data_8S7B
# 
_entry.id   8S7B 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8S7B         pdb_00008s7b 10.2210/pdb8s7b/pdb 
WWPDB D_1292136955 ?            ?                   
# 
_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       2025-03-12 
_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                        8S7B 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              christopher.schofield@chem.ox.ac.uk 
_pdbx_contact_author.name_first         Christopher 
_pdbx_contact_author.name_last          Schofield 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0290-6565 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dhingra, S.'     1 0000-0003-2573-2534 
'Alshref, F.'     2 0009-0002-6575-3372 
'Farcas, I.M.'    3 0000-0003-3276-2854 
'Brewitz, L.'     4 0000-0002-9465-777X 
'Allen, M.D.'     5 0000-0002-5344-4364 
'Schofield, C.J.' 6 0000-0002-0290-6565 
# 
_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                     'Fe(II)-2-oxoglutarate-dependent Oryza sativa dioxygenase His1 in complex with 2-oxoglutarate' 
_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 'Dhingra, S.'     1 0000-0003-2573-2534 
primary 'Alshref, F.'     2 0009-0002-6575-3372 
primary 'Farcas, I.M.'    3 0000-0003-3276-2854 
primary 'Brewitz, L.'     4 0000-0002-9465-777X 
primary 'Allen, M.D.'     5 0000-0002-5344-4364 
primary 'Schofield, C.J.' 6 0000-0002-0290-6565 
# 
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 'Fe(II)/2-oxoglutarate-dependent oxygenase'   40652.988 1   ? ? ? 
;The His-tag was removed by TEV protease before crystallography. Some residues at the N-termini was not visible in the electron density map.
;
2 non-polymer syn 'MANGANESE (II) ION'                          54.938    1   ? ? ? ? 
3 non-polymer syn '2-OXOGLUTARIC ACID'                          146.098   1   ? ? ? ? 
4 non-polymer syn 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL 370.436   1   ? ? ? ? 
5 water       nat water                                         18.015    252 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Os02g0280700 protein,cDNA clone:J013034J09,full insert sequence' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GHMASMADESWRAPAIVQELAAAGVEEPPSRYLLREKDRSDVKLVAAELPEPLPVVDLSRLDGAEEATKLRVALQNWGFF
LLTNHGVEASLMDSVMNLSREFFNQPIERKQKFSNLIDGKNFQIQGYGTDRVVTQDQILDWSDRLHLRVEPKEEQDLAFW
PDHPESFRDVLNKYASGTKRIRDDIIQAMAKLLELDEDYFLDRLNEAPAFARFNYYPPCPRPDLVFGIRPHSDGTLLTIL
LVDKDVSGLQVQRDGKWSNVEATPHTLLINLGDTMEVMCNGIFRSPVHRVVTNAEKERISLAMLYSVNDEKDIEPAAGLL
DENRPARYRKVSVEEFRAGIFGKFSRGERYIDSLRI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMASMADESWRAPAIVQELAAAGVEEPPSRYLLREKDRSDVKLVAAELPEPLPVVDLSRLDGAEEATKLRVALQNWGFF
LLTNHGVEASLMDSVMNLSREFFNQPIERKQKFSNLIDGKNFQIQGYGTDRVVTQDQILDWSDRLHLRVEPKEEQDLAFW
PDHPESFRDVLNKYASGTKRIRDDIIQAMAKLLELDEDYFLDRLNEAPAFARFNYYPPCPRPDLVFGIRPHSDGTLLTIL
LVDKDVSGLQVQRDGKWSNVEATPHTLLINLGDTMEVMCNGIFRSPVHRVVTNAEKERISLAMLYSVNDEKDIEPAAGLL
DENRPARYRKVSVEEFRAGIFGKFSRGERYIDSLRI
;
_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 'MANGANESE (II) ION'                          MN  
3 '2-OXOGLUTARIC ACID'                          AKG 
4 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL PE8 
5 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   ALA n 
1 5   SER n 
1 6   MET n 
1 7   ALA n 
1 8   ASP n 
1 9   GLU n 
1 10  SER n 
1 11  TRP n 
1 12  ARG n 
1 13  ALA n 
1 14  PRO n 
1 15  ALA n 
1 16  ILE n 
1 17  VAL n 
1 18  GLN n 
1 19  GLU n 
1 20  LEU n 
1 21  ALA n 
1 22  ALA n 
1 23  ALA n 
1 24  GLY n 
1 25  VAL n 
1 26  GLU n 
1 27  GLU n 
1 28  PRO n 
1 29  PRO n 
1 30  SER n 
1 31  ARG n 
1 32  TYR n 
1 33  LEU n 
1 34  LEU n 
1 35  ARG n 
1 36  GLU n 
1 37  LYS n 
1 38  ASP n 
1 39  ARG n 
1 40  SER n 
1 41  ASP n 
1 42  VAL n 
1 43  LYS n 
1 44  LEU n 
1 45  VAL n 
1 46  ALA n 
1 47  ALA n 
1 48  GLU n 
1 49  LEU n 
1 50  PRO n 
1 51  GLU n 
1 52  PRO n 
1 53  LEU n 
1 54  PRO n 
1 55  VAL n 
1 56  VAL n 
1 57  ASP n 
1 58  LEU n 
1 59  SER n 
1 60  ARG n 
1 61  LEU n 
1 62  ASP n 
1 63  GLY n 
1 64  ALA n 
1 65  GLU n 
1 66  GLU n 
1 67  ALA n 
1 68  THR n 
1 69  LYS n 
1 70  LEU n 
1 71  ARG n 
1 72  VAL n 
1 73  ALA n 
1 74  LEU n 
1 75  GLN n 
1 76  ASN n 
1 77  TRP n 
1 78  GLY n 
1 79  PHE n 
1 80  PHE n 
1 81  LEU n 
1 82  LEU n 
1 83  THR n 
1 84  ASN n 
1 85  HIS n 
1 86  GLY n 
1 87  VAL n 
1 88  GLU n 
1 89  ALA n 
1 90  SER n 
1 91  LEU n 
1 92  MET n 
1 93  ASP n 
1 94  SER n 
1 95  VAL n 
1 96  MET n 
1 97  ASN n 
1 98  LEU n 
1 99  SER n 
1 100 ARG n 
1 101 GLU n 
1 102 PHE n 
1 103 PHE n 
1 104 ASN n 
1 105 GLN n 
1 106 PRO n 
1 107 ILE n 
1 108 GLU n 
1 109 ARG n 
1 110 LYS n 
1 111 GLN n 
1 112 LYS n 
1 113 PHE n 
1 114 SER n 
1 115 ASN n 
1 116 LEU n 
1 117 ILE n 
1 118 ASP n 
1 119 GLY n 
1 120 LYS n 
1 121 ASN n 
1 122 PHE n 
1 123 GLN n 
1 124 ILE n 
1 125 GLN n 
1 126 GLY n 
1 127 TYR n 
1 128 GLY n 
1 129 THR n 
1 130 ASP n 
1 131 ARG n 
1 132 VAL n 
1 133 VAL n 
1 134 THR n 
1 135 GLN n 
1 136 ASP n 
1 137 GLN n 
1 138 ILE n 
1 139 LEU n 
1 140 ASP n 
1 141 TRP n 
1 142 SER n 
1 143 ASP n 
1 144 ARG n 
1 145 LEU n 
1 146 HIS n 
1 147 LEU n 
1 148 ARG n 
1 149 VAL n 
1 150 GLU n 
1 151 PRO n 
1 152 LYS n 
1 153 GLU n 
1 154 GLU n 
1 155 GLN n 
1 156 ASP n 
1 157 LEU n 
1 158 ALA n 
1 159 PHE n 
1 160 TRP n 
1 161 PRO n 
1 162 ASP n 
1 163 HIS n 
1 164 PRO n 
1 165 GLU n 
1 166 SER n 
1 167 PHE n 
1 168 ARG n 
1 169 ASP n 
1 170 VAL n 
1 171 LEU n 
1 172 ASN n 
1 173 LYS n 
1 174 TYR n 
1 175 ALA n 
1 176 SER n 
1 177 GLY n 
1 178 THR n 
1 179 LYS n 
1 180 ARG n 
1 181 ILE n 
1 182 ARG n 
1 183 ASP n 
1 184 ASP n 
1 185 ILE n 
1 186 ILE n 
1 187 GLN n 
1 188 ALA n 
1 189 MET n 
1 190 ALA n 
1 191 LYS n 
1 192 LEU n 
1 193 LEU n 
1 194 GLU n 
1 195 LEU n 
1 196 ASP n 
1 197 GLU n 
1 198 ASP n 
1 199 TYR n 
1 200 PHE n 
1 201 LEU n 
1 202 ASP n 
1 203 ARG n 
1 204 LEU n 
1 205 ASN n 
1 206 GLU n 
1 207 ALA n 
1 208 PRO n 
1 209 ALA n 
1 210 PHE n 
1 211 ALA n 
1 212 ARG n 
1 213 PHE n 
1 214 ASN n 
1 215 TYR n 
1 216 TYR n 
1 217 PRO n 
1 218 PRO n 
1 219 CYS n 
1 220 PRO n 
1 221 ARG n 
1 222 PRO n 
1 223 ASP n 
1 224 LEU n 
1 225 VAL n 
1 226 PHE n 
1 227 GLY n 
1 228 ILE n 
1 229 ARG n 
1 230 PRO n 
1 231 HIS n 
1 232 SER n 
1 233 ASP n 
1 234 GLY n 
1 235 THR n 
1 236 LEU n 
1 237 LEU n 
1 238 THR n 
1 239 ILE n 
1 240 LEU n 
1 241 LEU n 
1 242 VAL n 
1 243 ASP n 
1 244 LYS n 
1 245 ASP n 
1 246 VAL n 
1 247 SER n 
1 248 GLY n 
1 249 LEU n 
1 250 GLN n 
1 251 VAL n 
1 252 GLN n 
1 253 ARG n 
1 254 ASP n 
1 255 GLY n 
1 256 LYS n 
1 257 TRP n 
1 258 SER n 
1 259 ASN n 
1 260 VAL n 
1 261 GLU n 
1 262 ALA n 
1 263 THR n 
1 264 PRO n 
1 265 HIS n 
1 266 THR n 
1 267 LEU n 
1 268 LEU n 
1 269 ILE n 
1 270 ASN n 
1 271 LEU n 
1 272 GLY n 
1 273 ASP n 
1 274 THR n 
1 275 MET n 
1 276 GLU n 
1 277 VAL n 
1 278 MET n 
1 279 CYS n 
1 280 ASN n 
1 281 GLY n 
1 282 ILE n 
1 283 PHE n 
1 284 ARG n 
1 285 SER n 
1 286 PRO n 
1 287 VAL n 
1 288 HIS n 
1 289 ARG n 
1 290 VAL n 
1 291 VAL n 
1 292 THR n 
1 293 ASN n 
1 294 ALA n 
1 295 GLU n 
1 296 LYS n 
1 297 GLU n 
1 298 ARG n 
1 299 ILE n 
1 300 SER n 
1 301 LEU n 
1 302 ALA n 
1 303 MET n 
1 304 LEU n 
1 305 TYR n 
1 306 SER n 
1 307 VAL n 
1 308 ASN n 
1 309 ASP n 
1 310 GLU n 
1 311 LYS n 
1 312 ASP n 
1 313 ILE n 
1 314 GLU n 
1 315 PRO n 
1 316 ALA n 
1 317 ALA n 
1 318 GLY n 
1 319 LEU n 
1 320 LEU n 
1 321 ASP n 
1 322 GLU n 
1 323 ASN n 
1 324 ARG n 
1 325 PRO n 
1 326 ALA n 
1 327 ARG n 
1 328 TYR n 
1 329 ARG n 
1 330 LYS n 
1 331 VAL n 
1 332 SER n 
1 333 VAL n 
1 334 GLU n 
1 335 GLU n 
1 336 PHE n 
1 337 ARG n 
1 338 ALA n 
1 339 GLY n 
1 340 ILE n 
1 341 PHE n 
1 342 GLY n 
1 343 LYS n 
1 344 PHE n 
1 345 SER n 
1 346 ARG n 
1 347 GLY n 
1 348 GLU n 
1 349 ARG n 
1 350 TYR n 
1 351 ILE n 
1 352 ASP n 
1 353 SER n 
1 354 LEU n 
1 355 ARG n 
1 356 ILE 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                   356 
_entity_src_gen.gene_src_common_name               'Japanese rice' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HIS1, LOC_Os02g17940, Os02g0280700, OSNPB_020280700' 
_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      'Oryza sativa Japonica Group' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     39947 
_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              pLysS 
_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                       PET28a 
_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 
AKG non-polymer         . '2-OXOGLUTARIC ACID'                          ? 'C5 H6 O5'       146.098 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                      ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                         ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                    ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                       ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                        ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                    ? 'C5 H11 N O2 S'  149.211 
MN  non-polymer         . 'MANGANESE (II) ION'                          ? 'Mn 2'           54.938  
PE8 non-polymer         . 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL ? 'C16 H34 O9'     370.436 
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 
THR 'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -4  ?   ?   ?   A . n 
A 1 2   HIS 2   -3  ?   ?   ?   A . n 
A 1 3   MET 3   -2  ?   ?   ?   A . n 
A 1 4   ALA 4   -1  ?   ?   ?   A . n 
A 1 5   SER 5   0   ?   ?   ?   A . n 
A 1 6   MET 6   1   ?   ?   ?   A . n 
A 1 7   ALA 7   2   2   ALA ALA A . n 
A 1 8   ASP 8   3   3   ASP ASP A . n 
A 1 9   GLU 9   4   4   GLU GLU A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  TRP 11  6   6   TRP TRP A . n 
A 1 12  ARG 12  7   7   ARG ARG A . n 
A 1 13  ALA 13  8   8   ALA ALA A . n 
A 1 14  PRO 14  9   9   PRO PRO A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  ILE 16  11  11  ILE ILE A . n 
A 1 17  VAL 17  12  12  VAL VAL A . n 
A 1 18  GLN 18  13  13  GLN GLN A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  LEU 20  15  15  LEU LEU A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  ALA 22  17  17  ALA ALA A . n 
A 1 23  ALA 23  18  18  ALA ALA A . n 
A 1 24  GLY 24  19  19  GLY GLY A . n 
A 1 25  VAL 25  20  20  VAL VAL A . n 
A 1 26  GLU 26  21  21  GLU GLU A . n 
A 1 27  GLU 27  22  22  GLU GLU A . n 
A 1 28  PRO 28  23  23  PRO PRO A . n 
A 1 29  PRO 29  24  24  PRO PRO A . n 
A 1 30  SER 30  25  25  SER SER A . n 
A 1 31  ARG 31  26  26  ARG ARG A . n 
A 1 32  TYR 32  27  27  TYR TYR A . n 
A 1 33  LEU 33  28  28  LEU LEU A . n 
A 1 34  LEU 34  29  29  LEU LEU A . n 
A 1 35  ARG 35  30  30  ARG ARG A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  ASP 38  33  33  ASP ASP A . n 
A 1 39  ARG 39  34  34  ARG ARG A . n 
A 1 40  SER 40  35  35  SER SER A . n 
A 1 41  ASP 41  36  36  ASP ASP A . n 
A 1 42  VAL 42  37  37  VAL VAL A . n 
A 1 43  LYS 43  38  38  LYS LYS A . n 
A 1 44  LEU 44  39  39  LEU LEU A . n 
A 1 45  VAL 45  40  40  VAL VAL A . n 
A 1 46  ALA 46  41  41  ALA ALA A . n 
A 1 47  ALA 47  42  42  ALA ALA A . n 
A 1 48  GLU 48  43  43  GLU GLU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  PRO 50  45  45  PRO PRO A . n 
A 1 51  GLU 51  46  46  GLU GLU A . n 
A 1 52  PRO 52  47  47  PRO PRO A . n 
A 1 53  LEU 53  48  48  LEU LEU A . n 
A 1 54  PRO 54  49  49  PRO PRO A . n 
A 1 55  VAL 55  50  50  VAL VAL A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  ASP 57  52  52  ASP ASP A . n 
A 1 58  LEU 58  53  53  LEU LEU A . n 
A 1 59  SER 59  54  54  SER SER A . n 
A 1 60  ARG 60  55  55  ARG ARG A . n 
A 1 61  LEU 61  56  56  LEU LEU A . n 
A 1 62  ASP 62  57  57  ASP ASP A . n 
A 1 63  GLY 63  58  58  GLY GLY A . n 
A 1 64  ALA 64  59  59  ALA ALA A . n 
A 1 65  GLU 65  60  60  GLU GLU A . n 
A 1 66  GLU 66  61  61  GLU GLU A . n 
A 1 67  ALA 67  62  62  ALA ALA A . n 
A 1 68  THR 68  63  63  THR THR A . n 
A 1 69  LYS 69  64  64  LYS LYS A . n 
A 1 70  LEU 70  65  65  LEU LEU A . n 
A 1 71  ARG 71  66  66  ARG ARG A . n 
A 1 72  VAL 72  67  67  VAL VAL A . n 
A 1 73  ALA 73  68  68  ALA ALA A . n 
A 1 74  LEU 74  69  69  LEU LEU A . n 
A 1 75  GLN 75  70  70  GLN GLN A . n 
A 1 76  ASN 76  71  71  ASN ASN A . n 
A 1 77  TRP 77  72  72  TRP TRP A . n 
A 1 78  GLY 78  73  73  GLY GLY A . n 
A 1 79  PHE 79  74  74  PHE PHE A . n 
A 1 80  PHE 80  75  75  PHE PHE A . n 
A 1 81  LEU 81  76  76  LEU LEU A . n 
A 1 82  LEU 82  77  77  LEU LEU A . n 
A 1 83  THR 83  78  78  THR THR A . n 
A 1 84  ASN 84  79  79  ASN ASN A . n 
A 1 85  HIS 85  80  80  HIS HIS A . n 
A 1 86  GLY 86  81  81  GLY GLY A . n 
A 1 87  VAL 87  82  82  VAL VAL A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  ALA 89  84  84  ALA ALA A . n 
A 1 90  SER 90  85  85  SER SER A . n 
A 1 91  LEU 91  86  86  LEU LEU A . n 
A 1 92  MET 92  87  87  MET MET A . n 
A 1 93  ASP 93  88  88  ASP ASP A . n 
A 1 94  SER 94  89  89  SER SER A . n 
A 1 95  VAL 95  90  90  VAL VAL A . n 
A 1 96  MET 96  91  91  MET MET A . n 
A 1 97  ASN 97  92  92  ASN ASN A . n 
A 1 98  LEU 98  93  93  LEU LEU A . n 
A 1 99  SER 99  94  94  SER SER A . n 
A 1 100 ARG 100 95  95  ARG ARG A . n 
A 1 101 GLU 101 96  96  GLU GLU A . n 
A 1 102 PHE 102 97  97  PHE PHE A . n 
A 1 103 PHE 103 98  98  PHE PHE A . n 
A 1 104 ASN 104 99  99  ASN ASN A . n 
A 1 105 GLN 105 100 100 GLN GLN A . n 
A 1 106 PRO 106 101 101 PRO PRO A . n 
A 1 107 ILE 107 102 102 ILE ILE A . n 
A 1 108 GLU 108 103 103 GLU GLU A . n 
A 1 109 ARG 109 104 104 ARG ARG A . n 
A 1 110 LYS 110 105 105 LYS LYS A . n 
A 1 111 GLN 111 106 106 GLN GLN A . n 
A 1 112 LYS 112 107 107 LYS LYS A . n 
A 1 113 PHE 113 108 108 PHE PHE A . n 
A 1 114 SER 114 109 109 SER SER A . n 
A 1 115 ASN 115 110 110 ASN ASN A . n 
A 1 116 LEU 116 111 111 LEU LEU A . n 
A 1 117 ILE 117 112 112 ILE ILE A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 GLY 119 114 114 GLY GLY A . n 
A 1 120 LYS 120 115 115 LYS LYS A . n 
A 1 121 ASN 121 116 116 ASN ASN A . n 
A 1 122 PHE 122 117 117 PHE PHE A . n 
A 1 123 GLN 123 118 118 GLN GLN A . n 
A 1 124 ILE 124 119 119 ILE ILE A . n 
A 1 125 GLN 125 120 120 GLN GLN A . n 
A 1 126 GLY 126 121 121 GLY GLY A . n 
A 1 127 TYR 127 122 122 TYR TYR A . n 
A 1 128 GLY 128 123 123 GLY GLY A . n 
A 1 129 THR 129 124 124 THR THR A . n 
A 1 130 ASP 130 125 125 ASP ASP A . n 
A 1 131 ARG 131 126 126 ARG ARG A . n 
A 1 132 VAL 132 127 127 VAL VAL A . n 
A 1 133 VAL 133 128 128 VAL VAL A . n 
A 1 134 THR 134 129 129 THR THR A . n 
A 1 135 GLN 135 130 130 GLN GLN A . n 
A 1 136 ASP 136 131 131 ASP ASP A . n 
A 1 137 GLN 137 132 132 GLN GLN A . n 
A 1 138 ILE 138 133 133 ILE ILE A . n 
A 1 139 LEU 139 134 134 LEU LEU A . n 
A 1 140 ASP 140 135 135 ASP ASP A . n 
A 1 141 TRP 141 136 136 TRP TRP A . n 
A 1 142 SER 142 137 137 SER SER A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ARG 144 139 139 ARG ARG A . n 
A 1 145 LEU 145 140 140 LEU LEU A . n 
A 1 146 HIS 146 141 141 HIS HIS A . n 
A 1 147 LEU 147 142 142 LEU LEU A . n 
A 1 148 ARG 148 143 143 ARG ARG A . n 
A 1 149 VAL 149 144 144 VAL VAL A . n 
A 1 150 GLU 150 145 145 GLU GLU A . n 
A 1 151 PRO 151 146 146 PRO PRO A . n 
A 1 152 LYS 152 147 147 LYS LYS A . n 
A 1 153 GLU 153 148 148 GLU GLU A . n 
A 1 154 GLU 154 149 149 GLU GLU A . n 
A 1 155 GLN 155 150 150 GLN GLN A . n 
A 1 156 ASP 156 151 151 ASP ASP A . n 
A 1 157 LEU 157 152 152 LEU LEU A . n 
A 1 158 ALA 158 153 153 ALA ALA A . n 
A 1 159 PHE 159 154 154 PHE PHE A . n 
A 1 160 TRP 160 155 155 TRP TRP A . n 
A 1 161 PRO 161 156 156 PRO PRO A . n 
A 1 162 ASP 162 157 157 ASP ASP A . n 
A 1 163 HIS 163 158 158 HIS HIS A . n 
A 1 164 PRO 164 159 159 PRO PRO A . n 
A 1 165 GLU 165 160 160 GLU GLU A . n 
A 1 166 SER 166 161 161 SER SER A . n 
A 1 167 PHE 167 162 162 PHE PHE A . n 
A 1 168 ARG 168 163 163 ARG ARG A . n 
A 1 169 ASP 169 164 164 ASP ASP A . n 
A 1 170 VAL 170 165 165 VAL VAL A . n 
A 1 171 LEU 171 166 166 LEU LEU A . n 
A 1 172 ASN 172 167 167 ASN ASN A . n 
A 1 173 LYS 173 168 168 LYS LYS A . n 
A 1 174 TYR 174 169 169 TYR TYR A . n 
A 1 175 ALA 175 170 170 ALA ALA A . n 
A 1 176 SER 176 171 171 SER SER A . n 
A 1 177 GLY 177 172 172 GLY GLY A . n 
A 1 178 THR 178 173 173 THR THR A . n 
A 1 179 LYS 179 174 174 LYS LYS A . n 
A 1 180 ARG 180 175 175 ARG ARG A . n 
A 1 181 ILE 181 176 176 ILE ILE A . n 
A 1 182 ARG 182 177 177 ARG ARG A . n 
A 1 183 ASP 183 178 178 ASP ASP A . n 
A 1 184 ASP 184 179 179 ASP ASP A . n 
A 1 185 ILE 185 180 180 ILE ILE A . n 
A 1 186 ILE 186 181 181 ILE ILE A . n 
A 1 187 GLN 187 182 182 GLN GLN A . n 
A 1 188 ALA 188 183 183 ALA ALA A . n 
A 1 189 MET 189 184 184 MET MET A . n 
A 1 190 ALA 190 185 185 ALA ALA A . n 
A 1 191 LYS 191 186 186 LYS LYS A . n 
A 1 192 LEU 192 187 187 LEU LEU A . n 
A 1 193 LEU 193 188 188 LEU LEU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 LEU 195 190 190 LEU LEU A . n 
A 1 196 ASP 196 191 191 ASP ASP A . n 
A 1 197 GLU 197 192 192 GLU GLU A . n 
A 1 198 ASP 198 193 193 ASP ASP A . n 
A 1 199 TYR 199 194 194 TYR TYR A . n 
A 1 200 PHE 200 195 195 PHE PHE A . n 
A 1 201 LEU 201 196 196 LEU LEU A . n 
A 1 202 ASP 202 197 197 ASP ASP A . n 
A 1 203 ARG 203 198 198 ARG ARG A . n 
A 1 204 LEU 204 199 199 LEU LEU A . n 
A 1 205 ASN 205 200 200 ASN ASN A . n 
A 1 206 GLU 206 201 201 GLU GLU A . n 
A 1 207 ALA 207 202 202 ALA ALA A . n 
A 1 208 PRO 208 203 203 PRO PRO A . n 
A 1 209 ALA 209 204 204 ALA ALA A . n 
A 1 210 PHE 210 205 205 PHE PHE A . n 
A 1 211 ALA 211 206 206 ALA ALA A . n 
A 1 212 ARG 212 207 207 ARG ARG A . n 
A 1 213 PHE 213 208 208 PHE PHE A . n 
A 1 214 ASN 214 209 209 ASN ASN A . n 
A 1 215 TYR 215 210 210 TYR TYR A . n 
A 1 216 TYR 216 211 211 TYR TYR A . n 
A 1 217 PRO 217 212 212 PRO PRO A . n 
A 1 218 PRO 218 213 213 PRO PRO A . n 
A 1 219 CYS 219 214 214 CYS CYS A . n 
A 1 220 PRO 220 215 215 PRO PRO A . n 
A 1 221 ARG 221 216 216 ARG ARG A . n 
A 1 222 PRO 222 217 217 PRO PRO A . n 
A 1 223 ASP 223 218 218 ASP ASP A . n 
A 1 224 LEU 224 219 219 LEU LEU A . n 
A 1 225 VAL 225 220 220 VAL VAL A . n 
A 1 226 PHE 226 221 221 PHE PHE A . n 
A 1 227 GLY 227 222 222 GLY GLY A . n 
A 1 228 ILE 228 223 223 ILE ILE A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 PRO 230 225 225 PRO PRO A . n 
A 1 231 HIS 231 226 226 HIS HIS A . n 
A 1 232 SER 232 227 227 SER SER A . n 
A 1 233 ASP 233 228 228 ASP ASP A . n 
A 1 234 GLY 234 229 229 GLY GLY A . n 
A 1 235 THR 235 230 230 THR THR A . n 
A 1 236 LEU 236 231 231 LEU LEU A . n 
A 1 237 LEU 237 232 232 LEU LEU A . n 
A 1 238 THR 238 233 233 THR THR A . n 
A 1 239 ILE 239 234 234 ILE ILE A . n 
A 1 240 LEU 240 235 235 LEU LEU A . n 
A 1 241 LEU 241 236 236 LEU LEU A . n 
A 1 242 VAL 242 237 237 VAL VAL A . n 
A 1 243 ASP 243 238 238 ASP ASP A . n 
A 1 244 LYS 244 239 239 LYS LYS A . n 
A 1 245 ASP 245 240 240 ASP ASP A . n 
A 1 246 VAL 246 241 241 VAL VAL A . n 
A 1 247 SER 247 242 242 SER SER A . n 
A 1 248 GLY 248 243 243 GLY GLY A . n 
A 1 249 LEU 249 244 244 LEU LEU A . n 
A 1 250 GLN 250 245 245 GLN GLN A . n 
A 1 251 VAL 251 246 246 VAL VAL A . n 
A 1 252 GLN 252 247 247 GLN GLN A . n 
A 1 253 ARG 253 248 248 ARG ARG A . n 
A 1 254 ASP 254 249 249 ASP ASP A . n 
A 1 255 GLY 255 250 250 GLY GLY A . n 
A 1 256 LYS 256 251 251 LYS LYS A . n 
A 1 257 TRP 257 252 252 TRP TRP A . n 
A 1 258 SER 258 253 253 SER SER A . n 
A 1 259 ASN 259 254 254 ASN ASN A . n 
A 1 260 VAL 260 255 255 VAL VAL A . n 
A 1 261 GLU 261 256 256 GLU GLU A . n 
A 1 262 ALA 262 257 257 ALA ALA A . n 
A 1 263 THR 263 258 258 THR THR A . n 
A 1 264 PRO 264 259 259 PRO PRO A . n 
A 1 265 HIS 265 260 260 HIS HIS A . n 
A 1 266 THR 266 261 261 THR THR A . n 
A 1 267 LEU 267 262 262 LEU LEU A . n 
A 1 268 LEU 268 263 263 LEU LEU A . n 
A 1 269 ILE 269 264 264 ILE ILE A . n 
A 1 270 ASN 270 265 265 ASN ASN A . n 
A 1 271 LEU 271 266 266 LEU LEU A . n 
A 1 272 GLY 272 267 267 GLY GLY A . n 
A 1 273 ASP 273 268 268 ASP ASP A . n 
A 1 274 THR 274 269 269 THR THR A . n 
A 1 275 MET 275 270 270 MET MET A . n 
A 1 276 GLU 276 271 271 GLU GLU A . n 
A 1 277 VAL 277 272 272 VAL VAL A . n 
A 1 278 MET 278 273 273 MET MET A . n 
A 1 279 CYS 279 274 274 CYS CYS A . n 
A 1 280 ASN 280 275 275 ASN ASN A . n 
A 1 281 GLY 281 276 276 GLY GLY A . n 
A 1 282 ILE 282 277 277 ILE ILE A . n 
A 1 283 PHE 283 278 278 PHE PHE A . n 
A 1 284 ARG 284 279 279 ARG ARG A . n 
A 1 285 SER 285 280 280 SER SER A . n 
A 1 286 PRO 286 281 281 PRO PRO A . n 
A 1 287 VAL 287 282 282 VAL VAL A . n 
A 1 288 HIS 288 283 283 HIS HIS A . n 
A 1 289 ARG 289 284 284 ARG ARG A . n 
A 1 290 VAL 290 285 285 VAL VAL A . n 
A 1 291 VAL 291 286 286 VAL VAL A . n 
A 1 292 THR 292 287 287 THR THR A . n 
A 1 293 ASN 293 288 288 ASN ASN A . n 
A 1 294 ALA 294 289 289 ALA ALA A . n 
A 1 295 GLU 295 290 290 GLU GLU A . n 
A 1 296 LYS 296 291 291 LYS LYS A . n 
A 1 297 GLU 297 292 292 GLU GLU A . n 
A 1 298 ARG 298 293 293 ARG ARG A . n 
A 1 299 ILE 299 294 294 ILE ILE A . n 
A 1 300 SER 300 295 295 SER SER A . n 
A 1 301 LEU 301 296 296 LEU LEU A . n 
A 1 302 ALA 302 297 297 ALA ALA A . n 
A 1 303 MET 303 298 298 MET MET A . n 
A 1 304 LEU 304 299 299 LEU LEU A . n 
A 1 305 TYR 305 300 300 TYR TYR A . n 
A 1 306 SER 306 301 301 SER SER A . n 
A 1 307 VAL 307 302 302 VAL VAL A . n 
A 1 308 ASN 308 303 303 ASN ASN A . n 
A 1 309 ASP 309 304 304 ASP ASP A . n 
A 1 310 GLU 310 305 305 GLU GLU A . n 
A 1 311 LYS 311 306 306 LYS LYS A . n 
A 1 312 ASP 312 307 307 ASP ASP A . n 
A 1 313 ILE 313 308 308 ILE ILE A . n 
A 1 314 GLU 314 309 309 GLU GLU A . n 
A 1 315 PRO 315 310 310 PRO PRO A . n 
A 1 316 ALA 316 311 311 ALA ALA A . n 
A 1 317 ALA 317 312 312 ALA ALA A . n 
A 1 318 GLY 318 313 313 GLY GLY A . n 
A 1 319 LEU 319 314 314 LEU LEU A . n 
A 1 320 LEU 320 315 315 LEU LEU A . n 
A 1 321 ASP 321 316 316 ASP ASP A . n 
A 1 322 GLU 322 317 317 GLU GLU A . n 
A 1 323 ASN 323 318 318 ASN ASN A . n 
A 1 324 ARG 324 319 319 ARG ARG A . n 
A 1 325 PRO 325 320 320 PRO PRO A . n 
A 1 326 ALA 326 321 321 ALA ALA A . n 
A 1 327 ARG 327 322 322 ARG ARG A . n 
A 1 328 TYR 328 323 323 TYR TYR A . n 
A 1 329 ARG 329 324 324 ARG ARG A . n 
A 1 330 LYS 330 325 325 LYS LYS A . n 
A 1 331 VAL 331 326 326 VAL VAL A . n 
A 1 332 SER 332 327 327 SER SER A . n 
A 1 333 VAL 333 328 328 VAL VAL A . n 
A 1 334 GLU 334 329 329 GLU GLU A . n 
A 1 335 GLU 335 330 330 GLU GLU A . n 
A 1 336 PHE 336 331 331 PHE PHE A . n 
A 1 337 ARG 337 332 332 ARG ARG A . n 
A 1 338 ALA 338 333 333 ALA ALA A . n 
A 1 339 GLY 339 334 334 GLY GLY A . n 
A 1 340 ILE 340 335 335 ILE ILE A . n 
A 1 341 PHE 341 336 336 PHE PHE A . n 
A 1 342 GLY 342 337 337 GLY GLY A . n 
A 1 343 LYS 343 338 338 LYS LYS A . n 
A 1 344 PHE 344 339 339 PHE PHE A . n 
A 1 345 SER 345 340 340 SER SER A . n 
A 1 346 ARG 346 341 341 ARG ARG A . n 
A 1 347 GLY 347 342 342 GLY GLY A . n 
A 1 348 GLU 348 343 343 GLU GLU A . n 
A 1 349 ARG 349 344 344 ARG ARG A . n 
A 1 350 TYR 350 345 345 TYR TYR A . n 
A 1 351 ILE 351 346 346 ILE ILE A . n 
A 1 352 ASP 352 347 347 ASP ASP A . n 
A 1 353 SER 353 348 348 SER SER A . n 
A 1 354 LEU 354 349 349 LEU LEU A . n 
A 1 355 ARG 355 350 350 ARG ARG A . n 
A 1 356 ILE 356 351 351 ILE ILE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PE8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PE8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MN  1   401 400 MN  MN  A . 
C 3 AKG 1   402 401 AKG AKG A . 
D 4 PE8 1   403 501 PE8 PG9 A . 
E 5 HOH 1   501 165 HOH HOH A . 
E 5 HOH 2   502 224 HOH HOH A . 
E 5 HOH 3   503 186 HOH HOH A . 
E 5 HOH 4   504 118 HOH HOH A . 
E 5 HOH 5   505 1   HOH HOH A . 
E 5 HOH 6   506 202 HOH HOH A . 
E 5 HOH 7   507 204 HOH HOH A . 
E 5 HOH 8   508 234 HOH HOH A . 
E 5 HOH 9   509 3   HOH HOH A . 
E 5 HOH 10  510 60  HOH HOH A . 
E 5 HOH 11  511 241 HOH HOH A . 
E 5 HOH 12  512 112 HOH HOH A . 
E 5 HOH 13  513 115 HOH HOH A . 
E 5 HOH 14  514 211 HOH HOH A . 
E 5 HOH 15  515 50  HOH HOH A . 
E 5 HOH 16  516 62  HOH HOH A . 
E 5 HOH 17  517 10  HOH HOH A . 
E 5 HOH 18  518 183 HOH HOH A . 
