 313 GLN A CA  1 
ATOM   2545 C C   . GLN A 1 319 ? -17.70974 -6.15843  61.69287 1.000 27.36849 ? 313 GLN A C   1 
ATOM   2546 O O   . GLN A 1 319 ? -18.69767 -6.72028  61.20905 1.000 22.59094 ? 313 GLN A O   1 
ATOM   2547 C CB  . GLN A 1 319 ? -18.45176 -4.61357  63.50766 1.000 22.41367 ? 313 GLN A CB  1 
ATOM   2548 C CG  . GLN A 1 319 ? -18.47366 -4.25480  64.98475 0.700 28.17806 ? 313 GLN A CG  1 
ATOM   2549 C CD  . GLN A 1 319 ? -19.06739 -2.88470  65.24383 0.600 29.85992 ? 313 GLN A CD  1 
ATOM   2550 O OE1 . GLN A 1 319 ? -18.47159 -1.86390  64.89687 0.600 21.42211 ? 313 GLN A OE1 1 
ATOM   2551 N NE2 . GLN A 1 319 ? -20.23852 -2.85311  65.86640 0.600 38.00597 ? 313 GLN A NE2 1 
ATOM   2552 N N   . TYR A 1 320 ? -16.66169 -5.78646  60.95474 1.000 19.91535 ? 314 TYR A N   1 
ATOM   2553 C CA  . TYR A 1 320 ? -16.66085 -5.83957  59.50141 1.000 20.75727 ? 314 TYR A CA  1 
ATOM   2554 C C   . TYR A 1 320 ? -15.64739 -6.81623  58.92497 1.000 28.17615 ? 314 TYR A C   1 
ATOM   2555 O O   . TYR A 1 320 ? -15.79218 -7.21864  57.76523 1.000 23.29993 ? 314 TYR A O   1 
ATOM   2556 C CB  . TYR A 1 320 ? -16.36611 -4.44311  58.93235 1.000 21.48987 ? 314 TYR A CB  1 
ATOM   2557 C CG  . TYR A 1 320 ? -17.42660 -3.41923  59.26132 1.000 26.84573 ? 314 TYR A CG  1 
ATOM   2558 C CD1 . TYR A 1 320 ? -18.67932 -3.46460  58.65961 1.000 29.54737 ? 314 TYR A CD1 1 
ATOM   2559 C CD2 . TYR A 1 320 ? -17.18405 -2.42203  60.19658 1.000 24.28630 ? 314 TYR A CD2 1 
ATOM   2560 C CE1 . TYR A 1 320 ? -19.65360 -2.53190  58.96878 1.000 26.16766 ? 314 TYR A CE1 1 
ATOM   2561 C CE2 . TYR A 1 320 ? -18.15187 -1.48870  60.51420 1.000 25.16388 ? 314 TYR A CE2 1 
ATOM   2562 C CZ  . TYR A 1 320 ? -19.38492 -1.54874  59.89662 1.000 24.01988 ? 314 TYR A CZ  1 
ATOM   2563 O OH  . TYR A 1 320 ? -20.35178 -0.62097  60.20953 1.000 29.74561 ? 314 TYR A OH  1 
ATOM   2564 N N   . TYR A 1 321 ? -14.64319 -7.20751  59.70491 1.000 19.58516 ? 315 TYR A N   1 
ATOM   2565 C CA  . TYR A 1 321 ? -13.49554 -7.93579  59.18195 1.000 21.63133 ? 315 TYR A CA  1 
ATOM   2566 C C   . TYR A 1 321 ? -13.90431 -9.30422  58.65159 1.000 23.61001 ? 315 TYR A C   1 
ATOM   2567 O O   . TYR A 1 321 ? -14.52678 -10.09845 59.36290 1.000 21.34303 ? 315 TYR A O   1 
ATOM   2568 C CB  . TYR A 1 321 ? -12.44545 -8.08334  60.28145 1.000 17.92316 ? 315 TYR A CB  1 
ATOM   2569 C CG  . TYR A 1 321 ? -11.20024 -8.83644  59.87983 1.000 21.20524 ? 315 TYR A CG  1 
ATOM   2570 C CD1 . TYR A 1 321 ? -10.48059 -8.47874  58.74847 1.000 21.58939 ? 315 TYR A CD1 1 
ATOM   2571 C CD2 . TYR A 1 321 ? -10.72930 -9.89190  60.65052 1.000 20.49283 ? 315 TYR A CD2 1 
ATOM   2572 C CE1 . TYR A 1 321 ? -9.33042  -9.16147  58.38746 1.000 20.26490 ? 315 TYR A CE1 1 
ATOM   2573 C CE2 . TYR A 1 321 ? -9.58025  -10.57855 60.30050 1.000 21.59651 ? 315 TYR A CE2 1 
ATOM   2574 C CZ  . TYR A 1 321 ? -8.88521  -10.21078 59.17011 1.000 19.60904 ? 315 TYR A CZ  1 
ATOM   2575 O OH  . TYR A 1 321 ? -7.74394  -10.89655 58.82146 1.000 18.30858 ? 315 TYR A OH  1 
ATOM   2576 N N   . ASP A 1 322 ? -13.54451 -9.57828  57.39852 1.000 20.88393 ? 316 ASP A N   1 
ATOM   2577 C CA  . ASP A 1 322 ? -13.81356 -10.86101 56.76268 1.000 23.76607 ? 316 ASP A CA  1 
ATOM   2578 C C   . ASP A 1 322 ? -12.85475 -11.02558 55.58747 1.000 28.12905 ? 316 ASP A C   1 
ATOM   2579 O O   . ASP A 1 322 ? -13.11136 -10.49790 54.49630 1.000 21.75239 ? 316 ASP A O   1 
ATOM   2580 C CB  . ASP A 1 322 ? -15.27582 -10.94392 56.31085 1.000 21.69003 ? 316 ASP A CB  1 
ATOM   2581 C CG  . ASP A 1 322 ? -15.60506 -12.24792 55.60151 0.800 22.60574 ? 316 ASP A CG  1 
ATOM   2582 O OD1 . ASP A 1 322 ? -14.75407 -13.16221 55.58037 0.700 20.28651 ? 316 ASP A OD1 1 
ATOM   2583 O OD2 . ASP A 1 322 ? -16.72761 -12.35630 55.06309 0.700 18.63088 ? 316 ASP A OD2 1 
ATOM   2584 N N   . PRO A 1 323 ? -11.74431 -11.74829 55.77361 1.000 22.67000 ? 317 PRO A N   1 
ATOM   2585 C CA  . PRO A 1 323 ? -10.72480 -11.82223 54.71107 1.000 24.89925 ? 317 PRO A CA  1 
ATOM   2586 C C   . PRO A 1 323 ? -11.23150 -12.41533 53.40793 1.000 20.93004 ? 317 PRO A C   1 
ATOM   2587 O O   . PRO A 1 323 ? -10.72505 -12.05240 52.33867 1.000 20.97129 ? 317 PRO A O   1 
ATOM   2588 C CB  . PRO A 1 323 ? -9.63426  -12.70274 55.33967 1.000 21.14179 ? 317 PRO A CB  1 
ATOM   2589 C CG  . PRO A 1 323 ? -9.81980  -12.54206 56.81682 1.000 25.99189 ? 317 PRO A CG  1 
ATOM   2590 C CD  . PRO A 1 323 ? -11.30447 -12.41587 57.01186 1.000 18.69238 ? 317 PRO A CD  1 
ATOM   2591 N N   . SER A 1 324 ? -12.20747 -13.32413 53.46168 1.000 19.94760 ? 318 SER A N   1 
ATOM   2592 C CA  . SER A 1 324 ? -12.78711 -13.89134 52.24789 1.000 23.14126 ? 318 SER A CA  1 
ATOM   2593 C C   . SER A 1 324 ? -13.65390 -12.89434 51.49371 1.000 21.99352 ? 318 SER A C   1 
ATOM   2594 O O   . SER A 1 324 ? -13.98527 -13.14190 50.32732 1.000 22.00618 ? 318 SER A O   1 
ATOM   2595 C CB  A SER A 1 324 ? -13.61028 -15.13428 52.58823 0.500 19.44420 ? 318 SER A CB  1 
ATOM   2596 C CB  B SER A 1 324 ? -13.61370 -15.13102 52.59081 0.500 19.44532 ? 318 SER A CB  1 
ATOM   2597 O OG  A SER A 1 324 ? -14.73025 -14.79915 53.38968 0.500 18.60623 ? 318 SER A OG  1 
ATOM   2598 O OG  B SER A 1 324 ? -12.97026 -15.91156 53.58107 0.500 24.19556 ? 318 SER A OG  1 
ATOM   2599 N N   . ASP A 1 325 ? -14.03696 -11.78825 52.13264 1.000 19.96047 ? 319 ASP A N   1 
ATOM   2600 C CA  . ASP A 1 325 ? -14.81237 -10.72957 51.50040 1.000 19.10408 ? 319 ASP A CA  1 
ATOM   2601 C C   . ASP A 1 325 ? -13.96903 -9.47744  51.28075 1.000 18.88761 ? 319 ASP A C   1 
ATOM   2602 O O   . ASP A 1 325 ? -14.50992 -8.37916  51.12641 1.000 18.51439 ? 319 ASP A O   1 
ATOM   2603 C CB  . ASP A 1 325 ? -16.05295 -10.41861 52.34223 1.000 25.52545 ? 319 ASP A CB  1 
ATOM   2604 C CG  . ASP A 1 325 ? -17.05872 -9.54046  51.61240 1.000 26.94059 ? 319 ASP A CG  1 
ATOM   2605 O OD1 . ASP A 1 325 ? -17.18584 -9.67480  50.37863 1.000 22.44116 ? 319 ASP A OD1 1 
ATOM   2606 O OD2 . ASP A 1 325 ? -17.71921 -8.71499  52.27701 1.000 26.42893 ? 319 ASP A OD2 1 
ATOM   2607 N N   . GLU A 1 326 ? -12.64498 -9.62859  51.27016 1.000 16.58747 ? 320 GLU A N   1 
ATOM   2608 C CA  . GLU A 1 326 ? -11.70605 -8.52485  51.08087 1.000 16.59622 ? 320 GLU A CA  1 
ATOM   2609 C C   . GLU A 1 326 ? -10.76057 -8.94591  49.96423 1.000 18.69541 ? 320 GLU A C   1 
ATOM   2610 O O   . GLU A 1 326 ? -9.61424  -9.34474  50.21408 1.000 17.29221 ? 320 GLU A O   1 
ATOM   2611 C CB  . GLU A 1 326 ? -10.98965 -8.19827  52.39377 1.000 19.95005 ? 320 GLU A CB  1 
ATOM   2612 C CG  . GLU A 1 326 ? -11.96408 -7.67129  53.44816 1.000 15.11506 ? 320 GLU A CG  1 
ATOM   2613 C CD  . GLU A 1 326 ? -11.48486 -7.83910  54.87778 1.000 20.96658 ? 320 GLU A CD  1 
ATOM   2614 O OE1 . GLU A 1 326 ? -10.31572 -8.22360  55.08647 1.000 18.94041 ? 320 GLU A OE1 1 
ATOM   2615 O OE2 . GLU A 1 326 ? -12.29298 -7.58480  55.79904 1.000 18.59261 ? 320 GLU A OE2 1 
ATOM   2616 N N   . PRO A 1 327 ? -11.21688 -8.87229  48.71471 1.000 16.54170 ? 321 PRO A N   1 
ATOM   2617 C CA  . PRO A 1 327 ? -10.49946 -9.53005  47.61611 1.000 19.86851 ? 321 PRO A CA  1 
ATOM   2618 C C   . PRO A 1 327 ? -9.22807  -8.79510  47.22320 1.000 18.79001 ? 321 PRO A C   1 
ATOM   2619 O O   . PRO A 1 327 ? -9.03857  -7.61002  47.50813 1.000 16.24764 ? 321 PRO A O   1 
ATOM   2620 C CB  . PRO A 1 327 ? -11.51378 -9.51003  46.46600 1.000 19.47978 ? 321 PRO A CB  1 
ATOM   2621 C CG  . PRO A 1 327 ? -12.43260 -8.37707  46.79459 1.000 22.79872 ? 321 PRO A CG  1 
ATOM   2622 C CD  . PRO A 1 327 ? -12.52537 -8.34613  48.28779 1.000 16.47807 ? 321 PRO A CD  1 
ATOM   2623 N N   . ILE A 1 328 ? -8.35739  -9.52982  46.53109 1.000 19.62648 ? 322 ILE A N   1 
ATOM   2624 C CA  . ILE A 1 328 ? -7.07804  -9.02012  46.06025 1.000 20.59860 ? 322 ILE A CA  1 
ATOM   2625 C C   . ILE A 1 328 ? -7.06227  -9.07969  44.53510 1.000 20.71694 ? 322 ILE A C   1 
ATOM   2626 O O   . ILE A 1 328 ? -7.93125  -9.68415  43.90381 1.000 20.70725 ? 322 ILE A O   1 
ATOM   2627 C CB  . ILE A 1 328 ? -5.88412  -9.79468  46.65283 1.000 17.81107 ? 322 ILE A CB  1 
ATOM   2628 C CG1 . ILE A 1 328 ? -5.95138  -11.26922 46.26223 1.000 20.73337 ? 322 ILE A CG1 1 
ATOM   2629 C CG2 . ILE A 1 328 ? -5.85021  -9.64161  48.17077 1.000 23.06664 ? 322 ILE A CG2 1 
ATOM   2630 C CD1 . ILE A 1 328 ? -4.69462  -12.04653 46.60889 1.000 22.17069 ? 322 ILE A CD1 1 
ATOM   2631 N N   . ALA A 1 329 ? -6.04511  -8.45005  43.94961 1.000 17.77476 ? 323 ALA A N   1 
ATOM   2632 C CA  . ALA A 1 329 ? -5.98995  -8.29237  42.50237 1.000 24.14214 ? 323 ALA A CA  1 
ATOM   2633 C C   . ALA A 1 329 ? -5.61445  -9.59936  41.81697 1.000 26.82620 ? 323 ALA A C   1 
ATOM   2634 O O   . ALA A 1 329 ? -4.78044  -10.36457 42.30794 1.000 24.78351 ? 323 ALA A O   1 
ATOM   2635 C CB  . ALA A 1 329 ? -4.99118  -7.19964  42.12146 1.000 24.38341 ? 323 ALA A CB  1 
ATOM   2636 N N   . GLU A 1 330 ? -6.24758  -9.84877  40.66953 1.000 19.80157 ? 324 GLU A N   1 
ATOM   2637 C CA  . GLU A 1 330 ? -5.91741  -11.01794 39.86322 1.000 28.68358 ? 324 GLU A CA  1 
ATOM   2638 C C   . GLU A 1 330 ? -4.54683  -10.86805 39.21477 1.000 38.04328 ? 324 GLU A C   1 
ATOM   2639 O O   . GLU A 1 330 ? -3.70973  -11.77526 39.28864 1.000 44.69068 ? 324 GLU A O   1 
ATOM   2640 C CB  . GLU A 1 330 ? -6.99578  -11.22838 38.79809 1.000 33.60474 ? 324 GLU A CB  1 
ATOM   2641 C CG  . GLU A 1 330 ? -6.64455  -12.25167 37.73253 0.700 38.49458 ? 324 GLU A CG  1 
ATOM   2642 C CD  . GLU A 1 330 ? -7.81075  -12.54782 36.80920 0.600 45.18346 ? 324 GLU A CD  1 
ATOM   2643 O OE1 . GLU A 1 330 ? -7.97836  -13.71932 36.41059 0.600 45.16934 ? 324 GLU A OE1 1 
ATOM   2644 O OE2 . GLU A 1 330 ? -8.56287  -11.60350 36.48536 0.600 32.38456 ? 324 GLU A OE2 1 
ATOM   2645 N N   . ALA A 1 331 ? -4.29812  -9.72297  38.57692 1.000 39.18433 ? 325 ALA A N   1 
ATOM   2646 C CA  . ALA A 1 331 ? -3.07270  -9.47579  37.81869 1.000 44.65374 ? 325 ALA A CA  1 
ATOM   2647 C C   . ALA A 1 331 ? -2.36297  -8.25138  38.38160 1.000 43.97157 ? 325 ALA A C   1 
ATOM   2648 O O   . ALA A 1 331 ? -2.63967  -7.11549  37.96390 1.000 41.10534 ? 325 ALA A O   1 
ATOM   2649 C CB  . ALA A 1 331 ? -3.38182  -9.29215  36.33396 1.000 46.20832 ? 325 ALA A CB  1 
ATOM   2650 N N   . PRO A 1 332 ? -1.44317  -8.43096  39.32908 1.000 33.93543 ? 326 PRO A N   1 
ATOM   2651 C CA  . PRO A 1 332 ? -0.66873  -7.28932  39.83022 1.000 41.00838 ? 326 PRO A CA  1 
ATOM   2652 C C   . PRO A 1 332 ? 0.21853   -6.69819  38.74262 1.000 37.05591 ? 326 PRO A C   1 
ATOM   2653 O O   . PRO A 1 332 ? 0.52074   -7.33397  37.72988 1.000 31.83940 ? 326 PRO A O   1 
ATOM   2654 C CB  . PRO A 1 332 ? 0.17055   -7.88573  40.96916 1.000 35.99892 ? 326 PRO A CB  1 
ATOM   2655 C CG  . PRO A 1 332 ? 0.10576   -9.36158  40.80215 1.000 46.90155 ? 326 PRO A CG  1 
ATOM   2656 C CD  . PRO A 1 332 ? -1.11055  -9.69602  40.00485 1.000 34.37793 ? 326 PRO A CD  1 
ATOM   2657 N N   . PHE A 1 333 ? 0.63257   -5.45227  38.96239 1.000 24.99384 ? 327 PHE A N   1 
ATOM   2658 C CA  . PHE A 1 333 ? 1.50576   -4.75310  38.02922 1.000 33.74266 ? 327 PHE A CA  1 
ATOM   2659 C C   . PHE A 1 333 ? 2.95665   -5.08820  38.34753 1.000 42.86240 ? 327 PHE A C   1 
ATOM   2660 O O   . PHE A 1 333 ? 3.38437   -4.98520  39.50165 1.000 45.35900 ? 327 PHE A O   1 
ATOM   2661 C CB  . PHE A 1 333 ? 1.27941   -3.24239  38.09798 1.000 34.75631 ? 327 PHE A CB  1 
ATOM   2662 C CG  . PHE A 1 333 ? 0.03900   -2.78191  37.38325 1.000 31.95516 ? 327 PHE A CG  1 
ATOM   2663 C CD1 . PHE A 1 333 ? 0.10007   -2.35384  36.06634 1.000 45.59497 ? 327 PHE A CD1 1 
ATOM   2664 C CD2 . PHE A 1 333 ? -1.18555  -2.77179  38.02980 1.000 33.19760 ? 327 PHE A CD2 1 
ATOM   2665 C CE1 . PHE A 1 333 ? -1.04406  -1.92890  35.40403 1.000 37.30673 ? 327 PHE A CE1 1 
ATOM   2666 C CE2 . PHE A 1 333 ? -2.32908  -2.34802  37.37833 1.000 34.69281 ? 327 PHE A CE2 1 
ATOM   2667 C CZ  . PHE A 1 333 ? -2.26004  -1.92662  36.06296 1.000 27.67290 ? 327 PHE A CZ  1 
ATOM   2668 N N   . LYS A 1 334 ? 3.70961   -5.49010  37.32145 0.700 48.53737 ? 328 LYS A N   1 
ATOM   2669 C CA  . LYS A 1 334 ? 5.08615   -5.92612  37.53211 0.700 46.92864 ? 328 LYS A CA  1 
ATOM   2670 C C   . LYS A 1 334 ? 6.03598   -4.74057  37.65273 0.700 56.62580 ? 328 LYS A C   1 
ATOM   2671 O O   . LYS A 1 334 ? 6.85326   -4.68101  38.57821 0.700 52.57070 ? 328 LYS A O   1 
ATOM   2672 C CB  . LYS A 1 334 ? 5.52254   -6.84887  36.39283 0.700 49.67669 ? 328 LYS A CB  1 
ATOM   2673 N N   . PHE A 1 335 ? 5.94882   -3.79433  36.72233 0.700 49.69148 ? 329 PHE A N   1 
ATOM   2674 C CA  . PHE A 1 335 ? 6.78575   -2.60470  36.74835 0.700 39.00370 ? 329 PHE A CA  1 
ATOM   2675 C C   . PHE A 1 335 ? 6.02137   -1.46590  36.08737 0.700 47.84487 ? 329 PHE A C   1 
ATOM   2676 O O   . PHE A 1 335 ? 4.88378   -1.63257  35.63802 0.700 46.42507 ? 329 PHE A O   1 
ATOM   2677 C CB  . PHE A 1 335 ? 8.13002   -2.85804  36.05859 0.600 39.25641 ? 329 PHE A CB  1 
ATOM   2678 N N   . ASP A 1 336 ? 6.65818   -0.30102  36.03075 0.700 54.94284 ? 330 ASP A N   1 
ATOM   2679 C CA  . ASP A 1 336 ? 6.05190   0.87546   35.41814 0.700 62.89426 ? 330 ASP A CA  1 
ATOM   2680 C C   . ASP A 1 336 ? 5.81920   0.66297   33.92488 0.700 57.70507 ? 330 ASP A C   1 
ATOM   2681 O O   . ASP A 1 336 ? 6.29177   1.43977   33.09508 0.700 68.65159 ? 330 ASP A O   1 
ATOM   2682 C CB  . ASP A 1 336 ? 6.93000   2.10765   35.64142 0.700 64.46812 ? 330 ASP A CB  1 
ATOM   2683 N N   . PRO A 1 343 ? 8.37920   11.01777  24.76364 1.000 53.95591 ? 337 PRO A N   1 
ATOM   2684 C CA  . PRO A 1 343 ? 7.79956   12.32976  24.45206 1.000 49.94583 ? 337 PRO A CA  1 
ATOM   2685 C C   . PRO A 1 343 ? 6.27710   12.33450  24.54834 1.000 58.54155 ? 337 PRO A C   1 
ATOM   2686 O O   . PRO A 1 343 ? 5.66052   11.26845  24.57217 1.000 45.26630 ? 337 PRO A O   1 
ATOM   2687 C CB  . PRO A 1 343 ? 8.25425   12.58584  23.00900 1.000 57.90662 ? 337 PRO A CB  1 
ATOM   2688 C CG  . PRO A 1 343 ? 8.58026   11.23718  22.45911 1.000 56.04994 ? 337 PRO A CG  1 
ATOM   2689 C CD  . PRO A 1 343 ? 9.10734   10.44923  23.61675 1.000 50.54480 ? 337 PRO A CD  1 
ATOM   2690 N N   . LYS A 1 344 ? 5.68195   13.52928  24.59971 1.000 49.85930 ? 338 LYS A N   1 
ATOM   2691 C CA  . LYS A 1 344 ? 4.23244   13.63041  24.72088 1.000 53.52188 ? 338 LYS A CA  1 
ATOM   2692 C C   . LYS A 1 344 ? 3.51517   13.06835  23.50171 1.000 49.30857 ? 338 LYS A C   1 
ATOM   2693 O O   . LYS A 1 344 ? 2.35646   12.65299  23.61507 1.000 53.32229 ? 338 LYS A O   1 
ATOM   2694 C CB  . LYS A 1 344 ? 3.81809   15.08678  24.93479 0.900 49.39182 ? 338 LYS A CB  1 
ATOM   2695 C CG  . LYS A 1 344 ? 4.45584   16.05989  23.95959 0.800 45.82682 ? 338 LYS A CG  1 
ATOM   2696 C CD  . LYS A 1 344 ? 3.77114   17.41596  24.00924 0.700 50.37114 ? 338 LYS A CD  1 
ATOM   2697 C CE  . LYS A 1 344 ? 4.03928   18.21794  22.74606 0.600 53.16827 ? 338 LYS A CE  1 
ATOM   2698 N NZ  . LYS A 1 344 ? 5.41983   18.00423  22.23532 0.600 43.00235 ? 338 LYS A NZ  1 
ATOM   2699 N N   . GLU A 1 345 ? 4.17432   13.05177  22.33972 1.000 39.19333 ? 339 GLU A N   1 
ATOM   2700 C CA  . GLU A 1 345 ? 3.55658   12.49036  21.14256 1.000 53.98445 ? 339 GLU A CA  1 
ATOM   2701 C C   . GLU A 1 345 ? 3.36056   10.98703  21.28074 1.000 48.86708 ? 339 GLU A C   1 
ATOM   2702 O O   . GLU A 1 345 ? 2.30395   10.45612  20.91831 1.000 42.83489 ? 339 GLU A O   1 
ATOM   2703 C CB  . GLU A 1 345 ? 4.40890   12.80622  19.91365 1.000 53.83808 ? 339 GLU A CB  1 
ATOM   2704 C CG  . GLU A 1 345 ? 4.43445   14.27504  19.52677 0.700 45.41628 ? 339 GLU A CG  1 
ATOM   2705 C CD  . GLU A 1 345 ? 5.45545   15.06293  20.32036 0.600 50.71543 ? 339 GLU A CD  1 
ATOM   2706 O OE1 . GLU A 1 345 ? 6.41255   14.44567  20.83257 0.600 42.74296 ? 339 GLU A OE1 1 
ATOM   2707 O OE2 . GLU A 1 345 ? 5.30219   16.29763  20.42899 0.600 54.16444 ? 339 GLU A OE2 1 
ATOM   2708 N N   . LYS A 1 346 ? 4.37086   10.28467  21.79741 1.000 37.52210 ? 340 LYS A N   1 
ATOM   2709 C CA  . LYS A 1 346 ? 4.21931   8.85849   22.05657 1.000 47.02471 ? 340 LYS A CA  1 
ATOM   2710 C C   . LYS A 1 346 ? 3.18646   8.60527   23.14763 1.000 47.51850 ? 340 LYS A C   1 
ATOM   2711 O O   . LYS A 1 346 ? 2.47367   7.59640   23.10520 1.000 40.98140 ? 340 LYS A O   1 
ATOM   2712 C CB  . LYS A 1 346 ? 5.56488   8.25047   22.45478 0.800 39.07249 ? 340 LYS A CB  1 
ATOM   2713 C CG  . LYS A 1 346 ? 6.51227   7.97701   21.29076 0.700 47.46041 ? 340 LYS A CG  1 
ATOM   2714 C CD  . LYS A 1 346 ? 6.08623   6.77802   20.45824 0.600 43.29371 ? 340 LYS A CD  1 
ATOM   2715 C CE  . LYS A 1 346 ? 6.60756   6.89545   19.03220 0.600 46.39630 ? 340 LYS A CE  1 
ATOM   2716 N NZ  . LYS A 1 346 ? 5.58408   6.50912   18.02341 0.600 48.77621 ? 340 LYS A NZ  1 
ATOM   2717 N N   . LEU A 1 347 ? 3.08758   9.51253   24.12288 1.000 46.67624 ? 341 LEU A N   1 
ATOM   2718 C CA  . LEU A 1 347 ? 2.14602   9.33336   25.22360 1.000 36.13730 ? 341 LEU A CA  1 
ATOM   2719 C C   . LEU A 1 347 ? 0.71128   9.55894   24.75988 1.000 42.21330 ? 341 LEU A C   1 
ATOM   2720 O O   . LEU A 1 347 ? -0.19180  8.78962   25.11003 1.000 40.03343 ? 341 LEU A O   1 
ATOM   2721 C CB  . LEU A 1 347 ? 2.50260   10.27923  26.36843 1.000 36.83396 ? 341 LEU A CB  1 
ATOM   2722 C CG  . LEU A 1 347 ? 3.80480   9.97654   27.11691 1.000 47.31931 ? 341 LEU A CG  1 
ATOM   2723 C CD1 . LEU A 1 347 ? 4.11112   11.07104  28.12739 1.000 37.53834 ? 341 LEU A CD1 1 
ATOM   2724 C CD2 . LEU A 1 347 ? 3.74222   8.61485   27.79823 1.000 34.53808 ? 341 LEU A CD2 1 
ATOM   2725 N N   . LYS A 1 348 ? 0.48051   10.62450  23.98461 1.000 42.47313 ? 342 LYS A N   1 
ATOM   2726 C CA  . LYS A 1 348 ? -0.81292  10.80653  23.33034 1.000 33.66925 ? 342 LYS A CA  1 
ATOM   2727 C C   . LYS A 1 348 ? -1.19633  9.57249   22.53100 1.000 33.87756 ? 342 LYS A C   1 
ATOM   2728 O O   . LYS A 1 348 ? -2.34348  9.11216   22.58560 1.000 30.93164 ? 342 LYS A O   1 
ATOM   2729 C CB  . LYS A 1 348 ? -0.77359  12.03129  22.41471 1.000 35.96336 ? 342 LYS A CB  1 
ATOM   2730 C CG  . LYS A 1 348 ? -2.07159  12.27927  21.65820 1.000 33.26847 ? 342 LYS A CG  1 
ATOM   2731 C CD  . LYS A 1 348 ? -2.10447  13.65618  21.01241 1.000 33.14919 ? 342 LYS A CD  1 
ATOM   2732 C CE  . LYS A 1 348 ? -3.46157  13.92412  20.38133 1.000 33.77819 ? 342 LYS A CE  1 
ATOM   2733 N NZ  . LYS A 1 348 ? -3.54306  15.26935  19.75459 1.000 36.89267 ? 342 LYS A NZ  1 
ATOM   2734 N N   . GLU A 1 349 ? -0.23683  9.02105   21.78799 1.000 32.40059 ? 343 GLU A N   1 
ATOM   2735 C CA  . GLU A 1 349 ? -0.48736  7.82937   20.98656 1.000 36.90084 ? 343 GLU A CA  1 
ATOM   2736 C C   . GLU A 1 349 ? -0.87629  6.64498   21.86240 1.000 39.76765 ? 343 GLU A C   1 
ATOM   2737 O O   . GLU A 1 349 ? -1.75299  5.85172   21.49801 1.000 37.92822 ? 343 GLU A O   1 
ATOM   2738 C CB  . GLU A 1 349 ? 0.75598   7.52086   20.15245 1.000 40.24255 ? 343 GLU A CB  1 
ATOM   2739 C CG  . GLU A 1 349 ? 0.68701   6.28544   19.28411 1.000 45.47760 ? 343 GLU A CG  1 
ATOM   2740 C CD  . GLU A 1 349 ? 1.89453   6.17899   18.37183 0.800 59.90786 ? 343 GLU A CD  1 
ATOM   2741 O OE1 . GLU A 1 349 ? 2.10771   5.09977   17.78263 0.800 56.67325 ? 343 GLU A OE1 1 
ATOM   2742 O OE2 . GLU A 1 349 ? 2.63672   7.17917   18.25166 0.800 53.66235 ? 343 GLU A OE2 1 
ATOM   2743 N N   . LEU A 1 350 ? -0.24872  6.51897   23.03136 1.000 34.74855 ? 344 LEU A N   1 
ATOM   2744 C CA  . LEU A 1 350 ? -0.58749  5.43535   23.94613 1.000 34.08512 ? 344 LEU A CA  1 
ATOM   2745 C C   . LEU A 1 350 ? -1.91348  5.68260   24.65490 1.000 28.10931 ? 344 LEU A C   1 
ATOM   2746 O O   . LEU A 1 350 ? -2.65453  4.72920   24.92339 1.000 32.10692 ? 344 LEU A O   1 
ATOM   2747 C CB  . LEU A 1 350 ? 0.53358   5.24568   24.96460 1.000 33.85526 ? 344 LEU A CB  1 
ATOM   2748 C CG  . LEU A 1 350 ? 1.83996   4.71377   24.36947 1.000 34.99224 ? 344 LEU A CG  1 
ATOM   2749 C CD1 . LEU A 1 350 ? 2.96965   4.75285   25.39254 1.000 34.37559 ? 344 LEU A CD1 1 
ATOM   2750 C CD2 . LEU A 1 350 ? 1.64803   3.30927   23.81824 1.000 33.61123 ? 344 LEU A CD2 1 
ATOM   2751 N N   . ILE A 1 351 ? -2.22644  6.94302   24.96571 1.000 27.34465 ? 345 ILE A N   1 
ATOM   2752 C CA  . ILE A 1 351 ? -3.53817  7.26922   25.51972 1.000 25.69530 ? 345 ILE A CA  1 
ATOM   2753 C C   . ILE A 1 351 ? -4.62942  6.94456   24.50927 1.000 27.59766 ? 345 ILE A C   1 
ATOM   2754 O O   . ILE A 1 351 ? -5.66810  6.36414   24.85264 1.000 32.62481 ? 345 ILE A O   1 
ATOM   2755 C CB  . ILE A 1 351 ? -3.57946  8.74915   25.94613 1.000 26.81497 ? 345 ILE A CB  1 
ATOM   2756 C CG1 . ILE A 1 351 ? -2.66806  8.98515   27.15348 1.000 27.72611 ? 345 ILE A CG1 1 
ATOM   2757 C CG2 . ILE A 1 351 ? -5.00738  9.19378   26.23672 1.000 23.98635 ? 345 ILE A CG2 1 
ATOM   2758 C CD1 . ILE A 1 351 ? -2.54373  10.44383  27.54493 1.000 27.09983 ? 345 ILE A CD1 1 
ATOM   2759 N N   . PHE A 1 352 ? -4.40784  7.31530   23.24738 1.000 30.09142 ? 346 PHE A N   1 
ATOM   2760 C CA  . PHE A 1 352 ? -5.33903  6.96431   22.18058 1.000 26.81690 ? 346 PHE A CA  1 
ATOM   2761 C C   . PHE A 1 352 ? -5.53879  5.45530   22.10402 1.000 30.55740 ? 346 PHE A C   1 
ATOM   2762 O O   . PHE A 1 352 ? -6.67329  4.96701   22.02526 1.000 28.50468 ? 346 PHE A O   1 
ATOM   2763 C CB  . PHE A 1 352 ? -4.81336  7.50692   20.85254 1.000 31.00729 ? 346 PHE A CB  1 
ATOM   2764 C CG  . PHE A 1 352 ? -5.73670  7.28514   19.68949 1.000 28.61851 ? 346 PHE A CG  1 
ATOM   2765 C CD1 . PHE A 1 352 ? -6.78770  8.15420   19.44503 1.000 31.49672 ? 346 PHE A CD1 1 
ATOM   2766 C CD2 . PHE A 1 352 ? -5.53911  6.21858   18.82933 1.000 29.96494 ? 346 PHE A CD2 1 
ATOM   2767 C CE1 . PHE A 1 352 ? -7.63224  7.96005   18.36199 1.000 29.09852 ? 346 PHE A CE1 1 
ATOM   2768 C CE2 . PHE A 1 352 ? -6.37942  6.01697   17.74654 1.000 34.72904 ? 346 PHE A CE2 1 
ATOM   2769 C CZ  . PHE A 1 352 ? -7.42935  6.88893   17.51429 1.000 29.96216 ? 346 PHE A CZ  1 
ATOM   2770 N N   . GLU A 1 353 ? -4.43743  4.70044   22.12696 1.000 28.25042 ? 347 GLU A N   1 
ATOM   2771 C CA  . GLU A 1 353 ? -4.52156  3.24533   22.05644 1.000 29.60326 ? 347 GLU A CA  1 
ATOM   2772 C C   . GLU A 1 353 ? -5.24882  2.66920   23.26480 1.000 27.38110 ? 347 GLU A C   1 
ATOM   2773 O O   . GLU A 1 353 ? -6.09322  1.77715   23.12183 1.000 37.77155 ? 347 GLU A O   1 
ATOM   2774 C CB  . GLU A 1 353 ? -3.11684  2.64998   21.94528 1.000 40.69878 ? 347 GLU A CB  1 
ATOM   2775 C CG  . GLU A 1 353 ? -2.52275  2.68991   20.54600 1.000 45.68865 ? 347 GLU A CG  1 
ATOM   2776 C CD  . GLU A 1 353 ? -1.52735  1.56903   20.30300 0.800 53.99644 ? 347 GLU A CD  1 
ATOM   2777 O OE1 . GLU A 1 353 ? -1.27716  0.77940   21.23861 0.700 62.73751 ? 347 GLU A OE1 1 
ATOM   2778 O OE2 . GLU A 1 353 ? -0.99490  1.47731   19.17709 0.700 58.20156 ? 347 GLU A OE2 1 
ATOM   2779 N N   . GLU A 1 354 ? -4.93909  3.16963   24.46477 1.000 31.41599 ? 348 GLU A N   1 
ATOM   2780 C CA  . GLU A 1 354 ? -5.51317  2.60817   25.68249 1.000 29.84266 ? 348 GLU A CA  1 
ATOM   2781 C C   . GLU A 1 354 ? -7.00809  2.87531   25.80137 1.000 35.66167 ? 348 GLU A C   1 
ATOM   2782 O O   . GLU A 1 354 ? -7.70306  2.13324   26.50430 1.000 28.87159 ? 348 GLU A O   1 
ATOM   2783 C CB  . GLU A 1 354 ? -4.79428  3.16668   26.91328 1.000 30.85642 ? 348 GLU A CB  1 
ATOM   2784 C CG  . GLU A 1 354 ? -3.44505  2.52267   27.20351 0.800 37.73940 ? 348 GLU A CG  1 
ATOM   2785 C CD  . GLU A 1 354 ? -3.55632  1.05657   27.56698 0.750 35.82226 ? 348 GLU A CD  1 
ATOM   2786 O OE1 . GLU A 1 354 ? -4.29792  0.73162   28.51747 0.750 32.05900 ? 348 GLU A OE1 1 
ATOM   2787 O OE2 . GLU A 1 354 ? -2.89360  0.22954   26.90611 0.750 49.74995 ? 348 GLU A OE2 1 
ATOM   2788 N N   . THR A 1 355 ? -7.51617  3.91177   25.13833 1.000 35.93805 ? 349 THR A N   1 
ATOM   2789 C CA  . THR A 1 355 ? -8.92617  4.27032   25.20223 1.000 33.88372 ? 349 THR A CA  1 
ATOM   2790 C C   . THR A 1 355 ? -9.71897  3.73502   24.01721 1.000 31.63810 ? 349 THR A C   1 
ATOM   2791 O O   . THR A 1 355 ? -10.90599 4.05067   23.88336 1.000 33.51616 ? 349 THR A O   1 
ATOM   2792 C CB  . THR A 1 355 ? -9.07750  5.79158   25.28432 1.000 28.83353 ? 349 THR A CB  1 
ATOM   2793 O OG1 . THR A 1 355 ? -8.43992  6.39635   24.15301 1.000 26.04904 ? 349 THR A OG1 1 
ATOM   2794 C CG2 . THR A 1 355 ? -8.42884  6.31957   26.55452 1.000 25.54000 ? 349 THR A CG2 1 
ATOM   2795 N N   . ALA A 1 356 ? -9.09299  2.92101   23.16472 1.000 31.86667 ? 350 ALA A N   1 
ATOM   2796 C CA  . ALA A 1 356 ? -9.74219  2.48353   21.93481 1.000 27.35489 ? 350 ALA A CA  1 
ATOM   2797 C C   . ALA A 1 356 ? -10.94055 1.57997   22.19999 1.000 36.95691 ? 350 ALA A C   1 
ATOM   2798 O O   . ALA A 1 356 ? -11.86538 1.53025   21.37985 1.000 40.32570 ? 350 ALA A O   1 
ATOM   2799 C CB  . ALA A 1 356 ? -8.73209  1.76781   21.03934 1.000 37.10709 ? 350 ALA A CB  1 
ATOM   2800 N N   . ARG A 1 357 ? -10.95225 0.86623   23.32945 1.000 36.94273 ? 351 ARG A N   1 
ATOM   2801 C CA  . ARG A 1 357 ? -12.00198 -0.11907  23.56711 1.000 41.41916 ? 351 ARG A CA  1 
ATOM   2802 C C   . ARG A 1 357 ? -13.37448 0.51584   23.74918 1.000 33.16731 ? 351 ARG A C   1 
ATOM   2803 O O   . ARG A 1 357 ? -14.38619 -0.18101  23.61607 1.000 36.69306 ? 351 ARG A O   1 
ATOM   2804 C CB  . ARG A 1 357 ? -11.67229 -0.97337  24.79412 0.800 41.24485 ? 351 ARG A CB  1 
ATOM   2805 C CG  . ARG A 1 357 ? -11.04542 -0.21884  25.95513 0.700 46.37780 ? 351 ARG A CG  1 
ATOM   2806 C CD  . ARG A 1 357 ? -10.99697 -1.10131  27.19598 0.700 41.82543 ? 351 ARG A CD  1 
ATOM   2807 N NE  . ARG A 1 357 ? -9.73686  -1.82587  27.31184 0.600 42.60208 ? 351 ARG A NE  1 
ATOM   2808 C CZ  . ARG A 1 357 ? -9.19822  -2.21258  28.46039 0.600 44.69680 ? 351 ARG A CZ  1 
ATOM   2809 N NH1 . ARG A 1 357 ? -9.80611  -1.99863  29.61537 0.600 45.00984 ? 351 ARG A NH1 1 
ATOM   2810 N NH2 . ARG A 1 357 ? -8.02407  -2.83683  28.44904 0.600 44.66135 ? 351 ARG A NH2 1 
ATOM   2811 N N   . PHE A 1 358 ? -13.43728 1.81155   24.04245 1.000 29.33108 ? 352 PHE A N   1 
ATOM   2812 C CA  . PHE A 1 358 ? -14.70536 2.48122   24.29661 1.000 34.46486 ? 352 PHE A CA  1 
ATOM   2813 C C   . PHE A 1 358 ? -15.29348 3.13338   23.05310 1.000 30.49604 ? 352 PHE A C   1 
ATOM   2814 O O   . PHE A 1 358 ? -16.34854 3.76920   23.14559 1.000 39.66541 ? 352 PHE A O   1 
ATOM   2815 C CB  . PHE A 1 358 ? -14.53429 3.52321   25.40598 1.000 21.55087 ? 352 PHE A CB  1 
ATOM   2816 C CG  . PHE A 1 358 ? -14.15078 2.92987   26.73455 1.000 29.85937 ? 352 PHE A CG  1 
ATOM   2817 C CD1 . PHE A 1 358 ? -15.11966 2.44727   27.59968 1.000 25.05121 ? 352 PHE A CD1 1 
ATOM   2818 C CD2 . PHE A 1 358 ? -12.82078 2.84910   27.11393 1.000 30.67364 ? 352 PHE A CD2 1 
ATOM   2819 C CE1 . PHE A 1 358 ? -14.77006 1.89743   28.82113 1.000 30.90100 ? 352 PHE A CE1 1 
ATOM   2820 C CE2 . PHE A 1 358 ? -12.46273 2.30120   28.33447 1.000 33.06580 ? 352 PHE A CE2 1 
ATOM   2821 C CZ  . PHE A 1 358 ? -13.43882 1.82480   29.18974 1.000 36.54015 ? 352 PHE A CZ  1 
ATOM   2822 N N   . GLN A 1 359 ? -14.63292 2.98913   21.88333 1.000 31.42867 ? 353 GLN A N   1 
ATOM   2823 C CA  . GLN A 1 359 ? -15.14125 3.41914   20.58992 1.000 40.45661 ? 353 GLN A CA  1 
ATOM   2824 C C   . GLN A 1 359 ? -15.96882 2.31354   19.94076 1.000 34.06617 ? 353 GLN A C   1 
ATOM   2825 O O   . GLN A 1 359 ? -15.68479 1.12587   20.13128 1.000 44.36820 ? 353 GLN A O   1 
ATOM   2826 C CB  . GLN A 1 359 ? -13.99085 3.80227   19.66177 1.000 38.56302 ? 353 GLN A CB  1 
ATOM   2827 C CG  . GLN A 1 359 ? -13.10343 4.91674   20.18682 1.000 29.44527 ? 353 GLN A CG  1 
ATOM   2828 C CD  . GLN A 1 359 ? -13.80324 6.26208   20.16475 1.000 32.46270 ? 353 GLN A CD  1 
ATOM   2829 O OE1 . GLN A 1 359 ? -14.37966 6.65692   19.14804 1.000 29.93561 ? 353 GLN A OE1 1 
ATOM   2830 N NE2 . GLN A 1 359 ? -13.76148 6.97148   21.28493 1.000 27.84820 ? 353 GLN A NE2 1 
ATOM   2831 N N   . PRO A 1 360 ? -17.01737 2.68996   19.18775 0.700 52.10414 ? 354 PRO A N   1 
ATOM   2832 C CA  . PRO A 1 360 ? -17.88625 1.84647   18.37004 0.700 50.80327 ? 354 PRO A CA  1 
ATOM   2833 C C   . PRO A 1 360 ? -17.19948 0.61485   17.78137 0.700 51.46501 ? 354 PRO A C   1 
ATOM   2834 O O   . PRO A 1 360 ? -16.90662 0.61317   16.58552 0.700 55.16816 ? 354 PRO A O   1 
ATOM   2835 C CB  . PRO A 1 360 ? -18.30352 2.81199   17.25933 0.700 43.20507 ? 354 PRO A CB  1 
ATOM   2836 C CG  . PRO A 1 360 ? -18.30828 4.20105   17.96324 0.700 54.02242 ? 354 PRO A CG  1 
ATOM   2837 C CD  . PRO A 1 360 ? -17.64990 4.00951   19.33201 0.700 42.00125 ? 354 PRO A CD  1 
HETATM 2838 S S   A SO4 B 2 .   ? 3.62138   21.59778  49.55647 0.500 22.90017 ? 401 SO4 A S   1 
HETATM 2839 S S   B SO4 B 2 .   ? 5.55695   21.50609  48.83926 0.500 35.55170 ? 401 SO4 A S   1 
HETATM 2840 O O1  A SO4 B 2 .   ? 4.40224   22.74465  49.10185 0.500 26.96982 ? 401 SO4 A O1  1 
HETATM 2841 O O1  B SO4 B 2 .   ? 6.55508   22.56439  48.96599 0.500 30.15308 ? 401 SO4 A O1  1 
HETATM 2842 O O2  A SO4 B 2 .   ? 3.94321   20.43289  48.73635 0.500 19.36064 ? 401 SO4 A O2  1 
HETATM 2843 O O2  B SO4 B 2 .   ? 6.04644   20.49234  47.90948 0.500 38.21141 ? 401 SO4 A O2  1 
HETATM 2844 O O3  A SO4 B 2 .   ? 2.19913   21.90103  49.43657 0.500 20.47937 ? 401 SO4 A O3  1 
HETATM 2845 O O3  B SO4 B 2 .   ? 4.31376   22.08032  48.33739 0.500 30.57257 ? 401 SO4 A O3  1 
HETATM 2846 O O4  A SO4 B 2 .   ? 3.94055   21.31694  50.95288 0.500 22.20331 ? 401 SO4 A O4  1 
HETATM 2847 O O4  B SO4 B 2 .   ? 5.29507   20.88516  50.13404 0.500 36.75504 ? 401 SO4 A O4  1 
HETATM 2848 S S   . SO4 C 2 .   ? 4.87819   -4.99215  61.25173 0.600 46.93968 ? 402 SO4 A S   1 
HETATM 2849 O O1  . SO4 C 2 .   ? 4.69276   -5.06019  59.80455 0.600 32.35902 ? 402 SO4 A O1  1 
HETATM 2850 O O2  . SO4 C 2 .   ? 6.26834   -4.65789  61.54938 0.600 37.25012 ? 402 SO4 A O2  1 
HETATM 2851 O O3  . SO4 C 2 .   ? 4.55108   -6.28493  61.84742 0.600 35.66508 ? 402 SO4 A O3  1 
HETATM 2852 O O4  . SO4 C 2 .   ? 4.00181   -3.96531  61.80839 0.600 34.12131 ? 402 SO4 A O4  1 
HETATM 2853 C C4  . WN8 D 3 .   ? -10.77791 12.69625  41.68686 0.800 22.72876 ? 403 WN8 A C4  1 
HETATM 2854 C C5  . WN8 D 3 .   ? -10.86517 14.20764  41.79409 0.800 33.01328 ? 403 WN8 A C5  1 
HETATM 2855 C C6  . WN8 D 3 .   ? -10.90215 14.89897  43.13256 0.800 29.72188 ? 403 WN8 A C6  1 
HETATM 2856 C C7  . WN8 D 3 .   ? -12.26117 14.75242  43.80905 0.800 32.47634 ? 403 WN8 A C7  1 
HETATM 2857 C C8  . WN8 D 3 .   ? -13.40596 14.89355  42.81596 0.800 34.93121 ? 403 WN8 A C8  1 
HETATM 2858 C C9  . WN8 D 3 .   ? -14.08708 16.25425  42.86824 0.800 37.06458 ? 403 WN8 A C9  1 
HETATM 2859 C C10 . WN8 D 3 .   ? -15.54730 16.07425  42.47172 0.800 39.92118 ? 403 WN8 A C10 1 
HETATM 2860 C C11 . WN8 D 3 .   ? -17.00776 14.11705  42.54438 0.800 25.56241 ? 403 WN8 A C11 1 
HETATM 2861 C C12 . WN8 D 3 .   ? -17.91257 14.80278  43.34344 0.800 32.92800 ? 403 WN8 A C12 1 
HETATM 2862 C C3  . WN8 D 3 .   ? -12.12359 12.01575  41.39180 0.800 25.46204 ? 403 WN8 A C3  1 
HETATM 2863 C C2  . WN8 D 3 .   ? -12.77329 12.42604  40.07806 0.800 19.59818 ? 403 WN8 A C2  1 
HETATM 2864 C C1  . WN8 D 3 .   ? -14.21432 11.92738  39.97931 0.800 17.32101 ? 403 WN8 A C1  1 
HETATM 2865 C C   . WN8 D 3 .   ? -14.75141 12.24617  38.58793 0.800 18.26798 ? 403 WN8 A C   1 
HETATM 2866 O O   . WN8 D 3 .   ? -10.88542 14.88364  40.77836 0.800 36.03293 ? 403 WN8 A O   1 
HETATM 2867 C C13 . WN8 D 3 .   ? -19.16930 14.27489  43.59586 0.800 38.22462 ? 403 WN8 A C13 1 
HETATM 2868 C C14 . WN8 D 3 .   ? -19.51060 13.04433  43.05347 0.800 24.19437 ? 403 WN8 A C14 1 
HETATM 2869 C C15 . WN8 D 3 .   ? -18.60101 12.35276  42.26232 0.800 18.44676 ? 403 WN8 A C15 1 
HETATM 2870 C C16 . WN8 D 3 .   ? -17.34567 12.88401  42.00221 0.800 19.42372 ? 403 WN8 A C16 1 
HETATM 2871 C C17 . WN8 D 3 .   ? -16.37802 12.11096  41.14801 0.800 14.23473 ? 403 WN8 A C17 1 
HETATM 2872 O O1  . WN8 D 3 .   ? -10.64172 16.29521  42.95189 0.800 41.76416 ? 403 WN8 A O1  1 
HETATM 2873 O O2  . WN8 D 3 .   ? -12.39650 15.75342  44.82515 0.800 36.76208 ? 403 WN8 A O2  1 
HETATM 2874 O O3  . WN8 D 3 .   ? -15.77786 14.67403  42.32171 0.800 34.38974 ? 403 WN8 A O3  1 
HETATM 2875 O O4  . WN8 D 3 .   ? -20.05398 14.95979  44.37316 0.800 46.08211 ? 403 WN8 A O4  1 
HETATM 2876 O O5  . WN8 D 3 .   ? -18.95772 11.14675  41.74123 0.800 16.39577 ? 403 WN8 A O5  1 
HETATM 2877 O O6  . WN8 D 3 .   ? -16.74413 11.07477  40.61595 0.800 19.73250 ? 403 WN8 A O6  1 
HETATM 2878 O O7  . WN8 D 3 .   ? -14.99976 12.57332  40.98674 0.800 18.29696 ? 403 WN8 A O7  1 
HETATM 2879 O O   . HOH E 4 .   ? -5.28802  13.70302  43.82369 1.000 31.25924 ? 501 HOH A O   1 
HETATM 2880 O O   . HOH E 4 .   ? -20.19466 0.83789   61.90618 1.000 36.86588 ? 502 HOH A O   1 
HETATM 2881 O O   . HOH E 4 .   ? -3.83082  -5.41839  38.87067 1.000 43.97221 ? 503 HOH A O   1 
HETATM 2882 O O   . HOH E 4 .   ? -18.96180 0.18988   64.06726 1.000 37.50158 ? 504 HOH A O   1 
HETATM 2883 O O   . HOH E 4 .   ? 10.60807  2.31761   40.56199 1.000 41.46864 ? 505 HOH A O   1 
HETATM 2884 O O   . HOH E 4 .   ? 16.85022  4.94414   45.78517 1.000 43.05376 ? 506 HOH A O   1 
HETATM 2885 O O   . HOH E 4 .   ? -17.29024 10.61504  74.05233 1.000 55.59501 ? 507 HOH A O   1 
HETATM 2886 O O   . HOH E 4 .   ? 14.10248  5.71955   52.54397 1.000 32.45210 ? 508 HOH A O   1 
HETATM 2887 O O   . HOH E 4 .   ? 7.16205   18.54140  23.69128 1.000 43.96823 ? 509 HOH A O   1 
HETATM 2888 O O   . HOH E 4 .   ? -9.62112  18.48308  55.14695 1.000 38.35108 ? 510 HOH A O   1 
HETATM 2889 O O   . HOH E 4 .   ? 6.66196   11.14574  41.19230 1.000 45.93025 ? 511 HOH A O   1 
HETATM 2890 O O   . HOH E 4 .   ? -20.66872 19.98433  53.86587 1.000 39.32971 ? 512 HOH A O   1 
HETATM 2891 O O   . HOH E 4 .   ? 5.98198   -3.79597  56.69866 1.000 33.04967 ? 513 HOH A O   1 
HETATM 2892 O O   . HOH E 4 .   ? -9.73007  -10.60172 42.66446 1.000 40.74699 ? 514 HOH A O   1 
HETATM 2893 O O   . HOH E 4 .   ? 4.633     -8.237    63.235   1.000 37.90964 ? 515 HOH A O   1 
HETATM 2894 O O   . HOH E 4 .   ? -0.83155  24.91205  60.68077 1.000 39.58666 ? 516 HOH A O   1 
HETATM 2895 O O   . HOH E 4 .   ? -24.45936 13.37668  53.41586 0.500 25.97235 ? 517 HOH A O   1 
HETATM 2896 O O   . HOH E 4 .   ? -13.789   -17.350   55.344   1.000 26.27030 ? 518 HOH A O   1 
HETATM 2897 O O   . HOH E 4 .   ? 0.68079   10.38705  70.06030 1.000 25.87794 ? 519 HOH A O   1 
HETATM 2898 O O   . HOH E 4 .   ? -1.01686  7.77955   73.30899 1.000 32.11267 ? 520 HOH A O   1 
HETATM 2899 O O   . HOH E 4 .   ? -19.42325 7.18364   24.91815 1.000 25.07807 ? 521 HOH A O   1 
HETATM 2900 O O   . HOH E 4 .   ? 10.27118  6.41910   67.77509 1.000 17.80661 ? 522 HOH A O   1 
HETATM 2901 O O   . HOH E 4 .   ? 10.87032  19.69250  62.36869 1.000 25.44973 ? 523 HOH A O   1 
HETATM 2902 O O   . HOH E 4 .   ? 12.02845  -2.82788  44.57070 1.000 40.48239 ? 524 HOH A O   1 
HETATM 2903 O O   . HOH E 4 .   ? 12.41548  0.06093   51.23856 1.000 43.39447 ? 525 HOH A O   1 
HETATM 2904 O O   . HOH E 4 .   ? -2.54039  19.79343  65.39316 1.000 36.82241 ? 526 HOH A O   1 
HETATM 2905 O O   . HOH E 4 .   ? -8.78785  16.04146  45.40462 1.000 32.71061 ? 527 HOH A O   1 
HETATM 2906 O O   . HOH E 4 .   ? 7.76808   4.84381   50.91157 1.000 23.42811 ? 528 HOH A O   1 
HETATM 2907 O O   . HOH E 4 .   ? -3.60552  -11.21066 50.58115 1.000 30.49090 ? 529 HOH A O   1 
HETATM 2908 O O   . HOH E 4 .   ? -19.77722 -5.71484  49.60943 1.000 39.49974 ? 530 HOH A O   1 
HETATM 2909 O O   . HOH E 4 .   ? -16.42247 13.75243  63.00514 1.000 27.53428 ? 531 HOH A O   1 
HETATM 2910 O O   . HOH E 4 .   ? -15.70990 -2.96555  64.47394 1.000 27.27209 ? 532 HOH A O   1 
HETATM 2911 O O   . HOH E 4 .   ? -5.27562  11.06736  35.94380 1.000 41.66278 ? 533 HOH A O   1 
HETATM 2912 O O   . HOH E 4 .   ? 22.401    8.337     71.633   1.000 31.53518 ? 534 HOH A O   1 
HETATM 2913 O O   . HOH E 4 .   ? -5.65182  12.40026  38.16108 1.000 35.67721 ? 535 HOH A O   1 
HETATM 2914 O O   . HOH E 4 .   ? -14.26278 -12.53936 59.87485 1.000 39.23509 ? 536 HOH A O   1 
HETATM 2915 O O   . HOH E 4 .   ? -13.63496 -5.67766  69.02987 1.000 29.83963 ? 537 HOH A O   1 
HETATM 2916 O O   . HOH E 4 .   ? -26.76969 3.64479   47.63547 1.000 37.95390 ? 538 HOH A O   1 
HETATM 2917 O O   . HOH E 4 .   ? -7.97093  -9.16796  54.77724 1.000 18.22417 ? 539 HOH A O   1 
HETATM 2918 O O   . HOH E 4 .   ? -17.38361 2.84069   70.55809 1.000 38.90721 ? 540 HOH A O   1 
HETATM 2919 O O   . HOH E 4 .   ? -2.09093  15.91067  44.46514 1.000 37.48960 ? 541 HOH A O   1 
HETATM 2920 O O   . HOH E 4 .   ? -17.32982 4.17282   38.06506 1.000 25.08700 ? 542 HOH A O   1 
HETATM 2921 O O   . HOH E 4 .   ? -1.70247  -1.85810  71.78723 1.000 43.52007 ? 543 HOH A O   1 
HETATM 2922 O O   . HOH E 4 .   ? -19.29254 -8.75444  49.23223 1.000 34.94568 ? 544 HOH A O   1 
HETATM 2923 O O   . HOH E 4 .   ? -11.28718 10.02891  38.30660 1.000 26.81749 ? 545 HOH A O   1 
HETATM 2924 O O   . HOH E 4 .   ? 8.55454   19.37352  56.92588 1.000 40.27729 ? 546 HOH A O   1 
HETATM 2925 O O   . HOH E 4 .   ? -9.42563  21.63472  55.60910 1.000 35.04476 ? 547 HOH A O   1 
HETATM 2926 O O   . HOH E 4 .   ? -2.76616  16.44677  42.01946 1.000 49.01526 ? 548 HOH A O   1 
HETATM 2927 O O   . HOH E 4 .   ? -16.73459 -6.73098  53.61243 1.000 24.37502 ? 549 HOH A O   1 
HETATM 2928 O O   . HOH E 4 .   ? 1.96215   16.34084  77.48787 1.000 72.85885 ? 550 HOH A O   1 
HETATM 2929 O O   . HOH E 4 .   ? 16.17037  20.16344  49.08586 1.000 39.87158 ? 551 HOH A O   1 
HETATM 2930 O O   . HOH E 4 .   ? -8.04628  17.74101  53.28325 1.000 24.04742 ? 552 HOH A O   1 
HETATM 2931 O O   . HOH E 4 .   ? 5.09076   -1.13205  57.39361 1.000 25.53328 ? 553 HOH A O   1 
HETATM 2932 O O   . HOH E 4 .   ? -9.27684  -0.43073  74.06017 1.000 40.68748 ? 554 HOH A O   1 
HETATM 2933 O O   . HOH E 4 .   ? 17.32683  2.07424   47.73949 1.000 46.41469 ? 555 HOH A O   1 
HETATM 2934 O O   . HOH E 4 .   ? -10.90228 -6.75260  62.72835 1.000 20.42733 ? 556 HOH A O   1 
HETATM 2935 O O   . HOH E 4 .   ? 7.53126   4.62050   53.49127 1.000 22.07997 ? 557 HOH A O   1 
HETATM 2936 O O   . HOH E 4 .   ? 1.82594   25.66547  61.80949 1.000 37.60333 ? 558 HOH A O   1 
HETATM 2937 O O   . HOH E 4 .   ? 11.85462  2.36488   69.22155 1.000 31.87762 ? 559 HOH A O   1 
HETATM 2938 O O   . HOH E 4 .   ? 13.39321  -1.80664  40.19659 1.000 58.85724 ? 560 HOH A O   1 
HETATM 2939 O O   . HOH E 4 .   ? 9.52917   10.22699  44.60330 1.000 33.22801 ? 561 HOH A O   1 
HETATM 2940 O O   . HOH E 4 .   ? 0.73219   14.71216  23.40378 1.000 41.05096 ? 562 HOH A O   1 
HETATM 2941 O O   . HOH E 4 .   ? -13.40429 -11.75215 48.16963 1.000 32.67013 ? 563 HOH A O   1 
HETATM 2942 O O   . HOH E 4 .   ? -14.81283 9.22223   18.75241 1.000 27.40101 ? 564 HOH A O   1 
HETATM 2943 O O   . HOH E 4 .   ? -23.62805 1.22939   52.94110 1.000 38.54727 ? 565 HOH A O   1 
HETATM 2944 O O   . HOH E 4 .   ? -11.09411 14.21795  21.89869 1.000 18.26848 ? 566 HOH A O   1 
HETATM 2945 O O   . HOH E 4 .   ? -17.86334 -7.16185  56.13241 1.000 31.05683 ? 567 HOH A O   1 
HETATM 2946 O O   . HOH E 4 .   ? -12.60439 18.63084  55.15808 1.000 27.02844 ? 568 HOH A O   1 
HETATM 2947 O O   . HOH E 4 .   ? -8.28546  16.12136  35.17773 1.000 45.93685 ? 569 HOH A O   1 
HETATM 2948 O O   . HOH E 4 .   ? 8.23448   4.27646   65.07467 1.000 18.17878 ? 570 HOH A O   1 
HETATM 2949 O O   . HOH E 4 .   ? 12.63729  15.89695  68.51364 1.000 25.99797 ? 571 HOH A O   1 
HETATM 2950 O O   . HOH E 4 .   ? 25.37077  11.75463  63.73406 1.000 24.96432 ? 572 HOH A O   1 
HETATM 2951 O O   . HOH E 4 .   ? -10.66730 5.74558   17.20326 1.000 23.79300 ? 573 HOH A O   1 
HETATM 2952 O O   . HOH E 4 .   ? -14.50609 6.94193   67.83132 1.000 32.80197 ? 574 HOH A O   1 
HETATM 2953 O O   . HOH E 4 .   ? -0.12069  0.90995   69.50442 1.000 33.66845 ? 575 HOH A O   1 
HETATM 2954 O O   . HOH E 4 .   ? -13.49084 18.25115  23.66220 1.000 35.29722 ? 576 HOH A O   1 
HETATM 2955 O O   . HOH E 4 .   ? -14.58822 -10.04576 62.20108 1.000 32.49343 ? 577 HOH A O   1 
HETATM 2956 O O   . HOH E 4 .   ? 5.02776   17.55589  72.10747 1.000 29.73144 ? 578 HOH A O   1 
HETATM 2957 O O   . HOH E 4 .   ? -0.39915  25.60390  50.03813 1.000 49.83972 ? 579 HOH A O   1 
HETATM 2958 O O   . HOH E 4 .   ? -12.56434 0.55475   35.48906 1.000 21.59677 ? 580 HOH A O   1 
HETATM 2959 O O   . HOH E 4 .   ? 9.69773   8.17501   59.26167 1.000 30.08897 ? 581 HOH A O   1 
HETATM 2960 O O   . HOH E 4 .   ? 7.98756   -4.45471  58.43637 1.000 38.88169 ? 582 HOH A O   1 