E 5 HOH 19  519 106 HOH HOH A . 
E 5 HOH 20  520 213 HOH HOH A . 
E 5 HOH 21  521 114 HOH HOH A . 
E 5 HOH 22  522 208 HOH HOH A . 
E 5 HOH 23  523 128 HOH HOH A . 
E 5 HOH 24  524 139 HOH HOH A . 
E 5 HOH 25  525 97  HOH HOH A . 
E 5 HOH 26  526 229 HOH HOH A . 
E 5 HOH 27  527 41  HOH HOH A . 
E 5 HOH 28  528 21  HOH HOH A . 
E 5 HOH 29  529 78  HOH HOH A . 
E 5 HOH 30  530 232 HOH HOH A . 
E 5 HOH 31  531 7   HOH HOH A . 
E 5 HOH 32  532 147 HOH HOH A . 
E 5 HOH 33  533 177 HOH HOH A . 
E 5 HOH 34  534 160 HOH HOH A . 
E 5 HOH 35  535 127 HOH HOH A . 
E 5 HOH 36  536 14  HOH HOH A . 
E 5 HOH 37  537 242 HOH HOH A . 
E 5 HOH 38  538 26  HOH HOH A . 
E 5 HOH 39  539 18  HOH HOH A . 
E 5 HOH 40  540 248 HOH HOH A . 
E 5 HOH 41  541 145 HOH HOH A . 
E 5 HOH 42  542 57  HOH HOH A . 
E 5 HOH 43  543 210 HOH HOH A . 
E 5 HOH 44  544 172 HOH HOH A . 
E 5 HOH 45  545 212 HOH HOH A . 
E 5 HOH 46  546 30  HOH HOH A . 
E 5 HOH 47  547 39  HOH HOH A . 
E 5 HOH 48  548 84  HOH HOH A . 
E 5 HOH 49  549 126 HOH HOH A . 
E 5 HOH 50  550 124 HOH HOH A . 
E 5 HOH 51  551 222 HOH HOH A . 
E 5 HOH 52  552 56  HOH HOH A . 
E 5 HOH 53  553 136 HOH HOH A . 
E 5 HOH 54  554 164 HOH HOH A . 
E 5 HOH 55  555 17  HOH HOH A . 
E 5 HOH 56  556 28  HOH HOH A . 
E 5 HOH 57  557 73  HOH HOH A . 
E 5 HOH 58  558 5   HOH HOH A . 
E 5 HOH 59  559 250 HOH HOH A . 
E 5 HOH 60  560 221 HOH HOH A . 
E 5 HOH 61  561 225 HOH HOH A . 
E 5 HOH 62  562 91  HOH HOH A . 
E 5 HOH 63  563 95  HOH HOH A . 
E 5 HOH 64  564 54  HOH HOH A . 
E 5 HOH 65  565 194 HOH HOH A . 
E 5 HOH 66  566 99  HOH HOH A . 
E 5 HOH 67  567 130 HOH HOH A . 
E 5 HOH 68  568 140 HOH HOH A . 
E 5 HOH 69  569 156 HOH HOH A . 
E 5 HOH 70  570 135 HOH HOH A . 
E 5 HOH 71  571 42  HOH HOH A . 
E 5 HOH 72  572 249 HOH HOH A . 
E 5 HOH 73  573 43  HOH HOH A . 
E 5 HOH 74  574 102 HOH HOH A . 
E 5 HOH 75  575 203 HOH HOH A . 
E 5 HOH 76  576 93  HOH HOH A . 
E 5 HOH 77  577 13  HOH HOH A . 
E 5 HOH 78  578 120 HOH HOH A . 
E 5 HOH 79  579 173 HOH HOH A . 
E 5 HOH 80  580 142 HOH HOH A . 
E 5 HOH 81  581 88  HOH HOH A . 
E 5 HOH 82  582 8   HOH HOH A . 
E 5 HOH 83  583 20  HOH HOH A . 
E 5 HOH 84  584 11  HOH HOH A . 
E 5 HOH 85  585 191 HOH HOH A . 
E 5 HOH 86  586 2   HOH HOH A . 
E 5 HOH 87  587 68  HOH HOH A . 
E 5 HOH 88  588 100 HOH HOH A . 
E 5 HOH 89  589 32  HOH HOH A . 
E 5 HOH 90  590 169 HOH HOH A . 
E 5 HOH 91  591 44  HOH HOH A . 
E 5 HOH 92  592 12  HOH HOH A . 
E 5 HOH 93  593 90  HOH HOH A . 
E 5 HOH 94  594 4   HOH HOH A . 
E 5 HOH 95  595 166 HOH HOH A . 
E 5 HOH 96  596 98  HOH HOH A . 
E 5 HOH 97  597 121 HOH HOH A . 
E 5 HOH 98  598 104 HOH HOH A . 
E 5 HOH 99  599 201 HOH HOH A . 
E 5 HOH 100 600 15  HOH HOH A . 
E 5 HOH 101 601 23  HOH HOH A . 
E 5 HOH 102 602 81  HOH HOH A . 
E 5 HOH 103 603 58  HOH HOH A . 
E 5 HOH 104 604 110 HOH HOH A . 
E 5 HOH 105 605 74  HOH HOH A . 
E 5 HOH 106 606 64  HOH HOH A . 
E 5 HOH 107 607 125 HOH HOH A . 
E 5 HOH 108 608 122 HOH HOH A . 
E 5 HOH 109 609 153 HOH HOH A . 
E 5 HOH 110 610 69  HOH HOH A . 
E 5 HOH 111 611 137 HOH HOH A . 
E 5 HOH 112 612 94  HOH HOH A . 
E 5 HOH 113 613 29  HOH HOH A . 
E 5 HOH 114 614 89  HOH HOH A . 
E 5 HOH 115 615 132 HOH HOH A . 
E 5 HOH 116 616 35  HOH HOH A . 
E 5 HOH 117 617 53  HOH HOH A . 
E 5 HOH 118 618 33  HOH HOH A . 
E 5 HOH 119 619 113 HOH HOH A . 
E 5 HOH 120 620 24  HOH HOH A . 
E 5 HOH 121 621 189 HOH HOH A . 
E 5 HOH 122 622 129 HOH HOH A . 
E 5 HOH 123 623 9   HOH HOH A . 
E 5 HOH 124 624 174 HOH HOH A . 
E 5 HOH 125 625 251 HOH HOH A . 
E 5 HOH 126 626 19  HOH HOH A . 
E 5 HOH 127 627 83  HOH HOH A . 
E 5 HOH 128 628 226 HOH HOH A . 
E 5 HOH 129 629 45  HOH HOH A . 
E 5 HOH 130 630 116 HOH HOH A . 
E 5 HOH 131 631 77  HOH HOH A . 
E 5 HOH 132 632 185 HOH HOH A . 
E 5 HOH 133 633 27  HOH HOH A . 
E 5 HOH 134 634 71  HOH HOH A . 
E 5 HOH 135 635 168 HOH HOH A . 
E 5 HOH 136 636 190 HOH HOH A . 
E 5 HOH 137 637 6   HOH HOH A . 
E 5 HOH 138 638 38  HOH HOH A . 
E 5 HOH 139 639 49  HOH HOH A . 
E 5 HOH 140 640 244 HOH HOH A . 
E 5 HOH 141 641 197 HOH HOH A . 
E 5 HOH 142 642 87  HOH HOH A . 
E 5 HOH 143 643 36  HOH HOH A . 
E 5 HOH 144 644 149 HOH HOH A . 
E 5 HOH 145 645 117 HOH HOH A . 
E 5 HOH 146 646 34  HOH HOH A . 
E 5 HOH 147 647 25  HOH HOH A . 
E 5 HOH 148 648 67  HOH HOH A . 
E 5 HOH 149 649 46  HOH HOH A . 
E 5 HOH 150 650 119 HOH HOH A . 
E 5 HOH 151 651 37  HOH HOH A . 
E 5 HOH 152 652 55  HOH HOH A . 
E 5 HOH 153 653 199 HOH HOH A . 
E 5 HOH 154 654 150 HOH HOH A . 
E 5 HOH 155 655 76  HOH HOH A . 
E 5 HOH 156 656 86  HOH HOH A . 
E 5 HOH 157 657 184 HOH HOH A . 
E 5 HOH 158 658 144 HOH HOH A . 
E 5 HOH 159 659 52  HOH HOH A . 
E 5 HOH 160 660 92  HOH HOH A . 
E 5 HOH 161 661 79  HOH HOH A . 
E 5 HOH 162 662 103 HOH HOH A . 
E 5 HOH 163 663 31  HOH HOH A . 
E 5 HOH 164 664 65  HOH HOH A . 
E 5 HOH 165 665 51  HOH HOH A . 
E 5 HOH 166 666 111 HOH HOH A . 
E 5 HOH 167 667 72  HOH HOH A . 
E 5 HOH 168 668 16  HOH HOH A . 
E 5 HOH 169 669 47  HOH HOH A . 
E 5 HOH 170 670 233 HOH HOH A . 
E 5 HOH 171 671 178 HOH HOH A . 
E 5 HOH 172 672 96  HOH HOH A . 
E 5 HOH 173 673 123 HOH HOH A . 
E 5 HOH 174 674 228 HOH HOH A . 
E 5 HOH 175 675 192 HOH HOH A . 
E 5 HOH 176 676 245 HOH HOH A . 
E 5 HOH 177 677 40  HOH HOH A . 
E 5 HOH 178 678 243 HOH HOH A . 
E 5 HOH 179 679 22  HOH HOH A . 
E 5 HOH 180 680 133 HOH HOH A . 
E 5 HOH 181 681 182 HOH HOH A . 
E 5 HOH 182 682 154 HOH HOH A . 
E 5 HOH 183 683 176 HOH HOH A . 
E 5 HOH 184 684 236 HOH HOH A . 
E 5 HOH 185 685 171 HOH HOH A . 
E 5 HOH 186 686 195 HOH HOH A . 
E 5 HOH 187 687 85  HOH HOH A . 
E 5 HOH 188 688 59  HOH HOH A . 
E 5 HOH 189 689 107 HOH HOH A . 
E 5 HOH 190 690 109 HOH HOH A . 
E 5 HOH 191 691 200 HOH HOH A . 
E 5 HOH 192 692 206 HOH HOH A . 
E 5 HOH 193 693 163 HOH HOH A . 
E 5 HOH 194 694 131 HOH HOH A . 
E 5 HOH 195 695 198 HOH HOH A . 
E 5 HOH 196 696 75  HOH HOH A . 
E 5 HOH 197 697 143 HOH HOH A . 
E 5 HOH 198 698 216 HOH HOH A . 
E 5 HOH 199 699 179 HOH HOH A . 
E 5 HOH 200 700 161 HOH HOH A . 
E 5 HOH 201 701 218 HOH HOH A . 
E 5 HOH 202 702 101 HOH HOH A . 
E 5 HOH 203 703 235 HOH HOH A . 
E 5 HOH 204 704 188 HOH HOH A . 
E 5 HOH 205 705 105 HOH HOH A . 
E 5 HOH 206 706 134 HOH HOH A . 
E 5 HOH 207 707 180 HOH HOH A . 
E 5 HOH 208 708 187 HOH HOH A . 
E 5 HOH 209 709 158 HOH HOH A . 
E 5 HOH 210 710 82  HOH HOH A . 
E 5 HOH 211 711 61  HOH HOH A . 
E 5 HOH 212 712 231 HOH HOH A . 
E 5 HOH 213 713 215 HOH HOH A . 
E 5 HOH 214 714 146 HOH HOH A . 
E 5 HOH 215 715 159 HOH HOH A . 
E 5 HOH 216 716 80  HOH HOH A . 
E 5 HOH 217 717 162 HOH HOH A . 
E 5 HOH 218 718 223 HOH HOH A . 
E 5 HOH 219 719 152 HOH HOH A . 
E 5 HOH 220 720 108 HOH HOH A . 
E 5 HOH 221 721 239 HOH HOH A . 
E 5 HOH 222 722 227 HOH HOH A . 
E 5 HOH 223 723 252 HOH HOH A . 
E 5 HOH 224 724 175 HOH HOH A . 
E 5 HOH 225 725 70  HOH HOH A . 
E 5 HOH 226 726 66  HOH HOH A . 
E 5 HOH 227 727 205 HOH HOH A . 
E 5 HOH 228 728 247 HOH HOH A . 
E 5 HOH 229 729 209 HOH HOH A . 
E 5 HOH 230 730 138 HOH HOH A . 
E 5 HOH 231 731 151 HOH HOH A . 
E 5 HOH 232 732 148 HOH HOH A . 
E 5 HOH 233 733 63  HOH HOH A . 
E 5 HOH 234 734 157 HOH HOH A . 
E 5 HOH 235 735 220 HOH HOH A . 
E 5 HOH 236 736 141 HOH HOH A . 
E 5 HOH 237 737 237 HOH HOH A . 
E 5 HOH 238 738 193 HOH HOH A . 
E 5 HOH 239 739 196 HOH HOH A . 
E 5 HOH 240 740 214 HOH HOH A . 
E 5 HOH 241 741 246 HOH HOH A . 
E 5 HOH 242 742 48  HOH HOH A . 
E 5 HOH 243 743 155 HOH HOH A . 
E 5 HOH 244 744 170 HOH HOH A . 
E 5 HOH 245 745 207 HOH HOH A . 
E 5 HOH 246 746 238 HOH HOH A . 
E 5 HOH 247 747 240 HOH HOH A . 
E 5 HOH 248 748 181 HOH HOH A . 
E 5 HOH 249 749 230 HOH HOH A . 
E 5 HOH 250 750 217 HOH HOH A . 
E 5 HOH 251 751 167 HOH HOH A . 
E 5 HOH 252 752 219 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   92.090 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S7B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.332 
_cell.length_a_esd                 ? 
_cell.length_b                     67.432 
_cell.length_b_esd                 ? 
_cell.length_c                     83.176 
_cell.length_c_esd                 ? 
_cell.volume                       383000.379 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8S7B 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S7B 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.43 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.15 M Magnesium acetate tetrahydrate
0.1 M Sodium citrate 5.6 
20 % v/v PEG Smear Broad

15% Glycerol used for collection
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             100 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-21 
_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   0.9762 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9762 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          25.590 
_reflns.entry_id                                       8S7B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               47.98 
_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                                     38126 
_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                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.065 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.060 
_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                                    1.75 
_reflns_shell.d_res_low                                     1.878 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1899 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.979 
_reflns_shell.pdbx_Rpim_I_all                               0.389 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.804 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.895 
_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                               39.92 
_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                                 8S7B 
_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                            1.75 
_refine.ls_d_res_low                             47.98 
_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                     38097 
_refine.ls_number_reflns_R_free                  1983 
_refine.ls_number_reflns_R_work                  36114 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_percent_reflns_R_free                 5.21 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1762 
_refine.ls_R_factor_R_free                       0.2026 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1747 
_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                          1.39 
_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             1.1000 
_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                 23.7367 
_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                            0.1852 
_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                       1.75 
_refine_hist.d_res_low                        47.98 
_refine_hist.number_atoms_solvent             252 
_refine_hist.number_atoms_total               3109 
_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        2821 
_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' ? 0.0037  ? 2935 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6071  ? 3969 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0451  ? 426  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0051  ? 529  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.6093 ? 1136 ? 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' 1.75 1.79  . . 140 2557 97.79  . . . . 0.3373 . . . . . . . . . . . 0.3643 
'X-RAY DIFFRACTION' 1.79 1.84  . . 148 2568 99.56  . . . . 0.2733 . . . . . . . . . . . 0.2874 
'X-RAY DIFFRACTION' 1.84 1.90  . . 143 2535 99.93  . . . . 0.2317 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 1.90 1.96  . . 120 2575 99.67  . . . . 0.2210 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.96 2.03  . . 105 2624 99.82  . . . . 0.2006 . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 2.03 2.11  . . 167 2540 99.93  . . . . 0.1811 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 2.11 2.20  . . 125 2603 99.89  . . . . 0.1804 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 2.20 2.32  . . 162 2549 99.93  . . . . 0.1737 . . . . . . . . . . . 0.2299 
'X-RAY DIFFRACTION' 2.32 2.47  . . 165 2521 99.81  . . . . 0.1800 . . . . . . . . . . . 0.2423 
'X-RAY DIFFRACTION' 2.47 2.66  . . 145 2587 99.53  . . . . 0.1809 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 2.66 2.92  . . 118 2609 100.00 . . . . 0.1794 . . . . . . . . . . . 0.2414 
'X-RAY DIFFRACTION' 2.92 3.35  . . 122 2619 100.00 . . . . 0.1703 . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 3.35 4.21  . . 182 2566 99.93  . . . . 0.1497 . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 4.22 47.98 . . 141 2661 99.75  . . . . 0.1582 . . . . . . . . . . . 0.1761 
# 
_struct.entry_id                     8S7B 
_struct.title                        'Fe(II)-2-oxoglutarate-dependent Oryza sativa dioxygenase His1 in complex with 2-oxoglutarate' 
_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        8S7B 
_struct_keywords.text            'His1, HPPD-resistance, oxygenase, 2-oxoglutarate, complex, inhibitor, rice, OXYGEN BINDING' 
_struct_keywords.pdbx_keywords   'OXYGEN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q6ES21_ORYSJ 
_struct_ref.pdbx_db_accession          Q6ES21 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MADESWRAPAIVQELAAAGVEEPPSRYLLREKDRSDVKLVAAELPEPLPVVDLSRLDGAEEATKLRVALQNWGFFLLTNH
GVEASLMDSVMNLSREFFNQPIERKQKFSNLIDGKNFQIQGYGTDRVVTQDQILDWSDRLHLRVEPKEEQDLAFWPDHPE
SFRDVLNKYASGTKRIRDDIIQAMAKLLELDEDYFLDRLNEAPAFARFNYYPPCPRPDLVFGIRPHSDGTLLTILLVDKD
VSGLQVQRDGKWSNVEATPHTLLINLGDTMEVMCNGIFRSPVHRVVTNAEKERISLAMLYSVNDEKDIEPAAGLLDENRP
ARYRKVSVEEFRAGIFGKFSRGERYIDSLRI
;
_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              8S7B 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 6 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 356 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q6ES21 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  351 
_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       351 
# 
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 8S7B GLY A 1 ? UNP Q6ES21 ? ? 'expression tag' -4 1 
1 8S7B HIS A 2 ? UNP Q6ES21 ? ? 'expression tag' -3 2 
1 8S7B MET A 3 ? UNP Q6ES21 ? ? 'expression tag' -2 3 
1 8S7B ALA A 4 ? UNP Q6ES21 ? ? 'expression tag' -1 4 
1 8S7B SER A 5 ? UNP Q6ES21 ? ? 'expression tag' 0  5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 GLU A 9   ? ALA A 13  ? GLU A 4   ALA A 8   5 ? 5  
HELX_P HELX_P2  AA2 ILE A 16  ? GLY A 24  ? ILE A 11  GLY A 19  1 ? 9  
HELX_P HELX_P3  AA3 PRO A 29  ? LEU A 33  ? PRO A 24  LEU A 28  5 ? 5  
HELX_P HELX_P4  AA4 ASP A 38  ? VAL A 42  ? ASP A 33  VAL A 37  5 ? 5  
HELX_P HELX_P5  AA5 SER A 59  ? LEU A 61  ? SER A 54  LEU A 56  5 ? 3  
HELX_P HELX_P6  AA6 GLY A 63  ? TRP A 77  ? GLY A 58  TRP A 72  1 ? 15 
HELX_P HELX_P7  AA7 GLU A 88  ? ASN A 104 ? GLU A 83  ASN A 99  1 ? 17 
HELX_P HELX_P8  AA8 PRO A 106 ? GLN A 111 ? PRO A 101 GLN A 106 1 ? 6  
HELX_P HELX_P9  AA9 LYS A 112 ? SER A 114 ? LYS A 107 SER A 109 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 118 ? LYS A 120 ? ASP A 113 LYS A 115 5 ? 3  
HELX_P HELX_P11 AB2 PRO A 151 ? GLN A 155 ? PRO A 146 GLN A 150 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 156 ? TRP A 160 ? ASP A 151 TRP A 155 5 ? 5  
HELX_P HELX_P13 AB4 SER A 166 ? LEU A 193 ? SER A 161 LEU A 188 1 ? 28 
HELX_P HELX_P14 AB5 ASP A 198 ? ARG A 203 ? ASP A 193 ARG A 198 1 ? 6  
HELX_P HELX_P15 AB6 GLY A 272 ? CYS A 279 ? GLY A 267 CYS A 274 1 ? 8  
HELX_P HELX_P16 AB7 ALA A 316 ? LEU A 320 ? ALA A 311 LEU A 315 5 ? 5  
HELX_P HELX_P17 AB8 SER A 332 ? ARG A 346 ? SER A 327 ARG A 341 1 ? 15 
HELX_P HELX_P18 AB9 ARG A 349 ? ARG A 355 ? ARG A 344 ARG A 350 1 ? 7  
# 
_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 
metalc1 metalc ? ? A HIS 231 NE2 ? ? ? 1_555 B MN  . MN ? ? A HIS 226 A MN  401 1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc2 metalc ? ? A ASP 233 OD1 ? ? ? 1_555 B MN  . MN ? ? A ASP 228 A MN  401 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc3 metalc ? ? A HIS 288 NE2 ? ? ? 1_555 B MN  . MN ? ? A HIS 283 A MN  401 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc4 metalc ? ? B MN  .   MN  ? ? ? 1_555 C AKG . O1 ? ? A MN  401 A AKG 402 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc5 metalc ? ? B MN  .   MN  ? ? ? 1_555 C AKG . O5 ? ? A MN  401 A AKG 402 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc6 metalc ? ? B MN  .   MN  ? ? ? 1_555 E HOH . O  ? ? A MN  401 A HOH 549 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 231 ? A HIS 226 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 OD1 ? A ASP 233 ? A ASP 228 ? 1_555 90.7  ? 
2  NE2 ? A HIS 231 ? A HIS 226 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 NE2 ? A HIS 288 ? A HIS 283 ? 1_555 86.6  ? 
3  OD1 ? A ASP 233 ? A ASP 228 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 NE2 ? A HIS 288 ? A HIS 283 ? 1_555 95.5  ? 
4  NE2 ? A HIS 231 ? A HIS 226 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O1  ? C AKG .   ? A AKG 402 ? 1_555 100.1 ? 
5  OD1 ? A ASP 233 ? A ASP 228 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O1  ? C AKG .   ? A AKG 402 ? 1_555 97.8  ? 
6  NE2 ? A HIS 288 ? A HIS 283 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O1  ? C AKG .   ? A AKG 402 ? 1_555 165.0 ? 
7  NE2 ? A HIS 231 ? A HIS 226 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O5  ? C AKG .   ? A AKG 402 ? 1_555 96.5  ? 
8  OD1 ? A ASP 233 ? A ASP 228 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O5  ? C AKG .   ? A AKG 402 ? 1_555 172.8 ? 
9  NE2 ? A HIS 288 ? A HIS 283 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O5  ? C AKG .   ? A AKG 402 ? 1_555 85.2  ? 
10 O1  ? C AKG .   ? A AKG 402 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O5  ? C AKG .   ? A AKG 402 ? 1_555 80.7  ? 
11 NE2 ? A HIS 231 ? A HIS 226 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O   ? E HOH .   ? A HOH 549 ? 1_555 172.2 ? 
12 OD1 ? A ASP 233 ? A ASP 228 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O   ? E HOH .   ? A HOH 549 ? 1_555 92.5  ? 
13 NE2 ? A HIS 288 ? A HIS 283 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O   ? E HOH .   ? A HOH 549 ? 1_555 86.0  ? 
14 O1  ? C AKG .   ? A AKG 402 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O   ? E HOH .   ? A HOH 549 ? 1_555 86.6  ? 
15 O5  ? C AKG .   ? A AKG 402 ? 1_555 MN ? B MN . ? A MN 401 ? 1_555 O   ? E HOH .   ? A HOH 549 ? 1_555 80.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 150 A . ? GLU 145 A PRO 151 A ? PRO 146 A 1 -2.47 
2 HIS 163 A . ? HIS 158 A PRO 164 A ? PRO 159 A 1 1.10  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? 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 VAL A 55  ? ASP A 57  ? VAL A 50  ASP A 52  
AA1 2 PHE A 79  ? THR A 83  ? PHE A 74  THR A 78  
AA1 3 LEU A 267 ? LEU A 271 ? LEU A 262 LEU A 266 
AA1 4 LEU A 237 ? VAL A 242 ? LEU A 232 VAL A 237 
AA1 5 ARG A 298 ? TYR A 305 ? ARG A 293 TYR A 300 
AA1 6 ALA A 209 ? TYR A 216 ? ALA A 204 TYR A 211 
AA1 7 ASP A 143 ? GLU A 150 ? ASP A 138 GLU A 145 
AA1 8 GLY A 126 ? GLY A 128 ? GLY A 121 GLY A 123 
AA2 1 LEU A 116 ? ILE A 117 ? LEU A 111 ILE A 112 
AA2 2 ASN A 121 ? PHE A 122 ? ASN A 116 PHE A 117 
AA3 1 ILE A 228 ? HIS A 231 ? ILE A 223 HIS A 226 
AA3 2 HIS A 288 ? VAL A 290 ? HIS A 283 VAL A 285 
AA3 3 LEU A 249 ? ARG A 253 ? LEU A 244 ARG A 248 
AA3 4 LYS A 256 ? ASN A 259 ? LYS A 251 ASN A 254 
# 
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 56  ? N VAL A 51  O LEU A 81  ? O LEU A 76  
AA1 2 3 N LEU A 82  ? N LEU A 77  O LEU A 267 ? O LEU A 262 
AA1 3 4 O LEU A 268 ? O LEU A 263 N LEU A 240 ? N LEU A 235 
AA1 4 5 N ILE A 239 ? N ILE A 234 O MET A 303 ? O MET A 298 
AA1 5 6 O ARG A 298 ? O ARG A 293 N TYR A 216 ? N TYR A 211 
AA1 6 7 O ALA A 211 ? O ALA A 206 N LEU A 147 ? N LEU A 142 
AA1 7 8 O ARG A 144 ? O ARG A 139 N GLY A 128 ? N GLY A 123 
AA2 1 2 N ILE A 117 ? N ILE A 112 O ASN A 121 ? O ASN A 116 
AA3 1 2 N HIS A 231 ? N HIS A 226 O HIS A 288 ? O HIS A 283 
AA3 2 3 O ARG A 289 ? O ARG A 284 N GLN A 250 ? N GLN A 245 
AA3 3 4 N ARG A 253 ? N ARG A 248 O LYS A 256 ? O LYS A 251 
# 
_pdbx_entry_details.entry_id                   8S7B 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 657 ? ? O A HOH 745 ? ? 1.84 
2  1 NH1 A ARG 66  ? ? O A HOH 501 ? ? 1.88 
3  1 O   A HOH 675 ? ? O A HOH 686 ? ? 2.04 
4  1 O   A HOH 738 ? ? O A HOH 739 ? ? 2.05 
5  1 O   A HOH 624 ? ? O A HOH 722 ? ? 2.07 
6  1 O   A ALA 42  ? ? O A HOH 502 ? ? 2.08 
7  1 OD1 A ASP 193 ? ? O A HOH 503 ? ? 2.10 
8  1 O   A HOH 681 ? ? O A HOH 740 ? ? 2.12 
9  1 ND2 A ASN 99  ? ? O A HOH 504 ? ? 2.15 
10 1 O   A HOH 501 ? ? O A HOH 512 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 670 ? ? 1_555 O A HOH 721 ? ? 4_546 1.90 
2 1 O A HOH 554 ? ? 1_555 O A HOH 709 ? ? 4_556 2.03 
3 1 O A HOH 622 ? ? 1_555 O A HOH 622 ? ? 2_656 2.17 
# 
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 GLU A 31  ? ? 47.55   -66.39 
2 1 GLU A 43  ? ? 75.83   -35.07 
3 1 ASP A 113 ? ? 58.81   13.77  
4 1 LYS A 115 ? ? -148.67 -34.68 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 505 ? E HOH . 
2 1 A HOH 506 ? E HOH . 
3 1 A HOH 752 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         20.6140747179 
_pdbx_refine_tls.origin_y         1.39237469669 
_pdbx_refine_tls.origin_z         23.2583054893 
_pdbx_refine_tls.T[1][1]          0.193578109379 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0113935308294 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0015900728817 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.150925441845 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0227925512927 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.145852720916 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.31763839981 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.591009648164 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.236034349056 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.57930783224 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.277977235628 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.57955679086 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0210192495963 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.243632810417 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.105632429363 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.278506454832 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0567507389546 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.113501459749 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0369391302296 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0388906313585 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0336368322102 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     2 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     401 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   'chain A' 
# 
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 GLY -4 ? A GLY 1 
2 1 Y 1 A HIS -3 ? A HIS 2 
3 1 Y 1 A MET -2 ? A MET 3 
4 1 Y 1 A ALA -1 ? A ALA 4 
5 1 Y 1 A SER 0  ? A SER 5 
6 1 Y 1 A MET 1  ? A MET 6 
# 
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 
AKG C1   C  N N 1   
AKG O1   O  N N 2   
AKG O2   O  N N 3   
AKG C2   C  N N 4   
AKG O5   O  N N 5   
AKG C3   C  N N 6   
AKG C4   C  N N 7   
AKG C5   C  N N 8   
AKG O3   O  N N 9   
AKG O4   O  N N 10  
AKG HO2  H  N N 11  
AKG H31  H  N N 12  
AKG H32  H  N N 13  
AKG H41  H  N N 14  
AKG H42  H  N N 15  
AKG HO4  H  N N 16  
ALA N    N  N N 17  
ALA CA   C  N S 18  
ALA C    C  N N 19  
ALA O    O  N N 20  
ALA CB   C  N N 21  
ALA OXT  O  N N 22  
ALA H    H  N N 23  
ALA H2   H  N N 24  
ALA HA   H  N N 25  
ALA HB1  H  N N 26  
ALA HB2  H  N N 27  
ALA HB3  H  N N 28  
ALA HXT  H  N N 29  
ARG N    N  N N 30  
ARG CA   C  N S 31  
ARG C    C  N N 32  
ARG O    O  N N 33  
ARG CB   C  N N 34  
ARG CG   C  N N 35  
ARG CD   C  N N 36  
ARG NE   N  N N 37  
ARG CZ   C  N N 38  
ARG NH1  N  N N 39  
ARG NH2  N  N N 40  
ARG OXT  O  N N 41  
ARG H    H  N N 42  
ARG H2   H  N N 43  
ARG HA   H  N N 44  
ARG HB2  H  N N 45  
ARG HB3  H  N N 46  
ARG HG2  H  N N 47  
ARG HG3  H  N N 48  
ARG HD2  H  N N 49  
ARG HD3  H  N N 50  
ARG HE   H  N N 51  
ARG HH11 H  N N 52  
ARG HH12 H  N N 53  
ARG HH21 H  N N 54  
ARG HH22 H  N N 55  
ARG HXT  H  N N 56  
ASN N    N  N N 57  
ASN CA   C  N S 58  
ASN C    C  N N 59  
ASN O    O  N N 60  
ASN CB   C  N N 61  
ASN CG   C  N N 62  
ASN OD1  O  N N 63  
ASN ND2  N  N N 64  
ASN OXT  O  N N 65  
ASN H    H  N N 66  
ASN H2   H  N N 67  
ASN HA   H  N N 68  
ASN HB2  H  N N 69  
ASN HB3  H  N N 70  
ASN HD21 H  N N 71  
ASN HD22 H  N N 72  
ASN HXT  H  N N 73  
ASP N    N  N N 74  
ASP CA   C  N S 75  
ASP C    C  N N 76  
ASP O    O  N N 77  
ASP CB   C  N N 78  
ASP CG   C  N N 79  
ASP OD1  O  N N 80  
ASP OD2  O  N N 81  
ASP OXT  O  N N 82  
ASP H    H  N N 83  
ASP H2   H  N N 84  
ASP HA   H  N N 85  
ASP HB2  H  N N 86  
ASP HB3  H  N N 87  
ASP HD2  H  N N 88  
ASP HXT  H  N N 89  
CYS N    N  N N 90  
CYS CA   C  N R 91  
CYS C    C  N N 92  
CYS O    O  N N 93  
CYS CB   C  N N 94  
CYS SG   S  N N 95  
CYS OXT  O  N N 96  
CYS H    H  N N 97  
CYS H2   H  N N 98  
CYS HA   H  N N 99  
CYS HB2  H  N N 100 
CYS HB3  H  N N 101 
CYS HG   H  N N 102 
CYS HXT  H  N N 103 
GLN N    N  N N 104 
GLN CA   C  N S 105 
GLN C    C  N N 106 
GLN O    O  N N 107 
GLN CB   C  N N 108 
GLN CG   C  N N 109 
GLN CD   C  N N 110 
GLN OE1  O  N N 111 
GLN NE2  N  N N 112 
GLN OXT  O  N N 113 
GLN H    H  N N 114 
GLN H2   H  N N 115 
GLN HA   H  N N 116 
GLN HB2  H  N N 117 
GLN HB3  H  N N 118 
GLN HG2  H  N N 119 
GLN HG3  H  N N 120 
GLN HE21 H  N N 121 
GLN HE22 H  N N 122 
GLN HXT  H  N N 123 
GLU N    N  N N 124 
GLU CA   C  N S 125 
GLU C    C  N N 126 
GLU O    O  N N 127 
GLU CB   C  N N 128 
GLU CG   C  N N 129 
GLU CD   C  N N 130 
GLU OE1  O  N N 131 
GLU OE2  O  N N 132 
GLU OXT  O  N N 133 
GLU H    H  N N 134 
GLU H2   H  N N 135 
GLU HA   H  N N 136 
GLU HB2  H  N N 137 
GLU HB3  H  N N 138 
GLU HG2  H  N N 139 
GLU HG3  H  N N 140 
GLU HE2  H  N N 141 
GLU HXT  H  N N 142 
GLY N    N  N N 143 
GLY CA   C  N N 144 
GLY C    C  N N 145 
GLY O    O  N N 146 
GLY OXT  O  N N 147 
GLY H    H  N N 148 
GLY H2   H  N N 149 
GLY HA2  H  N N 150 
GLY HA3  H  N N 151 
GLY HXT  H  N N 152 
HIS N    N  N N 153 
HIS CA   C  N S 154 
HIS C    C  N N 155 
HIS O    O  N N 156 
HIS CB   C  N N 157 
HIS CG   C  Y N 158 
HIS ND1  N  Y N 159 
HIS CD2  C  Y N 160 
HIS CE1  C  Y N 161 
HIS NE2  N  Y N 162 
HIS OXT  O  N N 163 
HIS H    H  N N 164 
HIS H2   H  N N 165 
HIS HA   H  N N 166 
HIS HB2  H  N N 167 
HIS HB3  H  N N 168 
HIS HD1  H  N N 169 
HIS HD2  H  N N 170 
HIS HE1  H  N N 171 
HIS HE2  H  N N 172 
HIS HXT  H  N N 173 
HOH O    O  N N 174 
HOH H1   H  N N 175 
HOH H2   H  N N 176 
ILE N    N  N N 177 
ILE CA   C  N S 178 
ILE C    C  N N 179 
ILE O    O  N N 180 
ILE CB   C  N S 181 
ILE CG1  C  N N 182 
ILE CG2  C  N N 183 
ILE CD1  C  N N 184 
ILE OXT  O  N N 185 
ILE H    H  N N 186 
ILE H2   H  N N 187 
ILE HA   H  N N 188 
ILE HB   H  N N 189 
ILE HG12 H  N N 190 
ILE HG13 H  N N 191 
ILE HG21 H  N N 192 
ILE HG22 H  N N 193 
ILE HG23 H  N N 194 
ILE HD11 H  N N 195 
ILE HD12 H  N N 196 
ILE HD13 H  N N 197 
ILE HXT  H  N N 198 
LEU N    N  N N 199 
LEU CA   C  N S 200 
LEU C    C  N N 201 
LEU O    O  N N 202 
LEU CB   C  N N 203 
LEU CG   C  N N 204 
LEU CD1  C  N N 205 
LEU CD2  C  N N 206 
LEU OXT  O  N N 207 
LEU H    H  N N 208 
LEU H2   H  N N 209 
LEU HA   H  N N 210 
LEU HB2  H  N N 211 
LEU HB3  H  N N 212 
LEU HG   H  N N 213 
LEU HD11 H  N N 214 
LEU HD12 H  N N 215 
LEU HD13 H  N N 216 
LEU HD21 H  N N 217 
LEU HD22 H  N N 218 
LEU HD23 H  N N 219 
LEU HXT  H  N N 220 
LYS N    N  N N 221 
LYS CA   C  N S 222 
LYS C    C  N N 223 
LYS O    O  N N 224 
LYS CB   C  N N 225 
LYS CG   C  N N 226 
LYS CD   C  N N 227 
LYS CE   C  N N 228 
LYS NZ   N  N N 229 
LYS OXT  O  N N 230 
LYS H    H  N N 231 
LYS H2   H  N N 232 
LYS HA   H  N N 233 
LYS HB2  H  N N 234 
LYS HB3  H  N N 235 
LYS HG2  H  N N 236 
LYS HG3  H  N N 237 
LYS HD2  H  N N 238 
LYS HD3  H  N N 239 
LYS HE2  H  N N 240 
LYS HE3  H  N N 241 
LYS HZ1  H  N N 242 
LYS HZ2  H  N N 243 
LYS HZ3  H  N N 244 
LYS HXT  H  N N 245 
MET N    N  N N 246 
MET CA   C  N S 247 
MET C    C  N N 248 
MET O    O  N N 249 
MET CB   C  N N 250 
MET CG   C  N N 251 
MET SD   S  N N 252 
MET CE   C  N N 253 
MET OXT  O  N N 254 
MET H    H  N N 255 
MET H2   H  N N 256 
MET HA   H  N N 257 
MET HB2  H  N N 258 
MET HB3  H  N N 259 
MET HG2  H  N N 260 
MET HG3  H  N N 261 
MET HE1  H  N N 262 
MET HE2  H  N N 263 
MET HE3  H  N N 264 
MET HXT  H  N N 265 
MN  MN   MN N N 266 
PE8 O1   O  N N 267 
PE8 C2   C  N N 268 
PE8 C3   C  N N 269 
PE8 O4   O  N N 270 
PE8 C5   C  N N 271 
PE8 C6   C  N N 272 
PE8 O7   O  N N 273 
PE8 C8   C  N N 274 
PE8 C9   C  N N 275 
PE8 O10  O  N N 276 
PE8 C11  C  N N 277 
PE8 C12  C  N N 278 
PE8 O13  O  N N 279 
PE8 C14  C  N N 280 
PE8 C15  C  N N 281 
PE8 O16  O  N N 282 
PE8 C17  C  N N 283 
PE8 C18  C  N N 284 
PE8 O19  O  N N 285 
PE8 C20  C  N N 286 
PE8 C21  C  N N 287 
PE8 O22  O  N N 288 
PE8 C23  C  N N 289 
PE8 C24  C  N N 290 
PE8 O25  O  N N 291 
PE8 HO1  H  N N 292 
PE8 H21  H  N N 293 
PE8 H22  H  N N 294 
PE8 H31  H  N N 295 
PE8 H32  H  N N 296 
PE8 H51  H  N N 297 
PE8 H52  H  N N 298 
PE8 H61  H  N N 299 
PE8 H62  H  N N 300 
PE8 H81  H  N N 301 
PE8 H82  H  N N 302 
PE8 H91  H  N N 303 
PE8 H92  H  N N 304 
PE8 H111 H  N N 305 
PE8 H112 H  N N 306 
PE8 H121 H  N N 307 
PE8 H122 H  N N 308 
PE8 H141 H  N N 309 
PE8 H142 H  N N 310 
PE8 H151 H  N N 311 
PE8 H152 H  N N 312 
PE8 H171 H  N N 313 
PE8 H172 H  N N 314 
PE8 H181 H  N N 315 
PE8 H182 H  N N 316 
PE8 H201 H  N N 317 
PE8 H202 H  N N 318 
PE8 H211 H  N N 319 
PE8 H212 H  N N 320 
PE8 H231 H  N N 321 
PE8 H232 H  N N 322 
PE8 H241 H  N N 323 
PE8 H242 H  N N 324 
PE8 H25  H  N N 325 
PHE N    N  N N 326 
PHE CA   C  N S 327 
PHE C    C  N N 328 
PHE O    O  N N 329 
PHE CB   C  N N 330 
PHE CG   C  Y N 331 
PHE CD1  C  Y N 332 
PHE CD2  C  Y N 333 
PHE CE1  C  Y N 334 
PHE CE2  C  Y N 335 
PHE CZ   C  Y N 336 
PHE OXT  O  N N 337 
PHE H    H  N N 338 
PHE H2   H  N N 339 
PHE HA   H  N N 340 
PHE HB2  H  N N 341 
PHE HB3  H  N N 342 
PHE HD1  H  N N 343 
PHE HD2  H  N N 344 
PHE HE1  H  N N 345 
PHE HE2  H  N N 346 
PHE HZ   H  N N 347 
PHE HXT  H  N N 348 
PRO N    N  N N 349 
PRO CA   C  N S 350 
PRO C    C  N N 351 
PRO O    O  N N 352 
PRO CB   C  N N 353 
PRO CG   C  N N 354 
PRO CD   C  N N 355 
PRO OXT  O  N N 356 
PRO H    H  N N 357 
PRO HA   H  N N 358 
PRO HB2  H  N N 359 
PRO HB3  H  N N 360 
PRO HG2  H  N N 361 
PRO HG3  H  N N 362 
PRO HD2  H  N N 363 
PRO HD3  H  N N 364 
PRO HXT  H  N N 365 
SER N    N  N N 366 
SER CA   C  N S 367 
SER C    C  N N 368 
SER O    O  N N 369 
SER CB   C  N N 370 
SER OG   O  N N 371 
SER OXT  O  N N 372 
SER H    H  N N 373 
SER H2   H  N N 374 
SER HA   H  N N 375 
SER HB2  H  N N 376 
SER HB3  H  N N 377 
SER HG   H  N N 378 
SER HXT  H  N N 379 
THR N    N  N N 380 
THR CA   C  N S 381 
THR C    C  N N 382 
THR O    O  N N 383 
THR CB   C  N R 384 
THR OG1  O  N N 385 
THR CG2  C  N N 386 
THR OXT  O  N N 387 
THR H    H  N N 388 
THR H2   H  N N 389 
THR HA   H  N N 390 
THR HB   H  N N 391 
THR HG1  H  N N 392 
THR HG21 H  N N 393 
THR HG22 H  N N 394 
THR HG23 H  N N 395 
THR HXT  H  N N 396 
TRP N    N  N N 397 
TRP CA   C  N S 398 
TRP C    C  N N 399 
TRP O    O  N N 400 
TRP CB   C  N N 401 
TRP CG   C  Y N 402 
TRP CD1  C  Y N 403 
TRP CD2  C  Y N 404 
TRP NE1  N  Y N 405 
TRP CE2  C  Y N 406 
TRP CE3  C  Y N 407 
TRP CZ2  C  Y N 408 
TRP CZ3  C  Y N 409 
TRP CH2  C  Y N 410 
TRP OXT  O  N N 411 
TRP H    H  N N 412 
TRP H2   H  N N 413 
TRP HA   H  N N 414 
TRP HB2  H  N N 415 
TRP HB3  H  N N 416 
TRP HD1  H  N N 417 
TRP HE1  H  N N 418 
TRP HE3  H  N N 419 
TRP HZ2  H  N N 420 
TRP HZ3  H  N N 421 
TRP HH2  H  N N 422 
TRP HXT  H  N N 423 
TYR N    N  N N 424 
TYR CA   C  N S 425 
TYR C    C  N N 426 
TYR O    O  N N 427 
TYR CB   C  N N 428 
TYR CG   C  Y N 429 
TYR CD1  C  Y N 430 
TYR CD2  C  Y N 431 
TYR CE1  C  Y N 432 
TYR CE2  C  Y N 433 
TYR CZ   C  Y N 434 
TYR OH   O  N N 435 
TYR OXT  O  N N 436 
TYR H    H  N N 437 
TYR H2   H  N N 438 
TYR HA   H  N N 439 
TYR HB2  H  N N 440 
TYR HB3  H  N N 441 
TYR HD1  H  N N 442 
TYR HD2  H  N N 443 
TYR HE1  H  N N 444 
TYR HE2  H  N N 445 
TYR HH   H  N N 446 
TYR HXT  H  N N 447 
VAL N    N  N N 448 
VAL CA   C  N S 449 
VAL C    C  N N 450 
VAL O    O  N N 451 
VAL CB   C  N N 452 
VAL CG1  C  N N 453 
VAL CG2  C  N N 454 
VAL OXT  O  N N 455 
VAL H    H  N N 456 
VAL H2   H  N N 457 
VAL HA   H  N N 458 
VAL HB   H  N N 459 
VAL HG11 H  N N 460 
VAL HG12 H  N N 461 
VAL HG13 H  N N 462 
VAL HG21 H  N N 463 
VAL HG22 H  N N 464 
VAL HG23 H  N N 465 
VAL HXT  H  N N 466 
# 
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 
AKG C1  O1   doub N N 1   
AKG C1  O2   sing N N 2   
AKG C1  C2   sing N N 3   
AKG O2  HO2  sing N N 4   
AKG C2  O5   doub N N 5   
AKG C2  C3   sing N N 6   
AKG C3  C4   sing N N 7   
AKG C3  H31  sing N N 8   
AKG C3  H32  sing N N 9   
AKG C4  C5   sing N N 10  
AKG C4  H41  sing N N 11  
AKG C4  H42  sing N N 12  
AKG C5  O3   doub N N 13  
AKG C5  O4   sing N N 14  
AKG O4  HO4  sing N N 15  
ALA N   CA   sing N N 16  
ALA N   H    sing N N 17  
ALA N   H2   sing N N 18  
ALA CA  C    sing N N 19  
ALA CA  CB   sing N N 20  
ALA CA  HA   sing N N 21  
ALA C   O    doub N N 22  
ALA C   OXT  sing N N 23  
ALA CB  HB1  sing N N 24  
ALA CB  HB2  sing N N 25  
ALA CB  HB3  sing N N 26  
ALA OXT HXT  sing N N 27  
ARG N   CA   sing N N 28  
ARG N   H    sing N N 29  
ARG N   H2   sing N N 30  
ARG CA  C    sing N N 31  
ARG CA  CB   sing N N 32  
ARG CA  HA   sing N N 33  
ARG C   O    doub N N 34  
ARG C   OXT  sing N N 35  
ARG CB  CG   sing N N 36  
ARG CB  HB2  sing N N 37  
ARG CB  HB3  sing N N 38  
ARG CG  CD   sing N N 39  
ARG CG  HG2  sing N N 40  
ARG CG  HG3  sing N N 41  
ARG CD  NE   sing N N 42  
ARG CD  HD2  sing N N 43  
ARG CD  HD3  sing N N 44  
ARG NE  CZ   sing N N 45  
ARG NE  HE   sing N N 46  
ARG CZ  NH1  sing N N 47  
ARG CZ  NH2  doub N N 48  
ARG NH1 HH11 sing N N 49  
ARG NH1 HH12 sing N N 50  
ARG NH2 HH21 sing N N 51  
ARG NH2 HH22 sing N N 52  
ARG OXT HXT  sing N N 53  
ASN N   CA   sing N N 54  
ASN N   H    sing N N 55  
ASN N   H2   sing N N 56  
ASN CA  C    sing N N 57  
ASN CA  CB   sing N N 58  
ASN CA  HA   sing N N 59  
ASN C   O    doub N N 60  
ASN C   OXT  sing N N 61  
ASN CB  CG   sing N N 62  
ASN CB  HB2  sing N N 63  
ASN CB  HB3  sing N N 64  
ASN CG  OD1  doub N N 65  
ASN CG  ND2  sing N N 66  
ASN ND2 HD21 sing N N 67  
ASN ND2 HD22 sing N N 68  
ASN OXT HXT  sing N N 69  
ASP N   CA   sing N N 70  
ASP N   H    sing N N 71  
ASP N   H2   sing N N 72  
ASP CA  C    sing N N 73  
ASP CA  CB   sing N N 74  
ASP CA  HA   sing N N 75  
ASP C   O    doub N N 76  
ASP C   OXT  sing N N 77  
ASP CB  CG   sing N N 78  
ASP CB  HB2  sing N N 79  
ASP CB  HB3  sing N N 80  
ASP CG  OD1  doub N N 81  
ASP CG  OD2  sing N N 82  
ASP OD2 HD2  sing N N 83  
ASP OXT HXT  sing N N 84  
CYS N   CA   sing N N 85  
CYS N   H    sing N N 86  
CYS N   H2   sing N N 87  
CYS CA  C    sing N N 88  
CYS CA  CB   sing N N 89  
CYS CA  HA   sing N N 90  
CYS C   O    doub N N 91  
CYS C   OXT  sing N N 92  
CYS CB  SG   sing N N 93  
CYS CB  HB2  sing N N 94  
CYS CB  HB3  sing N N 95  
CYS SG  HG   sing N N 96  
CYS OXT HXT  sing N N 97  
GLN N   CA   sing N N 98  
GLN N   H    sing N N 99  
GLN N   H2   sing N N 100 
GLN CA  C    sing N N 101 
GLN CA  CB   sing N N 102 
GLN CA  HA   sing N N 103 
GLN C   O    doub N N 104 
GLN C   OXT  sing N N 105 
GLN CB  CG   sing N N 106 
GLN CB  HB2  sing N N 107 
GLN CB  HB3  sing N N 108 
GLN CG  CD   sing N N 109 
GLN CG  HG2  sing N N 110 
GLN CG  HG3  sing N N 111 
GLN CD  OE1  doub N N 112 
GLN CD  NE2  sing N N 113 
GLN NE2 HE21 sing N N 114 
GLN NE2 HE22 sing N N 115 
GLN OXT HXT  sing N N 116 
GLU N   CA   sing N N 117 
GLU N   H    sing N N 118 
GLU N   H2   sing N N 119 
GLU CA  C    sing N N 120 
GLU CA  CB   sing N N 121 
GLU CA  HA   sing N N 122 
GLU C   O    doub N N 123 
GLU C   OXT  sing N N 124 
GLU CB  CG   sing N N 125 
GLU CB  HB2  sing N N 126 
GLU CB  HB3  sing N N 127 
GLU CG  CD   sing N N 128 
GLU CG  HG2  sing N N 129 
GLU CG  HG3  sing N N 130 
GLU CD  OE1  doub N N 131 
GLU CD  OE2  sing N N 132 
GLU OE2 HE2  sing N N 133 
GLU OXT HXT  sing N N 134 
GLY N   CA   sing N N 135 
GLY N   H    sing N N 136 
GLY N   H2   sing N N 137 
GLY CA  C    sing N N 138 
GLY CA  HA2  sing N N 139 
GLY CA  HA3  sing N N 140 
GLY C   O    doub N N 141 
GLY C   OXT  sing N N 142 
GLY OXT HXT  sing N N 143 
HIS N   CA   sing N N 144 
HIS N   H    sing N N 145 
HIS N   H2   sing N N 146 
HIS CA  C    sing N N 147 
HIS CA  CB   sing N N 148 
HIS CA  HA   sing N N 149 
HIS C   O    doub N N 150 
HIS C   OXT  sing N N 151 
HIS CB  CG   sing N N 152 
HIS CB  HB2  sing N N 153 
HIS CB  HB3  sing N N 154 
HIS CG  ND1  sing Y N 155 
HIS CG  CD2  doub Y N 156 
HIS ND1 CE1  doub Y N 157 
HIS ND1 HD1  sing N N 158 
HIS CD2 NE2  sing Y N 159 
HIS CD2 HD2  sing N N 160 
HIS CE1 NE2  sing Y N 161 
HIS CE1 HE1  sing N N 162 
HIS NE2 HE2  sing N N 163 
HIS OXT HXT  sing N N 164 
HOH O   H1   sing N N 165 
HOH O   H2   sing N N 166 
ILE N   CA   sing N N 167 
ILE N   H    sing N N 168 
ILE N   H2   sing N N 169 
ILE CA  C    sing N N 170 
ILE CA  CB   sing N N 171 
ILE CA  HA   sing N N 172 
ILE C   O    doub N N 173 
ILE C   OXT  sing N N 174 
ILE CB  CG1  sing N N 175 
ILE CB  CG2  sing N N 176 
ILE CB  HB   sing N N 177 
ILE CG1 CD1  sing N N 178 
ILE CG1 HG12 sing N N 179 
ILE CG1 HG13 sing N N 180 
ILE CG2 HG21 sing N N 181 
ILE CG2 HG22 sing N N 182 
ILE CG2 HG23 sing N N 183 
ILE CD1 HD11 sing N N 184 
ILE CD1 HD12 sing N N 185 
ILE CD1 HD13 sing N N 186 
ILE OXT HXT  sing N N 187 
LEU N   CA   sing N N 188 
LEU N   H    sing N N 189 
LEU N   H2   sing N N 190 
LEU CA  C    sing N N 191 
LEU CA  CB   sing N N 192 
LEU CA  HA   sing N N 193 
LEU C   O    doub N N 194 
LEU C   OXT  sing N N 195 
LEU CB  CG   sing N N 196 
LEU CB  HB2  sing N N 197 
LEU CB  HB3  sing N N 198 
LEU CG  CD1  sing N N 199 
LEU CG  CD2  sing N N 200 
LEU CG  HG   sing N N 201 
LEU CD1 HD11 sing N N 202 
LEU CD1 HD12 sing N N 203 
LEU CD1 HD13 sing N N 204 
LEU CD2 HD21 sing N N 205 
LEU CD2 HD22 sing N N 206 
LEU CD2 HD23 sing N N 207 
LEU OXT HXT  sing N N 208 
LYS N   CA   sing N N 209 
LYS N   H    sing N N 210 
LYS N   H2   sing N N 211 
LYS CA  C    sing N N 212 
LYS CA  CB   sing N N 213 
LYS CA  HA   sing N N 214 
LYS C   O    doub N N 215 
LYS C   OXT  sing N N 216 
LYS CB  CG   sing N N 217 
LYS CB  HB2  sing N N 218 
LYS CB  HB3  sing N N 219 
LYS CG  CD   sing N N 220 
LYS CG  HG2  sing N N 221 
LYS CG  HG3  sing N N 222 
LYS CD  CE   sing N N 223 
LYS CD  HD2  sing N N 224 
LYS CD  HD3  sing N N 225 
LYS CE  NZ   sing N N 226 
LYS CE  HE2  sing N N 227 
LYS CE  HE3  sing N N 228 
LYS NZ  HZ1  sing N N 229 
LYS NZ  HZ2  sing N N 230 
LYS NZ  HZ3  sing N N 231 
LYS OXT HXT  sing N N 232 
MET N   CA   sing N N 233 
MET N   H    sing N N 234 
MET N   H2   sing N N 235 
MET CA  C    sing N N 236 
MET CA  CB   sing N N 237 
MET CA  HA   sing N N 238 
MET C   O    doub N N 239 
MET C   OXT  sing N N 240 
MET CB  CG   sing N N 241 
MET CB  HB2  sing N N 242 
MET CB  HB3  sing N N 243 
MET CG  SD   sing N N 244 
MET CG  HG2  sing N N 245 
MET CG  HG3  sing N N 246 
MET SD  CE   sing N N 247 
MET CE  HE1  sing N N 248 
MET CE  HE2  sing N N 249 
MET CE  HE3  sing N N 250 
MET OXT HXT  sing N N 251 
PE8 O1  C2   sing N N 252 
PE8 O1  HO1  sing N N 253 
PE8 C2  C3   sing N N 254 
PE8 C2  H21  sing N N 255 
PE8 C2  H22  sing N N 256 
PE8 C3  O4   sing N N 257 
PE8 C3  H31  sing N N 258 
PE8 C3  H32  sing N N 259 
PE8 O4  C5   sing N N 260 
PE8 C5  C6   sing N N 261 
PE8 C5  H51  sing N N 262 
PE8 C5  H52  sing N N 263 
PE8 C6  O7   sing N N 264 
PE8 C6  H61  sing N N 265 
PE8 C6  H62  sing N N 266 
PE8 O7  C8   sing N N 267 
PE8 C8  C9   sing N N 268 
PE8 C8  H81  sing N N 269 
PE8 C8  H82  sing N N 270 
PE8 C9  O10  sing N N 271 
PE8 C9  H91  sing N N 272 
PE8 C9  H92  sing N N 273 
PE8 O10 C11  sing N N 274 
PE8 C11 C12  sing N N 275 
PE8 C11 H111 sing N N 276 
PE8 C11 H112 sing N N 277 
PE8 C12 O13  sing N N 278 
PE8 C12 H121 sing N N 279 
PE8 C12 H122 sing N N 280 
PE8 O13 C14  sing N N 281 
PE8 C14 C15  sing N N 282 
PE8 C14 H141 sing N N 283 
PE8 C14 H142 sing N N 284 
PE8 C15 O16  sing N N 285 
PE8 C15 H151 sing N N 286 
PE8 C15 H152 sing N N 287 
PE8 O16 C17  sing N N 288 
PE8 C17 C18  sing N N 289 
PE8 C17 H171 sing N N 290 
PE8 C17 H172 sing N N 291 
PE8 C18 O19  sing N N 292 
PE8 C18 H181 sing N N 293 
PE8 C18 H182 sing N N 294 
PE8 O19 C20  sing N N 295 
PE8 C20 C21  sing N N 296 
PE8 C20 H201 sing N N 297 
PE8 C20 H202 sing N N 298 
PE8 C21 O22  sing N N 299 
PE8 C21 H211 sing N N 300 
PE8 C21 H212 sing N N 301 
PE8 O22 C23  sing N N 302 
PE8 C23 C24  sing N N 303 
PE8 C23 H231 sing N N 304 
PE8 C23 H232 sing N N 305 
PE8 C24 O25  sing N N 306 
PE8 C24 H241 sing N N 307 
PE8 C24 H242 sing N N 308 
PE8 O25 H25  sing N N 309 
PHE N   CA   sing N N 310 
PHE N   H    sing N N 311 
PHE N   H2   sing N N 312 
PHE CA  C    sing N N 313 
PHE CA  CB   sing N N 314 
PHE CA  HA   sing N N 315 
PHE C   O    doub N N 316 
PHE C   OXT  sing N N 317 
PHE CB  CG   sing N N 318 
PHE CB  HB2  sing N N 319 
PHE CB  HB3  sing N N 320 
PHE CG  CD1  doub Y N 321 
PHE CG  CD2  sing Y N 322 
PHE CD1 CE1  sing Y N 323 
PHE CD1 HD1  sing N N 324 
PHE CD2 CE2  doub Y N 325 
PHE CD2 HD2  sing N N 326 
PHE CE1 CZ   doub Y N 327 
PHE CE1 HE1  sing N N 328 
PHE CE2 CZ   sing Y N 329 
PHE CE2 HE2  sing N N 330 
PHE CZ  HZ   sing N N 331 
PHE OXT HXT  sing N N 332 
PRO N   CA   sing N N 333 
PRO N   CD   sing N N 334 
PRO N   H    sing N N 335 
PRO CA  C    sing N N 336 
PRO CA  CB   sing N N 337 
PRO CA  HA   sing N N 338 
PRO C   O    doub N N 339 
PRO C   OXT  sing N N 340 
PRO CB  CG   sing N N 341 
PRO CB  HB2  sing N N 342 
PRO CB  HB3  sing N N 343 
PRO CG  CD   sing N N 344 
PRO CG  HG2  sing N N 345 
PRO CG  HG3  sing N N 346 
PRO CD  HD2  sing N N 347 
PRO CD  HD3  sing N N 348 
PRO OXT HXT  sing N N 349 
SER N   CA   sing N N 350 
SER N   H    sing N N 351 
SER N   H2   sing N N 352 
SER CA  C    sing N N 353 
SER CA  CB   sing N N 354 
SER CA  HA   sing N N 355 
SER C   O    doub N N 356 
SER C   OXT  sing N N 357 
SER CB  OG   sing N N 358 
SER CB  HB2  sing N N 359 
SER CB  HB3  sing N N 360 
SER OG  HG   sing N N 361 
SER OXT HXT  sing N N 362 
THR N   CA   sing N N 363 
THR N   H    sing N N 364 
THR N   H2   sing N N 365 
THR CA  C    sing N N 366 
THR CA  CB   sing N N 367 
THR CA  HA   sing N N 368 
THR C   O    doub N N 369 
THR C   OXT  sing N N 370 
THR CB  OG1  sing N N 371 
THR CB  CG2  sing N N 372 
THR CB  HB   sing N N 373 
THR OG1 HG1  sing N N 374 
THR CG2 HG21 sing N N 375 
THR CG2 HG22 sing N N 376 
THR CG2 HG23 sing N N 377 
THR OXT HXT  sing N N 378 
TRP N   CA   sing N N 379 
TRP N   H    sing N N 380 
TRP N   H2   sing N N 381 
TRP CA  C    sing N N 382 
TRP CA  CB   sing N N 383 
TRP CA  HA   sing N N 384 
TRP C   O    doub N N 385 
TRP C   OXT  sing N N 386 
TRP CB  CG   sing N N 387 
TRP CB  HB2  sing N N 388 
TRP CB  HB3  sing N N 389 
TRP CG  CD1  doub Y N 390 
TRP CG  CD2  sing Y N 391 
TRP CD1 NE1  sing Y N 392 
TRP CD1 HD1  sing N N 393 
TRP CD2 CE2  doub Y N 394 
TRP CD2 CE3  sing Y N 395 
TRP NE1 CE2  sing Y N 396 
TRP NE1 HE1  sing N N 397 
TRP CE2 CZ2  sing Y N 398 
TRP CE3 CZ3  doub Y N 399 
TRP CE3 HE3  sing N N 400 
TRP CZ2 CH2  doub Y N 401 
TRP CZ2 HZ2  sing N N 402 
TRP CZ3 CH2  sing Y N 403 
TRP CZ3 HZ3  sing N N 404 
TRP CH2 HH2  sing N N 405 
TRP OXT HXT  sing N N 406 
TYR N   CA   sing N N 407 
TYR N   H    sing N N 408 
TYR N   H2   sing N N 409 
TYR CA  C    sing N N 410 
TYR CA  CB   sing N N 411 
TYR CA  HA   sing N N 412 
TYR C   O    doub N N 413 
TYR C   OXT  sing N N 414 
TYR CB  CG   sing N N 415 
TYR CB  HB2  sing N N 416 
TYR CB  HB3  sing N N 417 
TYR CG  CD1  doub Y N 418 
TYR CG  CD2  sing Y N 419 
TYR CD1 CE1  sing Y N 420 
TYR CD1 HD1  sing N N 421 
TYR CD2 CE2  doub Y N 422 
TYR CD2 HD2  sing N N 423 
TYR CE1 CZ   doub Y N 424 
TYR CE1 HE1  sing N N 425 
TYR CE2 CZ   sing Y N 426 
TYR CE2 HE2  sing N N 427 
TYR CZ  OH   sing N N 428 
TYR OH  HH   sing N N 429 
TYR OXT HXT  sing N N 430 
VAL N   CA   sing N N 431 
VAL N   H    sing N N 432 
VAL N   H2   sing N N 433 
VAL CA  C    sing N N 434 
VAL CA  CB   sing N N 435 
VAL CA  HA   sing N N 436 
VAL C   O    doub N N 437 
VAL C   OXT  sing N N 438 
VAL CB  CG1  sing N N 439 
VAL CB  CG2  sing N N 440 
VAL CB  HB   sing N N 441 
VAL CG1 HG11 sing N N 442 
VAL CG1 HG12 sing N N 443 
VAL CG1 HG13 sing N N 444 
VAL CG2 HG21 sing N N 445 
VAL CG2 HG22 sing N N 446 
VAL CG2 HG23 sing N N 447 
VAL OXT HXT  sing N N 448 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/V001892/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-Q6ES21-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8S7B 
_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]   0.014634 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000534 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014830 
_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]   0.012031 
_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.
;
? 