HETATM 2961 O O   . HOH E 4 .   ? 2.55930   15.58160  75.47330 1.000 33.58385 ? 583 HOH A O   1 
HETATM 2962 O O   . HOH E 4 .   ? 2.08138   9.55304   53.16794 1.000 13.34980 ? 584 HOH A O   1 
HETATM 2963 O O   . HOH E 4 .   ? 14.33430  14.49542  67.30535 1.000 15.88115 ? 585 HOH A O   1 
HETATM 2964 O O   . HOH E 4 .   ? -12.854   -15.417   56.217   1.000 31.05635 ? 586 HOH A O   1 
HETATM 2965 O O   . HOH E 4 .   ? 23.59274  4.54114   64.42354 1.000 44.61249 ? 587 HOH A O   1 
HETATM 2966 O O   . HOH E 4 .   ? 11.54801  9.98851   42.21829 1.000 43.62427 ? 588 HOH A O   1 
HETATM 2967 O O   . HOH E 4 .   ? -5.48369  14.68996  58.88726 1.000 16.53999 ? 589 HOH A O   1 
HETATM 2968 O O   . HOH E 4 .   ? -6.15597  16.50502  44.41495 1.000 44.53119 ? 590 HOH A O   1 
HETATM 2969 O O   . HOH E 4 .   ? -1.01477  -5.38390  69.38857 1.000 40.72313 ? 591 HOH A O   1 
HETATM 2970 O O   . HOH E 4 .   ? 5.10191   8.41222   69.34214 1.000 35.37592 ? 592 HOH A O   1 
HETATM 2971 O O   . HOH E 4 .   ? 9.514     13.591    79.204   1.000 40.84170 ? 593 HOH A O   1 
HETATM 2972 O O   . HOH E 4 .   ? -9.11455  11.56926  77.73225 1.000 41.30098 ? 594 HOH A O   1 
HETATM 2973 O O   . HOH E 4 .   ? 1.33628   14.10409  57.49429 1.000 18.32958 ? 595 HOH A O   1 
HETATM 2974 O O   . HOH E 4 .   ? 2.38550   6.79187   66.82167 1.000 27.97012 ? 596 HOH A O   1 
HETATM 2975 O O   . HOH E 4 .   ? -2.29099  12.85858  49.99104 1.000 18.95575 ? 597 HOH A O   1 
HETATM 2976 O O   . HOH E 4 .   ? 3.03064   -6.21324  46.02062 1.000 27.26278 ? 598 HOH A O   1 
HETATM 2977 O O   . HOH E 4 .   ? -6.21448  -9.58457  56.97517 1.000 21.03397 ? 599 HOH A O   1 
HETATM 2978 O O   . HOH E 4 .   ? 6.89553   -5.09152  45.78341 1.000 47.38487 ? 600 HOH A O   1 
HETATM 2979 O O   . HOH E 4 .   ? -16.65126 7.43387   70.40686 1.000 37.53651 ? 601 HOH A O   1 
HETATM 2980 O O   . HOH E 4 .   ? -1.32696  8.12254   50.11438 1.000 11.69206 ? 602 HOH A O   1 
HETATM 2981 O O   . HOH E 4 .   ? -13.58107 0.56422   72.71467 1.000 39.76114 ? 603 HOH A O   1 
HETATM 2982 O O   . HOH E 4 .   ? -24.17938 17.02357  26.06314 1.000 45.51544 ? 604 HOH A O   1 
HETATM 2983 O O   . HOH E 4 .   ? -12.49183 -6.91422  43.76463 1.000 20.78009 ? 605 HOH A O   1 
HETATM 2984 O O   . HOH E 4 .   ? -6.34468  3.49369   73.07085 1.000 26.18510 ? 606 HOH A O   1 
HETATM 2985 O O   . HOH E 4 .   ? -16.60403 0.09364   42.32066 1.000 22.45971 ? 607 HOH A O   1 
HETATM 2986 O O   . HOH E 4 .   ? 6.93855   11.54472  75.53876 1.000 38.72967 ? 608 HOH A O   1 
HETATM 2987 O O   . HOH E 4 .   ? 0.50461   15.83892  38.63133 1.000 43.20778 ? 609 HOH A O   1 
HETATM 2988 O O   . HOH E 4 .   ? -3.87596  -5.23589  68.07506 1.000 30.13216 ? 610 HOH A O   1 
HETATM 2989 O O   . HOH E 4 .   ? -10.27856 -5.93766  49.32828 1.000 15.22585 ? 611 HOH A O   1 
HETATM 2990 O O   . HOH E 4 .   ? -15.09033 5.80199   16.61591 1.000 26.05635 ? 612 HOH A O   1 
HETATM 2991 O O   . HOH E 4 .   ? 10.89543  20.96389  72.76948 1.000 38.66539 ? 613 HOH A O   1 
HETATM 2992 O O   . HOH E 4 .   ? -10.070   -12.762   49.742   1.000 28.91477 ? 614 HOH A O   1 
HETATM 2993 O O   . HOH E 4 .   ? 2.78995   0.25282   56.64598 1.000 16.02383 ? 615 HOH A O   1 
HETATM 2994 O O   . HOH E 4 .   ? -3.01310  16.16761  58.73302 1.000 16.81556 ? 616 HOH A O   1 
HETATM 2995 O O   . HOH E 4 .   ? 22.83007  17.33416  64.87235 1.000 28.00612 ? 617 HOH A O   1 
HETATM 2996 O O   . HOH E 4 .   ? -12.57427 6.26408   23.71716 1.000 25.31373 ? 618 HOH A O   1 
HETATM 2997 O O   . HOH E 4 .   ? 2.51755   -0.46482  64.13415 1.000 19.10552 ? 619 HOH A O   1 
HETATM 2998 O O   . HOH E 4 .   ? 13.49871  13.71493  51.22522 1.000 28.81472 ? 620 HOH A O   1 
HETATM 2999 O O   . HOH E 4 .   ? 6.12285   6.29035   66.33995 1.000 20.41834 ? 621 HOH A O   1 
HETATM 3000 O O   . HOH E 4 .   ? 8.20806   9.58651   70.56743 1.000 33.56115 ? 622 HOH A O   1 
HETATM 3001 O O   . HOH E 4 .   ? 15.064    12.011    68.575   1.000 18.80161 ? 623 HOH A O   1 
HETATM 3002 O O   . HOH E 4 .   ? 1.87840   19.18371  66.36448 1.000 20.00081 ? 624 HOH A O   1 
HETATM 3003 O O   . HOH E 4 .   ? -11.57396 18.18946  58.09412 1.000 30.84387 ? 625 HOH A O   1 
HETATM 3004 O O   . HOH E 4 .   ? -13.40515 -0.75275  40.53834 1.000 21.40030 ? 626 HOH A O   1 
HETATM 3005 O O   . HOH E 4 .   ? -13.58725 11.82560  68.52686 1.000 33.59728 ? 627 HOH A O   1 
HETATM 3006 O O   . HOH E 4 .   ? 12.95665  20.15877  75.13377 1.000 38.91863 ? 628 HOH A O   1 
HETATM 3007 O O   . HOH E 4 .   ? -21.40323 5.00594   24.37783 1.000 41.23260 ? 629 HOH A O   1 
HETATM 3008 O O   . HOH E 4 .   ? -16.85666 6.72011   23.81894 1.000 29.19852 ? 630 HOH A O   1 
HETATM 3009 O O   . HOH E 4 .   ? 0.67654   19.66041  48.72781 1.000 23.30441 ? 631 HOH A O   1 
HETATM 3010 O O   . HOH E 4 .   ? 16.92751  22.67372  66.91978 1.000 33.19859 ? 632 HOH A O   1 
HETATM 3011 O O   . HOH E 4 .   ? -0.71094  -3.54628  70.67646 0.500 23.11976 ? 633 HOH A O   1 
HETATM 3012 O O   . HOH E 4 .   ? -9.44042  3.96457   18.41607 1.000 37.61842 ? 634 HOH A O   1 
HETATM 3013 O O   . HOH E 4 .   ? -7.20610  15.53047  63.82884 1.000 24.04086 ? 635 HOH A O   1 
HETATM 3014 O O   . HOH E 4 .   ? -4.00631  -6.26327  63.80901 1.000 29.04855 ? 636 HOH A O   1 
HETATM 3015 O O   . HOH E 4 .   ? -24.07490 17.83171  40.09082 1.000 43.02487 ? 637 HOH A O   1 
HETATM 3016 O O   . HOH E 4 .   ? -14.87811 -5.64965  45.30821 1.000 26.47262 ? 638 HOH A O   1 
HETATM 3017 O O   . HOH E 4 .   ? -32.81240 9.51555   26.24900 1.000 48.64950 ? 639 HOH A O   1 
HETATM 3018 O O   . HOH E 4 .   ? -10.65535 8.87681   74.05258 1.000 36.80559 ? 640 HOH A O   1 
HETATM 3019 O O   . HOH E 4 .   ? 0.427     -8.914    63.128   1.000 33.67953 ? 641 HOH A O   1 
HETATM 3020 O O   . HOH E 4 .   ? -23.81865 6.63382   38.32673 1.000 26.44420 ? 642 HOH A O   1 
HETATM 3021 O O   . HOH E 4 .   ? 4.50741   -6.01491  49.92868 1.000 29.62809 ? 643 HOH A O   1 
HETATM 3022 O O   . HOH E 4 .   ? -8.58089  -10.17451 64.00968 1.000 30.75325 ? 644 HOH A O   1 
HETATM 3023 O O   . HOH E 4 .   ? 18.36710  6.72661   55.22623 1.000 29.20182 ? 645 HOH A O   1 
HETATM 3024 O O   . HOH E 4 .   ? 11.13528  12.19305  45.91126 1.000 36.27191 ? 646 HOH A O   1 
HETATM 3025 O O   . HOH E 4 .   ? 8.68036   10.45978  66.22151 1.000 18.20762 ? 647 HOH A O   1 
HETATM 3026 O O   . HOH E 4 .   ? -18.47654 -9.90123  54.72985 1.000 39.89413 ? 648 HOH A O   1 
HETATM 3027 O O   . HOH E 4 .   ? 17.82184  0.49927   64.77445 1.000 38.97056 ? 649 HOH A O   1 
HETATM 3028 O O   . HOH E 4 .   ? 7.68428   15.48621  25.02424 1.000 43.73456 ? 650 HOH A O   1 
HETATM 3029 O O   . HOH E 4 .   ? 12.76965  5.38298   61.43312 1.000 21.48076 ? 651 HOH A O   1 
HETATM 3030 O O   . HOH E 4 .   ? -1.86082  14.88369  17.50165 1.000 41.43127 ? 652 HOH A O   1 
HETATM 3031 O O   . HOH E 4 .   ? -13.45762 -0.13988  32.81127 1.000 39.57183 ? 653 HOH A O   1 
HETATM 3032 O O   . HOH E 4 .   ? -8.57211  16.32812  50.87499 1.000 12.72762 ? 654 HOH A O   1 
HETATM 3033 O O   . HOH E 4 .   ? 6.13613   18.23544  53.51362 1.000 20.22680 ? 655 HOH A O   1 
HETATM 3034 O O   . HOH E 4 .   ? -11.52907 -6.25694  71.97526 1.000 47.11975 ? 656 HOH A O   1 
HETATM 3035 O O   . HOH E 4 .   ? 15.45226  5.37709   72.41595 1.000 26.04533 ? 657 HOH A O   1 
HETATM 3036 O O   . HOH E 4 .   ? -15.13314 -1.36699  67.26933 1.000 37.59345 ? 658 HOH A O   1 
HETATM 3037 O O   . HOH E 4 .   ? -2.03986  19.94227  28.07393 1.000 45.00912 ? 659 HOH A O   1 
HETATM 3038 O O   . HOH E 4 .   ? 6.25844   -1.64137  49.68957 1.000 18.40273 ? 660 HOH A O   1 
HETATM 3039 O O   . HOH E 4 .   ? -10.40863 5.51994   41.14697 1.000 27.39712 ? 661 HOH A O   1 
HETATM 3040 O O   . HOH E 4 .   ? -2.99702  8.63697   42.71177 1.000 24.62559 ? 662 HOH A O   1 
HETATM 3041 O O   . HOH E 4 .   ? -21.81310 5.32945   66.51208 1.000 33.60601 ? 663 HOH A O   1 
HETATM 3042 O O   . HOH E 4 .   ? 20.75903  22.10145  68.06262 1.000 30.07429 ? 664 HOH A O   1 
HETATM 3043 O O   . HOH E 4 .   ? -6.79974  23.25911  60.75156 1.000 42.69645 ? 665 HOH A O   1 
HETATM 3044 O O   . HOH E 4 .   ? 0.00926   19.77900  64.67821 1.000 37.24793 ? 666 HOH A O   1 
HETATM 3045 O O   . HOH E 4 .   ? 1.69841   11.92047  44.88217 1.000 35.78410 ? 667 HOH A O   1 
HETATM 3046 O O   . HOH E 4 .   ? 24.64756  15.17552  65.21021 1.000 40.88589 ? 668 HOH A O   1 
HETATM 3047 O O   . HOH E 4 .   ? 3.11555   2.59967   67.46284 1.000 31.45517 ? 669 HOH A O   1 
HETATM 3048 O O   . HOH E 4 .   ? -4.82914  18.57149  25.62402 1.000 38.09875 ? 670 HOH A O   1 
HETATM 3049 O O   . HOH E 4 .   ? -10.22020 7.89877   39.54637 1.000 29.29788 ? 671 HOH A O   1 
HETATM 3050 O O   . HOH E 4 .   ? 10.78756  12.99091  48.54418 1.000 34.79850 ? 672 HOH A O   1 
HETATM 3051 O O   . HOH E 4 .   ? -15.60406 -9.97858  47.98090 1.000 28.63948 ? 673 HOH A O   1 
HETATM 3052 O O   . HOH E 4 .   ? 5.31167   25.05303  50.63324 1.000 43.02122 ? 674 HOH A O   1 
HETATM 3053 O O   . HOH E 4 .   ? -18.55189 1.70346   47.60771 1.000 30.62081 ? 675 HOH A O   1 
HETATM 3054 O O   . HOH E 4 .   ? -7.45743  14.52158  37.92510 1.000 43.04575 ? 676 HOH A O   1 
HETATM 3055 O O   . HOH E 4 .   ? 15.40023  3.10986   71.01248 1.000 23.05596 ? 677 HOH A O   1 
HETATM 3056 O O   . HOH E 4 .   ? -8.33693  21.83350  25.28385 1.000 48.50009 ? 678 HOH A O   1 
HETATM 3057 O O   . HOH E 4 .   ? -22.61648 17.83336  62.47107 1.000 27.52071 ? 679 HOH A O   1 
HETATM 3058 O O   . HOH E 4 .   ? 20.809    13.991    52.187   1.000 26.12988 ? 680 HOH A O   1 
HETATM 3059 O O   . HOH E 4 .   ? 1.61679   -7.83671  44.49218 1.000 34.11437 ? 681 HOH A O   1 
HETATM 3060 O O   . HOH E 4 .   ? 8.13772   6.72287   40.59007 1.000 45.11869 ? 682 HOH A O   1 
HETATM 3061 O O   . HOH E 4 .   ? 12.88790  6.21390   57.06787 1.000 31.35674 ? 683 HOH A O   1 
HETATM 3062 O O   . HOH E 4 .   ? 11.51184  8.72936   72.01702 1.000 38.00560 ? 684 HOH A O   1 
HETATM 3063 O O   . HOH E 4 .   ? -11.52113 0.26329   39.01820 1.000 27.15101 ? 685 HOH A O   1 
HETATM 3064 O O   . HOH E 4 .   ? 0.04989   -2.27944  53.26512 1.000 14.13351 ? 686 HOH A O   1 
HETATM 3065 O O   . HOH E 4 .   ? 18.66251  12.88157  47.19282 1.000 42.66790 ? 687 HOH A O   1 
HETATM 3066 O O   . HOH E 4 .   ? -21.23952 16.65386  52.22302 1.000 42.09364 ? 688 HOH A O   1 
HETATM 3067 O O   . HOH E 4 .   ? -3.87598  7.80547   74.47104 1.000 34.06558 ? 689 HOH A O   1 
HETATM 3068 O O   . HOH E 4 .   ? 19.51023  0.34992   66.71185 1.000 38.27222 ? 690 HOH A O   1 
HETATM 3069 O O   . HOH E 4 .   ? 0.57080   11.61084  18.85905 1.000 30.08872 ? 691 HOH A O   1 
HETATM 3070 O O   . HOH E 4 .   ? -18.34622 3.12313   25.31124 1.000 35.21418 ? 692 HOH A O   1 
HETATM 3071 O O   . HOH E 4 .   ? 18.06960  -2.44654  47.06385 1.000 47.06494 ? 693 HOH A O   1 
HETATM 3072 O O   . HOH E 4 .   ? -2.27955  24.73829  57.60384 1.000 40.27796 ? 694 HOH A O   1 
HETATM 3073 O O   . HOH E 4 .   ? -8.60794  22.85616  53.61610 0.500 18.64572 ? 695 HOH A O   1 
HETATM 3074 O O   . HOH E 4 .   ? -9.97747  -6.06417  34.58071 1.000 41.24446 ? 696 HOH A O   1 
HETATM 3075 O O   . HOH E 4 .   ? -5.92086  -7.26383  38.40940 1.000 38.76113 ? 697 HOH A O   1 
HETATM 3076 O O   . HOH E 4 .   ? -5.31563  -3.83029  69.95587 1.000 37.80538 ? 698 HOH A O   1 
HETATM 3077 O O   . HOH E 4 .   ? 1.75683   -0.85578  68.91377 1.000 39.85509 ? 699 HOH A O   1 
HETATM 3078 O O   . HOH E 4 .   ? -8.16699  16.32404  76.67745 1.000 43.99258 ? 700 HOH A O   1 
HETATM 3079 O O   . HOH E 4 .   ? -12.58985 13.11763  70.37744 1.000 32.10638 ? 701 HOH A O   1 
HETATM 3080 O O   . HOH E 4 .   ? -5.18658  -8.02384  65.28496 1.000 42.41823 ? 702 HOH A O   1 
HETATM 3081 O O   . HOH E 4 .   ? -6.503    -12.150   50.802   1.000 32.47708 ? 703 HOH A O   1 
HETATM 3082 O O   . HOH E 4 .   ? 18.17751  4.16196   55.82243 1.000 37.82321 ? 704 HOH A O   1 
HETATM 3083 O O   . HOH E 4 .   ? 16.65496  18.48472  74.33732 1.000 33.05794 ? 705 HOH A O   1 
HETATM 3084 O O   . HOH E 4 .   ? -21.34546 4.91991   31.43577 1.000 40.76655 ? 706 HOH A O   1 
HETATM 3085 O O   . HOH E 4 .   ? -0.15397  -6.06524  49.93420 1.000 19.18806 ? 707 HOH A O   1 
HETATM 3086 O O   . HOH E 4 .   ? -13.59109 3.26920   74.28916 1.000 34.41131 ? 708 HOH A O   1 
HETATM 3087 O O   . HOH E 4 .   ? -2.58733  -6.35244  50.23859 1.000 18.97884 ? 709 HOH A O   1 
HETATM 3088 O O   . HOH E 4 .   ? -17.13013 2.11649   40.52755 1.000 26.66345 ? 710 HOH A O   1 
HETATM 3089 O O   . HOH E 4 .   ? -20.87279 8.00774   68.12945 1.000 34.20855 ? 711 HOH A O   1 
HETATM 3090 O O   . HOH E 4 .   ? -5.40334  13.07721  34.32739 1.000 38.60955 ? 712 HOH A O   1 
HETATM 3091 O O   . HOH E 4 .   ? -16.01904 8.67173   22.34070 1.000 17.08934 ? 713 HOH A O   1 
HETATM 3092 O O   . HOH E 4 .   ? 6.31203   -0.35096  53.29966 1.000 39.33740 ? 714 HOH A O   1 
HETATM 3093 O O   . HOH E 4 .   ? 13.04852  3.46955   59.42207 1.000 34.79363 ? 715 HOH A O   1 
HETATM 3094 O O   . HOH E 4 .   ? 10.23813  3.91169   53.55074 1.000 29.33232 ? 716 HOH A O   1 
HETATM 3095 O O   . HOH E 4 .   ? -16.18528 12.66077  65.70945 1.000 44.20397 ? 717 HOH A O   1 
HETATM 3096 O O   . HOH E 4 .   ? -0.78220  -6.28025  54.26444 1.000 18.55078 ? 718 HOH A O   1 
HETATM 3097 O O   . HOH E 4 .   ? -4.58281  1.29674   73.32991 1.000 40.85874 ? 719 HOH A O   1 
HETATM 3098 O O   . HOH E 4 .   ? -33.68468 -0.53584  32.63171 1.000 47.21677 ? 720 HOH A O   1 
HETATM 3099 O O   . HOH E 4 .   ? 13.09044  -1.32691  62.02217 1.000 41.23198 ? 721 HOH A O   1 
HETATM 3100 O O   . HOH E 4 .   ? -2.95751  17.83738  21.29042 1.000 45.28202 ? 722 HOH A O   1 
HETATM 3101 O O   . HOH E 4 .   ? 9.68977   -0.94653  68.51226 1.000 46.31600 ? 723 HOH A O   1 
HETATM 3102 O O   . HOH E 4 .   ? -3.90383  -3.02353  71.98102 1.000 42.70461 ? 724 HOH A O   1 
HETATM 3103 O O   . HOH E 4 .   ? -11.42213 -8.30269  34.53388 1.000 39.58543 ? 725 HOH A O   1 
HETATM 3104 O O   . HOH E 4 .   ? 18.81201  7.25201   52.33631 1.000 32.19728 ? 726 HOH A O   1 
HETATM 3105 O O   . HOH E 4 .   ? -22.61429 9.46125   22.61676 1.000 54.83309 ? 727 HOH A O   1 
HETATM 3106 O O   . HOH E 4 .   ? -17.93394 -1.56072  51.15307 1.000 36.09659 ? 728 HOH A O   1 
HETATM 3107 O O   . HOH E 4 .   ? 11.883    21.031    58.187   1.000 34.32056 ? 729 HOH A O   1 
HETATM 3108 O O   . HOH E 4 .   ? -23.23740 4.67898   33.59542 1.000 52.40494 ? 730 HOH A O   1 
HETATM 3109 O O   . HOH E 4 .   ? -2.81331  -4.54623  65.40550 1.000 33.64977 ? 731 HOH A O   1 
HETATM 3110 O O   . HOH E 4 .   ? 9.17336   -4.52704  62.78886 1.000 47.22665 ? 732 HOH A O   1 
HETATM 3111 O O   . HOH E 4 .   ? -10.78308 -8.48062  67.08100 1.000 31.76286 ? 733 HOH A O   1 
HETATM 3112 O O   . HOH E 4 .   ? 5.46010   3.30252   38.22558 1.000 36.02069 ? 734 HOH A O   1 
HETATM 3113 O O   . HOH E 4 .   ? -7.38039  13.81219  35.43623 1.000 35.70212 ? 735 HOH A O   1 
HETATM 3114 O O   . HOH E 4 .   ? -11.37604 1.94326   18.21662 1.000 32.73282 ? 736 HOH A O   1 
HETATM 3115 O O   . HOH E 4 .   ? 4.66544   -1.95409  53.68187 1.000 25.69732 ? 737 HOH A O   1 
HETATM 3116 O O   . HOH E 4 .   ? -26.40626 16.09566  39.89859 1.000 40.69936 ? 738 HOH A O   1 
HETATM 3117 O O   . HOH E 4 .   ? 0.41349   16.93787  41.37067 1.000 46.93791 ? 739 HOH A O   1 
HETATM 3118 O O   . HOH E 4 .   ? -15.066   1.890     14.228   1.000 38.10153 ? 740 HOH A O   1 
HETATM 3119 O O   . HOH E 4 .   ? 23.29463  8.67252   65.75420 1.000 23.97850 ? 741 HOH A O   1 
HETATM 3120 O O   . HOH E 4 .   ? 22.76186  17.75828  67.84458 1.000 36.36614 ? 742 HOH A O   1 
HETATM 3121 O O   . HOH E 4 .   ? -15.988   -15.577   49.390   1.000 41.19200 ? 743 HOH A O   1 
HETATM 3122 O O   . HOH E 4 .   ? -9.85084  6.71949   74.39132 1.000 33.83467 ? 744 HOH A O   1 
HETATM 3123 O O   . HOH E 4 .   ? -14.96069 15.58836  68.09685 1.000 50.49456 ? 745 HOH A O   1 
HETATM 3124 O O   . HOH E 4 .   ? -20.39256 10.02661  23.85831 1.000 40.90995 ? 746 HOH A O   1 
HETATM 3125 O O   . HOH E 4 .   ? -16.46973 -7.67173  46.32394 1.000 29.34523 ? 747 HOH A O   1 
HETATM 3126 O O   . HOH E 4 .   ? 21.491    2.733     74.671   1.000 44.75015 ? 748 HOH A O   1 
HETATM 3127 O O   . HOH E 4 .   ? -7.18046  17.64412  66.17940 1.000 42.14181 ? 749 HOH A O   1 
HETATM 3128 O O   . HOH E 4 .   ? 1.60519   -3.02148  63.96557 1.000 40.24690 ? 750 HOH A O   1 
HETATM 3129 O O   . HOH E 4 .   ? -9.38791  -8.71120  39.59697 1.000 33.82301 ? 751 HOH A O   1 
HETATM 3130 O O   . HOH E 4 .   ? 5.69687   -2.81911  65.27708 1.000 44.45272 ? 752 HOH A O   1 
HETATM 3131 O O   . HOH E 4 .   ? -16.79934 13.74504  69.20947 1.000 46.68471 ? 753 HOH A O   1 
HETATM 3132 O O   . HOH E 4 .   ? -0.720    28.113    54.957   1.000 37.18663 ? 754 HOH A O   1 
HETATM 3133 O O   . HOH E 4 .   ? 1.69185   -6.28729  34.42111 1.000 48.82960 ? 755 HOH A O   1 
HETATM 3134 O O   . HOH E 4 .   ? -12.52341 -1.24028  74.50268 1.000 49.39827 ? 756 HOH A O   1 
HETATM 3135 O O   . HOH E 4 .   ? 3.27366   0.20296   66.63853 1.000 25.18196 ? 757 HOH A O   1 
HETATM 3136 O O   . HOH E 4 .   ? 8.23735   -0.25516  54.66823 1.000 37.01753 ? 758 HOH A O   1 
HETATM 3137 O O   . HOH E 4 .   ? 0.62901   7.95045   75.23931 1.000 40.51665 ? 759 HOH A O   1 
HETATM 3138 O O   . HOH E 4 .   ? 0.62892   -4.71784  52.67281 1.000 19.60071 ? 760 HOH A O   1 
HETATM 3139 O O   . HOH E 4 .   ? -7.40894  -0.66085  72.32019 1.000 37.72053 ? 761 HOH A O   1 
HETATM 3140 O O   . HOH E 4 .   ? -14.35911 15.30601  21.39178 1.000 42.65559 ? 762 HOH A O   1 
HETATM 3141 O O   . HOH E 4 .   ? 12.23687  4.92153   54.87898 1.000 33.38712 ? 763 HOH A O   1 
HETATM 3142 O O   . HOH E 4 .   ? -23.22990 25.59164  36.24234 1.000 55.21585 ? 764 HOH A O   1 
HETATM 3143 O O   . HOH E 4 .   ? -14.26484 17.76623  67.57693 1.000 50.27563 ? 765 HOH A O   1 
HETATM 3144 O O   . HOH E 4 .   ? 18.67342  3.72854   46.86361 1.000 45.12076 ? 766 HOH A O   1 
HETATM 3145 O O   . HOH E 4 .   ? -4.64389  -11.37990 55.54304 1.000 37.55609 ? 767 HOH A O   1 
HETATM 3146 O O   . HOH E 4 .   ? 13.06660  5.21738   40.94847 1.000 49.35752 ? 768 HOH A O   1 
HETATM 3147 O O   . HOH E 4 .   ? -27.333   6.821     24.529   1.000 45.50709 ? 769 HOH A O   1 
HETATM 3148 O O   . HOH E 4 .   ? -19.766   13.894    75.594   1.000 36.01170 ? 770 HOH A O   1 
HETATM 3149 O O   . HOH E 4 .   ? 17.92992  1.57909   71.29047 1.000 37.08783 ? 771 HOH A O   1 
HETATM 3150 O O   . HOH E 4 .   ? 6.10848   -4.06540  47.74307 1.000 34.92740 ? 772 HOH A O   1 
HETATM 3151 O O   . HOH E 4 .   ? -25.413   2.178     62.810   1.000 39.88761 ? 773 HOH A O   1 
HETATM 3152 O O   . HOH E 4 .   ? -17.79932 -4.17982  52.40857 1.000 36.29556 ? 774 HOH A O   1 
HETATM 3153 O O   . HOH E 4 .   ? -1.13965  4.37188   71.99675 1.000 33.27651 ? 775 HOH A O   1 
HETATM 3154 O O   . HOH E 4 .   ? -11.04919 -8.94011  64.07174 1.000 24.95825 ? 776 HOH A O   1 
HETATM 3155 O O   . HOH E 4 .   ? -15.53075 9.30406   68.10651 1.000 37.04500 ? 777 HOH A O   1 
HETATM 3156 O O   . HOH E 4 .   ? -25.39271 8.86431   45.09114 1.000 43.97107 ? 778 HOH A O   1 
HETATM 3157 O O   . HOH E 4 .   ? -0.37925  -4.53361  65.13270 1.000 37.30538 ? 779 HOH A O   1 
HETATM 3158 O O   . HOH E 4 .   ? 2.23468   -1.23723  54.24198 1.000 14.75807 ? 780 HOH A O   1 
HETATM 3159 O O   . HOH E 4 .   ? -17.30445 -6.28619  67.17443 1.000 45.50145 ? 781 HOH A O   1 
HETATM 3160 O O   . HOH E 4 .   ? -22.58874 3.92704   43.64476 1.000 46.02561 ? 782 HOH A O   1 
HETATM 3161 O O   . HOH E 4 .   ? -21.80722 -5.75181  59.25851 1.000 45.96584 ? 783 HOH A O   1 
HETATM 3162 O O   . HOH E 4 .   ? -7.58115  -2.64293  70.39665 1.000 27.72172 ? 784 HOH A O   1 
HETATM 3163 O O   . HOH E 4 .   ? -17.87524 -2.33633  41.94114 1.000 39.43217 ? 785 HOH A O   1 
HETATM 3164 O O   . HOH E 4 .   ? -26.965   8.417     22.170   1.000 49.74810 ? 786 HOH A O   1 
HETATM 3165 O O   . HOH E 4 .   ? 4.46253   -1.29896  31.07584 1.000 59.28265 ? 787 HOH A O   1 
HETATM 3166 O O   . HOH E 4 .   ? -10.598   -12.206   39.758   1.000 52.53466 ? 788 HOH A O   1 
HETATM 3167 O O   . HOH E 4 .   ? 9.80665   -2.18574  40.10142 1.000 54.92545 ? 789 HOH A O   1 
HETATM 3168 O O   . HOH E 4 .   ? -13.19373 -1.97890  20.18402 1.000 52.97363 ? 790 HOH A O   1 
HETATM 3169 O O   . HOH E 4 .   ? -9.37922  18.76594  67.64839 1.000 49.95508 ? 791 HOH A O   1 
HETATM 3170 O O   . HOH E 4 .   ? -16.27119 -5.72171  42.23575 1.000 39.87784 ? 792 HOH A O   1 
HETATM 3171 O O   . HOH E 4 .   ? -7.62321  0.43790   76.06257 1.000 42.58003 ? 793 HOH A O   1 
HETATM 3172 O O   . HOH E 4 .   ? 11.19304  10.12707  73.91498 1.000 47.77403 ? 794 HOH A O   1 
HETATM 3173 O O   . HOH E 4 .   ? -8.830    25.372    24.504   1.000 52.51017 ? 795 HOH A O   1 
HETATM 3174 O O   . HOH E 4 .   ? -20.59384 9.09119   21.45113 1.000 44.65649 ? 796 HOH A O   1 
HETATM 3175 O O   . HOH E 4 .   ? -12.35632 15.88875  69.30698 1.000 39.75344 ? 797 HOH A O   1 
HETATM 3176 O O   . HOH E 4 .   ? -24.80120 24.42418  37.60826 1.000 51.04442 ? 798 HOH A O   1 
HETATM 3177 O O   . HOH E 4 .   ? -16.27890 -3.84817  67.96505 1.000 44.09214 ? 799 HOH A O   1 
HETATM 3178 O O   . HOH E 4 .   ? 11.92528  7.08265   59.27304 1.000 31.79968 ? 800 HOH A O   1 
HETATM 3179 O O   . HOH E 4 .   ? 6.667     24.082    65.201   1.000 46.37237 ? 801 HOH A O   1 
HETATM 3180 O O   . HOH E 4 .   ? 3.56627   18.31440  74.37996 1.000 38.08456 ? 802 HOH A O   1 
HETATM 3181 O O   . HOH E 4 .   ? -20.54004 -6.43206  57.45834 1.000 45.65924 ? 803 HOH A O   1 
HETATM 3182 O O   . HOH E 4 .   ? 2.758     26.681    63.665   1.000 46.48488 ? 804 HOH A O   1 
HETATM 3183 O O   . HOH E 4 .   ? -17.78146 10.16761  21.14658 1.000 40.08010 ? 805 HOH A O   1 
HETATM 3184 O O   . HOH E 4 .   ? -26.207   21.608    23.342   1.000 50.79310 ? 806 HOH A O   1 
HETATM 3185 O O   . HOH E 4 .   ? -12.73054 -10.74353 63.84536 1.000 34.59426 ? 807 HOH A O   1 
HETATM 3186 O O   . HOH E 4 .   ? -9.23099  -4.66819  71.63721 1.000 28.42292 ? 808 HOH A O   1 
HETATM 3187 O O   . HOH E 4 .   ? 8.13322   8.27612   67.22680 1.000 23.11289 ? 809 HOH A O   1 
HETATM 3188 O O   . HOH E 4 .   ? 11.83729  -3.27906  62.44488 1.000 50.05621 ? 810 HOH A O   1 
HETATM 3189 O O   . HOH E 4 .   ? 2.31041   5.91791   74.59920 1.000 42.94054 ? 811 HOH A O   1 
HETATM 3190 O O   . HOH E 4 .   ? -15.45946 -1.35258  38.88367 1.000 39.95446 ? 812 HOH A O   1 
HETATM 3191 O O   . HOH E 4 .   ? -1.53143  -10.25682 48.24990 1.000 38.02508 ? 813 HOH A O   1 
HETATM 3192 O O   . HOH E 4 .   ? 7.16424   2.21670   66.93350 1.000 33.79984 ? 814 HOH A O   1 
HETATM 3193 O O   . HOH E 4 .   ? -19.62951 6.53432   70.09380 1.000 46.12897 ? 815 HOH A O   1 
HETATM 3194 O O   . HOH E 4 .   ? -5.04658  21.41755  25.30264 1.000 46.61470 ? 816 HOH A O   1 
HETATM 3195 O O   . HOH E 4 .   ? 5.92053   -0.06415  66.98215 1.000 27.88761 ? 817 HOH A O   1 
HETATM 3196 O O   . HOH E 4 .   ? -10.25750 -2.78681  74.33767 1.000 37.76019 ? 818 HOH A O   1 
HETATM 3197 O O   . HOH E 4 .   ? 9.01796   -2.96380  67.38352 1.000 46.76573 ? 819 HOH A O   1 
HETATM 3198 O O   . HOH E 4 .   ? -5.15101  -2.89479  74.17462 1.000 56.80906 ? 820 HOH A O   1 
HETATM 3199 O O   . HOH E 4 .   ? -6.89920  5.44817   74.68103 1.000 43.12998 ? 821 HOH A O   1 
HETATM 3200 O O   . HOH E 4 .   ? -3.81852  20.78345  48.29433 1.000 38.14516 ? 822 HOH A O   1 
HETATM 3201 O O   . HOH E 4 .   ? 20.104    20.580    54.409   1.000 46.46261 ? 823 HOH A O   1 
HETATM 3202 O O   . HOH E 4 .   ? -28.70027 11.94766  40.61120 1.000 48.66300 ? 824 HOH A O   1 
HETATM 3203 O O   . HOH E 4 .   ? 23.10657  20.16313  67.97284 1.000 41.11930 ? 825 HOH A O   1 
HETATM 3204 O O   . HOH E 4 .   ? -25.799   5.446     23.390   1.000 44.56109 ? 826 HOH A O   1 
HETATM 3205 O O   . HOH E 4 .   ? -5.11867  19.38526  51.52151 1.000 33.87153 ? 827 HOH A O   1 
HETATM 3206 O O   . HOH E 4 .   ? 5.32028   23.61918  21.26361 1.000 56.74822 ? 828 HOH A O   1 
HETATM 3207 O O   . HOH E 4 .   ? -0.28377  7.81531   77.47680 1.000 32.87771 ? 829 HOH A O   1 
HETATM 3208 O O   . HOH E 4 .   ? 4.64095   26.10044  21.73478 1.000 57.41944 ? 830 HOH A O   1 
HETATM 3209 O O   . HOH E 4 .   ? 4.29814   7.06875   75.56152 1.000 42.76433 ? 831 HOH A O   1 
HETATM 3210 O O   . HOH E 4 .   ? -26.46479 -6.10773  45.49872 1.000 50.42407 ? 832 HOH A O   1 
HETATM 3211 O O   . HOH E 4 .   ? -27.31655 -7.26806  43.59093 1.000 60.29042 ? 833 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  ? 0.96684 0.93030 0.67820 0.13994  -0.07717 0.18845  9   PRO A N   
2    C CA  . PRO A 15  ? 0.81460 0.78275 0.53834 0.13399  -0.07465 0.17944  9   PRO A CA  
3    C C   . PRO A 15  ? 0.91636 0.86357 0.63167 0.15780  -0.06970 0.17805  9   PRO A C   
4    O O   . PRO A 15  ? 1.01407 0.91922 0.70303 0.17405  -0.06619 0.18302  9   PRO A O   
5    C CB  . PRO A 15  ? 0.79427 0.72184 0.49949 0.11197  -0.07163 0.17728  9   PRO A CB  
6    C CG  . PRO A 15  ? 0.83862 0.72691 0.51612 0.11140  -0.07032 0.18576  9   PRO A CG  
7    C CD  . PRO A 15  ? 0.86026 0.78522 0.54839 0.12235  -0.07573 0.19212  9   PRO A CD  
8    N N   . GLU A 16  ? 1.03265 1.00767 0.76873 0.15978  -0.06888 0.17096  10  GLU A N   
9    C CA  . GLU A 16  ? 0.97252 0.93047 0.70051 0.18276  -0.06353 0.16853  10  GLU A CA  
10   C C   . GLU A 16  ? 0.99641 0.88535 0.69112 0.17894  -0.05892 0.16479  10  GLU A C   
11   O O   . GLU A 16  ? 0.98427 0.86577 0.68362 0.15814  -0.05866 0.15676  10  GLU A O   
12   C CB  . GLU A 16  ? 0.94646 0.95497 0.70592 0.18347  -0.06356 0.16219  10  GLU A CB  
13   C CG  . GLU A 16  ? 0.93882 0.96391 0.70227 0.21273  -0.05900 0.16332  10  GLU A CG  
14   C CD  . GLU A 16  ? 0.84563 0.93336 0.64495 0.21068  -0.05914 0.15928  10  GLU A CD  
15   O OE1 . GLU A 16  ? 0.69704 0.83134 0.52234 0.19366  -0.06425 0.15955  10  GLU A OE1 
16   O OE2 . GLU A 16  ? 0.65645 0.74451 0.45597 0.22529  -0.05365 0.15550  10  GLU A OE2 
17   N N   . MET A 17  ? 1.14505 0.98337 0.80845 0.19563  -0.05473 0.16822  11  MET A N   
18   C CA  . MET A 17  ? 1.00422 0.77207 0.63300 0.19174  -0.05011 0.16308  11  MET A CA  
19   C C   . MET A 17  ? 0.98770 0.75428 0.61760 0.20570  -0.04668 0.15485  11  MET A C   
20   O O   . MET A 17  ? 1.08661 0.88677 0.73006 0.23006  -0.04463 0.15565  11  MET A O   
21   C CB  . MET A 17  ? 0.92647 0.63987 0.52014 0.20539  -0.04627 0.16851  11  MET A CB  
22   C CG  . MET A 17  ? 1.07083 0.77737 0.65781 0.19196  -0.04878 0.17729  11  MET A CG  
23   S SD  . MET A 17  ? 1.10536 0.81834 0.70183 0.15156  -0.05232 0.17586  11  MET A SD  
24   C CE  . MET A 17  ? 1.08458 0.71533 0.64308 0.13264  -0.04714 0.16917  11  MET A CE  
25   N N   . VAL A 18  ? 1.07414 0.80641 0.69357 0.18731  -0.04540 0.14518  12  VAL A N   
26   C CA  . VAL A 18  ? 1.07073 0.79672 0.68960 0.19679  -0.04174 0.13512  12  VAL A CA  
27   C C   . VAL A 18  ? 1.16305 0.81328 0.74454 0.18505  -0.03859 0.12698  12  VAL A C   
28   O O   . VAL A 18  ? 1.14526 0.77927 0.72828 0.15228  -0.04015 0.12160  12  VAL A O   
29   C CB  . VAL A 18  ? 1.01235 0.79568 0.67415 0.17824  -0.04349 0.12578  12  VAL A CB  
30   C CG1 . VAL A 18  ? 0.97047 0.74988 0.62970 0.19214  -0.03937 0.11716  12  VAL A CG1 
31   C CG2 . VAL A 18  ? 0.99468 0.85009 0.69180 0.18267  -0.04747 0.13338  12  VAL A CG2 
32   N N   . ARG A 19  ? 1.21383 0.81873 0.76095 0.21149  -0.03411 0.12597  13  ARG A N   
33   C CA  . ARG A 19  ? 1.20544 0.73176 0.71028 0.20192  -0.03135 0.11779  13  ARG A CA  
34   C C   . ARG A 19  ? 1.33714 0.81531 0.81709 0.17948  -0.03274 0.12294  13  ARG A C   
35   O O   . ARG A 19  ? 1.37975 0.81647 0.84385 0.15057  -0.03299 0.11479  13  ARG A O   
36   C CB  . ARG A 19  ? 1.21238 0.74595 0.73274 0.17769  -0.03188 0.10210  13  ARG A CB  
37   C CG  . ARG A 19  ? 1.16595 0.73579 0.70310 0.19898  -0.02936 0.09631  13  ARG A CG  
38   C CD  . ARG A 19  ? 1.24884 0.76511 0.74168 0.23295  -0.02370 0.09560  13  ARG A CD  
39   N NE  . ARG A 19  ? 1.18735 0.73930 0.69479 0.25426  -0.02020 0.09037  13  ARG A NE  
40   C CZ  . ARG A 19  ? 1.18604 0.72961 0.69244 0.24286  -0.01928 0.07682  13  ARG A CZ  
41   N NH1 . ARG A 19  ? 1.25306 0.75616 0.74569 0.21024  -0.02227 0.06673  13  ARG A NH1 
42   N NH2 . ARG A 19  ? 1.17454 0.75384 0.69406 0.26435  -0.01535 0.07385  13  ARG A NH2 
43   N N   . GLY A 20  ? 1.29122 0.78582 0.77594 0.18900  -0.03286 0.13394  14  GLY A N   
44   C CA  . GLY A 20  ? 1.35073 0.81083 0.81846 0.16690  -0.03330 0.13878  14  GLY A CA  
45   C C   . GLY A 20  ? 1.44091 0.92126 0.92789 0.13025  -0.03778 0.13905  14  GLY A C   
46   O O   . GLY A 20  ? 1.58688 1.02846 1.05607 0.10329  -0.03715 0.13850  14  GLY A O   
47   N N   . GLN A 21  ? 1.28861 0.84168 0.82285 0.12470  -0.04068 0.13542  15  GLN A N   
48   C CA  . GLN A 21  ? 1.15363 0.74375 0.71936 0.09068  -0.04325 0.13170  15  GLN A CA  
49   C C   . GLN A 21  ? 1.04376 0.70485 0.64693 0.09780  -0.04663 0.13723  15  GLN A C   
50   O O   . GLN A 21  ? 1.03981 0.73580 0.65737 0.12217  -0.04743 0.13882  15  GLN A O   
51   C CB  . GLN A 21  ? 1.15129 0.75112 0.73522 0.06827  -0.04335 0.11676  15  GLN A CB  
52   C CG  . GLN A 21  ? 1.17410 0.71233 0.72678 0.04651  -0.04176 0.11042  15  GLN A CG  
53   C CD  . GLN A 21  ? 1.13154 0.69018 0.70689 0.02175  -0.04312 0.09686  15  GLN A CD  
54   O OE1 . GLN A 21  ? 1.06924 0.68670 0.68405 0.01791  -0.04482 0.09310  15  GLN A OE1 
55   N NE2 . GLN A 21  ? 1.17489 0.68388 0.72348 0.00454  -0.04268 0.08967  15  GLN A NE2 
56   N N   . VAL A 22  ? 1.02407 0.70677 0.64175 0.07549  -0.04846 0.14010  16  VAL A N   
57   C CA  . VAL A 22  ? 0.85352 0.59937 0.50319 0.07795  -0.05223 0.14425  16  VAL A CA  
58   C C   . VAL A 22  ? 0.83729 0.63138 0.52421 0.06932  -0.05343 0.13318  16  VAL A C   
59   O O   . VAL A 22  ? 0.72705 0.51974 0.42461 0.04578  -0.05232 0.12353  16  VAL A O   
60   C CB  . VAL A 22  ? 0.98625 0.73689 0.63638 0.05704  -0.05313 0.14968  16  VAL A CB  
61   C CG1 . VAL A 22  ? 1.08769 0.81652 0.73675 0.02528  -0.05026 0.14173  16  VAL A CG1 
62   C CG2 . VAL A 22  ? 0.91310 0.72780 0.59631 0.05447  -0.05730 0.15048  16  VAL A CG2 
63   N N   . PHE A 23  ? 0.79445 0.63201 0.50046 0.08864  -0.05563 0.13525  17  PHE A N   
64   C CA  . PHE A 23  ? 0.79271 0.67971 0.53367 0.08129  -0.05698 0.12706  17  PHE A CA  
65   C C   . PHE A 23  ? 0.58610 0.52553 0.34802 0.08299  -0.06170 0.13378  17  PHE A C   
66   O O   . PHE A 23  ? 0.68549 0.65614 0.45509 0.10378  -0.06376 0.13968  17  PHE A O   
67   C CB  . PHE A 23  ? 0.66964 0.55949 0.41200 0.10114  -0.05477 0.12304  17  PHE A CB  
68   C CG  . PHE A 23  ? 0.62043 0.53070 0.38586 0.08624  -0.05394 0.11126  17  PHE A CG  
69   C CD1 . PHE A 23  ? 0.76492 0.63986 0.52033 0.07080  -0.05164 0.10177  17  PHE A CD1 
70   C CD2 . PHE A 23  ? 0.58955 0.55446 0.38546 0.08679  -0.05577 0.11021  17  PHE A CD2 
71   C CE1 . PHE A 23  ? 0.62115 0.51586 0.39666 0.05886  -0.05124 0.09182  17  PHE A CE1 
72   C CE2 . PHE A 23  ? 0.54769 0.52837 0.36212 0.07405  -0.05472 0.10042  17  PHE A CE2 
73   C CZ  . PHE A 23  ? 0.51185 0.45792 0.31621 0.06131  -0.05249 0.09140  17  PHE A CZ  
74   N N   . ASP A 24  ? 0.63043 0.58058 0.40059 0.06080  -0.06339 0.13286  18  ASP A N   
75   C CA  . ASP A 24  ? 0.60527 0.59254 0.38508 0.06010  -0.06827 0.13988  18  ASP A CA  
76   C C   . ASP A 24  ? 0.56492 0.59953 0.37577 0.04602  -0.07075 0.13253  18  ASP A C   
77   O O   . ASP A 24  ? 0.62658 0.66553 0.44543 0.02441  -0.07040 0.12670  18  ASP A O   
78   C CB  . ASP A 24  ? 0.68544 0.64894 0.44835 0.04628  -0.06782 0.14412  18  ASP A CB  
79   C CG  . ASP A 24  ? 0.60883 0.60732 0.37758 0.04497  -0.07311 0.15087  18  ASP A CG  
80   O OD1 . ASP A 24  ? 0.53539 0.56910 0.31351 0.06069  -0.07786 0.15614  18  ASP A OD1 
81   O OD2 . ASP A 24  ? 0.59157 0.58412 0.35505 0.02794  -0.07254 0.15097  18  ASP A OD2 
82   N N   . VAL A 25  ? 0.58991 0.65993 0.41681 0.05892  -0.07285 0.13338  19  VAL A N   
83   C CA  . VAL A 25  ? 0.52476 0.63549 0.37846 0.04595  -0.07476 0.12679  19  VAL A CA  
84   C C   . VAL A 25  ? 0.50551 0.66433 0.37306 0.05093  -0.08056 0.13278  19  VAL A C   
85   O O   . VAL A 25  ? 0.46418 0.65423 0.35393 0.04010  -0.08121 0.12642  19  VAL A O   
86   C CB  . VAL A 25  ? 0.36746 0.47784 0.23108 0.05017  -0.07085 0.11967  19  VAL A CB  
87   C CG1 . VAL A 25  ? 0.44053 0.50621 0.29228 0.04119  -0.06598 0.11185  19  VAL A CG1 
88   C CG2 . VAL A 25  ? 0.46743 0.58612 0.32685 0.07781  -0.07012 0.12642  19  VAL A CG2 
89   N N   . GLY A 26  ? 0.49461 0.65227 0.35241 0.06425  -0.08240 0.14016  20  GLY A N   
90   C CA  . GLY A 26  ? 0.59918 0.79732 0.47392 0.06764  -0.08559 0.14145  20  GLY A CA  
91   C C   . GLY A 26  ? 0.64773 0.86206 0.52954 0.04605  -0.08928 0.13736  20  GLY A C   
92   O O   . GLY A 26  ? 0.59912 0.79170 0.47080 0.03075  -0.08896 0.13419  20  GLY A O   
93   N N   . PRO A 27  ? 0.46999 0.72385 0.36856 0.04436  -0.09223 0.13749  21  PRO A N   
94   C CA  . PRO A 27  ? 0.40642 0.69180 0.31854 0.06143  -0.09149 0.14200  21  PRO A CA  
95   C C   . PRO A 27  ? 0.45999 0.77307 0.39448 0.05391  -0.08858 0.13651  21  PRO A C   
96   O O   . PRO A 27  ? 0.35306 0.69552 0.29960 0.06719  -0.08655 0.14035  21  PRO A O   
97   C CB  . PRO A 27  ? 0.47936 0.79489 0.39637 0.05975  -0.09633 0.14600  21  PRO A CB  
98   C CG  . PRO A 27  ? 0.45885 0.76524 0.37088 0.03621  -0.09943 0.14018  21  PRO A CG  
99   C CD  . PRO A 27  ? 0.39040 0.66014 0.29277 0.02625  -0.09611 0.13425  21  PRO A CD  
100  N N   . ARG A 28  ? 0.39823 0.70260 0.33730 0.03332  -0.08770 0.12816  22  ARG A N   
101  C CA  . ARG A 28  ? 0.38568 0.71400 0.34384 0.02440  -0.08486 0.12353  22  ARG A CA  
102  C C   . ARG A 28  ? 0.42426 0.75028 0.38404 0.04333  -0.08015 0.12558  22  ARG A C   
103  O O   . ARG A 28  ? 0.40794 0.76564 0.38345 0.04688  -0.07723 0.12666  22  ARG A O   
104  C CB  . ARG A 28  ? 0.34137 0.65397 0.30022 0.00087  -0.08436 0.11441  22  ARG A CB  
105  C CG  . ARG A 28  ? 0.41891 0.74800 0.39325 -0.00779 -0.08088 0.11016  22  ARG A CG  
106  C CD  . ARG A 28  ? 0.38701 0.70466 0.36156 -0.03190 -0.08070 0.10184  22  ARG A CD  
107  N NE  . ARG A 28  ? 0.30853 0.62990 0.29229 -0.03743 -0.07685 0.09821  22  ARG A NE  
108  C CZ  . ARG A 28  ? 0.35397 0.66254 0.33688 -0.05518 -0.07554 0.09135  22  ARG A CZ  
109  N NH1 . ARG A 28  ? 0.35562 0.64664 0.32888 -0.06874 -0.07721 0.08668  22  ARG A NH1 
110  N NH2 . ARG A 28  ? 0.39512 0.70759 0.38526 -0.05813 -0.07209 0.08940  22  ARG A NH2 
111  N N   . TYR A 29  ? 0.35911 0.64730 0.30070 0.05528  -0.07883 0.12649  23  TYR A N   
112  C CA  . TYR A 29  ? 0.38751 0.66493 0.32545 0.07244  -0.07417 0.12695  23  TYR A CA  
113  C C   . TYR A 29  ? 0.45706 0.72110 0.37927 0.10055  -0.07262 0.13481  23  TYR A C   
114  O O   . TYR A 29  ? 0.41335 0.64398 0.31435 0.10528  -0.07442 0.13837  23  TYR A O   
115  C CB  . TYR A 29  ? 0.39875 0.63972 0.32464 0.06348  -0.07326 0.12155  23  TYR A CB  
116  C CG  . TYR A 29  ? 0.32231 0.57342 0.26200 0.03722  -0.07414 0.11358  23  TYR A CG  
117  C CD1 . TYR A 29  ? 0.31317 0.58551 0.26916 0.03186  -0.07141 0.10952  23  TYR A CD1 
118  C CD2 . TYR A 29  ? 0.31447 0.55233 0.24902 0.01865  -0.07685 0.11029  23  TYR A CD2 
119  C CE1 . TYR A 29  ? 0.27800 0.55395 0.24316 0.00911  -0.07158 0.10257  23  TYR A CE1 
120  C CE2 . TYR A 29  ? 0.29353 0.53598 0.23770 -0.00284 -0.07659 0.10254  23  TYR A CE2 
121  C CZ  . TYR A 29  ? 0.35896 0.61863 0.31766 -0.00732 -0.07408 0.09883  23  TYR A CZ  
122  O OH  . TYR A 29  ? 0.31754 0.57640 0.28216 -0.02724 -0.07332 0.09175  23  TYR A OH  
123  N N   . THR A 30  ? 0.41081 0.70011 0.34197 0.11914  -0.06843 0.13779  24  THR A N   
124  C CA  . THR A 30  ? 0.55160 0.83261 0.46903 0.14820  -0.06563 0.14493  24  THR A CA  
125  C C   . THR A 30  ? 0.53337 0.81079 0.44762 0.16905  -0.05834 0.14384  24  THR A C   
126  O O   . THR A 30  ? 0.54938 0.83680 0.47465 0.16010  -0.05611 0.13837  24  THR A O   
127  C CB  . THR A 30  ? 0.55485 0.88068 0.48654 0.15293  -0.06723 0.15113  24  THR A CB  
128  O OG1 . THR A 30  ? 0.43419 0.81051 0.39169 0.14620  -0.06453 0.14994  24  THR A OG1 
129  C CG2 . THR A 30  ? 0.44603 0.77312 0.37776 0.13325  -0.07450 0.15159  24  THR A CG2 
130  N N   . ASN A 31  ? 0.56505 0.82622 0.46194 0.19787  -0.05414 0.14895  25  ASN A N   
131  C CA  . ASN A 31  ? 0.65641 0.90949 0.54443 0.22259  -0.04600 0.14785  25  ASN A CA  
132  C C   . ASN A 31  ? 0.65481 0.86275 0.52634 0.21761  -0.04485 0.14054  25  ASN A C   
133  O O   . ASN A 31  ? 0.64583 0.87094 0.53043 0.21010  -0.04280 0.13546  25  ASN A O   
134  C CB  . ASN A 31  ? 0.62207 0.93721 0.53797 0.22489  -0.04153 0.14883  25  ASN A CB  
135  C CG  . ASN A 31  ? 0.62950 0.94937 0.53500 0.25863  -0.03238 0.15207  25  ASN A CG  
136  O OD1 . ASN A 31  ? 0.70115 0.97091 0.57671 0.28017  -0.02877 0.15125  25  ASN A OD1 
137  N ND2 . ASN A 31  ? 0.69003 1.06853 0.61746 0.26283  -0.02795 0.15580  25  ASN A ND2 
138  N N   . LEU A 32  ? 0.61997 0.76831 0.46030 0.22137  -0.04606 0.14057  26  LEU A N   
139  C CA  . LEU A 32  ? 0.65030 0.75076 0.47086 0.21118  -0.04656 0.13423  26  LEU A CA  
140  C C   . LEU A 32  ? 0.78379 0.84122 0.57579 0.23592  -0.03970 0.13089  26  LEU A C   
141  O O   . LEU A 32  ? 0.84331 0.87318 0.61303 0.25893  -0.03571 0.13426  26  LEU A O   
142  C CB  . LEU A 32  ? 0.68871 0.74640 0.48887 0.19641  -0.05122 0.13605  26  LEU A CB  
143  C CG  . LEU A 32  ? 0.66773 0.74681 0.48964 0.16262  -0.05651 0.13271  26  LEU A CG  
144  C CD1 . LEU A 32  ? 0.65838 0.80074 0.51027 0.15825  -0.06059 0.13767  26  LEU A CD1 
145  C CD2 . LEU A 32  ? 0.81959 0.85447 0.62036 0.15060  -0.05824 0.13390  26  LEU A CD2 
146  N N   . SER A 33  ? 0.64770 0.69671 0.44101 0.22797  -0.03722 0.12165  27  SER A N   
147  C CA  . SER A 33  ? 0.71015 0.71324 0.47489 0.24584  -0.03073 0.11503  27  SER A CA  
148  C C   . SER A 33  ? 0.78079 0.73752 0.53479 0.21851  -0.03123 0.10186  27  SER A C   
149  O O   . SER A 33  ? 0.69968 0.68042 0.47864 0.19118  -0.03414 0.09641  27  SER A O   
150  C CB  . SER A 33  ? 0.64446 0.68948 0.42332 0.26463  -0.02535 0.11488  27  SER A CB  
151  O OG  . SER A 33  ? 0.79361 0.90705 0.60561 0.26782  -0.02528 0.12258  27  SER A OG  
152  N N   . TYR A 34  ? 0.79114 0.68128 0.50650 0.22616  -0.02850 0.09704  28  TYR A N   
153  C CA  . TYR A 34  ? 0.84835 0.69457 0.55101 0.20015  -0.02953 0.08486  28  TYR A CA  
154  C C   . TYR A 34  ? 0.91048 0.77187 0.62315 0.19733  -0.02684 0.07496  28  TYR A C   
155  O O   . TYR A 34  ? 0.90055 0.77299 0.60797 0.22311  -0.02165 0.07546  28  TYR A O   
156  C CB  . TYR A 34  ? 0.89047 0.65931 0.54550 0.20802  -0.02764 0.08266  28  TYR A CB  
157  C CG  . TYR A 34  ? 0.98924 0.71283 0.62903 0.17907  -0.02953 0.07067  28  TYR A CG  
158  C CD1 . TYR A 34  ? 0.96932 0.68276 0.61422 0.14889  -0.03406 0.07073  28  TYR A CD1 
159  C CD2 . TYR A 34  ? 0.96202 0.65606 0.58212 0.18182  -0.02684 0.05948  28  TYR A CD2 
160  C CE1 . TYR A 34  ? 0.93435 0.61310 0.56736 0.12192  -0.03601 0.06064  28  TYR A CE1 
161  C CE2 . TYR A 34  ? 1.01601 0.67319 0.62274 0.15416  -0.02964 0.04877  28  TYR A CE2 
162  C CZ  . TYR A 34  ? 1.02702 0.67861 0.64141 0.12408  -0.03431 0.04972  28  TYR A CZ  
163  O OH  . TYR A 34  ? 1.11762 0.73878 0.72058 0.09606  -0.03729 0.03983  28  TYR A OH  
164  N N   . ILE A 35  ? 0.90598 0.76934 0.63251 0.16696  -0.03007 0.06647  29  ILE A N   
165  C CA  . ILE A 35  ? 0.90386 0.78140 0.64007 0.16089  -0.02846 0.05733  29  ILE A CA  
166  C C   . ILE A 35  ? 1.01071 0.83813 0.72413 0.14220  -0.03019 0.04552  29  ILE A C   
167  O O   . ILE A 35  ? 1.06718 0.87310 0.76199 0.15026  -0.02744 0.03750  29  ILE A O   
168  C CB  . ILE A 35  ? 0.78147 0.71919 0.55950 0.14319  -0.03091 0.05888  29  ILE A CB  
169  C CG1 . ILE A 35  ? 0.77239 0.76345 0.57249 0.15983  -0.02951 0.06985  29  ILE A CG1 
170  C CG2 . ILE A 35  ? 0.97783 0.92458 0.76243 0.13589  -0.02940 0.04994  29  ILE A CG2 
171  C CD1 . ILE A 35  ? 0.76780 0.81311 0.60403 0.14254  -0.03133 0.07083  29  ILE A CD1 
172  N N   . GLY A 36  ? 0.93282 0.74375 0.64729 0.11644  -0.03483 0.04437  30  GLY A N   
173  C CA  . GLY A 36  ? 0.97392 0.74565 0.67072 0.09492  -0.03740 0.03399  30  GLY A CA  
174  C C   . GLY A 36  ? 0.96952 0.72794 0.66822 0.06837  -0.04162 0.03539  30  GLY A C   
175  O O   . GLY A 36  ? 0.88937 0.64607 0.58749 0.07115  -0.04178 0.04430  30  GLY A O   
176  N N   . GLU A 37  ? 0.91687 0.66876 0.61794 0.04284  -0.04497 0.02719  31  GLU A N   