MN ? ? 20.23591 4.67902 ? ? 2.76514  44.01191 ? ? 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   . ALA A 1 7   ? 14.84518 10.37330  -8.60202 1.000 108.18108 ? 2   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 7   ? 15.60622 9.32824   -9.27525 1.000 106.27072 ? 2   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 7   ? 15.53287 8.02181   -8.49348 1.000 101.50618 ? 2   ALA A C   1 
ATOM   4    O  O   . ALA A 1 7   ? 14.74352 7.89808   -7.55501 1.000 101.52033 ? 2   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 7   ? 17.05437 9.75956   -9.45862 1.000 104.26609 ? 2   ALA A CB  1 
ATOM   6    N  N   . ASP A 1 8   ? 16.35377 7.04714   -8.89092 1.000 100.26051 ? 3   ASP A N   1 
ATOM   7    C  CA  . ASP A 1 8   ? 16.42893 5.77684   -8.17944 1.000 97.69051  ? 3   ASP A CA  1 
ATOM   8    C  C   . ASP A 1 8   ? 16.88648 6.02387   -6.74813 1.000 95.11125  ? 3   ASP A C   1 
ATOM   9    O  O   . ASP A 1 8   ? 18.02320 6.44856   -6.51492 1.000 97.35276  ? 3   ASP A O   1 
ATOM   10   C  CB  . ASP A 1 8   ? 17.37393 4.80620   -8.89479 1.000 97.71326  ? 3   ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 8   ? 17.21938 3.36869   -8.41333 1.000 97.60719  ? 3   ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 8   ? 17.02653 3.15255   -7.19827 1.000 102.20107 ? 3   ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 8   ? 17.28994 2.44938   -9.25634 1.000 104.55627 ? 3   ASP A OD2 1 
ATOM   14   N  N   . GLU A 1 9   ? 16.00623 5.75652   -5.78517 1.000 91.65497  ? 4   GLU A N   1 
ATOM   15   C  CA  . GLU A 1 9   ? 16.27075 6.06568   -4.38593 1.000 77.23619  ? 4   GLU A CA  1 
ATOM   16   C  C   . GLU A 1 9   ? 17.31293 5.13010   -3.78549 1.000 72.97924  ? 4   GLU A C   1 
ATOM   17   O  O   . GLU A 1 9   ? 17.06730 4.50947   -2.74579 1.000 66.71751  ? 4   GLU A O   1 
ATOM   18   C  CB  . GLU A 1 9   ? 14.97198 5.99217   -3.58302 1.000 80.00676  ? 4   GLU A CB  1 
ATOM   19   C  CG  . GLU A 1 9   ? 13.85990 6.87199   -4.12829 1.000 84.09423  ? 4   GLU A CG  1 
ATOM   20   C  CD  . GLU A 1 9   ? 12.52674 6.60080   -3.46118 1.000 94.82863  ? 4   GLU A CD  1 
ATOM   21   O  OE1 . GLU A 1 9   ? 12.27183 5.43456   -3.09148 1.000 95.62953  ? 4   GLU A OE1 1 
ATOM   22   O  OE2 . GLU A 1 9   ? 11.73574 7.55440   -3.30224 1.000 99.23832  ? 4   GLU A OE2 1 
ATOM   23   N  N   . SER A 1 10  ? 18.48228 5.02723   -4.42452 1.000 63.45055  ? 5   SER A N   1 
ATOM   24   C  CA  . SER A 1 10  ? 19.54491 4.18507   -3.88783 1.000 68.92747  ? 5   SER A CA  1 
ATOM   25   C  C   . SER A 1 10  ? 20.04895 4.69184   -2.54475 1.000 58.63921  ? 5   SER A C   1 
ATOM   26   O  O   . SER A 1 10  ? 20.63192 3.91485   -1.78025 1.000 58.23027  ? 5   SER A O   1 
ATOM   27   C  CB  . SER A 1 10  ? 20.70596 4.09389   -4.87995 1.000 64.12495  ? 5   SER A CB  1 
ATOM   28   O  OG  . SER A 1 10  ? 21.34813 5.34680   -5.03075 1.000 66.89582  ? 5   SER A OG  1 
ATOM   29   N  N   . TRP A 1 11  ? 19.83458 5.97442   -2.23835 1.000 57.11330  ? 6   TRP A N   1 
ATOM   30   C  CA  . TRP A 1 11  ? 20.20065 6.49435   -0.92659 1.000 61.83050  ? 6   TRP A CA  1 
ATOM   31   C  C   . TRP A 1 11  ? 19.37139 5.87437   0.18992  1.000 54.02264  ? 6   TRP A C   1 
ATOM   32   O  O   . TRP A 1 11  ? 19.76389 5.96360   1.35797  1.000 46.67745  ? 6   TRP A O   1 
ATOM   33   C  CB  . TRP A 1 11  ? 20.05945 8.01985   -0.89837 1.000 54.37532  ? 6   TRP A CB  1 
ATOM   34   C  CG  . TRP A 1 11  ? 18.71333 8.52891   -1.33458 1.000 56.70225  ? 6   TRP A CG  1 
ATOM   35   C  CD1 . TRP A 1 11  ? 18.35417 8.92009   -2.59269 1.000 63.66341  ? 6   TRP A CD1 1 
ATOM   36   C  CD2 . TRP A 1 11  ? 17.55317 8.71398   -0.51186 1.000 50.38787  ? 6   TRP A CD2 1 
ATOM   37   N  NE1 . TRP A 1 11  ? 17.04313 9.33242   -2.60474 1.000 65.89781  ? 6   TRP A NE1 1 
ATOM   38   C  CE2 . TRP A 1 11  ? 16.52854 9.21547   -1.34065 1.000 57.94539  ? 6   TRP A CE2 1 
ATOM   39   C  CE3 . TRP A 1 11  ? 17.28077 8.50178   0.84292  1.000 53.78408  ? 6   TRP A CE3 1 
ATOM   40   C  CZ2 . TRP A 1 11  ? 15.25360 9.50781   -0.85966 1.000 56.43907  ? 6   TRP A CZ2 1 
ATOM   41   C  CZ3 . TRP A 1 11  ? 16.01241 8.79393   1.31966  1.000 54.38752  ? 6   TRP A CZ3 1 
ATOM   42   C  CH2 . TRP A 1 11  ? 15.01565 9.28967   0.46988  1.000 55.29503  ? 6   TRP A CH2 1 
ATOM   43   N  N   . ARG A 1 12  ? 18.23608 5.25438   -0.13814 1.000 49.80901  ? 7   ARG A N   1 
ATOM   44   C  CA  . ARG A 1 12  ? 17.43027 4.56511   0.86180  1.000 55.70297  ? 7   ARG A CA  1 
ATOM   45   C  C   . ARG A 1 12  ? 18.02759 3.23149   1.28467  1.000 50.72597  ? 7   ARG A C   1 
ATOM   46   O  O   . ARG A 1 12  ? 17.60035 2.67736   2.30318  1.000 55.36167  ? 7   ARG A O   1 
ATOM   47   C  CB  . ARG A 1 12  ? 16.00629 4.34573   0.34058  1.000 51.69904  ? 7   ARG A CB  1 
ATOM   48   C  CG  . ARG A 1 12  ? 15.26339 5.63629   0.04918  1.000 64.89083  ? 7   ARG A CG  1 
ATOM   49   C  CD  . ARG A 1 12  ? 13.76949 5.41930   -0.11247 1.000 70.92521  ? 7   ARG A CD  1 
ATOM   50   N  NE  . ARG A 1 12  ? 13.04041 6.67715   0.00200  1.000 79.98337  ? 7   ARG A NE  1 
ATOM   51   C  CZ  . ARG A 1 12  ? 11.71899 6.78219   0.00878  1.000 85.95563  ? 7   ARG A CZ  1 
ATOM   52   N  NH1 . ARG A 1 12  ? 10.94057 5.71836   -0.10204 1.000 99.65327  ? 7   ARG A NH1 1 
ATOM   53   N  NH2 . ARG A 1 12  ? 11.16455 7.98481   0.13229  1.000 79.43357  ? 7   ARG A NH2 1 
ATOM   54   N  N   . ALA A 1 13  ? 18.99875 2.70706   0.53428  1.000 46.56913  ? 8   ALA A N   1 
ATOM   55   C  CA  . ALA A 1 13  ? 19.67810 1.45258   0.85016  1.000 45.98396  ? 8   ALA A CA  1 
ATOM   56   C  C   . ALA A 1 13  ? 21.15279 1.76136   1.08584  1.000 50.43257  ? 8   ALA A C   1 
ATOM   57   O  O   . ALA A 1 13  ? 21.98308 1.62345   0.17399  1.000 45.38476  ? 8   ALA A O   1 
ATOM   58   C  CB  . ALA A 1 13  ? 19.49489 0.42332   -0.26376 1.000 45.72188  ? 8   ALA A CB  1 
ATOM   59   N  N   . PRO A 1 14  ? 21.51471 2.18319   2.29388  1.000 43.79471  ? 9   PRO A N   1 
ATOM   60   C  CA  . PRO A 1 14  ? 22.90639 2.56001   2.55731  1.000 44.09835  ? 9   PRO A CA  1 
ATOM   61   C  C   . PRO A 1 14  ? 23.81446 1.34236   2.62854  1.000 45.47379  ? 9   PRO A C   1 
ATOM   62   O  O   . PRO A 1 14  ? 23.36921 0.20039   2.75922  1.000 41.65164  ? 9   PRO A O   1 
ATOM   63   C  CB  . PRO A 1 14  ? 22.83024 3.27563   3.90866  1.000 43.10702  ? 9   PRO A CB  1 
ATOM   64   C  CG  . PRO A 1 14  ? 21.64289 2.66990   4.57274  1.000 45.99107  ? 9   PRO A CG  1 
ATOM   65   C  CD  . PRO A 1 14  ? 20.65821 2.34925   3.47917  1.000 40.29203  ? 9   PRO A CD  1 
ATOM   66   N  N   . ALA A 1 15  ? 25.11478 1.61198   2.54783  1.000 43.33114  ? 10  ALA A N   1 
ATOM   67   C  CA  . ALA A 1 15  ? 26.11244 0.55475   2.52384  1.000 34.92579  ? 10  ALA A CA  1 
ATOM   68   C  C   . ALA A 1 15  ? 26.24625 -0.11819  3.88612  1.000 36.36173  ? 10  ALA A C   1 
ATOM   69   O  O   . ALA A 1 15  ? 25.90419 0.44450   4.93365  1.000 36.79488  ? 10  ALA A O   1 
ATOM   70   C  CB  . ALA A 1 15  ? 27.47357 1.10948   2.10614  1.000 45.93588  ? 10  ALA A CB  1 
ATOM   71   N  N   . ILE A 1 16  ? 26.76376 -1.34276  3.85704  1.000 34.50255  ? 11  ILE A N   1 
ATOM   72   C  CA  . ILE A 1 16  ? 27.23213 -2.00526  5.06811  1.000 36.06255  ? 11  ILE A CA  1 
ATOM   73   C  C   . ILE A 1 16  ? 28.58309 -1.40117  5.42632  1.000 31.34475  ? 11  ILE A C   1 
ATOM   74   O  O   . ILE A 1 16  ? 29.54667 -1.51943  4.66049  1.000 34.33109  ? 11  ILE A O   1 
ATOM   75   C  CB  . ILE A 1 16  ? 27.33217 -3.52403  4.86572  1.000 37.45008  ? 11  ILE A CB  1 
ATOM   76   C  CG1 . ILE A 1 16  ? 25.94010 -4.13225  4.68120  1.000 35.38643  ? 11  ILE A CG1 1 
ATOM   77   C  CG2 . ILE A 1 16  ? 28.05284 -4.17495  6.03628  1.000 34.85320  ? 11  ILE A CG2 1 
ATOM   78   C  CD1 . ILE A 1 16  ? 25.03508 -3.96406  5.89795  1.000 35.52729  ? 11  ILE A CD1 1 
ATOM   79   N  N   . VAL A 1 17  ? 28.64872 -0.72919  6.57929  1.000 35.36891  ? 12  VAL A N   1 
ATOM   80   C  CA  . VAL A 1 17  ? 29.85291 0.02724   6.90755  1.000 38.54950  ? 12  VAL A CA  1 
ATOM   81   C  C   . VAL A 1 17  ? 31.04687 -0.89832  7.09981  1.000 35.29314  ? 12  VAL A C   1 
ATOM   82   O  O   . VAL A 1 17  ? 32.17912 -0.53614  6.75642  1.000 33.51967  ? 12  VAL A O   1 
ATOM   83   C  CB  . VAL A 1 17  ? 29.61485 0.90602   8.14762  1.000 36.91400  ? 12  VAL A CB  1 
ATOM   84   C  CG1 . VAL A 1 17  ? 30.83991 1.76198   8.43056  1.000 33.72695  ? 12  VAL A CG1 1 
ATOM   85   C  CG2 . VAL A 1 17  ? 28.37756 1.77312   7.95369  1.000 32.34094  ? 12  VAL A CG2 1 
ATOM   86   N  N   . GLN A 1 18  ? 30.82835 -2.09937  7.64448  1.000 32.01114  ? 13  GLN A N   1 
ATOM   87   C  CA  . GLN A 1 18  ? 31.92829 -3.05387  7.75707  1.000 35.82962  ? 13  GLN A CA  1 
ATOM   88   C  C   . GLN A 1 18  ? 32.54761 -3.34959  6.39883  1.000 35.72311  ? 13  GLN A C   1 
ATOM   89   O  O   . GLN A 1 18  ? 33.76073 -3.57659  6.30363  1.000 37.19913  ? 13  GLN A O   1 
ATOM   90   C  CB  . GLN A 1 18  ? 31.44496 -4.34673  8.42436  1.000 32.87126  ? 13  GLN A CB  1 
ATOM   91   C  CG  . GLN A 1 18  ? 32.54709 -5.38165  8.63438  1.000 35.91722  ? 13  GLN A CG  1 
ATOM   92   C  CD  . GLN A 1 18  ? 32.05942 -6.63022  9.35263  1.000 35.43963  ? 13  GLN A CD  1 
ATOM   93   O  OE1 . GLN A 1 18  ? 30.90205 -6.71582  9.74662  1.000 32.62055  ? 13  GLN A OE1 1 
ATOM   94   N  NE2 . GLN A 1 18  ? 32.94318 -7.60977  9.51080  1.000 35.79330  ? 13  GLN A NE2 1 
ATOM   95   N  N   . GLU A 1 19  ? 31.74215 -3.32300  5.33409  1.000 34.52181  ? 14  GLU A N   1 
ATOM   96   C  CA  . GLU A 1 19  ? 32.26501 -3.57868  3.99570  1.000 38.90155  ? 14  GLU A CA  1 
ATOM   97   C  C   . GLU A 1 19  ? 33.03443 -2.38118  3.44960  1.000 33.43699  ? 14  GLU A C   1 
ATOM   98   O  O   . GLU A 1 19  ? 34.03718 -2.55563  2.74893  1.000 37.71363  ? 14  GLU A O   1 
ATOM   99   C  CB  . GLU A 1 19  ? 31.12333 -3.95597  3.05497  1.000 43.42173  ? 14  GLU A CB  1 
ATOM   100  C  CG  . GLU A 1 19  ? 30.53307 -5.31254  3.36237  1.000 38.28955  ? 14  GLU A CG  1 
ATOM   101  C  CD  . GLU A 1 19  ? 31.50973 -6.42921  3.06988  1.000 36.73463  ? 14  GLU A CD  1 
ATOM   102  O  OE1 . GLU A 1 19  ? 31.91328 -6.57596  1.89547  1.000 44.24850  ? 14  GLU A OE1 1 
ATOM   103  O  OE2 . GLU A 1 19  ? 31.88525 -7.15188  4.01322  1.000 44.11534  ? 14  GLU A OE2 1 
ATOM   104  N  N   . LEU A 1 20  ? 32.57825 -1.16208  3.74925  1.000 38.03360  ? 15  LEU A N   1 
ATOM   105  C  CA  . LEU A 1 20  ? 33.32994 0.02872   3.35491  1.000 45.09074  ? 15  LEU A CA  1 
ATOM   106  C  C   . LEU A 1 20  ? 34.73146 0.00323   3.94893  1.000 42.46106  ? 15  LEU A C   1 
ATOM   107  O  O   . LEU A 1 20  ? 35.71915 0.25299   3.25356  1.000 37.12171  ? 15  LEU A O   1 
ATOM   108  C  CB  . LEU A 1 20  ? 32.59177 1.29517   3.80173  1.000 38.68357  ? 15  LEU A CB  1 
ATOM   109  C  CG  . LEU A 1 20  ? 31.24937 1.61676   3.14954  1.000 39.04004  ? 15  LEU A CG  1 
ATOM   110  C  CD1 . LEU A 1 20  ? 30.63559 2.86141   3.78913  1.000 46.25621  ? 15  LEU A CD1 1 
ATOM   111  C  CD2 . LEU A 1 20  ? 31.43120 1.79670   1.64664  1.000 37.13766  ? 15  LEU A CD2 1 
ATOM   112  N  N   . ALA A 1 21  ? 34.83072 -0.29814  5.24424  1.000 37.87161  ? 16  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 21  ? 36.12770 -0.35128  5.91098  1.000 39.80620  ? 16  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 21  ? 36.99847 -1.46410  5.34401  1.000 42.98364  ? 16  ALA A C   1 
ATOM   115  O  O   . ALA A 1 21  ? 38.20452 -1.27736  5.14968  1.000 45.15790  ? 16  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 21  ? 35.92736 -0.53604  7.41777  1.000 37.83101  ? 16  ALA A CB  1 
ATOM   117  N  N   . ALA A 1 22  ? 36.40501 -2.62940  5.06828  1.000 36.78277  ? 17  ALA A N   1 
ATOM   118  C  CA  . ALA A 1 22  ? 37.16701 -3.73424  4.49433  1.000 37.98132  ? 17  ALA A CA  1 
ATOM   119  C  C   . ALA A 1 22  ? 37.63864 -3.42368  3.07805  1.000 38.89197  ? 17  ALA A C   1 
ATOM   120  O  O   . ALA A 1 22  ? 38.72461 -3.86065  2.67686  1.000 42.91745  ? 17  ALA A O   1 
ATOM   121  C  CB  . ALA A 1 22  ? 36.32689 -5.01101  4.50417  1.000 41.16971  ? 17  ALA A CB  1 
ATOM   122  N  N   . ALA A 1 23  ? 36.83981 -2.68440  2.30354  1.000 39.42957  ? 18  ALA A N   1 
ATOM   123  C  CA  . ALA A 1 23  ? 37.26762 -2.28347  0.96719  1.000 40.06336  ? 18  ALA A CA  1 
ATOM   124  C  C   . ALA A 1 23  ? 38.41287 -1.28246  1.00838  1.000 44.34547  ? 18  ALA A C   1 
ATOM   125  O  O   . ALA A 1 23  ? 39.12972 -1.13752  0.01408  1.000 48.74972  ? 18  ALA A O   1 
ATOM   126  C  CB  . ALA A 1 23  ? 36.08948 -1.69909  0.18935  1.000 43.57449  ? 18  ALA A CB  1 
ATOM   127  N  N   . GLY A 1 24  ? 38.59797 -0.58781  2.12695  1.000 44.57399  ? 19  GLY A N   1 
ATOM   128  C  CA  . GLY A 1 24  ? 39.73730 0.29219   2.27775  1.000 50.16550  ? 19  GLY A CA  1 
ATOM   129  C  C   . GLY A 1 24  ? 39.48322 1.74248   1.92053  1.000 47.52938  ? 19  GLY A C   1 
ATOM   130  O  O   . GLY A 1 24  ? 40.36697 2.40178   1.36896  1.000 47.34179  ? 19  GLY A O   1 
ATOM   131  N  N   . VAL A 1 25  ? 38.29365 2.26539   2.22875  1.000 41.99208  ? 20  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 25  ? 38.05852 3.68999   2.02043  1.000 58.77663  ? 20  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 25  ? 39.04550 4.48682   2.86197  1.000 45.69393  ? 20  VAL A C   1 
ATOM   134  O  O   . VAL A 1 25  ? 39.26623 4.19156   4.04296  1.000 49.89816  ? 20  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 25  ? 36.60390 4.05958   2.34683  1.000 56.48995  ? 20  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 25  ? 35.66239 3.42640   1.34272  1.000 52.71675  ? 20  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 25  ? 36.24161 3.63957   3.76567  1.000 49.70503  ? 20  VAL A CG2 1 
ATOM   138  N  N   . GLU A 1 26  ? 39.67623 5.48441   2.23970  1.000 57.10965  ? 21  GLU A N   1 
ATOM   139  C  CA  . GLU A 1 26  ? 40.68532 6.28105   2.92484  1.000 51.55321  ? 21  GLU A CA  1 
ATOM   140  C  C   . GLU A 1 26  ? 40.08161 7.38673   3.77847  1.000 51.34608  ? 21  GLU A C   1 
ATOM   141  O  O   . GLU A 1 26  ? 40.77996 7.93983   4.63391  1.000 48.85529  ? 21  GLU A O   1 
ATOM   142  C  CB  . GLU A 1 26  ? 41.64975 6.88270   1.90149  1.000 53.64181  ? 21  GLU A CB  1 
ATOM   143  C  CG  . GLU A 1 26  ? 42.37037 5.84292   1.06087  1.000 66.44720  ? 21  GLU A CG  1 
ATOM   144  C  CD  . GLU A 1 26  ? 42.65425 6.32943   -0.34239 1.000 68.30007  ? 21  GLU A CD  1 
ATOM   145  O  OE1 . GLU A 1 26  ? 41.91996 7.22063   -0.81947 1.000 82.02307  ? 21  GLU A OE1 1 
ATOM   146  O  OE2 . GLU A 1 26  ? 43.60502 5.82041   -0.97428 1.000 70.61758  ? 21  GLU A OE2 1 
ATOM   147  N  N   . GLU A 1 27  ? 38.81347 7.71823   3.55775  1.000 50.27084  ? 22  GLU A N   1 
ATOM   148  C  CA  . GLU A 1 27  ? 38.09083 8.74996   4.28552  1.000 45.62582  ? 22  GLU A CA  1 
ATOM   149  C  C   . GLU A 1 27  ? 36.63271 8.32826   4.35666  1.000 41.15590  ? 22  GLU A C   1 
ATOM   150  O  O   . GLU A 1 27  ? 36.17684 7.52696   3.53285  1.000 43.32826  ? 22  GLU A O   1 
ATOM   151  C  CB  . GLU A 1 27  ? 38.21409 10.11889  3.59701  1.000 44.57890  ? 22  GLU A CB  1 
ATOM   152  C  CG  . GLU A 1 27  ? 39.62927 10.65784  3.48694  1.000 75.51039  ? 22  GLU A CG  1 
ATOM   153  C  CD  . GLU A 1 27  ? 39.75349 11.74202  2.43522  1.000 81.74071  ? 22  GLU A CD  1 
ATOM   154  O  OE1 . GLU A 1 27  ? 38.70717 12.26996  2.00220  1.000 88.47095  ? 22  GLU A OE1 1 
ATOM   155  O  OE2 . GLU A 1 27  ? 40.89416 12.05990  2.03590  1.000 82.95328  ? 22  GLU A OE2 1 
ATOM   156  N  N   . PRO A 1 28  ? 35.87480 8.84056   5.32049  1.000 40.40059  ? 23  PRO A N   1 
ATOM   157  C  CA  . PRO A 1 28  ? 34.44304 8.52753   5.37159  1.000 39.05848  ? 23  PRO A CA  1 
ATOM   158  C  C   . PRO A 1 28  ? 33.71773 9.17231   4.20456  1.000 44.68732  ? 23  PRO A C   1 
ATOM   159  O  O   . PRO A 1 28  ? 33.93451 10.35878  3.91792  1.000 39.55582  ? 23  PRO A O   1 
ATOM   160  C  CB  . PRO A 1 28  ? 33.98908 9.13535   6.70839  1.000 39.28167  ? 23  PRO A CB  1 
ATOM   161  C  CG  . PRO A 1 28  ? 35.24627 9.38994   7.47836  1.000 43.86157  ? 23  PRO A CG  1 
ATOM   162  C  CD  . PRO A 1 28  ? 36.28310 9.69869   6.44349  1.000 45.18108  ? 23  PRO A CD  1 
ATOM   163  N  N   . PRO A 1 29  ? 32.86836 8.42504   3.49658  1.000 46.49263  ? 24  PRO A N   1 
ATOM   164  C  CA  . PRO A 1 29  ? 32.06274 9.03702   2.43209  1.000 51.88058  ? 24  PRO A CA  1 
ATOM   165  C  C   . PRO A 1 29  ? 31.19966 10.16596  2.97967  1.000 47.45026  ? 24  PRO A C   1 
ATOM   166  O  O   . PRO A 1 29  ? 30.94021 10.25701  4.18134  1.000 42.76705  ? 24  PRO A O   1 
ATOM   167  C  CB  . PRO A 1 29  ? 31.21259 7.87154   1.91434  1.000 39.80431  ? 24  PRO A CB  1 
ATOM   168  C  CG  . PRO A 1 29  ? 32.04423 6.65294   2.21737  1.000 43.26134  ? 24  PRO A CG  1 
ATOM   169  C  CD  . PRO A 1 29  ? 32.71789 6.95875   3.53377  1.000 44.67292  ? 24  PRO A CD  1 
ATOM   170  N  N   . SER A 1 30  ? 30.74407 11.03485  2.06924  1.000 42.89228  ? 25  SER A N   1 
ATOM   171  C  CA  . SER A 1 30  ? 30.21776 12.33138  2.49315  1.000 45.77350  ? 25  SER A CA  1 
ATOM   172  C  C   . SER A 1 30  ? 28.97959 12.20509  3.37848  1.000 46.07680  ? 25  SER A C   1 
ATOM   173  O  O   . SER A 1 30  ? 28.75723 13.05727  4.24465  1.000 40.30060  ? 25  SER A O   1 
ATOM   174  C  CB  . SER A 1 30  ? 29.91558 13.20635  1.27442  1.000 53.91994  ? 25  SER A CB  1 
ATOM   175  O  OG  . SER A 1 30  ? 28.79093 12.73164  0.55964  1.000 64.18728  ? 25  SER A OG  1 
ATOM   176  N  N   . ARG A 1 31  ? 28.17107 11.15812  3.19831  1.000 42.79046  ? 26  ARG A N   1 
ATOM   177  C  CA  . ARG A 1 31  ? 26.95173 11.03892  3.99748  1.000 39.46846  ? 26  ARG A CA  1 
ATOM   178  C  C   . ARG A 1 31  ? 27.21486 10.66437  5.45212  1.000 41.36172  ? 26  ARG A C   1 
ATOM   179  O  O   . ARG A 1 31  ? 26.27781 10.69446  6.25876  1.000 45.49059  ? 26  ARG A O   1 
ATOM   180  C  CB  . ARG A 1 31  ? 26.00159 10.01867  3.36961  1.000 47.32287  ? 26  ARG A CB  1 
ATOM   181  C  CG  . ARG A 1 31  ? 25.28855 10.53535  2.12730  1.000 61.32186  ? 26  ARG A CG  1 
ATOM   182  C  CD  . ARG A 1 31  ? 24.41589 9.45986   1.50566  1.000 71.78640  ? 26  ARG A CD  1 
ATOM   183  N  NE  . ARG A 1 31  ? 23.19581 9.24098   2.26956  1.000 62.24577  ? 26  ARG A NE  1 
ATOM   184  C  CZ  . ARG A 1 31  ? 22.50557 8.10900   2.28214  1.000 58.77624  ? 26  ARG A CZ  1 
ATOM   185  N  NH1 . ARG A 1 31  ? 22.91154 7.03925   1.61887  1.000 50.14989  ? 26  ARG A NH1 1 
ATOM   186  N  NH2 . ARG A 1 31  ? 21.38574 8.04496   2.99089  1.000 72.62947  ? 26  ARG A NH2 1 
ATOM   187  N  N   . TYR A 1 32  ? 28.44957 10.31387  5.81007  1.000 43.18747  ? 27  TYR A N   1 
ATOM   188  C  CA  . TYR A 1 32  ? 28.80054 10.03474  7.19465  1.000 36.96626  ? 27  TYR A CA  1 
ATOM   189  C  C   . TYR A 1 32  ? 29.43755 11.22775  7.89416  1.000 36.53574  ? 27  TYR A C   1 
ATOM   190  O  O   . TYR A 1 32  ? 29.61938 11.18370  9.11396  1.000 38.71078  ? 27  TYR A O   1 
ATOM   191  C  CB  . TYR A 1 32  ? 29.75352 8.83583   7.26875  1.000 36.91411  ? 27  TYR A CB  1 
ATOM   192  C  CG  . TYR A 1 32  ? 29.19714 7.58099   6.63564  1.000 38.33242  ? 27  TYR A CG  1 
ATOM   193  C  CD1 . TYR A 1 32  ? 29.35338 7.33539   5.27458  1.000 36.70092  ? 27  TYR A CD1 1 
ATOM   194  C  CD2 . TYR A 1 32  ? 28.52156 6.63566   7.40083  1.000 38.28166  ? 27  TYR A CD2 1 
ATOM   195  C  CE1 . TYR A 1 32  ? 28.84364 6.18678   4.69062  1.000 39.37285  ? 27  TYR A CE1 1 
ATOM   196  C  CE2 . TYR A 1 32  ? 28.00797 5.48374   6.82704  1.000 30.22460  ? 27  TYR A CE2 1 
ATOM   197  C  CZ  . TYR A 1 32  ? 28.17082 5.26474   5.47289  1.000 35.74077  ? 27  TYR A CZ  1 
ATOM   198  O  OH  . TYR A 1 32  ? 27.65761 4.12331   4.90087  1.000 39.45444  ? 27  TYR A OH  1 
ATOM   199  N  N   . LEU A 1 33  ? 29.77528 12.28610  7.15762  1.000 37.44403  ? 28  LEU A N   1 
ATOM   200  C  CA  . LEU A 1 33  ? 30.46887 13.41780  7.75585  1.000 39.06123  ? 28  LEU A CA  1 
ATOM   201  C  C   . LEU A 1 33  ? 29.51800 14.24376  8.61530  1.000 47.20791  ? 28  LEU A C   1 
ATOM   202  O  O   . LEU A 1 33  ? 28.42569 14.61645  8.17507  1.000 48.91136  ? 28  LEU A O   1 
ATOM   203  C  CB  . LEU A 1 33  ? 31.08758 14.29572  6.67034  1.000 33.94384  ? 28  LEU A CB  1 
ATOM   204  C  CG  . LEU A 1 33  ? 32.08645 13.61333  5.72913  1.000 39.63110  ? 28  LEU A CG  1 
ATOM   205  C  CD1 . LEU A 1 33  ? 32.73176 14.62748  4.79658  1.000 47.17375  ? 28  LEU A CD1 1 
ATOM   206  C  CD2 . LEU A 1 33  ? 33.14727 12.85805  6.51425  1.000 44.08778  ? 28  LEU A CD2 1 
ATOM   207  N  N   . LEU A 1 34  ? 29.94260 14.53647  9.84066  1.000 41.68005  ? 29  LEU A N   1 
ATOM   208  C  CA  . LEU A 1 34  ? 29.19730 15.43336  10.70790 1.000 46.69370  ? 29  LEU A CA  1 
ATOM   209  C  C   . LEU A 1 34  ? 29.21336 16.85800  10.15665 1.000 46.37526  ? 29  LEU A C   1 
ATOM   210  O  O   . LEU A 1 34  ? 30.03250 17.21967  9.30763  1.000 51.79899  ? 29  LEU A O   1 
ATOM   211  C  CB  . LEU A 1 34  ? 29.78344 15.41514  12.11564 1.000 47.41283  ? 29  LEU A CB  1 
ATOM   212  C  CG  . LEU A 1 34  ? 29.91463 14.01490  12.70796 1.000 37.03056  ? 29  LEU A CG  1 
ATOM   213  C  CD1 . LEU A 1 34  ? 30.69659 14.06967  14.00263 1.000 43.51053  ? 29  LEU A CD1 1 
ATOM   214  C  CD2 . LEU A 1 34  ? 28.54091 13.41250  12.92731 1.000 44.05507  ? 29  LEU A CD2 1 
ATOM   215  N  N   . ARG A 1 35  ? 28.30412 17.67750  10.67492 1.000 77.66603  ? 30  ARG A N   1 
ATOM   216  C  CA  . ARG A 1 35  ? 28.07220 19.03360  10.18086 1.000 84.98948  ? 30  ARG A CA  1 
ATOM   217  C  C   . ARG A 1 35  ? 28.47523 20.04227  11.25711 1.000 89.34824  ? 30  ARG A C   1 
ATOM   218  O  O   . ARG A 1 35  ? 27.65537 20.45190  12.08085 1.000 98.74821  ? 30  ARG A O   1 
ATOM   219  C  CB  . ARG A 1 35  ? 26.61017 19.19891  9.77307  1.000 85.07447  ? 30  ARG A CB  1 
ATOM   220  C  CG  . ARG A 1 35  ? 25.65045 18.44477  10.67865 1.000 82.09569  ? 30  ARG A CG  1 
ATOM   221  C  CD  . ARG A 1 35  ? 24.25422 18.35785  10.09099 1.000 86.96709  ? 30  ARG A CD  1 
ATOM   222  N  NE  . ARG A 1 35  ? 23.49731 17.26526  10.69115 1.000 86.00050  ? 30  ARG A NE  1 
ATOM   223  C  CZ  . ARG A 1 35  ? 22.80618 17.36089  11.81880 1.000 90.00363  ? 30  ARG A CZ  1 
ATOM   224  N  NH1 . ARG A 1 35  ? 22.73543 18.49769  12.49164 1.000 89.03886  ? 30  ARG A NH1 1 
ATOM   225  N  NH2 . ARG A 1 35  ? 22.17224 16.28788  12.28467 1.000 70.18488  ? 30  ARG A NH2 1 
ATOM   226  N  N   . GLU A 1 36  ? 29.75257 20.43716  11.23783 1.000 92.59291  ? 31  GLU A N   1 
ATOM   227  C  CA  . GLU A 1 36  ? 30.29020 21.53523  12.04236 1.000 90.73425  ? 31  GLU A CA  1 
ATOM   228  C  C   . GLU A 1 36  ? 29.88274 21.48846  13.51236 1.000 84.44229  ? 31  GLU A C   1 
ATOM   229  O  O   . GLU A 1 36  ? 30.73752 21.31857  14.38813 1.000 82.31905  ? 31  GLU A O   1 
ATOM   230  C  CB  . GLU A 1 36  ? 29.87436 22.88170  11.44326 1.000 85.69913  ? 31  GLU A CB  1 
ATOM   231  C  CG  . GLU A 1 36  ? 30.67107 23.29475  10.21177 1.000 94.56268  ? 31  GLU A CG  1 
ATOM   232  C  CD  . GLU A 1 36  ? 30.28625 22.51640  8.96747  1.000 100.05236 ? 31  GLU A CD  1 
ATOM   233  O  OE1 . GLU A 1 36  ? 29.20580 21.88975  8.96265  1.000 99.60280  ? 31  GLU A OE1 1 
ATOM   234  O  OE2 . GLU A 1 36  ? 31.06529 22.53304  7.99147  1.000 101.96611 ? 31  GLU A OE2 1 
ATOM   235  N  N   . LYS A 1 37  ? 28.58585 21.67025  13.78720 1.000 82.25803  ? 32  LYS A N   1 
ATOM   236  C  CA  . LYS A 1 37  ? 28.09035 21.67706  15.16225 1.000 82.15961  ? 32  LYS A CA  1 
ATOM   237  C  C   . LYS A 1 37  ? 28.54550 20.43904  15.92385 1.000 82.50071  ? 32  LYS A C   1 
ATOM   238  O  O   . LYS A 1 37  ? 28.98904 20.52940  17.07454 1.000 80.67863  ? 32  LYS A O   1 
ATOM   239  C  CB  . LYS A 1 37  ? 26.56407 21.77467  15.16558 1.000 77.02116  ? 32  LYS A CB  1 
ATOM   240  C  CG  . LYS A 1 37  ? 26.02173 23.06088  14.56175 1.000 99.51968  ? 32  LYS A CG  1 
ATOM   241  C  CD  . LYS A 1 37  ? 24.51747 22.98629  14.32330 1.000 93.83895  ? 32  LYS A CD  1 
ATOM   242  C  CE  . LYS A 1 37  ? 24.18864 22.41128  12.94947 1.000 84.14720  ? 32  LYS A CE  1 
ATOM   243  N  NZ  . LYS A 1 37  ? 24.52844 20.96760  12.82208 1.000 89.66676  ? 32  LYS A NZ  1 
ATOM   244  N  N   . ASP A 1 38  ? 28.44406 19.26834  15.29178 1.000 81.21525  ? 33  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 38  ? 28.93094 18.04343  15.91076 1.000 75.50388  ? 33  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 38  ? 30.43341 17.85656  15.74032 1.000 73.97878  ? 33  ASP A C   1 
ATOM   247  O  O   . ASP A 1 38  ? 31.04886 17.16342  16.55665 1.000 70.22358  ? 33  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 38  ? 28.18914 16.82782  15.34458 1.000 71.10389  ? 33  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 38  ? 26.91808 16.50500  16.11633 1.000 77.89754  ? 33  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 38  ? 26.89576 16.72328  17.34865 1.000 60.03286  ? 33  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 38  ? 25.94350 16.02790  15.49369 1.000 75.19067  ? 33  ASP A OD2 1 
ATOM   252  N  N   . ARG A 1 39  ? 31.03865 18.46339  14.71378 1.000 73.40944  ? 34  ARG A N   1 
ATOM   253  C  CA  . ARG A 1 39  ? 32.47311 18.28772  14.49583 1.000 73.10203  ? 34  ARG A CA  1 
ATOM   254  C  C   . ARG A 1 39  ? 33.29016 18.87668  15.64008 1.000 75.80552  ? 34  ARG A C   1 
ATOM   255  O  O   . ARG A 1 39  ? 34.29730 18.29263  16.05887 1.000 69.74431  ? 34  ARG A O   1 
ATOM   256  C  CB  . ARG A 1 39  ? 32.89225 18.91790  13.16776 1.000 73.85415  ? 34  ARG A CB  1 
ATOM   257  C  CG  . ARG A 1 39  ? 32.67060 18.03515  11.95065 1.000 67.34938  ? 34  ARG A CG  1 
ATOM   258  C  CD  . ARG A 1 39  ? 33.56552 18.47026  10.79566 1.000 77.98880  ? 34  ARG A CD  1 
ATOM   259  N  NE  . ARG A 1 39  ? 33.25537 17.76447  9.55777  1.000 74.43686  ? 34  ARG A NE  1 
ATOM   260  C  CZ  . ARG A 1 39  ? 33.98702 17.82990  8.45288  1.000 71.11721  ? 34  ARG A CZ  1 
ATOM   261  N  NH1 . ARG A 1 39  ? 35.10130 18.54269  8.40124  1.000 72.23092  ? 34  ARG A NH1 1 
ATOM   262  N  NH2 . ARG A 1 39  ? 33.59345 17.16015  7.37325  1.000 57.36490  ? 34  ARG A NH2 1 
ATOM   263  N  N   . SER A 1 40  ? 32.87473 20.03353  16.15875 1.000 74.18848  ? 35  SER A N   1 
ATOM   264  C  CA  . SER A 1 40  ? 33.60860 20.68118  17.23936 1.000 76.75876  ? 35  SER A CA  1 
ATOM   265  C  C   . SER A 1 40  ? 33.52288 19.92039  18.55739 1.000 78.11026  ? 35  SER A C   1 
ATOM   266  O  O   . SER A 1 40  ? 34.29477 20.22102  19.47491 1.000 80.12635  ? 35  SER A O   1 
ATOM   267  C  CB  . SER A 1 40  ? 33.09336 22.10918  17.44211 1.000 67.04439  ? 35  SER A CB  1 
ATOM   268  O  OG  . SER A 1 40  ? 31.74843 22.10733  17.89205 1.000 78.69398  ? 35  SER A OG  1 
ATOM   269  N  N   . ASP A 1 41  ? 32.62219 18.94472  18.67520 1.000 73.73232  ? 36  ASP A N   1 
ATOM   270  C  CA  . ASP A 1 41  ? 32.36494 18.27944  19.94523 1.000 65.51760  ? 36  ASP A CA  1 
ATOM   271  C  C   . ASP A 1 41  ? 32.80055 16.81830  19.95901 1.000 67.24788  ? 36  ASP A C   1 
ATOM   272  O  O   . ASP A 1 41  ? 32.49057 16.10395  20.91854 1.000 52.85562  ? 36  ASP A O   1 
ATOM   273  C  CB  . ASP A 1 41  ? 30.87991 18.38627  20.29741 1.000 69.86990  ? 36  ASP A CB  1 
ATOM   274  C  CG  . ASP A 1 41  ? 30.64527 18.52921  21.78788 1.000 70.63393  ? 36  ASP A CG  1 
ATOM   275  O  OD1 . ASP A 1 41  ? 31.63383 18.71318  22.53069 1.000 69.48374  ? 36  ASP A OD1 1 
ATOM   276  O  OD2 . ASP A 1 41  ? 29.47384 18.46122  22.21701 1.000 76.35276  ? 36  ASP A OD2 1 
ATOM   277  N  N   . VAL A 1 42  ? 33.50690 16.35516  18.92988 1.000 66.69850  ? 37  VAL A N   1 
ATOM   278  C  CA  . VAL A 1 42  ? 33.98609 14.97550  18.88841 1.000 62.03430  ? 37  VAL A CA  1 
ATOM   279  C  C   . VAL A 1 42  ? 35.22314 14.87565  19.77477 1.000 65.57040  ? 37  VAL A C   1 
ATOM   280  O  O   . VAL A 1 42  ? 36.27843 15.42483  19.44990 1.000 64.59775  ? 37  VAL A O   1 
ATOM   281  C  CB  . VAL A 1 42  ? 34.29688 14.51969  17.45809 1.000 63.49895  ? 37  VAL A CB  1 
ATOM   282  C  CG1 . VAL A 1 42  ? 34.65289 13.03621  17.44300 1.000 40.06446  ? 37  VAL A CG1 1 
ATOM   283  C  CG2 . VAL A 1 42  ? 33.12307 14.79233  16.54274 1.000 53.51527  ? 37  VAL A CG2 1 
ATOM   284  N  N   . LYS A 1 43  ? 35.09663 14.16923  20.89368 1.000 49.63132  ? 38  LYS A N   1 
ATOM   285  C  CA  . LYS A 1 43  ? 36.19893 13.96771  21.82436 1.000 61.69312  ? 38  LYS A CA  1 
ATOM   286  C  C   . LYS A 1 43  ? 36.80615 12.59036  21.58313 1.000 56.57892  ? 38  LYS A C   1 
ATOM   287  O  O   . LYS A 1 43  ? 36.13611 11.57119  21.77691 1.000 44.36173  ? 38  LYS A O   1 
ATOM   288  C  CB  . LYS A 1 43  ? 35.71937 14.10302  23.27056 1.000 51.09711  ? 38  LYS A CB  1 
ATOM   289  C  CG  . LYS A 1 43  ? 36.84429 14.17959  24.28919 1.000 63.02964  ? 38  LYS A CG  1 
ATOM   290  C  CD  . LYS A 1 43  ? 36.29923 14.23749  25.70625 1.000 46.75313  ? 38  LYS A CD  1 
ATOM   291  C  CE  . LYS A 1 43  ? 35.60446 12.94107  26.07315 1.000 53.41019  ? 38  LYS A CE  1 
ATOM   292  N  NZ  . LYS A 1 43  ? 36.52882 11.77263  26.02690 1.000 53.89547  ? 38  LYS A NZ  1 
ATOM   293  N  N   . LEU A 1 44  ? 38.06735 12.56146  21.15306 1.000 47.82959  ? 39  LEU A N   1 
ATOM   294  C  CA  . LEU A 1 44  ? 38.77755 11.30801  20.93808 1.000 60.51441  ? 39  LEU A CA  1 
ATOM   295  C  C   . LEU A 1 44  ? 39.79907 11.00263  22.02575 1.000 67.89525  ? 39  LEU A C   1 
ATOM   296  O  O   . LEU A 1 44  ? 40.25589 9.85793   22.11750 1.000 66.39929  ? 39  LEU A O   1 
ATOM   297  C  CB  . LEU A 1 44  ? 39.48478 11.31686  19.57338 1.000 62.01397  ? 39  LEU A CB  1 
ATOM   298  C  CG  . LEU A 1 44  ? 38.61650 11.38668  18.31383 1.000 52.79697  ? 39  LEU A CG  1 
ATOM   299  C  CD1 . LEU A 1 44  ? 39.48004 11.33817  17.06475 1.000 49.01896  ? 39  LEU A CD1 1 
ATOM   300  C  CD2 . LEU A 1 44  ? 37.58564 10.27113  18.29212 1.000 55.03849  ? 39  LEU A CD2 1 
ATOM   301  N  N   . VAL A 1 45  ? 40.16825 11.98543  22.84521 1.000 64.40329  ? 40  VAL A N   1 
ATOM   302  C  CA  . VAL A 1 45  ? 41.19889 11.81481  23.86360 1.000 63.43493  ? 40  VAL A CA  1 
ATOM   303  C  C   . VAL A 1 45  ? 40.53361 11.63288  25.22175 1.000 64.33263  ? 40  VAL A C   1 
ATOM   304  O  O   . VAL A 1 45  ? 39.51459 12.27025  25.52392 1.000 63.12277  ? 40  VAL A O   1 
ATOM   305  C  CB  . VAL A 1 45  ? 42.17761 13.00769  23.86813 1.000 69.22243  ? 40  VAL A CB  1 
ATOM   306  C  CG1 . VAL A 1 45  ? 41.47877 14.28964  24.31260 1.000 65.41461  ? 40  VAL A CG1 1 
ATOM   307  C  CG2 . VAL A 1 45  ? 43.39242 12.70881  24.73903 1.000 63.35739  ? 40  VAL A CG2 1 
ATOM   308  N  N   . ALA A 1 46  ? 41.09577 10.74199  26.03535 1.000 60.99591  ? 41  ALA A N   1 
ATOM   309  C  CA  . ALA A 1 46  ? 40.58136 10.52633  27.37837 1.000 65.50259  ? 41  ALA A CA  1 
ATOM   310  C  C   . ALA A 1 46  ? 40.98190 11.68284  28.29080 1.000 50.39487  ? 41  ALA A C   1 
ATOM   311  O  O   . ALA A 1 46  ? 41.93556 12.41743  28.02503 1.000 56.22644  ? 41  ALA A O   1 
ATOM   312  C  CB  . ALA A 1 46  ? 41.08717 9.19820   27.94119 1.000 60.79513  ? 41  ALA A CB  1 
ATOM   313  N  N   . ALA A 1 47  ? 40.24189 11.82843  29.39106 1.000 49.07578  ? 42  ALA A N   1 
ATOM   314  C  CA  . ALA A 1 47  ? 40.34136 13.01391  30.23616 1.000 59.02037  ? 42  ALA A CA  1 
ATOM   315  C  C   . ALA A 1 47  ? 41.56098 13.02340  31.15132 1.000 65.62643  ? 42  ALA A C   1 
ATOM   316  O  O   . ALA A 1 47  ? 41.84741 14.07138  31.74152 1.000 78.40431  ? 42  ALA A O   1 
ATOM   317  C  CB  . ALA A 1 47  ? 39.07446 13.15970  31.08213 1.000 48.27746  ? 42  ALA A CB  1 
ATOM   318  N  N   . GLU A 1 48  ? 42.25860 11.89193  31.29731 1.000 62.36274  ? 43  GLU A N   1 
ATOM   319  C  CA  . GLU A 1 48  ? 43.47283 11.75005  32.10516 1.000 61.94158  ? 43  GLU A CA  1 
ATOM   320  C  C   . GLU A 1 48  ? 43.18183 11.69695  33.60592 1.000 58.92709  ? 43  GLU A C   1 
ATOM   321  O  O   . GLU A 1 48  ? 43.87312 10.98238  34.34009 1.000 53.53512  ? 43  GLU A O   1 
ATOM   322  C  CB  . GLU A 1 48  ? 44.47949 12.86666  31.79511 1.000 69.98463  ? 43  GLU A CB  1 
ATOM   323  C  CG  . GLU A 1 48  ? 45.85060 12.66649  32.42565 1.000 70.80154  ? 43  GLU A CG  1 
ATOM   324  C  CD  . GLU A 1 48  ? 46.90718 13.58331  31.83477 1.000 87.82777  ? 43  GLU A CD  1 
ATOM   325  O  OE1 . GLU A 1 48  ? 46.56794 14.39166  30.94416 1.000 87.44172  ? 43  GLU A OE1 1 
ATOM   326  O  OE2 . GLU A 1 48  ? 48.07907 13.49216  32.25829 1.000 95.12379  ? 43  GLU A OE2 1 
ATOM   327  N  N   . LEU A 1 49  ? 42.17588 12.43462  34.07971 1.000 42.46614  ? 44  LEU A N   1 
ATOM   328  C  CA  . LEU A 1 49  ? 41.71556 12.34039  35.46885 1.000 46.78813  ? 44  LEU A CA  1 
ATOM   329  C  C   . LEU A 1 49  ? 40.19275 12.24030  35.52005 1.000 40.24192  ? 44  LEU A C   1 
ATOM   330  O  O   . LEU A 1 49  ? 39.51382 13.12240  36.05737 1.000 39.27420  ? 44  LEU A O   1 
ATOM   331  C  CB  . LEU A 1 49  ? 42.21795 13.52733  36.29115 1.000 41.50995  ? 44  LEU A CB  1 
ATOM   332  C  CG  . LEU A 1 49  ? 43.72654 13.59012  36.55001 1.000 47.39776  ? 44  LEU A CG  1 
ATOM   333  C  CD1 . LEU A 1 49  ? 44.08604 14.82877  37.36186 1.000 54.44168  ? 44  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A 1 49  ? 44.22252 12.32736  37.24489 1.000 42.93286  ? 44  LEU A CD2 1 
ATOM   335  N  N   . PRO A 1 50  ? 39.61833 11.15762  34.99127 1.000 33.94818  ? 45  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 50  ? 38.15670 11.02507  34.99866 1.000 30.71663  ? 45  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 50  ? 37.61261 10.84731  36.40743 1.000 33.38984  ? 45  PRO A C   1 
ATOM   338  O  O   . PRO A 1 50  ? 38.29138 10.33059  37.29788 1.000 33.63503  ? 45  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 50  ? 37.90819 9.76929   34.15374 1.000 36.38007  ? 45  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 50  ? 39.15898 8.96449   34.32459 1.000 31.74818  ? 45  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 50  ? 40.26963 9.99027   34.36708 1.000 37.56662  ? 45  PRO A CD  1 
ATOM   342  N  N   . GLU A 1 51  ? 36.37582 11.30520  36.60258 1.000 34.56817  ? 46  GLU A N   1 
ATOM   343  C  CA  . GLU A 1 51  ? 35.69107 11.09037  37.86773 1.000 31.90184  ? 46  GLU A CA  1 
ATOM   344  C  C   . GLU A 1 51  ? 35.24468 9.63390   37.97788 1.000 30.93550  ? 46  GLU A C   1 
ATOM   345  O  O   . GLU A 1 51  ? 34.91584 9.00341   36.97312 1.000 26.17804  ? 46  GLU A O   1 
ATOM   346  C  CB  . GLU A 1 51  ? 34.46695 11.99353  37.98857 1.000 40.35070  ? 46  GLU A CB  1 
ATOM   347  C  CG  . GLU A 1 51  ? 34.74756 13.44635  38.31355 1.000 50.18233  ? 46  GLU A CG  1 
ATOM   348  C  CD  . GLU A 1 51  ? 33.46864 14.20918  38.59398 1.000 68.24631  ? 46  GLU A CD  1 
ATOM   349  O  OE1 . GLU A 1 51  ? 32.41972 13.55382  38.78376 1.000 64.35675  ? 46  GLU A OE1 1 
ATOM   350  O  OE2 . GLU A 1 51  ? 33.50664 15.45693  38.62068 1.000 80.58060  ? 46  GLU A OE2 1 
ATOM   351  N  N   . PRO A 1 52  ? 35.22262 9.07817   39.18841 1.000 30.62507  ? 47  PRO A N   1 
ATOM   352  C  CA  . PRO A 1 52  ? 34.67806 7.72659   39.36304 1.000 28.97994  ? 47  PRO A CA  1 
ATOM   353  C  C   . PRO A 1 52  ? 33.23765 7.63969   38.87429 1.000 29.99557  ? 47  PRO A C   1 
ATOM   354  O  O   . PRO A 1 52  ? 32.43796 8.55547   39.06762 1.000 29.16223  ? 47  PRO A O   1 
ATOM   355  C  CB  . PRO A 1 52  ? 34.77324 7.50460   40.87699 1.000 28.84287  ? 47  PRO A CB  1 
ATOM   356  C  CG  . PRO A 1 52  ? 35.93166 8.36027   41.29756 1.000 31.48131  ? 47  PRO A CG  1 
ATOM   357  C  CD  . PRO A 1 52  ? 35.86181 9.58574   40.41495 1.000 29.72067  ? 47  PRO A CD  1 
ATOM   358  N  N   . LEU A 1 53  ? 32.92047 6.54408   38.23893 1.000 26.57453  ? 48  LEU A N   1 
ATOM   359  C  CA  . LEU A 1 53  ? 31.57486 6.32459   37.73750 1.000 21.44776  ? 48  LEU A CA  1 
ATOM   360  C  C   . LEU A 1 53  ? 30.71200 5.67004   38.81024 1.000 27.24794  ? 48  LEU A C   1 
ATOM   361  O  O   . LEU A 1 53  ? 31.23062 4.98544   39.69648 1.000 25.57932  ? 48  LEU A O   1 
ATOM   362  C  CB  . LEU A 1 53  ? 31.61068 5.42959   36.49944 1.000 25.94751  ? 48  LEU A CB  1 
ATOM   363  C  CG  . LEU A 1 53  ? 32.26236 6.02034   35.24604 1.000 32.30177  ? 48  LEU A CG  1 
ATOM   364  C  CD1 . LEU A 1 53  ? 32.15913 5.03184   34.10592 1.000 41.99022  ? 48  LEU A CD1 1 
ATOM   365  C  CD2 . LEU A 1 53  ? 31.60548 7.33566   34.87127 1.000 35.33490  ? 48  LEU A CD2 1 
ATOM   366  N  N   . PRO A 1 54  ? 29.39528 5.84782   38.77117 1.000 25.33583  ? 49  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 54  ? 28.54978 5.18333   39.77046 1.000 25.40328  ? 49  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 54  ? 28.48221 3.68262   39.52636 1.000 26.93803  ? 49  PRO A C   1 
ATOM   369  O  O   . PRO A 1 54  ? 28.32484 3.21942   38.39425 1.000 25.32647  ? 49  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 54  ? 27.18135 5.85439   39.59647 1.000 30.16953  ? 49  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 54  ? 27.19159 6.42187   38.23954 1.000 36.32019  ? 49  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 54  ? 28.62018 6.70198   37.85678 1.000 30.14830  ? 49  PRO A CD  1 
ATOM   373  N  N   . VAL A 1 55  ? 28.63500 2.92419   40.61008 1.000 24.71086  ? 50  VAL A N   1 
ATOM   374  C  CA  . VAL A 1 55  ? 28.59589 1.46638   40.58340 1.000 20.14258  ? 50  VAL A CA  1 
ATOM   375  C  C   . VAL A 1 55  ? 27.53345 1.02518   41.58175 1.000 23.48619  ? 50  VAL A C   1 
ATOM   376  O  O   . VAL A 1 55  ? 27.50421 1.51939   42.71514 1.000 25.81628  ? 50  VAL A O   1 
ATOM   377  C  CB  . VAL A 1 55  ? 29.96549 0.84878   40.93155 1.000 25.48393  ? 50  VAL A CB  1 
ATOM   378  C  CG1 . VAL A 1 55  ? 29.92210 -0.67705  40.80415 1.000 21.83070  ? 50  VAL A CG1 1 
ATOM   379  C  CG2 . VAL A 1 55  ? 31.06437 1.42594   40.04010 1.000 35.97617  ? 50  VAL A CG2 1 
ATOM   380  N  N   . VAL A 1 56  ? 26.64856 0.12446   41.15458 1.000 21.23037  ? 51  VAL A N   1 
ATOM   381  C  CA  . VAL A 1 56  ? 25.58700 -0.42047  41.99931 1.000 22.30037  ? 51  VAL A CA  1 
ATOM   382  C  C   . VAL A 1 56  ? 25.75401 -1.93199  42.04268 1.000 25.10754  ? 51  VAL A C   1 
ATOM   383  O  O   . VAL A 1 56  ? 25.96759 -2.56702  41.00403 1.000 24.02728  ? 51  VAL A O   1 
ATOM   384  C  CB  . VAL A 1 56  ? 24.18788 -0.04082  41.47597 1.000 23.35826  ? 51  VAL A CB  1 
ATOM   385  C  CG1 . VAL A 1 56  ? 23.08491 -0.71868  42.30365 1.000 23.63431  ? 51  VAL A CG1 1 
ATOM   386  C  CG2 . VAL A 1 56  ? 24.02092 1.47810   41.47059 1.000 25.90902  ? 51  VAL A CG2 1 
ATOM   387  N  N   . ASP A 1 57  ? 25.66830 -2.49910  43.24062 1.000 22.31047  ? 52  ASP A N   1 
ATOM   388  C  CA  . ASP A 1 57  ? 25.76362 -3.93787  43.45524 1.000 23.83279  ? 52  ASP A CA  1 
ATOM   389  C  C   . ASP A 1 57  ? 24.33710 -4.46521  43.57097 1.000 25.98689  ? 52  ASP A C   1 
ATOM   390  O  O   . ASP A 1 57  ? 23.65573 -4.21519  44.57285 1.000 23.29372  ? 52  ASP A O   1 
ATOM   391  C  CB  . ASP A 1 57  ? 26.59310 -4.23051  44.70815 1.000 25.35585  ? 52  ASP A CB  1 
ATOM   392  C  CG  . ASP A 1 57  ? 26.76761 -5.71917  44.98821 1.000 26.85533  ? 52  ASP A CG  1 
ATOM   393  O  OD1 . ASP A 1 57  ? 25.82146 -6.50683  44.77554 1.000 23.86537  ? 52  ASP A OD1 1 
ATOM   394  O  OD2 . ASP A 1 57  ? 27.86442 -6.11099  45.45312 1.000 26.43575  ? 52  ASP A OD2 1 
ATOM   395  N  N   . LEU A 1 58  ? 23.88606 -5.18688  42.54002 1.000 22.74531  ? 53  LEU A N   1 
ATOM   396  C  CA  . LEU A 1 58  ? 22.50969 -5.67691  42.51864 1.000 22.94410  ? 53  LEU A CA  1 
ATOM   397  C  C   . LEU A 1 58  ? 22.20101 -6.51905  43.74885 1.000 22.66397  ? 53  LEU A C   1 
ATOM   398  O  O   . LEU A 1 58  ? 21.09524 -6.44453  44.30020 1.000 29.08788  ? 53  LEU A O   1 
ATOM   399  C  CB  . LEU A 1 58  ? 22.26103 -6.50326  41.25497 1.000 23.32349  ? 53  LEU A CB  1 
ATOM   400  C  CG  . LEU A 1 58  ? 20.78763 -6.85698  41.04489 1.000 28.56436  ? 53  LEU A CG  1 
ATOM   401  C  CD1 . LEU A 1 58  ? 20.00611 -5.58497  40.70019 1.000 32.42205  ? 53  LEU A CD1 1 
ATOM   402  C  CD2 . LEU A 1 58  ? 20.60349 -7.92334  39.97991 1.000 27.08712  ? 53  LEU A CD2 1 
ATOM   403  N  N   . SER A 1 59  ? 23.16541 -7.32715  44.20076 1.000 24.38822  ? 54  SER A N   1 
ATOM   404  C  CA  . SER A 1 59  ? 22.88872 -8.21024  45.33192 1.000 28.67260  ? 54  SER A CA  1 
ATOM   405  C  C   . SER A 1 59  ? 22.70060 -7.46377  46.64871 1.000 31.16283  ? 54  SER A C   1 
ATOM   406  O  O   . SER A 1 59  ? 22.18931 -8.05617  47.60599 1.000 28.96083  ? 54  SER A O   1 
ATOM   407  C  CB  . SER A 1 59  ? 24.00544 -9.24051  45.48065 1.000 28.03360  ? 54  SER A CB  1 
ATOM   408  O  OG  . SER A 1 59  ? 25.18788 -8.65828  46.00092 1.000 27.50475  ? 54  SER A OG  1 
ATOM   409  N  N   . ARG A 1 60  ? 23.09234 -6.19533  46.72651 1.000 25.73786  ? 55  ARG A N   1 
ATOM   410  C  CA  . ARG A 1 60  ? 22.96239 -5.40954  47.94586 1.000 29.11080  ? 55  ARG A CA  1 
ATOM   411  C  C   . ARG A 1 60  ? 21.82295 -4.40278  47.87880 1.000 30.59984  ? 55  ARG A C   1 
ATOM   412  O  O   . ARG A 1 60  ? 21.65268 -3.61388  48.81479 1.000 28.80970  ? 55  ARG A O   1 
ATOM   413  C  CB  . ARG A 1 60  ? 24.27283 -4.66431  48.24853 1.000 28.51017  ? 55  ARG A CB  1 
ATOM   414  C  CG  . ARG A 1 60  ? 25.54298 -5.51200  48.23368 1.000 29.67085  ? 55  ARG A CG  1 
ATOM   415  C  CD  . ARG A 1 60  ? 25.39543 -6.80694  49.02649 1.000 27.35772  ? 55  ARG A CD  1 
ATOM   416  N  NE  . ARG A 1 60  ? 25.14841 -6.57973  50.44439 1.000 26.85315  ? 55  ARG A NE  1 
ATOM   417  C  CZ  . ARG A 1 60  ? 24.90464 -7.55108  51.31538 1.000 31.43853  ? 55  ARG A CZ  1 
ATOM   418  N  NH1 . ARG A 1 60  ? 24.86906 -8.82270  50.94223 1.000 33.34428  ? 55  ARG A NH1 1 
ATOM   419  N  NH2 . ARG A 1 60  ? 24.69357 -7.24235  52.59270 1.000 29.71643  ? 55  ARG A NH2 1 
ATOM   420  N  N   . LEU A 1 61  ? 21.02880 -4.42505  46.80843 1.000 27.76938  ? 56  LEU A N   1 
ATOM   421  C  CA  . LEU A 1 61  ? 20.14769 -3.31311  46.48115 1.000 28.02017  ? 56  LEU A CA  1 
ATOM   422  C  C   . LEU A 1 61  ? 18.98355 -3.15037  47.44860 1.000 32.74280  ? 56  LEU A C   1 
ATOM   423  O  O   . LEU A 1 61  ? 18.34690 -2.09244  47.43726 1.000 36.25211  ? 56  LEU A O   1 
ATOM   424  C  CB  . LEU A 1 61  ? 19.63135 -3.47861  45.05092 1.000 34.75875  ? 56  LEU A CB  1 
ATOM   425  C  CG  . LEU A 1 61  ? 19.04717 -2.26505  44.33153 1.000 34.38060  ? 56  LEU A CG  1 
ATOM   426  C  CD1 . LEU A 1 61  ? 19.83740 -1.00171  44.65241 1.000 29.63888  ? 56  LEU A CD1 1 
ATOM   427  C  CD2 . LEU A 1 61  ? 19.03985 -2.53326  42.82714 1.000 29.71765  ? 56  LEU A CD2 1 
ATOM   428  N  N   . ASP A 1 62  ? 18.68803 -4.15153  48.28087 1.000 34.21588  ? 57  ASP A N   1 
ATOM   429  C  CA  . ASP A 1 62  ? 17.65140 -3.97084  49.28970 1.000 33.55037  ? 57  ASP A CA  1 
ATOM   430  C  C   . ASP A 1 62  ? 18.09612 -3.04262  50.41116 1.000 42.26748  ? 57  ASP A C   1 
ATOM   431  O  O   . ASP A 1 62  ? 17.24468 -2.48273  51.11041 1.000 42.83728  ? 57  ASP A O   1 
ATOM   432  C  CB  . ASP A 1 62  ? 17.22936 -5.31908  49.87846 1.000 45.28889  ? 57  ASP A CB  1 
ATOM   433  C  CG  . ASP A 1 62  ? 16.42431 -6.15345  48.90403 1.000 51.82043  ? 57  ASP A CG  1 
ATOM   434  O  OD1 . ASP A 1 62  ? 15.84136 -5.57197  47.96296 1.000 52.81802  ? 57  ASP A OD1 1 
ATOM   435  O  OD2 . ASP A 1 62  ? 16.36772 -7.38823  49.08347 1.000 60.95468  ? 57  ASP A OD2 1 
ATOM   436  N  N   . GLY A 1 63  ? 19.40164 -2.86975  50.59745 1.000 33.41732  ? 58  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 63  ? 19.89184 -2.03887  51.67737 1.000 34.21774  ? 58  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 63  ? 19.78533 -0.55859  51.36171 1.000 34.97510  ? 58  GLY A C   1 
ATOM   439  O  O   . GLY A 1 63  ? 19.85077 -0.13127  50.20895 1.000 28.72696  ? 58  GLY A O   1 
ATOM   440  N  N   . ALA A 1 64  ? 19.62577 0.23664   52.42164 1.000 31.87809  ? 59  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 64  ? 19.46796 1.67588   52.24211 1.000 37.59130  ? 59  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 64  ? 20.69348 2.29238   51.58261 1.000 26.45518  ? 59  ALA A C   1 
ATOM   443  O  O   . ALA A 1 64  ? 20.56443 3.13509   50.68818 1.000 28.63406  ? 59  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 64  ? 19.19484 2.34631   53.58608 1.000 34.31187  ? 59  ALA A CB  1 
ATOM   445  N  N   . GLU A 1 65  ? 21.89107 1.88746   52.01373 1.000 30.51621  ? 60  GLU A N   1 
ATOM   446  C  CA  . GLU A 1 65  ? 23.10911 2.48523   51.47411 1.000 27.30404  ? 60  GLU A CA  1 
ATOM   447  C  C   . GLU A 1 65  ? 23.23283 2.22447   49.97959 1.000 30.88203  ? 60  GLU A C   1 
ATOM   448  O  O   . GLU A 1 65  ? 23.66506 3.09993   49.22277 1.000 27.20600  ? 60  GLU A O   1 
ATOM   449  C  CB  . GLU A 1 65  ? 24.34237 1.94791   52.20601 1.000 33.60529  ? 60  GLU A CB  1 
ATOM   450  C  CG  . GLU A 1 65  ? 24.44289 2.32244   53.68417 1.000 44.37681  ? 60  GLU A CG  1 
ATOM   451  C  CD  . GLU A 1 65  ? 23.55995 1.46751   54.58400 1.000 58.14567  ? 60  GLU A CD  1 
ATOM   452  O  OE1 . GLU A 1 65  ? 23.01530 0.44618   54.10702 1.000 43.67717  ? 60  GLU A OE1 1 
ATOM   453  O  OE2 . GLU A 1 65  ? 23.41426 1.81893   55.77436 1.000 61.35578  ? 60  GLU A OE2 1 
ATOM   454  N  N   . GLU A 1 66  ? 22.85315 1.02765   49.53318 1.000 30.15675  ? 61  GLU A N   1 
ATOM   455  C  CA  . GLU A 1 66  ? 22.96829 0.71997   48.11333 1.000 25.28872  ? 61  GLU A CA  1 
ATOM   456  C  C   . GLU A 1 66  ? 21.86734 1.39626   47.30846 1.000 27.97917  ? 61  GLU A C   1 
ATOM   457  O  O   . GLU A 1 66  ? 22.10673 1.84930   46.18836 1.000 26.90578  ? 61  GLU A O   1 
ATOM   458  C  CB  . GLU A 1 66  ? 22.94249 -0.78948  47.89053 1.000 24.53557  ? 61  GLU A CB  1 
ATOM   459  C  CG  . GLU A 1 66  ? 23.55526 -1.20729  46.54716 1.000 21.76318  ? 61  GLU A CG  1 
ATOM   460  C  CD  . GLU A 1 66  ? 25.06440 -1.05559  46.52010 1.000 26.28412  ? 61  GLU A CD  1 
ATOM   461  O  OE1 . GLU A 1 66  ? 25.66517 -0.92585  47.60378 1.000 26.33858  ? 61  GLU A OE1 1 
ATOM   462  O  OE2 . GLU A 1 66  ? 25.66125 -1.06205  45.41562 1.000 25.20917  ? 61  GLU A OE2 1 
ATOM   463  N  N   . ALA A 1 67  ? 20.65727 1.47518   47.86227 1.000 27.99931  ? 62  ALA A N   1 
ATOM   464  C  CA  . ALA A 1 67  ? 19.59452 2.22405   47.20145 1.000 24.89314  ? 62  ALA A CA  1 
ATOM   465  C  C   . ALA A 1 67  ? 19.96493 3.69001   47.04085 1.000 25.02257  ? 62  ALA A C   1 
ATOM   466  O  O   . ALA A 1 67  ? 19.55839 4.32857   46.06408 1.000 27.53519  ? 62  ALA A O   1 
ATOM   467  C  CB  . ALA A 1 67  ? 18.28769 2.09862   47.99100 1.000 27.64918  ? 62  ALA A CB  1 
ATOM   468  N  N   . THR A 1 68  ? 20.71861 4.24467   47.99350 1.000 27.99316  ? 63  THR A N   1 
ATOM   469  C  CA  . THR A 1 68  ? 21.17553 5.62594   47.86855 1.000 27.82077  ? 63  THR A CA  1 
ATOM   470  C  C   . THR A 1 68  ? 22.15054 5.78143   46.70704 1.000 24.81966  ? 63  THR A C   1 
ATOM   471  O  O   . THR A 1 68  ? 22.11148 6.78535   45.98465 1.000 23.92344  ? 63  THR A O   1 
ATOM   472  C  CB  . THR A 1 68  ? 21.81873 6.08723   49.17677 1.000 26.73126  ? 63  THR A CB  1 
ATOM   473  O  OG1 . THR A 1 68  ? 20.80940 6.19625   50.18565 1.000 28.74361  ? 63  THR A OG1 1 
ATOM   474  C  CG2 . THR A 1 68  ? 22.49177 7.44079   49.00435 1.000 37.24351  ? 63  THR A CG2 1 
ATOM   475  N  N   . LYS A 1 69  ? 23.04269 4.80625   46.51926 1.000 22.89720  ? 64  LYS A N   1 
ATOM   476  C  CA  . LYS A 1 69  ? 23.94267 4.85286   45.37034 1.000 24.48420  ? 64  LYS A CA  1 
ATOM   477  C  C   . LYS A 1 69  ? 23.16164 4.80833   44.06648 1.000 24.30422  ? 64  LYS A C   1 
ATOM   478  O  O   . LYS A 1 69  ? 23.52844 5.47726   43.09260 1.000 23.27600  ? 64  LYS A O   1 
ATOM   479  C  CB  . LYS A 1 69  ? 24.94019 3.69446   45.42099 1.000 24.00626  ? 64  LYS A CB  1 
ATOM   480  C  CG  . LYS A 1 69  ? 25.87868 3.71059   46.60961 1.000 28.61931  ? 64  LYS A CG  1 
ATOM   481  C  CD  . LYS A 1 69  ? 26.71440 2.44098   46.63187 1.000 27.51104  ? 64  LYS A CD  1 
ATOM   482  C  CE  . LYS A 1 69  ? 27.33873 2.19980   47.98755 1.000 34.22642  ? 64  LYS A CE  1 
ATOM   483  N  NZ  . LYS A 1 69  ? 27.87602 0.80552   48.07094 1.000 32.23480  ? 64  LYS A NZ  1 
ATOM   484  N  N   . LEU A 1 70  ? 22.09548 4.00109   44.02282 1.000 24.54336  ? 65  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 70  ? 21.21813 3.98237   42.85639 1.000 24.65307  ? 65  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 70  ? 20.55561 5.33779   42.64431 1.000 25.09767  ? 65  LEU A C   1 
ATOM   487  O  O   . LEU A 1 70  ? 20.48061 5.83433   41.51638 1.000 24.41219  ? 65  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 70  ? 20.15760 2.89159   43.01302 1.000 24.06521  ? 65  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 70  ? 19.15025 2.80264   41.86127 1.000 27.60318  ? 65  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 70  ? 19.85845 2.50862   40.54000 1.000 24.66756  ? 65  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 70  ? 18.07854 1.75516   42.13618 1.000 25.96128  ? 65  LEU A CD2 1 