177  C CA  . GLU A 37  ? 0.94778 0.69037 0.65102 0.01624  -0.04830 0.02818  31  GLU A CA  
178  C C   . GLU A 37  ? 0.96694 0.75280 0.70311 -0.00454 -0.05110 0.02456  31  GLU A C   
179  O O   . GLU A 37  ? 0.81338 0.60996 0.55488 -0.00741 -0.05215 0.01695  31  GLU A O   
180  C CB  . GLU A 37  ? 1.01226 0.69483 0.67785 0.00322  -0.04979 0.02232  31  GLU A CB  
181  C CG  . GLU A 37  ? 1.01037 0.63992 0.63753 0.02179  -0.04684 0.02679  31  GLU A CG  
182  C CD  . GLU A 37  ? 1.11855 0.74473 0.74617 0.01935  -0.04644 0.03811  31  GLU A CD  
183  O OE1 . GLU A 37  ? 1.08430 0.73079 0.73096 -0.00513 -0.04882 0.03994  31  GLU A OE1 
184  O OE2 . GLU A 37  ? 1.22651 0.83096 0.83471 0.04327  -0.04350 0.04556  31  GLU A OE2 
185  N N   . GLY A 38  ? 0.87994 0.68941 0.63597 -0.01739 -0.05204 0.03023  32  GLY A N   
186  C CA  . GLY A 38  ? 0.77257 0.61352 0.55333 -0.03842 -0.05427 0.02717  32  GLY A CA  
187  C C   . GLY A 38  ? 0.76574 0.58135 0.53293 -0.06242 -0.05664 0.02395  32  GLY A C   
188  O O   . GLY A 38  ? 0.87677 0.64620 0.61292 -0.06487 -0.05712 0.02185  32  GLY A O   
189  N N   . ALA A 39  ? 0.71611 0.56234 0.50570 -0.08065 -0.05789 0.02383  33  ALA A N   
190  C CA  . ALA A 39  ? 0.78945 0.62135 0.57049 -0.10554 -0.05995 0.02189  33  ALA A CA  
191  C C   . ALA A 39  ? 0.87314 0.67933 0.63855 -0.11178 -0.05806 0.02966  33  ALA A C   
192  O O   . ALA A 39  ? 0.77322 0.54225 0.51403 -0.12691 -0.05914 0.02878  33  ALA A O   
193  C CB  . ALA A 39  ? 0.76576 0.64261 0.57603 -0.12025 -0.06106 0.02026  33  ALA A CB  
194  N N   . TYR A 40  ? 0.78500 0.60898 0.56222 -0.10148 -0.05545 0.03753  34  TYR A N   
195  C CA  . TYR A 40  ? 0.83487 0.64237 0.60078 -0.10929 -0.05359 0.04576  34  TYR A CA  
196  C C   . TYR A 40  ? 0.81033 0.60146 0.56326 -0.08664 -0.05194 0.05325  34  TYR A C   
197  O O   . TYR A 40  ? 0.70186 0.49596 0.45440 -0.08690 -0.05044 0.06151  34  TYR A O   
198  C CB  . TYR A 40  ? 0.76393 0.61222 0.55564 -0.12219 -0.05219 0.04884  34  TYR A CB  
199  C CG  . TYR A 40  ? 0.78318 0.65474 0.59025 -0.14034 -0.05371 0.04221  34  TYR A CG  
200  C CD1 . TYR A 40  ? 0.83696 0.68388 0.62750 -0.15768 -0.05613 0.03781  34  TYR A CD1 
201  C CD2 . TYR A 40  ? 0.67281 0.59037 0.50912 -0.13988 -0.05304 0.04046  34  TYR A CD2 
202  C CE1 . TYR A 40  ? 0.83323 0.70633 0.63864 -0.17360 -0.05845 0.03219  34  TYR A CE1 
203  C CE2 . TYR A 40  ? 0.74185 0.68323 0.59204 -0.15352 -0.05450 0.03531  34  TYR A CE2 
204  C CZ  . TYR A 40  ? 0.77316 0.69523 0.60928 -0.17047 -0.05749 0.03144  34  TYR A CZ  
205  O OH  . TYR A 40  ? 0.70853 0.65924 0.55929 -0.18433 -0.05983 0.02688  34  TYR A OH  
206  N N   . GLY A 41  ? 0.79120 0.56743 0.53313 -0.06610 -0.05212 0.05084  35  GLY A N   
207  C CA  . GLY A 41  ? 0.72762 0.49405 0.45862 -0.04152 -0.05064 0.05833  35  GLY A CA  
208  C C   . GLY A 41  ? 0.67050 0.44402 0.40310 -0.01879 -0.05021 0.05453  35  GLY A C   
209  O O   . GLY A 41  ? 0.76329 0.55265 0.50783 -0.02223 -0.05104 0.04640  35  GLY A O   
210  N N   . MET A 42  ? 0.70019 0.46397 0.42027 0.00572  -0.04864 0.06135  36  MET A N   
211  C CA  . MET A 42  ? 0.73964 0.50934 0.45804 0.03022  -0.04704 0.05919  36  MET A CA  
212  C C   . MET A 42  ? 0.61018 0.44039 0.36485 0.03629  -0.04745 0.06081  36  MET A C   
213  O O   . MET A 42  ? 0.62507 0.48772 0.40218 0.02479  -0.04910 0.06429  36  MET A O   
214  C CB  . MET A 42  ? 0.85544 0.59202 0.54468 0.05651  -0.04468 0.06655  36  MET A CB  
215  C CG  . MET A 42  ? 0.80560 0.57556 0.50891 0.07165  -0.04501 0.07818  36  MET A CG  
216  S SD  . MET A 42  ? 1.00580 0.73581 0.67224 0.10515  -0.04229 0.08817  36  MET A SD  
217  C CE  . MET A 42  ? 0.96260 0.60970 0.58276 0.09123  -0.04108 0.08317  36  MET A CE  
218  N N   . VAL A 43  ? 0.63256 0.47601 0.39053 0.05406  -0.04558 0.05812  37  VAL A N   
219  C CA  . VAL A 43  ? 0.56530 0.46316 0.35409 0.06020  -0.04544 0.06004  37  VAL A CA  
220  C C   . VAL A 43  ? 0.64375 0.55302 0.42776 0.08932  -0.04305 0.06771  37  VAL A C   
221  O O   . VAL A 43  ? 0.74240 0.62072 0.50132 0.10854  -0.03995 0.06653  37  VAL A O   
222  C CB  . VAL A 43  ? 0.63192 0.54369 0.43212 0.05391  -0.04483 0.05096  37  VAL A CB  
223  C CG1 . VAL A 43  ? 0.55575 0.51993 0.38432 0.06000  -0.04404 0.05407  37  VAL A CG1 
224  C CG2 . VAL A 43  ? 0.55532 0.46161 0.36181 0.02696  -0.04751 0.04439  37  VAL A CG2 
225  N N   . CYS A 44  ? 0.59289 0.54689 0.39958 0.09285  -0.04452 0.07552  38  CYS A N   
226  C CA  . CYS A 44  ? 0.59643 0.57264 0.40332 0.11959  -0.04298 0.08441  38  CYS A CA  
227  C C   . CYS A 44  ? 0.52565 0.56243 0.36479 0.11896  -0.04337 0.08664  38  CYS A C   
228  O O   . CYS A 44  ? 0.46220 0.52320 0.32272 0.09707  -0.04611 0.08427  38  CYS A O   
229  C CB  . CYS A 44  ? 0.62628 0.59799 0.42471 0.12597  -0.04550 0.09470  38  CYS A CB  
230  S SG  . CYS A 44  ? 0.70652 0.60432 0.46049 0.13406  -0.04389 0.09597  38  CYS A SG  
231  N N   . SER A 45  ? 0.51376 0.57385 0.35450 0.14334  -0.04015 0.09145  39  SER A N   
232  C CA  . SER A 45  ? 0.46299 0.58513 0.33313 0.14381  -0.04101 0.09726  39  SER A CA  
233  C C   . SER A 45  ? 0.44285 0.59058 0.31896 0.14958  -0.04528 0.10834  39  SER A C   
234  O O   . SER A 45  ? 0.44930 0.56792 0.30421 0.16281  -0.04585 0.11310  39  SER A O   
235  C CB  . SER A 45  ? 0.53802 0.68259 0.41001 0.16665  -0.03525 0.09863  39  SER A CB  
236  O OG  . SER A 45  ? 0.50054 0.63369 0.35286 0.19790  -0.03234 0.10536  39  SER A OG  
237  N N   . ALA A 46  ? 0.46011 0.66132 0.36341 0.13847  -0.04862 0.11260  40  ALA A N   
238  C CA  . ALA A 46  ? 0.46592 0.69634 0.37741 0.13940  -0.05357 0.12177  40  ALA A CA  
239  C C   . ALA A 46  ? 0.42285 0.70937 0.36586 0.12635  -0.05317 0.12189  40  ALA A C   
240  O O   . ALA A 46  ? 0.36268 0.66329 0.31848 0.11195  -0.05219 0.11722  40  ALA A O   
241  C CB  . ALA A 46  ? 0.36957 0.57557 0.27376 0.11957  -0.05887 0.12062  40  ALA A CB  
242  N N   . TYR A 47  ? 0.37874 0.69533 0.33186 0.13075  -0.05379 0.12766  41  TYR A N   
243  C CA  . TYR A 47  ? 0.38027 0.74850 0.35949 0.11630  -0.05349 0.12888  41  TYR A CA  
244  C C   . TYR A 47  ? 0.34641 0.71603 0.33195 0.08828  -0.06003 0.12625  41  TYR A C   
245  O O   . TYR A 47  ? 0.30549 0.66461 0.28272 0.08851  -0.06435 0.12890  41  TYR A O   
246  C CB  . TYR A 47  ? 0.35803 0.76180 0.34365 0.13520  -0.05036 0.13674  41  TYR A CB  
247  C CG  . TYR A 47  ? 0.35094 0.80841 0.36048 0.11833  -0.05005 0.13922  41  TYR A CG  
248  C CD1 . TYR A 47  ? 0.33279 0.81756 0.35581 0.11181  -0.04485 0.13831  41  TYR A CD1 
249  C CD2 . TYR A 47  ? 0.41730 0.89640 0.43326 0.10780  -0.05498 0.14288  41  TYR A CD2 
250  C CE1 . TYR A 47  ? 0.28799 0.81831 0.32877 0.09417  -0.04441 0.14161  41  TYR A CE1 
251  C CE2 . TYR A 47  ? 0.30949 0.83460 0.34347 0.09053  -0.05493 0.14543  41  TYR A CE2 
252  C CZ  . TYR A 47  ? 0.33418 0.88375 0.37977 0.08318  -0.04958 0.14506  41  TYR A CZ  
253  O OH  . TYR A 47  ? 0.37142 0.96356 0.43103 0.06414  -0.04960 0.14860  41  TYR A OH  
254  N N   . ASP A 48  ? 0.34744 0.72728 0.34512 0.06506  -0.06021 0.12100  42  ASP A N   
255  C CA  . ASP A 48  ? 0.29978 0.68103 0.30210 0.03858  -0.06491 0.11757  42  ASP A CA  
256  C C   . ASP A 48  ? 0.38069 0.80455 0.39648 0.03299  -0.06560 0.12266  42  ASP A C   
257  O O   . ASP A 48  ? 0.31056 0.76670 0.33980 0.02706  -0.06210 0.12437  42  ASP A O   
258  C CB  . ASP A 48  ? 0.30898 0.68170 0.31583 0.01810  -0.06381 0.11046  42  ASP A CB  
259  C CG  . ASP A 48  ? 0.35202 0.71577 0.35793 -0.00713 -0.06761 0.10565  42  ASP A CG  
260  O OD1 . ASP A 48  ? 0.38392 0.76416 0.39235 -0.01401 -0.07051 0.10820  42  ASP A OD1 
261  O OD2 . ASP A 48  ? 0.48355 0.82317 0.48480 -0.01947 -0.06739 0.09913  42  ASP A OD2 
262  N N   . ASN A 49  ? 0.37673 0.80132 0.38739 0.03403  -0.07016 0.12570  43  ASN A N   
263  C CA  . ASN A 49  ? 0.45578 0.92215 0.47740 0.03018  -0.07148 0.13127  43  ASN A CA  
264  C C   . ASN A 49  ? 0.41352 0.89359 0.44254 0.00005  -0.07351 0.12753  43  ASN A C   
265  O O   . ASN A 49  ? 0.54128 1.05945 0.57984 -0.00699 -0.07394 0.13220  43  ASN A O   
266  C CB  . ASN A 49  ? 0.42514 0.88721 0.43721 0.04112  -0.07617 0.13588  43  ASN A CB  
267  C CG  . ASN A 49  ? 0.41508 0.87123 0.41898 0.07324  -0.07325 0.14214  43  ASN A CG  
268  O OD1 . ASN A 49  ? 0.43599 0.92693 0.44758 0.08842  -0.07056 0.14896  43  ASN A OD1 
269  N ND2 . ASN A 49  ? 0.38460 0.79514 0.37045 0.08381  -0.07325 0.14017  43  ASN A ND2 
270  N N   . LEU A 50  ? 0.37301 0.82194 0.39564 -0.01760 -0.07451 0.11959  44  LEU A N   
271  C CA  . LEU A 50  ? 0.40259 0.85734 0.42751 -0.04496 -0.07566 0.11582  44  LEU A CA  
272  C C   . LEU A 50  ? 0.56913 1.03860 0.60293 -0.05244 -0.07067 0.11595  44  LEU A C   
273  O O   . LEU A 50  ? 0.44672 0.94968 0.48820 -0.06222 -0.06989 0.12048  44  LEU A O   
274  C CB  . LEU A 50  ? 0.51330 0.92754 0.52497 -0.05915 -0.07811 0.10749  44  LEU A CB  
275  C CG  . LEU A 50  ? 0.43897 0.84746 0.44794 -0.08530 -0.07801 0.10231  44  LEU A CG  
276  C CD1 . LEU A 50  ? 0.51710 0.94441 0.52394 -0.09982 -0.08233 0.10418  44  LEU A CD1 
277  C CD2 . LEU A 50  ? 0.46888 0.83511 0.46523 -0.09310 -0.07774 0.09383  44  LEU A CD2 
278  N N   . ASN A 51  ? 0.39875 0.84421 0.43028 -0.04842 -0.06743 0.11159  45  ASN A N   
279  C CA  . ASN A 51  ? 0.41547 0.87210 0.45353 -0.05484 -0.06272 0.11184  45  ASN A CA  
280  C C   . ASN A 51  ? 0.42541 0.91626 0.47400 -0.03566 -0.05788 0.11914  45  ASN A C   
281  O O   . ASN A 51  ? 0.32166 0.82506 0.37534 -0.03910 -0.05341 0.12041  45  ASN A O   
282  C CB  . ASN A 51  ? 0.44770 0.86803 0.47906 -0.05654 -0.06122 0.10472  45  ASN A CB  
283  C CG  . ASN A 51  ? 0.54555 0.93643 0.56646 -0.07790 -0.06398 0.09774  45  ASN A CG  
284  O OD1 . ASN A 51  ? 0.66543 1.02428 0.67722 -0.07588 -0.06538 0.09221  45  ASN A OD1 
285  N ND2 . ASN A 51  ? 0.61769 1.01855 0.63750 -0.09826 -0.06458 0.09825  45  ASN A ND2 
286  N N   . LYS A 52  ? 0.39659 0.90248 0.44680 -0.01499 -0.05830 0.12433  46  LYS A N   
287  C CA  . LYS A 52  ? 0.35211 0.89167 0.41011 0.00657  -0.05287 0.13168  46  LYS A CA  
288  C C   . LYS A 52  ? 0.41804 0.94725 0.47540 0.01880  -0.04702 0.12969  46  LYS A C   
289  O O   . LYS A 52  ? 0.38161 0.94067 0.44636 0.02321  -0.04127 0.13416  46  LYS A O   
290  C CB  . LYS A 52  ? 0.33751 0.92502 0.40601 -0.00533 -0.05165 0.13871  46  LYS A CB  
291  C CG  . LYS A 52  ? 0.39783 0.98633 0.46442 -0.03389 -0.05769 0.13708  46  LYS A CG  
292  C CD  . LYS A 52  ? 0.50506 1.14180 0.57946 -0.04502 -0.05748 0.14499  46  LYS A CD  
293  C CE  . LYS A 52  ? 0.57780 1.21234 0.64679 -0.07052 -0.06442 0.14312  46  LYS A CE  
294  N NZ  . LYS A 52  ? 0.64482 1.26399 0.70705 -0.09898 -0.06512 0.13900  46  LYS A NZ  
295  N N   . VAL A 53  ? 0.41392 0.90083 0.46073 0.02391  -0.04862 0.12317  47  VAL A N   
296  C CA  . VAL A 53  ? 0.46562 0.93688 0.50803 0.03773  -0.04421 0.12054  47  VAL A CA  
297  C C   . VAL A 53  ? 0.36945 0.80309 0.39569 0.05809  -0.04619 0.11831  47  VAL A C   
298  O O   . VAL A 53  ? 0.37813 0.79020 0.39638 0.05384  -0.05160 0.11699  47  VAL A O   
299  C CB  . VAL A 53  ? 0.36859 0.82262 0.41102 0.01694  -0.04446 0.11434  47  VAL A CB  
300  C CG1 . VAL A 53  ? 0.47876 0.96167 0.53141 -0.00594 -0.04320 0.11711  47  VAL A CG1 
301  C CG2 . VAL A 53  ? 0.44083 0.85472 0.47277 0.00466  -0.05030 0.10741  47  VAL A CG2 
302  N N   . ARG A 54  ? 0.44353 0.86724 0.46181 0.08029  -0.04154 0.11825  48  ARG A N   
303  C CA  . ARG A 54  ? 0.39636 0.77551 0.39325 0.09674  -0.04340 0.11573  48  ARG A CA  
304  C C   . ARG A 54  ? 0.36930 0.71450 0.35773 0.08165  -0.04639 0.10829  48  ARG A C   
305  O O   . ARG A 54  ? 0.37447 0.72868 0.37094 0.06972  -0.04455 0.10510  48  ARG A O   
306  C CB  . ARG A 54  ? 0.29964 0.67436 0.28489 0.12849  -0.03696 0.11813  48  ARG A CB  
307  C CG  . ARG A 54  ? 0.57361 0.95044 0.55122 0.15063  -0.03592 0.12432  48  ARG A CG  
308  C CD  . ARG A 54  ? 0.37443 0.73940 0.33544 0.18412  -0.02834 0.12569  48  ARG A CD  
309  N NE  . ARG A 54  ? 0.46334 0.76870 0.39352 0.19875  -0.02996 0.12303  48  ARG A NE  
310  C CZ  . ARG A 54  ? 0.50059 0.78136 0.41642 0.20586  -0.03313 0.12638  48  ARG A CZ  
311  N NH1 . ARG A 54  ? 0.47434 0.78651 0.40431 0.20185  -0.03554 0.13225  48  ARG A NH1 
312  N NH2 . ARG A 54  ? 0.51439 0.73569 0.39851 0.21643  -0.03385 0.12402  48  ARG A NH2 
313  N N   . VAL A 55  ? 0.35221 0.65793 0.32338 0.08128  -0.05039 0.10584  49  VAL A N   
314  C CA  . VAL A 55  ? 0.29541 0.56344 0.26047 0.06230  -0.05053 0.09588  49  VAL A CA  
315  C C   . VAL A 55  ? 0.30978 0.52706 0.25181 0.07340  -0.04826 0.09087  49  VAL A C   
316  O O   . VAL A 55  ? 0.35509 0.56046 0.28310 0.09446  -0.04704 0.09513  49  VAL A O   
317  C CB  . VAL A 55  ? 0.37777 0.64644 0.34771 0.03986  -0.05619 0.09513  49  VAL A CB  
318  C CG1 . VAL A 55  ? 0.35574 0.66363 0.34455 0.02316  -0.05786 0.09699  49  VAL A CG1 
319  C CG2 . VAL A 55  ? 0.27781 0.54277 0.23901 0.04788  -0.06016 0.10132  49  VAL A CG2 
320  N N   . ALA A 56  ? 0.35782 0.54481 0.29474 0.05862  -0.04781 0.08197  50  ALA A N   
321  C CA  . ALA A 56  ? 0.29686 0.43559 0.21243 0.06113  -0.04694 0.07644  50  ALA A CA  
322  C C   . ALA A 56  ? 0.34968 0.47165 0.26282 0.04382  -0.05062 0.07536  50  ALA A C   
323  O O   . ALA A 56  ? 0.37590 0.51484 0.30289 0.02644  -0.05270 0.07407  50  ALA A O   
324  C CB  . ALA A 56  ? 0.29601 0.41656 0.20730 0.05696  -0.04406 0.06744  50  ALA A CB  
325  N N   . ILE A 57  ? 0.33953 0.42656 0.23287 0.04890  -0.05090 0.07617  51  ILE A N   
326  C CA  . ILE A 57  ? 0.40232 0.47323 0.29112 0.03378  -0.05346 0.07634  51  ILE A CA  
327  C C   . ILE A 57  ? 0.38522 0.40989 0.25320 0.02982  -0.05204 0.07125  51  ILE A C   
328  O O   . ILE A 57  ? 0.43775 0.43385 0.28504 0.04472  -0.05039 0.07242  51  ILE A O   
329  C CB  . ILE A 57  ? 0.33029 0.41084 0.21544 0.04142  -0.05619 0.08595  51  ILE A CB  
330  C CG1 . ILE A 57  ? 0.30808 0.43808 0.21372 0.04316  -0.05865 0.09108  51  ILE A CG1 
331  C CG2 . ILE A 57  ? 0.33201 0.39632 0.21133 0.02521  -0.05805 0.08611  51  ILE A CG2 
332  C CD1 . ILE A 57  ? 0.33841 0.48437 0.24173 0.05014  -0.06259 0.10075  51  ILE A CD1 
333  N N   . LYS A 58  ? 0.33350 0.35079 0.20558 0.00969  -0.05261 0.06579  52  LYS A N   
334  C CA  . LYS A 58  ? 0.43445 0.41415 0.28972 0.00017  -0.05198 0.06108  52  LYS A CA  
335  C C   . LYS A 58  ? 0.38514 0.35345 0.23387 -0.01099 -0.05286 0.06548  52  LYS A C   
336  O O   . LYS A 58  ? 0.37167 0.36252 0.23507 -0.02272 -0.05361 0.06599  52  LYS A O   
337  C CB  . LYS A 58  ? 0.37425 0.35962 0.24003 -0.01404 -0.05182 0.05244  52  LYS A CB  
338  C CG  . LYS A 58  ? 0.35580 0.31082 0.20785 -0.02839 -0.05212 0.04772  52  LYS A CG  
339  C CD  . LYS A 58  ? 0.43132 0.39593 0.29327 -0.03835 -0.05263 0.03961  52  LYS A CD  
340  C CE  . LYS A 58  ? 0.39077 0.39078 0.27672 -0.04611 -0.05253 0.03947  52  LYS A CE  
341  N NZ  . LYS A 58  ? 0.37025 0.37822 0.26412 -0.05653 -0.05315 0.03286  52  LYS A NZ  
342  N N   . LYS A 59  ? 0.44273 0.37387 0.26697 -0.00705 -0.05231 0.06876  53  LYS A N   
343  C CA  . LYS A 59  ? 0.45595 0.37154 0.27020 -0.01870 -0.05242 0.07354  53  LYS A CA  
344  C C   . LYS A 59  ? 0.54288 0.44256 0.35438 -0.04059 -0.05159 0.06746  53  LYS A C   
345  O O   . LYS A 59  ? 0.56499 0.44116 0.36526 -0.04303 -0.05146 0.06161  53  LYS A O   
346  C CB  . LYS A 59  ? 0.58504 0.46539 0.37144 -0.00453 -0.05196 0.08124  53  LYS A CB  
347  C CG  . LYS A 59  ? 0.55306 0.40419 0.32160 -0.01904 -0.05117 0.08557  53  LYS A CG  
348  C CD  . LYS A 59  ? 0.60933 0.42447 0.34828 -0.00273 -0.05066 0.09475  53  LYS A CD  
349  C CE  . LYS A 59  ? 0.68252 0.49367 0.41408 -0.01200 -0.05060 0.10341  53  LYS A CE  
350  N NZ  . LYS A 59  ? 0.71110 0.46650 0.40769 -0.01704 -0.04854 0.10784  53  LYS A NZ  
351  N N   . ILE A 60  ? 0.48625 0.40082 0.30749 -0.05642 -0.05109 0.06885  54  ILE A N   
352  C CA  . ILE A 60  ? 0.45611 0.36661 0.27924 -0.07761 -0.05000 0.06436  54  ILE A CA  
353  C C   . ILE A 60  ? 0.55997 0.45511 0.36997 -0.08907 -0.04826 0.07122  54  ILE A C   
354  O O   . ILE A 60  ? 0.51692 0.42627 0.33028 -0.08561 -0.04778 0.07722  54  ILE A O   
355  C CB  . ILE A 60  ? 0.45318 0.40279 0.30306 -0.08520 -0.04968 0.05907  54  ILE A CB  
356  C CG1 . ILE A 60  ? 0.44588 0.41307 0.30838 -0.07226 -0.05105 0.05464  54  ILE A CG1 
357  C CG2 . ILE A 60  ? 0.51289 0.46285 0.36600 -0.10386 -0.04892 0.05420  54  ILE A CG2 
358  C CD1 . ILE A 60  ? 0.53342 0.53148 0.41755 -0.07869 -0.05058 0.04944  54  ILE A CD1 
359  N N   . SER A 61  ? 0.52444 0.39080 0.31826 -0.10409 -0.04745 0.07044  55  SER A N   
360  C CA  . SER A 61  ? 0.57052 0.41964 0.34965 -0.11830 -0.04508 0.07747  55  SER A CA  
361  C C   . SER A 61  ? 0.56632 0.42474 0.35297 -0.14305 -0.04379 0.07334  55  SER A C   
362  O O   . SER A 61  ? 0.62947 0.45717 0.39802 -0.15672 -0.04432 0.07211  55  SER A O   
363  C CB  . SER A 61  ? 0.58416 0.38120 0.32878 -0.11234 -0.04516 0.08318  55  SER A CB  
364  O OG  . SER A 61  ? 0.66549 0.45885 0.40461 -0.08651 -0.04645 0.08716  55  SER A OG  
365  N N   . PRO A 62  ? 0.57823 0.47906 0.39019 -0.14947 -0.04208 0.07130  56  PRO A N   
366  C CA  . PRO A 62  ? 0.52752 0.44717 0.35163 -0.16906 -0.04129 0.06668  56  PRO A CA  
367  C C   . PRO A 62  ? 0.58871 0.52183 0.41455 -0.18733 -0.03676 0.07236  56  PRO A C   
368  O O   . PRO A 62  ? 0.46673 0.41575 0.30069 -0.20541 -0.03599 0.07012  56  PRO A O   
369  C CB  . PRO A 62  ? 0.51808 0.47700 0.36898 -0.15923 -0.04199 0.06025  56  PRO A CB  
370  C CG  . PRO A 62  ? 0.52053 0.49094 0.37559 -0.14495 -0.04047 0.06458  56  PRO A CG  
371  C CD  . PRO A 62  ? 0.50802 0.44279 0.33953 -0.13616 -0.04171 0.07100  56  PRO A CD  
372  N N   . PHE A 63  ? 0.52931 0.45933 0.34767 -0.18308 -0.03374 0.08010  57  PHE A N   
373  C CA  . PHE A 63  ? 0.60000 0.55661 0.42665 -0.19521 -0.02828 0.08447  57  PHE A CA  
374  C C   . PHE A 63  ? 0.63301 0.57667 0.44706 -0.21981 -0.02543 0.08959  57  PHE A C   
375  O O   . PHE A 63  ? 0.55653 0.52940 0.38078 -0.23188 -0.02020 0.09268  57  PHE A O   
376  C CB  . PHE A 63  ? 0.52287 0.48083 0.34360 -0.18320 -0.02626 0.09078  57  PHE A CB  
377  C CG  . PHE A 63  ? 0.44372 0.41812 0.27705 -0.16301 -0.02918 0.08619  57  PHE A CG  
378  C CD1 . PHE A 63  ? 0.40994 0.41966 0.26576 -0.16037 -0.02799 0.07952  57  PHE A CD1 
379  C CD2 . PHE A 63  ? 0.54329 0.49834 0.36509 -0.14682 -0.03299 0.08907  57  PHE A CD2 
380  C CE1 . PHE A 63  ? 0.43480 0.45655 0.29981 -0.14478 -0.03062 0.07555  57  PHE A CE1 
381  C CE2 . PHE A 63  ? 0.50373 0.47744 0.33793 -0.13137 -0.03586 0.08536  57  PHE A CE2 
382  C CZ  . PHE A 63  ? 0.42421 0.42943 0.27923 -0.13176 -0.03471 0.07846  57  PHE A CZ  
383  N N   . GLU A 64  ? 0.57587 0.47677 0.36687 -0.22812 -0.02826 0.09063  58  GLU A N   
384  C CA  . GLU A 64  ? 0.74737 0.63558 0.52549 -0.25560 -0.02585 0.09534  58  GLU A CA  
385  C C   . GLU A 64  ? 0.67594 0.59575 0.47425 -0.26919 -0.02776 0.08659  58  GLU A C   
386  O O   . GLU A 64  ? 0.66707 0.59230 0.46350 -0.28499 -0.02651 0.08665  58  GLU A O   
387  C CB  . GLU A 64  ? 0.74292 0.56878 0.48498 -0.25825 -0.02829 0.09833  58  GLU A CB  
388  C CG  . GLU A 64  ? 0.68122 0.47856 0.40123 -0.24697 -0.02556 0.10853  58  GLU A CG  
389  C CD  . GLU A 64  ? 0.78442 0.58126 0.49806 -0.26138 -0.02104 0.11300  58  GLU A CD  
390  O OE1 . GLU A 64  ? 0.77091 0.61142 0.50553 -0.26487 -0.01668 0.11433  58  GLU A OE1 
391  O OE2 . GLU A 64  ? 0.83372 0.58539 0.51982 -0.26861 -0.02152 0.11524  58  GLU A OE2 
392  N N   . HIS A 65  ? 0.72417 0.66737 0.54161 -0.26206 -0.03094 0.07950  59  HIS A N   
393  C CA  . HIS A 65  ? 0.77780 0.74852 0.61127 -0.27213 -0.03396 0.07158  59  HIS A CA  
394  C C   . HIS A 65  ? 0.67425 0.69676 0.53935 -0.26096 -0.03307 0.06732  59  HIS A C   
395  O O   . HIS A 65  ? 0.58639 0.60973 0.45779 -0.24062 -0.03433 0.06423  59  HIS A O   
396  C CB  . HIS A 65  ? 0.68026 0.61285 0.49584 -0.27647 -0.04075 0.06536  59  HIS A CB  
397  C CG  . HIS A 65  ? 0.86419 0.74528 0.64640 -0.28863 -0.04147 0.06802  59  HIS A CG  
398  N ND1 . HIS A 65  ? 0.94239 0.76660 0.69472 -0.28547 -0.04541 0.06593  59  HIS A ND1 
399  C CD2 . HIS A 65  ? 0.77958 0.65593 0.55184 -0.30339 -0.03856 0.07239  59  HIS A CD2 
400  C CE1 . HIS A 65  ? 0.84067 0.62544 0.56498 -0.29673 -0.04472 0.06869  59  HIS A CE1 
401  N NE2 . HIS A 65  ? 0.86950 0.68577 0.60607 -0.30905 -0.04081 0.07279  59  HIS A NE2 
402  N N   . GLN A 66  ? 0.54246 0.60669 0.42559 -0.26668 -0.03095 0.06574  60  GLN A N   
403  C CA  . GLN A 66  ? 0.55670 0.66941 0.46722 -0.25473 -0.02919 0.06236  60  GLN A CA  
404  C C   . GLN A 66  ? 0.48893 0.60186 0.40664 -0.24588 -0.03524 0.05489  60  GLN A C   
405  O O   . GLN A 66  ? 0.44378 0.57538 0.37582 -0.23062 -0.03465 0.05276  60  GLN A O   
406  C CB  . GLN A 66  ? 0.62814 0.78000 0.55174 -0.26359 -0.02658 0.06296  60  GLN A CB  
407  C CG  . GLN A 66  ? 0.50657 0.70184 0.45328 -0.25466 -0.02746 0.05825  60  GLN A CG  
408  C CD  . GLN A 66  ? 0.62792 0.86020 0.59213 -0.23980 -0.02074 0.06021  60  GLN A CD  
409  O OE1 . GLN A 66  ? 0.57281 0.80598 0.53330 -0.23998 -0.01484 0.06528  60  GLN A OE1 
410  N NE2 . GLN A 66  ? 0.57529 0.83689 0.55655 -0.22643 -0.02130 0.05628  60  GLN A NE2 
411  N N   . THR A 67  ? 0.57776 0.66830 0.48362 -0.25533 -0.04116 0.05056  61  THR A N   
412  C CA  . THR A 67  ? 0.53904 0.62933 0.44967 -0.24697 -0.04716 0.04297  61  THR A CA  
413  C C   . THR A 67  ? 0.53932 0.60160 0.44192 -0.22875 -0.04851 0.04148  61  THR A C   
414  O O   . THR A 67  ? 0.45156 0.52885 0.36652 -0.21123 -0.04976 0.03707  61  THR A O   
415  C CB  . THR A 67  ? 0.52790 0.59487 0.42240 -0.26056 -0.05269 0.03843  61  THR A CB  
416  O OG1 . THR A 67  ? 0.65317 0.66669 0.51805 -0.27013 -0.05378 0.04061  61  THR A OG1 
417  C CG2 . THR A 67  ? 0.48317 0.58196 0.38655 -0.27356 -0.05113 0.03983  61  THR A CG2 
418  N N   . TYR A 68  ? 0.58797 0.60891 0.46842 -0.22732 -0.04734 0.04549  62  TYR A N   
419  C CA  . TYR A 68  ? 0.54776 0.54556 0.42067 -0.20422 -0.04800 0.04442  62  TYR A CA  
420  C C   . TYR A 68  ? 0.48299 0.50936 0.37362 -0.18823 -0.04396 0.04665  62  TYR A C   
421  O O   . TYR A 68  ? 0.47358 0.50269 0.37001 -0.17018 -0.04516 0.04365  62  TYR A O   
422  C CB  . TYR A 68  ? 0.54009 0.48904 0.38445 -0.20358 -0.04772 0.04916  62  TYR A CB  
423  C CG  . TYR A 68  ? 0.73964 0.64882 0.55865 -0.21996 -0.05113 0.04716  62  TYR A CG  
424  C CD1 . TYR A 68  ? 0.72076 0.63077 0.53995 -0.22670 -0.05618 0.03885  62  TYR A CD1 
425  C CD2 . TYR A 68  ? 0.75285 0.61700 0.54311 -0.22572 -0.04973 0.05321  62  TYR A CD2 
426  C CE1 . TYR A 68  ? 0.68673 0.55529 0.47837 -0.24241 -0.05981 0.03586  62  TYR A CE1 
427  C CE2 . TYR A 68  ? 0.76555 0.58491 0.52711 -0.24027 -0.05278 0.05083  62  TYR A CE2 
428  C CZ  . TYR A 68  ? 0.79449 0.61574 0.55646 -0.24936 -0.05793 0.04165  62  TYR A CZ  
429  O OH  . TYR A 68  ? 0.83031 0.60314 0.55996 -0.26546 -0.06137 0.03829  62  TYR A OH  
430  N N   . CYS A 69  ? 0.40839 0.45593 0.30623 -0.19565 -0.03892 0.05184  63  CYS A N   
431  C CA  . CYS A 69  ? 0.44977 0.52231 0.36102 -0.18200 -0.03487 0.05298  63  CYS A CA  
432  C C   . CYS A 69  ? 0.34479 0.44896 0.27615 -0.17310 -0.03545 0.04709  63  CYS A C   
433  O O   . CYS A 69  ? 0.40509 0.51450 0.34191 -0.15718 -0.03491 0.04523  63  CYS A O   
434  C CB  . CYS A 69  ? 0.50074 0.58956 0.41322 -0.19220 -0.02865 0.05923  63  CYS A CB  
435  S SG  . CYS A 69  ? 0.51689 0.56895 0.40399 -0.19873 -0.02687 0.06805  63  CYS A SG  
436  N N   . GLN A 70  ? 0.39078 0.51658 0.33222 -0.18381 -0.03673 0.04463  64  GLN A N   
437  C CA  . GLN A 70  ? 0.36913 0.52306 0.32742 -0.17389 -0.03786 0.03975  64  GLN A CA  
438  C C   . GLN A 70  ? 0.32120 0.45599 0.27534 -0.16044 -0.04253 0.03489  64  GLN A C   
439  O O   . GLN A 70  ? 0.40175 0.54645 0.36365 -0.14527 -0.04151 0.03302  64  GLN A O   
440  C CB  . GLN A 70  ? 0.37303 0.55429 0.34155 -0.18829 -0.04002 0.03845  64  GLN A CB  
441  C CG  . GLN A 70  ? 0.37158 0.59392 0.35486 -0.19381 -0.03422 0.04249  64  GLN A CG  
442  C CD  . GLN A 70  ? 0.49629 0.72976 0.47934 -0.20773 -0.03520 0.04295  64  GLN A CD  
443  O OE1 . GLN A 70  ? 0.45754 0.66456 0.42714 -0.21981 -0.04019 0.04108  64  GLN A OE1 
444  N NE2 . GLN A 70  ? 0.53973 0.81361 0.53711 -0.20551 -0.03087 0.04510  64  GLN A NE2 
445  N N   . ARG A 71  ? 0.37035 0.47656 0.31042 -0.16606 -0.04725 0.03288  65  ARG A N   
446  C CA  . ARG A 71  ? 0.39957 0.48940 0.33480 -0.15285 -0.05089 0.02851  65  ARG A CA  
447  C C   . ARG A 71  ? 0.42041 0.50151 0.35426 -0.13667 -0.04857 0.03077  65  ARG A C   
448  O O   . ARG A 71  ? 0.37986 0.46716 0.31971 -0.12380 -0.04924 0.02832  65  ARG A O   
449  C CB  . ARG A 71  ? 0.48280 0.53808 0.39806 -0.16042 -0.05516 0.02617  65  ARG A CB  
450  C CG  . ARG A 71  ? 0.55825 0.59645 0.46629 -0.14570 -0.05799 0.02180  65  ARG A CG  
451  C CD  . ARG A 71  ? 0.53647 0.54461 0.42428 -0.15400 -0.06244 0.01720  65  ARG A CD  
452  N NE  . ARG A 71  ? 0.52212 0.51187 0.40015 -0.13750 -0.06376 0.01361  65  ARG A NE  
453  C CZ  . ARG A 71  ? 0.51522 0.47862 0.37414 -0.13937 -0.06733 0.00795  65  ARG A CZ  
454  N NH1 . ARG A 71  ? 0.57910 0.52829 0.42511 -0.15915 -0.07090 0.00481  65  ARG A NH1 
455  N NH2 . ARG A 71  ? 0.49305 0.44424 0.34436 -0.12171 -0.06717 0.00532  65  ARG A NH2 
456  N N   . THR A 72  ? 0.36838 0.43645 0.29378 -0.13826 -0.04607 0.03595  66  THR A N   
457  C CA  . THR A 72  ? 0.36693 0.43017 0.29075 -0.12495 -0.04487 0.03855  66  THR A CA  
458  C C   . THR A 72  ? 0.32622 0.41556 0.26395 -0.11906 -0.04185 0.03786  66  THR A C   
459  O O   . THR A 72  ? 0.24305 0.33493 0.18406 -0.10810 -0.04247 0.03666  66  THR A O   
460  C CB  . THR A 72  ? 0.40451 0.44878 0.31433 -0.12844 -0.04346 0.04482  66  THR A CB  
461  O OG1 . THR A 72  ? 0.45932 0.47243 0.35165 -0.13242 -0.04592 0.04550  66  THR A OG1 
462  C CG2 . THR A 72  ? 0.36147 0.40499 0.26991 -0.11538 -0.04344 0.04777  66  THR A CG2 
463  N N   . LEU A 73  ? 0.30464 0.41296 0.24915 -0.12634 -0.03819 0.03875  67  LEU A N   
464  C CA  . LEU A 73  ? 0.33163 0.45970 0.28464 -0.11919 -0.03438 0.03787  67  LEU A CA  
465  C C   . LEU A 73  ? 0.21392 0.35253 0.17587 -0.11007 -0.03571 0.03339  67  LEU A C   
466  O O   . LEU A 73  ? 0.29985 0.43788 0.26187 -0.10073 -0.03484 0.03231  67  LEU A O   
467  C CB  . LEU A 73  ? 0.34202 0.49065 0.29999 -0.12679 -0.02928 0.03985  67  LEU A CB  
468  C CG  . LEU A 73  ? 0.35703 0.52131 0.31867 -0.11752 -0.02406 0.03887  67  LEU A CG  
469  C CD1 . LEU A 73  ? 0.36481 0.51234 0.31608 -0.11118 -0.02423 0.03935  67  LEU A CD1 
470  C CD2 . LEU A 73  ? 0.28477 0.47079 0.24991 -0.12352 -0.01783 0.04166  67  LEU A CD2 
471  N N   . ARG A 74  ? 0.26287 0.41068 0.23083 -0.11373 -0.03806 0.03100  68  ARG A N   
472  C CA  . ARG A 74  ? 0.28016 0.43953 0.25559 -0.10445 -0.03913 0.02768  68  ARG A CA  
473  C C   . ARG A 74  ? 0.21710 0.35944 0.18752 -0.09588 -0.04184 0.02631  68  ARG A C   
474  O O   . ARG A 74  ? 0.23239 0.37852 0.20523 -0.08666 -0.04075 0.02534  68  ARG A O   
475  C CB  . ARG A 74  ? 0.35915 0.53382 0.34101 -0.11101 -0.04223 0.02567  68  ARG A CB  
476  C CG  . ARG A 74  ? 0.49280 0.64818 0.46608 -0.11820 -0.04770 0.02354  68  ARG A CG  
477  C CD  . ARG A 74  ? 0.54186 0.71360 0.51995 -0.12684 -0.05174 0.02084  68  ARG A CD  
478  N NE  . ARG A 74  ? 0.54342 0.74086 0.53031 -0.13828 -0.04970 0.02337  68  ARG A NE  
479  C CZ  . ARG A 74  ? 0.53155 0.73304 0.51654 -0.15617 -0.05299 0.02307  68  ARG A CZ  
480  N NH1 . ARG A 74  ? 0.66450 0.84022 0.63585 -0.16438 -0.05851 0.01957  68  ARG A NH1 
481  N NH2 . ARG A 74  ? 0.57360 0.80365 0.56853 -0.16540 -0.04986 0.02639  68  ARG A NH2 
482  N N   . GLU A 75  ? 0.29125 0.41429 0.25328 -0.09837 -0.04483 0.02675  69  GLU A N   
483  C CA  . GLU A 75  ? 0.28987 0.40155 0.24806 -0.08930 -0.04655 0.02641  69  GLU A CA  
484  C C   . GLU A 75  ? 0.28588 0.39876 0.24432 -0.08413 -0.04433 0.02884  69  GLU A C   
485  O O   . GLU A 75  ? 0.24866 0.36439 0.20926 -0.07763 -0.04424 0.02828  69  GLU A O   
486  C CB  . GLU A 75  ? 0.27841 0.36893 0.22539 -0.09025 -0.04913 0.02712  69  GLU A CB  
487  C CG  . GLU A 75  ? 0.25928 0.34319 0.20317 -0.07933 -0.04972 0.02853  69  GLU A CG  
488  C CD  . GLU A 75  ? 0.41903 0.48355 0.35117 -0.07512 -0.05183 0.02768  69  GLU A CD  
489  O OE1 . GLU A 75  ? 0.43725 0.48385 0.35820 -0.07733 -0.05218 0.03010  69  GLU A OE1 
490  O OE2 . GLU A 75  ? 0.31327 0.37846 0.24508 -0.06866 -0.05273 0.02480  69  GLU A OE2 
491  N N   . ILE A 76  ? 0.28206 0.39224 0.23668 -0.08835 -0.04270 0.03172  70  ILE A N   
492  C CA  . ILE A 76  ? 0.19976 0.31051 0.15211 -0.08550 -0.04161 0.03351  70  ILE A CA  
493  C C   . ILE A 76  ? 0.28542 0.40514 0.24108 -0.08284 -0.03863 0.03100  70  ILE A C   
494  O O   . ILE A 76  ? 0.30983 0.42779 0.26385 -0.07948 -0.03888 0.03063  70  ILE A O   
495  C CB  . ILE A 76  ? 0.27785 0.38390 0.22322 -0.09058 -0.04065 0.03710  70  ILE A CB  
496  C CG1 . ILE A 76  ? 0.33483 0.42678 0.27299 -0.09027 -0.04358 0.04060  70  ILE A CG1 
497  C CG2 . ILE A 76  ? 0.29194 0.40041 0.23348 -0.08939 -0.03996 0.03791  70  ILE A CG2 
498  C CD1 . ILE A 76  ? 0.33510 0.41956 0.26424 -0.09588 -0.04250 0.04507  70  ILE A CD1 
499  N N   . LYS A 77  ? 0.25943 0.38876 0.21860 -0.08421 -0.03555 0.02964  71  LYS A N   
500  C CA  . LYS A 77  ? 0.21958 0.35503 0.17904 -0.07837 -0.03190 0.02756  71  LYS A CA  
501  C C   . LYS A 77  ? 0.24656 0.38021 0.20794 -0.07183 -0.03342 0.02603  71  LYS A C   
502  O O   . LYS A 77  ? 0.32219 0.44878 0.27764 -0.06769 -0.03176 0.02532  71  LYS A O   
503  C CB  . LYS A 77  ? 0.22552 0.37760 0.19054 -0.07862 -0.02827 0.02726  71  LYS A CB  
504  C CG  . LYS A 77  ? 0.44847 0.60405 0.40981 -0.08417 -0.02464 0.02923  71  LYS A CG  
505  C CD  . LYS A 77  ? 0.41016 0.58536 0.37554 -0.07987 -0.01877 0.02890  71  LYS A CD  
506  C CE  . LYS A 77  ? 0.50532 0.67423 0.45915 -0.07434 -0.01329 0.02795  71  LYS A CE  
507  N NZ  . LYS A 77  ? 0.49339 0.68171 0.44902 -0.07437 -0.00675 0.02959  71  LYS A NZ  
508  N N   . ILE A 78  ? 0.27077 0.40829 0.23782 -0.07166 -0.03655 0.02554  72  ILE A N   
509  C CA  . ILE A 78  ? 0.24392 0.38078 0.21179 -0.06523 -0.03773 0.02465  72  ILE A CA  
510  C C   . ILE A 78  ? 0.32161 0.44776 0.28493 -0.06479 -0.03891 0.02605  72  ILE A C   
511  O O   . ILE A 78  ? 0.26931 0.39099 0.22875 -0.06150 -0.03748 0.02639  72  ILE A O   
512  C CB  . ILE A 78  ? 0.27899 0.42263 0.25174 -0.06583 -0.04117 0.02325  72  ILE A CB  
513  C CG1 . ILE A 78  ? 0.30825 0.46959 0.28738 -0.06682 -0.04043 0.02240  72  ILE A CG1 
514  C CG2 . ILE A 78  ? 0.27476 0.41586 0.24616 -0.05933 -0.04257 0.02290  72  ILE A CG2 
515  C CD1 . ILE A 78  ? 0.25032 0.41796 0.23248 -0.07337 -0.04487 0.02068  72  ILE A CD1 
516  N N   . LEU A 79  ? 0.27719 0.39958 0.24005 -0.06807 -0.04138 0.02750  73  LEU A N   
517  C CA  . LEU A 79  ? 0.30825 0.42808 0.26954 -0.06667 -0.04269 0.02966  73  LEU A CA  
518  C C   . LEU A 79  ? 0.29893 0.41658 0.25574 -0.07043 -0.04171 0.03111  73  LEU A C   
519  O O   . LEU A 79  ? 0.36675 0.48526 0.32247 -0.07112 -0.04212 0.03278  73  LEU A O   
520  C CB  . LEU A 79  ? 0.30117 0.41868 0.26192 -0.06595 -0.04522 0.03137  73  LEU A CB  
521  C CG  . LEU A 79  ? 0.26489 0.37977 0.22547 -0.06189 -0.04662 0.02932  73  LEU A CG  
522  C CD1 . LEU A 79  ? 0.31340 0.41927 0.26842 -0.05956 -0.04834 0.03074  73  LEU A CD1 
523  C CD2 . LEU A 79  ? 0.33490 0.45475 0.29704 -0.05647 -0.04605 0.02917  73  LEU A CD2 
524  N N   . LEU A 80  ? 0.29631 0.41146 0.24923 -0.07408 -0.04042 0.03049  74  LEU A N   
525  C CA  . LEU A 80  ? 0.43590 0.54613 0.38087 -0.07858 -0.03984 0.03062  74  LEU A CA  
526  C C   . LEU A 80  ? 0.39237 0.49396 0.33069 -0.07696 -0.03692 0.02845  74  LEU A C   
527  O O   . LEU A 80  ? 0.39328 0.48658 0.32224 -0.08232 -0.03705 0.02830  74  LEU A O   
528  C CB  . LEU A 80  ? 0.46842 0.57686 0.40805 -0.08192 -0.03868 0.03018  74  LEU A CB  
529  C CG  . LEU A 80  ? 0.37802 0.49012 0.31870 -0.08451 -0.04171 0.03365  74  LEU A CG  
530  C CD1 . LEU A 80  ? 0.46047 0.56989 0.39249 -0.08873 -0.04037 0.03372  74  LEU A CD1 
531  C CD2 . LEU A 80  ? 0.36026 0.47764 0.30258 -0.08517 -0.04580 0.03691  74  LEU A CD2 
532  N N   . ARG A 81  ? 0.33826 0.44050 0.27924 -0.07000 -0.03460 0.02701  75  ARG A N   
533  C CA  . ARG A 81  ? 0.36560 0.45670 0.29789 -0.06593 -0.03169 0.02607  75  ARG A CA  
534  C C   . ARG A 81  ? 0.37057 0.46201 0.30531 -0.06423 -0.03291 0.02821  75  ARG A C   
535  O O   . ARG A 81  ? 0.42188 0.50010 0.34631 -0.06524 -0.03129 0.02900  75  ARG A O   
536  C CB  . ARG A 81  ? 0.35877 0.45213 0.29052 -0.05671 -0.02787 0.02419  75  ARG A CB  
537  C CG  . ARG A 81  ? 0.45629 0.53278 0.37399 -0.04973 -0.02399 0.02355  75  ARG A CG  
538  C CD  . ARG A 81  ? 0.48235 0.56652 0.40129 -0.03669 -0.02031 0.02298  75  ARG A CD  
539  N NE  . ARG A 81  ? 0.42550 0.51840 0.34540 -0.03506 -0.01723 0.02126  75  ARG A NE  
540  C CZ  . ARG A 81  ? 0.41932 0.52356 0.34038 -0.02348 -0.01299 0.02111  75  ARG A CZ  
541  N NH1 . ARG A 81  ? 0.46673 0.57394 0.38734 -0.01135 -0.01186 0.02258  75  ARG A NH1 
542  N NH2 . ARG A 81  ? 0.46753 0.58265 0.39007 -0.02332 -0.00961 0.02015  75  ARG A NH2 
543  N N   . PHE A 82  ? 0.38666 0.49050 0.33218 -0.06217 -0.03542 0.02919  76  PHE A N   
544  C CA  . PHE A 82  ? 0.24064 0.34643 0.18759 -0.05962 -0.03601 0.03124  76  PHE A CA  
545  C C   . PHE A 82  ? 0.28797 0.39463 0.23366 -0.06679 -0.03699 0.03442  76  PHE A C   
546  O O   . PHE A 82  ? 0.23691 0.34979 0.18583 -0.07172 -0.03910 0.03527  76  PHE A O   
547  C CB  . PHE A 82  ? 0.21443 0.33121 0.17001 -0.05528 -0.03837 0.03044  76  PHE A CB  
548  C CG  . PHE A 82  ? 0.20175 0.32284 0.15924 -0.04926 -0.03826 0.02822  76  PHE A CG  
549  C CD1 . PHE A 82  ? 0.24243 0.36092 0.19616 -0.04554 -0.03553 0.02758  76  PHE A CD1 
550  C CD2 . PHE A 82  ? 0.24875 0.37750 0.21059 -0.04683 -0.04101 0.02676  76  PHE A CD2 
551  C CE1 . PHE A 82  ? 0.27452 0.40372 0.23198 -0.03905 -0.03575 0.02650  76  PHE A CE1 
552  C CE2 . PHE A 82  ? 0.27840 0.41581 0.24275 -0.04303 -0.04205 0.02496  76  PHE A CE2 
553  C CZ  . PHE A 82  ? 0.24251 0.38303 0.20626 -0.03891 -0.03952 0.02533  76  PHE A CZ  
554  N N   . ARG A 83  ? 0.26208 0.36458 0.20296 -0.06749 -0.03548 0.03698  77  ARG A N   
555  C CA  . ARG A 83  ? 0.31439 0.42511 0.25694 -0.07456 -0.03615 0.04114  77  ARG A CA  
556  C C   . ARG A 83  ? 0.24642 0.35950 0.18840 -0.07012 -0.03420 0.04397  77  ARG A C   
557  O O   . ARG A 83  ? 0.29216 0.39065 0.22373 -0.07000 -0.03168 0.04500  77  ARG A O   
558  C CB  A ARG A 83  ? 0.29899 0.39943 0.23138 -0.08692 -0.03597 0.04223  77  ARG A CB  
559  C CB  B ARG A 83  ? 0.29900 0.39929 0.23132 -0.08688 -0.03596 0.04219  77  ARG A CB  
560  C CG  A ARG A 83  ? 0.30809 0.42405 0.24452 -0.09681 -0.03724 0.04732  77  ARG A CG  
561  C CG  B ARG A 83  ? 0.42963 0.53646 0.36414 -0.09375 -0.03909 0.04126  77  ARG A CG  
562  C CD  A ARG A 83  ? 0.38200 0.48746 0.30652 -0.11277 -0.03813 0.04798  77  ARG A CD  
563  C CD  B ARG A 83  ? 0.49110 0.57733 0.41169 -0.09751 -0.03810 0.03719  77  ARG A CD  
564  N NE  A ARG A 83  ? 0.41764 0.49788 0.32550 -0.11703 -0.03472 0.04847  77  ARG A NE  
565  N NE  B ARG A 83  ? 0.43021 0.52253 0.35056 -0.10480 -0.04135 0.03649  77  ARG A NE  
566  C CZ  A ARG A 83  ? 0.45148 0.50201 0.34177 -0.11640 -0.03281 0.04443  77  ARG A CZ  
567  C CZ  B ARG A 83  ? 0.41157 0.51162 0.33840 -0.09967 -0.04256 0.03527  77  ARG A CZ  
568  N NH1 A ARG A 83  ? 0.47650 0.52157 0.36476 -0.11259 -0.03367 0.03944  77  ARG A NH1 
569  N NH1 B ARG A 83  ? 0.34889 0.45176 0.28336 -0.08917 -0.04105 0.03417  77  ARG A NH1 
570  N NH2 A ARG A 83  ? 0.62183 0.64644 0.49434 -0.11873 -0.02937 0.04586  77  ARG A NH2 
571  N NH2 B ARG A 83  ? 0.47701 0.58182 0.40122 -0.10642 -0.04563 0.03546  77  ARG A NH2 
572  N N   . HIS A 84  ? 0.20654 0.33585 0.15715 -0.06534 -0.03494 0.04541  78  HIS A N   
573  C CA  . HIS A 84  ? 0.20710 0.34033 0.15628 -0.06005 -0.03281 0.04789  78  HIS A CA  
574  C C   . HIS A 84  ? 0.19191 0.34508 0.14898 -0.05711 -0.03276 0.05050  78  HIS A C   
575  O O   . HIS A 84  ? 0.20586 0.36566 0.16868 -0.05330 -0.03492 0.04860  78  HIS A O   
576  C CB  . HIS A 84  ? 0.19709 0.32439 0.14418 -0.04981 -0.03333 0.04415  78  HIS A CB  
577  C CG  . HIS A 84  ? 0.23478 0.36249 0.17641 -0.04454 -0.03122 0.04683  78  HIS A CG  
578  N ND1 . HIS A 84  ? 0.21575 0.35549 0.15977 -0.03880 -0.03092 0.04734  78  HIS A ND1 
579  C CD2 . HIS A 84  ? 0.23054 0.34648 0.16204 -0.04307 -0.02898 0.04945  78  HIS A CD2 
580  C CE1 . HIS A 84  ? 0.23377 0.37121 0.17031 -0.03500 -0.02875 0.05013  78  HIS A CE1 
581  N NE2 . HIS A 84  ? 0.21902 0.34181 0.14796 -0.03748 -0.02768 0.05188  78  HIS A NE2 
582  N N   . GLU A 85  ? 0.20827 0.37005 0.16391 -0.05773 -0.02967 0.05532  79  GLU A N   
583  C CA  . GLU A 85  ? 0.19323 0.37766 0.15593 -0.05343 -0.02825 0.05879  79  GLU A CA  
584  C C   . GLU A 85  ? 0.23668 0.42158 0.19972 -0.03922 -0.02909 0.05431  79  GLU A C   
585  O O   . GLU A 85  ? 0.18771 0.38608 0.15535 -0.03280 -0.02888 0.05534  79  GLU A O   
586  C CB  . GLU A 85  ? 0.20134 0.39523 0.16114 -0.05668 -0.02375 0.06509  79  GLU A CB  
587  C CG  . GLU A 85  ? 0.33613 0.53218 0.29449 -0.07384 -0.02280 0.07070  79  GLU A CG  
588  C CD  . GLU A 85  ? 0.31970 0.52377 0.27367 -0.07887 -0.01780 0.07782  79  GLU A CD  
589  O OE1 . GLU A 85  ? 0.27030 0.47443 0.22049 -0.06772 -0.01501 0.07790  79  GLU A OE1 
590  O OE2 . GLU A 85  ? 0.32123 0.53141 0.27422 -0.09521 -0.01678 0.08348  79  GLU A OE2 
591  N N   . ASN A 86  ? 0.21230 0.38241 0.16889 -0.03395 -0.03018 0.04947  80  ASN A N   
592  C CA  . ASN A 86  ? 0.19335 0.36014 0.14632 -0.02324 -0.03155 0.04440  80  ASN A CA  
593  C C   . ASN A 86  ? 0.19343 0.34776 0.14664 -0.02414 -0.03583 0.03861  80  ASN A C   
594  O O   . ASN A 86  ? 0.19806 0.34407 0.14557 -0.01946 -0.03806 0.03336  80  ASN A O   
595  C CB  . ASN A 86  ? 0.20000 0.36280 0.14467 -0.01810 -0.03062 0.04318  80  ASN A CB  
596  C CG  . ASN A 86  ? 0.25098 0.42551 0.19380 -0.01796 -0.02559 0.04985  80  ASN A CG  
597  O OD1 . ASN A 86  ? 0.20945 0.37921 0.14814 -0.02265 -0.02407 0.05338  80  ASN A OD1 
598  N ND2 . ASN A 86  ? 0.20692 0.39673 0.15161 -0.01204 -0.02244 0.05227  80  ASN A ND2 
599  N N   . ILE A 87  ? 0.18545 0.33855 0.14387 -0.03145 -0.03707 0.03959  81  ILE A N   
600  C CA  . ILE A 87  ? 0.18400 0.32765 0.14290 -0.03349 -0.04022 0.03561  81  ILE A CA  
601  C C   . ILE A 87  ? 0.19708 0.34647 0.16015 -0.03551 -0.04059 0.03877  81  ILE A C   
602  O O   . ILE A 87  ? 0.18941 0.34682 0.15639 -0.04215 -0.03985 0.04269  81  ILE A O   
603  C CB  . ILE A 87  ? 0.18111 0.31800 0.14051 -0.03957 -0.04106 0.03380  81  ILE A CB  
604  C CG1 . ILE A 87  ? 0.18394 0.31890 0.13956 -0.03567 -0.04132 0.03158  81  ILE A CG1 
605  C CG2 . ILE A 87  ? 0.18623 0.31726 0.14699 -0.04304 -0.04339 0.03087  81  ILE A CG2 
606  C CD1 . ILE A 87  ? 0.22419 0.35560 0.17985 -0.03798 -0.04114 0.03108  81  ILE A CD1 
607  N N   . ILE A 88  ? 0.20624 0.35033 0.16645 -0.03015 -0.04201 0.03732  82  ILE A N   
608  C CA  . ILE A 88  ? 0.20767 0.35840 0.17069 -0.02951 -0.04268 0.04131  82  ILE A CA  
609  C C   . ILE A 88  ? 0.21843 0.36374 0.18317 -0.03936 -0.04467 0.04089  82  ILE A C   
610  O O   . ILE A 88  ? 0.31256 0.44463 0.27396 -0.04229 -0.04581 0.03700  82  ILE A O   
611  C CB  . ILE A 88  ? 0.21397 0.35613 0.16943 -0.01833 -0.04300 0.04066  82  ILE A CB  
612  C CG1 . ILE A 88  ? 0.34572 0.49925 0.30422 -0.01454 -0.04356 0.04655  82  ILE A CG1 
613  C CG2 . ILE A 88  ? 0.30000 0.41871 0.24660 -0.02087 -0.04525 0.03520  82  ILE A CG2 
614  C CD1 . ILE A 88  ? 0.32622 0.47939 0.27762 0.00202  -0.04190 0.04852  82  ILE A CD1 
615  N N   . GLY A 89  ? 0.19576 0.35287 0.16506 -0.04550 -0.04502 0.04489  83  GLY A N   
616  C CA  . GLY A 89  ? 0.29568 0.44744 0.26405 -0.05459 -0.04647 0.04419  83  GLY A CA  
617  C C   . GLY A 89  ? 0.33315 0.48504 0.29992 -0.05300 -0.04878 0.04651  83  GLY A C   
618  O O   . GLY A 89  ? 0.34160 0.49620 0.30731 -0.04371 -0.04925 0.04901  83  GLY A O   
619  N N   . ILE A 90  ? 0.29142 0.43876 0.25578 -0.06095 -0.04985 0.04590  84  ILE A N   
620  C CA  . ILE A 90  ? 0.25911 0.40628 0.22018 -0.06071 -0.05214 0.04882  84  ILE A CA  
621  C C   . ILE A 90  ? 0.24446 0.40930 0.20796 -0.06620 -0.05466 0.05295  84  ILE A C   
622  O O   . ILE A 90  ? 0.31847 0.48297 0.28004 -0.07655 -0.05478 0.05110  84  ILE A O   
623  C CB  . ILE A 90  ? 0.30586 0.43859 0.26136 -0.06629 -0.05148 0.04584  84  ILE A CB  
624  C CG1 . ILE A 90  ? 0.24136 0.36071 0.19499 -0.06317 -0.05000 0.04255  84  ILE A CG1 
625  C CG2 . ILE A 90  ? 0.30322 0.43621 0.25350 -0.06724 -0.05373 0.04977  84  ILE A CG2 
626  C CD1 . ILE A 90  ? 0.28963 0.40128 0.24068 -0.06993 -0.04845 0.03990  84  ILE A CD1 
627  N N   . ASN A 91  ? 0.25334 0.43357 0.21960 -0.05906 -0.05682 0.05859  85  ASN A N   
628  C CA  . ASN A 91  ? 0.23989 0.44322 0.20974 -0.06502 -0.06038 0.06335  85  ASN A CA  
629  C C   . ASN A 91  ? 0.31647 0.51622 0.27917 -0.07009 -0.06371 0.06438  85  ASN A C   
630  O O   . ASN A 91  ? 0.25924 0.46759 0.22182 -0.08043 -0.06533 0.06444  85  ASN A O   
631  C CB  . ASN A 91  ? 0.19969 0.42748 0.17663 -0.05321 -0.06128 0.07007  85  ASN A CB  
632  C CG  . ASN A 91  ? 0.29025 0.52492 0.27333 -0.04789 -0.05746 0.06964  85  ASN A CG  
633  O OD1 . ASN A 91  ? 0.23784 0.46057 0.22021 -0.05465 -0.05492 0.06492  85  ASN A OD1 
634  N ND2 . ASN A 91  ? 0.26318 0.51770 0.25111 -0.03414 -0.05667 0.07503  85  ASN A ND2 
635  N N   . ASP A 92  ? 0.28266 0.46541 0.23848 -0.06328 -0.06302 0.06444  86  ASP A N   
636  C CA  . ASP A 92  ? 0.33306 0.51349 0.28078 -0.06538 -0.06585 0.06726  86  ASP A CA  
637  C C   . ASP A 92  ? 0.35328 0.50840 0.29243 -0.06054 -0.06315 0.06623  86  ASP A C   
638  O O   . ASP A 92  ? 0.28496 0.42846 0.22406 -0.05257 -0.06076 0.06525  86  ASP A O   
639  C CB  . ASP A 92  ? 0.25633 0.46063 0.20635 -0.05771 -0.07042 0.07543  86  ASP A CB  
640  C CG  . ASP A 92  ? 0.37016 0.57261 0.31222 -0.05998 -0.07282 0.07798  86  ASP A CG  
641  O OD1 . ASP A 92  ? 0.29568 0.48390 0.22982 -0.07039 -0.07211 0.07384  86  ASP A OD1 
642  O OD2 . ASP A 92  ? 0.28259 0.49890 0.22572 -0.05004 -0.07511 0.08436  86  ASP A OD2 
643  N N   . ILE A 93  ? 0.25471 0.40101 0.18512 -0.06669 -0.06346 0.06637  87  ILE A N   
644  C CA  . ILE A 93  ? 0.29101 0.41533 0.21211 -0.06500 -0.06096 0.06696  87  ILE A CA  
645  C C   . ILE A 93  ? 0.28234 0.40682 0.19283 -0.06330 -0.06376 0.07361  87  ILE A C   
646  O O   . ILE A 93  ? 0.29505 0.43077 0.20314 -0.07032 -0.06611 0.07390  87  ILE A O   
647  C CB  . ILE A 93  ? 0.32130 0.43472 0.24179 -0.07481 -0.05674 0.06069  87  ILE A CB  
648  C CG1 . ILE A 93  ? 0.26062 0.37444 0.19051 -0.07475 -0.05446 0.05500  87  ILE A CG1 
649  C CG2 . ILE A 93  ? 0.34870 0.44369 0.26009 -0.07607 -0.05426 0.06246  87  ILE A CG2 
650  C CD1 . ILE A 93  ? 0.29774 0.40569 0.22840 -0.08157 -0.05040 0.04961  87  ILE A CD1 
651  N N   . ILE A 94  ? 0.31281 0.42221 0.21421 -0.05393 -0.06359 0.07890  88  ILE A N   
652  C CA  . ILE A 94  ? 0.33607 0.44289 0.22494 -0.04921 -0.06621 0.08693  88  ILE A CA  
653  C C   . ILE A 94  ? 0.30534 0.38489 0.18058 -0.05477 -0.06245 0.08779  88  ILE A C   
654  O O   . ILE A 94  ? 0.36835 0.42611 0.23961 -0.05397 -0.05933 0.08612  88  ILE A O   
655  C CB  . ILE A 94  ? 0.31046 0.42031 0.19621 -0.03127 -0.06880 0.09427  88  ILE A CB  
656  C CG1 . ILE A 94  ? 0.29702 0.43989 0.19864 -0.02699 -0.07184 0.09412  88  ILE A CG1 
657  C CG2 . ILE A 94  ? 0.36114 0.46797 0.23217 -0.02452 -0.07177 0.10372  88  ILE A CG2 
658  C CD1 . ILE A 94  ? 0.36017 0.50580 0.26242 -0.00782 -0.07151 0.09849  88  ILE A CD1 
659  N N   . ARG A 95  ? 0.31148 0.39269 0.17833 -0.06154 -0.06280 0.09051  89  ARG A N   
660  C CA  . ARG A 95  ? 0.32956 0.38828 0.18222 -0.06750 -0.05895 0.09342  89  ARG A CA  
661  C C   . ARG A 95  ? 0.34044 0.40620 0.18176 -0.06965 -0.06098 0.09903  89  ARG A C   
662  O O   . ARG A 95  ? 0.33552 0.42383 0.18093 -0.06925 -0.06549 0.09863  89  ARG A O   
663  C CB  . ARG A 95  ? 0.36586 0.42012 0.22492 -0.08026 -0.05338 0.08593  89  ARG A CB  
664  C CG  . ARG A 95  ? 0.40203 0.47664 0.27184 -0.08708 -0.05261 0.07877  89  ARG A CG  
665  C CD  . ARG A 95  ? 0.37360 0.44940 0.23402 -0.09542 -0.04940 0.07942  89  ARG A CD  
666  N NE  . ARG A 95  ? 0.33811 0.42581 0.20489 -0.10109 -0.04669 0.07154  89  ARG A NE  
667  C CZ  . ARG A 95  ? 0.36933 0.46444 0.22811 -0.10438 -0.04703 0.07000  89  ARG A CZ  
668  N NH1 . ARG A 95  ? 0.31683 0.41322 0.16305 -0.10347 -0.05081 0.07586  89  ARG A NH1 
669  N NH2 . ARG A 95  ? 0.38345 0.48328 0.24461 -0.10791 -0.04360 0.06236  89  ARG A NH2 
670  N N   . ALA A 96  ? 0.36600 0.41178 0.19140 -0.07328 -0.05778 0.10449  90  ALA A N   
671  C CA  . ALA A 96  ? 0.39955 0.44883 0.21057 -0.07455 -0.05925 0.11097  90  ALA A CA  
672  C C   . ALA A 96  ? 0.36247 0.43053 0.17799 -0.08540 -0.05805 0.10415  90  ALA A C   
673  O O   . ALA A 96  ? 0.34532 0.41742 0.17237 -0.09252 -0.05410 0.09551  90  ALA A O   
674  C CB  . ALA A 96  ? 0.40492 0.42644 0.19706 -0.07827 -0.05463 0.11830  90  ALA A CB  
675  N N   . PRO A 97  ? 0.37185 0.44992 0.17779 -0.08520 -0.06108 0.10700  91  PRO A N   
676  C CA  . PRO A 97  ? 0.37487 0.46538 0.18356 -0.09365 -0.05921 0.09816  91  PRO A CA  
677  C C   . PRO A 97  ? 0.36876 0.45044 0.16939 -0.10314 -0.05088 0.09638  91  PRO A C   
678  O O   . PRO A 97  ? 0.41571 0.50496 0.21766 -0.10867 -0.04791 0.08825  91  PRO A O   
679  C CB  . PRO A 97  ? 0.37618 0.47636 0.17817 -0.08894 -0.06429 0.10060  91  PRO A CB  
680  C CG  . PRO A 97  ? 0.39675 0.48475 0.18744 -0.07904 -0.06578 0.11229  91  PRO A CG  
681  C CD  . PRO A 97  ? 0.39035 0.46926 0.18741 -0.07384 -0.06599 0.11520  91  PRO A CD  
682  N N   . THR A 98  ? 0.38392 0.44945 0.17521 -0.10514 -0.04647 0.10382  92  THR A N   
683  C CA  . THR A 98  ? 0.39065 0.45258 0.17643 -0.11459 -0.03764 0.10315  92  THR A CA  
684  C C   . THR A 98  ? 0.43736 0.48764 0.23004 -0.11997 -0.03269 0.10430  92  THR A C   
685  O O   . THR A 98  ? 0.39375 0.42952 0.18790 -0.11556 -0.03587 0.10769  92  THR A O   
686  C CB  . THR A 98  ? 0.41599 0.47032 0.18504 -0.11416 -0.03553 0.11003  92  THR A CB  
687  O OG1 . THR A 98  ? 0.43561 0.47025 0.19485 -0.10956 -0.03775 0.12050  92  THR A OG1 
688  C CG2 . THR A 98  ? 0.44003 0.50604 0.20430 -0.10869 -0.04076 0.10708  92  THR A CG2 
689  N N   . ILE A 99  ? 0.44624 0.50371 0.24340 -0.12887 -0.02465 0.10071  93  ILE A N   
690  C CA  . ILE A 99  ? 0.45423 0.50509 0.25950 -0.13664 -0.02011 0.10123  93  ILE A CA  
691  C C   . ILE A 99  ? 0.53570 0.56290 0.32386 -0.14186 -0.01920 0.11227  93  ILE A C   
692  O O   . ILE A 99  ? 0.47705 0.48658 0.26598 -0.14527 -0.01999 0.11395  93  ILE A O   
693  C CB  A ILE A 99  ? 0.47385 0.54467 0.28862 -0.14412 -0.01162 0.09609  93  ILE A CB  
694  C CB  B ILE A 99  ? 0.47488 0.54540 0.28904 -0.14434 -0.01150 0.09641  93  ILE A CB  
695  C CG1 A ILE A 99  ? 0.43056 0.50460 0.26206 -0.14982 -0.00997 0.09255  93  ILE A CG1 
696  C CG1 B ILE A 99  ? 0.51567 0.60286 0.34384 -0.13753 -0.01215 0.08561  93  ILE A CG1 
697  C CG2 A ILE A 99  ? 0.44693 0.52033 0.24774 -0.15256 -0.00414 0.10312  93  ILE A CG2 
698  C CG2 B ILE A 99  ? 0.41136 0.47983 0.23345 -0.15537 -0.00746 0.09824  93  ILE A CG2 
699  C CD1 A ILE A 99  ? 0.46752 0.56759 0.31272 -0.15196 -0.00316 0.08633  93  ILE A CD1 
700  C CD1 B ILE A 99  ? 0.47651 0.58360 0.31448 -0.14094 -0.00363 0.08090  93  ILE A CD1 
701  N N   . GLU A 100 ? 0.45274 0.47597 0.22407 -0.14154 -0.01774 0.11902  94  GLU A N   
702  C CA  . GLU A 100 ? 0.56705 0.56407 0.32142 -0.14405 -0.01658 0.12897  94  GLU A CA  
703  C C   . GLU A 100 ? 0.49208 0.46406 0.23741 -0.13521 -0.02374 0.13412  94  GLU A C   
704  O O   . GLU A 100 ? 0.52076 0.46464 0.25530 -0.14016 -0.02250 0.13943  94  GLU A O   
705  C CB  . GLU A 100 ? 0.48544 0.48323 0.22557 -0.13935 -0.01536 0.13372  94  GLU A CB  
706  C CG  . GLU A 100 ? 0.57321 0.58567 0.31364 -0.14818 -0.00635 0.13249  94  GLU A CG  
707  C CD  . GLU A 100 ? 0.50611 0.54710 0.25949 -0.14690 -0.00410 0.12212  94  GLU A CD  
708  O OE1 . GLU A 100 ? 0.54521 0.59992 0.29806 -0.15117 0.00372  0.12064  94  GLU A OE1 
709  O OE2 . GLU A 100 ? 0.44241 0.49088 0.20481 -0.14083 -0.00977 0.11566  94  GLU A OE2 
710  N N   . GLN A 101 ? 0.53525 0.51693 0.28423 -0.12177 -0.03117 0.13224  95  GLN A N   
711  C CA  . GLN A 101 ? 0.47831 0.44198 0.21994 -0.10751 -0.03775 0.13714  95  GLN A CA  
712  C C   . GLN A 101 ? 0.46127 0.42259 0.21914 -0.10313 -0.03998 0.12948  95  GLN A C   
713  O O   . GLN A 101 ? 0.55680 0.50037 0.30743 -0.09049 -0.04396 0.13323  95  GLN A O   
714  C CB  . GLN A 101 ? 0.47334 0.45551 0.21392 -0.09389 -0.04462 0.13891  95  GLN A CB  
715  C CG  . GLN A 101 ? 0.49660 0.47566 0.22162 -0.09121 -0.04318 0.14532  95  GLN A CG  
716  C CD  . GLN A 101 ? 0.48876 0.49173 0.21718 -0.07999 -0.05004 0.14382  95  GLN A CD  
717  O OE1 . GLN A 101 ? 0.50980 0.50730 0.22572 -0.06713 -0.05420 0.15196  95  GLN A OE1 
718  N NE2 . GLN A 101 ? 0.46140 0.49011 0.20572 -0.08490 -0.05128 0.13330  95  GLN A NE2 
719  N N   . MET A 102 ? 0.44312 0.42183 0.22117 -0.11140 -0.03733 0.11927  96  MET A N   
720  C CA  . MET A 102 ? 0.48478 0.46450 0.27810 -0.10643 -0.03987 0.11183  96  MET A CA  
721  C C   . MET A 102 ? 0.55171 0.50402 0.33821 -0.11480 -0.03697 0.11235  96  MET A C   
722  O O   . MET A 102 ? 0.50693 0.46276 0.29783 -0.13038 -0.03199 0.10999  96  MET A O   
723  C CB  . MET A 102 ? 0.41028 0.41938 0.22594 -0.10966 -0.03908 0.10129  96  MET A CB  
724  C CG  . MET A 102 ? 0.41315 0.42233 0.24377 -0.10973 -0.03942 0.09367  96  MET A CG  
725  S SD  . MET A 102 ? 0.38707 0.42605 0.24005 -0.11368 -0.03718 0.08275  96  MET A SD  
726  C CE  . MET A 102 ? 0.34335 0.38797 0.19585 -0.12888 -0.02924 0.08309  96  MET A CE  
727  N N   . LYS A 103 ? 0.48729 0.41248 0.26123 -0.10435 -0.04012 0.11578  97  LYS A N   
728  C CA  . LYS A 103 ? 0.61819 0.51037 0.38070 -0.11085 -0.03868 0.11527  97  LYS A CA  
729  C C   . LYS A 103 ? 0.61132 0.50543 0.38637 -0.10405 -0.04137 0.10637  97  LYS A C   
730  O O   . LYS A 103 ? 0.61226 0.49160 0.38590 -0.11500 -0.04011 0.10169  97  LYS A O   
731  C CB  . LYS A 103 ? 0.66996 0.52075 0.40178 -0.10225 -0.03945 0.12570  97  LYS A CB  
732  C CG  . LYS A 103 ? 0.77364 0.58461 0.48318 -0.11883 -0.03571 0.12933  97  LYS A CG  
733  C CD  . LYS A 103 ? 0.79467 0.57177 0.47275 -0.11362 -0.03480 0.14255  97  LYS A CD  
734  C CE  . LYS A 103 ? 0.76649 0.52850 0.43212 -0.08555 -0.03934 0.14702  97  LYS A CE  
735  N NZ  . LYS A 103 ? 0.72234 0.43848 0.36721 -0.07892 -0.03968 0.14545  97  LYS A NZ  
736  N N   . ASP A 104 ? 0.52578 0.43941 0.31248 -0.08741 -0.04516 0.10422  98  ASP A N   
737  C CA  . ASP A 104 ? 0.63393 0.55127 0.43146 -0.07874 -0.04731 0.09692  98  ASP A CA  
738  C C   . ASP A 104 ? 0.51257 0.47056 0.33518 -0.07556 -0.04899 0.09141  98  ASP A C   
739  O O   . ASP A 104 ? 0.48281 0.46174 0.31026 -0.07559 -0.04975 0.09399  98  ASP A O   
740  C CB  . ASP A 104 ? 0.62896 0.52332 0.41020 -0.05836 -0.04977 0.10162  98  ASP A CB  
741  C CG  . ASP A 104 ? 0.68934 0.53565 0.43950 -0.05965 -0.04801 0.10800  98  ASP A CG  
742  O OD1 . ASP A 104 ? 0.71085 0.53489 0.45344 -0.07626 -0.04575 0.10421  98  ASP A OD1 
743  O OD2 . ASP A 104 ? 0.70587 0.53656 0.43800 -0.04451 -0.04910 0.11720  98  ASP A OD2 
744  N N   . VAL A 105 ? 0.39378 0.44082 0.24580 -0.18123 -0.10087 0.13743  99  VAL A N   
745  C CA  . VAL A 105 ? 0.36399 0.42020 0.22057 -0.17200 -0.09251 0.12867  99  VAL A CA  
746  C C   . VAL A 105 ? 0.39555 0.43993 0.26926 -0.15538 -0.09726 0.13094  99  VAL A C   
747  O O   . VAL A 105 ? 0.39794 0.43301 0.28069 -0.14794 -0.09856 0.13270  99  VAL A O   
748  C CB  . VAL A 105 ? 0.50656 0.57819 0.36010 -0.17101 -0.07693 0.11604  99  VAL A CB  
749  C CG1 . VAL A 105 ? 0.48599 0.56474 0.34390 -0.16154 -0.06961 0.10711  99  VAL A CG1 
750  C CG2 . VAL A 105 ? 0.52620 0.61195 0.36478 -0.18709 -0.07192 0.11230  99  VAL A CG2 
751  N N   . TYR A 106 ? 0.36186 0.40744 0.24036 -0.14988 -0.09986 0.13039  100 TYR A N   
752  C CA  . TYR A 106 ? 0.40879 0.44665 0.30469 -0.13445 -0.10418 0.13137  100 TYR A CA  
753  C C   . TYR A 106 ? 0.37292 0.42162 0.27211 -0.12685 -0.09412 0.12168  100 TYR A C   
754  O O   . TYR A 106 ? 0.32727 0.38601 0.21778 -0.13238 -0.09028 0.11703  100 TYR A O   
755  C CB  . TYR A 106 ? 0.34213 0.37213 0.24392 -0.13350 -0.11777 0.13933  100 TYR A CB  
756  C CG  . TYR A 106 ? 0.43277 0.44987 0.33147 -0.14084 -0.12955 0.14934  100 TYR A CG  
757  C CD1 . TYR A 106 ? 0.44860 0.46845 0.33032 -0.15750 -0.13201 0.15354  100 TYR A CD1 
758  C CD2 . TYR A 106 ? 0.37479 0.37689 0.28747 -0.13150 -0.13842 0.15403  100 TYR A CD2 
759  C CE1 . TYR A 106 ? 0.53625 0.54352 0.41422 -0.16542 -0.14383 0.16330  100 TYR A CE1 
760  C CE2 . TYR A 106 ? 0.45410 0.44276 0.36357 -0.13840 -0.15022 0.16294  100 TYR A CE2 
761  C CZ  . TYR A 106 ? 0.56305 0.55401 0.45476 -0.15575 -0.15323 0.16810  100 TYR A CZ  
762  O OH  . TYR A 106 ? 0.56362 0.54051 0.45131 -0.16377 -0.16599 0.17760  100 TYR A OH  
763  N N   . ILE A 107 ? 0.28768 0.33370 0.19903 -0.11468 -0.09031 0.11854  101 ILE A N   
764  C CA  . ILE A 107 ? 0.35092 0.40542 0.26629 -0.10709 -0.08176 0.11006  101 ILE A CA  
765  C C   . ILE A 107 ? 0.31264 0.36373 0.24526 -0.09579 -0.08915 0.11241  101 ILE A C   
766  O O   . ILE A 107 ? 0.31423 0.35637 0.26101 -0.08698 -0.09451 0.11616  101 ILE A O   
767  C CB  . ILE A 107 ? 0.29030 0.34604 0.20687 -0.10232 -0.07152 0.10445  101 ILE A CB  
768  C CG1 . ILE A 107 ? 0.44122 0.50228 0.34391 -0.11321 -0.06479 0.10157  101 ILE A CG1 
769  C CG2 . ILE A 107 ? 0.27633 0.34002 0.19543 -0.09564 -0.06314 0.09575  101 ILE A CG2 
770  C CD1 . ILE A 107 ? 0.37033 0.44423 0.25944 -0.12268 -0.05893 0.09458  101 ILE A CD1 
771  N N   . VAL A 108 ? 0.35545 0.41463 0.28795 -0.09604 -0.08929 0.10907  102 VAL A N   
772  C CA  . VAL A 108 ? 0.28018 0.34060 0.23026 -0.08648 -0.09568 0.10978  102 VAL A CA  
773  C C   . VAL A 108 ? 0.26400 0.33037 0.22291 -0.07816 -0.08564 0.10010  102 VAL A C   
774  O O   . VAL A 108 ? 0.26743 0.33932 0.21668 -0.08193 -0.07578 0.09155  102 VAL A O   
775  C CB  . VAL A 108 ? 0.32317 0.38858 0.26984 -0.09241 -0.10174 0.11119  102 VAL A CB  
776  C CG1 . VAL A 108 ? 0.36923 0.43812 0.33670 -0.08254 -0.10830 0.11130  102 VAL A CG1 
777  C CG2 . VAL A 108 ? 0.36075 0.41908 0.29813 -0.10153 -0.10944 0.11916  102 VAL A CG2 
778  N N   . GLN A 109 ? 0.26243 0.32615 0.24188 -0.06607 -0.08595 0.09858  103 GLN A N   
779  C CA  . GLN A 109 ? 0.27318 0.34016 0.26340 -0.05775 -0.07453 0.08801  103 GLN A CA  
780  C C   . GLN A 109 ? 0.33128 0.40276 0.34307 -0.04872 -0.07892 0.08715  103 GLN A C   
781  O O   . GLN A 109 ? 0.30114 0.37247 0.32198 -0.04677 -0.09078 0.09404  103 GLN A O   
782  C CB  . GLN A 109 ? 0.26840 0.32891 0.25935 -0.05309 -0.06650 0.08489  103 GLN A CB  
783  C CG  . GLN A 109 ? 0.26763 0.32657 0.23926 -0.06223 -0.06216 0.08541  103 GLN A CG  
784  C CD  . GLN A 109 ? 0.30285 0.35680 0.27627 -0.05803 -0.05490 0.08243  103 GLN A CD  
785  O OE1 . GLN A 109 ? 0.23080 0.27706 0.20839 -0.05602 -0.06014 0.08854  103 GLN A OE1 
786  N NE2 . GLN A 109 ? 0.25274 0.31032 0.22311 -0.05671 -0.04366 0.07294  103 GLN A NE2 
787  N N   . ASP A 110 ? 0.33239 0.40856 0.35256 -0.04356 -0.06963 0.07841  104 ASP A N   
788  C CA  . ASP A 110 ? 0.33156 0.41534 0.37228 -0.03598 -0.07156 0.07599  104 ASP A CA  
789  C C   . ASP A 110 ? 0.41312 0.49302 0.46935 -0.02666 -0.07677 0.07868  104 ASP A C   
790  O O   . ASP A 110 ? 0.28836 0.35878 0.34079 -0.02437 -0.07395 0.07923  104 ASP A O   
791  C CB  . ASP A 110 ? 0.38373 0.47134 0.42783 -0.03357 -0.05992 0.06681  104 ASP A CB  
792  C CG  . ASP A 110 ? 0.43952 0.53055 0.47223 -0.04164 -0.05679 0.06336  104 ASP A CG  
793  O OD1 . ASP A 110 ? 0.36726 0.46167 0.39377 -0.04824 -0.06402 0.06728  104 ASP A OD1 
794  O OD2 . ASP A 110 ? 0.30403 0.39333 0.33355 -0.04158 -0.04784 0.05674  104 ASP A OD2 
795  N N   . LEU A 111 ? 0.21910 0.30677 0.29372 -0.02112 -0.08479 0.07966  105 LEU A N   
796  C CA  . LEU A 111 ? 0.31989 0.40469 0.41230 -0.01067 -0.09030 0.08009  105 LEU A CA  
797  C C   . LEU A 111 ? 0.34011 0.43254 0.44683 -0.00279 -0.07977 0.07004  105 LEU A C   
798  O O   . LEU A 111 ? 0.29198 0.39873 0.40870 -0.00233 -0.07635 0.06481  105 LEU A O   
799  C CB  . LEU A 111 ? 0.33314 0.42335 0.44048 -0.00732 -0.10520 0.08511  105 LEU A CB  
800  C CG  . LEU A 111 ? 0.33627 0.42313 0.46417 0.00521  -0.11093 0.08288  105 LEU A CG  
801  C CD1 . LEU A 111 ? 0.25660 0.32247 0.37300 0.00498  -0.11423 0.08806  105 LEU A CD1 
802  C CD2 . LEU A 111 ? 0.41544 0.50772 0.55668 0.00969  -0.12027 0.08213  105 LEU A CD2 
803  N N   . MET A 112 ? 0.26784 0.35127 0.37447 0.00215  -0.07472 0.06753  106 MET A N   
804  C CA  . MET A 112 ? 0.19553 0.28512 0.31362 0.00895  -0.06502 0.05831  106 MET A CA  
805  C C   . MET A 112 ? 0.34536 0.43652 0.48484 0.02016  -0.07148 0.05571  106 MET A C   
806  O O   . MET A 112 ? 0.41969 0.50304 0.56358 0.02296  -0.08388 0.06183  106 MET A O   
807  C CB  . MET A 112 ? 0.19122 0.27051 0.29484 0.00692  -0.05498 0.05617  106 MET A CB  
808  C CG  . MET A 112 ? 0.19586 0.27286 0.27974 -0.00276 -0.04958 0.05754  106 MET A CG  
809  S SD  . MET A 112 ? 0.23896 0.32825 0.32350 -0.00654 -0.04153 0.05122  106 MET A SD  
810  C CE  . MET A 112 ? 0.23531 0.32192 0.32054 -0.00228 -0.03005 0.04409  106 MET A CE  
811  N N   . GLU A 113 ? 0.22596 0.32715 0.37864 0.02638  -0.06343 0.04619  107 GLU A N   
812  C CA  . GLU A 113 ? 0.18938 0.29512 0.36481 0.03794  -0.06883 0.04098  107 GLU A CA  
813  C C   . GLU A 113 ? 0.26493 0.35351 0.43814 0.04331  -0.07005 0.04084  107 GLU A C   
814  O O   . GLU A 113 ? 0.26239 0.34360 0.44675 0.05078  -0.08054 0.04167  107 GLU A O   
815  C CB  . GLU A 113 ? 0.16054 0.28735 0.35198 0.04176  -0.05967 0.02966  107 GLU A CB  
816  C CG  . GLU A 113 ? 0.27246 0.40817 0.48987 0.05430  -0.06529 0.02207  107 GLU A CG  
817  C CD  . GLU A 113 ? 0.30343 0.46146 0.53428 0.05701  -0.05417 0.00949  107 GLU A CD  
818  O OE1 . GLU A 113 ? 0.23501 0.41279 0.47375 0.05341  -0.05260 0.00743  107 GLU A OE1 
819  O OE2 . GLU A 113 ? 0.30017 0.45629 0.53204 0.06153  -0.04681 0.00185  107 GLU A OE2 
820  N N   . THR A 114 ? 0.18830 0.26918 0.34636 0.03937  -0.05988 0.03947  108 THR A N   
821  C CA  . THR A 114 ? 0.17195 0.23774 0.32772 0.04358  -0.06020 0.03862  108 THR A CA  
822  C C   . THR A 114 ? 0.18068 0.23784 0.31488 0.03562  -0.05116 0.04088  108 THR A C   
823  O O   . THR A 114 ? 0.19371 0.25562 0.31593 0.02801  -0.04545 0.04258  108 THR A O   
824  C CB  . THR A 114 ? 0.20616 0.28009 0.38022 0.05371  -0.05592 0.02689  108 THR A CB  
825  O OG1 . THR A 114 ? 0.30560 0.36306 0.47819 0.05806  -0.05841 0.02619  108 THR A OG1 
826  C CG2 . THR A 114 ? 0.14851 0.23594 0.31883 0.05038  -0.04131 0.01932  108 THR A CG2 
827  N N   . ASP A 115 ? 0.21415 0.25839 0.34426 0.03768  -0.05059 0.04043  109 ASP A N   
828  C CA  . ASP A 115 ? 0.23626 0.27412 0.34953 0.03187  -0.04201 0.04081  109 ASP A CA  
829  C C   . ASP A 115 ? 0.23206 0.27058 0.35084 0.03748  -0.03468 0.03189  109 ASP A C   
830  O O   . ASP A 115 ? 0.23131 0.27246 0.36582 0.04578  -0.03722 0.02579  109 ASP A O   
831  C CB  . ASP A 115 ? 0.26118 0.28360 0.36100 0.02618  -0.04810 0.04970  109 ASP A CB  
832  C CG  . ASP A 115 ? 0.32904 0.33802 0.43623 0.03158  -0.05688 0.05097  109 ASP A CG  
833  O OD1 . ASP A 115 ? 0.25858 0.26326 0.36833 0.03565  -0.05248 0.04506  109 ASP A OD1 
834  O OD2 . ASP A 115 ? 0.37308 0.37464 0.48294 0.03141  -0.06906 0.05806  109 ASP A OD2 
835  N N   . LEU A 116 ? 0.21588 0.25267 0.32192 0.03304  -0.02583 0.03049  110 LEU A N   
836  C CA  . LEU A 116 ? 0.19279 0.23156 0.30177 0.03684  -0.01844 0.02225  110 LEU A CA  
837  C C   . LEU A 116 ? 0.21945 0.24601 0.33246 0.04177  -0.02295 0.02077  110 LEU A C   
838  O O   . LEU A 116 ? 0.24312 0.27264 0.36477 0.04759  -0.01978 0.01227  110 LEU A O   
839  C CB  . LEU A 116 ? 0.19905 0.23772 0.29330 0.03085  -0.00974 0.02202  110 LEU A CB  
840  C CG  . LEU A 116 ? 0.22676 0.26849 0.32114 0.03284  -0.00201 0.01440  110 LEU A CG  
841  C CD1 . LEU A 116 ? 0.19497 0.25161 0.30129 0.03592  0.00151  0.00735  110 LEU A CD1 
842  C CD2 . LEU A 116 ? 0.17962 0.21939 0.25941 0.02698  0.00410  0.01566  110 LEU A CD2 
843  N N   . TYR A 117 ? 0.24329 0.25623 0.34955 0.03873  -0.03044 0.02865  111 TYR A N   
844  C CA  . TYR A 117 ? 0.24865 0.24762 0.35881 0.04263  -0.03676 0.02821  111 TYR A CA  
845  C C   . TYR A 117 ? 0.24347 0.24365 0.37311 0.05272  -0.04358 0.02263  111 TYR A C   
846  O O   . TYR A 117 ? 0.25595 0.25464 0.39439 0.05951  -0.04209 0.01378  111 TYR A O   
847  C CB  . TYR A 117 ? 0.28041 0.26539 0.37938 0.03561  -0.04489 0.03916  111 TYR A CB  
848  C CG  . TYR A 117 ? 0.25164 0.21940 0.35318 0.03799  -0.05309 0.04023  111 TYR A CG  
849  C CD1 . TYR A 117 ? 0.40604 0.36257 0.51505 0.04087  -0.06663 0.04531  111 TYR A CD1 
850  C CD2 . TYR A 117 ? 0.36218 0.32372 0.45844 0.03702  -0.04843 0.03647  111 TYR A CD2 
851  C CE1 . TYR A 117 ? 0.35086 0.28915 0.46124 0.04248  -0.07509 0.04628  111 TYR A CE1 
852  C CE2 . TYR A 117 ? 0.39586 0.34033 0.49389 0.03843  -0.05643 0.03730  111 TYR A CE2 
853  C CZ  . TYR A 117 ? 0.42515 0.35704 0.53034 0.04125  -0.07003 0.04234  111 TYR A CZ  
854  O OH  . TYR A 117 ? 0.46212 0.37653 0.56620 0.04116  -0.07743 0.04227  111 TYR A OH  
855  N N   . LYS A 118 ? 0.20068 0.20432 0.33791 0.05408  -0.05147 0.02698  112 LYS A N   
856  C CA  . LYS A 118 ? 0.25471 0.26122 0.41310 0.06473  -0.05912 0.02119  112 LYS A CA  
857  C C   . LYS A 118 ? 0.24362 0.26937 0.41460 0.07085  -0.04899 0.00776  112 LYS A C   
858  O O   . LYS A 118 ? 0.25868 0.28496 0.43815 0.07771  -0.04876 -0.00181 112 LYS A O   
859  C CB  . LYS A 118 ? 0.23748 0.24652 0.39784 0.06292  -0.06803 0.02838  112 LYS A CB  
860  C CG  . LYS A 118 ? 0.29314 0.28366 0.43969 0.05565  -0.07866 0.04106  112 LYS A CG  
861  C CD  . LYS A 118 ? 0.36068 0.33252 0.50649 0.05824  -0.08523 0.03971  112 LYS A CD  
862  C CE  . LYS A 118 ? 0.40867 0.36730 0.54960 0.05413  -0.09856 0.04903  112 LYS A CE  
863  N NZ  . LYS A 118 ? 0.40810 0.35343 0.55694 0.06037  -0.10637 0.04442  112 LYS A NZ  
864  N N   . LEU A 119 ? 0.17509 0.21606 0.33984 0.06516  -0.03877 0.00689  113 LEU A N   
865  C CA  . LEU A 119 ? 0.24857 0.30891 0.42270 0.06820  -0.02869 -0.00468 113 LEU A CA  
866  C C   . LEU A 119 ? 0.24751 0.30423 0.42054 0.07131  -0.02242 -0.01361 113 LEU A C   
867  O O   . LEU A 119 ? 0.32397 0.39067 0.50907 0.07767  -0.01940 -0.02491 113 LEU A O   
868  C CB  . LEU A 119 ? 0.24549 0.31726 0.40765 0.05892  -0.01970 -0.00183 113 LEU A CB  
869  C CG  . LEU A 119 ? 0.36522 0.46026 0.53741 0.05872  -0.01258 -0.00938 113 LEU A CG  
870  C CD1 . LEU A 119 ? 0.21141 0.31794 0.40366 0.06473  -0.02047 -0.01092 113 LEU A CD1 
871  C CD2 . LEU A 119 ? 0.34289 0.44175 0.49898 0.04805  -0.00592 -0.00410 113 LEU A CD2 
872  N N   . LEU A 120 ? 0.20344 0.24622 0.35906 0.06556  -0.01994 -0.00879 114 LEU A N   
873  C CA  . LEU A 120 ? 0.21476 0.25423 0.36685 0.06694  -0.01385 -0.01656 114 LEU A CA  
874  C C   . LEU A 120 ? 0.20481 0.23389 0.36950 0.07618  -0.02111 -0.02307 114 LEU A C   
875  O O   . LEU A 120 ? 0.26385 0.29447 0.42921 0.07880  -0.01572 -0.03296 114 LEU A O   
876  C CB  . LEU A 120 ? 0.18258 0.21018 0.31441 0.05865  -0.01092 -0.00930 114 LEU A CB  
877  C CG  . LEU A 120 ? 0.27205 0.30910 0.39132 0.05077  -0.00216 -0.00664 114 LEU A CG  
878  C CD1 . LEU A 120 ? 0.31514 0.34086 0.41749 0.04429  -0.00079 -0.00035 114 LEU A CD1 
879  C CD2 . LEU A 120 ? 0.32296 0.37477 0.44496 0.05124  0.00711  -0.01644 114 LEU A CD2 
880  N N   . LYS A 121 ? 0.21762 0.23461 0.38627 0.07869  -0.03290 -0.01702 115 LYS A N   
881  C CA  . LYS A 121 ? 0.28578 0.29001 0.45870 0.08418  -0.03954 -0.02190 115 LYS A CA  
882  C C   . LYS A 121 ? 0.37392 0.39320 0.56054 0.09137  -0.03583 -0.03502 115 LYS A C   
883  O O   . LYS A 121 ? 0.33685 0.34956 0.52714 0.09602  -0.03718 -0.04319 115 LYS A O   
884  C CB  . LYS A 121 ? 0.29087 0.27845 0.46275 0.08337  -0.05334 -0.01150 115 LYS A CB  
885  C CG  . LYS A 121 ? 0.31789 0.29256 0.47523 0.07450  -0.05740 0.00245  115 LYS A CG  
886  C CD  . LYS A 121 ? 0.38811 0.34145 0.53624 0.07157  -0.06238 0.00527  115 LYS A CD  
887  C CE  . LYS A 121 ? 0.31418 0.26821 0.45557 0.06932  -0.05300 0.00122  115 LYS A CE  
888  N NZ  . LYS A 121 ? 0.23163 0.16565 0.36144 0.06332  -0.05819 0.00753  115 LYS A NZ  
889  N N   . THR A 122 ? 0.30017 0.34007 0.49467 0.09184  -0.03130 -0.03744 116 THR A N   
890  C CA  . THR A 122 ? 0.24066 0.29613 0.44926 0.09805  -0.02874 -0.04910 116 THR A CA  
891  C C   . THR A 122 ? 0.29192 0.37289 0.50241 0.09500  -0.01586 -0.05640 116 THR A C   
892  O O   . THR A 122 ? 0.37205 0.46683 0.59247 0.09893  -0.01189 -0.06756 116 THR A O   
893  C CB  . THR A 122 ? 0.34278 0.39882 0.56329 0.10251  -0.03917 -0.04561 116 THR A CB  
894  O OG1 . THR A 122 ? 0.31597 0.37993 0.53394 0.09730  -0.03960 -0.03621 116 THR A OG1 
895  C CG2 . THR A 122 ? 0.38472 0.41543 0.60373 0.10512  -0.05272 -0.03962 116 THR A CG2 
896  N N   . GLN A 123 ? 0.24442 0.33220 0.44569 0.08750  -0.00949 -0.05070 117 GLN A N   
897  C CA  . GLN A 123 ? 0.28210 0.39355 0.48402 0.08256  0.00145  -0.05567 117 GLN A CA  
898  C C   . GLN A 123 ? 0.24961 0.36240 0.43755 0.07597  0.01168  -0.05792 117 GLN A C   
899  O O   . GLN A 123 ? 0.20836 0.30940 0.38585 0.07217  0.01116  -0.05054 117 GLN A O   
900  C CB  . GLN A 123 ? 0.24217 0.36310 0.44609 0.07813  -0.00019 -0.04736 117 GLN A CB  
901  C CG  . GLN A 123 ? 0.17816 0.29741 0.39431 0.08367  -0.01129 -0.04368 117 GLN A CG  
902  C CD  . GLN A 123 ? 0.31331 0.44736 0.54452 0.08960  -0.01043 -0.05423 117 GLN A CD  
903  O OE1 . GLN A 123 ? 0.19803 0.35118 0.43120 0.08666  -0.00038 -0.06242 117 GLN A OE1 
904  N NE2 . GLN A 123 ? 0.28797 0.41311 0.52952 0.09736  -0.02128 -0.05406 117 GLN A NE2 
905  N N   . HIS A 124 ? 0.18338 0.31084 0.37100 0.07413  0.02064  -0.06803 118 HIS A N   
906  C CA  . HIS A 124 ? 0.25684 0.38936 0.42983 0.06576  0.03075  -0.06961 118 HIS A CA  
907  C C   . HIS A 124 ? 0.22763 0.37342 0.39550 0.05670  0.03577  -0.06369 118 HIS A C   
908  O O   . HIS A 124 ? 0.23573 0.39696 0.41232 0.05563  0.03638  -0.06479 118 HIS A O   
909  C CB  . HIS A 124 ? 0.29263 0.43632 0.46564 0.06550  0.03774  -0.08195 118 HIS A CB  
910  C CG  . HIS A 124 ? 0.37282 0.52688 0.53057 0.05465  0.04816  -0.08317 118 HIS A CG  
911  N ND1 . HIS A 124 ? 0.32509 0.49664 0.48007 0.04609  0.05397  -0.08157 118 HIS A ND1 
912  C CD2 . HIS A 124 ? 0.36229 0.51061 0.50553 0.05007  0.05293  -0.08511 118 HIS A CD2 
913  C CE1 . HIS A 124 ? 0.36135 0.53623 0.49980 0.03633  0.06137  -0.08180 118 HIS A CE1 
914  N NE2 . HIS A 124 ? 0.44800 0.60952 0.57922 0.03877  0.06094  -0.08402 118 HIS A NE2 
915  N N   . LEU A 125 ? 0.20870 0.34824 0.36265 0.04989  0.03894  -0.05756 119 LEU A N   
916  C CA  . LEU A 125 ? 0.17830 0.32325 0.32115 0.03940  0.04204  -0.04944 119 LEU A CA  
917  C C   . LEU A 125 ? 0.28656 0.44647 0.42011 0.03024  0.05233  -0.05475 119 LEU A C   
918  O O   . LEU A 125 ? 0.26547 0.42036 0.38851 0.02835  0.05622  -0.05819 119 LEU A O   
919  C CB  . LEU A 125 ? 0.17006 0.29297 0.29504 0.03483  0.03776  -0.03654 119 LEU A CB  
920  C CG  . LEU A 125 ? 0.28726 0.39841 0.41522 0.03789  0.02867  -0.02752 119 LEU A CG  
921  C CD1 . LEU A 125 ? 0.33937 0.44562 0.48320 0.04858  0.02117  -0.03079 119 LEU A CD1 
922  C CD2 . LEU A 125 ? 0.23115 0.32351 0.34095 0.03308  0.02660  -0.01779 119 LEU A CD2 
923  N N   . SER A 126 ? 0.26452 0.44093 0.39970 0.02334  0.05574  -0.05429 120 SER A N   
924  C CA  . SER A 126 ? 0.26495 0.44954 0.38475 0.01103  0.06335  -0.05449 120 SER A CA  
925  C C   . SER A 126 ? 0.17889 0.34757 0.27798 0.00263  0.06294  -0.04400 120 SER A C   
926  O O   . SER A 126 ? 0.19068 0.34173 0.28606 0.00505  0.05604  -0.03492 120 SER A O   
927  C CB  . SER A 126 ? 0.22933 0.43129 0.35406 0.00464  0.06524  -0.05463 120 SER A CB  
928  O OG  . SER A 126 ? 0.16561 0.36514 0.28727 -0.00089 0.06241  -0.04512 120 SER A OG  
929  N N   . ASN A 127 ? 0.28653 0.45750 0.36937 -0.00752 0.06870  -0.04417 121 ASN A N   
930  C CA  . ASN A 127 ? 0.27093 0.42196 0.33219 -0.01520 0.06572  -0.03299 121 ASN A CA  
931  C C   . ASN A 127 ? 0.27999 0.42673 0.33824 -0.02052 0.06178  -0.02378 121 ASN A C   
932  O O   . ASN A 127 ? 0.23650 0.36329 0.28443 -0.02078 0.05613  -0.01505 121 ASN A O   
933  C CB  . ASN A 127 ? 0.27486 0.43006 0.31890 -0.02661 0.07141  -0.03399 121 ASN A CB  
934  C CG  . ASN A 127 ? 0.38491 0.51804 0.40779 -0.03346 0.06656  -0.02256 121 ASN A CG  
935  O OD1 . ASN A 127 ? 0.23499 0.34921 0.25524 -0.02680 0.06081  -0.01814 121 ASN A OD1 
936  N ND2 . ASN A 127 ? 0.32875 0.46442 0.33696 -0.04703 0.06829  -0.01781 121 ASN A ND2 
937  N N   . ASP A 128 ? 0.24225 0.40854 0.31018 -0.02477 0.06466  -0.02647 122 ASP A N   
938  C CA  . ASP A 128 ? 0.20093 0.36363 0.26660 -0.03016 0.06060  -0.01846 122 ASP A CA  
939  C C   . ASP A 128 ? 0.18944 0.33960 0.26356 -0.02005 0.05305  -0.01457 122 ASP A C   
940  O O   . ASP A 128 ? 0.21734 0.35280 0.28239 -0.02291 0.04811  -0.00642 122 ASP A O   
941  C CB  . ASP A 128 ? 0.24310 0.43188 0.31930 -0.03687 0.06518  -0.02296 122 ASP A CB  
942  C CG  . ASP A 128 ? 0.20520 0.39595 0.26463 -0.04995 0.06887  -0.02205 122 ASP A CG  
943  O OD1 . ASP A 128 ? 0.25162 0.42670 0.29143 -0.05808 0.06766  -0.01470 122 ASP A OD1 
944  O OD2 . ASP A 128 ? 0.22641 0.43415 0.29219 -0.05222 0.07222  -0.02857 122 ASP A OD2 
945  N N   . HIS A 129 ? 0.15420 0.30950 0.24512 -0.00857 0.05161  -0.02050 123 HIS A N   
946  C CA  . HIS A 129 ? 0.16883 0.31150 0.26572 -0.00036 0.04384  -0.01590 123 HIS A CA  
947  C C   . HIS A 129 ? 0.15688 0.27612 0.23958 0.00128  0.04053  -0.01000 123 HIS A C   
948  O O   . HIS A 129 ? 0.13402 0.24094 0.21144 0.00114  0.03543  -0.00310 123 HIS A O   
949  C CB  . HIS A 129 ? 0.14350 0.29497 0.26107 0.01105  0.04156  -0.02302 123 HIS A CB  
950  C CG  . HIS A 129 ? 0.20131 0.37447 0.33678 0.01185  0.04140  -0.02729 123 HIS A CG  
951  N ND1 . HIS A 129 ? 0.15869 0.35612 0.30406 0.00950  0.04851  -0.03687 123 HIS A ND1 
952  C CD2 . HIS A 129 ? 0.20386 0.37968 0.34933 0.01424  0.03486  -0.02354 123 HIS A CD2 
953  C CE1 . HIS A 129 ? 0.19423 0.40721 0.35539 0.01104  0.04598  -0.03864 123 HIS A CE1 
954  N NE2 . HIS A 129 ? 0.16046 0.36183 0.32294 0.01402  0.03758  -0.03079 123 HIS A NE2 
955  N N   . ILE A 130 ? 0.15566 0.27007 0.23238 0.00254  0.04349  -0.01333 124 ILE A N   
956  C CA  . ILE A 130 ? 0.11555 0.21018 0.17987 0.00369  0.04050  -0.00835 124 ILE A CA  
957  C C   . ILE A 130 ? 0.17043 0.25501 0.21961 -0.00406 0.03903  -0.00092 124 ILE A C   
958  O O   . ILE A 130 ? 0.19821 0.26908 0.24212 -0.00226 0.03455  0.00418  124 ILE A O   
959  C CB  . ILE A 130 ? 0.12065 0.21387 0.18037 0.00471  0.04409  -0.01358 124 ILE A CB  
960  C CG1 . ILE A 130 ? 0.12997 0.22968 0.20525 0.01377  0.04421  -0.02178 124 ILE A CG1 
961  C CG2 . ILE A 130 ? 0.12646 0.20132 0.17364 0.00489  0.04086  -0.00836 124 ILE A CG2 
962  C CD1 . ILE A 130 ? 0.20249 0.30203 0.27370 0.01459  0.04803  -0.02860 124 ILE A CD1 
963  N N   . CYS A 131 ? 0.17470 0.26612 0.21677 -0.01314 0.04250  -0.00062 125 CYS A N   
964  C CA  . CYS A 131 ? 0.16998 0.24955 0.19744 -0.02073 0.03985  0.00627  125 CYS A CA  
965  C C   . CYS A 131 ? 0.21603 0.29222 0.24671 -0.02046 0.03546  0.01027  125 CYS A C   
966  O O   . CYS A 131 ? 0.18766 0.24880 0.21006 -0.02042 0.03112  0.01471  125 CYS A O   
967  C CB  . CYS A 131 ? 0.20876 0.29658 0.22753 -0.03213 0.04389  0.00628  125 CYS A CB  
968  S SG  . CYS A 131 ? 0.28812 0.35787 0.28712 -0.04251 0.03903  0.01505  125 CYS A SG  
969  N N   . TYR A 132 ? 0.17421 0.26515 0.21745 -0.02005 0.03628  0.00800  126 TYR A N   
970  C CA  . TYR A 132 ? 0.20689 0.29582 0.25264 -0.02070 0.03184  0.01164  126 TYR A CA  
971  C C   . TYR A 132 ? 0.13183 0.21078 0.18050 -0.01244 0.02724  0.01333  126 TYR A C   
972  O O   . TYR A 132 ? 0.10971 0.17873 0.15208 -0.01367 0.02342  0.01709  126 TYR A O   
973  C CB  . TYR A 132 ? 0.23219 0.34136 0.29177 -0.02246 0.03332  0.00862  126 TYR A CB  
974  C CG  . TYR A 132 ? 0.16071 0.27004 0.22282 -0.02455 0.02854  0.01222  126 TYR A CG  
975  C CD1 . TYR A 132 ? 0.20179 0.29775 0.25040 -0.03109 0.02564  0.01711  126 TYR A CD1 
976  C CD2 . TYR A 132 ? 0.13052 0.25326 0.20875 -0.02000 0.02621  0.01028  126 TYR A CD2 
977  C CE1 . TYR A 132 ? 0.23992 0.33616 0.28998 -0.03355 0.02132  0.01955  126 TYR A CE1 
978  C CE2 . TYR A 132 ? 0.12217 0.24563 0.20184 -0.02272 0.02135  0.01372  126 TYR A CE2 
979  C CZ  . TYR A 132 ? 0.16130 0.27177 0.22633 -0.02982 0.01935  0.01812  126 TYR A CZ  
980  O OH  . TYR A 132 ? 0.30981 0.42094 0.37537 -0.03298 0.01455  0.02075  126 TYR A OH  
981  N N   . PHE A 133 ? 0.14794 0.22931 0.20551 -0.00470 0.02744  0.01026  127 PHE A N   
982  C CA  . PHE A 133 ? 0.13990 0.21164 0.19867 0.00133  0.02292  0.01266  127 PHE A CA  
983  C C   . PHE A 133 ? 0.17073 0.22748 0.21626 0.00037  0.02216  0.01541  127 PHE A C   
984  O O   . PHE A 133 ? 0.15495 0.20478 0.19652 0.00048  0.01883  0.01841  127 PHE A O   
985  C CB  . PHE A 133 ? 0.17893 0.25346 0.24836 0.00885  0.02261  0.00897  127 PHE A CB  
986  C CG  . PHE A 133 ? 0.26173 0.34989 0.34750 0.01251  0.02104  0.00583  127 PHE A CG  
987  C CD1 . PHE A 133 ? 0.16673 0.26450 0.25707 0.00890  0.01959  0.00731  127 PHE A CD1 
988  C CD2 . PHE A 133 ? 0.23638 0.32749 0.33385 0.01995  0.02023  0.00087  127 PHE A CD2 
989  C CE1 . PHE A 133 ? 0.28022 0.39206 0.38761 0.01298  0.01732  0.00402  127 PHE A CE1 
990  C CE2 . PHE A 133 ? 0.19292 0.29659 0.30764 0.02480  0.01768  -0.00295 127 PHE A CE2 
991  C CZ  . PHE A 133 ? 0.17828 0.29318 0.29854 0.02149  0.01618  -0.00130 127 PHE A CZ  
992  N N   . LEU A 134 ? 0.19822 0.25104 0.23716 -0.00063 0.02507  0.01386  128 LEU A N   
993  C CA  . LEU A 134 ? 0.14699 0.18680 0.17538 -0.00065 0.02360  0.01584  128 LEU A CA  
994  C C   . LEU A 134 ? 0.17024 0.20317 0.19048 -0.00509 0.02116  0.01864  128 LEU A C   
995  O O   . LEU A 134 ? 0.12189 0.14673 0.13832 -0.00315 0.01851  0.01954  128 LEU A O   
996  C CB  . LEU A 134 ? 0.15715 0.19467 0.17957 -0.00188 0.02619  0.01409  128 LEU A CB  
997  C CG  . LEU A 134 ? 0.14599 0.17096 0.15897 -0.00136 0.02369  0.01589  128 LEU A CG  
998  C CD1 . LEU A 134 ? 0.23937 0.26119 0.25643 0.00441  0.02193  0.01558  128 LEU A CD1 
999  C CD2 . LEU A 134 ? 0.18013 0.20307 0.18572 -0.00413 0.02527  0.01505  128 LEU A CD2 
1000 N N   . TYR A 135 ? 0.14154 0.17800 0.15919 -0.01144 0.02198  0.01941  129 TYR A N   
1001 C CA  . TYR A 135 ? 0.17529 0.20317 0.18501 -0.01605 0.01873  0.02178  129 TYR A CA  
1002 C C   . TYR A 135 ? 0.18827 0.21614 0.20146 -0.01380 0.01600  0.02201  129 TYR A C   
1003 O O   . TYR A 135 ? 0.16462 0.18266 0.17172 -0.01352 0.01307  0.02200  129 TYR A O   
1004 C CB  . TYR A 135 ? 0.19117 0.22410 0.19798 -0.02481 0.01985  0.02304  129 TYR A CB  
1005 C CG  . TYR A 135 ? 0.22220 0.24534 0.22154 -0.03005 0.01558  0.02535  129 TYR A CG  
1006 C CD1 . TYR A 135 ? 0.17480 0.18106 0.16288 -0.03174 0.01163  0.02698  129 TYR A CD1 
1007 C CD2 . TYR A 135 ? 0.20587 0.23581 0.20984 -0.03289 0.01454  0.02554  129 TYR A CD2 
1008 C CE1 . TYR A 135 ? 0.18069 0.17591 0.16231 -0.03587 0.00686  0.02812  129 TYR A CE1 
1009 C CE2 . TYR A 135 ? 0.26025 0.28020 0.25688 -0.03791 0.01033  0.02688  129 TYR A CE2 
1010 C CZ  . TYR A 135 ? 0.21593 0.21793 0.20143 -0.03920 0.00655  0.02784  129 TYR A CZ  
1011 O OH  . TYR A 135 ? 0.20580 0.19587 0.18433 -0.04360 0.00155  0.02824  129 TYR A OH  
1012 N N   . GLN A 136 ? 0.18372 0.22279 0.20673 -0.01214 0.01646  0.02177  130 GLN A N   
1013 C CA  . GLN A 136 ? 0.17106 0.21069 0.19568 -0.01160 0.01325  0.02279  130 GLN A CA  
1014 C C   . GLN A 136 ? 0.15356 0.18730 0.17611 -0.00689 0.01210  0.02259  130 GLN A C   
1015 O O   . GLN A 136 ? 0.16743 0.19747 0.18527 -0.00785 0.01002  0.02241  130 GLN A O   
1016 C CB  . GLN A 136 ? 0.11672 0.16940 0.15271 -0.01105 0.01248  0.02331  130 GLN A CB  
1017 C CG  . GLN A 136 ? 0.10249 0.16494 0.14210 -0.01667 0.01373  0.02288  130 GLN A CG  
1018 C CD  . GLN A 136 ? 0.18588 0.26307 0.23960 -0.01465 0.01222  0.02245  130 GLN A CD  
1019 O OE1 . GLN A 136 ? 0.14785 0.22764 0.20352 -0.01613 0.00809  0.02445  130 GLN A OE1 
1020 N NE2 . GLN A 136 ? 0.11710 0.20414 0.18113 -0.01092 0.01502  0.01930  130 GLN A NE2 
1021 N N   . ILE A 137 ? 0.12038 0.15428 0.14629 -0.00247 0.01359  0.02208  131 ILE A N   
1022 C CA  . ILE A 137 ? 0.12935 0.15869 0.15291 0.00059  0.01284  0.02197  131 ILE A CA  
1023 C C   . ILE A 137 ? 0.17819 0.19963 0.19361 0.00014  0.01267  0.01997  131 ILE A C   
1024 O O   . ILE A 137 ? 0.16824 0.18881 0.18081 0.00021  0.01161  0.01880  131 ILE A O   
1025 C CB  . ILE A 137 ? 0.15764 0.18707 0.18536 0.00448  0.01425  0.02145  131 ILE A CB  
1026 C CG1 . ILE A 137 ? 0.14818 0.18403 0.18557 0.00647  0.01301  0.02240  131 ILE A CG1 
1027 C CG2 . ILE A 137 ? 0.14861 0.17402 0.17322 0.00616  0.01370  0.02136  131 ILE A CG2 
1028 C CD1 . ILE A 137 ? 0.12413 0.16038 0.16646 0.01009  0.01486  0.01996  131 ILE A CD1 
1029 N N   . LEU A 138 ? 0.13108 0.14697 0.14273 -0.00046 0.01328  0.01919  132 LEU A N   
1030 C CA  . LEU A 138 ? 0.19109 0.19771 0.19642 0.00036  0.01144  0.01713  132 LEU A CA  
1031 C C   . LEU A 138 ? 0.18251 0.18520 0.18384 -0.00240 0.00898  0.01587  132 LEU A C   
1032 O O   . LEU A 138 ? 0.15022 0.14811 0.14903 -0.00015 0.00725  0.01228  132 LEU A O   
1033 C CB  . LEU A 138 ? 0.13646 0.13650 0.13750 -0.00064 0.01106  0.01796  132 LEU A CB  
1034 C CG  . LEU A 138 ? 0.20790 0.21039 0.21122 0.00208  0.01311  0.01799  132 LEU A CG  
1035 C CD1 . LEU A 138 ? 0.22947 0.22735 0.22681 -0.00121 0.01293  0.01944  132 LEU A CD1 
1036 C CD2 . LEU A 138 ? 0.20456 0.20499 0.20889 0.00684  0.01199  0.01579  132 LEU A CD2 
1037 N N   . ARG A 139 ? 0.18083 0.18627 0.18217 -0.00724 0.00873  0.01791  133 ARG A N   
1038 C CA  . ARG A 139 ? 0.17850 0.18012 0.17573 -0.01071 0.00604  0.01660  133 ARG A CA  
1039 C C   . ARG A 139 ? 0.13887 0.14564 0.13716 -0.00912 0.00597  0.01428  133 ARG A C   
1040 O O   . ARG A 139 ? 0.17509 0.17685 0.16910 -0.00871 0.00430  0.01001  133 ARG A O   
1041 C CB  . ARG A 139 ? 0.18072 0.18720 0.17896 -0.01707 0.00594  0.01954  133 ARG A CB  
1042 C CG  . ARG A 139 ? 0.15707 0.15832 0.15011 -0.02227 0.00260  0.01858  133 ARG A CG  
1043 C CD  . ARG A 139 ? 0.21489 0.22293 0.20978 -0.02955 0.00278  0.02178  133 ARG A CD  
1044 N NE  . ARG A 139 ? 0.20927 0.21196 0.19879 -0.03582 -0.00086 0.02123  133 ARG A NE  
1045 C CZ  . ARG A 139 ? 0.31008 0.32111 0.30244 -0.03869 -0.00202 0.02121  133 ARG A CZ  
1046 N NH1 . ARG A 139 ? 0.26826 0.29260 0.26885 -0.03563 -0.00059 0.02228  133 ARG A NH1 
1047 N NH2 . ARG A 139 ? 0.25052 0.25528 0.23694 -0.04511 -0.00564 0.02035  133 ARG A NH2 
1048 N N   . GLY A 140 ? 0.17557 0.19215 0.17917 -0.00848 0.00739  0.01675  134 GLY A N   
1049 C CA  . GLY A 140 ? 0.11980 0.14133 0.12242 -0.00850 0.00707  0.01572  134 GLY A CA  
1050 C C   . GLY A 140 ? 0.14540 0.16528 0.14614 -0.00486 0.00854  0.01169  134 GLY A C   
1051 O O   . GLY A 140 ? 0.17543 0.19727 0.17248 -0.00563 0.00859  0.00753  134 GLY A O   
1052 N N   . LEU A 141 ? 0.15052 0.16826 0.15410 -0.00113 0.00989  0.01210  135 LEU A N   
1053 C CA  . LEU A 141 ? 0.21740 0.23560 0.22094 0.00232  0.01105  0.00809  135 LEU A CA  
1054 C C   . LEU A 141 ? 0.14025 0.15199 0.14094 0.00455  0.00950  0.00178  135 LEU A C   
1055 O O   . LEU A 141 ? 0.17743 0.19341 0.17853 0.00664  0.01040  -0.00395 135 LEU A O   
1056 C CB  . LEU A 141 ? 0.13532 0.15209 0.14234 0.00541  0.01201  0.00997  135 LEU A CB  
1057 C CG  . LEU A 141 ? 0.12220 0.14264 0.13095 0.00821  0.01320  0.00675  135 LEU A CG  
1058 C CD1 . LEU A 141 ? 0.16438 0.19423 0.17310 0.00499  0.01467  0.00770  135 LEU A CD1 
1059 C CD2 . LEU A 141 ? 0.19634 0.21413 0.20769 0.01073  0.01342  0.00853  135 LEU A CD2 
1060 N N   . LYS A 142 ? 0.16239 0.16402 0.16049 0.00393  0.00680  0.00235  136 LYS A N   
1061 C CA  . LYS A 142 ? 0.16828 0.16027 0.16378 0.00644  0.00345  -0.00347 136 LYS A CA  
1062 C C   . LYS A 142 ? 0.17312 0.16906 0.16664 0.00540  0.00367  -0.00959 136 LYS A C   
1063 O O   . LYS A 142 ? 0.17462 0.17055 0.16943 0.00968  0.00313  -0.01761 136 LYS A O   