ATOM   492  N  N   . ARG A 1 71  ? 20.05238 5.95008   43.71940 1.000 24.17426  ? 66  ARG A N   1 
ATOM   493  C  CA  . ARG A 1 71  ? 19.40954 7.25468   43.57683 1.000 21.39630  ? 66  ARG A CA  1 
ATOM   494  C  C   . ARG A 1 71  ? 20.37946 8.28163   43.00668 1.000 22.20432  ? 66  ARG A C   1 
ATOM   495  O  O   . ARG A 1 71  ? 20.03956 9.02416   42.07659 1.000 27.65497  ? 66  ARG A O   1 
ATOM   496  C  CB  . ARG A 1 71  ? 18.84164 7.72957   44.92309 1.000 23.02723  ? 66  ARG A CB  1 
ATOM   497  C  CG  . ARG A 1 71  ? 18.26201 9.14204   44.84411 1.000 27.91304  ? 66  ARG A CG  1 
ATOM   498  C  CD  . ARG A 1 71  ? 17.56522 9.56701   46.14912 1.000 33.40328  ? 66  ARG A CD  1 
ATOM   499  N  NE  . ARG A 1 71  ? 16.11558 9.41124   46.06108 1.000 41.15669  ? 66  ARG A NE  1 
ATOM   500  C  CZ  . ARG A 1 71  ? 15.40669 8.54070   46.76538 1.000 38.28134  ? 66  ARG A CZ  1 
ATOM   501  N  NH1 . ARG A 1 71  ? 15.97167 7.76171   47.67306 1.000 64.02703  ? 66  ARG A NH1 1 
ATOM   502  N  NH2 . ARG A 1 71  ? 14.09546 8.45526   46.56187 1.000 47.16322  ? 66  ARG A NH2 1 
ATOM   503  N  N   . VAL A 1 72  ? 21.60553 8.32310   43.53473 1.000 25.87406  ? 67  VAL A N   1 
ATOM   504  C  CA  . VAL A 1 72  ? 22.59753 9.27139   43.03224 1.000 27.47948  ? 67  VAL A CA  1 
ATOM   505  C  C   . VAL A 1 72  ? 22.86178 9.03008   41.55451 1.000 29.55496  ? 67  VAL A C   1 
ATOM   506  O  O   . VAL A 1 72  ? 22.93482 9.97524   40.75809 1.000 27.54224  ? 67  VAL A O   1 
ATOM   507  C  CB  . VAL A 1 72  ? 23.89348 9.17757   43.85877 1.000 27.29269  ? 67  VAL A CB  1 
ATOM   508  C  CG1 . VAL A 1 72  ? 25.02744 9.98127   43.19989 1.000 30.05719  ? 67  VAL A CG1 1 
ATOM   509  C  CG2 . VAL A 1 72  ? 23.64016 9.62937   45.28397 1.000 26.63654  ? 67  VAL A CG2 1 
ATOM   510  N  N   . ALA A 1 73  ? 22.99022 7.76091   41.16215 1.000 24.18041  ? 68  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 73  ? 23.22256 7.44595   39.75842 1.000 27.96862  ? 68  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 73  ? 22.05932 7.91343   38.89482 1.000 27.20614  ? 68  ALA A C   1 
ATOM   513  O  O   . ALA A 1 73  ? 22.26640 8.52241   37.83729 1.000 26.14990  ? 68  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 73  ? 23.45129 5.94242   39.59074 1.000 21.47676  ? 68  ALA A CB  1 
ATOM   515  N  N   . LEU A 1 74  ? 20.82490 7.66039   39.34044 1.000 24.84548  ? 69  LEU A N   1 
ATOM   516  C  CA  . LEU A 1 74  ? 19.67728 7.92933   38.48045 1.000 26.11327  ? 69  LEU A CA  1 
ATOM   517  C  C   . LEU A 1 74  ? 19.38507 9.41582   38.38517 1.000 28.91382  ? 69  LEU A C   1 
ATOM   518  O  O   . LEU A 1 74  ? 18.99219 9.90428   37.32214 1.000 25.30002  ? 69  LEU A O   1 
ATOM   519  C  CB  . LEU A 1 74  ? 18.45106 7.17758   38.97835 1.000 27.01097  ? 69  LEU A CB  1 
ATOM   520  C  CG  . LEU A 1 74  ? 18.55657 5.66003   38.85009 1.000 25.51725  ? 69  LEU A CG  1 
ATOM   521  C  CD1 . LEU A 1 74  ? 17.29503 5.00412   39.38019 1.000 36.01420  ? 69  LEU A CD1 1 
ATOM   522  C  CD2 . LEU A 1 74  ? 18.83099 5.25736   37.39954 1.000 27.58499  ? 69  LEU A CD2 1 
ATOM   523  N  N   . GLN A 1 75  ? 19.56440 10.15017  39.48240 1.000 27.63500  ? 70  GLN A N   1 
ATOM   524  C  CA  . GLN A 1 75  ? 19.27871 11.58013  39.46899 1.000 27.49180  ? 70  GLN A CA  1 
ATOM   525  C  C   . GLN A 1 75  ? 20.38777 12.38198  38.79606 1.000 29.89126  ? 70  GLN A C   1 
ATOM   526  O  O   . GLN A 1 75  ? 20.10590 13.34477  38.07268 1.000 36.52526  ? 70  GLN A O   1 
ATOM   527  C  CB  . GLN A 1 75  ? 19.05121 12.08287  40.89932 1.000 28.32500  ? 70  GLN A CB  1 
ATOM   528  C  CG  . GLN A 1 75  ? 17.83090 11.48160  41.58002 1.000 31.36758  ? 70  GLN A CG  1 
ATOM   529  C  CD  . GLN A 1 75  ? 17.54570 12.10460  42.93791 1.000 34.12849  ? 70  GLN A CD  1 
ATOM   530  O  OE1 . GLN A 1 75  ? 18.25112 13.00983  43.38167 1.000 39.94218  ? 70  GLN A OE1 1 
ATOM   531  N  NE2 . GLN A 1 75  ? 16.50436 11.62017  43.60146 1.000 32.48655  ? 70  GLN A NE2 1 
ATOM   532  N  N   . ASN A 1 76  ? 21.65153 12.00924  39.01288 1.000 29.90124  ? 71  ASN A N   1 
ATOM   533  C  CA  . ASN A 1 76  ? 22.76934 12.82803  38.55820 1.000 29.91375  ? 71  ASN A CA  1 
ATOM   534  C  C   . ASN A 1 76  ? 23.45157 12.31291  37.29662 1.000 32.61438  ? 71  ASN A C   1 
ATOM   535  O  O   . ASN A 1 76  ? 24.14556 13.08872  36.62748 1.000 30.77232  ? 71  ASN A O   1 
ATOM   536  C  CB  . ASN A 1 76  ? 23.82115 12.95903  39.66722 1.000 33.94018  ? 71  ASN A CB  1 
ATOM   537  C  CG  . ASN A 1 76  ? 23.33971 13.81510  40.81946 1.000 41.03889  ? 71  ASN A CG  1 
ATOM   538  O  OD1 . ASN A 1 76  ? 22.30313 14.47329  40.72283 1.000 36.84458  ? 71  ASN A OD1 1 
ATOM   539  N  ND2 . ASN A 1 76  ? 24.08926 13.81550  41.91416 1.000 40.06560  ? 71  ASN A ND2 1 
ATOM   540  N  N   . TRP A 1 77  ? 23.28106 11.04615  36.95168 1.000 25.22508  ? 72  TRP A N   1 
ATOM   541  C  CA  . TRP A 1 77  ? 23.94868 10.50392  35.77504 1.000 26.03499  ? 72  TRP A CA  1 
ATOM   542  C  C   . TRP A 1 77  ? 22.99207 9.90861   34.75565 1.000 28.70055  ? 72  TRP A C   1 
ATOM   543  O  O   . TRP A 1 77  ? 23.23840 10.02317  33.54811 1.000 28.12896  ? 72  TRP A O   1 
ATOM   544  C  CB  . TRP A 1 77  ? 24.97016 9.43291   36.19440 1.000 29.24776  ? 72  TRP A CB  1 
ATOM   545  C  CG  . TRP A 1 77  ? 25.98553 9.88124   37.22086 1.000 28.32942  ? 72  TRP A CG  1 
ATOM   546  C  CD1 . TRP A 1 77  ? 25.75235 10.16381  38.54077 1.000 32.76721  ? 72  TRP A CD1 1 
ATOM   547  C  CD2 . TRP A 1 77  ? 27.39483 10.04711  37.02123 1.000 28.68079  ? 72  TRP A CD2 1 
ATOM   548  N  NE1 . TRP A 1 77  ? 26.92726 10.51611  39.16252 1.000 37.75544  ? 72  TRP A NE1 1 
ATOM   549  C  CE2 . TRP A 1 77  ? 27.94842 10.44963  38.25182 1.000 33.39638  ? 72  TRP A CE2 1 
ATOM   550  C  CE3 . TRP A 1 77  ? 28.24178 9.89947   35.91815 1.000 31.73515  ? 72  TRP A CE3 1 
ATOM   551  C  CZ2 . TRP A 1 77  ? 29.30790 10.70687  38.40904 1.000 30.48657  ? 72  TRP A CZ2 1 
ATOM   552  C  CZ3 . TRP A 1 77  ? 29.58788 10.15312  36.07638 1.000 32.15813  ? 72  TRP A CZ3 1 
ATOM   553  C  CH2 . TRP A 1 77  ? 30.10951 10.55323  37.31087 1.000 38.80298  ? 72  TRP A CH2 1 
ATOM   554  N  N   . GLY A 1 78  ? 21.91121 9.27005   35.20305 1.000 23.04048  ? 73  GLY A N   1 
ATOM   555  C  CA  . GLY A 1 78  ? 21.01436 8.56060   34.31720 1.000 21.25335  ? 73  GLY A CA  1 
ATOM   556  C  C   . GLY A 1 78  ? 21.43524 7.14211   33.99850 1.000 25.56840  ? 73  GLY A C   1 
ATOM   557  O  O   . GLY A 1 78  ? 20.70529 6.43762   33.29173 1.000 23.02131  ? 73  GLY A O   1 
ATOM   558  N  N   . PHE A 1 79  ? 22.58788 6.70408   34.49226 1.000 20.31125  ? 74  PHE A N   1 
ATOM   559  C  CA  . PHE A 1 79  ? 23.08514 5.36713   34.21741 1.000 22.71099  ? 74  PHE A CA  1 
ATOM   560  C  C   . PHE A 1 79  ? 23.95631 4.93187   35.38469 1.000 29.06288  ? 74  PHE A C   1 
ATOM   561  O  O   . PHE A 1 79  ? 24.33406 5.74308   36.23668 1.000 25.94626  ? 74  PHE A O   1 
ATOM   562  C  CB  . PHE A 1 79  ? 23.87715 5.32515   32.89978 1.000 20.59155  ? 74  PHE A CB  1 
ATOM   563  C  CG  . PHE A 1 79  ? 25.23074 5.96624   32.98959 1.000 26.69826  ? 74  PHE A CG  1 
ATOM   564  C  CD1 . PHE A 1 79  ? 25.36894 7.34202   32.88399 1.000 25.00040  ? 74  PHE A CD1 1 
ATOM   565  C  CD2 . PHE A 1 79  ? 26.36761 5.19274   33.18167 1.000 28.00941  ? 74  PHE A CD2 1 
ATOM   566  C  CE1 . PHE A 1 79  ? 26.61279 7.93610   32.97609 1.000 21.88384  ? 74  PHE A CE1 1 
ATOM   567  C  CE2 . PHE A 1 79  ? 27.61244 5.78220   33.27715 1.000 26.38976  ? 74  PHE A CE2 1 
ATOM   568  C  CZ  . PHE A 1 79  ? 27.73498 7.15723   33.17380 1.000 26.35534  ? 74  PHE A CZ  1 
ATOM   569  N  N   . PHE A 1 80  ? 24.28238 3.63782   35.40999 1.000 23.43035  ? 75  PHE A N   1 
ATOM   570  C  CA  . PHE A 1 80  ? 25.20366 3.10900   36.40750 1.000 23.63593  ? 75  PHE A CA  1 
ATOM   571  C  C   . PHE A 1 80  ? 25.82605 1.81338   35.89450 1.000 21.60378  ? 75  PHE A C   1 
ATOM   572  O  O   . PHE A 1 80  ? 25.23952 1.11102   35.06541 1.000 21.75999  ? 75  PHE A O   1 
ATOM   573  C  CB  . PHE A 1 80  ? 24.50819 2.87754   37.76064 1.000 23.21345  ? 75  PHE A CB  1 
ATOM   574  C  CG  . PHE A 1 80  ? 23.20751 2.11994   37.67036 1.000 23.13558  ? 75  PHE A CG  1 
ATOM   575  C  CD1 . PHE A 1 80  ? 22.02201 2.77488   37.34642 1.000 24.64177  ? 75  PHE A CD1 1 
ATOM   576  C  CD2 . PHE A 1 80  ? 23.16040 0.76475   37.95078 1.000 21.80922  ? 75  PHE A CD2 1 
ATOM   577  C  CE1 . PHE A 1 80  ? 20.82452 2.07863   37.27830 1.000 24.78849  ? 75  PHE A CE1 1 
ATOM   578  C  CE2 . PHE A 1 80  ? 21.96423 0.06105   37.88000 1.000 25.46171  ? 75  PHE A CE2 1 
ATOM   579  C  CZ  . PHE A 1 80  ? 20.79548 0.72521   37.54709 1.000 26.95694  ? 75  PHE A CZ  1 
ATOM   580  N  N   . LEU A 1 81  ? 27.04335 1.53740   36.36298 1.000 19.48236  ? 76  LEU A N   1 
ATOM   581  C  CA  . LEU A 1 81  ? 27.63216 0.20954   36.24633 1.000 20.86315  ? 76  LEU A CA  1 
ATOM   582  C  C   . LEU A 1 81  ? 26.97970 -0.70695  37.27308 1.000 24.81521  ? 76  LEU A C   1 
ATOM   583  O  O   . LEU A 1 81  ? 26.69912 -0.28213  38.39474 1.000 24.45031  ? 76  LEU A O   1 
ATOM   584  C  CB  . LEU A 1 81  ? 29.13581 0.26377   36.50357 1.000 22.76002  ? 76  LEU A CB  1 
ATOM   585  C  CG  . LEU A 1 81  ? 30.02349 1.05304   35.54950 1.000 28.79138  ? 76  LEU A CG  1 
ATOM   586  C  CD1 . LEU A 1 81  ? 31.36800 1.32760   36.20558 1.000 36.94952  ? 76  LEU A CD1 1 
ATOM   587  C  CD2 . LEU A 1 81  ? 30.20898 0.23797   34.29878 1.000 38.17320  ? 76  LEU A CD2 1 
ATOM   588  N  N   . LEU A 1 82  ? 26.75338 -1.96804  36.89957 1.000 19.98807  ? 77  LEU A N   1 
ATOM   589  C  CA  . LEU A 1 82  ? 26.06132 -2.91568  37.77201 1.000 19.49913  ? 77  LEU A CA  1 
ATOM   590  C  C   . LEU A 1 82  ? 26.92471 -4.15057  37.96488 1.000 21.15161  ? 77  LEU A C   1 
ATOM   591  O  O   . LEU A 1 82  ? 27.33542 -4.78381  36.98496 1.000 23.42690  ? 77  LEU A O   1 
ATOM   592  C  CB  . LEU A 1 82  ? 24.69740 -3.30897  37.19854 1.000 18.69462  ? 77  LEU A CB  1 
ATOM   593  C  CG  . LEU A 1 82  ? 23.85064 -4.20846  38.11178 1.000 21.39864  ? 77  LEU A CG  1 
ATOM   594  C  CD1 . LEU A 1 82  ? 23.37550 -3.40658  39.32027 1.000 25.48735  ? 77  LEU A CD1 1 
ATOM   595  C  CD2 . LEU A 1 82  ? 22.66960 -4.79148  37.35731 1.000 23.31009  ? 77  LEU A CD2 1 
ATOM   596  N  N   . THR A 1 83  ? 27.19378 -4.49539  39.21866 1.000 23.36973  ? 78  THR A N   1 
ATOM   597  C  CA  . THR A 1 83  ? 27.97027 -5.67657  39.56058 1.000 21.09043  ? 78  THR A CA  1 
ATOM   598  C  C   . THR A 1 83  ? 27.08645 -6.67617  40.29773 1.000 22.22513  ? 78  THR A C   1 
ATOM   599  O  O   . THR A 1 83  ? 25.99227 -6.34144  40.76501 1.000 22.58038  ? 78  THR A O   1 
ATOM   600  C  CB  . THR A 1 83  ? 29.18157 -5.30751  40.42576 1.000 22.87707  ? 78  THR A CB  1 
ATOM   601  O  OG1 . THR A 1 83  ? 28.71923 -4.77910  41.67690 1.000 25.99682  ? 78  THR A OG1 1 
ATOM   602  C  CG2 . THR A 1 83  ? 30.04098 -4.25867  39.73707 1.000 29.86351  ? 78  THR A CG2 1 
ATOM   603  N  N   . ASN A 1 84  ? 27.57804 -7.91644  40.39303 1.000 24.12158  ? 79  ASN A N   1 
ATOM   604  C  CA  . ASN A 1 84  ? 26.90903 -8.97303  41.16510 1.000 28.93674  ? 79  ASN A CA  1 
ATOM   605  C  C   . ASN A 1 84  ? 25.44918 -9.12324  40.74209 1.000 24.56613  ? 79  ASN A C   1 
ATOM   606  O  O   . ASN A 1 84  ? 24.54529 -9.29016  41.56734 1.000 27.20779  ? 79  ASN A O   1 
ATOM   607  C  CB  . ASN A 1 84  ? 27.02450 -8.71058  42.66854 1.000 25.18553  ? 79  ASN A CB  1 
ATOM   608  C  CG  . ASN A 1 84  ? 28.37261 -9.12635  43.22802 1.000 29.10624  ? 79  ASN A CG  1 
ATOM   609  O  OD1 . ASN A 1 84  ? 29.08757 -9.91211  42.61696 1.000 28.98786  ? 79  ASN A OD1 1 
ATOM   610  N  ND2 . ASN A 1 84  ? 28.71984 -8.60594  44.40265 1.000 31.85291  ? 79  ASN A ND2 1 
ATOM   611  N  N   . HIS A 1 85  ? 25.22788 -9.06259  39.43298 1.000 24.40852  ? 80  HIS A N   1 
ATOM   612  C  CA  . HIS A 1 85  ? 23.91025 -9.02448  38.81386 1.000 23.97922  ? 80  HIS A CA  1 
ATOM   613  C  C   . HIS A 1 85  ? 23.35503 -10.40837 38.49427 1.000 25.10969  ? 80  HIS A C   1 
ATOM   614  O  O   . HIS A 1 85  ? 22.23070 -10.50916 37.99213 1.000 31.26351  ? 80  HIS A O   1 
ATOM   615  C  CB  . HIS A 1 85  ? 23.99038 -8.19826  37.53235 1.000 21.71104  ? 80  HIS A CB  1 
ATOM   616  C  CG  . HIS A 1 85  ? 25.13613 -8.59365  36.65270 1.000 19.61260  ? 80  HIS A CG  1 
ATOM   617  N  ND1 . HIS A 1 85  ? 25.26138 -9.85677  36.11880 1.000 24.81759  ? 80  HIS A ND1 1 
ATOM   618  C  CD2 . HIS A 1 85  ? 26.22896 -7.90234  36.24742 1.000 19.12347  ? 80  HIS A CD2 1 
ATOM   619  C  CE1 . HIS A 1 85  ? 26.37762 -9.92705  35.41435 1.000 26.76146  ? 80  HIS A CE1 1 
ATOM   620  N  NE2 . HIS A 1 85  ? 26.97796 -8.75121  35.46837 1.000 23.31047  ? 80  HIS A NE2 1 
ATOM   621  N  N   . GLY A 1 86  ? 24.11280 -11.47148 38.74853 1.000 21.91349  ? 81  GLY A N   1 
ATOM   622  C  CA  . GLY A 1 86  ? 23.59157 -12.81699 38.64843 1.000 27.21093  ? 81  GLY A CA  1 
ATOM   623  C  C   . GLY A 1 86  ? 23.74164 -13.48965 37.29861 1.000 24.35508  ? 81  GLY A C   1 
ATOM   624  O  O   . GLY A 1 86  ? 23.48216 -14.69605 37.19939 1.000 27.38617  ? 81  GLY A O   1 
ATOM   625  N  N   . VAL A 1 87  ? 24.13447 -12.76361 36.25440 1.000 26.90980  ? 82  VAL A N   1 
ATOM   626  C  CA  . VAL A 1 87  ? 24.32999 -13.38550 34.94703 1.000 25.12634  ? 82  VAL A CA  1 
ATOM   627  C  C   . VAL A 1 87  ? 25.71850 -14.00463 34.89732 1.000 33.59674  ? 82  VAL A C   1 
ATOM   628  O  O   . VAL A 1 87  ? 26.71994 -13.32027 35.14069 1.000 28.70034  ? 82  VAL A O   1 
ATOM   629  C  CB  . VAL A 1 87  ? 24.14071 -12.36108 33.81924 1.000 26.67337  ? 82  VAL A CB  1 
ATOM   630  C  CG1 . VAL A 1 87  ? 24.43677 -13.00200 32.45811 1.000 26.55877  ? 82  VAL A CG1 1 
ATOM   631  C  CG2 . VAL A 1 87  ? 22.73130 -11.79202 33.85504 1.000 28.93960  ? 82  VAL A CG2 1 
ATOM   632  N  N   . GLU A 1 88  ? 25.78008 -15.29881 34.57321 1.000 26.83366  ? 83  GLU A N   1 
ATOM   633  C  CA  . GLU A 1 88  ? 27.05271 -16.00882 34.52139 1.000 27.72841  ? 83  GLU A CA  1 
ATOM   634  C  C   . GLU A 1 88  ? 28.01581 -15.29812 33.58443 1.000 32.48106  ? 83  GLU A C   1 
ATOM   635  O  O   . GLU A 1 88  ? 27.65070 -14.92648 32.46510 1.000 28.82546  ? 83  GLU A O   1 
ATOM   636  C  CB  . GLU A 1 88  ? 26.84816 -17.45185 34.05561 1.000 33.20303  ? 83  GLU A CB  1 
ATOM   637  C  CG  . GLU A 1 88  ? 26.38546 -18.40704 35.14336 1.000 41.76371  ? 83  GLU A CG  1 
ATOM   638  C  CD  . GLU A 1 88  ? 26.48744 -19.86956 34.72938 1.000 47.47825  ? 83  GLU A CD  1 
ATOM   639  O  OE1 . GLU A 1 88  ? 27.41673 -20.22105 33.97344 1.000 47.16647  ? 83  GLU A OE1 1 
ATOM   640  O  OE2 . GLU A 1 88  ? 25.63419 -20.66941 35.16769 1.000 68.01181  ? 83  GLU A OE2 1 
ATOM   641  N  N   . ALA A 1 89  ? 29.24837 -15.09768 34.05364 1.000 30.34118  ? 84  ALA A N   1 
ATOM   642  C  CA  . ALA A 1 89  ? 30.24277 -14.42331 33.22765 1.000 29.57473  ? 84  ALA A CA  1 
ATOM   643  C  C   . ALA A 1 89  ? 30.46862 -15.16708 31.91444 1.000 27.55001  ? 84  ALA A C   1 
ATOM   644  O  O   . ALA A 1 89  ? 30.64210 -14.53864 30.86357 1.000 30.20801  ? 84  ALA A O   1 
ATOM   645  C  CB  . ALA A 1 89  ? 31.55150 -14.27288 34.00079 1.000 30.11431  ? 84  ALA A CB  1 
ATOM   646  N  N   . SER A 1 90  ? 30.44230 -16.50250 31.94210 1.000 27.50708  ? 85  SER A N   1 
ATOM   647  C  CA  . SER A 1 90  ? 30.66868 -17.25576 30.70702 1.000 28.39638  ? 85  SER A CA  1 
ATOM   648  C  C   . SER A 1 90  ? 29.52644 -17.07996 29.71468 1.000 28.69323  ? 85  SER A C   1 
ATOM   649  O  O   . SER A 1 90  ? 29.74732 -17.16621 28.49857 1.000 28.78484  ? 85  SER A O   1 
ATOM   650  C  CB  . SER A 1 90  ? 30.87637 -18.74050 31.00912 1.000 29.95763  ? 85  SER A CB  1 
ATOM   651  O  OG  . SER A 1 90  ? 29.74468 -19.29208 31.65466 1.000 34.89106  ? 85  SER A OG  1 
ATOM   652  N  N   . LEU A 1 91  ? 28.30690 -16.84476 30.20471 1.000 27.51820  ? 86  LEU A N   1 
ATOM   653  C  CA  . LEU A 1 91  ? 27.19550 -16.55686 29.30344 1.000 30.83762  ? 86  LEU A CA  1 
ATOM   654  C  C   . LEU A 1 91  ? 27.38420 -15.20736 28.62184 1.000 27.23090  ? 86  LEU A C   1 
ATOM   655  O  O   . LEU A 1 91  ? 27.07594 -15.05185 27.43370 1.000 29.75734  ? 86  LEU A O   1 
ATOM   656  C  CB  . LEU A 1 91  ? 25.87228 -16.60037 30.06925 1.000 32.24704  ? 86  LEU A CB  1 
ATOM   657  C  CG  . LEU A 1 91  ? 24.59785 -16.29677 29.27424 1.000 32.74389  ? 86  LEU A CG  1 
ATOM   658  C  CD1 . LEU A 1 91  ? 24.43924 -17.29133 28.13289 1.000 34.75260  ? 86  LEU A CD1 1 
ATOM   659  C  CD2 . LEU A 1 91  ? 23.35828 -16.31465 30.17725 1.000 33.34848  ? 86  LEU A CD2 1 
ATOM   660  N  N   . MET A 1 92  ? 27.90856 -14.22675 29.35272 1.000 23.16384  ? 87  MET A N   1 
ATOM   661  C  CA  . MET A 1 92  ? 28.22367 -12.93624 28.74887 1.000 26.73446  ? 87  MET A CA  1 
ATOM   662  C  C   . MET A 1 92  ? 29.30163 -13.08778 27.68560 1.000 26.49430  ? 87  MET A C   1 
ATOM   663  O  O   . MET A 1 92  ? 29.20046 -12.50985 26.59732 1.000 27.89155  ? 87  MET A O   1 
ATOM   664  C  CB  . MET A 1 92  ? 28.66252 -11.95086 29.82865 1.000 27.86198  ? 87  MET A CB  1 
ATOM   665  C  CG  . MET A 1 92  ? 27.65664 -11.82080 30.95553 1.000 26.39721  ? 87  MET A CG  1 
ATOM   666  S  SD  . MET A 1 92  ? 28.19367 -10.66564 32.22591 1.000 26.85203  ? 87  MET A SD  1 
ATOM   667  C  CE  . MET A 1 92  ? 27.83734 -9.10687  31.44805 1.000 30.73219  ? 87  MET A CE  1 
ATOM   668  N  N   . ASP A 1 93  ? 30.34877 -13.86058 27.98953 1.000 23.93080  ? 88  ASP A N   1 
ATOM   669  C  CA  . ASP A 1 93  ? 31.38121 -14.12690 26.98869 1.000 25.57093  ? 88  ASP A CA  1 
ATOM   670  C  C   . ASP A 1 93  ? 30.77996 -14.73737 25.73414 1.000 31.65671  ? 88  ASP A C   1 
ATOM   671  O  O   . ASP A 1 93  ? 31.14119 -14.35429 24.61255 1.000 31.48559  ? 88  ASP A O   1 
ATOM   672  C  CB  . ASP A 1 93  ? 32.44525 -15.06780 27.55182 1.000 31.38868  ? 88  ASP A CB  1 
ATOM   673  C  CG  . ASP A 1 93  ? 33.23104 -14.45405 28.68378 1.000 31.80232  ? 88  ASP A CG  1 
ATOM   674  O  OD1 . ASP A 1 93  ? 33.31661 -13.21201 28.74066 1.000 32.17744  ? 88  ASP A OD1 1 
ATOM   675  O  OD2 . ASP A 1 93  ? 33.76451 -15.22471 29.51298 1.000 35.39766  ? 88  ASP A OD2 1 
ATOM   676  N  N   . SER A 1 94  ? 29.85823 -15.69183 25.90389 1.000 29.90843  ? 89  SER A N   1 
ATOM   677  C  CA  . SER A 1 94  ? 29.34982 -16.42715 24.75132 1.000 35.64632  ? 89  SER A CA  1 
ATOM   678  C  C   . SER A 1 94  ? 28.50106 -15.53854 23.85099 1.000 31.21552  ? 89  SER A C   1 
ATOM   679  O  O   . SER A 1 94  ? 28.63694 -15.58991 22.62394 1.000 32.22339  ? 89  SER A O   1 
ATOM   680  C  CB  . SER A 1 94  ? 28.55287 -17.64832 25.20663 1.000 35.31666  ? 89  SER A CB  1 
ATOM   681  O  OG  . SER A 1 94  ? 29.40290 -18.64290 25.75586 1.000 40.19312  ? 89  SER A OG  1 
ATOM   682  N  N   . VAL A 1 95  ? 27.62387 -14.71440 24.43170 1.000 29.48601  ? 90  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 95  ? 26.75730 -13.90635 23.57977 1.000 29.86724  ? 90  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 95  ? 27.57916 -12.88110 22.80945 1.000 36.20734  ? 90  VAL A C   1 
ATOM   685  O  O   . VAL A 1 95  ? 27.28227 -12.58667 21.64431 1.000 32.07629  ? 90  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 95  ? 25.61888 -13.25332 24.38993 1.000 31.93265  ? 90  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 95  ? 26.10334 -12.04514 25.23071 1.000 25.84338  ? 90  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 95  ? 24.47049 -12.86508 23.45708 1.000 29.46481  ? 90  VAL A CG2 1 
ATOM   689  N  N   . MET A 1 96  ? 28.64907 -12.36215 23.41320 1.000 26.83664  ? 91  MET A N   1 
ATOM   690  C  CA  . MET A 1 96  ? 29.49919 -11.41605 22.69746 1.000 30.32720  ? 91  MET A CA  1 
ATOM   691  C  C   . MET A 1 96  ? 30.35229 -12.11850 21.64494 1.000 30.73347  ? 91  MET A C   1 
ATOM   692  O  O   . MET A 1 96  ? 30.52600 -11.59783 20.53683 1.000 36.99128  ? 91  MET A O   1 
ATOM   693  C  CB  . MET A 1 96  ? 30.38178 -10.65474 23.68173 1.000 27.72071  ? 91  MET A CB  1 
ATOM   694  C  CG  . MET A 1 96  ? 29.59959 -9.77604  24.62803 1.000 28.29847  ? 91  MET A CG  1 
ATOM   695  S  SD  . MET A 1 96  ? 28.63200 -8.52572  23.76378 1.000 34.45061  ? 91  MET A SD  1 
ATOM   696  C  CE  . MET A 1 96  ? 29.86137 -7.22676  23.63129 1.000 33.06280  ? 91  MET A CE  1 
ATOM   697  N  N   A ASN A 1 97  ? 30.89054 -13.29829 21.96489 0.500 29.65039  ? 92  ASN A N   1 
ATOM   698  N  N   B ASN A 1 97  ? 30.89390 -13.29546 21.97913 0.500 29.64053  ? 92  ASN A N   1 
ATOM   699  C  CA  A ASN A 1 97  ? 31.73255 -13.99656 20.99633 0.500 34.22047  ? 92  ASN A CA  1 
ATOM   700  C  CA  B ASN A 1 97  ? 31.72362 -14.03370 21.02893 0.500 34.24846  ? 92  ASN A CA  1 
ATOM   701  C  C   A ASN A 1 97  ? 30.92161 -14.53560 19.82667 0.500 36.93893  ? 92  ASN A C   1 
ATOM   702  C  C   B ASN A 1 97  ? 30.91019 -14.50118 19.83196 0.500 36.89464  ? 92  ASN A C   1 
ATOM   703  O  O   A ASN A 1 97  ? 31.42452 -14.58754 18.69597 0.500 37.50027  ? 92  ASN A O   1 
ATOM   704  O  O   B ASN A 1 97  ? 31.39368 -14.47501 18.69178 0.500 37.61282  ? 92  ASN A O   1 
ATOM   705  C  CB  A ASN A 1 97  ? 32.49777 -15.12844 21.67811 0.500 38.20990  ? 92  ASN A CB  1 
ATOM   706  C  CB  B ASN A 1 97  ? 32.38097 -15.22842 21.72185 0.500 37.99637  ? 92  ASN A CB  1 
ATOM   707  C  CG  A ASN A 1 97  ? 33.62569 -14.61920 22.55032 0.500 43.83695  ? 92  ASN A CG  1 
ATOM   708  C  CG  B ASN A 1 97  ? 33.18569 -16.09190 20.76475 0.500 40.92712  ? 92  ASN A CG  1 
ATOM   709  O  OD1 A ASN A 1 97  ? 33.65502 -14.86793 23.75323 0.500 46.43353  ? 92  ASN A OD1 1 
ATOM   710  O  OD1 B ASN A 1 97  ? 34.32261 -15.76799 20.43027 0.500 34.79025  ? 92  ASN A OD1 1 
ATOM   711  N  ND2 A ASN A 1 97  ? 34.56259 -13.89602 21.94434 0.500 42.41103  ? 92  ASN A ND2 1 
ATOM   712  N  ND2 B ASN A 1 97  ? 32.60001 -17.20359 20.32841 0.500 36.78276  ? 92  ASN A ND2 1 
ATOM   713  N  N   . LEU A 1 98  ? 29.67808 -14.95227 20.07253 1.000 32.96759  ? 93  LEU A N   1 
ATOM   714  C  CA  . LEU A 1 98  ? 28.82514 -15.36793 18.96896 1.000 38.97788  ? 93  LEU A CA  1 
ATOM   715  C  C   . LEU A 1 98  ? 28.41585 -14.16887 18.12569 1.000 36.62398  ? 93  LEU A C   1 
ATOM   716  O  O   . LEU A 1 98  ? 28.20121 -14.30708 16.91504 1.000 40.80677  ? 93  LEU A O   1 
ATOM   717  C  CB  . LEU A 1 98  ? 27.60106 -16.11395 19.49895 1.000 38.85605  ? 93  LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 98  ? 27.90169 -17.40698 20.27018 1.000 37.42185  ? 93  LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 98  ? 26.61890 -18.01913 20.80810 1.000 45.51676  ? 93  LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 98  ? 28.68262 -18.42213 19.43751 1.000 40.64894  ? 93  LEU A CD2 1 
ATOM   721  N  N   . SER A 1 99  ? 28.31771 -12.99137 18.74774 1.000 31.25711  ? 94  SER A N   1 
ATOM   722  C  CA  . SER A 1 99  ? 28.16124 -11.74732 18.00189 1.000 36.30203  ? 94  SER A CA  1 
ATOM   723  C  C   . SER A 1 99  ? 29.35111 -11.51685 17.07349 1.000 36.91661  ? 94  SER A C   1 
ATOM   724  O  O   . SER A 1 99  ? 29.18214 -11.31728 15.86311 1.000 33.23507  ? 94  SER A O   1 
ATOM   725  C  CB  . SER A 1 99  ? 27.98411 -10.57638 18.97690 1.000 28.90282  ? 94  SER A CB  1 
ATOM   726  O  OG  . SER A 1 99  ? 28.13911 -9.33477  18.31462 1.000 45.83903  ? 94  SER A OG  1 
ATOM   727  N  N   . ARG A 1 100 ? 30.57143 -11.54639 17.62551 1.000 32.45284  ? 95  ARG A N   1 
ATOM   728  C  CA  . ARG A 1 100 ? 31.76565 -11.40479 16.79338 1.000 35.25386  ? 95  ARG A CA  1 
ATOM   729  C  C   . ARG A 1 100 ? 31.78554 -12.43089 15.67003 1.000 40.97003  ? 95  ARG A C   1 
ATOM   730  O  O   . ARG A 1 100 ? 32.16300 -12.11496 14.53462 1.000 36.20638  ? 95  ARG A O   1 
ATOM   731  C  CB  . ARG A 1 100 ? 33.03253 -11.53931 17.64047 1.000 40.25580  ? 95  ARG A CB  1 
ATOM   732  C  CG  . ARG A 1 100 ? 33.24605 -10.40919 18.62799 1.000 43.32035  ? 95  ARG A CG  1 
ATOM   733  C  CD  . ARG A 1 100 ? 34.57674 -10.53597 19.35265 1.000 46.07594  ? 95  ARG A CD  1 
ATOM   734  N  NE  . ARG A 1 100 ? 34.67360 -9.57557  20.44542 1.000 44.87354  ? 95  ARG A NE  1 
ATOM   735  C  CZ  . ARG A 1 100 ? 35.12199 -8.33565  20.31018 1.000 44.32720  ? 95  ARG A CZ  1 
ATOM   736  N  NH1 . ARG A 1 100 ? 35.54836 -7.87845  19.14243 1.000 35.42872  ? 95  ARG A NH1 1 
ATOM   737  N  NH2 . ARG A 1 100 ? 35.14149 -7.53343  21.37206 1.000 38.83510  ? 95  ARG A NH2 1 
ATOM   738  N  N   . GLU A 1 101 ? 31.38130 -13.66823 15.96580 1.000 32.79709  ? 96  GLU A N   1 