1064 C CB  . LYS A 142 ? 0.14069 0.11972 0.13171 0.00348  -0.00042 -0.00018 136 LYS A CB  
1065 C CG  . LYS A 142 ? 0.17133 0.13679 0.15896 0.00545  -0.00580 -0.00569 136 LYS A CG  
1066 C CD  . LYS A 142 ? 0.18872 0.14001 0.16988 0.00005  -0.01048 -0.00116 136 LYS A CD  
1067 C CE  . LYS A 142 ? 0.22836 0.16299 0.20613 0.00243  -0.01747 -0.00683 136 LYS A CE  
1068 N NZ  . LYS A 142 ? 0.23053 0.15055 0.20026 -0.00519 -0.02267 -0.00226 136 LYS A NZ  
1069 N N   . TYR A 143 ? 0.16198 0.16257 0.15281 -0.00025 0.00434  -0.00659 137 TYR A N   
1070 C CA  . TYR A 143 ? 0.14251 0.14809 0.12977 -0.00268 0.00467  -0.01203 137 TYR A CA  
1071 C C   . TYR A 143 ? 0.20212 0.22046 0.19088 -0.00134 0.00848  -0.01606 137 TYR A C   
1072 O O   . TYR A 143 ? 0.19701 0.21877 0.18452 0.00016  0.00936  -0.02511 137 TYR A O   
1073 C CB  . TYR A 143 ? 0.17074 0.18022 0.15524 -0.00950 0.00396  -0.00646 137 TYR A CB  
1074 C CG  . TYR A 143 ? 0.21389 0.22874 0.19287 -0.01362 0.00378  -0.01108 137 TYR A CG  
1075 C CD1 . TYR A 143 ? 0.27045 0.27699 0.24468 -0.01548 0.00081  -0.01636 137 TYR A CD1 
1076 C CD2 . TYR A 143 ? 0.26289 0.29039 0.24017 -0.01664 0.00606  -0.00995 137 TYR A CD2 
1077 C CE1 . TYR A 143 ? 0.18578 0.19761 0.15400 -0.01975 0.00074  -0.02142 137 TYR A CE1 
1078 C CE2 . TYR A 143 ? 0.25698 0.29028 0.22735 -0.02171 0.00590  -0.01408 137 TYR A CE2 
1079 C CZ  . TYR A 143 ? 0.22547 0.25147 0.19148 -0.02299 0.00355  -0.02032 137 TYR A CZ  
1080 O OH  . TYR A 143 ? 0.28822 0.32033 0.24647 -0.02845 0.00348  -0.02528 137 TYR A OH  
1081 N N   . ILE A 144 ? 0.19593 0.22184 0.18739 -0.00232 0.01072  -0.00994 138 ILE A N   
1082 C CA  . ILE A 144 ? 0.18884 0.22717 0.18058 -0.00329 0.01411  -0.01222 138 ILE A CA  
1083 C C   . ILE A 144 ? 0.18801 0.22814 0.18398 0.00271  0.01554  -0.02108 138 ILE A C   
1084 O O   . ILE A 144 ? 0.20472 0.25465 0.19991 0.00234  0.01805  -0.02935 138 ILE A O   
1085 C CB  . ILE A 144 ? 0.11959 0.16162 0.11381 -0.00508 0.01477  -0.00355 138 ILE A CB  
1086 C CG1 . ILE A 144 ? 0.17370 0.21582 0.16566 -0.01017 0.01242  0.00413  138 ILE A CG1 
1087 C CG2 . ILE A 144 ? 0.15180 0.20557 0.14560 -0.00735 0.01785  -0.00527 138 ILE A CG2 
1088 C CD1 . ILE A 144 ? 0.16678 0.20847 0.16325 -0.00986 0.01149  0.01192  138 ILE A CD1 
1089 N N   . HIS A 145 ? 0.14309 0.17497 0.14394 0.00822  0.01377  -0.01996 139 HIS A N   
1090 C CA  . HIS A 145 ? 0.16649 0.19995 0.17317 0.01480  0.01368  -0.02781 139 HIS A CA  
1091 C C   . HIS A 145 ? 0.17928 0.20770 0.18612 0.01883  0.01126  -0.03807 139 HIS A C   
1092 O O   . HIS A 145 ? 0.19457 0.23064 0.20703 0.02373  0.01226  -0.04802 139 HIS A O   
1093 C CB  . HIS A 145 ? 0.17105 0.19499 0.18128 0.01893  0.01090  -0.02314 139 HIS A CB  
1094 C CG  . HIS A 145 ? 0.16417 0.19488 0.17643 0.01692  0.01348  -0.01687 139 HIS A CG  
1095 N ND1 . HIS A 145 ? 0.16350 0.18833 0.17830 0.01969  0.01178  -0.01316 139 HIS A ND1 
1096 C CD2 . HIS A 145 ? 0.18374 0.22535 0.19502 0.01185  0.01690  -0.01363 139 HIS A CD2 
1097 C CE1 . HIS A 145 ? 0.22405 0.25583 0.24008 0.01699  0.01433  -0.00878 139 HIS A CE1 
1098 N NE2 . HIS A 145 ? 0.17176 0.21293 0.18576 0.01220  0.01706  -0.00857 139 HIS A NE2 
1099 N N   . SER A 146 ? 0.17858 0.19474 0.18007 0.01681  0.00784  -0.03657 140 SER A N   
1100 C CA  . SER A 146 ? 0.19966 0.20882 0.20046 0.02008  0.00473  -0.04665 140 SER A CA  
1101 C C   . SER A 146 ? 0.22323 0.24748 0.22229 0.01771  0.00919  -0.05588 140 SER A C   
1102 O O   . SER A 146 ? 0.19771 0.22059 0.19871 0.02222  0.00783  -0.06792 140 SER A O   
1103 C CB  . SER A 146 ? 0.26382 0.25647 0.25805 0.01638  -0.00009 -0.04197 140 SER A CB  
1104 O OG  . SER A 146 ? 0.22729 0.22652 0.21543 0.00839  0.00237  -0.03789 140 SER A OG  
1105 N N   . ALA A 147 ? 0.25281 0.29102 0.24787 0.01048  0.01400  -0.05078 141 ALA A N   
1106 C CA  . ALA A 147 ? 0.25815 0.31281 0.24941 0.00600  0.01866  -0.05826 141 ALA A CA  
1107 C C   . ALA A 147 ? 0.25899 0.33134 0.25637 0.00787  0.02368  -0.06429 141 ALA A C   
1108 O O   . ALA A 147 ? 0.25713 0.34659 0.25046 0.00209  0.02863  -0.06930 141 ALA A O   
1109 C CB  . ALA A 147 ? 0.21126 0.27103 0.19351 -0.00422 0.01977  -0.04858 141 ALA A CB  
1110 N N   . ASN A 148 ? 0.21582 0.28538 0.22230 0.01483  0.02240  -0.06384 142 ASN A N   
1111 C CA  . ASN A 148 ? 0.18682 0.27381 0.20064 0.01636  0.02669  -0.06865 142 ASN A CA  
1112 C C   . ASN A 148 ? 0.22274 0.32180 0.23103 0.00643  0.03088  -0.05914 142 ASN A C   
1113 O O   . ASN A 148 ? 0.21616 0.33428 0.22603 0.00273  0.03590  -0.06365 142 ASN A O   
1114 C CB  . ASN A 148 ? 0.23487 0.33704 0.25353 0.01976  0.03007  -0.08569 142 ASN A CB  
1115 C CG  . ASN A 148 ? 0.29350 0.40964 0.32514 0.02606  0.03199  -0.09334 142 ASN A CG  
1116 O OD1 . ASN A 148 ? 0.24417 0.35093 0.28285 0.03223  0.02777  -0.08890 142 ASN A OD1 
1117 N ND2 . ASN A 148 ? 0.34336 0.48356 0.37813 0.02386  0.03842  -0.10519 142 ASN A ND2 
1118 N N   . VAL A 149 ? 0.15059 0.23873 0.15280 0.00184  0.02836  -0.04608 143 VAL A N   
1119 C CA  . VAL A 149 ? 0.22105 0.31591 0.21782 -0.00709 0.03002  -0.03590 143 VAL A CA  
1120 C C   . VAL A 149 ? 0.17530 0.26096 0.17664 -0.00451 0.02761  -0.02651 143 VAL A C   
1121 O O   . VAL A 149 ? 0.16313 0.23449 0.16742 0.00125  0.02410  -0.02406 143 VAL A O   
1122 C CB  . VAL A 149 ? 0.17482 0.26607 0.16146 -0.01455 0.02825  -0.02947 143 VAL A CB  
1123 C CG1 . VAL A 149 ? 0.20155 0.29507 0.18354 -0.02253 0.02737  -0.01738 143 VAL A CG1 
1124 C CG2 . VAL A 149 ? 0.18242 0.28482 0.16276 -0.01876 0.03114  -0.03918 143 VAL A CG2 
1125 N N   . LEU A 150 ? 0.18418 0.27811 0.18520 -0.00969 0.02939  -0.02149 144 LEU A N   
1126 C CA  . LEU A 150 ? 0.13418 0.21995 0.13814 -0.00877 0.02713  -0.01262 144 LEU A CA  
1127 C C   . LEU A 150 ? 0.16016 0.24298 0.15741 -0.01654 0.02505  -0.00195 144 LEU A C   
1128 O O   . LEU A 150 ? 0.19298 0.28561 0.18363 -0.02505 0.02636  -0.00051 144 LEU A O   
1129 C CB  . LEU A 150 ? 0.14968 0.24557 0.15930 -0.00861 0.02949  -0.01532 144 LEU A CB  
1130 C CG  . LEU A 150 ? 0.26001 0.36470 0.27759 -0.00184 0.03149  -0.02750 144 LEU A CG  
1131 C CD1 . LEU A 150 ? 0.20072 0.31799 0.22412 -0.00346 0.03368  -0.02898 144 LEU A CD1 
1132 C CD2 . LEU A 150 ? 0.24990 0.33935 0.27227 0.00803  0.02737  -0.02934 144 LEU A CD2 
1133 N N   . HIS A 151 ? 0.14182 0.21172 0.14085 -0.01387 0.02141  0.00527  145 HIS A N   
1134 C CA  . HIS A 151 ? 0.16934 0.23535 0.16452 -0.01947 0.01795  0.01488  145 HIS A CA  
1135 C C   . HIS A 151 ? 0.17640 0.24503 0.17112 -0.02430 0.01751  0.01966  145 HIS A C   
1136 O O   . HIS A 151 ? 0.17374 0.24616 0.16168 -0.03297 0.01586  0.02497  145 HIS A O   
1137 C CB  . HIS A 151 ? 0.12354 0.17749 0.12298 -0.01441 0.01458  0.01921  145 HIS A CB  
1138 C CG  . HIS A 151 ? 0.22140 0.27133 0.21957 -0.01818 0.00985  0.02781  145 HIS A CG  
1139 N ND1 . HIS A 151 ? 0.17273 0.21846 0.17284 -0.01944 0.00708  0.03352  145 HIS A ND1 
1140 C CD2 . HIS A 151 ? 0.18518 0.23400 0.18108 -0.02061 0.00635  0.03149  145 HIS A CD2 
1141 C CE1 . HIS A 151 ? 0.20526 0.24673 0.20490 -0.02178 0.00158  0.04025  145 HIS A CE1 
1142 N NE2 . HIS A 151 ? 0.18426 0.22839 0.18164 -0.02253 0.00107  0.03931  145 HIS A NE2 
1143 N N   . ARG A 152 ? 0.13956 0.20520 0.14046 -0.01967 0.01822  0.01842  146 ARG A N   
1144 C CA  . ARG A 152 ? 0.14201 0.21036 0.14341 -0.02384 0.01819  0.02114  146 ARG A CA  
1145 C C   . ARG A 152 ? 0.22702 0.28503 0.22656 -0.02758 0.01285  0.03072  146 ARG A C   
1146 O O   . ARG A 152 ? 0.19835 0.25718 0.19620 -0.03332 0.01172  0.03420  146 ARG A O   
1147 C CB  . ARG A 152 ? 0.17547 0.26008 0.17247 -0.03195 0.02188  0.01787  146 ARG A CB  
1148 C CG  . ARG A 152 ? 0.23879 0.33505 0.23991 -0.02718 0.02680  0.00641  146 ARG A CG  
1149 C CD  . ARG A 152 ? 0.29193 0.40789 0.28931 -0.03548 0.03142  0.00137  146 ARG A CD  
1150 N NE  . ARG A 152 ? 0.29172 0.41742 0.29222 -0.03992 0.03321  0.00123  146 ARG A NE  
1151 C CZ  . ARG A 152 ? 0.32694 0.45956 0.32022 -0.05231 0.03330  0.00720  146 ARG A CZ  
1152 N NH1 . ARG A 152 ? 0.34764 0.47749 0.32964 -0.06140 0.03097  0.01457  146 ARG A NH1 
1153 N NH2 . ARG A 152 ? 0.24239 0.38475 0.23935 -0.05651 0.03506  0.00626  146 ARG A NH2 
1154 N N   . ASP A 153 ? 0.17147 0.21985 0.17204 -0.02451 0.00897  0.03474  147 ASP A N   
1155 C CA  . ASP A 153 ? 0.17489 0.21213 0.17696 -0.02523 0.00296  0.04214  147 ASP A CA  
1156 C C   . ASP A 153 ? 0.19151 0.22101 0.20022 -0.01731 0.00086  0.04194  147 ASP A C   
1157 O O   . ASP A 153 ? 0.19420 0.21798 0.20424 -0.01757 -0.00469 0.04715  147 ASP A O   
1158 C CB  . ASP A 153 ? 0.21370 0.25061 0.20776 -0.03502 -0.00205 0.05010  147 ASP A CB  
1159 C CG  . ASP A 153 ? 0.25405 0.27824 0.24933 -0.03683 -0.00926 0.05749  147 ASP A CG  
1160 O OD1 . ASP A 153 ? 0.23390 0.25244 0.23499 -0.03224 -0.00875 0.05523  147 ASP A OD1 
1161 O OD2 . ASP A 153 ? 0.26512 0.28401 0.25517 -0.04297 -0.01620 0.06550  147 ASP A OD2 
1162 N N   . LEU A 154 ? 0.16269 0.19274 0.17586 -0.01059 0.00490  0.03588  148 LEU A N   
1163 C CA  . LEU A 154 ? 0.12975 0.15498 0.14892 -0.00443 0.00400  0.03505  148 LEU A CA  
1164 C C   . LEU A 154 ? 0.22498 0.24250 0.25006 -0.00109 0.00120  0.03641  148 LEU A C   
1165 O O   . LEU A 154 ? 0.16438 0.17961 0.18975 -0.00053 0.00247  0.03469  148 LEU A O   
1166 C CB  . LEU A 154 ? 0.13410 0.16129 0.15406 -0.00015 0.00852  0.02906  148 LEU A CB  
1167 C CG  . LEU A 154 ? 0.12669 0.15929 0.14199 -0.00206 0.01043  0.02632  148 LEU A CG  
1168 C CD1 . LEU A 154 ? 0.11171 0.14327 0.12733 0.00202  0.01329  0.02071  148 LEU A CD1 
1169 C CD2 . LEU A 154 ? 0.13990 0.17284 0.15501 -0.00350 0.00791  0.02898  148 LEU A CD2 
1170 N N   . LYS A 155 ? 0.13605 0.15012 0.16657 0.00136  -0.00298 0.03877  149 LYS A N   
1171 C CA  . LYS A 155 ? 0.15182 0.15862 0.18975 0.00568  -0.00645 0.03867  149 LYS A CA  
1172 C C   . LYS A 155 ? 0.20502 0.21311 0.25137 0.00999  -0.00958 0.03862  149 LYS A C   
1173 O O   . LYS A 155 ? 0.18182 0.19501 0.22663 0.00782  -0.01047 0.04080  149 LYS A O   
1174 C CB  . LYS A 155 ? 0.12329 0.12200 0.15859 0.00133  -0.01238 0.04418  149 LYS A CB  
1175 C CG  . LYS A 155 ? 0.24232 0.24098 0.27184 -0.00544 -0.01776 0.05160  149 LYS A CG  
1176 C CD  . LYS A 155 ? 0.18494 0.17479 0.20953 -0.01187 -0.02373 0.05788  149 LYS A CD  
1177 C CE  . LYS A 155 ? 0.26712 0.25685 0.28358 -0.02044 -0.02966 0.06629  149 LYS A CE  
1178 N NZ  . LYS A 155 ? 0.29200 0.27139 0.30232 -0.02837 -0.03676 0.07385  149 LYS A NZ  
1179 N N   . PRO A 156 ? 0.17565 0.18058 0.23161 0.01615  -0.01114 0.03519  150 PRO A N   
1180 C CA  . PRO A 156 ? 0.14659 0.15648 0.21316 0.02095  -0.01341 0.03341  150 PRO A CA  
1181 C C   . PRO A 156 ? 0.18344 0.19185 0.25155 0.01896  -0.02162 0.04014  150 PRO A C   
1182 O O   . PRO A 156 ? 0.20304 0.21941 0.27598 0.01990  -0.02226 0.03992  150 PRO A O   
1183 C CB  . PRO A 156 ? 0.11817 0.12420 0.19493 0.02783  -0.01448 0.02774  150 PRO A CB  
1184 C CG  . PRO A 156 ? 0.13121 0.13456 0.20083 0.02642  -0.00868 0.02444  150 PRO A CG  
1185 C CD  . PRO A 156 ? 0.17588 0.17543 0.23401 0.01930  -0.00949 0.03075  150 PRO A CD  
1186 N N   . SER A 157 ? 0.16349 0.16199 0.22683 0.01517  -0.02847 0.04669  151 SER A N   
1187 C CA  . SER A 157 ? 0.23701 0.23280 0.30022 0.01227  -0.03775 0.05427  151 SER A CA  
1188 C C   . SER A 157 ? 0.25373 0.25776 0.30673 0.00507  -0.03532 0.05762  151 SER A C   
1189 O O   . SER A 157 ? 0.22409 0.22894 0.27715 0.00271  -0.04224 0.06297  151 SER A O   
1190 C CB  . SER A 157 ? 0.21178 0.19346 0.26986 0.00795  -0.04637 0.06158  151 SER A CB  
1191 O OG  . SER A 157 ? 0.30500 0.28704 0.34857 -0.00129 -0.04222 0.06472  151 SER A OG  
1192 N N   . ASN A 158 ? 0.18932 0.19911 0.23389 0.00180  -0.02642 0.05415  152 ASN A N   
1193 C CA  . ASN A 158 ? 0.19773 0.21522 0.23334 -0.00404 -0.02355 0.05500  152 ASN A CA  
1194 C C   . ASN A 158 ? 0.25962 0.28521 0.30000 -0.00049 -0.01858 0.04941  152 ASN A C   
1195 O O   . ASN A 158 ? 0.17202 0.20278 0.20507 -0.00450 -0.01514 0.04813  152 ASN A O   
1196 C CB  . ASN A 158 ? 0.19669 0.21581 0.22086 -0.00980 -0.01792 0.05395  152 ASN A CB  
1197 C CG  . ASN A 158 ? 0.24278 0.25831 0.25790 -0.01818 -0.02301 0.06115  152 ASN A CG  
1198 O OD1 . ASN A 158 ? 0.17716 0.18908 0.19121 -0.02130 -0.03119 0.06799  152 ASN A OD1 
1199 N ND2 . ASN A 158 ? 0.17210 0.18917 0.18055 -0.02257 -0.01874 0.05997  152 ASN A ND2 
1200 N N   . LEU A 159 ? 0.18299 0.21007 0.23529 0.00634  -0.01828 0.04567  153 LEU A N   
1201 C CA  . LEU A 159 ? 0.12120 0.15672 0.17810 0.00829  -0.01374 0.04085  153 LEU A CA  
1202 C C   . LEU A 159 ? 0.14300 0.18397 0.21228 0.01153  -0.01962 0.04177  153 LEU A C   
1203 O O   . LEU A 159 ? 0.16213 0.20228 0.24314 0.01776  -0.02247 0.03977  153 LEU A O   
1204 C CB  . LEU A 159 ? 0.16282 0.19872 0.22240 0.01219  -0.00696 0.03456  153 LEU A CB  
1205 C CG  . LEU A 159 ? 0.12005 0.15090 0.16943 0.01004  -0.00229 0.03339  153 LEU A CG  
1206 C CD1 . LEU A 159 ? 0.09460 0.12539 0.14623 0.01348  0.00295  0.02798  153 LEU A CD1 
1207 C CD2 . LEU A 159 ? 0.09870 0.13164 0.13838 0.00513  0.00010  0.03358  153 LEU A CD2 
1208 N N   . LEU A 160 ? 0.11698 0.16393 0.18446 0.00761  -0.02184 0.04407  154 LEU A N   
1209 C CA  . LEU A 160 ? 0.14463 0.19853 0.22423 0.01004  -0.02846 0.04540  154 LEU A CA  
1210 C C   . LEU A 160 ? 0.11016 0.17638 0.19813 0.01144  -0.02319 0.03940  154 LEU A C   
1211 O O   . LEU A 160 ? 0.16002 0.22798 0.23970 0.00727  -0.01645 0.03694  154 LEU A O   
1212 C CB  . LEU A 160 ? 0.13037 0.18426 0.20240 0.00360  -0.03516 0.05213  154 LEU A CB  
1213 C CG  . LEU A 160 ? 0.16965 0.21320 0.22963 -0.00123 -0.03988 0.05892  154 LEU A CG  
1214 C CD1 . LEU A 160 ? 0.23736 0.28276 0.28990 -0.00830 -0.04711 0.06544  154 LEU A CD1 
1215 C CD2 . LEU A 160 ? 0.30329 0.33773 0.37110 0.00405  -0.04623 0.06142  154 LEU A CD2 
1216 N N   . LEU A 161 ? 0.16921 0.24423 0.27410 0.01706  -0.02688 0.03693  155 LEU A N   
1217 C CA  . LEU A 161 ? 0.14081 0.23099 0.25564 0.01761  -0.02204 0.03093  155 LEU A CA  
1218 C C   . LEU A 161 ? 0.13811 0.23957 0.26581 0.01850  -0.02971 0.03252  155 LEU A C   
1219 O O   . LEU A 161 ? 0.13921 0.23818 0.27672 0.02389  -0.03892 0.03510  155 LEU A O   
1220 C CB  . LEU A 161 ? 0.18198 0.27736 0.30814 0.02431  -0.01693 0.02303  155 LEU A CB  
1221 C CG  . LEU A 161 ? 0.18274 0.27042 0.29886 0.02385  -0.00889 0.01987  155 LEU A CG  
1222 C CD1 . LEU A 161 ? 0.13988 0.22654 0.24111 0.01585  -0.00241 0.02079  155 LEU A CD1 
1223 C CD2 . LEU A 161 ? 0.20284 0.27439 0.31234 0.02609  -0.01247 0.02348  155 LEU A CD2 
1224 N N   . ASN A 162 ? 0.15510 0.26822 0.28286 0.01294  -0.02691 0.03127  156 ASN A N   
1225 C CA  . ASN A 162 ? 0.14866 0.27614 0.29109 0.01374  -0.03357 0.03154  156 ASN A CA  
1226 C C   . ASN A 162 ? 0.17009 0.31569 0.33250 0.01937  -0.02949 0.02272  156 ASN A C   
1227 O O   . ASN A 162 ? 0.17035 0.31582 0.33365 0.02240  -0.02202 0.01690  156 ASN A O   
1228 C CB  . ASN A 162 ? 0.15005 0.28122 0.28240 0.00394  -0.03380 0.03484  156 ASN A CB  
1229 C CG  . ASN A 162 ? 0.20791 0.34496 0.33431 -0.00243 -0.02388 0.03038  156 ASN A CG  
1230 O OD1 . ASN A 162 ? 0.26824 0.41070 0.39979 -0.00013 -0.01676 0.02471  156 ASN A OD1 
1231 N ND2 . ASN A 162 ? 0.33920 0.47472 0.45394 -0.01127 -0.02408 0.03300  156 ASN A ND2 
1232 N N   . THR A 163 ? 0.12533 0.28845 0.30415 0.02035  -0.03427 0.02108  157 THR A N   
1233 C CA  . THR A 163 ? 0.19007 0.37423 0.39107 0.02638  -0.03098 0.01143  157 THR A CA  
1234 C C   . THR A 163 ? 0.22302 0.41880 0.41918 0.01927  -0.01819 0.00551  157 THR A C   
1235 O O   . THR A 163 ? 0.18143 0.39295 0.39161 0.02344  -0.01243 -0.00369 157 THR A O   
1236 C CB  . THR A 163 ? 0.18072 0.38281 0.40157 0.02879  -0.03993 0.01113  157 THR A CB  
1237 O OG1 . THR A 163 ? 0.33411 0.55340 0.58075 0.03943  -0.04021 0.00115  157 THR A OG1 
1238 C CG2 . THR A 163 ? 0.22222 0.43932 0.43954 0.01757  -0.03593 0.01155  157 THR A CG2 
1239 N N   . THR A 164 ? 0.13334 0.32142 0.30969 0.00840  -0.01406 0.01027  158 THR A N   
1240 C CA  . THR A 164 ? 0.09196 0.28713 0.26076 0.00018  -0.00356 0.00651  158 THR A CA  
1241 C C   . THR A 164 ? 0.24277 0.41805 0.39257 -0.00096 0.00203  0.00794  158 THR A C   
1242 O O   . THR A 164 ? 0.22986 0.40116 0.36538 -0.00960 0.00794  0.00876  158 THR A O   
1243 C CB  . THR A 164 ? 0.14275 0.34244 0.30324 -0.01174 -0.00368 0.01029  158 THR A CB  
1244 O OG1 . THR A 164 ? 0.18141 0.36328 0.32812 -0.01395 -0.01032 0.01793  158 THR A OG1 
1245 C CG2 . THR A 164 ? 0.25252 0.47841 0.43388 -0.01233 -0.00656 0.00673  158 THR A CG2 
1246 N N   . CME A 165 ? 0.13956 0.30189 0.28959 0.00757  -0.00095 0.00857  159 CME A N   
1247 C CA  . CME A 165 ? 0.17816 0.32281 0.31272 0.00807  0.00406  0.00896  159 CME A CA  
1248 C CB  . CME A 165 ? 0.20278 0.35703 0.33910 0.00697  0.01292  0.00190  159 CME A CB  
1249 S SG  . CME A 165 ? 0.17064 0.34251 0.33216 0.01817  0.01314  -0.00841 159 CME A SG  
1250 S SD  . CME A 165 ? 0.25880 0.40785 0.42160 0.03000  0.00445  -0.00552 159 CME A SD  
1251 C CE  . CME A 165 ? 0.24071 0.39253 0.41968 0.03587  -0.00888 -0.00120 159 CME A CE  
1252 C CZ  . CME A 165 ? 0.23933 0.41014 0.44159 0.04279  -0.01098 -0.00886 159 CME A CZ  
1253 O OH  . CME A 165 ? 0.20013 0.37159 0.41201 0.05135  -0.00840 -0.01775 159 CME A OH  
1254 C C   . CME A 165 ? 0.22791 0.35557 0.33994 -0.00016 0.00459  0.01559  159 CME A C   
1255 O O   . CME A 165 ? 0.18818 0.30527 0.28786 -0.00196 0.00924  0.01544  159 CME A O   
1256 N N   . ASP A 166 ? 0.17949 0.30578 0.28803 -0.00431 -0.00068 0.02029  160 ASP A N   
1257 C CA  . ASP A 166 ? 0.19071 0.30113 0.28084 -0.00947 -0.00124 0.02469  160 ASP A CA  
1258 C C   . ASP A 166 ? 0.15500 0.25213 0.24026 -0.00418 -0.00425 0.02742  160 ASP A C   
1259 O O   . ASP A 166 ? 0.12497 0.22366 0.21927 0.00090  -0.00997 0.02916  160 ASP A O   
1260 C CB  . ASP A 166 ? 0.19289 0.30605 0.27986 -0.01591 -0.00591 0.02788  160 ASP A CB  
1261 C CG  . ASP A 166 ? 0.19671 0.32380 0.28874 -0.02259 -0.00352 0.02564  160 ASP A CG  
1262 O OD1 . ASP A 166 ? 0.27664 0.39899 0.35838 -0.02887 0.00128  0.02475  160 ASP A OD1 
1263 O OD2 . ASP A 166 ? 0.27555 0.41835 0.38188 -0.02205 -0.00712 0.02504  160 ASP A OD2 
1264 N N   . LEU A 167 ? 0.15398 0.23817 0.22531 -0.00572 -0.00106 0.02791  161 LEU A N   
1265 C CA  . LEU A 167 ? 0.09591 0.16937 0.16239 -0.00186 -0.00239 0.02972  161 LEU A CA  
1266 C C   . LEU A 167 ? 0.13660 0.20214 0.19018 -0.00621 -0.00457 0.03275  161 LEU A C   
1267 O O   . LEU A 167 ? 0.16634 0.22940 0.21135 -0.01097 -0.00263 0.03153  161 LEU A O   
1268 C CB  . LEU A 167 ? 0.13756 0.20516 0.20030 0.00054  0.00332  0.02657  161 LEU A CB  
1269 C CG  . LEU A 167 ? 0.18179 0.23957 0.24036 0.00410  0.00296  0.02753  161 LEU A CG  
1270 C CD1 . LEU A 167 ? 0.18753 0.24473 0.24900 0.00772  0.00738  0.02355  161 LEU A CD1 
1271 C CD2 . LEU A 167 ? 0.19461 0.24387 0.23980 0.00070  0.00390  0.02864  161 LEU A CD2 
1272 N N   . LYS A 168 ? 0.14283 0.20437 0.19474 -0.00504 -0.00886 0.03633  162 LYS A N   
1273 C CA  . LYS A 168 ? 0.16768 0.22407 0.20697 -0.00968 -0.01007 0.03830  162 LYS A CA  
1274 C C   . LYS A 168 ? 0.19385 0.24381 0.22903 -0.00812 -0.01012 0.04001  162 LYS A C   
1275 O O   . LYS A 168 ? 0.15353 0.20206 0.19572 -0.00460 -0.01348 0.04261  162 LYS A O   
1276 C CB  . LYS A 168 ? 0.12012 0.18108 0.15853 -0.01405 -0.01662 0.04238  162 LYS A CB  
1277 C CG  . LYS A 168 ? 0.14353 0.21167 0.18505 -0.01723 -0.01716 0.04086  162 LYS A CG  
1278 C CD  . LYS A 168 ? 0.21544 0.28815 0.25569 -0.02175 -0.02462 0.04527  162 LYS A CD  
1279 C CE  . LYS A 168 ? 0.33007 0.41167 0.37564 -0.02512 -0.02609 0.04405  162 LYS A CE  
1280 N NZ  . LYS A 168 ? 0.30488 0.38269 0.34082 -0.02982 -0.02089 0.03955  162 LYS A NZ  
1281 N N   . ILE A 169 ? 0.13444 0.18083 0.15885 -0.01089 -0.00678 0.03802  163 ILE A N   
1282 C CA  . ILE A 169 ? 0.14547 0.18807 0.16529 -0.01094 -0.00588 0.03895  163 ILE A CA  
1283 C C   . ILE A 169 ? 0.13047 0.17461 0.14330 -0.01697 -0.01061 0.04394  163 ILE A C   
1284 O O   . ILE A 169 ? 0.17406 0.22180 0.17981 -0.02195 -0.01123 0.04335  163 ILE A O   
1285 C CB  . ILE A 169 ? 0.21559 0.25623 0.22915 -0.01060 -0.00001 0.03329  163 ILE A CB  
1286 C CG1 . ILE A 169 ? 0.13784 0.17541 0.15654 -0.00572 0.00340  0.02991  163 ILE A CG1 
1287 C CG2 . ILE A 169 ? 0.21040 0.25061 0.21953 -0.01202 0.00108  0.03380  163 ILE A CG2 
1288 C CD1 . ILE A 169 ? 0.15577 0.18995 0.16907 -0.00497 0.00711  0.02468  163 ILE A CD1 
1289 N N   . CYS A 170 ? 0.15888 0.19961 0.17243 -0.01742 -0.01432 0.04890  164 CYS A N   
1290 C CA  A CYS A 170 ? 0.19750 0.23813 0.20363 -0.02439 -0.02042 0.05570  164 CYS A CA  
1291 C CA  B CYS A 170 ? 0.19662 0.23767 0.20213 -0.02467 -0.02002 0.05535  164 CYS A CA  
1292 C C   . CYS A 170 ? 0.27912 0.31857 0.27693 -0.02897 -0.01812 0.05661  164 CYS A C   
1293 O O   . CYS A 170 ? 0.19389 0.23130 0.19477 -0.02518 -0.01349 0.05298  164 CYS A O   
1294 C CB  A CYS A 170 ? 0.21375 0.24976 0.22853 -0.02196 -0.02969 0.06251  164 CYS A CB  
1295 C CB  B CYS A 170 ? 0.22238 0.25988 0.23580 -0.02295 -0.02950 0.06226  164 CYS A CB  
1296 S SG  A CYS A 170 ? 0.23853 0.27278 0.24369 -0.03139 -0.04053 0.07301  164 CYS A SG  
1297 S SG  B CYS A 170 ? 0.25503 0.28327 0.27886 -0.01623 -0.03256 0.06406  164 CYS A SG  
1298 N N   . ASP A 171 ? 0.22301 0.26469 0.20986 -0.03815 -0.02176 0.06181  165 ASP A N   
1299 C CA  . ASP A 171 ? 0.24868 0.29164 0.22605 -0.04568 -0.02056 0.06416  165 ASP A CA  
1300 C C   . ASP A 171 ? 0.25346 0.30498 0.22729 -0.04600 -0.01070 0.05501  165 ASP A C   
1301 O O   . ASP A 171 ? 0.26721 0.31696 0.24771 -0.03996 -0.00637 0.05060  165 ASP A O   
1302 C CB  . ASP A 171 ? 0.24643 0.27938 0.22923 -0.04357 -0.02497 0.06943  165 ASP A CB  
1303 C CG  . ASP A 171 ? 0.24146 0.27478 0.21296 -0.05433 -0.02633 0.07477  165 ASP A CG  
1304 O OD1 . ASP A 171 ? 0.19950 0.24270 0.15894 -0.06374 -0.02355 0.07434  165 ASP A OD1 
1305 O OD2 . ASP A 171 ? 0.27942 0.30361 0.25370 -0.05410 -0.03011 0.07903  165 ASP A OD2 
1306 N N   . PHE A 172 ? 0.24693 0.30827 0.21047 -0.05302 -0.00758 0.05164  166 PHE A N   
1307 C CA  . PHE A 172 ? 0.23179 0.30326 0.19260 -0.05366 0.00099  0.04206  166 PHE A CA  
1308 C C   . PHE A 172 ? 0.22461 0.30545 0.17487 -0.06501 0.00248  0.04418  166 PHE A C   
1309 O O   . PHE A 172 ? 0.33882 0.43287 0.28457 -0.06832 0.00924  0.03565  166 PHE A O   
1310 C CB  . PHE A 172 ? 0.21794 0.29497 0.17640 -0.05214 0.00455  0.03347  166 PHE A CB  
1311 C CG  . PHE A 172 ? 0.25460 0.32407 0.22316 -0.04165 0.00527  0.02920  166 PHE A CG  
1312 C CD1 . PHE A 172 ? 0.25354 0.31552 0.22695 -0.03887 -0.00010 0.03469  166 PHE A CD1 
1313 C CD2 . PHE A 172 ? 0.25092 0.32125 0.22434 -0.03507 0.01075  0.01994  166 PHE A CD2 
1314 C CE1 . PHE A 172 ? 0.29932 0.35595 0.28081 -0.03124 0.00098  0.03113  166 PHE A CE1 
1315 C CE2 . PHE A 172 ? 0.17846 0.24066 0.15900 -0.02727 0.01058  0.01734  166 PHE A CE2 
1316 C CZ  . PHE A 172 ? 0.19172 0.24760 0.17563 -0.02610 0.00619  0.02303  166 PHE A CZ  
1317 N N   . GLY A 173 ? 0.27108 0.34553 0.21758 -0.07135 -0.00402 0.05504  167 GLY A N   
1318 C CA  . GLY A 173 ? 0.33444 0.41718 0.26904 -0.08465 -0.00348 0.05887  167 GLY A CA  
1319 C C   . GLY A 173 ? 0.39914 0.48954 0.33748 -0.08462 0.00329  0.05336  167 GLY A C   
1320 O O   . GLY A 173 ? 0.38994 0.49314 0.31952 -0.09555 0.00663  0.05237  167 GLY A O   
1321 N N   . LEU A 174 ? 0.31253 0.39620 0.26393 -0.07298 0.00502  0.04943  168 LEU A N   
1322 C CA  . LEU A 174 ? 0.34430 0.43564 0.30097 -0.07158 0.01098  0.04337  168 LEU A CA  
1323 C C   . LEU A 174 ? 0.28071 0.38218 0.24453 -0.06291 0.01866  0.02987  168 LEU A C   
1324 O O   . LEU A 174 ? 0.25110 0.35928 0.22165 -0.05963 0.02303  0.02374  168 LEU A O   
1325 C CB  . LEU A 174 ? 0.27681 0.35381 0.24225 -0.06527 0.00707  0.04784  168 LEU A CB  
1326 C CG  . LEU A 174 ? 0.38295 0.44529 0.34479 -0.07074 -0.00213 0.06028  168 LEU A CG  
1327 C CD1 . LEU A 174 ? 0.42655 0.49578 0.37504 -0.08704 -0.00373 0.06688  168 LEU A CD1 
1328 C CD2 . LEU A 174 ? 0.41591 0.46540 0.37945 -0.06612 -0.00965 0.06602  168 LEU A CD2 
1329 N N   . ALA A 175 ? 0.22004 0.32193 0.18279 -0.05921 0.01942  0.02522  169 ALA A N   
1330 C CA  . ALA A 175 ? 0.25624 0.36315 0.22599 -0.05008 0.02463  0.01292  169 ALA A CA  
1331 C C   . ALA A 175 ? 0.25512 0.38219 0.22345 -0.05427 0.03163  0.00258  169 ALA A C   
1332 O O   . ALA A 175 ? 0.24337 0.38289 0.20207 -0.06620 0.03341  0.00424  169 ALA A O   
1333 C CB  . ALA A 175 ? 0.24334 0.34463 0.21097 -0.04680 0.02285  0.01095  169 ALA A CB  
1334 N N   . ARG A 176 ? 0.22297 0.35376 0.20128 -0.04446 0.03527  -0.00847 170 ARG A N   
1335 C CA  . ARG A 176 ? 0.26906 0.42019 0.25034 -0.04521 0.04183  -0.02118 170 ARG A CA  
1336 C C   . ARG A 176 ? 0.23248 0.38103 0.22195 -0.03311 0.04274  -0.03333 170 ARG A C   
1337 O O   . ARG A 176 ? 0.19009 0.32123 0.18434 -0.02420 0.03855  -0.03097 170 ARG A O   
1338 C CB  . ARG A 176 ? 0.30944 0.47019 0.29807 -0.04591 0.04419  -0.02206 170 ARG A CB  
1339 C CG  . ARG A 176 ? 0.32007 0.48399 0.30045 -0.05919 0.04313  -0.01096 170 ARG A CG  
1340 C CD  . ARG A 176 ? 0.49676 0.67437 0.46664 -0.07127 0.04482  -0.01284 170 ARG A CD  
1341 N NE  . ARG A 176 ? 0.51631 0.69476 0.48024 -0.08258 0.04191  -0.00424 170 ARG A NE  
1342 C CZ  . ARG A 176 ? 0.50877 0.67223 0.46551 -0.08872 0.03569  0.01006  170 ARG A CZ  
1343 N NH1 . ARG A 176 ? 0.42181 0.56955 0.37652 -0.08515 0.03173  0.01797  170 ARG A NH1 
1344 N NH2 . ARG A 176 ? 0.51876 0.68268 0.47057 -0.09863 0.03263  0.01634  170 ARG A NH2 
1345 N N   . VAL A 177 ? 0.29799 0.46419 0.28887 -0.03331 0.04799  -0.04680 171 VAL A N   
1346 C CA  . VAL A 177 ? 0.23164 0.39583 0.23258 -0.02086 0.04806  -0.06000 171 VAL A CA  
1347 C C   . VAL A 177 ? 0.22853 0.39395 0.24340 -0.01213 0.04749  -0.06321 171 VAL A C   
1348 O O   . VAL A 177 ? 0.26335 0.44481 0.28167 -0.01678 0.05097  -0.06372 171 VAL A O   
1349 C CB  . VAL A 177 ? 0.28641 0.46978 0.28592 -0.02295 0.05358  -0.07516 171 VAL A CB  
1350 C CG1 . VAL A 177 ? 0.27031 0.45006 0.28262 -0.00880 0.05205  -0.08952 171 VAL A CG1 
1351 C CG2 . VAL A 177 ? 0.27279 0.45321 0.25741 -0.03150 0.05323  -0.07201 171 VAL A CG2 
1352 N N   . ALA A 178 ? 0.20737 0.35575 0.22953 -0.00049 0.04251  -0.06471 172 ALA A N   
1353 C CA  . ALA A 178 ? 0.19742 0.34488 0.23195 0.00797  0.04040  -0.06693 172 ALA A CA  
1354 C C   . ALA A 178 ? 0.21889 0.38999 0.26454 0.01119  0.04476  -0.08195 172 ALA A C   
1355 O O   . ALA A 178 ? 0.23811 0.41560 0.28420 0.01250  0.04603  -0.09259 172 ALA A O   
1356 C CB  . ALA A 178 ? 0.21676 0.34165 0.25506 0.01873  0.03358  -0.06650 172 ALA A CB  
1357 N N   . ASP A 179 ? 0.24116 0.42047 0.29489 0.01157  0.04473  -0.08068 173 ASP A N   
1358 C CA  . ASP A 179 ? 0.22402 0.41899 0.28698 0.01286  0.04528  -0.09031 173 ASP A CA  
1359 C C   . ASP A 179 ? 0.27203 0.46524 0.34637 0.01953  0.04140  -0.08903 173 ASP A C   
1360 O O   . ASP A 179 ? 0.29055 0.49530 0.36638 0.01317  0.04323  -0.08576 173 ASP A O   
1361 C CB  . ASP A 179 ? 0.28634 0.49952 0.34158 -0.00127 0.05058  -0.08861 173 ASP A CB  
1362 C CG  . ASP A 179 ? 0.35520 0.58757 0.41899 -0.00076 0.05213  -0.10104 173 ASP A CG  
1363 O OD1 . ASP A 179 ? 0.27157 0.50297 0.34821 0.01106  0.04873  -0.11073 173 ASP A OD1 
1364 O OD2 . ASP A 179 ? 0.35177 0.60008 0.40921 -0.01256 0.05618  -0.10100 173 ASP A OD2 
1365 N N   . PRO A 180 ? 0.35309 0.53083 0.43480 0.03182  0.03513  -0.09120 174 PRO A N   
1366 C CA  . PRO A 180 ? 0.28696 0.46047 0.37746 0.03746  0.03030  -0.08795 174 PRO A CA  
1367 C C   . PRO A 180 ? 0.33063 0.52037 0.43217 0.03904  0.02968  -0.09572 174 PRO A C   
1368 O O   . PRO A 180 ? 0.35529 0.54736 0.46225 0.03945  0.02751  -0.09192 174 PRO A O   
1369 C CB  . PRO A 180 ? 0.29891 0.45004 0.39217 0.04921  0.02248  -0.08853 174 PRO A CB  
1370 C CG  . PRO A 180 ? 0.36658 0.51485 0.45766 0.05178  0.02270  -0.09708 174 PRO A CG  
1371 C CD  . PRO A 180 ? 0.35834 0.52035 0.43953 0.04022  0.03118  -0.09620 174 PRO A CD  
1372 N N   . ASP A 181 ? 0.32965 0.53170 0.43512 0.03984  0.03142  -0.10703 175 ASP A N   
1373 C CA  . ASP A 181 ? 0.34717 0.56694 0.46425 0.04155  0.03101  -0.11566 175 ASP A CA  
1374 C C   . ASP A 181 ? 0.34701 0.58725 0.46048 0.02868  0.03754  -0.11287 175 ASP A C   
1375 O O   . ASP A 181 ? 0.35919 0.61436 0.48202 0.02893  0.03725  -0.11795 175 ASP A O   
1376 C CB  . ASP A 181 ? 0.43910 0.66624 0.56280 0.04714  0.03042  -0.12996 175 ASP A CB  
1377 C CG  . ASP A 181 ? 0.40242 0.60800 0.53053 0.05990  0.02226  -0.13311 175 ASP A CG  
1378 O OD1 . ASP A 181 ? 0.41410 0.60294 0.54453 0.06615  0.01553  -0.12647 175 ASP A OD1 
1379 O OD2 . ASP A 181 ? 0.43354 0.63833 0.56212 0.06304  0.02206  -0.14201 175 ASP A OD2 
1380 N N   . HIS A 182 ? 0.31637 0.55710 0.41614 0.01702  0.04272  -0.10467 176 HIS A N   
1381 C CA  . HIS A 182 ? 0.38842 0.64484 0.48209 0.00318  0.04760  -0.10005 176 HIS A CA  
1382 C C   . HIS A 182 ? 0.30594 0.55090 0.39133 -0.00339 0.04727  -0.08521 176 HIS A C   
1383 O O   . HIS A 182 ? 0.31235 0.56150 0.38640 -0.01653 0.05056  -0.07775 176 HIS A O   
1384 C CB  A HIS A 182 ? 0.36323 0.63178 0.44692 -0.00714 0.05293  -0.10342 176 HIS A CB  
1385 C CB  B HIS A 182 ? 0.36338 0.63185 0.44677 -0.00744 0.05297  -0.10309 176 HIS A CB  
1386 C CG  A HIS A 182 ? 0.44381 0.72792 0.53638 -0.00244 0.05397  -0.11914 176 HIS A CG  
1387 C CG  B HIS A 182 ? 0.42562 0.70331 0.51577 -0.00114 0.05351  -0.11786 176 HIS A CG  
1388 N ND1 A HIS A 182 ? 0.42258 0.69885 0.51896 0.00739  0.05188  -0.12742 176 HIS A ND1 
1389 N ND1 B HIS A 182 ? 0.48165 0.76115 0.58746 0.01185  0.04951  -0.12874 176 HIS A ND1 
1390 C CD2 A HIS A 182 ? 0.41175 0.71921 0.51067 -0.00627 0.05666  -0.12867 176 HIS A CD2 
1391 C CD2 B HIS A 182 ? 0.43745 0.72297 0.52090 -0.00639 0.05703  -0.12367 176 HIS A CD2 
1392 C CE1 A HIS A 182 ? 0.48844 0.78232 0.59367 0.00976  0.05312  -0.14153 176 HIS A CE1 
1393 C CE1 B HIS A 182 ? 0.48068 0.76847 0.58976 0.01475  0.05064  -0.14100 176 HIS A CE1 
1394 N NE2 A HIS A 182 ? 0.39077 0.70473 0.49796 0.00166  0.05628  -0.14285 176 HIS A NE2 
1395 N NE2 B HIS A 182 ? 0.51850 0.81073 0.61420 0.00371  0.05557  -0.13846 176 HIS A NE2 
1396 N N   . ASP A 183 ? 0.19906 0.42901 0.28972 0.00524  0.04255  -0.08074 177 ASP A N   
1397 C CA  . ASP A 183 ? 0.23653 0.45495 0.32028 0.00012  0.04198  -0.06776 177 ASP A CA  
1398 C C   . ASP A 183 ? 0.30234 0.52750 0.39017 -0.00485 0.04106  -0.06335 177 ASP A C   
1399 O O   . ASP A 183 ? 0.20736 0.42637 0.28810 -0.01287 0.04132  -0.05271 177 ASP A O   
1400 C CB  . ASP A 183 ? 0.30891 0.50766 0.39479 0.01106  0.03738  -0.06515 177 ASP A CB  
1401 C CG  . ASP A 183 ? 0.29719 0.47888 0.37363 0.00599  0.03546  -0.05134 177 ASP A CG  
1402 O OD1 . ASP A 183 ? 0.28131 0.45712 0.34553 -0.00259 0.03764  -0.04392 177 ASP A OD1 
1403 O OD2 . ASP A 183 ? 0.24183 0.41264 0.32143 0.01035  0.03049  -0.04733 177 ASP A OD2 
1404 N N   . HIS A 184 ? 0.23581 0.47331 0.33496 -0.00068 0.03958  -0.07130 178 HIS A N   
1405 C CA  . HIS A 184 ? 0.21964 0.46388 0.32351 -0.00498 0.03815  -0.06776 178 HIS A CA  
1406 C C   . HIS A 184 ? 0.19280 0.44957 0.28789 -0.02095 0.04272  -0.06362 178 HIS A C   
1407 O O   . HIS A 184 ? 0.25508 0.52455 0.34624 -0.02645 0.04666  -0.06901 178 HIS A O   
1408 C CB  . HIS A 184 ? 0.24436 0.49843 0.36337 0.00452  0.03452  -0.07762 178 HIS A CB  
1409 C CG  . HIS A 184 ? 0.33535 0.57539 0.46187 0.01978  0.02833  -0.08182 178 HIS A CG  
1410 N ND1 . HIS A 184 ? 0.48741 0.71746 0.62061 0.02735  0.02135  -0.07888 178 HIS A ND1 
1411 C CD2 . HIS A 184 ? 0.48887 0.72183 0.61614 0.02807  0.02712  -0.08828 178 HIS A CD2 
1412 C CE1 . HIS A 184 ? 0.47562 0.69179 0.61239 0.03933  0.01572  -0.08254 178 HIS A CE1 
1413 N NE2 . HIS A 184 ? 0.50322 0.72059 0.63686 0.04006  0.01913  -0.08839 178 HIS A NE2 
1414 N N   . THR A 185 ? 0.19677 0.44921 0.28822 -0.02888 0.04146  -0.05403 179 THR A N   
1415 C CA  . THR A 185 ? 0.20130 0.46189 0.28368 -0.04467 0.04386  -0.04852 179 THR A CA  
1416 C C   . THR A 185 ? 0.19691 0.45603 0.28335 -0.04836 0.04052  -0.04304 179 THR A C   
1417 O O   . THR A 185 ? 0.19631 0.45122 0.29324 -0.03852 0.03664  -0.04480 179 THR A O   
1418 C CB  . THR A 185 ? 0.25719 0.50612 0.32296 -0.05483 0.04519  -0.03871 179 THR A CB  
1419 O OG1 . THR A 185 ? 0.28951 0.54647 0.34531 -0.07018 0.04649  -0.03445 179 THR A OG1 
1420 C CG2 . THR A 185 ? 0.22911 0.45752 0.29137 -0.05442 0.04171  -0.02784 179 THR A CG2 
1421 N N   . GLY A 186 ? 0.19982 0.46142 0.27701 -0.06314 0.04115  -0.03617 180 GLY A N   
1422 C CA  . GLY A 186 ? 0.23373 0.49489 0.31377 -0.06866 0.03792  -0.03157 180 GLY A CA  
1423 C C   . GLY A 186 ? 0.39047 0.62988 0.46490 -0.07129 0.03378  -0.02051 180 GLY A C   
1424 O O   . GLY A 186 ? 0.24048 0.46538 0.30956 -0.06815 0.03353  -0.01608 180 GLY A O   
1425 N N   . PHE A 187 ? 0.26047 0.49804 0.33614 -0.07774 0.03028  -0.01639 181 PHE A N   
1426 C CA  . PHE A 187 ? 0.32799 0.54419 0.39928 -0.08001 0.02517  -0.00744 181 PHE A CA  
1427 C C   . PHE A 187 ? 0.25404 0.45447 0.30928 -0.09390 0.02384  0.00392  181 PHE A C   
1428 O O   . PHE A 187 ? 0.27077 0.47631 0.31820 -0.10524 0.02430  0.00635  181 PHE A O   
1429 C CB  . PHE A 187 ? 0.14294 0.36223 0.22149 -0.08102 0.02093  -0.00872 181 PHE A CB  
1430 C CG  . PHE A 187 ? 0.21418 0.40273 0.28382 -0.08001 0.01424  -0.00121 181 PHE A CG  
1431 C CD1 . PHE A 187 ? 0.21455 0.37963 0.28019 -0.06736 0.01164  -0.00001 181 PHE A CD1 
1432 C CD2 . PHE A 187 ? 0.29057 0.47507 0.35636 -0.09208 0.01059  0.00362  181 PHE A CD2 
1433 C CE1 . PHE A 187 ? 0.22778 0.36758 0.28610 -0.06639 0.00630  0.00497  181 PHE A CE1 
1434 C CE2 . PHE A 187 ? 0.25460 0.41137 0.31284 -0.09064 0.00447  0.00866  181 PHE A CE2 
1435 C CZ  . PHE A 187 ? 0.24652 0.38185 0.30136 -0.07746 0.00270  0.00879  181 PHE A CZ  
1436 N N   . LEU A 188 ? 0.27256 0.44414 0.31875 -0.08807 0.02002  0.01026  182 LEU A N   
1437 C CA  . LEU A 188 ? 0.28462 0.43599 0.31675 -0.09853 0.01621  0.02136  182 LEU A CA  
1438 C C   . LEU A 188 ? 0.44813 0.61107 0.47218 -0.10922 0.01990  0.02420  182 LEU A C   
1439 O O   . LEU A 188 ? 0.29942 0.45269 0.31120 -0.12075 0.01612  0.03185  182 LEU A O   
1440 C CB  . LEU A 188 ? 0.45398 0.59677 0.48268 -0.10957 0.01093  0.02686  182 LEU A CB  
1441 C CG  . LEU A 188 ? 0.35397 0.47994 0.38670 -0.10008 0.00606  0.02496  182 LEU A CG  
1442 C CD1 . LEU A 188 ? 0.32957 0.44184 0.35612 -0.11208 -0.00011 0.03125  182 LEU A CD1 
1443 C CD2 . LEU A 188 ? 0.27760 0.38015 0.30757 -0.08625 0.00399  0.02569  182 LEU A CD2 
1444 N N   . THR A 189 ? 0.26930 0.44626 0.29717 -0.10158 0.02540  0.01685  183 THR A N   
1445 C CA  . THR A 189 ? 0.39260 0.57434 0.40978 -0.10722 0.02754  0.01758  183 THR A CA  
1446 C C   . THR A 189 ? 0.36690 0.52847 0.37478 -0.10673 0.02461  0.02586  183 THR A C   
1447 O O   . THR A 189 ? 0.33261 0.48214 0.34525 -0.09609 0.02366  0.02596  183 THR A O   
1448 C CB  . THR A 189 ? 0.30045 0.50536 0.32550 -0.09970 0.03404  0.00484  183 THR A CB  
1449 O OG1 . THR A 189 ? 0.68944 0.89036 0.72127 -0.08651 0.03567  0.00080  183 THR A OG1 
1450 C CG2 . THR A 189 ? 0.43712 0.66128 0.47429 -0.09740 0.03601  -0.00407 183 THR A CG2 
1451 N N   . GLU A 190 ? 0.33417 0.49069 0.32803 -0.11695 0.02201  0.03223  184 GLU A N   
1452 C CA  . GLU A 190 ? 0.69434 0.82973 0.67777 -0.11877 0.01667  0.04197  184 GLU A CA  
1453 C C   . GLU A 190 ? 0.66907 0.80315 0.65690 -0.10762 0.01977  0.03883  184 GLU A C   
1454 O O   . GLU A 190 ? 0.65110 0.80278 0.64713 -0.09996 0.02636  0.02828  184 GLU A O   
1455 C CB  . GLU A 190 ? 0.60454 0.74250 0.57340 -0.13101 0.01415  0.04629  184 GLU A CB  
1456 C CG  . GLU A 190 ? 0.70506 0.84238 0.66684 -0.14380 0.00990  0.05103  184 GLU A CG  
1457 C CD  . GLU A 190 ? 0.76025 0.92545 0.72622 -0.14774 0.01661  0.04132  184 GLU A CD  
1458 O OE1 . GLU A 190 ? 0.60883 0.79036 0.58794 -0.13769 0.02348  0.03050  184 GLU A OE1 
1459 O OE2 . GLU A 190 ? 0.76095 0.93170 0.71730 -0.16078 0.01439  0.04435  184 GLU A OE2 
1460 N N   . TYR A 191 ? 0.65586 0.76843 0.63854 -0.10617 0.01429  0.04762  185 TYR A N   
1461 C CA  . TYR A 191 ? 0.68560 0.79292 0.67118 -0.09358 0.01549  0.04414  185 TYR A CA  
1462 C C   . TYR A 191 ? 0.68939 0.77604 0.66592 -0.09580 0.00807  0.05452  185 TYR A C   
1463 O O   . TYR A 191 ? 0.59981 0.67133 0.57000 -0.10390 0.00071  0.06420  185 TYR A O   
1464 C CB  . TYR A 191 ? 0.53423 0.63371 0.53155 -0.07725 0.01585  0.03747  185 TYR A CB  
1465 C CG  . TYR A 191 ? 0.59920 0.70081 0.60048 -0.06559 0.01911  0.03100  185 TYR A CG  
1466 C CD1 . TYR A 191 ? 0.64537 0.76797 0.65036 -0.06407 0.02571  0.02167  185 TYR A CD1 
1467 C CD2 . TYR A 191 ? 0.59796 0.68109 0.59975 -0.05640 0.01539  0.03358  185 TYR A CD2 
1468 C CE1 . TYR A 191 ? 0.35267 0.47482 0.36063 -0.05394 0.02769  0.01581  185 TYR A CE1 
1469 C CE2 . TYR A 191 ? 0.52732 0.61195 0.53193 -0.04731 0.01796  0.02824  185 TYR A CE2 
1470 C CZ  . TYR A 191 ? 0.41713 0.51978 0.42422 -0.04625 0.02369  0.01975  185 TYR A CZ  
1471 O OH  . TYR A 191 ? 0.54072 0.64233 0.55001 -0.03761 0.02524  0.01452  185 TYR A OH  
1472 N N   . VAL A 192 ? 0.57676 0.66226 0.55347 -0.08816 0.00923  0.05220  186 VAL A N   
1473 C CA  . VAL A 192 ? 0.69196 0.76336 0.66052 -0.09096 0.00264  0.06111  186 VAL A CA  
1474 C C   . VAL A 192 ? 0.49582 0.54830 0.47160 -0.07690 -0.00182 0.06145  186 VAL A C   
1475 O O   . VAL A 192 ? 0.61309 0.64854 0.58572 -0.07808 -0.01018 0.06990  186 VAL A O   
1476 C CB  . VAL A 192 ? 0.61949 0.70644 0.58048 -0.09650 0.00687  0.05906  186 VAL A CB  
1477 C CG1 . VAL A 192 ? 0.68162 0.75503 0.63217 -0.10241 -0.00182 0.06915  186 VAL A CG1 
1478 C CG2 . VAL A 192 ? 0.70064 0.80897 0.65854 -0.10474 0.01245  0.05221  186 VAL A CG2 
1479 N N   . ALA A 193 ? 0.61237 0.66770 0.59783 -0.06409 0.00299  0.05251  187 ALA A N   
1480 C CA  . ALA A 193 ? 0.53881 0.58054 0.53016 -0.05236 0.00017  0.05206  187 ALA A CA  
1481 C C   . ALA A 193 ? 0.33126 0.35505 0.32661 -0.04900 -0.00608 0.05591  187 ALA A C   
1482 O O   . ALA A 193 ? 0.52327 0.54370 0.51720 -0.05477 -0.00818 0.05831  187 ALA A O   
1483 C CB  . ALA A 193 ? 0.28827 0.33683 0.28716 -0.04150 0.00635  0.04233  187 ALA A CB  
1484 N N   . THR A 194 ? 0.44182 0.45491 0.44276 -0.03957 -0.00891 0.05555  188 THR A N   
1485 C CA  . THR A 194 ? 0.29902 0.29515 0.30456 -0.03552 -0.01547 0.05812  188 THR A CA  
1486 C C   . THR A 194 ? 0.31872 0.31346 0.32962 -0.03042 -0.01232 0.05185  188 THR A C   
1487 O O   . THR A 194 ? 0.25290 0.25512 0.26771 -0.02377 -0.00631 0.04493  188 THR A O   
1488 C CB  . THR A 194 ? 0.25589 0.24522 0.26743 -0.02690 -0.01861 0.05800  188 THR A CB  
1489 O OG1 . THR A 194 ? 0.21377 0.20583 0.21979 -0.03206 -0.02171 0.06374  188 THR A OG1 
1490 C CG2 . THR A 194 ? 0.18856 0.16109 0.20585 -0.02279 -0.02638 0.05995  188 THR A CG2 
1491 N N   . ARG A 195 ? 0.25686 0.24026 0.26725 -0.03391 -0.01750 0.05472  189 ARG A N   
1492 C CA  A ARG A 195 ? 0.25796 0.24080 0.27106 -0.03237 -0.01525 0.04969  189 ARG A CA  
1493 C CA  B ARG A 195 ? 0.25778 0.24096 0.27086 -0.03237 -0.01510 0.04962  189 ARG A CA  
1494 C C   . ARG A 195 ? 0.26622 0.24906 0.28625 -0.02078 -0.01130 0.04175  189 ARG A C   
1495 O O   . ARG A 195 ? 0.25036 0.24261 0.27139 -0.01858 -0.00583 0.03641  189 ARG A O   
1496 C CB  A ARG A 195 ? 0.31265 0.27880 0.32435 -0.03699 -0.02325 0.05408  189 ARG A CB  
1497 C CB  B ARG A 195 ? 0.31291 0.28011 0.32441 -0.03735 -0.02280 0.05391  189 ARG A CB  
1498 C CG  A ARG A 195 ? 0.28783 0.25176 0.30132 -0.03682 -0.02215 0.04929  189 ARG A CG  
1499 C CG  B ARG A 195 ? 0.28365 0.25136 0.29648 -0.03799 -0.02082 0.04913  189 ARG A CG  
1500 C CD  A ARG A 195 ? 0.29651 0.23982 0.30958 -0.03922 -0.03122 0.05247  189 ARG A CD  
1501 C CD  B ARG A 195 ? 0.31723 0.26756 0.32770 -0.04385 -0.02912 0.05335  189 ARG A CD  
1502 N NE  A ARG A 195 ? 0.28487 0.21851 0.29226 -0.04749 -0.03920 0.06241  189 ARG A NE  
1503 N NE  B ARG A 195 ? 0.36540 0.31373 0.36763 -0.05685 -0.03413 0.06311  189 ARG A NE  
1504 C CZ  A ARG A 195 ? 0.38106 0.29528 0.39077 -0.04429 -0.04869 0.06578  189 ARG A CZ  
1505 C CZ  B ARG A 195 ? 0.37557 0.30563 0.37488 -0.06013 -0.04407 0.07060  189 ARG A CZ  
1506 N NH1 A ARG A 195 ? 0.35599 0.25978 0.37461 -0.03269 -0.05054 0.05871  189 ARG A NH1 
1507 N NH1 B ARG A 195 ? 0.38375 0.29659 0.38983 -0.05009 -0.05005 0.06829  189 ARG A NH1 
1508 N NH2 A ARG A 195 ? 0.35855 0.26407 0.36159 -0.05304 -0.05692 0.07616  189 ARG A NH2 
1509 N NH2 B ARG A 195 ? 0.40502 0.33440 0.39446 -0.07409 -0.04855 0.08039  189 ARG A NH2 
1510 N N   . TRP A 196 ? 0.25063 0.22333 0.27565 -0.01364 -0.01455 0.04081  190 TRP A N   
1511 C CA  . TRP A 196 ? 0.22244 0.19515 0.25297 -0.00450 -0.01093 0.03317  190 TRP A CA  
1512 C C   . TRP A 196 ? 0.27262 0.25804 0.30287 -0.00119 -0.00402 0.02953  190 TRP A C   
1513 O O   . TRP A 196 ? 0.22951 0.21651 0.26154 0.00384  -0.00057 0.02391  190 TRP A O   
1514 C CB  . TRP A 196 ? 0.25206 0.21545 0.28953 0.00240  -0.01506 0.03177  190 TRP A CB  
1515 C CG  . TRP A 196 ? 0.27504 0.22257 0.31440 0.00138  -0.02321 0.03374  190 TRP A CG  
1516 C CD1 . TRP A 196 ? 0.29828 0.23834 0.33304 -0.00521 -0.02641 0.03590  190 TRP A CD1 
1517 C CD2 . TRP A 196 ? 0.31708 0.25358 0.36426 0.00741  -0.03001 0.03318  190 TRP A CD2 
1518 N NE1 . TRP A 196 ? 0.35914 0.28185 0.39719 -0.00406 -0.03528 0.03721  190 TRP A NE1 
1519 C CE2 . TRP A 196 ? 0.38759 0.30779 0.43399 0.00442  -0.03786 0.03521  190 TRP A CE2 
1520 C CE3 . TRP A 196 ? 0.33582 0.27512 0.39153 0.01508  -0.03074 0.03084  190 TRP A CE3 
1521 C CZ2 . TRP A 196 ? 0.37786 0.28283 0.43208 0.00992  -0.04708 0.03464  190 TRP A CZ2 
1522 C CZ3 . TRP A 196 ? 0.33263 0.25958 0.39729 0.02075  -0.03930 0.02989  190 TRP A CZ3 
1523 C CH2 . TRP A 196 ? 0.33513 0.24427 0.39917 0.01869  -0.04770 0.03162  190 TRP A CH2 
1524 N N   . TYR A 197 ? 0.17981 0.17353 0.20700 -0.00449 -0.00242 0.03252  191 TYR A N   
1525 C CA  . TYR A 197 ? 0.19297 0.19615 0.21992 -0.00127 0.00276  0.02913  191 TYR A CA  
1526 C C   . TYR A 197 ? 0.23440 0.24798 0.25825 -0.00504 0.00601  0.02769  191 TYR A C   
1527 O O   . TYR A 197 ? 0.23501 0.25584 0.25840 -0.00304 0.00920  0.02504  191 TYR A O   
1528 C CB  . TYR A 197 ? 0.19401 0.19842 0.22135 -0.00060 0.00172  0.03185  191 TYR A CB  
1529 C CG  . TYR A 197 ? 0.23291 0.22889 0.26606 0.00390  -0.00213 0.03228  191 TYR A CG  
1530 C CD1 . TYR A 197 ? 0.26984 0.26637 0.30779 0.01032  0.00055  0.02705  191 TYR A CD1 
1531 C CD2 . TYR A 197 ? 0.18171 0.16930 0.21586 0.00149  -0.00892 0.03747  191 TYR A CD2 
1532 C CE1 . TYR A 197 ? 0.19783 0.18956 0.24317 0.01506  -0.00241 0.02549  191 TYR A CE1 
1533 C CE2 . TYR A 197 ? 0.23197 0.21197 0.27385 0.00714  -0.01336 0.03651  191 TYR A CE2 
1534 C CZ  . TYR A 197 ? 0.18966 0.17308 0.23800 0.01435  -0.00956 0.02972  191 TYR A CZ  
1535 O OH  . TYR A 197 ? 0.22806 0.20694 0.28603 0.02057  -0.01337 0.02693  191 TYR A OH  
1536 N N   . ARG A 198 ? 0.21225 0.22683 0.23486 -0.01025 0.00491  0.02869  192 ARG A N   
1537 C CA  . ARG A 198 ? 0.19609 0.22339 0.21784 -0.01434 0.00780  0.02658  192 ARG A CA  
1538 C C   . ARG A 198 ? 0.22002 0.25033 0.24506 -0.00914 0.00975  0.02086  192 ARG A C   
1539 O O   . ARG A 198 ? 0.19589 0.21881 0.22169 -0.00754 0.00804  0.02004  192 ARG A O   
1540 C CB  . ARG A 198 ? 0.25065 0.27843 0.26964 -0.02377 0.00528  0.03077  192 ARG A CB  
1541 C CG  . ARG A 198 ? 0.39472 0.43607 0.41006 -0.03237 0.00729  0.03241  192 ARG A CG  
1542 C CD  . ARG A 198 ? 0.26526 0.30371 0.27633 -0.04327 0.00362  0.03821  192 ARG A CD  
1543 N NE  . ARG A 198 ? 0.25171 0.28306 0.25596 -0.05008 -0.00068 0.04614  192 ARG A NE  
1544 C CZ  . ARG A 198 ? 0.37532 0.39645 0.37439 -0.05908 -0.00677 0.05355  192 ARG A CZ  
1545 N NH1 . ARG A 198 ? 0.34962 0.36575 0.34969 -0.06237 -0.00896 0.05365  192 ARG A NH1 
1546 N NH2 . ARG A 198 ? 0.41580 0.43040 0.40796 -0.06540 -0.01171 0.06141  192 ARG A NH2 
1547 N N   . ALA A 199 ? 0.15039 0.19094 0.17719 -0.00653 0.01258  0.01666  193 ALA A N   
1548 C CA  . ALA A 199 ? 0.17842 0.22133 0.20833 -0.00161 0.01277  0.01194  193 ALA A CA  
1549 C C   . ALA A 199 ? 0.16466 0.21427 0.19707 -0.00584 0.01190  0.01088  193 ALA A C   
1550 O O   . ALA A 199 ? 0.16555 0.22327 0.19787 -0.01301 0.01259  0.01245  193 ALA A O   
1551 C CB  . ALA A 199 ? 0.18807 0.23889 0.22032 0.00269  0.01446  0.00747  193 ALA A CB  
1552 N N   . PRO A 200 ? 0.22184 0.26887 0.25579 -0.00262 0.01015  0.00848  194 PRO A N   
1553 C CA  . PRO A 200 ? 0.15333 0.20666 0.18987 -0.00719 0.00871  0.00758  194 PRO A CA  
1554 C C   . PRO A 200 ? 0.20418 0.27643 0.24667 -0.00996 0.01054  0.00424  194 PRO A C   
1555 O O   . PRO A 200 ? 0.15650 0.23671 0.20024 -0.01764 0.01052  0.00512  194 PRO A O   
1556 C CB  . PRO A 200 ? 0.16570 0.21355 0.20221 -0.00218 0.00615  0.00512  194 PRO A CB  
1557 C CG  . PRO A 200 ? 0.12644 0.17022 0.16172 0.00478  0.00658  0.00393  194 PRO A CG  
1558 C CD  . PRO A 200 ? 0.19527 0.23469 0.22785 0.00412  0.00906  0.00671  194 PRO A CD  
1559 N N   . GLU A 201 ? 0.14020 0.22045 0.18671 -0.00434 0.01210  -0.00016 195 GLU A N   
1560 C CA  . GLU A 201 ? 0.15927 0.26007 0.21353 -0.00574 0.01421  -0.00571 195 GLU A CA  
1561 C C   . GLU A 201 ? 0.14648 0.25755 0.19806 -0.01533 0.01802  -0.00378 195 GLU A C   
1562 O O   . GLU A 201 ? 0.15365 0.28463 0.21099 -0.01979 0.02055  -0.00813 195 GLU A O   
1563 C CB  . GLU A 201 ? 0.16620 0.27105 0.22570 0.00343  0.01421  -0.01192 195 GLU A CB  
1564 C CG  . GLU A 201 ? 0.20399 0.30169 0.25806 0.00521  0.01627  -0.01078 195 GLU A CG  
1565 C CD  . GLU A 201 ? 0.18370 0.26159 0.23169 0.01008  0.01355  -0.00680 195 GLU A CD  
1566 O OE1 . GLU A 201 ? 0.14999 0.21882 0.19593 0.01064  0.01080  -0.00412 195 GLU A OE1 
1567 O OE2 . GLU A 201 ? 0.19636 0.26887 0.24136 0.01270  0.01436  -0.00682 195 GLU A OE2 
1568 N N   . ILE A 202 ? 0.21037 0.30936 0.25341 -0.01905 0.01815  0.00256  196 ILE A N   
1569 C CA  . ILE A 202 ? 0.15656 0.26260 0.19453 -0.02992 0.02018  0.00638  196 ILE A CA  
1570 C C   . ILE A 202 ? 0.23429 0.34514 0.27194 -0.03989 0.01889  0.00930  196 ILE A C   
1571 O O   . ILE A 202 ? 0.23161 0.35928 0.26897 -0.04962 0.02166  0.00883  196 ILE A O   
1572 C CB  . ILE A 202 ? 0.16915 0.25859 0.19859 -0.03121 0.01835  0.01352  196 ILE A CB  
1573 C CG1 . ILE A 202 ? 0.22136 0.30887 0.25091 -0.02331 0.01998  0.01047  196 ILE A CG1 
1574 C CG2 . ILE A 202 ? 0.20906 0.30276 0.23130 -0.04388 0.01841  0.01945  196 ILE A CG2 
1575 C CD1 . ILE A 202 ? 0.19654 0.30196 0.22708 -0.02548 0.02435  0.00501  196 ILE A CD1 
1576 N N   . MET A 203 ? 0.18794 0.28484 0.22510 -0.03855 0.01480  0.01195  197 MET A N   
1577 C CA  . MET A 203 ? 0.28211 0.38152 0.31871 -0.04823 0.01273  0.01455  197 MET A CA  
1578 C C   . MET A 203 ? 0.30160 0.42202 0.34780 -0.04850 0.01446  0.00770  197 MET A C   
1579 O O   . MET A 203 ? 0.29674 0.42523 0.34341 -0.05858 0.01371  0.00914  197 MET A O   
1580 C CB  . MET A 203 ? 0.22370 0.30133 0.25691 -0.04644 0.00757  0.01809  197 MET A CB  
1581 C CG  . MET A 203 ? 0.27056 0.32739 0.29624 -0.04740 0.00429  0.02474  197 MET A CG  
1582 S SD  . MET A 203 ? 0.26903 0.32206 0.29317 -0.03948 0.00654  0.02505  197 MET A SD  
1583 C CE  . MET A 203 ? 0.28390 0.32418 0.31082 -0.02677 0.00565  0.02096  197 MET A CE  
1584 N N   . LEU A 204 ? 0.17961 0.30871 0.23392 -0.03788 0.01591  0.00039  198 LEU A N   
1585 C CA  . LEU A 204 ? 0.19655 0.34297 0.26206 -0.03516 0.01550  -0.00655 198 LEU A CA  
1586 C C   . LEU A 204 ? 0.17481 0.34804 0.24954 -0.03527 0.02036  -0.01447 198 LEU A C   
1587 O O   . LEU A 204 ? 0.22372 0.41831 0.30505 -0.04271 0.02219  -0.01774 198 LEU A O   
1588 C CB  . LEU A 204 ? 0.17525 0.31039 0.24390 -0.02262 0.01148  -0.00921 198 LEU A CB  
1589 C CG  . LEU A 204 ? 0.23205 0.34562 0.29333 -0.02241 0.00708  -0.00411 198 LEU A CG  
1590 C CD1 . LEU A 204 ? 0.19049 0.29352 0.25203 -0.01132 0.00391  -0.00615 198 LEU A CD1 
1591 C CD2 . LEU A 204 ? 0.16001 0.27911 0.22330 -0.03024 0.00451  -0.00359 198 LEU A CD2 
1592 N N   . ASN A 205 ? 0.16276 0.33648 0.23851 -0.02745 0.02263  -0.01850 199 ASN A N   
1593 C CA  . ASN A 205 ? 0.18259 0.38223 0.26933 -0.02500 0.02683  -0.02886 199 ASN A CA  
1594 C C   . ASN A 205 ? 0.26642 0.46474 0.35007 -0.02042 0.03009  -0.03202 199 ASN A C   
1595 O O   . ASN A 205 ? 0.12323 0.33853 0.21730 -0.01402 0.03229  -0.04259 199 ASN A O   
1596 C CB  . ASN A 205 ? 0.09381 0.30134 0.19503 -0.01384 0.02290  -0.03688 199 ASN A CB  
1597 C CG  . ASN A 205 ? 0.15548 0.34082 0.25495 -0.00089 0.01771  -0.03617 199 ASN A CG  
1598 O OD1 . ASN A 205 ? 0.12974 0.29411 0.21755 -0.00067 0.01739  -0.02950 199 ASN A OD1 
1599 N ND2 . ASN A 205 ? 0.13759 0.32793 0.24883 0.00945  0.01305  -0.04291 199 ASN A ND2 
1600 N N   . SER A 206 ? 0.14925 0.32885 0.22012 -0.02300 0.03004  -0.02422 200 SER A N   
1601 C CA  . SER A 206 ? 0.15284 0.32911 0.22060 -0.01805 0.03210  -0.02707 200 SER A CA  
1602 C C   . SER A 206 ? 0.25325 0.43089 0.30935 -0.02965 0.03556  -0.02142 200 SER A C   
1603 O O   . SER A 206 ? 0.15421 0.31975 0.20123 -0.03785 0.03342  -0.01137 200 SER A O   
1604 C CB  . SER A 206 ? 0.19610 0.34716 0.26013 -0.00821 0.02748  -0.02337 200 SER A CB  
1605 O OG  . SER A 206 ? 0.18894 0.33490 0.24807 -0.00571 0.02910  -0.02440 200 SER A OG  
1606 N N   . LYS A 207 ? 0.20759 0.39933 0.26375 -0.03027 0.04017  -0.02819 201 LYS A N   
1607 C CA  . LYS A 207 ? 0.20909 0.40141 0.25263 -0.04101 0.04276  -0.02286 201 LYS A CA  
1608 C C   . LYS A 207 ? 0.22453 0.39394 0.25980 -0.03628 0.03956  -0.01694 201 LYS A C   
1609 O O   . LYS A 207 ? 0.28421 0.45129 0.30863 -0.04458 0.04011  -0.01130 201 LYS A O   
1610 C CB  . LYS A 207 ? 0.21699 0.42761 0.26021 -0.04338 0.04704  -0.03260 201 LYS A CB  
1611 C CG  . LYS A 207 ? 0.25936 0.48810 0.30964 -0.04557 0.04835  -0.04012 201 LYS A CG  
1612 C CD  . LYS A 207 ? 0.27754 0.52125 0.32739 -0.04588 0.05173  -0.05093 201 LYS A CD  
1613 C CE  . LYS A 207 ? 0.36268 0.62633 0.41312 -0.05484 0.05388  -0.05540 201 LYS A CE  
1614 N NZ  . LYS A 207 ? 0.28234 0.56226 0.34669 -0.04559 0.05527  -0.07044 201 LYS A NZ  
1615 N N   . GLY A 208 ? 0.21235 0.36588 0.25217 -0.02408 0.03593  -0.01791 202 GLY A N   
1616 C CA  . GLY A 208 ? 0.24662 0.38136 0.27989 -0.01998 0.03339  -0.01329 202 GLY A CA  
1617 C C   . GLY A 208 ? 0.24828 0.38843 0.28086 -0.01660 0.03586  -0.02051 202 GLY A C   
1618 O O   . GLY A 208 ? 0.24008 0.37098 0.26448 -0.01874 0.03498  -0.01594 202 GLY A O   
1619 N N   . TYR A 209 ? 0.16189 0.31686 0.20359 -0.01100 0.03838  -0.03234 203 TYR A N   
1620 C CA  . TYR A 209 ? 0.17282 0.33330 0.21483 -0.00715 0.04057  -0.04145 203 TYR A CA  
1621 C C   . TYR A 209 ? 0.21293 0.35872 0.26075 0.00591  0.03613  -0.04599 203 TYR A C   
1622 O O   . TYR A 209 ? 0.20804 0.35794 0.25880 0.01101  0.03695  -0.05581 203 TYR A O   
1623 C CB  . TYR A 209 ? 0.25932 0.44778 0.30815 -0.00966 0.04642  -0.05378 203 TYR A CB  
1624 C CG  . TYR A 209 ? 0.22397 0.42475 0.26350 -0.02457 0.04972  -0.04925 203 TYR A CG  
1625 C CD1 . TYR A 209 ? 0.28712 0.47996 0.31434 -0.03517 0.04917  -0.03627 203 TYR A CD1 
1626 C CD2 . TYR A 209 ? 0.34005 0.55834 0.38251 -0.02816 0.05194  -0.05760 203 TYR A CD2 
1627 C CE1 . TYR A 209 ? 0.18923 0.38886 0.20642 -0.04890 0.04977  -0.03113 203 TYR A CE1 
1628 C CE2 . TYR A 209 ? 0.39874 0.62666 0.43128 -0.04237 0.05381  -0.05323 203 TYR A CE2 
1629 C CZ  . TYR A 209 ? 0.38380 0.60127 0.40323 -0.05276 0.05227  -0.03968 203 TYR A CZ  
1630 O OH  . TYR A 209 ? 0.39942 0.62401 0.40802 -0.06715 0.05241  -0.03468 203 TYR A OH  
1631 N N   . THR A 210 ? 0.19701 0.32526 0.24559 0.01069  0.03115  -0.03923 204 THR A N   
1632 C CA  . THR A 210 ? 0.20318 0.31594 0.25501 0.02102  0.02604  -0.04163 204 THR A CA  
1633 C C   . THR A 210 ? 0.20450 0.29657 0.24709 0.01983  0.02324  -0.03158 204 THR A C   
1634 O O   . THR A 210 ? 0.17887 0.26712 0.21597 0.01374  0.02390  -0.02279 204 THR A O   
1635 C CB  . THR A 210 ? 0.20330 0.31542 0.26460 0.02782  0.02200  -0.04371 204 THR A CB  
1636 O OG1 . THR A 210 ? 0.32187 0.42418 0.37869 0.02426  0.02033  -0.03355 204 THR A OG1 
1637 C CG2 . THR A 210 ? 0.25593 0.39227 0.32819 0.02778  0.02512  -0.05300 204 THR A CG2 
1638 N N   . LYS A 211 ? 0.15516 0.23396 0.19677 0.02572  0.01963  -0.03338 205 LYS A N   
1639 C CA  . LYS A 211 ? 0.16042 0.22279 0.19394 0.02384  0.01764  -0.02512 205 LYS A CA  
1640 C C   . LYS A 211 ? 0.22539 0.27875 0.25759 0.02329  0.01570  -0.01704 205 LYS A C   
1641 O O   . LYS A 211 ? 0.14913 0.19436 0.17580 0.01999  0.01571  -0.01007 205 LYS A O   
1642 C CB  . LYS A 211 ? 0.26091 0.31096 0.29358 0.02927  0.01358  -0.02888 205 LYS A CB  
1643 C CG  . LYS A 211 ? 0.15604 0.21294 0.18812 0.02898  0.01561  -0.03696 205 LYS A CG  
1644 C CD  . LYS A 211 ? 0.18879 0.23235 0.22122 0.03506  0.01046  -0.04232 205 LYS A CD  
1645 C CE  . LYS A 211 ? 0.19712 0.24847 0.22905 0.03478  0.01283  -0.05206 205 LYS A CE  
1646 N NZ  . LYS A 211 ? 0.22171 0.25762 0.25338 0.04029  0.00698  -0.05755 205 LYS A NZ  
1647 N N   . SER A 212 ? 0.16037 0.21643 0.19811 0.02637  0.01406  -0.01857 206 SER A N   
1648 C CA  . SER A 212 ? 0.12619 0.17356 0.16187 0.02585  0.01205  -0.01217 206 SER A CA  
1649 C C   . SER A 212 ? 0.12672 0.17667 0.15944 0.01936  0.01499  -0.00619 206 SER A C   
1650 O O   . SER A 212 ? 0.15957 0.20095 0.18956 0.01870  0.01384  -0.00131 206 SER A O   
1651 C CB  . SER A 212 ? 0.22322 0.27362 0.26541 0.03029  0.00880  -0.01555 206 SER A CB  
1652 O OG  . SER A 212 ? 0.18465 0.25256 0.23434 0.02966  0.01136  -0.02135 206 SER A OG  
1653 N N   . ILE A 213 ? 0.10852 0.16957 0.14126 0.01418  0.01825  -0.00658 207 ILE A N   
1654 C CA  . ILE A 213 ? 0.12893 0.18878 0.15835 0.00795  0.01903  0.00007  207 ILE A CA  
1655 C C   . ILE A 213 ? 0.14809 0.19731 0.17267 0.00718  0.01818  0.00540  207 ILE A C   
1656 O O   . ILE A 213 ? 0.15266 0.19557 0.17606 0.00532  0.01706  0.01047  207 ILE A O   
1657 C CB  . ILE A 213 ? 0.21496 0.28837 0.24373 0.00056  0.02172  -0.00010 207 ILE A CB  
1658 C CG1 . ILE A 213 ? 0.28860 0.37179 0.31614 -0.00055 0.02436  -0.00519 207 ILE A CG1 
1659 C CG2 . ILE A 213 ? 0.30900 0.39321 0.34332 -0.00069 0.02237  -0.00329 207 ILE A CG2 
1660 C CD1 . ILE A 213 ? 0.29637 0.37355 0.31694 -0.00369 0.02399  -0.00077 207 ILE A CD1 
1661 N N   . ASP A 214 ? 0.11056 0.15802 0.13319 0.00881  0.01831  0.00364  208 ASP A N   
1662 C CA  . ASP A 214 ? 0.13348 0.17308 0.15287 0.00796  0.01735  0.00817  208 ASP A CA  
1663 C C   . ASP A 214 ? 0.16275 0.19259 0.18253 0.01157  0.01593  0.00961  208 ASP A C   
1664 O O   . ASP A 214 ? 0.15149 0.17706 0.17110 0.01071  0.01554  0.01344  208 ASP A O   
1665 C CB  . ASP A 214 ? 0.09835 0.13927 0.11508 0.00768  0.01766  0.00556  208 ASP A CB  
1666 C CG  . ASP A 214 ? 0.13551 0.18528 0.14904 0.00177  0.01900  0.00628  208 ASP A CG  
1667 O OD1 . ASP A 214 ? 0.16367 0.21508 0.17604 -0.00286 0.01848  0.01153  208 ASP A OD1 
1668 O OD2 . ASP A 214 ? 0.16944 0.22374 0.18082 0.00125  0.02003  0.00158  208 ASP A OD2 
1669 N N   . ILE A 215 ? 0.16974 0.19656 0.19012 0.01542  0.01477  0.00628  209 ILE A N   
1670 C CA  . ILE A 215 ? 0.21569 0.23375 0.23405 0.01708  0.01333  0.00799  209 ILE A CA  
1671 C C   . ILE A 215 ? 0.17330 0.19069 0.19259 0.01620  0.01389  0.01023  209 ILE A C   
1672 O O   . ILE A 215 ? 0.13710 0.15025 0.15489 0.01574  0.01434  0.01208  209 ILE A O   
1673 C CB  . ILE A 215 ? 0.22560 0.23914 0.24337 0.02071  0.01023  0.00488  209 ILE A CB  
1674 C CG1 . ILE A 215 ? 0.18653 0.19702 0.20287 0.02183  0.00875  0.00231  209 ILE A CG1 
1675 C CG2 . ILE A 215 ? 0.12361 0.12889 0.13721 0.02050  0.00845  0.00754  209 ILE A CG2 
1676 C CD1 . ILE A 215 ? 0.21696 0.22116 0.22849 0.01877  0.00887  0.00582  209 ILE A CD1 
1677 N N   . TRP A 216 ? 0.20753 0.22990 0.22951 0.01557  0.01399  0.00935  210 TRP A N   
1678 C CA  . TRP A 216 ? 0.18565 0.20603 0.20824 0.01429  0.01393  0.01104  210 TRP A CA  
1679 C C   . TRP A 216 ? 0.16522 0.18314 0.18835 0.01254  0.01443  0.01415  210 TRP A C   
1680 O O   . TRP A 216 ? 0.17876 0.19218 0.20230 0.01337  0.01439  0.01432  210 TRP A O   
1681 C CB  . TRP A 216 ? 0.16757 0.19432 0.19284 0.01228  0.01363  0.01005  210 TRP A CB  
1682 C CG  . TRP A 216 ? 0.19212 0.21495 0.21746 0.01042  0.01280  0.01158  210 TRP A CG  
1683 C CD1 . TRP A 216 ? 0.16550 0.18550 0.19116 0.00727  0.01223  0.01461  210 TRP A CD1 
1684 C CD2 . TRP A 216 ? 0.14317 0.16312 0.16785 0.01147  0.01150  0.00992  210 TRP A CD2 
1685 N NE1 . TRP A 216 ? 0.20810 0.22300 0.23386 0.00675  0.01084  0.01417  210 TRP A NE1 
1686 C CE2 . TRP A 216 ? 0.15928 0.17490 0.18407 0.00897  0.01081  0.01115  210 TRP A CE2 
1687 C CE3 . TRP A 216 ? 0.14971 0.16939 0.17324 0.01406  0.00993  0.00767  210 TRP A CE3 
1688 C CZ2 . TRP A 216 ? 0.17473 0.18675 0.19824 0.00877  0.00952  0.00936  210 TRP A CZ2 
1689 C CZ3 . TRP A 216 ? 0.13699 0.15366 0.15872 0.01341  0.00834  0.00685  210 TRP A CZ3 
1690 C CH2 . TRP A 216 ? 0.18137 0.19475 0.20297 0.01069  0.00861  0.00727  210 TRP A CH2 
1691 N N   . SER A 217 ? 0.17823 0.19954 0.20166 0.01019  0.01446  0.01612  211 SER A N   
1692 C CA  . SER A 217 ? 0.17450 0.19299 0.19935 0.00898  0.01319  0.01958  211 SER A CA  
1693 C C   . SER A 217 ? 0.13651 0.15235 0.16263 0.01179  0.01383  0.01894  211 SER A C   
1694 O O   . SER A 217 ? 0.18058 0.19375 0.21032 0.01321  0.01305  0.01922  211 SER A O   
1695 C CB  . SER A 217 ? 0.17238 0.19527 0.19554 0.00503  0.01237  0.02234  211 SER A CB  
1696 O OG  . SER A 217 ? 0.19076 0.21829 0.21228 0.00066  0.01232  0.02300  211 SER A OG  
1697 N N   . VAL A 218 ? 0.12244 0.13934 0.14604 0.01240  0.01504  0.01752  212 VAL A N   
1698 C CA  . VAL A 218 ? 0.09063 0.10654 0.11454 0.01319  0.01595  0.01713  212 VAL A CA  
1699 C C   . VAL A 218 ? 0.16735 0.18101 0.19101 0.01447  0.01721  0.01507  212 VAL A C   
1700 O O   . VAL A 218 ? 0.14906 0.16443 0.17569 0.01499  0.01846  0.01403  212 VAL A O   
1701 C CB  . VAL A 218 ? 0.12757 0.14283 0.14726 0.01230  0.01602  0.01646  212 VAL A CB  
1702 C CG1 . VAL A 218 ? 0.19086 0.20580 0.20982 0.01110  0.01700  0.01665  212 VAL A CG1 
1703 C CG2 . VAL A 218 ? 0.13003 0.14846 0.14941 0.01067  0.01515  0.01725  212 VAL A CG2 
1704 N N   . GLY A 219 ? 0.11426 0.12549 0.13472 0.01486  0.01687  0.01381  213 GLY A N   
1705 C CA  . GLY A 219 ? 0.15883 0.16807 0.17761 0.01519  0.01772  0.01179  213 GLY A CA  
1706 C C   . GLY A 219 ? 0.16138 0.17072 0.18531 0.01637  0.01805  0.01043  213 GLY A C   
1707 O O   . GLY A 219 ? 0.15722 0.16761 0.18214 0.01699  0.01992  0.00750  213 GLY A O   
1708 N N   . CYS A 220 ? 0.13713 0.14541 0.16431 0.01631  0.01594  0.01219  214 CYS A N   
1709 C CA  . CYS A 220 ? 0.14311 0.14836 0.17542 0.01757  0.01437  0.01145  214 CYS A CA  
1710 C C   . CYS A 220 ? 0.14356 0.15107 0.18198 0.01988  0.01444  0.01078  214 CYS A C   
1711 O O   . CYS A 220 ? 0.14370 0.15002 0.18752 0.02275  0.01414  0.00714  214 CYS A O   
1712 C CB  . CYS A 220 ? 0.09981 0.10251 0.13271 0.01513  0.01104  0.01515  214 CYS A CB  
1713 S SG  . CYS A 220 ? 0.16613 0.16921 0.19483 0.01204  0.01078  0.01489  214 CYS A SG  
1714 N N   . ILE A 221 ? 0.15207 0.16355 0.19057 0.01891  0.01460  0.01341  215 ILE A N   
1715 C CA  . ILE A 221 ? 0.09514 0.11072 0.14060 0.02083  0.01412  0.01292  215 ILE A CA  
1716 C C   . ILE A 221 ? 0.10282 0.12422 0.14944 0.02166  0.01836  0.00798  215 ILE A C   
1717 O O   . ILE A 221 ? 0.13703 0.16292 0.19205 0.02472  0.01875  0.00410  215 ILE A O   
1718 C CB  . ILE A 221 ? 0.12003 0.13849 0.16415 0.01844  0.01276  0.01718  215 ILE A CB  
1719 C CG1 . ILE A 221 ? 0.15888 0.17349 0.20150 0.01637  0.00867  0.02183  215 ILE A CG1 
1720 C CG2 . ILE A 221 ? 0.12194 0.14668 0.17353 0.01991  0.01228  0.01648  215 ILE A CG2 
1721 C CD1 . ILE A 221 ? 0.20009 0.21794 0.23785 0.01274  0.00837  0.02491  215 ILE A CD1 
1722 N N   . LEU A 222 ? 0.19859 0.22042 0.23690 0.01864  0.02122  0.00780  216 LEU A N   
1723 C CA  . LEU A 222 ? 0.22890 0.25628 0.26533 0.01704  0.02525  0.00398  216 LEU A CA  
1724 C C   . LEU A 222 ? 0.22334 0.25158 0.26254 0.01939  0.02697  -0.00190 216 LEU A C   
1725 O O   . LEU A 222 ? 0.17334 0.20999 0.21795 0.02027  0.03009  -0.00724 216 LEU A O   
1726 C CB  . LEU A 222 ? 0.20008 0.22408 0.22518 0.01271  0.02593  0.00620  216 LEU A CB  
1727 C CG  . LEU A 222 ? 0.20572 0.23406 0.22512 0.00875  0.02956  0.00342  216 LEU A CG  
1728 C CD1 . LEU A 222 ? 0.15706 0.19618 0.18175 0.00674  0.03262  0.00158  216 LEU A CD1 
1729 C CD2 . LEU A 222 ? 0.16530 0.18674 0.17250 0.00431  0.02786  0.00700  216 LEU A CD2 
1730 N N   . ALA A 223 ? 0.22626 0.24701 0.26216 0.02017  0.02513  -0.00186 217 ALA A N   
1731 C CA  . ALA A 223 ? 0.20280 0.22273 0.24073 0.02226  0.02614  -0.00802 217 ALA A CA  
1732 C C   . ALA A 223 ? 0.18404 0.20552 0.23468 0.02760  0.02457  -0.01196 217 ALA A C   
1733 O O   . ALA A 223 ? 0.20301 0.22959 0.25869 0.03013  0.02716  -0.01981 217 ALA A O   
1734 C CB  . ALA A 223 ? 0.25572 0.26688 0.28862 0.02159  0.02332  -0.00650 217 ALA A CB  
1735 N N   . GLU A 224 ? 0.19690 0.21440 0.25296 0.02933  0.01989  -0.00698 218 GLU A N   
1736 C CA  . GLU A 224 ? 0.20080 0.21730 0.26925 0.03477  0.01604  -0.00952 218 GLU A CA  
1737 C C   . GLU A 224 ? 0.17670 0.20604 0.25443 0.03725  0.01874  -0.01392 218 GLU A C   
1738 O O   . GLU A 224 ? 0.18178 0.21418 0.27156 0.04311  0.01743  -0.02057 218 GLU A O   
1739 C CB  . GLU A 224 ? 0.24234 0.25063 0.31156 0.03411  0.00942  -0.00152 218 GLU A CB  
1740 C CG  . GLU A 224 ? 0.29905 0.30183 0.37976 0.03930  0.00258  -0.00214 218 GLU A CG  
1741 C CD  . GLU A 224 ? 0.26334 0.25485 0.34031 0.03607  -0.00456 0.00661  218 GLU A CD  
1742 O OE1 . GLU A 224 ? 0.24483 0.23465 0.31125 0.03021  -0.00297 0.01131  218 GLU A OE1 
1743 O OE2 . GLU A 224 ? 0.19606 0.18088 0.28065 0.03905  -0.01212 0.00867  218 GLU A OE2 
1744 N N   . MET A 225 ? 0.17250 0.20986 0.24560 0.03290  0.02219  -0.01098 219 MET A N   
1745 C CA  . MET A 225 ? 0.18382 0.23581 0.26514 0.03353  0.02560  -0.01555 219 MET A CA  
1746 C C   . MET A 225 ? 0.26259 0.32405 0.34371 0.03299  0.03214  -0.02478 219 MET A C   
1747 O O   . MET A 225 ? 0.22115 0.29671 0.31326 0.03538  0.03505  -0.03197 219 MET A O   
1748 C CB  . MET A 225 ? 0.14256 0.19929 0.21750 0.02753  0.02715  -0.00976 219 MET A CB  
1749 C CG  . MET A 225 ? 0.19506 0.24546 0.26962 0.02715  0.02157  -0.00186 219 MET A CG  
1750 S SD  . MET A 225 ? 0.21056 0.26834 0.28067 0.02086  0.02322  0.00221  219 MET A SD  
1751 C CE  . MET A 225 ? 0.24175 0.28922 0.29457 0.01544  0.02486  0.00610  219 MET A CE  
1752 N N   . LEU A 226 ? 0.15234 0.20786 0.22124 0.02947  0.03453  -0.02515 220 LEU A N   
1753 C CA  . LEU A 226 ? 0.22157 0.28648 0.28727 0.02716  0.04088  -0.03354 220 LEU A CA  
1754 C C   . LEU A 226 ? 0.28705 0.35377 0.36408 0.03438  0.04087  -0.04414 220 LEU A C   
1755 O O   . LEU A 226 ? 0.25698 0.33726 0.33716 0.03412  0.04678  -0.05406 220 LEU A O   
1756 C CB  . LEU A 226 ? 0.16569 0.22295 0.21414 0.02086  0.04206  -0.03012 220 LEU A CB  
1757 C CG  . LEU A 226 ? 0.23756 0.29287 0.27399 0.01362  0.04205  -0.02158 220 LEU A CG  
1758 C CD1 . LEU A 226 ? 0.28672 0.33099 0.30928 0.01015  0.04007  -0.01765 220 LEU A CD1 
1759 C CD2 . LEU A 226 ? 0.18366 0.25308 0.21726 0.00717  0.04761  -0.02398 220 LEU A CD2 
1760 N N   . SER A 227 ? 0.20388 0.25723 0.28688 0.04035  0.03415  -0.04269 221 SER A N   
1761 C CA  . SER A 227 ? 0.27828 0.32851 0.37057 0.04724  0.03252  -0.05257 221 SER A CA  
1762 C C   . SER A 227 ? 0.21630 0.25872 0.32388 0.05552  0.02417  -0.05207 221 SER A C   
1763 O O   . SER A 227 ? 0.28831 0.32601 0.40528 0.06229  0.02127  -0.06068 221 SER A O   
1764 C CB  . SER A 227 ? 0.28872 0.32572 0.36924 0.04469  0.03144  -0.05225 221 SER A CB  
1765 O OG  . SER A 227 ? 0.23918 0.26150 0.31467 0.04307  0.02510  -0.04144 221 SER A OG  
1766 N N   . ASN A 228 ? 0.17908 0.21902 0.28885 0.05494  0.01949  -0.04240 222 ASN A N   
1767 C CA  . ASN A 228 ? 0.18090 0.21219 0.30305 0.06131  0.01001  -0.03958 222 ASN A CA  
1768 C C   . ASN A 228 ? 0.31171 0.32228 0.43017 0.06222  0.00257  -0.03624 222 ASN A C   
1769 O O   . ASN A 228 ? 0.34216 0.34305 0.47158 0.06845  -0.00604 -0.03707 222 ASN A O   
1770 C CB  . ASN A 228 ? 0.25536 0.29794 0.39755 0.07045  0.00909  -0.05071 222 ASN A CB  
1771 C CG  . ASN A 228 ? 0.28374 0.34831 0.43153 0.06872  0.01530  -0.05299 222 ASN A CG  
1772 O OD1 . ASN A 228 ? 0.27164 0.35014 0.41390 0.06415  0.02476  -0.05865 222 ASN A OD1 
1773 N ND2 . ASN A 228 ? 0.19842 0.26625 0.35649 0.07136  0.00949  -0.04817 222 ASN A ND2 
1774 N N   . ARG A 229 ? 0.23631 0.23965 0.33983 0.05577  0.00493  -0.03229 223 ARG A N   
1775 C CA  . ARG A 229 ? 0.25015 0.23531 0.34881 0.05430  -0.00187 -0.02772 223 ARG A CA  
1776 C C   . ARG A 229 ? 0.25627 0.23922 0.33964 0.04561  0.00029  -0.01857 223 ARG A C   
1777 O O   . ARG A 229 ? 0.21332 0.20596 0.28902 0.04195  0.00736  -0.01910 223 ARG A O   
1778 C CB  . ARG A 229 ? 0.28360 0.26214 0.38399 0.05766  -0.00186 -0.03800 223 ARG A CB  
1779 C CG  . ARG A 229 ? 0.39347 0.37380 0.48025 0.05174  0.00457  -0.04011 223 ARG A CG  
1780 C CD  . ARG A 229 ? 0.47868 0.44871 0.56661 0.05441  0.00223  -0.04909 223 ARG A CD  
1781 N NE  . ARG A 229 ? 0.49546 0.45760 0.57000 0.04736  0.00213  -0.04525 223 ARG A NE  
1782 C CZ  . ARG A 229 ? 0.44635 0.39542 0.51648 0.04303  -0.00438 -0.03624 223 ARG A CZ  
1783 N NH1 . ARG A 229 ? 0.44049 0.38137 0.51623 0.04403  -0.01159 -0.02896 223 ARG A NH1 
1784 N NH2 . ARG A 229 ? 0.38338 0.32845 0.44291 0.03674  -0.00390 -0.03436 223 ARG A NH2 
1785 N N   . PRO A 230 ? 0.20849 0.17940 0.28752 0.04190  -0.00611 -0.01016 224 PRO A N   
1786 C CA  . PRO A 230 ? 0.23049 0.20187 0.29710 0.03418  -0.00387 -0.00305 224 PRO A CA  
1787 C C   . PRO A 230 ? 0.24413 0.21557 0.30348 0.03194  0.00036  -0.00780 224 PRO A C   
1788 O O   . PRO A 230 ? 0.26113 0.22494 0.32220 0.03378  -0.00166 -0.01342 224 PRO A O   
1789 C CB  . PRO A 230 ? 0.28402 0.24331 0.34882 0.03023  -0.01192 0.00525  224 PRO A CB  
1790 C CG  . PRO A 230 ? 0.33449 0.28184 0.40874 0.03580  -0.01923 0.00162  224 PRO A CG  
1791 C CD  . PRO A 230 ? 0.28238 0.23946 0.36776 0.04400  -0.01620 -0.00647 224 PRO A CD  
1792 N N   . ILE A 231 ? 0.17759 0.15696 0.22877 0.02800  0.00542  -0.00563 225 ILE A N   
1793 C CA  . ILE A 231 ? 0.21464 0.19505 0.25856 0.02575  0.00870  -0.00957 225 ILE A CA  
1794 C C   . ILE A 231 ? 0.23131 0.20379 0.27084 0.02137  0.00478  -0.00631 225 ILE A C   
1795 O O   . ILE A 231 ? 0.24866 0.21762 0.28495 0.02038  0.00477  -0.01085 225 ILE A O   
1796 C CB  A ILE A 231 ? 0.25077 0.24071 0.28796 0.02338  0.01368  -0.00801 225 ILE A CB  
1797 C CB  B ILE A 231 ? 0.25096 0.24092 0.28815 0.02338  0.01369  -0.00802 225 ILE A CB  
1798 C CG1 A ILE A 231 ? 0.22862 0.21884 0.25747 0.02061  0.01549  -0.01096 225 ILE A CG1 
1799 C CG1 B ILE A 231 ? 0.22826 0.21857 0.25712 0.02065  0.01555  -0.01104 225 ILE A CG1 
1800 C CG2 A ILE A 231 ? 0.20473 0.19640 0.23984 0.02065  0.01239  -0.00032 225 ILE A CG2 
1801 C CG2 B ILE A 231 ? 0.20129 0.19295 0.23634 0.02062  0.01239  -0.00032 225 ILE A CG2 
1802 C CD1 A ILE A 231 ? 0.22554 0.22210 0.24715 0.01816  0.01838  -0.00877 225 ILE A CD1 
1803 C CD1 B ILE A 231 ? 0.23738 0.22990 0.26574 0.02223  0.01879  -0.01969 225 ILE A CD1 
1804 N N   . PHE A 232 ? 0.21704 0.18754 0.25610 0.01783  0.00146  0.00120  226 PHE A N   
1805 C CA  . PHE A 232 ? 0.22392 0.18966 0.25909 0.01198  -0.00190 0.00479  226 PHE A CA  
1806 C C   . PHE A 232 ? 0.26491 0.22061 0.30290 0.00975  -0.00851 0.00995  226 PHE A C   
1807 O O   . PHE A 232 ? 0.26878 0.22704 0.30441 0.00470  -0.00999 0.01697  226 PHE A O   
1808 C CB  . PHE A 232 ? 0.21192 0.18762 0.24249 0.00779  0.00068  0.00883  226 PHE A CB  
1809 C CG  . PHE A 232 ? 0.22213 0.20547 0.24951 0.00986  0.00519  0.00533  226 PHE A CG  
1810 C CD1 . PHE A 232 ? 0.19497 0.17667 0.21921 0.01018  0.00586  0.00034  226 PHE A CD1 
1811 C CD2 . PHE A 232 ? 0.18758 0.17863 0.21406 0.01079  0.00788  0.00733  226 PHE A CD2 
1812 C CE1 . PHE A 232 ? 0.24284 0.23020 0.26247 0.01092  0.00865  -0.00152 226 PHE A CE1 
1813 C CE2 . PHE A 232 ? 0.21568 0.21104 0.23835 0.01206  0.01036  0.00517  226 PHE A CE2 
1814 C CZ  . PHE A 232 ? 0.20798 0.20140 0.22688 0.01186  0.01048  0.00129  226 PHE A CZ  
1815 N N   . PRO A 233 ? 0.29456 0.23828 0.33718 0.01306  -0.01315 0.00644  227 PRO A N   
1816 C CA  . PRO A 233 ? 0.33045 0.26162 0.37566 0.01119  -0.02152 0.01228  227 PRO A CA  
1817 C C   . PRO A 233 ? 0.29499 0.21708 0.33419 0.00223  -0.02659 0.01729  227 PRO A C   
1818 O O   . PRO A 233 ? 0.33628 0.24304 0.37673 0.00190  -0.03308 0.01573  227 PRO A O   
1819 C CB  . PRO A 233 ? 0.40455 0.32689 0.45895 0.02001  -0.02472 0.00464  227 PRO A CB  
1820 C CG  . PRO A 233 ? 0.32415 0.24942 0.37680 0.02205  -0.01953 -0.00491 227 PRO A CG  
1821 C CD  . PRO A 233 ? 0.32460 0.26535 0.37036 0.01878  -0.01157 -0.00351 227 PRO A CD  
1822 N N   . GLY A 234 ? 0.30788 0.23998 0.34079 -0.00556 -0.02379 0.02291  228 GLY A N   
1823 C CA  . GLY A 234 ? 0.30766 0.23488 0.33492 -0.01587 -0.02789 0.02807  228 GLY A CA  
1824 C C   . GLY A 234 ? 0.45626 0.36750 0.48252 -0.02050 -0.03750 0.03558  228 GLY A C   
1825 O O   . GLY A 234 ? 0.36474 0.27549 0.39215 -0.01931 -0.03987 0.04045  228 GLY A O   
1826 N N   . LYS A 235 ? 0.37491 0.27186 0.39846 -0.02631 -0.04402 0.03688  229 LYS A N   
1827 C CA  . LYS A 235 ? 0.49483 0.37156 0.51698 -0.03064 -0.05542 0.04400  229 LYS A CA  
1828 C C   . LYS A 235 ? 0.46474 0.34347 0.47699 -0.04606 -0.05853 0.05550  229 LYS A C   
1829 O O   . LYS A 235 ? 0.46504 0.32693 0.47357 -0.05211 -0.06886 0.06388  229 LYS A O   
1830 C CB  . LYS A 235 ? 0.44077 0.29768 0.46561 -0.02786 -0.06201 0.03816  229 LYS A CB  
1831 C CG  . LYS A 235 ? 0.53440 0.38243 0.57015 -0.01323 -0.06439 0.02983  229 LYS A CG  
1832 C CD  . LYS A 235 ? 0.55536 0.39190 0.59549 -0.00691 -0.06596 0.01832  229 LYS A CD  
1833 C CE  . LYS A 235 ? 0.59292 0.40330 0.63101 -0.01204 -0.07857 0.02105  229 LYS A CE  
1834 N NZ  . LYS A 235 ? 0.57188 0.38349 0.59962 -0.02540 -0.07773 0.02510  229 LYS A NZ  
1835 N N   . HIS A 236 ? 0.38766 0.28728 0.39581 -0.05255 -0.05009 0.05583  230 HIS A N   
1836 C CA  . HIS A 236 ? 0.43381 0.34323 0.43331 -0.06716 -0.04995 0.06474  230 HIS A CA  
1837 C C   . HIS A 236 ? 0.35386 0.29012 0.35448 -0.06738 -0.03851 0.05973  230 HIS A C   
1838 O O   . HIS A 236 ? 0.41529 0.35826 0.42192 -0.05764 -0.03279 0.05104  230 HIS A O   
1839 C CB  . HIS A 236 ? 0.49019 0.38649 0.48267 -0.08087 -0.05779 0.07087  230 HIS A CB  
1840 C CG  . HIS A 236 ? 0.40169 0.29528 0.39694 -0.07966 -0.05676 0.06355  230 HIS A CG  
1841 N ND1 . HIS A 236 ? 0.30880 0.22312 0.30428 -0.08393 -0.04890 0.05951  230 HIS A ND1 
1842 C CD2 . HIS A 236 ? 0.32279 0.19562 0.32090 -0.07460 -0.06308 0.05897  230 HIS A CD2 
1843 C CE1 . HIS A 236 ? 0.36059 0.26691 0.35804 -0.08221 -0.05063 0.05364  230 HIS A CE1 
1844 N NE2 . HIS A 236 ? 0.32379 0.20493 0.32234 -0.07676 -0.05880 0.05283  230 HIS A NE2 
1845 N N   . TYR A 237 ? 0.40674 0.35841 0.40142 -0.07874 -0.03568 0.06503  231 TYR A N   
1846 C CA  . TYR A 237 ? 0.42009 0.39822 0.41734 -0.07819 -0.02550 0.05961  231 TYR A CA  
1847 C C   . TYR A 237 ? 0.35567 0.34090 0.35889 -0.07350 -0.02156 0.05135  231 TYR A C   
1848 O O   . TYR A 237 ? 0.35174 0.34876 0.36067 -0.06391 -0.01532 0.04432  231 TYR A O   
1849 C CB  . TYR A 237 ? 0.45240 0.44660 0.44258 -0.09385 -0.02363 0.06510  231 TYR A CB  
1850 C CG  . TYR A 237 ? 0.44139 0.46419 0.43616 -0.09260 -0.01355 0.05794  231 TYR A CG  
1851 C CD1 . TYR A 237 ? 0.43891 0.47337 0.43454 -0.08729 -0.00832 0.05555  231 TYR A CD1 
1852 C CD2 . TYR A 237 ? 0.40209 0.44000 0.40120 -0.09635 -0.01002 0.05300  231 TYR A CD2 
1853 C CE1 . TYR A 237 ? 0.32483 0.38380 0.32574 -0.08503 -0.00008 0.04785  231 TYR A CE1 
1854 C CE2 . TYR A 237 ? 0.41141 0.47529 0.41691 -0.09374 -0.00196 0.04550  231 TYR A CE2 
1855 C CZ  . TYR A 237 ? 0.41102 0.48467 0.41751 -0.08775 0.00287  0.04268  231 TYR A CZ  
1856 O OH  . TYR A 237 ? 0.37366 0.47167 0.38752 -0.08417 0.00997  0.03413  231 TYR A OH  
1857 N N   . LEU A 238 ? 0.47253 0.44987 0.47376 -0.08102 -0.02604 0.05262  232 LEU A N   
1858 C CA  . LEU A 238 ? 0.41943 0.40508 0.42526 -0.07911 -0.02319 0.04564  232 LEU A CA  
1859 C C   . LEU A 238 ? 0.25732 0.23061 0.26735 -0.06567 -0.02367 0.03879  232 LEU A C   
1860 O O   . LEU A 238 ? 0.36409 0.34757 0.37819 -0.06011 -0.01959 0.03213  232 LEU A O   
1861 C CB  . LEU A 238 ? 0.44184 0.42293 0.44334 -0.09312 -0.02832 0.04956  232 LEU A CB  
1862 C CG  . LEU A 238 ? 0.32390 0.31739 0.31936 -0.10891 -0.02796 0.05720  232 LEU A CG  
1863 C CD1 . LEU A 238 ? 0.43004 0.40591 0.41724 -0.12363 -0.03699 0.06535  232 LEU A CD1 
1864 C CD2 . LEU A 238 ? 0.43836 0.46355 0.43894 -0.11305 -0.01985 0.05232  232 LEU A CD2 
1865 N N   . ASP A 239 ? 0.41621 0.36868 0.42546 -0.06047 -0.02881 0.04005  233 ASP A N   
1866 C CA  . ASP A 239 ? 0.31665 0.25887 0.32978 -0.04864 -0.02878 0.03252  233 ASP A CA  
1867 C C   . ASP A 239 ? 0.32997 0.28464 0.34709 -0.03791 -0.02156 0.02761  233 ASP A C   
1868 O O   . ASP A 239 ? 0.31153 0.26504 0.33066 -0.03024 -0.01936 0.02067  233 ASP A O   
1869 C CB  . ASP A 239 ? 0.36315 0.28208 0.37661 -0.04537 -0.03635 0.03412  233 ASP A CB  
1870 C CG  . ASP A 239 ? 0.39117 0.29903 0.40837 -0.03573 -0.03708 0.02486  233 ASP A CG  
1871 O OD1 . ASP A 239 ? 0.36593 0.27523 0.38172 -0.03755 -0.03610 0.01988  233 ASP A OD1 
1872 O OD2 . ASP A 239 ? 0.36977 0.26875 0.39154 -0.02662 -0.03863 0.02205  233 ASP A OD2 
1873 N N   . GLN A 240 ? 0.28002 0.24616 0.29727 -0.03814 -0.01812 0.03109  234 GLN A N   
1874 C CA  . GLN A 240 ? 0.26689 0.24140 0.28729 -0.02850 -0.01257 0.02720  234 GLN A CA  
1875 C C   . GLN A 240 ? 0.35362 0.33872 0.37567 -0.02458 -0.00824 0.02098  234 GLN A C   
1876 O O   . GLN A 240 ? 0.26676 0.24948 0.28986 -0.01668 -0.00626 0.01624  234 GLN A O   
1877 C CB  . GLN A 240 ? 0.26056 0.24624 0.28003 -0.03093 -0.00993 0.03146  234 GLN A CB  
1878 C CG  . GLN A 240 ? 0.27193 0.26229 0.29403 -0.02171 -0.00573 0.02848  234 GLN A CG  
1879 C CD  . GLN A 240 ? 0.19526 0.17239 0.21980 -0.01455 -0.00816 0.02739  234 GLN A CD  
1880 O OE1 . GLN A 240 ? 0.27166 0.23550 0.29638 -0.01611 -0.01396 0.03023  234 GLN A OE1 
1881 N NE2 . GLN A 240 ? 0.23185 0.21284 0.25878 -0.00681 -0.00417 0.02294  234 GLN A NE2 
1882 N N   . LEU A 241 ? 0.29500 0.29261 0.31732 -0.03055 -0.00717 0.02099  235 LEU A N   
1883 C CA  . LEU A 241 ? 0.25048 0.25803 0.27509 -0.02665 -0.00475 0.01568  235 LEU A CA  
1884 C C   . LEU A 241 ? 0.22095 0.21764 0.24361 -0.02429 -0.00716 0.01162  235 LEU A C   
1885 O O   . LEU A 241 ? 0.24984 0.24932 0.27224 -0.01870 -0.00561 0.00749  235 LEU A O   
1886 C CB  . LEU A 241 ? 0.23578 0.26037 0.26330 -0.03348 -0.00397 0.01578  235 LEU A CB  
1887 C CG  . LEU A 241 ? 0.31002 0.34797 0.34217 -0.02929 -0.00269 0.01070  235 LEU A CG  
1888 C CD1 . LEU A 241 ? 0.23817 0.28068 0.27232 -0.02033 0.00029  0.00851  235 LEU A CD1 
1889 C CD2 . LEU A 241 ? 0.31922 0.37573 0.35646 -0.03678 -0.00226 0.01021  235 LEU A CD2 
1890 N N   . ASN A 242 ? 0.28225 0.26566 0.30268 -0.02891 -0.01146 0.01265  236 ASN A N   
1891 C CA  . ASN A 242 ? 0.33182 0.30392 0.34999 -0.02647 -0.01362 0.00738  236 ASN A CA  
1892 C C   . ASN A 242 ? 0.28298 0.25076 0.30095 -0.01696 -0.01072 0.00292  236 ASN A C   
1893 O O   . ASN A 242 ? 0.27839 0.24719 0.29381 -0.01387 -0.00936 -0.00231 236 ASN A O   
1894 C CB  . ASN A 242 ? 0.23578 0.19104 0.25219 -0.03183 -0.01951 0.00881  236 ASN A CB  
1895 C CG  . ASN A 242 ? 0.39402 0.35303 0.40910 -0.04349 -0.02277 0.01305  236 ASN A CG  
1896 O OD1 . ASN A 242 ? 0.29668 0.27135 0.31310 -0.04672 -0.02073 0.01226  236 ASN A OD1 
1897 N ND2 . ASN A 242 ? 0.22355 0.16821 0.23632 -0.05022 -0.02852 0.01761  236 ASN A ND2 
1898 N N   . HIS A 243 ? 0.22823 0.19217 0.24847 -0.01316 -0.00991 0.00508  237 HIS A N   
1899 C CA  . HIS A 243 ? 0.22725 0.18872 0.24843 -0.00508 -0.00703 0.00055  237 HIS A CA  
1900 C C   . HIS A 243 ? 0.20091 0.17449 0.22049 -0.00186 -0.00225 -0.00043 237 HIS A C   
1901 O O   . HIS A 243 ? 0.25419 0.22785 0.27124 0.00185  0.00012  -0.00530 237 HIS A O   
1902 C CB  . HIS A 243 ? 0.20523 0.16093 0.23056 -0.00217 -0.00830 0.00348  237 HIS A CB  
1903 C CG  . HIS A 243 ? 0.25394 0.19371 0.28128 -0.00309 -0.01452 0.00328  237 HIS A CG  
1904 N ND1 . HIS A 243 ? 0.37755 0.30836 0.40923 0.00383  -0.01572 -0.00299 237 HIS A ND1 
1905 C CD2 . HIS A 243 ? 0.32290 0.25362 0.34868 -0.01034 -0.02052 0.00830  237 HIS A CD2 
1906 C CE1 . HIS A 243 ? 0.47602 0.39115 0.50941 0.00207  -0.02301 -0.00206 237 HIS A CE1 
1907 N NE2 . HIS A 243 ? 0.31387 0.22769 0.34277 -0.00722 -0.02629 0.00551  237 HIS A NE2 
1908 N N   . ILE A 244 ? 0.14954 0.13323 0.17015 -0.00368 -0.00112 0.00384  238 ILE A N   
1909 C CA  . ILE A 244 ? 0.18704 0.17967 0.20658 -0.00026 0.00186  0.00314  238 ILE A CA  
1910 C C   . ILE A 244 ? 0.23865 0.23340 0.25450 -0.00077 0.00081  -0.00007 238 ILE A C   
1911 O O   . ILE A 244 ? 0.21073 0.20520 0.22242 0.00211  0.00213  -0.00229 238 ILE A O   
1912 C CB  . ILE A 244 ? 0.17015 0.17298 0.19274 -0.00162 0.00272  0.00678  238 ILE A CB  
1913 C CG1 . ILE A 244 ? 0.22855 0.22925 0.25279 -0.00118 0.00368  0.01013  238 ILE A CG1 
1914 C CG2 . ILE A 244 ? 0.15698 0.16707 0.17913 0.00211  0.00394  0.00542  238 ILE A CG2 
1915 C CD1 . ILE A 244 ? 0.22602 0.23676 0.25206 -0.00452 0.00456  0.01318  238 ILE A CD1 
1916 N N   . LEU A 245 ? 0.21882 0.21610 0.23549 -0.00547 -0.00205 0.00004  239 LEU A N   
1917 C CA  . LEU A 245 ? 0.28581 0.28543 0.29914 -0.00643 -0.00421 -0.00271 239 LEU A CA  
1918 C C   . LEU A 245 ? 0.24389 0.23366 0.25101 -0.00624 -0.00438 -0.00729 239 LEU A C   
1919 O O   . LEU A 245 ? 0.23467 0.22549 0.23607 -0.00614 -0.00523 -0.00967 239 LEU A O   
1920 C CB  . LEU A 245 ? 0.19072 0.19718 0.20765 -0.01216 -0.00732 -0.00182 239 LEU A CB  
1921 C CG  . LEU A 245 ? 0.33611 0.35628 0.36001 -0.01269 -0.00642 0.00077  239 LEU A CG  
1922 C CD1 . LEU A 245 ? 0.26903 0.29854 0.29724 -0.01976 -0.00881 0.00102  239 LEU A CD1 
1923 C CD2 . LEU A 245 ? 0.24000 0.26719 0.26529 -0.00670 -0.00642 -0.00021 239 LEU A CD2 
1924 N N   . GLY A 246 ? 0.19923 0.17945 0.20727 -0.00622 -0.00406 -0.00900 240 GLY A N   
1925 C CA  . GLY A 246 ? 0.23834 0.21035 0.24194 -0.00503 -0.00360 -0.01548 240 GLY A CA  
1926 C C   . GLY A 246 ? 0.32600 0.30098 0.32540 -0.00101 0.00059  -0.01844 240 GLY A C   
1927 O O   . GLY A 246 ? 0.26765 0.24030 0.26119 -0.00131 0.00168  -0.02462 240 GLY A O   
1928 N N   . ILE A 247 ? 0.28240 0.26294 0.28385 0.00176  0.00302  -0.01444 241 ILE A N   
1929 C CA  . ILE A 247 ? 0.19543 0.17924 0.19247 0.00399  0.00679  -0.01603 241 ILE A CA  
1930 C C   . ILE A 247 ? 0.21458 0.20381 0.20645 0.00277  0.00544  -0.01197 241 ILE A C   
1931 O O   . ILE A 247 ? 0.23605 0.22605 0.21924 0.00102  0.00586  -0.01346 241 ILE A O   
1932 C CB  . ILE A 247 ? 0.18527 0.16968 0.18852 0.00789  0.00987  -0.01502 241 ILE A CB  
1933 C CG1 . ILE A 247 ? 0.29487 0.27397 0.30234 0.01047  0.01096  -0.02138 241 ILE A CG1 
1934 C CG2 . ILE A 247 ? 0.18804 0.17808 0.18708 0.00853  0.01305  -0.01373 241 ILE A CG2 
1935 C CD1 . ILE A 247 ? 0.31091 0.28845 0.32746 0.01420  0.01088  -0.01924 241 ILE A CD1 
1936 N N   . LEU A 248 ? 0.19523 0.18821 0.19219 0.00346  0.00331  -0.00708 242 LEU A N   
1937 C CA  . LEU A 248 ? 0.26692 0.26380 0.26106 0.00377  0.00059  -0.00400 242 LEU A CA  
1938 C C   . LEU A 248 ? 0.29192 0.28954 0.28160 0.00094  -0.00413 -0.00487 242 LEU A C   
1939 O O   . LEU A 248 ? 0.23300 0.23113 0.21753 0.00089  -0.00760 -0.00285 242 LEU A O   
1940 C CB  A LEU A 248 ? 0.23071 0.23302 0.23310 0.00602  -0.00028 -0.00069 242 LEU A CB  
1941 C CB  B LEU A 248 ? 0.23071 0.23302 0.23310 0.00601  -0.00028 -0.00070 242 LEU A CB  
1942 C CG  A LEU A 248 ? 0.19290 0.19565 0.19779 0.00886  0.00270  0.00137  242 LEU A CG  
1943 C CG  B LEU A 248 ? 0.19337 0.19591 0.19840 0.00874  0.00294  0.00124  242 LEU A CG  
1944 C CD1 A LEU A 248 ? 0.21419 0.21338 0.22007 0.00908  0.00670  0.00026  242 LEU A CD1 
1945 C CD1 B LEU A 248 ? 0.18160 0.18954 0.19103 0.01114  0.00086  0.00315  242 LEU A CD1 
1946 C CD2 A LEU A 248 ? 0.15970 0.16928 0.17236 0.01016  0.00197  0.00295  242 LEU A CD2 
1947 C CD2 B LEU A 248 ? 0.22879 0.22734 0.22696 0.00893  0.00538  0.00078  242 LEU A CD2 
1948 N N   . GLY A 249 ? 0.25549 0.25228 0.24676 -0.00181 -0.00531 -0.00743 243 GLY A N   
1949 C CA  . GLY A 249 ? 0.23419 0.23307 0.22252 -0.00496 -0.01038 -0.00814 243 GLY A CA  
1950 C C   . GLY A 249 ? 0.30845 0.31622 0.30613 -0.00439 -0.01404 -0.00559 243 GLY A C   