ATOM   739  C  CA  . GLU A 1 101 ? 31.40396 -14.70592 14.94059 1.000 34.18572  ? 96  GLU A CA  1 
ATOM   740  C  C   . GLU A 1 101 ? 30.41964 -14.39400 13.81927 1.000 31.99414  ? 96  GLU A C   1 
ATOM   741  O  O   . GLU A 1 101 ? 30.71148 -14.65278 12.64423 1.000 37.75030  ? 96  GLU A O   1 
ATOM   742  C  CB  . GLU A 1 101 ? 31.10796 -16.07117 15.56641 1.000 35.75841  ? 96  GLU A CB  1 
ATOM   743  C  CG  . GLU A 1 101 ? 31.43660 -17.24866 14.66526 1.000 58.76613  ? 96  GLU A CG  1 
ATOM   744  C  CD  . GLU A 1 101 ? 31.33920 -18.58071 15.38665 1.000 65.98566  ? 96  GLU A CD  1 
ATOM   745  O  OE1 . GLU A 1 101 ? 31.40449 -18.59136 16.63620 1.000 51.34740  ? 96  GLU A OE1 1 
ATOM   746  O  OE2 . GLU A 1 101 ? 31.19648 -19.61632 14.70031 1.000 74.35379  ? 96  GLU A OE2 1 
ATOM   747  N  N   . PHE A 1 102 ? 29.25622 -13.82369 14.15504 1.000 35.49321  ? 97  PHE A N   1 
ATOM   748  C  CA  . PHE A 1 102 ? 28.29422 -13.46633 13.11523 1.000 40.05082  ? 97  PHE A CA  1 
ATOM   749  C  C   . PHE A 1 102 ? 28.83748 -12.37134 12.20660 1.000 37.44663  ? 97  PHE A C   1 
ATOM   750  O  O   . PHE A 1 102 ? 28.82115 -12.50520 10.97889 1.000 38.09052  ? 97  PHE A O   1 
ATOM   751  C  CB  . PHE A 1 102 ? 26.96976 -13.01142 13.71757 1.000 38.26631  ? 97  PHE A CB  1 
ATOM   752  C  CG  . PHE A 1 102 ? 26.05612 -12.37713 12.70627 1.000 38.36144  ? 97  PHE A CG  1 
ATOM   753  C  CD1 . PHE A 1 102 ? 25.41534 -13.15590 11.75782 1.000 46.20804  ? 97  PHE A CD1 1 
ATOM   754  C  CD2 . PHE A 1 102 ? 25.87259 -11.00383 12.67446 1.000 35.86684  ? 97  PHE A CD2 1 
ATOM   755  C  CE1 . PHE A 1 102 ? 24.58695 -12.58316 10.80738 1.000 44.58121  ? 97  PHE A CE1 1 
ATOM   756  C  CE2 . PHE A 1 102 ? 25.04665 -10.42288 11.72692 1.000 38.57862  ? 97  PHE A CE2 1 
ATOM   757  C  CZ  . PHE A 1 102 ? 24.40106 -11.21300 10.79424 1.000 39.04076  ? 97  PHE A CZ  1 
ATOM   758  N  N   . PHE A 1 103 ? 29.30461 -11.26659 12.79157 1.000 34.14442  ? 98  PHE A N   1 
ATOM   759  C  CA  . PHE A 1 103 ? 29.78017 -10.15687 11.96859 1.000 31.12908  ? 98  PHE A CA  1 
ATOM   760  C  C   . PHE A 1 103 ? 31.00378 -10.54114 11.14373 1.000 38.21176  ? 98  PHE A C   1 
ATOM   761  O  O   . PHE A 1 103 ? 31.24188 -9.94917  10.08502 1.000 37.09748  ? 98  PHE A O   1 
ATOM   762  C  CB  . PHE A 1 103 ? 30.08028 -8.94145  12.84274 1.000 29.16201  ? 98  PHE A CB  1 
ATOM   763  C  CG  . PHE A 1 103 ? 28.85624 -8.33467  13.46601 1.000 30.90803  ? 98  PHE A CG  1 
ATOM   764  C  CD1 . PHE A 1 103 ? 27.91118 -7.69261  12.68184 1.000 29.40640  ? 98  PHE A CD1 1 
ATOM   765  C  CD2 . PHE A 1 103 ? 28.64324 -8.41620  14.83042 1.000 25.53220  ? 98  PHE A CD2 1 
ATOM   766  C  CE1 . PHE A 1 103 ? 26.77962 -7.13432  13.24916 1.000 29.46673  ? 98  PHE A CE1 1 
ATOM   767  C  CE2 . PHE A 1 103 ? 27.51329 -7.85738  15.40490 1.000 30.55524  ? 98  PHE A CE2 1 
ATOM   768  C  CZ  . PHE A 1 103 ? 26.57966 -7.21919  14.61079 1.000 29.31732  ? 98  PHE A CZ  1 
ATOM   769  N  N   . ASN A 1 104 ? 31.77596 -11.52997 11.59240 1.000 36.21295  ? 99  ASN A N   1 
ATOM   770  C  CA  . ASN A 1 104 ? 32.92692 -12.01970 10.83558 1.000 38.61058  ? 99  ASN A CA  1 
ATOM   771  C  C   . ASN A 1 104 ? 32.55186 -12.94106 9.68042  1.000 44.07726  ? 99  ASN A C   1 
ATOM   772  O  O   . ASN A 1 104 ? 33.43646 -13.36390 8.92324  1.000 39.98010  ? 99  ASN A O   1 
ATOM   773  C  CB  . ASN A 1 104 ? 33.88679 -12.74240 11.77653 1.000 44.83608  ? 99  ASN A CB  1 
ATOM   774  C  CG  . ASN A 1 104 ? 34.68842 -11.78686 12.62060 1.000 45.09961  ? 99  ASN A CG  1 
ATOM   775  O  OD1 . ASN A 1 104 ? 34.83062 -11.97140 13.82911 1.000 68.88729  ? 99  ASN A OD1 1 
ATOM   776  N  ND2 . ASN A 1 104 ? 35.22659 -10.75295 11.98503 1.000 63.40168  ? 99  ASN A ND2 1 
ATOM   777  N  N   . GLN A 1 105 ? 31.27780 -13.26424 9.51475  1.000 35.49863  ? 100 GLN A N   1 
ATOM   778  C  CA  . GLN A 1 105 ? 30.88552 -14.13838 8.42738  1.000 39.97741  ? 100 GLN A CA  1 
ATOM   779  C  C   . GLN A 1 105 ? 30.96093 -13.39468 7.09441  1.000 42.45743  ? 100 GLN A C   1 
ATOM   780  O  O   . GLN A 1 105 ? 30.95177 -12.16066 7.05965  1.000 40.57226  ? 100 GLN A O   1 
ATOM   781  C  CB  . GLN A 1 105 ? 29.47742 -14.67322 8.66643  1.000 43.80891  ? 100 GLN A CB  1 
ATOM   782  C  CG  . GLN A 1 105 ? 29.38578 -15.56767 9.88678  1.000 50.87752  ? 100 GLN A CG  1 
ATOM   783  C  CD  . GLN A 1 105 ? 28.04159 -16.24723 10.01788 1.000 67.94160  ? 100 GLN A CD  1 
ATOM   784  O  OE1 . GLN A 1 105 ? 27.01961 -15.73023 9.56180  1.000 62.26544  ? 100 GLN A OE1 1 
ATOM   785  N  NE2 . GLN A 1 105 ? 28.03488 -17.41917 10.64199 1.000 73.53771  ? 100 GLN A NE2 1 
ATOM   786  N  N   . PRO A 1 106 ? 31.05563 -14.12873 5.98400  1.000 42.93013  ? 101 PRO A N   1 
ATOM   787  C  CA  . PRO A 1 106 ? 31.06227 -13.48046 4.66807  1.000 41.41428  ? 101 PRO A CA  1 
ATOM   788  C  C   . PRO A 1 106 ? 29.80870 -12.65047 4.44841  1.000 42.30530  ? 101 PRO A C   1 
ATOM   789  O  O   . PRO A 1 106 ? 28.72425 -12.98222 4.93341  1.000 45.34821  ? 101 PRO A O   1 
ATOM   790  C  CB  . PRO A 1 106 ? 31.12295 -14.66127 3.69256  1.000 40.51046  ? 101 PRO A CB  1 
ATOM   791  C  CG  . PRO A 1 106 ? 31.75125 -15.75877 4.47087  1.000 46.46832  ? 101 PRO A CG  1 
ATOM   792  C  CD  . PRO A 1 106 ? 31.27800 -15.58253 5.88089  1.000 45.50239  ? 101 PRO A CD  1 
ATOM   793  N  N   . ILE A 1 107 ? 29.96984 -11.56039 3.69234  1.000 44.35951  ? 102 ILE A N   1 
ATOM   794  C  CA  . ILE A 1 107 ? 28.86389 -10.62727 3.49419  1.000 41.07481  ? 102 ILE A CA  1 
ATOM   795  C  C   . ILE A 1 107 ? 27.70298 -11.31576 2.78676  1.000 45.18505  ? 102 ILE A C   1 
ATOM   796  O  O   . ILE A 1 107 ? 26.53221 -11.03286 3.07065  1.000 50.64833  ? 102 ILE A O   1 
ATOM   797  C  CB  . ILE A 1 107 ? 29.34395 -9.37423  2.73417  1.000 42.12401  ? 102 ILE A CB  1 
ATOM   798  C  CG1 . ILE A 1 107 ? 28.21789 -8.34028  2.64014  1.000 39.39135  ? 102 ILE A CG1 1 
ATOM   799  C  CG2 . ILE A 1 107 ? 29.87210 -9.73277  1.34793  1.000 46.18956  ? 102 ILE A CG2 1 
ATOM   800  C  CD1 . ILE A 1 107 ? 27.74793 -7.82234  3.98092  1.000 39.76974  ? 102 ILE A CD1 1 
ATOM   801  N  N   . GLU A 1 108 ? 28.00726 -12.24600 1.87559  1.000 47.82799  ? 103 GLU A N   1 
ATOM   802  C  CA  . GLU A 1 108 ? 26.96107 -13.00148 1.19327  1.000 49.33611  ? 103 GLU A CA  1 
ATOM   803  C  C   . GLU A 1 108 ? 26.04763 -13.70039 2.19132  1.000 51.71232  ? 103 GLU A C   1 
ATOM   804  O  O   . GLU A 1 108 ? 24.82505 -13.73959 2.00859  1.000 57.60182  ? 103 GLU A O   1 
ATOM   805  C  CB  . GLU A 1 108 ? 27.58538 -14.02415 0.23784  1.000 51.23093  ? 103 GLU A CB  1 
ATOM   806  C  CG  . GLU A 1 108 ? 28.34100 -13.42326 -0.93960 1.000 57.96862  ? 103 GLU A CG  1 
ATOM   807  C  CD  . GLU A 1 108 ? 29.79256 -13.10059 -0.62556 1.000 60.05469  ? 103 GLU A CD  1 
ATOM   808  O  OE1 . GLU A 1 108 ? 30.23101 -13.32815 0.51991  1.000 46.57466  ? 103 GLU A OE1 1 
ATOM   809  O  OE2 . GLU A 1 108 ? 30.50150 -12.62047 -1.53637 1.000 67.63698  ? 103 GLU A OE2 1 
ATOM   810  N  N   . ARG A 1 109 ? 26.62587 -14.24445 3.26295  1.000 49.99824  ? 104 ARG A N   1 
ATOM   811  C  CA  . ARG A 1 109 ? 25.84688 -14.95705 4.26951  1.000 48.03630  ? 104 ARG A CA  1 
ATOM   812  C  C   . ARG A 1 109 ? 25.08834 -13.98955 5.17152  1.000 52.16691  ? 104 ARG A C   1 
ATOM   813  O  O   . ARG A 1 109 ? 23.91058 -14.20472 5.47892  1.000 48.90924  ? 104 ARG A O   1 
ATOM   814  C  CB  . ARG A 1 109 ? 26.77407 -15.84731 5.09639  1.000 50.43055  ? 104 ARG A CB  1 
ATOM   815  C  CG  . ARG A 1 109 ? 26.07519 -16.92938 5.89091  1.000 70.77592  ? 104 ARG A CG  1 
ATOM   816  C  CD  . ARG A 1 109 ? 27.06611 -17.67287 6.77318  1.000 77.55535  ? 104 ARG A CD  1 
ATOM   817  N  NE  . ARG A 1 109 ? 26.44407 -18.79143 7.47088  1.000 91.79954  ? 104 ARG A NE  1 
ATOM   818  C  CZ  . ARG A 1 109 ? 26.42321 -20.03708 7.01712  1.000 81.61622  ? 104 ARG A CZ  1 
ATOM   819  N  NH1 . ARG A 1 109 ? 26.99010 -20.36343 5.86708  1.000 75.72185  ? 104 ARG A NH1 1 
ATOM   820  N  NH2 . ARG A 1 109 ? 25.81794 -20.97857 7.73488  1.000 80.78814  ? 104 ARG A NH2 1 
ATOM   821  N  N   . LYS A 1 110 ? 25.75225 -12.91757 5.60720  1.000 43.00177  ? 105 LYS A N   1 
ATOM   822  C  CA  . LYS A 1 110 ? 25.10310 -11.95906 6.49281  1.000 41.24876  ? 105 LYS A CA  1 
ATOM   823  C  C   . LYS A 1 110 ? 23.92041 -11.28589 5.80869  1.000 39.64899  ? 105 LYS A C   1 
ATOM   824  O  O   . LYS A 1 110 ? 22.88318 -11.04932 6.43892  1.000 44.17154  ? 105 LYS A O   1 
ATOM   825  C  CB  . LYS A 1 110 ? 26.11553 -10.91794 6.96750  1.000 42.87308  ? 105 LYS A CB  1 
ATOM   826  C  CG  . LYS A 1 110 ? 27.19015 -11.47086 7.88624  1.000 37.27675  ? 105 LYS A CG  1 
ATOM   827  C  CD  . LYS A 1 110 ? 27.98807 -10.34923 8.53984  1.000 35.33603  ? 105 LYS A CD  1 
ATOM   828  C  CE  . LYS A 1 110 ? 28.81964 -9.57998  7.50915  1.000 34.94133  ? 105 LYS A CE  1 
ATOM   829  N  NZ  . LYS A 1 110 ? 29.59902 -8.49359  8.18086  1.000 41.67625  ? 105 LYS A NZ  1 
ATOM   830  N  N   . GLN A 1 111 ? 24.04348 -10.99364 4.51223  1.000 45.86169  ? 106 GLN A N   1 
ATOM   831  C  CA  . GLN A 1 111 ? 23.00107 -10.23805 3.82802  1.000 49.80014  ? 106 GLN A CA  1 
ATOM   832  C  C   . GLN A 1 111 ? 21.70160 -11.01635 3.67718  1.000 49.43218  ? 106 GLN A C   1 
ATOM   833  O  O   . GLN A 1 111 ? 20.68110 -10.41234 3.33022  1.000 44.44468  ? 106 GLN A O   1 
ATOM   834  C  CB  . GLN A 1 111 ? 23.49617 -9.77351  2.45742  1.000 53.20081  ? 106 GLN A CB  1 
ATOM   835  C  CG  . GLN A 1 111 ? 24.53669 -8.65677  2.51507  1.000 45.41001  ? 106 GLN A CG  1 
ATOM   836  C  CD  . GLN A 1 111 ? 23.94569 -7.28996  2.83485  1.000 61.50464  ? 106 GLN A CD  1 
ATOM   837  O  OE1 . GLN A 1 111 ? 23.28530 -7.10133  3.85958  1.000 57.63587  ? 106 GLN A OE1 1 
ATOM   838  N  NE2 . GLN A 1 111 ? 24.18933 -6.32511  1.95406  1.000 58.29199  ? 106 GLN A NE2 1 
ATOM   839  N  N   . LYS A 1 112 ? 21.70534 -12.32784 3.93122  1.000 45.75060  ? 107 LYS A N   1 
ATOM   840  C  CA  . LYS A 1 112 ? 20.45005 -13.06692 3.98982  1.000 43.83481  ? 107 LYS A CA  1 
ATOM   841  C  C   . LYS A 1 112 ? 19.57107 -12.59949 5.13694  1.000 44.36103  ? 107 LYS A C   1 
ATOM   842  O  O   . LYS A 1 112 ? 18.38001 -12.92656 5.16078  1.000 46.47447  ? 107 LYS A O   1 
ATOM   843  C  CB  . LYS A 1 112 ? 20.71886 -14.56569 4.12804  1.000 46.28946  ? 107 LYS A CB  1 
ATOM   844  C  CG  . LYS A 1 112 ? 21.58199 -15.14416 3.01631  1.000 49.93625  ? 107 LYS A CG  1 
ATOM   845  C  CD  . LYS A 1 112 ? 21.84073 -16.63014 3.22496  1.000 75.07813  ? 107 LYS A CD  1 
ATOM   846  C  CE  . LYS A 1 112 ? 22.54420 -16.89257 4.54819  1.000 65.73843  ? 107 LYS A CE  1 
ATOM   847  N  NZ  . LYS A 1 112 ? 23.05782 -18.28709 4.63867  1.000 84.57142  ? 107 LYS A NZ  1 
ATOM   848  N  N   . PHE A 1 113 ? 20.13190 -11.84793 6.08054  1.000 40.98288  ? 108 PHE A N   1 
ATOM   849  C  CA  . PHE A 1 113 ? 19.39949 -11.30402 7.21414  1.000 39.28580  ? 108 PHE A CA  1 
ATOM   850  C  C   . PHE A 1 113 ? 19.22919 -9.79464  7.11378  1.000 40.08298  ? 108 PHE A C   1 
ATOM   851  O  O   . PHE A 1 113 ? 18.85407 -9.15764  8.10044  1.000 38.70233  ? 108 PHE A O   1 
ATOM   852  C  CB  . PHE A 1 113 ? 20.10902 -11.67709 8.51692  1.000 40.42931  ? 108 PHE A CB  1 
ATOM   853  C  CG  . PHE A 1 113 ? 20.40662 -13.14345 8.63673  1.000 43.80661  ? 108 PHE A CG  1 
ATOM   854  C  CD1 . PHE A 1 113 ? 19.41357 -14.03740 9.00338  1.000 48.86507  ? 108 PHE A CD1 1 
ATOM   855  C  CD2 . PHE A 1 113 ? 21.67539 -13.63232 8.36907  1.000 39.06109  ? 108 PHE A CD2 1 
ATOM   856  C  CE1 . PHE A 1 113 ? 19.68218 -15.39367 9.10502  1.000 46.27764  ? 108 PHE A CE1 1 
ATOM   857  C  CE2 . PHE A 1 113 ? 21.95052 -14.98473 8.47177  1.000 45.52287  ? 108 PHE A CE2 1 
ATOM   858  C  CZ  . PHE A 1 113 ? 20.95197 -15.86642 8.84078  1.000 41.73455  ? 108 PHE A CZ  1 
ATOM   859  N  N   . SER A 1 114 ? 19.49311 -9.21632  5.94084  1.000 42.44296  ? 109 SER A N   1 
ATOM   860  C  CA  . SER A 1 114 ? 19.37364 -7.77819  5.74201  1.000 41.94211  ? 109 SER A CA  1 
ATOM   861  C  C   . SER A 1 114 ? 17.98887 -7.28132  6.13396  1.000 36.19798  ? 109 SER A C   1 
ATOM   862  O  O   . SER A 1 114 ? 16.97954 -7.94122  5.87564  1.000 44.32954  ? 109 SER A O   1 
ATOM   863  C  CB  . SER A 1 114 ? 19.65144 -7.43270  4.27608  1.000 43.53064  ? 109 SER A CB  1 
ATOM   864  O  OG  . SER A 1 114 ? 19.37607 -6.06488  4.02048  1.000 46.42227  ? 109 SER A OG  1 
ATOM   865  N  N   . ASN A 1 115 ? 17.94357 -6.10943  6.76508  1.000 35.93115  ? 110 ASN A N   1 
ATOM   866  C  CA  . ASN A 1 115 ? 16.67359 -5.47768  7.09273  1.000 38.26603  ? 110 ASN A CA  1 
ATOM   867  C  C   . ASN A 1 115 ? 16.13293 -4.64279  5.94075  1.000 47.82218  ? 110 ASN A C   1 
ATOM   868  O  O   . ASN A 1 115 ? 15.11559 -3.96195  6.10265  1.000 46.27385  ? 110 ASN A O   1 
ATOM   869  C  CB  . ASN A 1 115 ? 16.80579 -4.62298  8.35841  1.000 36.72553  ? 110 ASN A CB  1 
ATOM   870  C  CG  . ASN A 1 115 ? 17.67151 -3.39810  8.15517  1.000 38.96012  ? 110 ASN A CG  1 
ATOM   871  O  OD1 . ASN A 1 115 ? 18.55674 -3.38121  7.30065  1.000 40.41462  ? 110 ASN A OD1 1 
ATOM   872  N  ND2 . ASN A 1 115 ? 17.42427 -2.36346  8.95396  1.000 37.67448  ? 110 ASN A ND2 1 
ATOM   873  N  N   . LEU A 1 116 ? 16.78776 -4.68451  4.78270  1.000 41.93801  ? 111 LEU A N   1 
ATOM   874  C  CA  . LEU A 1 116 ? 16.28869 -4.04129  3.57079  1.000 43.34324  ? 111 LEU A CA  1 
ATOM   875  C  C   . LEU A 1 116 ? 15.63615 -5.13512  2.73255  1.000 49.59087  ? 111 LEU A C   1 
ATOM   876  O  O   . LEU A 1 116 ? 16.29771 -5.84092  1.96962  1.000 49.41552  ? 111 LEU A O   1 
ATOM   877  C  CB  . LEU A 1 116 ? 17.41273 -3.33127  2.82738  1.000 53.64413  ? 111 LEU A CB  1 
ATOM   878  C  CG  . LEU A 1 116 ? 17.99064 -2.11393  3.54981  1.000 48.77514  ? 111 LEU A CG  1 
ATOM   879  C  CD1 . LEU A 1 116 ? 19.28945 -1.66724  2.89190  1.000 60.84423  ? 111 LEU A CD1 1 
ATOM   880  C  CD2 . LEU A 1 116 ? 16.97603 -0.98182  3.56171  1.000 50.72659  ? 111 LEU A CD2 1 
ATOM   881  N  N   . ILE A 1 117 ? 14.31944 -5.28056  2.89698  1.000 52.38192  ? 112 ILE A N   1 
ATOM   882  C  CA  . ILE A 1 117 ? 13.58579 -6.32417  2.19422  1.000 57.01263  ? 112 ILE A CA  1 
ATOM   883  C  C   . ILE A 1 117 ? 13.65958 -6.07451  0.69710  1.000 62.33656  ? 112 ILE A C   1 
ATOM   884  O  O   . ILE A 1 117 ? 13.47370 -4.94449  0.22714  1.000 63.51290  ? 112 ILE A O   1 
ATOM   885  C  CB  . ILE A 1 117 ? 12.13326 -6.37356  2.68699  1.000 57.22284  ? 112 ILE A CB  1 
ATOM   886  C  CG1 . ILE A 1 117 ? 12.09834 -6.41790  4.21465  1.000 58.03936  ? 112 ILE A CG1 1 
ATOM   887  C  CG2 . ILE A 1 117 ? 11.41526 -7.58051  2.10213  1.000 55.78589  ? 112 ILE A CG2 1 
ATOM   888  C  CD1 . ILE A 1 117 ? 10.71783 -6.23179  4.79526  1.000 78.37061  ? 112 ILE A CD1 1 
ATOM   889  N  N   . ASP A 1 118 ? 13.94776 -7.13085  -0.05961 1.000 65.67392  ? 113 ASP A N   1 
ATOM   890  C  CA  . ASP A 1 118 ? 14.13764 -7.07343  -1.50543 1.000 63.66391  ? 113 ASP A CA  1 
ATOM   891  C  C   . ASP A 1 118 ? 15.26301 -6.12800  -1.90985 1.000 67.28258  ? 113 ASP A C   1 
ATOM   892  O  O   . ASP A 1 118 ? 15.38212 -5.78179  -3.09137 1.000 69.66890  ? 113 ASP A O   1 
ATOM   893  C  CB  . ASP A 1 118 ? 12.83896 -6.68020  -2.22336 1.000 72.15486  ? 113 ASP A CB  1 
ATOM   894  C  CG  . ASP A 1 118 ? 11.66830 -7.56573  -1.83794 1.000 74.81751  ? 113 ASP A CG  1 
ATOM   895  O  OD1 . ASP A 1 118 ? 11.85612 -8.79715  -1.73930 1.000 67.83400  ? 113 ASP A OD1 1 
ATOM   896  O  OD2 . ASP A 1 118 ? 10.56093 -7.02750  -1.62745 1.000 77.54696  ? 113 ASP A OD2 1 
ATOM   897  N  N   . GLY A 1 119 ? 16.09562 -5.70676  -0.96115 1.000 60.33496  ? 114 GLY A N   1 
ATOM   898  C  CA  . GLY A 1 119 ? 17.17028 -4.77882  -1.23232 1.000 56.73057  ? 114 GLY A CA  1 
ATOM   899  C  C   . GLY A 1 119 ? 16.79812 -3.31629  -1.15288 1.000 66.25085  ? 114 GLY A C   1 
ATOM   900  O  O   . GLY A 1 119 ? 17.63176 -2.46739  -1.49119 1.000 66.83413  ? 114 GLY A O   1 
ATOM   901  N  N   . LYS A 1 120 ? 15.58434 -2.98779  -0.70536 1.000 64.18264  ? 115 LYS A N   1 
ATOM   902  C  CA  . LYS A 1 120 ? 15.12382 -1.60530  -0.76600 1.000 64.88744  ? 115 LYS A CA  1 
ATOM   903  C  C   . LYS A 1 120 ? 14.16932 -1.23080  0.36458  1.000 62.50125  ? 115 LYS A C   1 
ATOM   904  O  O   . LYS A 1 120 ? 14.19114 -0.09107  0.84019  1.000 72.26388  ? 115 LYS A O   1 
ATOM   905  C  CB  . LYS A 1 120 ? 14.44824 -1.34474  -2.11567 1.000 67.60183  ? 115 LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 120 ? 13.28212 -2.28006  -2.41849 1.000 71.22138  ? 115 LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 120 ? 12.73281 -2.06383  -3.82052 1.000 80.45745  ? 115 LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 120 ? 13.78317 -2.36599  -4.87442 1.000 76.12031  ? 115 LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 120 ? 13.23853 -2.24142  -6.25332 1.000 89.94146  ? 115 LYS A NZ  1 
ATOM   910  N  N   . ASN A 1 121 ? 13.33023 -2.16790  0.80350  1.000 63.44322  ? 116 ASN A N   1 
ATOM   911  C  CA  . ASN A 1 121 ? 12.21816 -1.86065  1.70110  1.000 59.10061  ? 116 ASN A CA  1 
ATOM   912  C  C   . ASN A 1 121 ? 12.66870 -2.00549  3.15123  1.000 55.13544  ? 116 ASN A C   1 
ATOM   913  O  O   . ASN A 1 121 ? 12.90159 -3.12043  3.62885  1.000 50.96956  ? 116 ASN A O   1 
ATOM   914  C  CB  . ASN A 1 121 ? 11.03025 -2.76767  1.39425  1.000 66.90716  ? 116 ASN A CB  1 
ATOM   915  C  CG  . ASN A 1 121 ? 10.51059 -2.57908  -0.01769 1.000 75.81051  ? 116 ASN A CG  1 
ATOM   916  O  OD1 . ASN A 1 121 ? 10.49207 -1.46235  -0.53605 1.000 72.03089  ? 116 ASN A OD1 1 
ATOM   917  N  ND2 . ASN A 1 121 ? 10.09562 -3.67226  -0.65211 1.000 66.46799  ? 116 ASN A ND2 1 
ATOM   918  N  N   . PHE A 1 122 ? 12.76161 -0.87972  3.85785  1.000 58.25989  ? 117 PHE A N   1 
ATOM   919  C  CA  . PHE A 1 122 ? 13.30637 -0.88277  5.20878  1.000 53.28373  ? 117 PHE A CA  1 
ATOM   920  C  C   . PHE A 1 122 ? 12.32702 -1.47476  6.21347  1.000 47.50085  ? 117 PHE A C   1 
ATOM   921  O  O   . PHE A 1 122 ? 11.12579 -1.18996  6.18723  1.000 51.69349  ? 117 PHE A O   1 
ATOM   922  C  CB  . PHE A 1 122 ? 13.67801 0.53576   5.65373  1.000 45.96645  ? 117 PHE A CB  1 
ATOM   923  C  CG  . PHE A 1 122 ? 14.06138 0.62782   7.11245  1.000 44.55949  ? 117 PHE A CG  1 
ATOM   924  C  CD1 . PHE A 1 122 ? 15.37338 0.42467   7.51053  1.000 46.22635  ? 117 PHE A CD1 1 
ATOM   925  C  CD2 . PHE A 1 122 ? 13.10948 0.90584   8.08584  1.000 41.31417  ? 117 PHE A CD2 1 
ATOM   926  C  CE1 . PHE A 1 122 ? 15.72898 0.49820   8.84650  1.000 39.00397  ? 117 PHE A CE1 1 
ATOM   927  C  CE2 . PHE A 1 122 ? 13.45853 0.97153   9.42174  1.000 40.57302  ? 117 PHE A CE2 1 
ATOM   928  C  CZ  . PHE A 1 122 ? 14.77020 0.77066   9.80314  1.000 36.68504  ? 117 PHE A CZ  1 
ATOM   929  N  N   . GLN A 1 123 ? 12.86432 -2.29134  7.11589  1.000 45.92468  ? 118 GLN A N   1 
ATOM   930  C  CA  . GLN A 1 123 ? 12.21819 -2.62714  8.37392  1.000 42.11817  ? 118 GLN A CA  1 
ATOM   931  C  C   . GLN A 1 123 ? 13.28419 -2.58316  9.45692  1.000 38.09093  ? 118 GLN A C   1 
ATOM   932  O  O   . GLN A 1 123 ? 14.48387 -2.59866  9.17075  1.000 38.77399  ? 118 GLN A O   1 
ATOM   933  C  CB  . GLN A 1 123 ? 11.54624 -4.00441  8.33618  1.000 44.35917  ? 118 GLN A CB  1 
ATOM   934  C  CG  . GLN A 1 123 ? 12.52529 -5.16014  8.23088  1.000 47.28885  ? 118 GLN A CG  1 
ATOM   935  C  CD  . GLN A 1 123 ? 11.85045 -6.50573  8.38662  1.000 55.74171  ? 118 GLN A CD  1 
ATOM   936  O  OE1 . GLN A 1 123 ? 10.69783 -6.68340  7.99510  1.000 60.01709  ? 118 GLN A OE1 1 
ATOM   937  N  NE2 . GLN A 1 123 ? 12.56280 -7.45982  8.97307  1.000 49.11532  ? 118 GLN A NE2 1 
ATOM   938  N  N   . ILE A 1 124 ? 12.84091 -2.51889  10.71136 1.000 41.61695  ? 119 ILE A N   1 
ATOM   939  C  CA  . ILE A 1 124 ? 13.79083 -2.43429  11.81679 1.000 37.63781  ? 119 ILE A CA  1 
ATOM   940  C  C   . ILE A 1 124 ? 14.57853 -3.73310  11.94557 1.000 36.82988  ? 119 ILE A C   1 
ATOM   941  O  O   . ILE A 1 124 ? 15.81291 -3.72699  12.02587 1.000 35.33661  ? 119 ILE A O   1 
ATOM   942  C  CB  . ILE A 1 124 ? 13.06291 -2.08260  13.12629 1.000 35.62197  ? 119 ILE A CB  1 
ATOM   943  C  CG1 . ILE A 1 124 ? 12.44208 -0.68576  13.02919 1.000 37.26489  ? 119 ILE A CG1 1 
ATOM   944  C  CG2 . ILE A 1 124 ? 14.02351 -2.14347  14.29193 1.000 34.72016  ? 119 ILE A CG2 1 
ATOM   945  C  CD1 . ILE A 1 124 ? 11.63438 -0.27544  14.24970 1.000 37.66606  ? 119 ILE A CD1 1 
ATOM   946  N  N   . GLN A 1 125 ? 13.87938 -4.86330  11.94266 1.000 34.46261  ? 120 GLN A N   1 
ATOM   947  C  CA  . GLN A 1 125 ? 14.50034 -6.13465  12.28733 1.000 37.71862  ? 120 GLN A CA  1 
ATOM   948  C  C   . GLN A 1 125 ? 15.43692 -6.60945  11.18715 1.000 38.92738  ? 120 GLN A C   1 
ATOM   949  O  O   . GLN A 1 125 ? 15.05044 -6.68784  10.01714 1.000 41.13039  ? 120 GLN A O   1 
ATOM   950  C  CB  . GLN A 1 125 ? 13.42722 -7.18668  12.54725 1.000 39.23600  ? 120 GLN A CB  1 
ATOM   951  C  CG  . GLN A 1 125 ? 13.97969 -8.56009  12.86655 1.000 45.11742  ? 120 GLN A CG  1 
ATOM   952  C  CD  . GLN A 1 125 ? 13.07054 -9.33833  13.78970 1.000 46.96848  ? 120 GLN A CD  1 
ATOM   953  O  OE1 . GLN A 1 125 ? 13.37102 -9.51339  14.97023 1.000 36.63691  ? 120 GLN A OE1 1 
ATOM   954  N  NE2 . GLN A 1 125 ? 11.94360 -9.80096  13.25909 1.000 40.70600  ? 120 GLN A NE2 1 
ATOM   955  N  N   . GLY A 1 126 ? 16.66971 -6.94260  11.56857 1.000 34.64288  ? 121 GLY A N   1 
ATOM   956  C  CA  . GLY A 1 126 ? 17.62107 -7.51331  10.64634 1.000 36.71654  ? 121 GLY A CA  1 
ATOM   957  C  C   . GLY A 1 126 ? 18.95165 -6.79895  10.71440 1.000 35.09947  ? 121 GLY A C   1 
ATOM   958  O  O   . GLY A 1 126 ? 19.22741 -6.03810  11.64924 1.000 31.01948  ? 121 GLY A O   1 
ATOM   959  N  N   . TYR A 1 127 ? 19.76727 -7.04322  9.69184  1.000 35.93693  ? 122 TYR A N   1 
ATOM   960  C  CA  . TYR A 1 127 ? 21.15158 -6.58928  9.61827  1.000 40.69051  ? 122 TYR A CA  1 
ATOM   961  C  C   . TYR A 1 127 ? 21.25207 -5.43327  8.62948  1.000 32.80277  ? 122 TYR A C   1 
ATOM   962  O  O   . TYR A 1 127 ? 20.85602 -5.56751  7.46646  1.000 35.72530  ? 122 TYR A O   1 
ATOM   963  C  CB  . TYR A 1 127 ? 22.05924 -7.74582  9.19114  1.000 38.71541  ? 122 TYR A CB  1 
ATOM   964  C  CG  . TYR A 1 127 ? 23.52345 -7.40348  9.01919  1.000 35.27210  ? 122 TYR A CG  1 
ATOM   965  C  CD1 . TYR A 1 127 ? 24.24707 -6.80110  10.04070 1.000 34.53206  ? 122 TYR A CD1 1 
ATOM   966  C  CD2 . TYR A 1 127 ? 24.18697 -7.71178  7.84206  1.000 39.11480  ? 122 TYR A CD2 1 
ATOM   967  C  CE1 . TYR A 1 127 ? 25.59357 -6.50320  9.88176  1.000 34.72890  ? 122 TYR A CE1 1 
ATOM   968  C  CE2 . TYR A 1 127 ? 25.52312 -7.42114  7.67583  1.000 39.39964  ? 122 TYR A CE2 1 
ATOM   969  C  CZ  . TYR A 1 127 ? 26.22183 -6.81712  8.69550  1.000 35.75634  ? 122 TYR A CZ  1 
ATOM   970  O  OH  . TYR A 1 127 ? 27.55864 -6.53568  8.51410  1.000 36.24428  ? 122 TYR A OH  1 
ATOM   971  N  N   . GLY A 1 128 ? 21.79159 -4.31128  9.08899  1.000 31.15865  ? 123 GLY A N   1 
ATOM   972  C  CA  . GLY A 1 128 ? 21.91010 -3.12484  8.26522  1.000 34.38474  ? 123 GLY A CA  1 
ATOM   973  C  C   . GLY A 1 128 ? 22.13020 -1.92343  9.15434  1.000 31.65129  ? 123 GLY A C   1 
ATOM   974  O  O   . GLY A 1 128 ? 22.94110 -1.98417  10.08276 1.000 30.43004  ? 123 GLY A O   1 
ATOM   975  N  N   . THR A 1 129 ? 21.41220 -0.83226  8.90312  1.000 29.61505  ? 124 THR A N   1 
ATOM   976  C  CA  . THR A 1 129 ? 21.43649 0.30308   9.81193  1.000 32.92881  ? 124 THR A CA  1 
ATOM   977  C  C   . THR A 1 129 ? 20.00722 0.81290   9.97278  1.000 31.34030  ? 124 THR A C   1 
ATOM   978  O  O   . THR A 1 129 ? 19.04256 0.18590   9.52285  1.000 34.75530  ? 124 THR A O   1 
ATOM   979  C  CB  . THR A 1 129 ? 22.40769 1.38333   9.31299  1.000 34.34794  ? 124 THR A CB  1 
ATOM   980  O  OG1 . THR A 1 129 ? 22.52073 2.41971   10.29735 1.000 29.83432  ? 124 THR A OG1 1 
ATOM   981  C  CG2 . THR A 1 129 ? 21.93927 1.97210   7.99118  1.000 32.56268  ? 124 THR A CG2 1 
ATOM   982  N  N   . ASP A 1 130 ? 19.86903 1.96090   10.61982 1.000 31.45544  ? 125 ASP A N   1 
ATOM   983  C  CA  . ASP A 1 130 ? 18.55405 2.50237   10.90923 1.000 30.33443  ? 125 ASP A CA  1 
ATOM   984  C  C   . ASP A 1 130 ? 17.99506 3.21829   9.68252  1.000 34.67102  ? 125 ASP A C   1 
ATOM   985  O  O   . ASP A 1 130 ? 18.69478 3.44557   8.69132  1.000 33.49108  ? 125 ASP A O   1 
ATOM   986  C  CB  . ASP A 1 130 ? 18.64466 3.41826   12.11986 1.000 29.23949  ? 125 ASP A CB  1 