1951 O O   . GLY A 249 ? 0.20533 0.21786 0.21075 -0.00179 -0.01221 -0.00366 243 GLY A O   
1952 N N   . SER A 250 ? 0.22558 0.23716 0.22276 -0.00714 -0.01928 -0.00632 244 SER A N   
1953 C CA  . SER A 250 ? 0.16910 0.19244 0.17697 -0.00682 -0.02285 -0.00539 244 SER A CA  
1954 C C   . SER A 250 ? 0.22168 0.24988 0.23413 -0.00076 -0.02493 -0.00340 244 SER A C   
1955 O O   . SER A 250 ? 0.20896 0.23071 0.21368 0.00128  -0.02752 -0.00178 244 SER A O   
1956 C CB  . SER A 250 ? 0.16485 0.19197 0.17154 -0.01092 -0.02892 -0.00683 244 SER A CB  
1957 O OG  . SER A 250 ? 0.26485 0.28571 0.26675 -0.01671 -0.02762 -0.00937 244 SER A OG  
1958 N N   . PRO A 251 ? 0.24317 0.28233 0.26749 0.00167  -0.02407 -0.00376 245 PRO A N   
1959 C CA  . PRO A 251 ? 0.23078 0.27428 0.26088 0.00832  -0.02696 -0.00351 245 PRO A CA  
1960 C C   . PRO A 251 ? 0.24379 0.28987 0.27516 0.01047  -0.03595 -0.00361 245 PRO A C   
1961 O O   . PRO A 251 ? 0.21637 0.26853 0.24986 0.00692  -0.03956 -0.00482 245 PRO A O   
1962 C CB  . PRO A 251 ? 0.17261 0.23063 0.21583 0.00916  -0.02362 -0.00588 245 PRO A CB  
1963 C CG  . PRO A 251 ? 0.30622 0.36373 0.34755 0.00231  -0.01832 -0.00525 245 PRO A CG  
1964 C CD  . PRO A 251 ? 0.19218 0.23899 0.22382 -0.00212 -0.01996 -0.00456 245 PRO A CD  
1965 N N   . SER A 252 ? 0.17433 0.21495 0.20437 0.01605  -0.04055 -0.00199 246 SER A N   
1966 C CA  . SER A 252 ? 0.28223 0.32358 0.31416 0.01911  -0.05110 -0.00131 246 SER A CA  
1967 C C   . SER A 252 ? 0.30708 0.36689 0.35797 0.02348  -0.05436 -0.00606 246 SER A C   
1968 O O   . SER A 252 ? 0.20352 0.27537 0.26491 0.02412  -0.04792 -0.00975 246 SER A O   
1969 C CB  . SER A 252 ? 0.29914 0.32771 0.32478 0.02366  -0.05627 0.00216  246 SER A CB  
1970 O OG  . SER A 252 ? 0.23063 0.26309 0.26694 0.03027  -0.05427 -0.00042 246 SER A OG  
1971 N N   . GLN A 253 ? 0.27923 0.34247 0.33453 0.02604  -0.06478 -0.00615 247 GLN A N   
1972 C CA  . GLN A 253 ? 0.26736 0.35036 0.34304 0.03144  -0.06891 -0.01180 247 GLN A CA  
1973 C C   . GLN A 253 ? 0.25877 0.34564 0.34593 0.04053  -0.06813 -0.01574 247 GLN A C   
1974 O O   . GLN A 253 ? 0.19187 0.29824 0.29524 0.04305  -0.06407 -0.02239 247 GLN A O   
1975 C CB  . GLN A 253 ? 0.27334 0.35750 0.35181 0.03369  -0.08215 -0.01076 247 GLN A CB  
1976 C CG  . GLN A 253 ? 0.33495 0.44180 0.43708 0.04032  -0.08746 -0.01766 247 GLN A CG  
1977 C CD  A GLN A 253 ? 0.35910 0.46820 0.46458 0.04176  -0.10130 -0.01632 247 GLN A CD  
1978 C CD  B GLN A 253 ? 0.24957 0.37812 0.36174 0.03379  -0.07955 -0.02236 247 GLN A CD  
1979 O OE1 A GLN A 253 ? 0.40508 0.49684 0.50037 0.04428  -0.11151 -0.01084 247 GLN A OE1 
1980 O OE1 B GLN A 253 ? 0.28754 0.43089 0.41127 0.03506  -0.07170 -0.02768 247 GLN A OE1 
1981 N NE2 A GLN A 253 ? 0.32721 0.45793 0.44650 0.03926  -0.10229 -0.02085 247 GLN A NE2 
1982 N NE2 B GLN A 253 ? 0.23431 0.36457 0.34091 0.02567  -0.08182 -0.02029 247 GLN A NE2 
1983 N N   . GLU A 254 ? 0.20933 0.27816 0.28768 0.04470  -0.07190 -0.01211 248 GLU A N   
1984 C CA  . GLU A 254 ? 0.22918 0.29868 0.31717 0.05339  -0.07208 -0.01623 248 GLU A CA  
1985 C C   . GLU A 254 ? 0.29859 0.37622 0.38882 0.05095  -0.05901 -0.01956 248 GLU A C   
1986 O O   . GLU A 254 ? 0.25531 0.34740 0.36024 0.05636  -0.05652 -0.02685 248 GLU A O   
1987 C CB  . GLU A 254 ? 0.37071 0.41633 0.44564 0.05587  -0.07882 -0.01030 248 GLU A CB  
1988 C CG  A GLU A 254 ? 0.40473 0.44768 0.48926 0.06538  -0.08154 -0.01477 248 GLU A CG  
1989 C CG  B GLU A 254 ? 0.40479 0.44731 0.48815 0.06469  -0.08025 -0.01453 248 GLU A CG  
1990 C CD  A GLU A 254 ? 0.45016 0.46840 0.52260 0.06740  -0.09178 -0.00825 248 GLU A CD  
1991 C CD  B GLU A 254 ? 0.48157 0.49905 0.54863 0.06374  -0.08438 -0.00749 248 GLU A CD  
1992 O OE1 A GLU A 254 ? 0.34067 0.35338 0.41762 0.07294  -0.10564 -0.00732 248 GLU A OE1 
1993 O OE1 B GLU A 254 ? 0.53572 0.54144 0.58449 0.05504  -0.08224 0.00001  248 GLU A OE1 
1994 O OE2 A GLU A 254 ? 0.51824 0.52257 0.57666 0.06294  -0.08662 -0.00375 248 GLU A OE2 
1995 O OE2 B GLU A 254 ? 0.47080 0.48088 0.54338 0.07126  -0.08968 -0.01002 248 GLU A OE2 
1996 N N   . ASP A 255 ? 0.23331 0.30238 0.30927 0.04280  -0.05094 -0.01476 249 ASP A N   
1997 C CA  . ASP A 255 ? 0.26057 0.33584 0.33750 0.03978  -0.03995 -0.01664 249 ASP A CA  
1998 C C   . ASP A 255 ? 0.27937 0.37644 0.36770 0.03576  -0.03511 -0.02123 249 ASP A C   
1999 O O   . ASP A 255 ? 0.22142 0.33001 0.31608 0.03521  -0.02831 -0.02504 249 ASP A O   
2000 C CB  . ASP A 255 ? 0.14119 0.20135 0.20150 0.03305  -0.03413 -0.01058 249 ASP A CB  
2001 C CG  . ASP A 255 ? 0.17019 0.21222 0.21973 0.03551  -0.03663 -0.00660 249 ASP A CG  
2002 O OD1 . ASP A 255 ? 0.17385 0.21314 0.22843 0.04234  -0.04254 -0.00826 249 ASP A OD1 
2003 O OD2 . ASP A 255 ? 0.19836 0.22920 0.23490 0.03045  -0.03296 -0.00225 249 ASP A OD2 
2004 N N   . LEU A 256 ? 0.17487 0.27826 0.26503 0.03175  -0.03861 -0.02078 250 LEU A N   
2005 C CA  . LEU A 256 ? 0.26395 0.38925 0.36530 0.02667  -0.03479 -0.02496 250 LEU A CA  
2006 C C   . LEU A 256 ? 0.24306 0.39023 0.36413 0.03387  -0.03685 -0.03351 250 LEU A C   
2007 O O   . LEU A 256 ? 0.23662 0.40322 0.36664 0.03063  -0.02995 -0.03841 250 LEU A O   
2008 C CB  . LEU A 256 ? 0.27109 0.39735 0.36954 0.02024  -0.03885 -0.02267 250 LEU A CB  
2009 C CG  . LEU A 256 ? 0.37369 0.48437 0.45586 0.01143  -0.03458 -0.01702 250 LEU A CG  
2010 C CD1 . LEU A 256 ? 0.31027 0.42244 0.39018 0.00519  -0.03913 -0.01617 250 LEU A CD1 
2011 C CD2 . LEU A 256 ? 0.25139 0.36665 0.33318 0.00529  -0.02550 -0.01679 250 LEU A CD2 
2012 N N   . ASN A 257 ? 0.23372 0.37835 0.36178 0.04345  -0.04661 -0.03571 251 ASN A N   
2013 C CA  . ASN A 257 ? 0.28774 0.45258 0.43687 0.05260  -0.04999 -0.04544 251 ASN A CA  
2014 C C   . ASN A 257 ? 0.34305 0.51251 0.49627 0.05654  -0.04279 -0.05105 251 ASN A C   
2015 O O   . ASN A 257 ? 0.30868 0.49701 0.47591 0.05996  -0.04010 -0.05992 251 ASN A O   
2016 C CB  . ASN A 257 ? 0.25820 0.41316 0.41214 0.06297  -0.06397 -0.04546 251 ASN A CB  
2017 C CG  . ASN A 257 ? 0.42366 0.58039 0.57739 0.05960  -0.07220 -0.04196 251 ASN A CG  
2018 O OD1 . ASN A 257 ? 0.35335 0.52717 0.51161 0.05190  -0.06815 -0.04335 251 ASN A OD1 
2019 N ND2 . ASN A 257 ? 0.29573 0.43431 0.44315 0.06435  -0.08437 -0.03700 251 ASN A ND2 
2020 N N   . CME A 258 ? 0.30179 0.45078 0.43893 0.05432  -0.03859 -0.04514 252 CME A N   
2021 C CA  . CME A 258 ? 0.34211 0.49334 0.48033 0.05667  -0.03187 -0.04949 252 CME A CA  
2022 C CB  . CME A 258 ? 0.32190 0.44505 0.44196 0.05633  -0.03143 -0.04171 252 CME A CB  
2023 S SG  . CME A 258 ? 0.30906 0.41092 0.42840 0.06758  -0.04459 -0.04078 252 CME A SG  
2024 S SD  . CME A 258 ? 0.63868 0.75959 0.78217 0.08001  -0.04843 -0.05580 252 CME A SD  
2025 C CE  . CME A 258 ? 0.58598 0.69105 0.72343 0.08434  -0.04685 -0.05811 252 CME A CE  
2026 C CZ  . CME A 258 ? 0.46383 0.57347 0.59569 0.07917  -0.03644 -0.05796 252 CME A CZ  
2027 O OH  . CME A 258 ? 0.56605 0.65654 0.68967 0.08211  -0.03820 -0.05641 252 CME A OH  
2028 C C   . CME A 258 ? 0.27864 0.44974 0.41782 0.04629  -0.02012 -0.05142 252 CME A C   
2029 O O   . CME A 258 ? 0.31878 0.50087 0.46222 0.04683  -0.01394 -0.05724 252 CME A O   
2030 N N   . ILE A 259 ? 0.23042 0.40392 0.36421 0.03641  -0.01820 -0.04609 253 ILE A N   
2031 C CA  . ILE A 259 ? 0.23186 0.42208 0.36564 0.02529  -0.00942 -0.04648 253 ILE A CA  
2032 C C   . ILE A 259 ? 0.27402 0.49417 0.42564 0.02411  -0.00984 -0.05450 253 ILE A C   
2033 O O   . ILE A 259 ? 0.17788 0.40211 0.33147 0.01960  -0.01357 -0.05224 253 ILE A O   
2034 C CB  . ILE A 259 ? 0.19671 0.37144 0.31474 0.01462  -0.00757 -0.03651 253 ILE A CB  
2035 C CG1 . ILE A 259 ? 0.19877 0.34722 0.30155 0.01641  -0.00684 -0.02994 253 ILE A CG1 
2036 C CG2 . ILE A 259 ? 0.11080 0.30062 0.22801 0.00219  -0.00022 -0.03584 253 ILE A CG2 
2037 C CD1 . ILE A 259 ? 0.21543 0.34652 0.30469 0.00926  -0.00703 -0.02184 253 ILE A CD1 
2038 N N   . ILE A 260 ? 0.18285 0.41878 0.34336 0.02731  -0.00574 -0.06316 254 ILE A N   
2039 C CA  . ILE A 260 ? 0.24244 0.49791 0.41389 0.02635  -0.00560 -0.06982 254 ILE A CA  
2040 C C   . ILE A 260 ? 0.19685 0.46939 0.36498 0.01136  0.00231  -0.06850 254 ILE A C   
2041 O O   . ILE A 260 ? 0.20543 0.49433 0.38151 0.00784  0.00185  -0.07189 254 ILE A O   
2042 C CB  . ILE A 260 ? 0.32903 0.58828 0.50789 0.03637  -0.00555 -0.07969 254 ILE A CB  
2043 C CG1 . ILE A 260 ? 0.22480 0.49100 0.39712 0.03069  0.00416  -0.08298 254 ILE A CG1 
2044 C CG2 . ILE A 260 ? 0.29827 0.53556 0.47694 0.04936  -0.01398 -0.07909 254 ILE A CG2 
2045 C CD1 . ILE A 260 ? 0.29400 0.57165 0.47509 0.03741  0.00523  -0.09494 254 ILE A CD1 
2046 N N   . ASN A 261 ? 0.15577 0.42390 0.31165 0.00184  0.00883  -0.06298 255 ASN A N   
2047 C CA  . ASN A 261 ? 0.18862 0.46790 0.33815 -0.01399 0.01454  -0.05933 255 ASN A CA  
2048 C C   . ASN A 261 ? 0.16035 0.43864 0.31044 -0.02099 0.00992  -0.05348 255 ASN A C   
2049 O O   . ASN A 261 ? 0.18366 0.44706 0.33006 -0.01975 0.00528  -0.04767 255 ASN A O   
2050 C CB  . ASN A 261 ? 0.21038 0.48024 0.34519 -0.02258 0.02027  -0.05275 255 ASN A CB  
2051 C CG  . ASN A 261 ? 0.26032 0.53880 0.38611 -0.03935 0.02508  -0.04840 255 ASN A CG  
2052 O OD1 . ASN A 261 ? 0.25004 0.52197 0.36985 -0.04947 0.02322  -0.04032 255 ASN A OD1 
2053 N ND2 . ASN A 261 ? 0.28142 0.57354 0.40518 -0.04287 0.03053  -0.05382 255 ASN A ND2 
2054 N N   . LEU A 262 ? 0.16003 0.45472 0.31424 -0.02894 0.01104  -0.05550 256 LEU A N   
2055 C CA  . LEU A 262 ? 0.17887 0.47387 0.33566 -0.03424 0.00542  -0.05175 256 LEU A CA  
2056 C C   . LEU A 262 ? 0.19191 0.47343 0.33471 -0.04821 0.00588  -0.04145 256 LEU A C   
2057 O O   . LEU A 262 ? 0.11629 0.38739 0.25767 -0.04950 -0.00029 -0.03724 256 LEU A O   
2058 C CB  A LEU A 262 ? 0.14479 0.46179 0.31061 -0.03866 0.00640  -0.05721 256 LEU A CB  
2059 C CB  B LEU A 262 ? 0.14477 0.46187 0.31060 -0.03859 0.00649  -0.05730 256 LEU A CB  
2060 C CG  A LEU A 262 ? 0.12098 0.44899 0.30371 -0.02458 0.00159  -0.06640 256 LEU A CG  
2061 C CG  B LEU A 262 ? 0.12110 0.44163 0.29531 -0.03827 -0.00123 -0.05693 256 LEU A CG  
2062 C CD1 A LEU A 262 ? 0.15884 0.51230 0.35041 -0.02874 0.00549  -0.07386 256 LEU A CD1 
2063 C CD1 B LEU A 262 ? 0.18867 0.49910 0.37057 -0.02270 -0.00978 -0.05895 256 LEU A CD1 
2064 C CD2 A LEU A 262 ? 0.19791 0.51755 0.38565 -0.01991 -0.00845 -0.06338 256 LEU A CD2 
2065 C CD2 B LEU A 262 ? 0.20847 0.55336 0.39351 -0.04115 0.00053  -0.06366 256 LEU A CD2 
2066 N N   . LYS A 263 ? 0.18163 0.46173 0.31297 -0.05914 0.01215  -0.03726 257 LYS A N   
2067 C CA  . LYS A 263 ? 0.23458 0.49800 0.35203 -0.07237 0.01119  -0.02685 257 LYS A CA  
2068 C C   . LYS A 263 ? 0.13726 0.37171 0.24588 -0.06452 0.00766  -0.02160 257 LYS A C   
2069 O O   . LYS A 263 ? 0.13392 0.34612 0.23279 -0.06780 0.00298  -0.01527 257 LYS A O   
2070 C CB  . LYS A 263 ? 0.23544 0.49885 0.34022 -0.08424 0.01700  -0.02253 257 LYS A CB  
2071 C CG  . LYS A 263 ? 0.23843 0.52191 0.34470 -0.09265 0.01996  -0.02608 257 LYS A CG  
2072 C CD  . LYS A 263 ? 0.35872 0.63736 0.44829 -0.10814 0.02286  -0.01873 257 LYS A CD  
2073 C CE  . LYS A 263 ? 0.40547 0.69502 0.49302 -0.12106 0.02222  -0.01752 257 LYS A CE  
2074 N NZ  . LYS A 263 ? 0.31550 0.60247 0.38616 -0.13618 0.02434  -0.01092 257 LYS A NZ  
2075 N N   . ALA A 264 ? 0.10912 0.33853 0.21830 -0.05276 0.00965  -0.02444 258 ALA A N   
2076 C CA  . ALA A 264 ? 0.12383 0.32245 0.22210 -0.04410 0.00666  -0.01948 258 ALA A CA  
2077 C C   . ALA A 264 ? 0.14554 0.33376 0.24645 -0.03521 -0.00026 -0.02062 258 ALA A C   
2078 O O   . ALA A 264 ? 0.15496 0.31967 0.24499 -0.03539 -0.00364 -0.01520 258 ALA A O   
2079 C CB  . ALA A 264 ? 0.12648 0.32399 0.22495 -0.03507 0.01027  -0.02239 258 ALA A CB  
2080 N N   . ARG A 265 ? 0.10319 0.30903 0.21855 -0.02733 -0.00287 -0.02807 259 ARG A N   
2081 C CA  . ARG A 265 ? 0.12427 0.32041 0.24121 -0.01954 -0.01073 -0.02841 259 ARG A CA  
2082 C C   . ARG A 265 ? 0.11080 0.30343 0.22354 -0.02896 -0.01450 -0.02487 259 ARG A C   
2083 O O   . ARG A 265 ? 0.13624 0.30828 0.23938 -0.02708 -0.01926 -0.02120 259 ARG A O   
2084 C CB  . ARG A 265 ? 0.20170 0.41811 0.33660 -0.00932 -0.01443 -0.03706 259 ARG A CB  
2085 C CG  . ARG A 265 ? 0.25000 0.45304 0.38458 -0.00034 -0.02400 -0.03620 259 ARG A CG  
2086 C CD  . ARG A 265 ? 0.20696 0.43091 0.36130 0.00889  -0.02999 -0.04446 259 ARG A CD  
2087 N NE  . ARG A 265 ? 0.21212 0.44158 0.37536 0.01965  -0.02850 -0.05079 259 ARG A NE  
2088 C CZ  . ARG A 265 ? 0.25215 0.49183 0.43074 0.03076  -0.03453 -0.05799 259 ARG A CZ  
2089 N NH1 . ARG A 265 ? 0.26047 0.50573 0.44670 0.03253  -0.04237 -0.05885 259 ARG A NH1 
2090 N NH2 . ARG A 265 ? 0.21800 0.45389 0.39869 0.03918  -0.03216 -0.06260 259 ARG A NH2 
2091 N N   . ASN A 266 ? 0.11303 0.32623 0.23235 -0.03999 -0.01238 -0.02632 260 ASN A N   
2092 C CA  . ASN A 266 ? 0.12061 0.33088 0.23634 -0.04989 -0.01655 -0.02335 260 ASN A CA  
2093 C C   . ASN A 266 ? 0.14694 0.32895 0.24454 -0.05714 -0.01629 -0.01560 260 ASN A C   
2094 O O   . ASN A 266 ? 0.16412 0.33296 0.25519 -0.06074 -0.02127 -0.01349 260 ASN A O   
2095 C CB  . ASN A 266 ? 0.12248 0.36260 0.24946 -0.06155 -0.01417 -0.02652 260 ASN A CB  
2096 C CG  . ASN A 266 ? 0.25546 0.52373 0.40272 -0.05443 -0.01734 -0.03526 260 ASN A CG  
2097 O OD1 . ASN A 266 ? 0.21105 0.47240 0.36202 -0.04253 -0.02395 -0.03725 260 ASN A OD1 
2098 N ND2 . ASN A 266 ? 0.15422 0.44429 0.30920 -0.05982 -0.01266 -0.03912 260 ASN A ND2 
2099 N N   . TYR A 267 ? 0.12751 0.30005 0.21730 -0.05921 -0.01116 -0.01188 261 TYR A N   
2100 C CA  . TYR A 267 ? 0.17840 0.32251 0.25291 -0.06306 -0.01213 -0.00540 261 TYR A CA  
2101 C C   . TYR A 267 ? 0.13416 0.25727 0.20226 -0.05244 -0.01563 -0.00568 261 TYR A C   
2102 O O   . TYR A 267 ? 0.17210 0.27808 0.23187 -0.05538 -0.01927 -0.00398 261 TYR A O   
2103 C CB  . TYR A 267 ? 0.13471 0.27268 0.20301 -0.06551 -0.00715 -0.00132 261 TYR A CB  
2104 C CG  . TYR A 267 ? 0.14235 0.25050 0.19746 -0.06636 -0.00935 0.00425  261 TYR A CG  
2105 C CD1 . TYR A 267 ? 0.16929 0.26575 0.21759 -0.07778 -0.01279 0.00855  261 TYR A CD1 
2106 C CD2 . TYR A 267 ? 0.19493 0.28682 0.24530 -0.05561 -0.00858 0.00452  261 TYR A CD2 
2107 C CE1 . TYR A 267 ? 0.24069 0.30989 0.27902 -0.07708 -0.01564 0.01209  261 TYR A CE1 
2108 C CE2 . TYR A 267 ? 0.14485 0.21219 0.18564 -0.05544 -0.01055 0.00798  261 TYR A CE2 
2109 C CZ  . TYR A 267 ? 0.20052 0.25647 0.23594 -0.06547 -0.01424 0.01131  261 TYR A CZ  
2110 O OH  . TYR A 267 ? 0.29102 0.32246 0.31883 -0.06399 -0.01696 0.01336  261 TYR A OH  
2111 N N   . LEU A 268 ? 0.12586 0.25023 0.19722 -0.04072 -0.01464 -0.00819 262 LEU A N   
2112 C CA  . LEU A 268 ? 0.14318 0.24910 0.20720 -0.03214 -0.01759 -0.00792 262 LEU A CA  
2113 C C   . LEU A 268 ? 0.13152 0.23855 0.19628 -0.03211 -0.02404 -0.00993 262 LEU A C   
2114 O O   . LEU A 268 ? 0.15370 0.24345 0.20819 -0.03130 -0.02668 -0.00896 262 LEU A O   
2115 C CB  . LEU A 268 ? 0.11856 0.22632 0.18595 -0.02125 -0.01604 -0.00963 262 LEU A CB  
2116 C CG  . LEU A 268 ? 0.26918 0.37304 0.33359 -0.02111 -0.01010 -0.00746 262 LEU A CG  
2117 C CD1 . LEU A 268 ? 0.18081 0.29109 0.25103 -0.01156 -0.00882 -0.01052 262 LEU A CD1 
2118 C CD2 . LEU A 268 ? 0.17465 0.25521 0.22664 -0.02166 -0.00931 -0.00328 262 LEU A CD2 
2119 N N   . LEU A 269 ? 0.12997 0.25863 0.20705 -0.03331 -0.02667 -0.01329 263 LEU A N   
2120 C CA  . LEU A 269 ? 0.14493 0.27665 0.22366 -0.03399 -0.03384 -0.01496 263 LEU A CA  
2121 C C   . LEU A 269 ? 0.19425 0.31709 0.26484 -0.04518 -0.03551 -0.01316 263 LEU A C   
2122 O O   . LEU A 269 ? 0.18237 0.29873 0.24794 -0.04590 -0.04125 -0.01384 263 LEU A O   
2123 C CB  . LEU A 269 ? 0.13163 0.29131 0.22830 -0.03228 -0.03650 -0.01972 263 LEU A CB  
2124 C CG  . LEU A 269 ? 0.16641 0.33315 0.27257 -0.01916 -0.03857 -0.02308 263 LEU A CG  
2125 C CD1 . LEU A 269 ? 0.23410 0.43096 0.36093 -0.01713 -0.04123 -0.02954 263 LEU A CD1 
2126 C CD2 . LEU A 269 ? 0.22930 0.37744 0.32615 -0.01222 -0.04567 -0.02081 263 LEU A CD2 
2127 N N   . SER A 270 ? 0.16165 0.28285 0.22988 -0.05438 -0.03138 -0.01077 264 SER A N   
2128 C CA  . SER A 270 ? 0.20174 0.31261 0.26253 -0.06565 -0.03388 -0.00906 264 SER A CA  
2129 C C   . SER A 270 ? 0.17244 0.25464 0.21855 -0.06379 -0.03450 -0.00783 264 SER A C   
2130 O O   . SER A 270 ? 0.27759 0.34818 0.31690 -0.07119 -0.03790 -0.00802 264 SER A O   
2131 C CB  . SER A 270 ? 0.16306 0.28148 0.22601 -0.07729 -0.03047 -0.00607 264 SER A CB  
2132 O OG  . SER A 270 ? 0.27087 0.37365 0.32632 -0.07612 -0.02636 -0.00228 264 SER A OG  
2133 N N   . LEU A 271 ? 0.20859 0.28010 0.25032 -0.05432 -0.03137 -0.00739 265 LEU A N   
2134 C CA  . LEU A 271 ? 0.19478 0.24254 0.22461 -0.05201 -0.03093 -0.00750 265 LEU A CA  
2135 C C   . LEU A 271 ? 0.36412 0.40572 0.38713 -0.04877 -0.03482 -0.01090 265 LEU A C   
2136 O O   . LEU A 271 ? 0.23314 0.28565 0.25974 -0.04421 -0.03734 -0.01166 265 LEU A O   
2137 C CB  . LEU A 271 ? 0.20854 0.25007 0.23705 -0.04405 -0.02586 -0.00586 265 LEU A CB  
2138 C CG  . LEU A 271 ? 0.23676 0.28287 0.26965 -0.04719 -0.02205 -0.00214 265 LEU A CG  
2139 C CD1 . LEU A 271 ? 0.17494 0.21580 0.20655 -0.03877 -0.01775 -0.00098 265 LEU A CD1 
2140 C CD2 . LEU A 271 ? 0.25448 0.28767 0.28261 -0.05658 -0.02375 0.00043  265 LEU A CD2 
2141 N N   . PRO A 272 ? 0.32567 0.34966 0.33856 -0.05120 -0.03593 -0.01330 266 PRO A N   
2142 C CA  . PRO A 272 ? 0.35368 0.37170 0.35753 -0.04870 -0.03859 -0.01696 266 PRO A CA  
2143 C C   . PRO A 272 ? 0.29958 0.31506 0.29971 -0.03966 -0.03524 -0.01654 266 PRO A C   
2144 O O   . PRO A 272 ? 0.24336 0.25730 0.24659 -0.03509 -0.03050 -0.01442 266 PRO A O   
2145 C CB  . PRO A 272 ? 0.36575 0.36550 0.36060 -0.05316 -0.03916 -0.02106 266 PRO A CB  
2146 C CG  . PRO A 272 ? 0.40123 0.39760 0.40135 -0.05953 -0.03922 -0.01837 266 PRO A CG  
2147 C CD  . PRO A 272 ? 0.33638 0.34450 0.34534 -0.05625 -0.03532 -0.01324 266 PRO A CD  
2148 N N   . HIS A 273 ? 0.27143 0.28641 0.26387 -0.03814 -0.03828 -0.01814 267 HIS A N   
2149 C CA  . HIS A 273 ? 0.34806 0.36026 0.33518 -0.03151 -0.03589 -0.01702 267 HIS A CA  
2150 C C   . HIS A 273 ? 0.32740 0.32680 0.30810 -0.02951 -0.02965 -0.01976 267 HIS A C   
2151 O O   . HIS A 273 ? 0.38156 0.37151 0.35619 -0.03282 -0.02904 -0.02473 267 HIS A O   
2152 C CB  . HIS A 273 ? 0.43479 0.44751 0.41223 -0.03238 -0.04128 -0.01739 267 HIS A CB  
2153 C CG  . HIS A 273 ? 0.42532 0.43422 0.39535 -0.02768 -0.03953 -0.01531 267 HIS A CG  
2154 N ND1 . HIS A 273 ? 0.45760 0.47230 0.43379 -0.02217 -0.04151 -0.01067 267 HIS A ND1 
2155 C CD2 . HIS A 273 ? 0.49355 0.49376 0.45066 -0.02827 -0.03585 -0.01762 267 HIS A CD2 
2156 C CE1 . HIS A 273 ? 0.39185 0.39994 0.35820 -0.02035 -0.03982 -0.00912 267 HIS A CE1 
2157 N NE2 . HIS A 273 ? 0.49597 0.49661 0.45067 -0.02437 -0.03593 -0.01324 267 HIS A NE2 
2158 N N   . LYS A 274 ? 0.26969 0.26931 0.25269 -0.02377 -0.02538 -0.01723 268 LYS A N   
2159 C CA  . LYS A 274 ? 0.35115 0.34183 0.32953 -0.02086 -0.01964 -0.01982 268 LYS A CA  
2160 C C   . LYS A 274 ? 0.33490 0.32691 0.30620 -0.01784 -0.01834 -0.01832 268 LYS A C   
2161 O O   . LYS A 274 ? 0.29366 0.29160 0.26841 -0.01516 -0.02049 -0.01348 268 LYS A O   
2162 C CB  . LYS A 274 ? 0.35232 0.34164 0.33983 -0.01797 -0.01587 -0.01759 268 LYS A CB  
2163 C CG  . LYS A 274 ? 0.34288 0.33166 0.33728 -0.02238 -0.01795 -0.01651 268 LYS A CG  
2164 C CD  . LYS A 274 ? 0.35318 0.34354 0.35531 -0.02025 -0.01508 -0.01227 268 LYS A CD  
2165 C CE  . LYS A 274 ? 0.32364 0.31626 0.33149 -0.02668 -0.01744 -0.00944 268 LYS A CE  
2166 N NZ  . LYS A 274 ? 0.38678 0.36469 0.39174 -0.03074 -0.01967 -0.01172 268 LYS A NZ  
2167 N N   . ASN A 275 ? 0.35328 0.33991 0.31469 -0.01867 -0.01501 -0.02289 269 ASN A N   
2168 C CA  . ASN A 275 ? 0.39944 0.38721 0.35232 -0.01792 -0.01331 -0.02116 269 ASN A CA  
2169 C C   . ASN A 275 ? 0.32291 0.31062 0.28143 -0.01313 -0.00759 -0.01976 269 ASN A C   
2170 O O   . ASN A 275 ? 0.36365 0.34878 0.32960 -0.01063 -0.00395 -0.02250 269 ASN A O   
2171 C CB  . ASN A 275 ? 0.42544 0.41074 0.36427 -0.02251 -0.01143 -0.02730 269 ASN A CB  
2172 C CG  . ASN A 275 ? 0.41721 0.40154 0.35012 -0.02781 -0.01676 -0.03015 269 ASN A CG  
2173 O OD1 . ASN A 275 ? 0.49370 0.48108 0.42358 -0.03017 -0.02359 -0.02535 269 ASN A OD1 
2174 N ND2 . ASN A 275 ? 0.45280 0.43248 0.38454 -0.02949 -0.01445 -0.03835 269 ASN A ND2 
2175 N N   . LYS A 276 ? 0.27804 0.26774 0.23287 -0.01219 -0.00794 -0.01501 270 LYS A N   
2176 C CA  . LYS A 276 ? 0.27712 0.26718 0.23505 -0.00892 -0.00270 -0.01385 270 LYS A CA  
2177 C C   . LYS A 276 ? 0.37828 0.36802 0.33096 -0.01031 0.00367  -0.02054 270 LYS A C   
2178 O O   . LYS A 276 ? 0.28662 0.27681 0.22778 -0.01508 0.00409  -0.02430 270 LYS A O   
2179 C CB  . LYS A 276 ? 0.31268 0.30314 0.26563 -0.00904 -0.00557 -0.00754 270 LYS A CB  
2180 C CG  A LYS A 276 ? 0.31739 0.30834 0.27394 -0.00623 -0.00116 -0.00549 270 LYS A CG  
2181 C CG  B LYS A 276 ? 0.31760 0.30848 0.27206 -0.00709 -0.00061 -0.00608 270 LYS A CG  
2182 C CD  A LYS A 276 ? 0.31255 0.30121 0.26427 -0.00661 -0.00586 0.00098  270 LYS A CD  
2183 C CD  B LYS A 276 ? 0.32290 0.31144 0.26735 -0.00997 -0.00392 -0.00058 270 LYS A CD  
2184 C CE  A LYS A 276 ? 0.39782 0.38649 0.35289 -0.00452 -0.00206 0.00306  270 LYS A CE  
2185 C CE  B LYS A 276 ? 0.43425 0.42302 0.38185 -0.00815 -0.00027 0.00179  270 LYS A CE  
2186 N NZ  A LYS A 276 ? 0.35010 0.34169 0.31894 0.00076  0.00103  0.00173  270 LYS A NZ  
2187 N NZ  B LYS A 276 ? 0.39313 0.38641 0.34289 -0.00844 0.00800  -0.00360 270 LYS A NZ  
2188 N N   . VAL A 277 ? 0.27059 0.26066 0.23213 -0.00620 0.00843  -0.02266 271 VAL A N   
2189 C CA  . VAL A 277 ? 0.30953 0.30195 0.26976 -0.00591 0.01471  -0.02992 271 VAL A CA  
2190 C C   . VAL A 277 ? 0.28217 0.27977 0.23833 -0.00713 0.01797  -0.02656 271 VAL A C   
2191 O O   . VAL A 277 ? 0.33553 0.33309 0.29848 -0.00406 0.01747  -0.02094 271 VAL A O   
2192 C CB  . VAL A 277 ? 0.35686 0.34647 0.33010 -0.00042 0.01659  -0.03408 271 VAL A CB  
2193 C CG1 . VAL A 277 ? 0.33284 0.32725 0.30784 0.00146  0.02282  -0.04246 271 VAL A CG1 
2194 C CG2 . VAL A 277 ? 0.29239 0.27490 0.26801 -0.00081 0.01266  -0.03720 271 VAL A CG2 
2195 N N   . PRO A 278 ? 0.31305 0.31534 0.25744 -0.01258 0.02118  -0.02970 272 PRO A N   
2196 C CA  . PRO A 278 ? 0.30206 0.30899 0.24110 -0.01579 0.02375  -0.02558 272 PRO A CA  
2197 C C   . PRO A 278 ? 0.25638 0.26844 0.20780 -0.01091 0.02912  -0.02817 272 PRO A C   
2198 O O   . PRO A 278 ? 0.25414 0.26981 0.21369 -0.00722 0.03324  -0.03674 272 PRO A O   
2199 C CB  . PRO A 278 ? 0.34585 0.35856 0.26938 -0.02410 0.02705  -0.03029 272 PRO A CB  
2200 C CG  . PRO A 278 ? 0.38252 0.39122 0.30087 -0.02551 0.02360  -0.03406 272 PRO A CG  
2201 C CD  . PRO A 278 ? 0.33674 0.34067 0.27072 -0.01745 0.02244  -0.03711 272 PRO A CD  
2202 N N   . TRP A 279 ? 0.26487 0.27665 0.21819 -0.01059 0.02817  -0.02098 273 TRP A N   
2203 C CA  . TRP A 279 ? 0.24613 0.26320 0.21099 -0.00650 0.03234  -0.02248 273 TRP A CA  
2204 C C   . TRP A 279 ? 0.23870 0.26757 0.20286 -0.00913 0.03973  -0.03083 273 TRP A C   
2205 O O   . TRP A 279 ? 0.35138 0.38576 0.32846 -0.00361 0.04321  -0.03716 273 TRP A O   
2206 C CB  . TRP A 279 ? 0.27856 0.29348 0.24280 -0.00742 0.03001  -0.01383 273 TRP A CB  
2207 C CG  . TRP A 279 ? 0.27928 0.28563 0.24699 -0.00377 0.02367  -0.00752 273 TRP A CG  
2208 C CD1 . TRP A 279 ? 0.30025 0.30045 0.26064 -0.00592 0.01796  -0.00109 273 TRP A CD1 
2209 C CD2 . TRP A 279 ? 0.20606 0.21011 0.18577 0.00239  0.02219  -0.00761 273 TRP A CD2 
2210 N NE1 . TRP A 279 ? 0.23856 0.23511 0.20717 -0.00079 0.01397  0.00141  273 TRP A NE1 
2211 C CE2 . TRP A 279 ? 0.24207 0.24128 0.22148 0.00337  0.01683  -0.00206 273 TRP A CE2 
2212 C CE3 . TRP A 279 ? 0.18785 0.19329 0.17839 0.00680  0.02424  -0.01177 273 TRP A CE3 
2213 C CZ2 . TRP A 279 ? 0.20052 0.19871 0.18920 0.00736  0.01486  -0.00089 273 TRP A CZ2 
2214 C CZ3 . TRP A 279 ? 0.28613 0.28768 0.28436 0.01018  0.02106  -0.00903 273 TRP A CZ3 
2215 C CH2 . TRP A 279 ? 0.21530 0.21445 0.21212 0.00984  0.01710  -0.00378 273 TRP A CH2 
2216 N N   . ASN A 280 ? 0.31152 0.34520 0.26084 -0.01783 0.04186  -0.03126 274 ASN A N   
2217 C CA  . ASN A 280 ? 0.26221 0.31074 0.21006 -0.02196 0.04996  -0.03983 274 ASN A CA  
2218 C C   . ASN A 280 ? 0.41481 0.46859 0.36820 -0.01811 0.05395  -0.05298 274 ASN A C   
2219 O O   . ASN A 280 ? 0.39292 0.46131 0.35001 -0.01899 0.06128  -0.06291 274 ASN A O   
2220 C CB  . ASN A 280 ? 0.34587 0.39820 0.27376 -0.03451 0.05088  -0.03588 274 ASN A CB  
2221 C CG  . ASN A 280 ? 0.32909 0.37932 0.24279 -0.03984 0.04965  -0.03912 274 ASN A CG  
2222 O OD1 . ASN A 280 ? 0.34239 0.38136 0.25609 -0.03608 0.04350  -0.03691 274 ASN A OD1 
2223 N ND2 . ASN A 280 ? 0.40352 0.46609 0.30477 -0.04946 0.05568  -0.04480 274 ASN A ND2 
2224 N N   . ARG A 281 ? 0.36871 0.41169 0.32310 -0.01414 0.04928  -0.05409 275 ARG A N   
2225 C CA  . ARG A 281 ? 0.43939 0.48393 0.40179 -0.00882 0.05169  -0.06675 275 ARG A CA  
2226 C C   . ARG A 281 ? 0.38708 0.42677 0.36927 0.00191  0.04964  -0.06854 275 ARG A C   
2227 O O   . ARG A 281 ? 0.37595 0.42005 0.36907 0.00767  0.05252  -0.08009 275 ARG A O   
2228 C CB  . ARG A 281 ? 0.40689 0.44157 0.36006 -0.01096 0.04713  -0.06760 275 ARG A CB  
2229 C CG  . ARG A 281 ? 0.38659 0.42367 0.31905 -0.02174 0.04695  -0.06501 275 ARG A CG  
2230 C CD  . ARG A 281 ? 0.58446 0.61762 0.51079 -0.02303 0.04559  -0.07321 275 ARG A CD  
2231 N NE  . ARG A 281 ? 0.63709 0.65662 0.57250 -0.01679 0.03863  -0.07013 275 ARG A NE  
2232 C CZ  . ARG A 281 ? 0.62513 0.63676 0.55283 -0.01986 0.03293  -0.06848 275 ARG A CZ  
2233 N NH1 . ARG A 281 ? 0.46207 0.47647 0.37213 -0.02867 0.03221  -0.06849 275 ARG A NH1 
2234 N NH2 . ARG A 281 ? 0.55908 0.56029 0.49647 -0.01491 0.02738  -0.06626 275 ARG A NH2 
2235 N N   . LEU A 282 ? 0.30109 0.33143 0.28788 0.00462  0.04411  -0.05768 276 LEU A N   
2236 C CA  . LEU A 282 ? 0.28578 0.31198 0.28927 0.01302  0.04168  -0.05749 276 LEU A CA  
2237 C C   . LEU A 282 ? 0.29363 0.33219 0.30672 0.01542  0.04629  -0.06018 276 LEU A C   
2238 O O   . LEU A 282 ? 0.37247 0.41184 0.40065 0.02294  0.04566  -0.06559 276 LEU A O   
2239 C CB  . LEU A 282 ? 0.37084 0.38650 0.37499 0.01362  0.03541  -0.04554 276 LEU A CB  
2240 C CG  . LEU A 282 ? 0.34723 0.35102 0.34923 0.01357  0.02967  -0.04319 276 LEU A CG  
2241 C CD1 . LEU A 282 ? 0.40425 0.40300 0.40729 0.01328  0.02517  -0.03225 276 LEU A CD1 
2242 C CD2 . LEU A 282 ? 0.40211 0.39904 0.41415 0.01897  0.02751  -0.05031 276 LEU A CD2 
2243 N N   . PHE A 283 ? 0.34665 0.39443 0.35143 0.00882  0.05003  -0.05621 277 PHE A N   
2244 C CA  . PHE A 283 ? 0.34830 0.40907 0.36125 0.00925  0.05421  -0.05735 277 PHE A CA  
2245 C C   . PHE A 283 ? 0.26019 0.33623 0.26258 0.00041  0.06149  -0.06217 277 PHE A C   
2246 O O   . PHE A 283 ? 0.30120 0.37979 0.29329 -0.00752 0.06217  -0.05435 277 PHE A O   
2247 C CB  . PHE A 283 ? 0.28030 0.33571 0.29344 0.00847  0.05038  -0.04514 277 PHE A CB  
2248 C CG  . PHE A 283 ? 0.28831 0.32978 0.30797 0.01446  0.04355  -0.03927 277 PHE A CG  
2249 C CD1 . PHE A 283 ? 0.31143 0.35135 0.34638 0.02227  0.04126  -0.04238 277 PHE A CD1 
2250 C CD2 . PHE A 283 ? 0.22783 0.25848 0.23842 0.01180  0.03898  -0.03066 277 PHE A CD2 
2251 C CE1 . PHE A 283 ? 0.33980 0.36728 0.37855 0.02561  0.03489  -0.03611 277 PHE A CE1 
2252 C CE2 . PHE A 283 ? 0.26365 0.28448 0.27979 0.01582  0.03364  -0.02581 277 PHE A CE2 
2253 C CZ  . PHE A 283 ? 0.25709 0.27617 0.28614 0.02186  0.03178  -0.02807 277 PHE A CZ  
2254 N N   . PRO A 284 ? 0.34202 0.42845 0.34612 0.00089  0.06688  -0.07538 278 PRO A N   
2255 C CA  . PRO A 284 ? 0.30210 0.40481 0.29361 -0.00961 0.07445  -0.08036 278 PRO A CA  
2256 C C   . PRO A 284 ? 0.40320 0.52371 0.40007 -0.01350 0.07995  -0.08056 278 PRO A C   
2257 O O   . PRO A 284 ? 0.39608 0.52557 0.37935 -0.02496 0.08328  -0.07844 278 PRO A O   
2258 C CB  . PRO A 284 ? 0.34612 0.45681 0.34191 -0.00610 0.07909  -0.09691 278 PRO A CB  
2259 C CG  . PRO A 284 ? 0.28170 0.38414 0.29831 0.00781  0.07465  -0.10175 278 PRO A CG  
2260 C CD  . PRO A 284 ? 0.32348 0.40683 0.34031 0.01041  0.06596  -0.08673 278 PRO A CD  
2261 N N   . ASN A 285 ? 0.32184 0.44508 0.33768 -0.00495 0.07858  -0.08087 279 ASN A N   
2262 C CA  . ASN A 285 ? 0.41854 0.55658 0.44084 -0.00829 0.08141  -0.07939 279 ASN A CA  
2263 C C   . ASN A 285 ? 0.41273 0.54424 0.42840 -0.01364 0.07848  -0.06563 279 ASN A C   
2264 O O   . ASN A 285 ? 0.30420 0.44775 0.32176 -0.01910 0.08109  -0.06351 279 ASN A O   
2265 C CB  . ASN A 285 ? 0.37126 0.51534 0.41769 0.00366  0.07980  -0.08660 279 ASN A CB  
2266 C CG  . ASN A 285 ? 0.42585 0.57890 0.47935 0.00733  0.08211  -0.09982 279 ASN A CG  
2267 O OD1 . ASN A 285 ? 0.46834 0.61221 0.52826 0.01584  0.07921  -0.10631 279 ASN A OD1 
2268 N ND2 . ASN A 285 ? 0.48610 0.65711 0.53872 0.00057  0.08703  -0.10418 279 ASN A ND2 
2269 N N   . ALA A 286 ? 0.20761 0.31750 0.21562 -0.01206 0.07091  -0.05510 280 ALA A N   
2270 C CA  . ALA A 286 ? 0.35336 0.45348 0.35794 -0.01438 0.06585  -0.04244 280 ALA A CA  
2271 C C   . ALA A 286 ? 0.25418 0.35529 0.24002 -0.02786 0.06689  -0.03533 280 ALA A C   
2272 O O   . ALA A 286 ? 0.27140 0.37294 0.24208 -0.03555 0.06863  -0.03625 280 ALA A O   
2273 C CB  . ALA A 286 ? 0.32205 0.40126 0.32520 -0.00849 0.05793  -0.03502 280 ALA A CB  
2274 N N   . ASP A 287 ? 0.29861 0.39908 0.28486 -0.03128 0.06502  -0.02788 281 ASP A N   
2275 C CA  . ASP A 287 ? 0.28239 0.37780 0.25060 -0.04375 0.06318  -0.01878 281 ASP A CA  
2276 C C   . ASP A 287 ? 0.27085 0.34554 0.22482 -0.04438 0.05589  -0.01122 281 ASP A C   
2277 O O   . ASP A 287 ? 0.28704 0.34896 0.24725 -0.03515 0.05060  -0.00886 281 ASP A O   
2278 C CB  . ASP A 287 ? 0.27971 0.37345 0.25279 -0.04492 0.06051  -0.01217 281 ASP A CB  
2279 C CG  . ASP A 287 ? 0.28154 0.36980 0.23678 -0.05865 0.05817  -0.00321 281 ASP A CG  
2280 O OD1 . ASP A 287 ? 0.39297 0.46304 0.33389 -0.06144 0.05158  0.00432  281 ASP A OD1 
2281 O OD2 . ASP A 287 ? 0.28959 0.39152 0.24561 -0.06682 0.06218  -0.00357 281 ASP A OD2 
2282 N N   . SER A 288 ? 0.24840 0.32071 0.18319 -0.05588 0.05525  -0.00738 282 SER A N   
2283 C CA  . SER A 288 ? 0.29663 0.35010 0.21856 -0.05638 0.04719  -0.00035 282 SER A CA  
2284 C C   . SER A 288 ? 0.27751 0.31354 0.20004 -0.05299 0.03857  0.00919  282 SER A C   
2285 O O   . SER A 288 ? 0.29578 0.31818 0.21827 -0.04674 0.03198  0.01223  282 SER A O   
2286 C CB  . SER A 288 ? 0.30496 0.35876 0.20490 -0.07060 0.04691  0.00298  282 SER A CB  
2287 O OG  . SER A 288 ? 0.39203 0.44589 0.28197 -0.08218 0.04597  0.01014  282 SER A OG  
2288 N N   . LYS A 289 ? 0.23577 0.27298 0.15946 -0.05708 0.03851  0.01312  283 LYS A N   
2289 C CA  . LYS A 289 ? 0.28628 0.30742 0.21159 -0.05314 0.03067  0.02030  283 LYS A CA  
2290 C C   . LYS A 289 ? 0.26608 0.28699 0.20915 -0.03976 0.03068  0.01661  283 LYS A C   
2291 O O   . LYS A 289 ? 0.27347 0.28130 0.21820 -0.03389 0.02427  0.02017  283 LYS A O   
2292 C CB  . LYS A 289 ? 0.33703 0.35906 0.25824 -0.06191 0.03041  0.02499  283 LYS A CB  
2293 C CG  . LYS A 289 ? 0.40561 0.42667 0.30709 -0.07756 0.02954  0.03025  283 LYS A CG  
2294 C CD  . LYS A 289 ? 0.32473 0.34469 0.22172 -0.08723 0.02821  0.03572  283 LYS A CD  
2295 C CE  . LYS A 289 ? 0.37714 0.39493 0.25437 -0.10343 0.02597  0.04135  283 LYS A CE  
2296 N NZ  . LYS A 289 ? 0.51326 0.52994 0.38939 -0.11143 0.02331  0.04489  283 LYS A NZ  
2297 N N   . ALA A 290 ? 0.25008 0.28572 0.20664 -0.03509 0.03740  0.00929  284 ALA A N   
2298 C CA  . ALA A 290 ? 0.30057 0.33505 0.27215 -0.02372 0.03658  0.00663  284 ALA A CA  
2299 C C   . ALA A 290 ? 0.25032 0.27628 0.22106 -0.01807 0.03343  0.00582  284 ALA A C   
2300 O O   . ALA A 290 ? 0.20376 0.22198 0.18007 -0.01163 0.02938  0.00782  284 ALA A O   
2301 C CB  . ALA A 290 ? 0.19779 0.24820 0.18372 -0.01988 0.04277  -0.00092 284 ALA A CB  
2302 N N   . LEU A 291 ? 0.26921 0.29777 0.23268 -0.02125 0.03542  0.00253  285 LEU A N   
2303 C CA  . LEU A 291 ? 0.24040 0.26175 0.20277 -0.01692 0.03222  0.00153  285 LEU A CA  
2304 C C   . LEU A 291 ? 0.24465 0.25230 0.19867 -0.01768 0.02434  0.00876  285 LEU A C   
2305 O O   . LEU A 291 ? 0.27529 0.27728 0.23377 -0.01186 0.02058  0.00896  285 LEU A O   
2306 C CB  . LEU A 291 ? 0.24340 0.27130 0.19883 -0.02104 0.03615  -0.00436 285 LEU A CB  
2307 C CG  . LEU A 291 ? 0.26105 0.30256 0.22789 -0.01767 0.04334  -0.01412 285 LEU A CG  
2308 C CD1 . LEU A 291 ? 0.31169 0.35874 0.27167 -0.02084 0.04693  -0.02158 285 LEU A CD1 
2309 C CD2 . LEU A 291 ? 0.27502 0.31330 0.25780 -0.00734 0.04163  -0.01596 285 LEU A CD2 
2310 N N   . ASP A 292 ? 0.27210 0.27443 0.21457 -0.02495 0.02123  0.01451  286 ASP A N   
2311 C CA  . ASP A 292 ? 0.29203 0.28003 0.22856 -0.02431 0.01225  0.02090  286 ASP A CA  
2312 C C   . ASP A 292 ? 0.31327 0.29722 0.26157 -0.01622 0.00968  0.02150  286 ASP A C   
2313 O O   . ASP A 292 ? 0.21035 0.18792 0.16194 -0.01067 0.00432  0.02222  286 ASP A O   
2314 C CB  . ASP A 292 ? 0.32579 0.30669 0.24722 -0.03437 0.00835  0.02742  286 ASP A CB  
2315 C CG  . ASP A 292 ? 0.34661 0.31072 0.26183 -0.03320 -0.00276 0.03370  286 ASP A CG  
2316 O OD1 . ASP A 292 ? 0.41470 0.37402 0.32234 -0.03448 -0.00760 0.03528  286 ASP A OD1 
2317 O OD2 . ASP A 292 ? 0.30988 0.26560 0.22832 -0.03069 -0.00718 0.03652  286 ASP A OD2 
2318 N N   . LEU A 293 ? 0.18586 0.17507 0.14082 -0.01583 0.01354  0.02066  287 LEU A N   
2319 C CA  . LEU A 293 ? 0.18286 0.16978 0.14783 -0.00915 0.01177  0.02060  287 LEU A CA  
2320 C C   . LEU A 293 ? 0.17709 0.16926 0.15288 -0.00203 0.01386  0.01657  287 LEU A C   
2321 O O   . LEU A 293 ? 0.24304 0.23204 0.22388 0.00300  0.01065  0.01661  287 LEU A O   
2322 C CB  . LEU A 293 ? 0.14648 0.13831 0.11494 -0.01155 0.01496  0.02091  287 LEU A CB  
2323 C CG  . LEU A 293 ? 0.20942 0.19997 0.18651 -0.00623 0.01356  0.02066  287 LEU A CG  
2324 C CD1 . LEU A 293 ? 0.19744 0.17659 0.17231 -0.00286 0.00679  0.02217  287 LEU A CD1 
2325 C CD2 . LEU A 293 ? 0.24236 0.23633 0.22003 -0.01056 0.01531  0.02185  287 LEU A CD2 
2326 N N   . LEU A 294 ? 0.18669 0.18710 0.16618 -0.00191 0.01899  0.01264  288 LEU A N   
2327 C CA  . LEU A 294 ? 0.12630 0.12920 0.11457 0.00358  0.01985  0.00947  288 LEU A CA  
2328 C C   . LEU A 294 ? 0.21181 0.20922 0.19767 0.00537  0.01539  0.01020  288 LEU A C   
2329 O O   . LEU A 294 ? 0.17989 0.17727 0.17243 0.00934  0.01373  0.01005  288 LEU A O   
2330 C CB  . LEU A 294 ? 0.15307 0.16298 0.14412 0.00329  0.02465  0.00430  288 LEU A CB  
2331 C CG  . LEU A 294 ? 0.21242 0.22241 0.21177 0.00816  0.02460  0.00106  288 LEU A CG  
2332 C CD1 . LEU A 294 ? 0.17170 0.18225 0.18059 0.01186  0.02372  0.00280  288 LEU A CD1 
2333 C CD2 . LEU A 294 ? 0.23867 0.25385 0.24019 0.00834  0.02850  -0.00554 288 LEU A CD2 
2334 N N   . ASP A 295 ? 0.22663 0.22049 0.20268 0.00168  0.01316  0.01110  289 ASP A N   
2335 C CA  . ASP A 295 ? 0.20270 0.19228 0.17686 0.00322  0.00795  0.01180  289 ASP A CA  
2336 C C   . ASP A 295 ? 0.23991 0.22548 0.21832 0.00720  0.00280  0.01408  289 ASP A C   
2337 O O   . ASP A 295 ? 0.21518 0.20251 0.19972 0.01093  0.00037  0.01272  289 ASP A O   
2338 C CB  . ASP A 295 ? 0.24216 0.22774 0.20321 -0.00249 0.00519  0.01354  289 ASP A CB  
2339 C CG  . ASP A 295 ? 0.29842 0.28004 0.25790 -0.00092 -0.00137 0.01447  289 ASP A CG  
2340 O OD1 . ASP A 295 ? 0.25617 0.24172 0.22013 0.00083  -0.00018 0.01100  289 ASP A OD1 
2341 O OD2 . ASP A 295 ? 0.30637 0.28056 0.26061 -0.00147 -0.00849 0.01865  289 ASP A OD2 
2342 N N   . LYS A 296 ? 0.21924 0.20023 0.19496 0.00623  0.00113  0.01676  290 LYS A N   
2343 C CA  . LYS A 296 ? 0.26403 0.24058 0.24392 0.01061  -0.00413 0.01734  290 LYS A CA  
2344 C C   . LYS A 296 ? 0.20036 0.18415 0.19130 0.01497  -0.00073 0.01430  290 LYS A C   
2345 O O   . LYS A 296 ? 0.20069 0.18586 0.19778 0.01940  -0.00369 0.01226  290 LYS A O   
2346 C CB  . LYS A 296 ? 0.24490 0.21200 0.21733 0.00752  -0.00783 0.02095  290 LYS A CB  
2347 C CG  . LYS A 296 ? 0.27927 0.23677 0.23953 0.00287  -0.01422 0.02521  290 LYS A CG  
2348 C CD  A LYS A 296 ? 0.26899 0.21504 0.22046 -0.00179 -0.01884 0.02983  290 LYS A CD  
2349 C CD  B LYS A 296 ? 0.26698 0.21465 0.21690 -0.00348 -0.01725 0.03004  290 LYS A CD  
2350 C CE  A LYS A 296 ? 0.37110 0.30480 0.30977 -0.00650 -0.02783 0.03533  290 LYS A CE  
2351 C CE  B LYS A 296 ? 0.36366 0.30097 0.29948 -0.00961 -0.02461 0.03548  290 LYS A CE  
2352 N NZ  A LYS A 296 ? 0.36010 0.29931 0.28937 -0.01333 -0.02440 0.03642  290 LYS A NZ  
2353 N NZ  B LYS A 296 ? 0.36193 0.28670 0.28611 -0.01701 -0.02974 0.04150  290 LYS A NZ  
2354 N N   . MET A 297 ? 0.19541 0.18477 0.18915 0.01357  0.00511  0.01368  291 MET A N   
2355 C CA  . MET A 297 ? 0.22275 0.21843 0.22496 0.01618  0.00759  0.01196  291 MET A CA  
2356 C C   . MET A 297 ? 0.17407 0.17493 0.18123 0.01732  0.00839  0.01025  291 MET A C   
2357 O O   . MET A 297 ? 0.19265 0.19869 0.20550 0.01885  0.00843  0.00896  291 MET A O   
2358 C CB  A MET A 297 ? 0.14886 0.14753 0.15256 0.01430  0.01170  0.01271  291 MET A CB  
2359 C CB  B MET A 297 ? 0.15571 0.15437 0.15937 0.01428  0.01171  0.01270  291 MET A CB  
2360 C CG  A MET A 297 ? 0.14741 0.14301 0.14842 0.01285  0.01092  0.01412  291 MET A CG  
2361 C CG  B MET A 297 ? 0.15727 0.15216 0.15576 0.01140  0.01141  0.01456  291 MET A CG  
2362 S SD  A MET A 297 ? 0.15434 0.15604 0.15937 0.01092  0.01490  0.01477  291 MET A SD  
2363 S SD  B MET A 297 ? 0.22186 0.22352 0.22442 0.00932  0.01597  0.01476  291 MET A SD  
2364 C CE  A MET A 297 ? 0.18604 0.19147 0.19077 0.00908  0.01834  0.01371  291 MET A CE  
2365 C CE  B MET A 297 ? 0.15185 0.14963 0.15149 0.00726  0.01383  0.01652  291 MET A CE  
2366 N N   . LEU A 298 ? 0.17875 0.17882 0.18329 0.01569  0.00916  0.00986  292 LEU A N   
2367 C CA  . LEU A 298 ? 0.15537 0.15852 0.16360 0.01578  0.00915  0.00834  292 LEU A CA  
2368 C C   . LEU A 298 ? 0.25198 0.25477 0.25876 0.01635  0.00492  0.00766  292 LEU A C   
2369 O O   . LEU A 298 ? 0.21550 0.21795 0.22044 0.01478  0.00423  0.00661  292 LEU A O   
2370 C CB  . LEU A 298 ? 0.15359 0.15566 0.16088 0.01420  0.01189  0.00699  292 LEU A CB  
2371 C CG  . LEU A 298 ? 0.17740 0.18087 0.18927 0.01472  0.01477  0.00726  292 LEU A CG  
2372 C CD1 . LEU A 298 ? 0.18482 0.18727 0.19776 0.01470  0.01670  0.00418  292 LEU A CD1 
2373 C CD2 . LEU A 298 ? 0.15054 0.15656 0.16801 0.01497  0.01395  0.00895  292 LEU A CD2 
2374 N N   . THR A 299 ? 0.20717 0.20982 0.21525 0.01890  0.00138  0.00776  293 THR A N   
2375 C CA  . THR A 299 ? 0.23431 0.23774 0.24368 0.02073  -0.00401 0.00679  293 THR A CA  
2376 C C   . THR A 299 ? 0.31431 0.32830 0.33313 0.02173  -0.00334 0.00399  293 THR A C   
2377 O O   . THR A 299 ? 0.14766 0.16775 0.17192 0.02246  -0.00055 0.00267  293 THR A O   
2378 C CB  . THR A 299 ? 0.23848 0.23654 0.24696 0.02402  -0.00921 0.00731  293 THR A CB  
2379 O OG1 . THR A 299 ? 0.28926 0.27706 0.28671 0.02084  -0.01124 0.01100  293 THR A OG1 
2380 C CG2 . THR A 299 ? 0.18888 0.19032 0.20352 0.02807  -0.01559 0.00501  293 THR A CG2 
2381 N N   . PHE A 300 ? 0.20767 0.22470 0.22764 0.02060  -0.00584 0.00310  294 PHE A N   
2382 C CA  . PHE A 300 ? 0.18357 0.21195 0.21192 0.01948  -0.00491 0.00074  294 PHE A CA  
2383 C C   . PHE A 300 ? 0.18354 0.22203 0.22120 0.02353  -0.00603 -0.00277 294 PHE A C   
2384 O O   . PHE A 300 ? 0.19689 0.24525 0.23992 0.02183  -0.00213 -0.00450 294 PHE A O   
2385 C CB  . PHE A 300 ? 0.14963 0.17953 0.17754 0.01735  -0.00846 0.00019  294 PHE A CB  
2386 C CG  . PHE A 300 ? 0.17033 0.21298 0.20678 0.01476  -0.00789 -0.00204 294 PHE A CG  
2387 C CD1 . PHE A 300 ? 0.18528 0.22821 0.22075 0.00910  -0.00435 -0.00091 294 PHE A CD1 
2388 C CD2 . PHE A 300 ? 0.25958 0.31424 0.30552 0.01766  -0.01140 -0.00543 294 PHE A CD2 
2389 C CE1 . PHE A 300 ? 0.25306 0.30764 0.29499 0.00467  -0.00403 -0.00213 294 PHE A CE1 
2390 C CE2 . PHE A 300 ? 0.26481 0.33415 0.31896 0.01394  -0.01022 -0.00783 294 PHE A CE2 
2391 C CZ  . PHE A 300 ? 0.20857 0.27768 0.25976 0.00658  -0.00636 -0.00569 294 PHE A CZ  
2392 N N   . ASN A 301 ? 0.20350 0.23966 0.24298 0.02866  -0.01176 -0.00419 295 ASN A N   
2393 C CA  . ASN A 301 ? 0.19255 0.23869 0.24290 0.03415  -0.01377 -0.00956 295 ASN A CA  
2394 C C   . ASN A 301 ? 0.19245 0.23533 0.24172 0.03609  -0.01077 -0.01052 295 ASN A C   
2395 O O   . ASN A 301 ? 0.21403 0.24320 0.25613 0.03751  -0.01334 -0.00769 295 ASN A O   
2396 C CB  . ASN A 301 ? 0.21043 0.25259 0.26370 0.03986  -0.02294 -0.01070 295 ASN A CB  
2397 C CG  . ASN A 301 ? 0.31038 0.36464 0.37815 0.04713  -0.02598 -0.01826 295 ASN A CG  
2398 O OD1 . ASN A 301 ? 0.24357 0.30284 0.31564 0.04933  -0.02214 -0.02247 295 ASN A OD1 
2399 N ND2 . ASN A 301 ? 0.31543 0.37546 0.39142 0.05106  -0.03316 -0.02080 295 ASN A ND2 
2400 N N   . PRO A 302 ? 0.20948 0.26483 0.26469 0.03515  -0.00557 -0.01434 296 PRO A N   
2401 C CA  . PRO A 302 ? 0.19096 0.24314 0.24385 0.03611  -0.00274 -0.01532 296 PRO A CA  
2402 C C   . PRO A 302 ? 0.24134 0.28727 0.29725 0.04353  -0.00827 -0.01936 296 PRO A C   
2403 O O   . PRO A 302 ? 0.21818 0.25422 0.26851 0.04388  -0.00808 -0.01816 296 PRO A O   
2404 C CB  . PRO A 302 ? 0.24871 0.31837 0.30731 0.03269  0.00323  -0.01932 296 PRO A CB  
2405 C CG  . PRO A 302 ? 0.23927 0.32328 0.30682 0.03246  0.00217  -0.02285 296 PRO A CG  
2406 C CD  . PRO A 302 ? 0.18239 0.25565 0.24520 0.03155  -0.00197 -0.01753 296 PRO A CD  
2407 N N   . HIS A 303 ? 0.19048 0.24140 0.25565 0.04955  -0.01408 -0.02427 297 HIS A N   
2408 C CA  . HIS A 303 ? 0.16396 0.20612 0.23273 0.05751  -0.02138 -0.02824 297 HIS A CA  
2409 C C   . HIS A 303 ? 0.19264 0.21244 0.24966 0.05683  -0.02805 -0.02050 297 HIS A C   
2410 O O   . HIS A 303 ? 0.31162 0.31841 0.36655 0.06061  -0.03352 -0.02111 297 HIS A O   
2411 C CB  . HIS A 303 ? 0.27278 0.32720 0.35665 0.06496  -0.02690 -0.03604 297 HIS A CB  
2412 C CG  . HIS A 303 ? 0.27764 0.35727 0.37342 0.06456  -0.01987 -0.04458 297 HIS A CG  
2413 N ND1 . HIS A 303 ? 0.38859 0.48468 0.48927 0.05989  -0.01656 -0.04458 297 HIS A ND1 
2414 C CD2 . HIS A 303 ? 0.27807 0.37005 0.38094 0.06707  -0.01538 -0.05361 297 HIS A CD2 
2415 C CE1 . HIS A 303 ? 0.33078 0.44892 0.44081 0.05880  -0.01019 -0.05263 297 HIS A CE1 
2416 N NE2 . HIS A 303 ? 0.29966 0.41640 0.41109 0.06324  -0.00907 -0.05859 297 HIS A NE2 
2417 N N   . LYS A 304 ? 0.21338 0.22849 0.26205 0.05132  -0.02787 -0.01353 298 LYS A N   
2418 C CA  . LYS A 304 ? 0.27162 0.26829 0.30699 0.04811  -0.03244 -0.00601 298 LYS A CA  
2419 C C   . LYS A 304 ? 0.22607 0.21747 0.25110 0.04153  -0.02541 -0.00145 298 LYS A C   
2420 O O   . LYS A 304 ? 0.23092 0.20887 0.24494 0.03796  -0.02805 0.00400  298 LYS A O   
2421 C CB  . LYS A 304 ? 0.21212 0.20764 0.24320 0.04527  -0.03600 -0.00202 298 LYS A CB  
2422 C CG  . LYS A 304 ? 0.33552 0.33606 0.37688 0.05152  -0.04458 -0.00564 298 LYS A CG  
2423 C CD  . LYS A 304 ? 0.22123 0.22185 0.25722 0.04728  -0.04741 -0.00160 298 LYS A CD  
2424 C CE  . LYS A 304 ? 0.25344 0.25845 0.29963 0.05343  -0.05765 -0.00443 298 LYS A CE  
2425 N NZ  . LYS A 304 ? 0.33688 0.34553 0.37896 0.04853  -0.05932 -0.00153 298 LYS A NZ  
2426 N N   . ARG A 305 ? 0.24006 0.24239 0.26846 0.03932  -0.01708 -0.00339 299 ARG A N   
2427 C CA  . ARG A 305 ? 0.23040 0.22944 0.25142 0.03395  -0.01113 0.00043  299 ARG A CA  
2428 C C   . ARG A 305 ? 0.20012 0.18920 0.21686 0.03438  -0.01301 0.00110  299 ARG A C   
2429 O O   . ARG A 305 ? 0.21715 0.20628 0.23926 0.03909  -0.01572 -0.00363 299 ARG A O   
2430 C CB  . ARG A 305 ? 0.20012 0.21187 0.22625 0.03192  -0.00401 -0.00151 299 ARG A CB  
2431 C CG  . ARG A 305 ? 0.19659 0.20642 0.21714 0.02675  0.00108  0.00272  299 ARG A CG  
2432 C CD  . ARG A 305 ? 0.20294 0.22317 0.22793 0.02426  0.00575  0.00204  299 ARG A CD  
2433 N NE  . ARG A 305 ? 0.18075 0.20724 0.20949 0.02357  0.00517  0.00098  299 ARG A NE  
2434 C CZ  . ARG A 305 ? 0.20174 0.23947 0.23579 0.02156  0.00732  -0.00093 299 ARG A CZ  
2435 N NH1 . ARG A 305 ? 0.17770 0.22201 0.21318 0.01989  0.01037  -0.00200 299 ARG A NH1 
2436 N NH2 . ARG A 305 ? 0.12748 0.17059 0.16467 0.02011  0.00626  -0.00168 299 ARG A NH2 
2437 N N   . ILE A 306 ? 0.23466 0.21590 0.24201 0.02915  -0.01151 0.00626  300 ILE A N   
2438 C CA  . ILE A 306 ? 0.18838 0.15972 0.19043 0.02768  -0.01356 0.00780  300 ILE A CA  
2439 C C   . ILE A 306 ? 0.18032 0.15825 0.18764 0.02894  -0.00942 0.00392  300 ILE A C   
2440 O O   . ILE A 306 ? 0.21188 0.20110 0.22328 0.02788  -0.00347 0.00284  300 ILE A O   
2441 C CB  . ILE A 306 ? 0.20446 0.17074 0.19639 0.02044  -0.01134 0.01358  300 ILE A CB  
2442 C CG1 . ILE A 306 ? 0.23638 0.19115 0.22136 0.01722  -0.01485 0.01618  300 ILE A CG1 
2443 C CG2 . ILE A 306 ? 0.15246 0.12941 0.14706 0.01786  -0.00321 0.01350  300 ILE A CG2 
2444 C CD1 . ILE A 306 ? 0.25324 0.20507 0.22802 0.00884  -0.01287 0.02156  300 ILE A CD1 
2445 N N   . GLU A 307 ? 0.23647 0.20632 0.24291 0.03074  -0.01339 0.00186  301 GLU A N   
2446 C CA  . GLU A 307 ? 0.20460 0.17993 0.21421 0.03115  -0.00994 -0.00225 301 GLU A CA  
2447 C C   . GLU A 307 ? 0.16324 0.13435 0.16584 0.02477  -0.00752 0.00232  301 GLU A C   
2448 O O   . GLU A 307 ? 0.17350 0.13702 0.16901 0.02024  -0.00888 0.00782  301 GLU A O   
2449 C CB  . GLU A 307 ? 0.18773 0.15783 0.20162 0.03726  -0.01548 -0.00911 301 GLU A CB  
2450 C CG  . GLU A 307 ? 0.25692 0.23636 0.28104 0.04413  -0.01695 -0.01550 301 GLU A CG  
2451 C CD  . GLU A 307 ? 0.33534 0.31589 0.36702 0.05102  -0.02004 -0.02539 301 GLU A CD  
2452 O OE1 . GLU A 307 ? 0.35121 0.31991 0.37883 0.05106  -0.02337 -0.02670 301 GLU A OE1 
2453 O OE2 . GLU A 307 ? 0.30902 0.30338 0.35120 0.05616  -0.01895 -0.03264 301 GLU A OE2 
2454 N N   . VAL A 308 ? 0.22042 0.19799 0.22494 0.02377  -0.00394 -0.00027 302 VAL A N   
2455 C CA  . VAL A 308 ? 0.15072 0.12812 0.15079 0.01776  -0.00126 0.00385  302 VAL A CA  
2456 C C   . VAL A 308 ? 0.19180 0.15505 0.18465 0.01445  -0.00617 0.00631  302 VAL A C   
2457 O O   . VAL A 308 ? 0.22937 0.19120 0.21738 0.00846  -0.00496 0.01154  302 VAL A O   
2458 C CB  . VAL A 308 ? 0.19534 0.18237 0.19820 0.01695  0.00236  0.00086  302 VAL A CB  
2459 C CG1 . VAL A 308 ? 0.17782 0.16124 0.18108 0.01993  -0.00052 -0.00604 302 VAL A CG1 
2460 C CG2 . VAL A 308 ? 0.23741 0.22638 0.23758 0.01114  0.00456  0.00552  302 VAL A CG2 
2461 N N   . GLU A 309 ? 0.17987 0.13262 0.17214 0.01796  -0.01209 0.00228  303 GLU A N   
2462 C CA  . GLU A 309 ? 0.22797 0.16447 0.21222 0.01377  -0.01812 0.00530  303 GLU A CA  
2463 C C   . GLU A 309 ? 0.26259 0.18953 0.24005 0.01053  -0.02216 0.01179  303 GLU A C   
2464 O O   . GLU A 309 ? 0.23295 0.15118 0.20156 0.00276  -0.02439 0.01733  303 GLU A O   
2465 C CB  . GLU A 309 ? 0.25513 0.18069 0.24099 0.01906  -0.02463 -0.00152 303 GLU A CB  
2466 C CG  . GLU A 309 ? 0.22766 0.16050 0.21604 0.01899  -0.02099 -0.00746 303 GLU A CG  
2467 C CD  . GLU A 309 ? 0.27432 0.19896 0.26593 0.02557  -0.02648 -0.01700 303 GLU A CD  
2468 O OE1 . GLU A 309 ? 0.32880 0.24277 0.32295 0.03172  -0.03354 -0.01943 303 GLU A OE1 
2469 O OE2 . GLU A 309 ? 0.36599 0.29495 0.35785 0.02478  -0.02419 -0.02259 303 GLU A OE2 
2470 N N   . GLN A 310 ? 0.23506 0.16439 0.21568 0.01514  -0.02318 0.01139  304 GLN A N   
2471 C CA  . GLN A 310 ? 0.23026 0.15282 0.20298 0.01074  -0.02621 0.01788  304 GLN A CA  
2472 C C   . GLN A 310 ? 0.23625 0.16981 0.20572 0.00362  -0.01836 0.02204  304 GLN A C   
2473 O O   . GLN A 310 ? 0.21455 0.14298 0.17437 -0.00422 -0.01944 0.02759  304 GLN A O   
2474 C CB  . GLN A 310 ? 0.25949 0.18339 0.23676 0.01718  -0.02934 0.01613  304 GLN A CB  
2475 C CG  . GLN A 310 ? 0.30250 0.21834 0.28601 0.02583  -0.03752 0.01073  304 GLN A CG  
2476 C CD  . GLN A 310 ? 0.25091 0.17295 0.24102 0.03177  -0.03949 0.00873  304 GLN A CD  
2477 O OE1 . GLN A 310 ? 0.23331 0.17169 0.23236 0.03517  -0.03303 0.00424  304 GLN A OE1 
2478 N NE2 . GLN A 310 ? 0.33294 0.24181 0.31785 0.03195  -0.04899 0.01278  304 GLN A NE2 
2479 N N   . ALA A 311 ? 0.20217 0.15114 0.17965 0.00604  -0.01081 0.01911  305 ALA A N   
2480 C CA  . ALA A 311 ? 0.23019 0.18984 0.20725 0.00118  -0.00404 0.02147  305 ALA A CA  
2481 C C   . ALA A 311 ? 0.25654 0.21579 0.22892 -0.00640 -0.00275 0.02433  305 ALA A C   
2482 O O   . ALA A 311 ? 0.22129 0.18443 0.18901 -0.01283 0.00001  0.02724  305 ALA A O   
2483 C CB  . ALA A 311 ? 0.18253 0.15564 0.16933 0.00543  0.00169  0.01816  305 ALA A CB  
2484 N N   . LEU A 312 ? 0.23361 0.18939 0.20715 -0.00630 -0.00457 0.02290  306 LEU A N   
2485 C CA  . LEU A 312 ? 0.23023 0.18604 0.19973 -0.01416 -0.00392 0.02555  306 LEU A CA  
2486 C C   . LEU A 312 ? 0.22384 0.16767 0.18151 -0.02229 -0.00855 0.03074  306 LEU A C   
2487 O O   . LEU A 312 ? 0.24840 0.19752 0.20200 -0.03115 -0.00582 0.03388  306 LEU A O   
2488 C CB  . LEU A 312 ? 0.22405 0.17630 0.19571 -0.01265 -0.00618 0.02256  306 LEU A CB  
2489 C CG  . LEU A 312 ? 0.24564 0.21220 0.22625 -0.00931 -0.00105 0.01941  306 LEU A CG  
2490 C CD1 . LEU A 312 ? 0.20632 0.16874 0.18783 -0.00649 -0.00373 0.01488  306 LEU A CD1 
2491 C CD2 . LEU A 312 ? 0.20371 0.18193 0.18673 -0.01519 0.00319  0.02199  306 LEU A CD2 
2492 N N   . ALA A 313 ? 0.28387 0.21234 0.23603 -0.01996 -0.01595 0.03184  307 ALA A N   
2493 C CA  . ALA A 313 ? 0.27241 0.18645 0.21135 -0.02842 -0.02235 0.03810  307 ALA A CA  
2494 C C   . ALA A 313 ? 0.30923 0.22861 0.24219 -0.03278 -0.01988 0.04156  307 ALA A C   
2495 O O   . ALA A 313 ? 0.28552 0.19304 0.20560 -0.04072 -0.02567 0.04754  307 ALA A O   
2496 C CB  . ALA A 313 ? 0.35507 0.24799 0.29104 -0.02349 -0.03355 0.03786  307 ALA A CB  
2497 N N   . HIS A 314 ? 0.25933 0.19522 0.20025 -0.02853 -0.01208 0.03805  308 HIS A N   
2498 C CA  . HIS A 314 ? 0.27469 0.21615 0.20989 -0.03246 -0.00940 0.03982  308 HIS A CA  
2499 C C   . HIS A 314 ? 0.30987 0.25936 0.23722 -0.04486 -0.00473 0.04282  308 HIS A C   
2500 O O   . HIS A 314 ? 0.25834 0.21751 0.19114 -0.04739 -0.00004 0.04132  308 HIS A O   
2501 C CB  . HIS A 314 ? 0.28241 0.23827 0.22873 -0.02463 -0.00271 0.03441  308 HIS A CB  
2502 C CG  . HIS A 314 ? 0.31869 0.27825 0.25946 -0.02698 -0.00106 0.03479  308 HIS A CG  
2503 N ND1 . HIS A 314 ? 0.27273 0.24434 0.20984 -0.03419 0.00565  0.03415  308 HIS A ND1 
2504 C CD2 . HIS A 314 ? 0.25364 0.20752 0.19209 -0.02327 -0.00530 0.03499  308 HIS A CD2 
2505 C CE1 . HIS A 314 ? 0.29674 0.26901 0.22822 -0.03512 0.00565  0.03380  308 HIS A CE1 
2506 N NE2 . HIS A 314 ? 0.26780 0.22902 0.19981 -0.02875 -0.00127 0.03483  308 HIS A NE2 
2507 N N   . PRO A 315 ? 0.29112 0.23825 0.20558 -0.05343 -0.00596 0.04688  309 PRO A N   
2508 C CA  . PRO A 315 ? 0.28258 0.24011 0.18882 -0.06689 -0.00076 0.04915  309 PRO A CA  
2509 C C   . PRO A 315 ? 0.29121 0.27314 0.20990 -0.06534 0.01065  0.04234  309 PRO A C   
2510 O O   . PRO A 315 ? 0.27272 0.26626 0.18998 -0.07474 0.01531  0.04258  309 PRO A O   
2511 C CB  . PRO A 315 ? 0.35340 0.30628 0.24416 -0.07464 -0.00342 0.05330  309 PRO A CB  
2512 C CG  . PRO A 315 ? 0.37443 0.30569 0.26184 -0.06787 -0.01486 0.05677  309 PRO A CG  
2513 C CD  . PRO A 315 ? 0.29533 0.22936 0.20076 -0.05260 -0.01342 0.05022  309 PRO A CD  
2514 N N   . TYR A 316 ? 0.25617 0.24628 0.18751 -0.05404 0.01466  0.03623  310 TYR A N   
2515 C CA  . TYR A 316 ? 0.30162 0.31245 0.24627 -0.05114 0.02361  0.02964  310 TYR A CA  
2516 C C   . TYR A 316 ? 0.28460 0.30073 0.23791 -0.05131 0.02449  0.02942  310 TYR A C   
2517 O O   . TYR A 316 ? 0.26001 0.29411 0.22131 -0.05379 0.03081  0.02567  310 TYR A O   
2518 C CB  . TYR A 316 ? 0.21675 0.23050 0.17272 -0.03901 0.02534  0.02438  310 TYR A CB  
2519 C CG  . TYR A 316 ? 0.24879 0.28098 0.21899 -0.03494 0.03266  0.01757  310 TYR A CG  
2520 C CD1 . TYR A 316 ? 0.28326 0.33140 0.25330 -0.04074 0.03934  0.01321  310 TYR A CD1 
2521 C CD2 . TYR A 316 ? 0.25552 0.28949 0.23940 -0.02554 0.03239  0.01521  310 TYR A CD2 
2522 C CE1 . TYR A 316 ? 0.27700 0.34191 0.26225 -0.03556 0.04503  0.00580  310 TYR A CE1 
2523 C CE2 . TYR A 316 ? 0.25009 0.29875 0.24753 -0.02125 0.03712  0.00949  310 TYR A CE2 
2524 C CZ  . TYR A 316 ? 0.30523 0.36909 0.30436 -0.02545 0.04317  0.00438  310 TYR A CZ  
2525 O OH  . TYR A 316 ? 0.25060 0.32901 0.26537 -0.01974 0.04693  -0.00249 310 TYR A OH  
2526 N N   . LEU A 317 ? 0.24891 0.25047 0.20127 -0.04862 0.01800  0.03267  311 LEU A N   
2527 C CA  . LEU A 317 ? 0.28493 0.28977 0.24477 -0.04822 0.01786  0.03227  311 LEU A CA  
2528 C C   . LEU A 317 ? 0.25844 0.25508 0.20758 -0.05964 0.01385  0.03750  311 LEU A C   
2529 O O   . LEU A 317 ? 0.27052 0.26408 0.22291 -0.05969 0.01136  0.03787  311 LEU A O   
2530 C CB  . LEU A 317 ? 0.24752 0.24343 0.21394 -0.03761 0.01401  0.03077  311 LEU A CB  
2531 C CG  . LEU A 317 ? 0.20486 0.20841 0.18188 -0.02758 0.01734  0.02640  311 LEU A CG  
2532 C CD1 . LEU A 317 ? 0.24800 0.24443 0.22969 -0.01973 0.01384  0.02529  311 LEU A CD1 
2533 C CD2 . LEU A 317 ? 0.21340 0.23553 0.20175 -0.02682 0.02355  0.02281  311 LEU A CD2 
2534 N N   . GLU A 318 ? 0.22450 0.21727 0.15992 -0.07036 0.01281  0.04176  312 GLU A N   
2535 C CA  . GLU A 318 ? 0.28865 0.26879 0.21103 -0.08249 0.00696  0.04825  312 GLU A CA  
2536 C C   . GLU A 318 ? 0.35255 0.34717 0.28010 -0.09029 0.01101  0.04759  312 GLU A C   
2537 O O   . GLU A 318 ? 0.31342 0.29622 0.23447 -0.09731 0.00532  0.05172  312 GLU A O   
2538 C CB  . GLU A 318 ? 0.31595 0.29068 0.22119 -0.09418 0.00514  0.05376  312 GLU A CB  
2539 C CG  . GLU A 318 ? 0.51147 0.46458 0.40013 -0.10594 -0.00457 0.06233  312 GLU A CG  
2540 C CD  . GLU A 318 ? 0.49370 0.44749 0.36947 -0.11580 -0.00648 0.06480  312 GLU A CD  
2541 O OE1 . GLU A 318 ? 0.36761 0.32883 0.24155 -0.11413 -0.00267 0.06307  312 GLU A OE1 
2542 O OE2 . GLU A 318 ? 0.58802 0.53502 0.45494 -0.12578 -0.01205 0.06828  312 GLU A OE2 
2543 N N   . GLN A 319 ? 0.31533 0.33531 0.25516 -0.08909 0.02012  0.04203  313 GLN A N   
2544 C CA  . GLN A 319 ? 0.36319 0.40024 0.31047 -0.09594 0.02385  0.04070  313 GLN A CA  
2545 C C   . GLN A 319 ? 0.35115 0.38206 0.30667 -0.08956 0.01966  0.04011  313 GLN A C   
2546 O O   . GLN A 319 ? 0.28800 0.32522 0.24514 -0.09741 0.01930  0.04123  313 GLN A O   
2547 C CB  . GLN A 319 ? 0.27459 0.34046 0.23657 -0.09295 0.03358  0.03326  313 GLN A CB  
2548 C CG  . GLN A 319 ? 0.34698 0.42243 0.30122 -0.09951 0.03909  0.03181  313 GLN A CG  
2549 C CD  . GLN A 319 ? 0.35391 0.45584 0.32480 -0.09298 0.04812  0.02210  313 GLN A CD  
2550 O OE1 . GLN A 319 ? 0.24390 0.34475 0.22530 -0.07917 0.04847  0.01756  313 GLN A OE1 
2551 N NE2 . GLN A 319 ? 0.44975 0.57011 0.42419 -0.09858 0.05218  0.01726  313 GLN A NE2 
2552 N N   . TYR A 320 ? 0.25894 0.27869 0.21906 -0.07652 0.01656  0.03820  314 TYR A N   
2553 C CA  . TYR A 320 ? 0.26775 0.28494 0.23599 -0.06992 0.01376  0.03641  314 TYR A CA  
2554 C C   . TYR A 320 ? 0.37281 0.36537 0.33239 -0.06701 0.00569  0.03831  314 TYR A C   
2555 O O   . TYR A 320 ? 0.31136 0.30020 0.27373 -0.06538 0.00272  0.03707  314 TYR A O   
2556 C CB  . TYR A 320 ? 0.26839 0.29703 0.25110 -0.05727 0.01751  0.03140  314 TYR A CB  
2557 C CG  . TYR A 320 ? 0.32397 0.37693 0.31911 -0.05750 0.02428  0.02774  314 TYR A CG  
2558 C CD1 . TYR A 320 ? 0.35010 0.41832 0.35425 -0.06156 0.02544  0.02675  314 TYR A CD1 
2559 C CD2 . TYR A 320 ? 0.28766 0.34884 0.28627 -0.05350 0.02909  0.02447  314 TYR A CD2 
2560 C CE1 . TYR A 320 ? 0.29478 0.38664 0.31283 -0.06052 0.03104  0.02214  314 TYR A CE1 
2561 C CE2 . TYR A 320 ? 0.28701 0.37060 0.29850 -0.05257 0.03499  0.01935  314 TYR A CE2 
2562 C CZ  . TYR A 320 ? 0.26380 0.36308 0.28577 -0.05563 0.03586  0.01800  314 TYR A CZ  
2563 O OH  . TYR A 320 ? 0.32334 0.44626 0.36060 -0.05345 0.04116  0.01171  314 TYR A OH  
2564 N N   . TYR A 321 ? 0.27270 0.24910 0.22235 -0.06618 0.00172  0.04063  315 TYR A N   
2565 C CA  . TYR A 321 ? 0.30720 0.26221 0.25248 -0.05983 -0.00590 0.04027  315 TYR A CA  
2566 C C   . TYR A 321 ? 0.33982 0.27976 0.27749 -0.06701 -0.01277 0.04246  315 TYR A C   
2567 O O   . TYR A 321 ? 0.31679 0.25032 0.24383 -0.07924 -0.01563 0.04784  315 TYR A O   
2568 C CB  . TYR A 321 ? 0.26735 0.20939 0.20426 -0.05828 -0.00973 0.04278  315 TYR A CB  
2569 C CG  . TYR A 321 ? 0.31674 0.23783 0.25113 -0.05064 -0.01831 0.04149  315 TYR A CG  
2570 C CD1 . TYR A 321 ? 0.31750 0.24081 0.26199 -0.03924 -0.01765 0.03520  315 TYR A CD1 
2571 C CD2 . TYR A 321 ? 0.31891 0.21867 0.24106 -0.05499 -0.02747 0.04626  315 TYR A CD2 
2572 C CE1 . TYR A 321 ? 0.30617 0.21349 0.25031 -0.03168 -0.02484 0.03214  315 TYR A CE1 
2573 C CE2 . TYR A 321 ? 0.33901 0.22025 0.26131 -0.04649 -0.03612 0.04381  315 TYR A CE2 
2574 C CZ  . TYR A 321 ? 0.30818 0.19455 0.24233 -0.03448 -0.03424 0.03596  315 TYR A CZ  
2575 O OH  . TYR A 321 ? 0.29618 0.16715 0.23231 -0.02556 -0.04222 0.03174  315 TYR A OH  
2576 N N   . ASP A 322 ? 0.30568 0.23987 0.24794 -0.06023 -0.01557 0.03809  316 ASP A N   
2577 C CA  . ASP A 322 ? 0.34973 0.26786 0.28541 -0.06540 -0.02269 0.03835  316 ASP A CA  
2578 C C   . ASP A 322 ? 0.40596 0.31631 0.34651 -0.05405 -0.02566 0.03132  316 ASP A C   
2579 O O   . ASP A 322 ? 0.31829 0.24151 0.26669 -0.05047 -0.02161 0.02710  316 ASP A O   
2580 C CB  . ASP A 322 ? 0.31842 0.24978 0.25593 -0.07543 -0.01964 0.03974  316 ASP A CB  
2581 C CG  . ASP A 322 ? 0.33798 0.25261 0.26833 -0.08167 -0.02716 0.03967  316 ASP A CG  
2582 O OD1 . ASP A 322 ? 0.31889 0.20977 0.24214 -0.07868 -0.03532 0.03870  316 ASP A OD1 
2583 O OD2 . ASP A 322 ? 0.28337 0.20863 0.21589 -0.08938 -0.02545 0.04011  316 ASP A OD2 
2584 N N   . PRO A 323 ? 0.34489 0.23530 0.28116 -0.04842 -0.03298 0.02955  317 PRO A N   
2585 C CA  . PRO A 323 ? 0.37215 0.25913 0.31478 -0.03678 -0.03456 0.02096  317 PRO A CA  
2586 C C   . PRO A 323 ? 0.32239 0.20771 0.26515 -0.03860 -0.03596 0.01601  317 PRO A C   
2587 O O   . PRO A 323 ? 0.31800 0.21146 0.26736 -0.03104 -0.03308 0.00870  317 PRO A O   
2588 C CB  . PRO A 323 ? 0.33365 0.19801 0.27163 -0.03198 -0.04400 0.02036  317 PRO A CB  
2589 C CG  . PRO A 323 ? 0.39833 0.26007 0.32917 -0.03868 -0.04484 0.02926  317 PRO A CG  
2590 C CD  . PRO A 323 ? 0.30387 0.17610 0.23025 -0.05188 -0.04008 0.03503  317 PRO A CD  
2591 N N   . SER A 324 ? 0.31594 0.19129 0.25069 -0.04947 -0.04040 0.01976  318 SER A N   
2592 C CA  . SER A 324 ? 0.35709 0.23107 0.29111 -0.05260 -0.04199 0.01520  318 SER A CA  
2593 C C   . SER A 324 ? 0.33182 0.23094 0.27289 -0.05484 -0.03375 0.01522  318 SER A C   
2594 O O   . SER A 324 ? 0.33098 0.23261 0.27254 -0.05579 -0.03425 0.01053  318 SER A O   
2595 C CB  A SER A 324 ? 0.32008 0.17567 0.24304 -0.06504 -0.04975 0.01999  318 SER A CB  
2596 C CB  B SER A 324 ? 0.32007 0.17573 0.24303 -0.06507 -0.04973 0.02002  318 SER A CB  
2597 O OG  A SER A 324 ? 0.30639 0.17375 0.22681 -0.07692 -0.04589 0.02872  318 SER A OG  
2598 O OG  B SER A 324 ? 0.39055 0.22294 0.30583 -0.06514 -0.05817 0.02336  318 SER A OG  
2599 N N   . ASP A 325 ? 0.29827 0.21538 0.24475 -0.05568 -0.02700 0.02006  319 ASP A N   
2600 C CA  . ASP A 325 ? 0.27681 0.21722 0.23184 -0.05621 -0.02044 0.02028  319 ASP A CA  
2601 C C   . ASP A 325 ? 0.26731 0.21969 0.23064 -0.04557 -0.01520 0.01763  319 ASP A C   
2602 O O   . ASP A 325 ? 0.25398 0.22446 0.22502 -0.04503 -0.01023 0.01936  319 ASP A O   
2603 C CB  . ASP A 325 ? 0.35340 0.30653 0.30992 -0.06574 -0.01722 0.02672  319 ASP A CB  
2604 C CG  . ASP A 325 ? 0.36047 0.33624 0.32692 -0.06700 -0.01280 0.02663  319 ASP A CG  
2605 O OD1 . ASP A 325 ? 0.30274 0.27981 0.27011 -0.06618 -0.01465 0.02341  319 ASP A OD1 
2606 O OD2 . ASP A 325 ? 0.34609 0.33850 0.31959 -0.06867 -0.00793 0.02936  319 ASP A OD2 
2607 N N   . GLU A 326 ? 0.22306 0.16273 0.24446 -0.00164 -0.04341 -0.05165 320 GLU A N   
2608 C CA  . GLU A 326 ? 0.22323 0.16690 0.24045 -0.00640 -0.04150 -0.05449 320 GLU A CA  
2609 C C   . GLU A 326 ? 0.25087 0.19673 0.26274 -0.00583 -0.04231 -0.06148 320 GLU A C   
2610 O O   . GLU A 326 ? 0.22903 0.18334 0.24466 -0.00218 -0.04257 -0.06813 320 GLU A O   
2611 C CB  . GLU A 326 ? 0.26266 0.21164 0.28371 -0.00670 -0.04065 -0.05515 320 GLU A CB  
2612 C CG  . GLU A 326 ? 0.20406 0.14551 0.22474 -0.00576 -0.03905 -0.04960 320 GLU A CG  
2613 C CD  . GLU A 326 ? 0.27693 0.22008 0.29963 -0.00417 -0.03884 -0.05021 320 GLU A CD  
2614 O OE1 . GLU A 326 ? 0.24688 0.19941 0.27336 -0.00555 -0.04098 -0.05451 320 GLU A OE1 
2615 O OE2 . GLU A 326 ? 0.25010 0.18525 0.27109 -0.00125 -0.03712 -0.04657 320 GLU A OE2 
2616 N N   . PRO A 327 ? 0.22889 0.16770 0.23192 -0.00836 -0.04320 -0.06132 321 PRO A N   
2617 C CA  . PRO A 327 ? 0.27613 0.21069 0.26809 -0.00456 -0.04344 -0.06895 321 PRO A CA  
2618 C C   . PRO A 327 ? 0.25804 0.20619 0.24970 -0.00535 -0.04211 -0.07376 321 PRO A C   
2619 O O   . PRO A 327 ? 0.22074 0.17822 0.21837 -0.01362 -0.04295 -0.06991 321 PRO A O   
2620 C CB  . PRO A 327 ? 0.27866 0.20150 0.25998 -0.00955 -0.04550 -0.06555 321 PRO A CB  
2621 C CG  . PRO A 327 ? 0.31612 0.24353 0.30660 -0.01607 -0.04615 -0.05773 321 PRO A CG  
2622 C CD  . PRO A 327 ? 0.23046 0.16321 0.23243 -0.01293 -0.04458 -0.05470 321 PRO A CD  
2623 N N   . ILE A 328 ? 0.27032 0.22288 0.25252 0.00367  -0.03559 -0.07505 322 ILE A N   
2624 C CA  . ILE A 328 ? 0.27440 0.25042 0.25783 0.00507  -0.02843 -0.06968 322 ILE A CA  
2625 C C   . ILE A 328 ? 0.28567 0.25200 0.24949 0.00827  -0.02528 -0.07162 322 ILE A C   
2626 O O   . ILE A 328 ? 0.30026 0.23967 0.24685 0.00959  -0.02903 -0.07777 322 ILE A O   
2627 C CB  . ILE A 328 ? 0.22968 0.22603 0.22103 0.01632  -0.02021 -0.06505 322 ILE A CB  
2628 C CG1 . ILE A 328 ? 0.27855 0.25558 0.25364 0.03208  -0.01456 -0.07048 322 ILE A CG1 
2629 C CG2 . ILE A 328 ? 0.28684 0.29347 0.29611 0.01101  -0.02446 -0.06241 322 ILE A CG2 
2630 C CD1 . ILE A 328 ? 0.28801 0.28574 0.26863 0.04716  -0.00309 -0.06366 322 ILE A CD1 
2631 N N   . ALA A 329 ? 0.24044 0.22910 0.20582 0.00852  -0.01911 -0.06489 323 ALA A N   
2632 C CA  . ALA A 329 ? 0.32956 0.31139 0.27634 0.01075  -0.01567 -0.06551 323 ALA A CA  
2633 C C   . ALA A 329 ? 0.37654 0.34296 0.29977 0.02870  -0.00618 -0.06905 323 ALA A C   
2634 O O   . ALA A 329 ? 0.34564 0.32335 0.27267 0.04205  0.00276  -0.06548 323 ALA A O   
2635 C CB  . ALA A 329 ? 0.31887 0.33171 0.27588 0.00563  -0.01176 -0.05499 323 ALA A CB  
2636 N N   . GLU A 330 ? 0.30626 0.24404 0.20207 0.02908  -0.00816 -0.07538 324 GLU A N   
2637 C CA  . GLU A 330 ? 0.43814 0.35112 0.30059 0.04612  0.00105  -0.07962 324 GLU A CA  
2638 C C   . GLU A 330 ? 0.54956 0.48738 0.40853 0.06073  0.01731  -0.07038 324 GLU A C   
2639 O O   . GLU A 330 ? 0.63645 0.57550 0.48610 0.08051  0.03079  -0.06717 324 GLU A O   
2640 C CB  . GLU A 330 ? 0.52465 0.39748 0.35470 0.03899  -0.00796 -0.08791 324 GLU A CB  
2641 C CG  . GLU A 330 ? 0.61315 0.45195 0.39752 0.05512  0.00129  -0.09284 324 GLU A CG  
2642 C CD  . GLU A 330 ? 0.71792 0.52099 0.47785 0.04179  -0.01109 -0.09694 324 GLU A CD  
2643 O OE1 . GLU A 330 ? 0.73412 0.50986 0.47225 0.04652  -0.00998 -0.09742 324 GLU A OE1 
2644 O OE2 . GLU A 330 ? 0.55028 0.35982 0.32037 0.02491  -0.02198 -0.09548 324 GLU A OE2 
2645 N N   . ALA A 331 ? 0.55416 0.51338 0.42128 0.05216  0.01698  -0.06405 325 ALA A N   
2646 C CA  . ALA A 331 ? 0.61549 0.60109 0.48006 0.06468  0.03173  -0.05256 325 ALA A CA  
2647 C C   . ALA A 331 ? 0.57794 0.61199 0.48079 0.05243  0.02948  -0.03858 325 ALA A C   
2648 O O   . ALA A 331 ? 0.53678 0.57862 0.44642 0.03683  0.02197  -0.03661 325 ALA A O   
2649 C CB  . ALA A 331 ? 0.65343 0.61649 0.48578 0.06568  0.03330  -0.05655 325 ALA A CB  
2650 N N   . PRO A 332 ? 0.43218 0.49815 0.35906 0.05767  0.03475  -0.02759 326 PRO A N   
2651 C CA  . PRO A 332 ? 0.49626 0.60667 0.45520 0.04363  0.03084  -0.01194 326 PRO A CA  
2652 C C   . PRO A 332 ? 0.43703 0.57529 0.39564 0.04780  0.03990  0.00253  326 PRO A C   
2653 O O   . PRO A 332 ? 0.38146 0.51135 0.31693 0.06749  0.05385  0.00328  326 PRO A O   
2654 C CB  . PRO A 332 ? 0.41703 0.55388 0.39689 0.05107  0.03557  -0.00165 326 PRO A CB  
2655 C CG  . PRO A 332 ? 0.57086 0.68256 0.52862 0.07514  0.04757  -0.00903 326 PRO A CG  
2656 C CD  . PRO A 332 ? 0.44039 0.50110 0.36471 0.07503  0.04303  -0.02822 326 PRO A CD  
2657 N N   . PHE A 333 ? 0.26622 0.43538 0.24805 0.02880  0.03168  0.01472  327 PHE A N   
2658 C CA  . PHE A 333 ? 0.36441 0.56613 0.35153 0.02916  0.03811  0.03173  327 PHE A CA  
2659 C C   . PHE A 333 ? 0.45622 0.70732 0.46504 0.04104  0.04970  0.05597  327 PHE A C   
2660 O O   . PHE A 333 ? 0.47237 0.74600 0.50506 0.03111  0.04282  0.06501  327 PHE A O   
2661 C CB  . PHE A 333 ? 0.37021 0.58002 0.37034 0.00171  0.02271  0.03527  327 PHE A CB  
2662 C CG  . PHE A 333 ? 0.35436 0.52564 0.33415 -0.00628 0.01555  0.01828  327 PHE A CG  
2663 C CD1 . PHE A 333 ? 0.53045 0.70394 0.49801 -0.00391 0.02035  0.02152  327 PHE A CD1 
2664 C CD2 . PHE A 333 ? 0.38387 0.51947 0.35801 -0.01573 0.00438  0.00138  327 PHE A CD2 
2665 C CE1 . PHE A 333 ? 0.44222 0.58282 0.39245 -0.01210 0.01310  0.00794  327 PHE A CE1 
2666 C CE2 . PHE A 333 ? 0.41810 0.52324 0.37682 -0.02289 -0.00207 -0.01032 327 PHE A CE2 
2667 C CZ  . PHE A 333 ? 0.33231 0.43993 0.27921 -0.02174 0.00176  -0.00714 327 PHE A CZ  
2668 N N   . LYS A 334 ? 0.52548 0.79370 0.52502 0.06282  0.06767  0.06813  328 LYS A N   
2669 C CA  . LYS A 334 ? 0.48164 0.79954 0.50189 0.07921  0.08220  0.09471  328 LYS A CA  
2670 C C   . LYS A 334 ? 0.57440 0.94850 0.62862 0.05956  0.07473  0.12204  328 LYS A C   
2671 O O   . LYS A 334 ? 0.49967 0.91422 0.58355 0.05251  0.07112  0.14200  328 LYS A O   
2672 C CB  . LYS A 334 ? 0.52741 0.83926 0.52082 0.11378  0.10696  0.09894  328 LYS A CB  
2673 N N   . PHE A 335 ? 0.48699 0.86432 0.53673 0.04914  0.07120  0.12466  329 PHE A N   
2674 C CA  . PHE A 335 ? 0.32561 0.75195 0.40441 0.02764  0.06198  0.15064  329 PHE A CA  
2675 C C   . PHE A 335 ? 0.44963 0.85178 0.51648 0.00696  0.04918  0.13862  329 PHE A C   
2676 O O   . PHE A 335 ? 0.45741 0.80993 0.49660 0.01007  0.04804  0.11241  329 PHE A O   
2677 C CB  . PHE A 335 ? 0.30513 0.78747 0.39897 0.04859  0.08145  0.18333  329 PHE A CB  
2678 N N   . ASP A 336 ? 0.52038 0.95869 0.60850 -0.01518 0.03877  0.15992  330 ASP A N   
2679 C CA  . ASP A 336 ? 0.63044 1.04981 0.70945 -0.03552 0.02674  0.15231  330 ASP A CA  
2680 C C   . ASP A 336 ? 0.57547 0.98443 0.63263 -0.01553 0.04193  0.14697  330 ASP A C   
2681 O O   . ASP A 336 ? 0.70320 1.13837 0.76688 -0.02125 0.04277  0.16325  330 ASP A O   
2682 C CB  . ASP A 336 ? 0.62758 1.08942 0.73250 -0.06310 0.01274  0.17980  330 ASP A CB  
2683 N N   . PRO A 343 ? 0.46285 1.02343 0.56380 -0.11611 -0.00883 0.26880  337 PRO A N   
2684 C CA  . PRO A 343 ? 0.42191 0.95998 0.51582 -0.14024 -0.02486 0.26408  337 PRO A CA  
2685 C C   . PRO A 343 ? 0.55565 1.04324 0.62542 -0.14831 -0.02426 0.23625  337 PRO A C   
2686 O O   . PRO A 343 ? 0.39696 0.87039 0.45257 -0.13300 -0.00915 0.22141  337 PRO A O   
2687 C CB  . PRO A 343 ? 0.51169 1.07801 0.61049 -0.12738 -0.01534 0.27740  337 PRO A CB  
2688 C CG  . PRO A 343 ? 0.48383 1.06743 0.57838 -0.09317 0.01036  0.27832  337 PRO A CG  
2689 C CD  . PRO A 343 ? 0.40695 1.00107 0.51245 -0.08751 0.01068  0.28261  337 PRO A CD  
2690 N N   . LYS A 344 ? 0.45805 0.91636 0.52001 -0.17076 -0.04078 0.23025  338 LYS A N   
2691 C CA  . LYS A 344 ? 0.52735 0.93765 0.56859 -0.17839 -0.04183 0.20635  338 LYS A CA  
2692 C C   . LYS A 344 ? 0.48004 0.88750 0.50597 -0.16298 -0.02459 0.19775  338 LYS A C   
2693 O O   . LYS A 344 ? 0.54977 0.91987 0.55636 -0.16068 -0.02212 0.17681  338 LYS A O   
2694 C CB  . LYS A 344 ? 0.48909 0.86589 0.52168 -0.20019 -0.06103 0.20355  338 LYS A CB  
2695 C CG  . LYS A 344 ? 0.43386 0.83368 0.47366 -0.20468 -0.06636 0.22083  338 LYS A CG  
2696 C CD  . LYS A 344 ? 0.51065 0.86886 0.53437 -0.22178 -0.08078 0.21425  338 LYS A CD  
2697 C CE  . LYS A 344 ? 0.53759 0.91590 0.56666 -0.22335 -0.08188 0.22657  338 LYS A CE  
2698 N NZ  . LYS A 344 ? 0.38283 0.81720 0.43386 -0.21624 -0.07908 0.25050  338 LYS A NZ  
2699 N N   . GLU A 345 ? 0.34003 0.77897 0.37017 -0.14933 -0.01485 0.21113  339 GLU A N   
2700 C CA  . GLU A 345 ? 0.53845 0.96819 0.54452 -0.13210 0.00097  0.20233  339 GLU A CA  
2701 C C   . GLU A 345 ? 0.48428 0.90278 0.46966 -0.10769 0.01721  0.18966  339 GLU A C   
2702 O O   . GLU A 345 ? 0.43088 0.80761 0.38904 -0.09872 0.01928  0.16628  339 GLU A O   
2703 C CB  . GLU A 345 ? 0.52252 0.98613 0.53695 -0.12076 0.00793  0.21941  339 GLU A CB  
2704 C CG  . GLU A 345 ? 0.41020 0.87759 0.43782 -0.14199 -0.00813 0.22832  339 GLU A CG  
2705 C CD  . GLU A 345 ? 0.46079 0.95123 0.51494 -0.15732 -0.02490 0.24601  339 GLU A CD  
2706 O OE1 . GLU A 345 ? 0.34553 0.86441 0.41411 -0.14744 -0.02102 0.25789  339 GLU A OE1 
2707 O OE2 . GLU A 345 ? 0.50827 0.98515 0.56458 -0.17829 -0.04254 0.24848  339 GLU A OE2 
2708 N N   . LYS A 346 ? 0.32619 0.77382 0.32566 -0.09415 0.02552  0.20132  340 LYS A N   
2709 C CA  . LYS A 346 ? 0.45864 0.88975 0.43833 -0.06975 0.03963  0.18770  340 LYS A CA  
2710 C C   . LYS A 346 ? 0.48221 0.86749 0.45578 -0.07963 0.02702  0.16224  340 LYS A C   
2711 O O   . LYS A 346 ? 0.41996 0.76915 0.36799 -0.06388 0.03303  0.14097  340 LYS A O   
2712 C CB  . LYS A 346 ? 0.33697 0.80930 0.33832 -0.05309 0.04979  0.20726  340 LYS A CB  
2713 C CG  . LYS A 346 ? 0.43431 0.93317 0.43580 -0.02749 0.06563  0.22238  340 LYS A CG  
2714 C CD  . LYS A 346 ? 0.40660 0.87348 0.36488 0.00299  0.08640  0.20642  340 LYS A CD  
2715 C CE  . LYS A 346 ? 0.44524 0.92350 0.39410 0.02045  0.09838  0.21652  340 LYS A CE  
2716 N NZ  . LYS A 346 ? 0.50741 0.93862 0.40724 0.02919  0.10545  0.19536  340 LYS A NZ  
2717 N N   . LEU A 347 ? 0.46527 0.84906 0.45915 -0.10571 0.00940  0.16494  341 LEU A N   
2718 C CA  . LEU A 347 ? 0.34745 0.68958 0.33603 -0.11402 -0.00141 0.14328  341 LEU A CA  
2719 C C   . LEU A 347 ? 0.44688 0.74300 0.41403 -0.11761 -0.00693 0.12188  341 LEU A C   
2720 O O   . LEU A 347 ? 0.43608 0.69712 0.38789 -0.10974 -0.00684 0.10153  341 LEU A O   
2721 C CB  . LEU A 347 ? 0.34661 0.69628 0.35663 -0.14007 -0.01779 0.15367  341 LEU A CB  
2722 C CG  . LEU A 347 ? 0.45750 0.85002 0.49040 -0.14047 -0.01634 0.17473  341 LEU A CG  
2723 C CD1 . LEU A 347 ? 0.33037 0.71998 0.37594 -0.16912 -0.03703 0.18383  341 LEU A CD1 
2724 C CD2 . LEU A 347 ? 0.30036 0.68374 0.32819 -0.12037 -0.00705 0.16222  341 LEU A CD2 
2725 N N   . LYS A 348 ? 0.44952 0.74725 0.41701 -0.13034 -0.01242 0.12836  342 LYS A N   
2726 C CA  . LYS A 348 ? 0.35643 0.61808 0.30477 -0.13165 -0.01578 0.11262  342 LYS A CA  
2727 C C   . LYS A 348 ? 0.37286 0.61964 0.29470 -0.10945 -0.00407 0.09997  342 LYS A C   
2728 O O   . LYS A 348 ? 0.35349 0.56318 0.25860 -0.10774 -0.00798 0.08204  342 LYS A O   
2729 C CB  . LYS A 348 ? 0.37990 0.65389 0.33266 -0.14488 -0.02013 0.12543  342 LYS A CB  
2730 C CG  . LYS A 348 ? 0.36218 0.60434 0.29753 -0.14680 -0.02363 0.11299  342 LYS A CG  
2731 C CD  . LYS A 348 ? 0.35517 0.60605 0.29830 -0.16313 -0.03023 0.12585  342 LYS A CD  
2732 C CE  . LYS A 348 ? 0.37809 0.59837 0.30695 -0.16572 -0.03445 0.11528  342 LYS A CE  
2733 N NZ  . LYS A 348 ? 0.41295 0.63983 0.34898 -0.18067 -0.04029 0.12791  342 LYS A NZ  
2734 N N   . GLU A 349 ? 0.34714 0.62122 0.26272 -0.09223 0.01034  0.11073  343 GLU A N   
2735 C CA  . GLU A 349 ? 0.42214 0.67599 0.30393 -0.06981 0.02265  0.09932  343 GLU A CA  
2736 C C   . GLU A 349 ? 0.47150 0.69730 0.34220 -0.05951 0.02379  0.08248  343 GLU A C   
2737 O O   . GLU A 349 ? 0.47113 0.65848 0.31149 -0.05220 0.02380  0.06542  343 GLU A O   
2738 C CB  . GLU A 349 ? 0.45399 0.74385 0.33120 -0.05051 0.04056  0.11729  343 GLU A CB  
2739 C CG  . GLU A 349 ? 0.54259 0.80816 0.37719 -0.02415 0.05619  0.10748  343 GLU A CG  
2740 C CD  . GLU A 349 ? 0.71483 1.01715 0.54425 -0.00387 0.07568  0.12843  343 GLU A CD  
2741 O OE1 . GLU A 349 ? 0.69217 0.97648 0.48467 0.02256  0.09256  0.12372  343 GLU A OE1 
2742 O OE2 . GLU A 349 ? 0.61010 0.95809 0.47074 -0.01402 0.07438  0.15088  343 GLU A OE2 
2743 N N   . LEU A 350 ? 0.39401 0.63792 0.28836 -0.06066 0.02324  0.08799  344 LEU A N   
2744 C CA  . LEU A 350 ? 0.39619 0.61580 0.28310 -0.05166 0.02391  0.07313  344 LEU A CA  
2745 C C   . LEU A 350 ? 0.33220 0.51567 0.22016 -0.06771 0.00818  0.05648  344 LEU A C   
2746 O O   . LEU A 350 ? 0.39957 0.55065 0.26969 -0.06038 0.00746  0.04041  344 LEU A O   
2747 C CB  . LEU A 350 ? 0.37326 0.62687 0.28622 -0.04825 0.02816  0.08651  344 LEU A CB  
2748 C CG  . LEU A 350 ? 0.37554 0.66640 0.28760 -0.02618 0.04722  0.10503  344 LEU A CG  
2749 C CD1 . LEU A 350 ? 0.34237 0.67590 0.28784 -0.02799 0.04841  0.12426  344 LEU A CD1 
2750 C CD2 . LEU A 350 ? 0.38095 0.64166 0.25447 0.00143  0.06246  0.09181  344 LEU A CD2 
2751 N N   . ILE A 351 ? 0.31479 0.50221 0.22197 -0.08876 -0.00394 0.06152  345 ILE A N   
2752 C CA  . ILE A 351 ? 0.30532 0.45898 0.21200 -0.10112 -0.01632 0.04871  345 ILE A CA  
2753 C C   . ILE A 351 ? 0.34676 0.47303 0.22880 -0.09814 -0.01769 0.03857  345 ILE A C   
2754 O O   . ILE A 351 ? 0.42361 0.52008 0.29590 -0.09775 -0.02308 0.02584  345 ILE A O   
2755 C CB  . ILE A 351 ? 0.31094 0.47070 0.23721 -0.12186 -0.02669 0.05801  345 ILE A CB  
2756 C CG1 . ILE A 351 ? 0.31013 0.48750 0.25583 -0.12869 -0.02944 0.06624  345 ILE A CG1 
2757 C CG2 . ILE A 351 ? 0.28787 0.41311 0.21039 -0.13093 -0.03615 0.04799  345 ILE A CG2 
2758 C CD1 . ILE A 351 ? 0.29782 0.47643 0.25542 -0.15033 -0.04026 0.07668  345 ILE A CD1 
2759 N N   . PHE A 352 ? 0.37817 0.51536 0.24980 -0.09715 -0.01376 0.04583  346 PHE A N   
2760 C CA  . PHE A 352 ? 0.35427 0.46628 0.19837 -0.09526 -0.01565 0.03795  346 PHE A CA  
2761 C C   . PHE A 352 ? 0.42034 0.50608 0.23462 -0.07971 -0.01062 0.02477  346 PHE A C   
2762 O O   . PHE A 352 ? 0.41060 0.46429 0.20816 -0.08366 -0.01903 0.01413  346 PHE A O   
2763 C CB  . PHE A 352 ? 0.40386 0.53502 0.23926 -0.09396 -0.00981 0.04906  346 PHE A CB  
2764 C CG  . PHE A 352 ? 0.39194 0.49799 0.19745 -0.09500 -0.01338 0.04290  346 PHE A CG  
2765 C CD1 . PHE A 352 ? 0.42876 0.52601 0.24196 -0.11158 -0.02535 0.04449  346 PHE A CD1 
2766 C CD2 . PHE A 352 ? 0.42733 0.51689 0.19432 -0.07929 -0.00463 0.03693  346 PHE A CD2 
2767 C CE1 . PHE A 352 ? 0.41396 0.49101 0.20065 -0.11472 -0.03028 0.04138  346 PHE A CE1 
2768 C CE2 . PHE A 352 ? 0.50726 0.57033 0.24196 -0.08294 -0.01004 0.03186  346 PHE A CE2 
2769 C CZ  . PHE A 352 ? 0.44425 0.50343 0.19074 -0.10184 -0.02377 0.03469  346 PHE A CZ  
2770 N N   . GLU A 353 ? 0.38934 0.48808 0.19597 -0.06199 0.00301  0.02724  347 GLU A N   
2771 C CA  . GLU A 353 ? 0.42729 0.49672 0.20078 -0.04507 0.00955  0.01512  347 GLU A CA  
2772 C C   . GLU A 353 ? 0.40368 0.45145 0.18523 -0.04938 0.00073  0.00348  347 GLU A C   
2773 O O   . GLU A 353 ? 0.55688 0.56740 0.31086 -0.04780 -0.00435 -0.00884 347 GLU A O   
2774 C CB  . GLU A 353 ? 0.56216 0.65408 0.33013 -0.02270 0.02842  0.02362  347 GLU A CB  
2775 C CG  . GLU A 353 ? 0.63154 0.73096 0.37347 -0.01009 0.04107  0.03197  347 GLU A CG  
2776 C CD  . GLU A 353 ? 0.74572 0.84434 0.46156 0.01925  0.06190  0.03475  347 GLU A CD  
2777 O OE1 . GLU A 353 ? 0.85614 0.95061 0.57699 0.02878  0.06585  0.03061  347 GLU A OE1 
2778 O OE2 . GLU A 353 ? 0.80691 0.90843 0.49606 0.03422  0.07542  0.04194  347 GLU A OE2 
2779 N N   . GLU A 354 ? 0.43570 0.50501 0.25295 -0.05597 -0.00211 0.00813  348 GLU A N   
2780 C CA  . GLU A 354 ? 0.41879 0.47061 0.24449 -0.05790 -0.00856 -0.00164 348 GLU A CA  
2781 C C   . GLU A 354 ? 0.50131 0.52690 0.32677 -0.07257 -0.02313 -0.00857 348 GLU A C   
2782 O O   . GLU A 354 ? 0.42365 0.42738 0.24596 -0.07203 -0.02844 -0.01755 348 GLU A O   
2783 C CB  . GLU A 354 ? 0.41075 0.49047 0.27118 -0.06268 -0.00863 0.00614  348 GLU A CB  
2784 C CG  . GLU A 354 ? 0.48821 0.59291 0.35280 -0.04676 0.00457  0.01330  348 GLU A CG  
2785 C CD  . GLU A 354 ? 0.47825 0.55945 0.32339 -0.03036 0.01032  0.00178  348 GLU A CD  
2786 O OE1 . GLU A 354 ? 0.43505 0.49697 0.28607 -0.03584 0.00187  -0.00793 348 GLU A OE1 
2787 O OE2 . GLU A 354 ? 0.66241 0.74309 0.48477 -0.01094 0.02409  0.00327  348 GLU A OE2 
2788 N N   . THR A 355 ? 0.50193 0.53141 0.33214 -0.08509 -0.02932 -0.00250 349 THR A N   
2789 C CA  . THR A 355 ? 0.48108 0.49163 0.31471 -0.09803 -0.04188 -0.00430 349 THR A CA  
2790 C C   . THR A 355 ? 0.47069 0.45816 0.27325 -0.09989 -0.04714 -0.00772 349 THR A C   
2791 O O   . THR A 355 ? 0.49713 0.47342 0.30291 -0.11160 -0.05817 -0.00528 349 THR A O   
2792 C CB  . THR A 355 ? 0.40362 0.43031 0.26161 -0.11086 -0.04574 0.00623  349 THR A CB  
2793 O OG1 . THR A 355 ? 0.36454 0.40861 0.21659 -0.11182 -0.04126 0.01421  349 THR A OG1 
2794 C CG2 . THR A 355 ? 0.34914 0.38959 0.23167 -0.11256 -0.04386 0.00915  349 THR A CG2 
2795 N N   . ALA A 356 ? 0.48719 0.46600 0.25760 -0.08831 -0.03940 -0.01191 350 ALA A N   
2796 C CA  . ALA A 356 ? 0.45105 0.40392 0.18439 -0.09162 -0.04502 -0.01474 350 ALA A CA  
2797 C C   . ALA A 356 ? 0.58932 0.50818 0.30670 -0.09868 -0.05821 -0.02208 350 ALA A C   
2798 O O   . ALA A 356 ? 0.64480 0.54519 0.34221 -0.11036 -0.06971 -0.02032 350 ALA A O   
2799 C CB  . ALA A 356 ? 0.58955 0.53483 0.28552 -0.07451 -0.03147 -0.01791 350 ALA A CB  
2800 N N   . ARG A 357 ? 0.58853 0.50018 0.31495 -0.09323 -0.05792 -0.02850 351 ARG A N   
2801 C CA  . ARG A 357 ? 0.66185 0.54098 0.37090 -0.09953 -0.07047 -0.03435 351 ARG A CA  
2802 C C   . ARG A 357 ? 0.54561 0.43085 0.28375 -0.11553 -0.08384 -0.02420 351 ARG A C   
2803 O O   . ARG A 357 ? 0.59734 0.46408 0.33275 -0.11962 -0.09198 -0.02186 351 ARG A O   
2804 C CB  . ARG A 357 ? 0.65866 0.53264 0.37582 -0.08903 -0.06595 -0.04196 351 ARG A CB  
2805 C CG  . ARG A 357 ? 0.69782 0.60578 0.45855 -0.08477 -0.05807 -0.03808 351 ARG A CG  
2806 C CD  . ARG A 357 ? 0.64010 0.54031 0.40876 -0.07761 -0.05709 -0.04481 351 ARG A CD  
2807 N NE  . ARG A 357 ? 0.65353 0.55596 0.40920 -0.05951 -0.04277 -0.04990 351 ARG A NE  
2808 C CZ  . ARG A 357 ? 0.67083 0.58317 0.44427 -0.05095 -0.03699 -0.05209 351 ARG A CZ  
2809 N NH1 . ARG A 357 ? 0.66391 0.58101 0.46525 -0.05845 -0.04427 -0.05161 351 ARG A NH1 
2810 N NH2 . ARG A 357 ? 0.67223 0.59024 0.43445 -0.03336 -0.02280 -0.05341 351 ARG A NH2 
2811 N N   . PHE A 358 ? 0.47795 0.39008 0.24642 -0.12267 -0.08411 -0.01548 352 PHE A N   
2812 C CA  . PHE A 358 ? 0.53095 0.45024 0.32832 -0.13319 -0.09267 -0.00331 352 PHE A CA  
2813 C C   . PHE A 358 ? 0.48166 0.40390 0.27315 -0.14352 -0.09833 0.00710  352 PHE A C   
2814 O O   . PHE A 358 ? 0.58752 0.51802 0.40157 -0.15142 -0.10417 0.02022  352 PHE A O   
2815 C CB  . PHE A 358 ? 0.34874 0.28935 0.18075 -0.13325 -0.08867 0.00103  352 PHE A CB  
2816 C CG  . PHE A 358 ? 0.45118 0.38943 0.29391 -0.12404 -0.08386 -0.00691 352 PHE A CG  
2817 C CD1 . PHE A 358 ? 0.38806 0.31843 0.24534 -0.12266 -0.08795 -0.00429 352 PHE A CD1 
2818 C CD2 . PHE A 358 ? 0.45808 0.40613 0.30125 -0.11355 -0.07252 -0.01387 352 PHE A CD2 
2819 C CE1 . PHE A 358 ? 0.45974 0.38825 0.32611 -0.11443 -0.08383 -0.01141 352 PHE A CE1 
2820 C CE2 . PHE A 358 ? 0.48529 0.43250 0.33856 -0.10589 -0.06874 -0.02004 352 PHE A CE2 
2821 C CZ  . PHE A 358 ? 0.53030 0.46558 0.39248 -0.10781 -0.07564 -0.02032 352 PHE A CZ  
2822 N N   . GLN A 359 ? 0.50610 0.42195 0.26609 -0.14237 -0.09571 0.00280  353 GLN A N   
2823 C CA  . GLN A 359 ? 0.62455 0.53928 0.37334 -0.15164 -0.10109 0.01131  353 GLN A CA  
2824 C C   . GLN A 359 ? 0.56133 0.44663 0.28639 -0.15530 -0.10914 0.01071  353 GLN A C   
2825 O O   . GLN A 359 ? 0.70709 0.56879 0.40991 -0.14706 -0.10724 -0.00014 353 GLN A O   
2826 C CB  . GLN A 359 ? 0.60602 0.52827 0.33093 -0.14712 -0.09286 0.00803  353 GLN A CB  
2827 C CG  . GLN A 359 ? 0.46969 0.42418 0.22492 -0.14249 -0.08230 0.01212  353 GLN A CG  
2828 C CD  . GLN A 359 ? 0.49113 0.46480 0.27750 -0.15417 -0.08742 0.02616  353 GLN A CD  
2829 O OE1 . GLN A 359 ? 0.46207 0.43590 0.23944 -0.16396 -0.09429 0.03435  353 GLN A OE1 
2830 N NE2 . GLN A 359 ? 0.41690 0.40413 0.23707 -0.15280 -0.08385 0.02950  353 GLN A NE2 
2831 N N   . PRO A 360 ? 0.78810 0.67412 0.51750 -0.16859 -0.11856 0.02385  354 PRO A N   
2832 C CA  . PRO A 360 ? 0.78788 0.64812 0.49429 -0.17756 -0.12858 0.02765  354 PRO A CA  
2833 C C   . PRO A 360 ? 0.82316 0.64875 0.48352 -0.16906 -0.12549 0.01240  354 PRO A C   
2834 O O   . PRO A 360 ? 0.88423 0.69739 0.51452 -0.17013 -0.12500 0.01023  354 PRO A O   
2835 C CB  . PRO A 360 ? 0.68676 0.55963 0.39520 -0.18943 -0.13313 0.04008  354 PRO A CB  
2836 C CG  . PRO A 360 ? 0.79803 0.70691 0.54767 -0.18962 -0.12909 0.04990  354 PRO A CG  
2837 C CD  . PRO A 360 ? 0.63939 0.55316 0.40331 -0.17733 -0.12131 0.03977  354 PRO A CD  
# 