ATOM   987  C  CG  . ASP A 1 130 ? 19.33355 2.73859   13.28869 1.000 35.18339  ? 125 ASP A CG  1 
ATOM   988  O  OD1 . ASP A 1 130 ? 18.78966 1.72835   13.78682 1.000 30.64904  ? 125 ASP A OD1 1 
ATOM   989  O  OD2 . ASP A 1 130 ? 20.43855 3.17643   13.67888 1.000 30.22847  ? 125 ASP A OD2 1 
ATOM   990  N  N   . ARG A 1 131 ? 16.71177 3.57221   9.75270  1.000 34.64729  ? 126 ARG A N   1 
ATOM   991  C  CA  . ARG A 1 131 ? 16.00776 4.03258   8.56041  1.000 35.41591  ? 126 ARG A CA  1 
ATOM   992  C  C   . ARG A 1 131 ? 16.64007 5.29910   7.99670  1.000 37.04293  ? 126 ARG A C   1 
ATOM   993  O  O   . ARG A 1 131 ? 16.99171 6.22464   8.73431  1.000 35.24842  ? 126 ARG A O   1 
ATOM   994  C  CB  . ARG A 1 131 ? 14.53155 4.28930   8.86805  1.000 35.87770  ? 126 ARG A CB  1 
ATOM   995  C  CG  . ARG A 1 131 ? 13.69184 4.54950   7.62108  1.000 44.25579  ? 126 ARG A CG  1 
ATOM   996  C  CD  . ARG A 1 131 ? 12.30312 5.06638   7.96153  1.000 51.42567  ? 126 ARG A CD  1 
ATOM   997  N  NE  . ARG A 1 131 ? 11.49766 4.08038   8.67289  1.000 48.89365  ? 126 ARG A NE  1 
ATOM   998  C  CZ  . ARG A 1 131 ? 10.63355 3.25800   8.09375  1.000 46.31161  ? 126 ARG A CZ  1 
ATOM   999  N  NH1 . ARG A 1 131 ? 10.44916 3.25837   6.78416  1.000 42.86725  ? 126 ARG A NH1 1 
ATOM   1000 N  NH2 . ARG A 1 131 ? 9.93419  2.41589   8.84873  1.000 50.37309  ? 126 ARG A NH2 1 
ATOM   1001 N  N   . VAL A 1 132 ? 16.78725 5.33108   6.67724  1.000 40.04112  ? 127 VAL A N   1 
ATOM   1002 C  CA  . VAL A 1 132 ? 17.23311 6.52123   5.96574  1.000 41.52042  ? 127 VAL A CA  1 
ATOM   1003 C  C   . VAL A 1 132 ? 15.99289 7.22141   5.43040  1.000 41.53474  ? 127 VAL A C   1 
ATOM   1004 O  O   . VAL A 1 132 ? 15.35096 6.73963   4.49052  1.000 42.65814  ? 127 VAL A O   1 
ATOM   1005 C  CB  . VAL A 1 132 ? 18.20987 6.18089   4.83673  1.000 37.66675  ? 127 VAL A CB  1 
ATOM   1006 C  CG1 . VAL A 1 132 ? 18.59059 7.44947   4.10878  1.000 43.47542  ? 127 VAL A CG1 1 
ATOM   1007 C  CG2 . VAL A 1 132 ? 19.43893 5.47647   5.39325  1.000 46.96284  ? 127 VAL A CG2 1 
ATOM   1008 N  N   . VAL A 1 133 ? 15.65425 8.36170   6.02268  1.000 39.81704  ? 128 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 133 ? 14.42227 9.05338   5.66199  1.000 43.25277  ? 128 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 133 ? 14.64779 10.04699  4.53221  1.000 40.95394  ? 128 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 133 ? 13.80938 10.17233  3.63713  1.000 47.80383  ? 128 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 133 ? 13.82630 9.73986   6.90461  1.000 42.88161  ? 128 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 133 ? 12.47906 10.35849  6.57365  1.000 51.12076  ? 128 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 133 ? 13.69476 8.73922   8.04290  1.000 45.00220  ? 128 VAL A CG2 1 
ATOM   1015 N  N   . THR A 1 134 ? 15.76570 10.76901  4.55319  1.000 47.99097  ? 129 THR A N   1 
ATOM   1016 C  CA  . THR A 1 134 ? 16.04516 11.79464  3.55856  1.000 48.63095  ? 129 THR A CA  1 
ATOM   1017 C  C   . THR A 1 134 ? 17.41110 11.55008  2.93253  1.000 49.39181  ? 129 THR A C   1 
ATOM   1018 O  O   . THR A 1 134 ? 18.28397 10.90705  3.52120  1.000 48.89958  ? 129 THR A O   1 
ATOM   1019 C  CB  . THR A 1 134 ? 15.99652 13.20541  4.16849  1.000 51.25622  ? 129 THR A CB  1 
ATOM   1020 O  OG1 . THR A 1 134 ? 17.01211 13.33233  5.17093  1.000 48.30270  ? 129 THR A OG1 1 
ATOM   1021 C  CG2 . THR A 1 134 ? 14.64000 13.46983  4.80234  1.000 48.50086  ? 129 THR A CG2 1 
ATOM   1022 N  N   . GLN A 1 135 ? 17.59056 12.08167  1.72044  1.000 48.68252  ? 130 GLN A N   1 
ATOM   1023 C  CA  . GLN A 1 135 ? 18.86726 11.91669  1.03424  1.000 51.73373  ? 130 GLN A CA  1 
ATOM   1024 C  C   . GLN A 1 135 ? 19.98457 12.67503  1.74177  1.000 45.03565  ? 130 GLN A C   1 
ATOM   1025 O  O   . GLN A 1 135 ? 21.14809 12.26371  1.67424  1.000 54.37492  ? 130 GLN A O   1 
ATOM   1026 C  CB  . GLN A 1 135 ? 18.74379 12.36970  -0.42169 1.000 52.85816  ? 130 GLN A CB  1 
ATOM   1027 C  CG  . GLN A 1 135 ? 19.85744 11.87082  -1.33021 1.000 56.98167  ? 130 GLN A CG  1 
ATOM   1028 C  CD  . GLN A 1 135 ? 19.67510 12.30841  -2.77373 1.000 65.20328  ? 130 GLN A CD  1 
ATOM   1029 O  OE1 . GLN A 1 135 ? 18.80388 13.12295  -3.08168 1.000 66.44291  ? 130 GLN A OE1 1 
ATOM   1030 N  NE2 . GLN A 1 135 ? 20.49620 11.76478  -3.66720 1.000 62.09535  ? 130 GLN A NE2 1 
ATOM   1031 N  N   . ASP A 1 136 ? 19.65660 13.76671  2.43103  1.000 53.31660  ? 131 ASP A N   1 
ATOM   1032 C  CA  . ASP A 1 136 ? 20.64343 14.55553  3.15738  1.000 56.80166  ? 131 ASP A CA  1 
ATOM   1033 C  C   . ASP A 1 136 ? 20.82768 14.08825  4.59788  1.000 54.22315  ? 131 ASP A C   1 
ATOM   1034 O  O   . ASP A 1 136 ? 21.42027 14.81272  5.40485  1.000 54.94673  ? 131 ASP A O   1 
ATOM   1035 C  CB  . ASP A 1 136 ? 20.26285 16.04241  3.12671  1.000 58.36328  ? 131 ASP A CB  1 
ATOM   1036 C  CG  . ASP A 1 136 ? 19.10003 16.37842  4.04799  1.000 69.10455  ? 131 ASP A CG  1 
ATOM   1037 O  OD1 . ASP A 1 136 ? 18.27485 15.48614  4.33505  1.000 68.78372  ? 131 ASP A OD1 1 
ATOM   1038 O  OD2 . ASP A 1 136 ? 19.00894 17.54716  4.48267  1.000 70.04091  ? 131 ASP A OD2 1 
ATOM   1039 N  N   . GLN A 1 137 ? 20.33616 12.90127  4.93782  1.000 47.37847  ? 132 GLN A N   1 
ATOM   1040 C  CA  . GLN A 1 137 ? 20.46853 12.40558  6.29841  1.000 47.90815  ? 132 GLN A CA  1 
ATOM   1041 C  C   . GLN A 1 137 ? 21.89445 11.93948  6.55853  1.000 38.39739  ? 132 GLN A C   1 
ATOM   1042 O  O   . GLN A 1 137 ? 22.52755 11.31464  5.70304  1.000 42.41569  ? 132 GLN A O   1 
ATOM   1043 C  CB  . GLN A 1 137 ? 19.48329 11.26284  6.53903  1.000 43.87164  ? 132 GLN A CB  1 
ATOM   1044 C  CG  . GLN A 1 137 ? 19.53039 10.65413  7.93128  1.000 42.85650  ? 132 GLN A CG  1 
ATOM   1045 C  CD  . GLN A 1 137 ? 18.47742 9.58304   8.10731  1.000 39.79277  ? 132 GLN A CD  1 
ATOM   1046 O  OE1 . GLN A 1 137 ? 17.32662 9.76449   7.70770  1.000 40.98593  ? 132 GLN A OE1 1 
ATOM   1047 N  NE2 . GLN A 1 137 ? 18.86783 8.45110   8.68474  1.000 37.99694  ? 132 GLN A NE2 1 
ATOM   1048 N  N   . ILE A 1 138 ? 22.40156 12.25570  7.74541  1.000 42.50891  ? 133 ILE A N   1 
ATOM   1049 C  CA  . ILE A 1 138 ? 23.71194 11.77651  8.16224  1.000 41.01086  ? 133 ILE A CA  1 
ATOM   1050 C  C   . ILE A 1 138 ? 23.59264 10.31520  8.57245  1.000 38.70792  ? 133 ILE A C   1 
ATOM   1051 O  O   . ILE A 1 138 ? 22.64009 9.91988   9.25355  1.000 37.02801  ? 133 ILE A O   1 
ATOM   1052 C  CB  . ILE A 1 138 ? 24.26647 12.63095  9.31594  1.000 47.21374  ? 133 ILE A CB  1 
ATOM   1053 C  CG1 . ILE A 1 138 ? 24.06647 14.12166  9.03951  1.000 47.72846  ? 133 ILE A CG1 1 
ATOM   1054 C  CG2 . ILE A 1 138 ? 25.74557 12.33214  9.52871  1.000 47.19062  ? 133 ILE A CG2 1 
ATOM   1055 C  CD1 . ILE A 1 138 ? 24.90760 14.64995  7.90994  1.000 43.03212  ? 133 ILE A CD1 1 
ATOM   1056 N  N   . LEU A 1 139 ? 24.56238 9.50962   8.15761  1.000 36.00649  ? 134 LEU A N   1 
ATOM   1057 C  CA  . LEU A 1 139 ? 24.62016 8.09493   8.48787  1.000 30.87489  ? 134 LEU A CA  1 
ATOM   1058 C  C   . LEU A 1 139 ? 25.66220 7.85722   9.57092  1.000 32.24581  ? 134 LEU A C   1 
ATOM   1059 O  O   . LEU A 1 139 ? 26.69531 8.53044   9.61710  1.000 32.70171  ? 134 LEU A O   1 
ATOM   1060 C  CB  . LEU A 1 139 ? 24.96874 7.26689   7.24793  1.000 33.61352  ? 134 LEU A CB  1 
ATOM   1061 C  CG  . LEU A 1 139 ? 24.06833 7.47010   6.03349  1.000 36.59025  ? 134 LEU A CG  1 
ATOM   1062 C  CD1 . LEU A 1 139 ? 24.61791 6.71431   4.82607  1.000 41.01540  ? 134 LEU A CD1 1 
ATOM   1063 C  CD2 . LEU A 1 139 ? 22.65076 7.02829   6.35447  1.000 43.72222  ? 134 LEU A CD2 1 
ATOM   1064 N  N   . ASP A 1 140 ? 25.38075 6.89705   10.44833 1.000 30.36413  ? 135 ASP A N   1 
ATOM   1065 C  CA  . ASP A 1 140 ? 26.33323 6.54503   11.48816 1.000 30.29460  ? 135 ASP A CA  1 
ATOM   1066 C  C   . ASP A 1 140 ? 27.36034 5.55249   10.95526 1.000 25.89814  ? 135 ASP A C   1 
ATOM   1067 O  O   . ASP A 1 140 ? 27.10036 4.78843   10.02172 1.000 30.22620  ? 135 ASP A O   1 
ATOM   1068 C  CB  . ASP A 1 140 ? 25.62474 5.94207   12.70168 1.000 28.14637  ? 135 ASP A CB  1 
ATOM   1069 C  CG  . ASP A 1 140 ? 24.78199 6.95554   13.45079 1.000 28.77977  ? 135 ASP A CG  1 
ATOM   1070 O  OD1 . ASP A 1 140 ? 25.05753 8.17164   13.34009 1.000 36.74320  ? 135 ASP A OD1 1 
ATOM   1071 O  OD2 . ASP A 1 140 ? 23.84482 6.53039   14.14809 1.000 30.21830  ? 135 ASP A OD2 1 
ATOM   1072 N  N   . TRP A 1 141 ? 28.53921 5.55846   11.57783 1.000 29.84426  ? 136 TRP A N   1 
ATOM   1073 C  CA  . TRP A 1 141 ? 29.62268 4.65715   11.18015 1.000 32.72477  ? 136 TRP A CA  1 
ATOM   1074 C  C   . TRP A 1 141 ? 29.51021 3.35015   11.96384 1.000 28.10221  ? 136 TRP A C   1 
ATOM   1075 O  O   . TRP A 1 141 ? 30.33516 3.01459   12.81570 1.000 31.24781  ? 136 TRP A O   1 
ATOM   1076 C  CB  . TRP A 1 141 ? 30.97864 5.31757   11.39192 1.000 29.23793  ? 136 TRP A CB  1 
ATOM   1077 C  CG  . TRP A 1 141 ? 32.09721 4.59083   10.69204 1.000 34.30365  ? 136 TRP A CG  1 
ATOM   1078 C  CD1 . TRP A 1 141 ? 32.91659 3.63304   11.21891 1.000 30.79935  ? 136 TRP A CD1 1 
ATOM   1079 C  CD2 . TRP A 1 141 ? 32.50703 4.76568   9.33245  1.000 32.56423  ? 136 TRP A CD2 1 
ATOM   1080 N  NE1 . TRP A 1 141 ? 33.80816 3.19844   10.26563 1.000 31.80292  ? 136 TRP A NE1 1 
ATOM   1081 C  CE2 . TRP A 1 141 ? 33.57991 3.88276   9.10050  1.000 32.85903  ? 136 TRP A CE2 1 
ATOM   1082 C  CE3 . TRP A 1 141 ? 32.06875 5.58063   8.28831  1.000 32.80968  ? 136 TRP A CE3 1 
ATOM   1083 C  CZ2 . TRP A 1 141 ? 34.22248 3.79555   7.86470  1.000 34.18218  ? 136 TRP A CZ2 1 
ATOM   1084 C  CZ3 . TRP A 1 141 ? 32.70714 5.49196   7.06178  1.000 35.04152  ? 136 TRP A CZ3 1 
ATOM   1085 C  CH2 . TRP A 1 141 ? 33.77258 4.60654   6.86244  1.000 40.20433  ? 136 TRP A CH2 1 
ATOM   1086 N  N   . SER A 1 142 ? 28.44941 2.60829   11.65946 1.000 32.47745  ? 137 SER A N   1 
ATOM   1087 C  CA  . SER A 1 142 ? 28.19801 1.33218   12.31550 1.000 26.30854  ? 137 SER A CA  1 
ATOM   1088 C  C   . SER A 1 142 ? 27.10573 0.60103   11.55537 1.000 32.96197  ? 137 SER A C   1 
ATOM   1089 O  O   . SER A 1 142 ? 26.30072 1.20815   10.84204 1.000 30.43064  ? 137 SER A O   1 
ATOM   1090 C  CB  . SER A 1 142 ? 27.78155 1.50065   13.78570 1.000 23.80852  ? 137 SER A CB  1 
ATOM   1091 O  OG  . SER A 1 142 ? 26.51685 2.13995   13.90061 1.000 30.39452  ? 137 SER A OG  1 
ATOM   1092 N  N   . ASP A 1 143 ? 27.09654 -0.71240  11.72099 1.000 25.91157  ? 138 ASP A N   1 
ATOM   1093 C  CA  . ASP A 1 143 ? 25.98514 -1.56675  11.34621 1.000 26.00171  ? 138 ASP A CA  1 
ATOM   1094 C  C   . ASP A 1 143 ? 25.37756 -2.12942  12.62072 1.000 25.22705  ? 138 ASP A C   1 
ATOM   1095 O  O   . ASP A 1 143 ? 25.97839 -2.06320  13.69320 1.000 27.58141  ? 138 ASP A O   1 
ATOM   1096 C  CB  . ASP A 1 143 ? 26.45354 -2.69699  10.43156 1.000 28.50981  ? 138 ASP A CB  1 
ATOM   1097 C  CG  . ASP A 1 143 ? 27.33492 -2.19717  9.31149  1.000 33.44705  ? 138 ASP A CG  1 
ATOM   1098 O  OD1 . ASP A 1 143 ? 26.88280 -1.30133  8.56955  1.000 31.25768  ? 138 ASP A OD1 1 
ATOM   1099 O  OD2 . ASP A 1 143 ? 28.47878 -2.68521  9.19289  1.000 34.59149  ? 138 ASP A OD2 1 
ATOM   1100 N  N   . ARG A 1 144 ? 24.18087 -2.69608  12.50306 1.000 30.03665  ? 139 ARG A N   1 
ATOM   1101 C  CA  . ARG A 1 144 ? 23.60901 -3.35926  13.66333 1.000 25.07347  ? 139 ARG A CA  1 
ATOM   1102 C  C   . ARG A 1 144 ? 22.66131 -4.46624  13.22698 1.000 33.53631  ? 139 ARG A C   1 
ATOM   1103 O  O   . ARG A 1 144 ? 22.00773 -4.38404  12.18024 1.000 30.02880  ? 139 ARG A O   1 
ATOM   1104 C  CB  . ARG A 1 144 ? 22.89975 -2.36568  14.59574 1.000 26.26120  ? 139 ARG A CB  1 
ATOM   1105 C  CG  . ARG A 1 144 ? 21.42748 -2.13362  14.31498 1.000 26.30252  ? 139 ARG A CG  1 
ATOM   1106 C  CD  . ARG A 1 144 ? 21.18822 -1.30155  13.06731 1.000 30.80573  ? 139 ARG A CD  1 
ATOM   1107 N  NE  . ARG A 1 144 ? 19.76715 -1.02208  12.90135 1.000 29.82969  ? 139 ARG A NE  1 
ATOM   1108 C  CZ  . ARG A 1 144 ? 18.89398 -1.88353  12.39490 1.000 32.40868  ? 139 ARG A CZ  1 
ATOM   1109 N  NH1 . ARG A 1 144 ? 19.27193 -3.07429  11.95045 1.000 29.20025  ? 139 ARG A NH1 1 
ATOM   1110 N  NH2 . ARG A 1 144 ? 17.60991 -1.54411  12.33115 1.000 32.51821  ? 139 ARG A NH2 1 
ATOM   1111 N  N   . LEU A 1 145 ? 22.63072 -5.52043  14.03671 1.000 30.54993  ? 140 LEU A N   1 
ATOM   1112 C  CA  . LEU A 1 145 ? 21.66016 -6.59839  13.91778 1.000 30.11142  ? 140 LEU A CA  1 
ATOM   1113 C  C   . LEU A 1 145 ? 20.62309 -6.39518  15.01372 1.000 26.27529  ? 140 LEU A C   1 
ATOM   1114 O  O   . LEU A 1 145 ? 20.95238 -6.44984  16.20270 1.000 28.39820  ? 140 LEU A O   1 
ATOM   1115 C  CB  . LEU A 1 145 ? 22.33777 -7.96398  14.03997 1.000 32.68158  ? 140 LEU A CB  1 
ATOM   1116 C  CG  . LEU A 1 145 ? 21.41438 -9.18139  14.08285 1.000 32.83892  ? 140 LEU A CG  1 
ATOM   1117 C  CD1 . LEU A 1 145 ? 20.66995 -9.33704  12.76650 1.000 33.31143  ? 140 LEU A CD1 1 
ATOM   1118 C  CD2 . LEU A 1 145 ? 22.20292 -10.43681 14.41890 1.000 36.72392  ? 140 LEU A CD2 1 
ATOM   1119 N  N   . HIS A 1 146 ? 19.38411 -6.13344  14.61113 1.000 32.27485  ? 141 HIS A N   1 
ATOM   1120 C  CA  . HIS A 1 146 ? 18.31622 -5.71818  15.51567 1.000 27.15495  ? 141 HIS A CA  1 
ATOM   1121 C  C   . HIS A 1 146 ? 17.25971 -6.81591  15.53746 1.000 31.88946  ? 141 HIS A C   1 
ATOM   1122 O  O   . HIS A 1 146 ? 16.63511 -7.09594  14.50886 1.000 33.78239  ? 141 HIS A O   1 
ATOM   1123 C  CB  . HIS A 1 146 ? 17.71737 -4.38841  15.04680 1.000 27.45572  ? 141 HIS A CB  1 
ATOM   1124 C  CG  . HIS A 1 146 ? 17.19160 -3.52879  16.15293 1.000 29.36971  ? 141 HIS A CG  1 
ATOM   1125 N  ND1 . HIS A 1 146 ? 16.10471 -3.88472  16.92128 1.000 33.49682  ? 141 HIS A ND1 1 
ATOM   1126 C  CD2 . HIS A 1 146 ? 17.59304 -2.31759  16.60746 1.000 28.14810  ? 141 HIS A CD2 1 
ATOM   1127 C  CE1 . HIS A 1 146 ? 15.86605 -2.93672  17.80961 1.000 31.40915  ? 141 HIS A CE1 1 
ATOM   1128 N  NE2 . HIS A 1 146 ? 16.75425 -1.97322  17.64010 1.000 28.87220  ? 141 HIS A NE2 1 
ATOM   1129 N  N   . LEU A 1 147 ? 17.06194 -7.44023  16.69941 1.000 29.06380  ? 142 LEU A N   1 
ATOM   1130 C  CA  . LEU A 1 147 ? 16.17970 -8.59411  16.81867 1.000 30.02270  ? 142 LEU A CA  1 
ATOM   1131 C  C   . LEU A 1 147 ? 15.17033 -8.36871  17.93342 1.000 33.59800  ? 142 LEU A C   1 
ATOM   1132 O  O   . LEU A 1 147 ? 15.54285 -7.96693  19.03979 1.000 30.63202  ? 142 LEU A O   1 
ATOM   1133 C  CB  . LEU A 1 147 ? 16.97433 -9.87308  17.10808 1.000 28.33503  ? 142 LEU A CB  1 
ATOM   1134 C  CG  . LEU A 1 147 ? 18.07826 -10.27589 16.13694 1.000 29.56794  ? 142 LEU A CG  1 
ATOM   1135 C  CD1 . LEU A 1 147 ? 18.79203 -11.50883 16.66482 1.000 35.40607  ? 142 LEU A CD1 1 
ATOM   1136 C  CD2 . LEU A 1 147 ? 17.49705 -10.54361 14.75923 1.000 33.21466  ? 142 LEU A CD2 1 
ATOM   1137 N  N   . ARG A 1 148 ? 13.90089 -8.64165  17.64901 1.000 36.37695  ? 143 ARG A N   1 
ATOM   1138 C  CA  . ARG A 1 148 ? 12.88311 -8.64164  18.69304 1.000 35.74503  ? 143 ARG A CA  1 
ATOM   1139 C  C   . ARG A 1 148 ? 13.00473 -9.93124  19.49218 1.000 32.95500  ? 143 ARG A C   1 
ATOM   1140 O  O   . ARG A 1 148 ? 12.86735 -11.02663 18.93511 1.000 34.35186  ? 143 ARG A O   1 
ATOM   1141 C  CB  . ARG A 1 148 ? 11.48337 -8.51722  18.09676 1.000 40.29911  ? 143 ARG A CB  1 
ATOM   1142 C  CG  . ARG A 1 148 ? 10.37452 -8.61760  19.14134 1.000 45.00301  ? 143 ARG A CG  1 
ATOM   1143 C  CD  . ARG A 1 148 ? 9.01136  -8.80742  18.50171 1.000 47.27689  ? 143 ARG A CD  1 
ATOM   1144 N  NE  . ARG A 1 148 ? 8.48625  -7.56773  17.94366 1.000 49.40495  ? 143 ARG A NE  1 
ATOM   1145 C  CZ  . ARG A 1 148 ? 7.80348  -6.66788  18.63809 1.000 50.71997  ? 143 ARG A CZ  1 
ATOM   1146 N  NH1 . ARG A 1 148 ? 7.56258  -6.82877  19.92969 1.000 49.85709  ? 143 ARG A NH1 1 
ATOM   1147 N  NH2 . ARG A 1 148 ? 7.34744  -5.58181  18.02098 1.000 55.11143  ? 143 ARG A NH2 1 
ATOM   1148 N  N   . VAL A 1 149 ? 13.27908 -9.80788  20.78868 1.000 33.67959  ? 144 VAL A N   1 
ATOM   1149 C  CA  . VAL A 1 149 ? 13.42915 -10.98268 21.63853 1.000 35.51229  ? 144 VAL A CA  1 
ATOM   1150 C  C   . VAL A 1 149 ? 12.13415 -11.23665 22.39642 1.000 35.16730  ? 144 VAL A C   1 
ATOM   1151 O  O   . VAL A 1 149 ? 11.81870 -12.38315 22.73063 1.000 36.13860  ? 144 VAL A O   1 
ATOM   1152 C  CB  . VAL A 1 149 ? 14.61761 -10.83365 22.60778 1.000 34.93447  ? 144 VAL A CB  1 
ATOM   1153 C  CG1 . VAL A 1 149 ? 15.92996 -10.69919 21.82849 1.000 33.99183  ? 144 VAL A CG1 1 
ATOM   1154 C  CG2 . VAL A 1 149 ? 14.42090 -9.63913  23.52533 1.000 48.33162  ? 144 VAL A CG2 1 
ATOM   1155 N  N   . GLU A 1 150 ? 11.37257 -10.18057 22.66796 1.000 34.47663  ? 145 GLU A N   1 
ATOM   1156 C  CA  . GLU A 1 150 ? 10.16871 -10.32837 23.46805 1.000 43.83800  ? 145 GLU A CA  1 
ATOM   1157 C  C   . GLU A 1 150 ? 9.01257  -9.54581  22.86648 1.000 42.04886  ? 145 GLU A C   1 
ATOM   1158 O  O   . GLU A 1 150 ? 9.21442  -8.48221  22.26968 1.000 40.77697  ? 145 GLU A O   1 
ATOM   1159 C  CB  . GLU A 1 150 ? 10.40306 -9.87512  24.91561 1.000 39.84796  ? 145 GLU A CB  1 
ATOM   1160 C  CG  . GLU A 1 150 ? 11.26685 -10.84171 25.70021 1.000 44.15092  ? 145 GLU A CG  1 
ATOM   1161 C  CD  . GLU A 1 150 ? 10.99165 -10.79402 27.18254 1.000 56.88435  ? 145 GLU A CD  1 
ATOM   1162 O  OE1 . GLU A 1 150 ? 11.28677 -9.75604  27.80934 1.000 56.91214  ? 145 GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A 1 150 ? 10.46960 -11.79443 27.71706 1.000 59.83638  ? 145 GLU A OE2 1 
ATOM   1164 N  N   . PRO A 1 151 ? 7.78064  -10.06098 22.99672 1.000 45.68385  ? 146 PRO A N   1 
ATOM   1165 C  CA  . PRO A 1 151 ? 7.41425  -11.34487 23.62308 1.000 48.30931  ? 146 PRO A CA  1 
ATOM   1166 C  C   . PRO A 1 151 ? 7.95928  -12.52814 22.82614 1.000 54.19355  ? 146 PRO A C   1 
ATOM   1167 O  O   . PRO A 1 151 ? 8.08405  -12.44907 21.60350 1.000 49.81452  ? 146 PRO A O   1 
ATOM   1168 C  CB  . PRO A 1 151 ? 5.87965  -11.29749 23.64347 1.000 54.44811  ? 146 PRO A CB  1 
ATOM   1169 C  CG  . PRO A 1 151 ? 5.50810  -10.37131 22.52681 1.000 59.49425  ? 146 PRO A CG  1 
ATOM   1170 C  CD  . PRO A 1 151 ? 6.60087  -9.33599  22.49401 1.000 44.14757  ? 146 PRO A CD  1 
ATOM   1171 N  N   . LYS A 1 152 ? 8.31351  -13.61534 23.52101 1.000 55.34520  ? 147 LYS A N   1 
ATOM   1172 C  CA  . LYS A 1 152 ? 9.01286  -14.73229 22.88803 1.000 53.80507  ? 147 LYS A CA  1 
ATOM   1173 C  C   . LYS A 1 152 ? 8.25912  -15.24982 21.67091 1.000 52.24176  ? 147 LYS A C   1 
ATOM   1174 O  O   . LYS A 1 152 ? 8.86966  -15.63274 20.66554 1.000 53.55971  ? 147 LYS A O   1 
ATOM   1175 C  CB  . LYS A 1 152 ? 9.21879  -15.85534 23.90823 1.000 53.36535  ? 147 LYS A CB  1 
ATOM   1176 C  CG  . LYS A 1 152 ? 10.05664 -17.02529 23.41632 1.000 66.76110  ? 147 LYS A CG  1 
ATOM   1177 C  CD  . LYS A 1 152 ? 11.54150 -16.78181 23.63885 1.000 62.26839  ? 147 LYS A CD  1 
ATOM   1178 C  CE  . LYS A 1 152 ? 12.38705 -17.89724 23.03162 1.000 64.80191  ? 147 LYS A CE  1 
ATOM   1179 N  NZ  . LYS A 1 152 ? 12.19750 -19.21628 23.70064 1.000 65.04749  ? 147 LYS A NZ  1 
ATOM   1180 N  N   . GLU A 1 153 ? 6.92835  -15.24762 21.73643 1.000 57.29307  ? 148 GLU A N   1 
ATOM   1181 C  CA  . GLU A 1 153 ? 6.10564  -15.77887 20.65941 1.000 56.30914  ? 148 GLU A CA  1 
ATOM   1182 C  C   . GLU A 1 153 ? 6.12930  -14.91420 19.40584 1.000 58.87509  ? 148 GLU A C   1 
ATOM   1183 O  O   . GLU A 1 153 ? 5.68552  -15.37824 18.35034 1.000 58.40703  ? 148 GLU A O   1 
ATOM   1184 C  CB  . GLU A 1 153 ? 4.65936  -15.94753 21.13807 1.000 62.90434  ? 148 GLU A CB  1 
ATOM   1185 C  CG  . GLU A 1 153 ? 4.47405  -16.96919 22.25749 1.000 69.62994  ? 148 GLU A CG  1 
ATOM   1186 C  CD  . GLU A 1 153 ? 4.85706  -16.43148 23.62911 1.000 76.13645  ? 148 GLU A CD  1 
ATOM   1187 O  OE1 . GLU A 1 153 ? 5.09332  -15.20770 23.74982 1.000 69.19765  ? 148 GLU A OE1 1 
ATOM   1188 O  OE2 . GLU A 1 153 ? 4.92180  -17.23516 24.58666 1.000 62.75521  ? 148 GLU A OE2 1 
ATOM   1189 N  N   . GLU A 1 154 ? 6.62296  -13.68042 19.48494 1.000 60.44778  ? 149 GLU A N   1 
ATOM   1190 C  CA  . GLU A 1 154 ? 6.64579  -12.79138 18.33200 1.000 55.21496  ? 149 GLU A CA  1 
ATOM   1191 C  C   . GLU A 1 154 ? 8.01575  -12.71655 17.67127 1.000 50.98364  ? 149 GLU A C   1 
ATOM   1192 O  O   . GLU A 1 154 ? 8.22059  -11.87789 16.78795 1.000 54.26946  ? 149 GLU A O   1 
ATOM   1193 C  CB  . GLU A 1 154 ? 6.17244  -11.39301 18.73233 1.000 62.04423  ? 149 GLU A CB  1 
ATOM   1194 C  CG  . GLU A 1 154 ? 4.68645  -11.32550 19.05437 1.000 63.53576  ? 149 GLU A CG  1 
ATOM   1195 C  CD  . GLU A 1 154 ? 4.22056  -9.92520  19.40530 1.000 64.23727  ? 149 GLU A CD  1 
ATOM   1196 O  OE1 . GLU A 1 154 ? 5.03984  -8.98383  19.33580 1.000 70.41496  ? 149 GLU A OE1 1 
ATOM   1197 O  OE2 . GLU A 1 154 ? 3.03256  -9.76735  19.75661 1.000 67.46784  ? 149 GLU A OE2 1 
ATOM   1198 N  N   . GLN A 1 155 ? 8.95395  -13.56750 18.07711 1.000 50.23858  ? 150 GLN A N   1 
ATOM   1199 C  CA  . GLN A 1 155 ? 10.24095 -13.63762 17.40033 1.000 48.03775  ? 150 GLN A CA  1 
ATOM   1200 C  C   . GLN A 1 155 ? 10.06453 -14.15261 15.97716 1.000 54.95699  ? 150 GLN A C   1 
ATOM   1201 O  O   . GLN A 1 155 ? 9.29633  -15.08565 15.72874 1.000 53.99559  ? 150 GLN A O   1 
ATOM   1202 C  CB  . GLN A 1 155 ? 11.19712 -14.55251 18.16461 1.000 46.19816  ? 150 GLN A CB  1 
ATOM   1203 C  CG  . GLN A 1 155 ? 11.53777 -14.08430 19.56469 1.000 42.35866  ? 150 GLN A CG  1 
ATOM   1204 C  CD  . GLN A 1 155 ? 12.47276 -15.03748 20.28454 1.000 46.04466  ? 150 GLN A CD  1 
ATOM   1205 O  OE1 . GLN A 1 155 ? 12.78112 -16.12329 19.78497 1.000 48.55448  ? 150 GLN A OE1 1 
ATOM   1206 N  NE2 . GLN A 1 155 ? 12.93068 -14.63563 21.46601 1.000 41.53888  ? 150 GLN A NE2 1 
ATOM   1207 N  N   . ASP A 1 156 ? 10.77954 -13.53729 15.03768 1.000 47.21815  ? 151 ASP A N   1 
ATOM   1208 C  CA  . ASP A 1 156 ? 10.83513 -14.00011 13.65208 1.000 47.43280  ? 151 ASP A CA  1 
ATOM   1209 C  C   . ASP A 1 156 ? 12.21418 -14.61949 13.45369 1.000 46.83424  ? 151 ASP A C   1 
ATOM   1210 O  O   . ASP A 1 156 ? 13.20116 -13.90833 13.24452 1.000 51.48423  ? 151 ASP A O   1 
ATOM   1211 C  CB  . ASP A 1 156 ? 10.57372 -12.85747 12.67216 1.000 52.37472  ? 151 ASP A CB  1 
ATOM   1212 C  CG  . ASP A 1 156 ? 10.50807 -13.32628 11.22110 1.000 51.71555  ? 151 ASP A CG  1 
ATOM   1213 O  OD1 . ASP A 1 156 ? 10.76260 -14.51834 10.95551 1.000 47.55506  ? 151 ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A 1 156 ? 10.19676 -12.49607 10.34267 1.000 56.53877  ? 151 ASP A OD2 1 
ATOM   1215 N  N   . LEU A 1 157 ? 12.27794 -15.94953 13.52078 1.000 43.51495  ? 152 LEU A N   1 
ATOM   1216 C  CA  . LEU A 1 157 ? 13.55909 -16.64479 13.48207 1.000 47.51941  ? 152 LEU A CA  1 
ATOM   1217 C  C   . LEU A 1 157 ? 14.22313 -16.60340 12.11181 1.000 53.11219  ? 152 LEU A C   1 
ATOM   1218 O  O   . LEU A 1 157 ? 15.38191 -17.01635 11.99496 1.000 53.37502  ? 152 LEU A O   1 
ATOM   1219 C  CB  . LEU A 1 157 ? 13.37882 -18.09455 13.93332 1.000 51.75048  ? 152 LEU A CB  1 
ATOM   1220 C  CG  . LEU A 1 157 ? 12.99065 -18.26784 15.40315 1.000 57.47855  ? 152 LEU A CG  1 
ATOM   1221 C  CD1 . LEU A 1 157 ? 12.82112 -19.74354 15.75054 1.000 56.28255  ? 152 LEU A CD1 1 
ATOM   1222 C  CD2 . LEU A 1 157 ? 14.02182 -17.60879 16.30742 1.000 51.96756  ? 152 LEU A CD2 1 
ATOM   1223 N  N   . ALA A 1 158 ? 13.53559 -16.11201 11.07902 1.000 45.31220  ? 153 ALA A N   1 
ATOM   1224 C  CA  . ALA A 1 158 ? 14.18743 -15.95358 9.78618  1.000 47.35241  ? 153 ALA A CA  1 
ATOM   1225 C  C   . ALA A 1 158 ? 15.28102 -14.89395 9.82100  1.000 44.82954  ? 153 ALA A C   1 
ATOM   1226 O  O   . ALA A 1 158 ? 16.12660 -14.86290 8.92092  1.000 47.41250  ? 153 ALA A O   1 
ATOM   1227 C  CB  . ALA A 1 158 ? 13.15807 -15.60863 8.70895  1.000 47.18425  ? 153 ALA A CB  1 
ATOM   1228 N  N   . PHE A 1 159 ? 15.28993 -14.03084 10.83505 1.000 45.08890  ? 154 PHE A N   1 
ATOM   1229 C  CA  . PHE A 1 159 ? 16.31246 -13.00446 10.96463 1.000 45.29987  ? 154 PHE A CA  1 
ATOM   1230 C  C   . PHE A 1 159 ? 17.32542 -13.31375 12.05324 1.000 44.45778  ? 154 PHE A C   1 
ATOM   1231 O  O   . PHE A 1 159 ? 18.26848 -12.53754 12.24344 1.000 40.93507  ? 154 PHE A O   1 
ATOM   1232 C  CB  . PHE A 1 159 ? 15.65974 -11.64379 11.21839 1.000 43.84610  ? 154 PHE A CB  1 
ATOM   1233 C  CG  . PHE A 1 159 ? 14.86834 -11.14345 10.05034 1.000 48.32718  ? 154 PHE A CG  1 
ATOM   1234 C  CD1 . PHE A 1 159 ? 13.51578 -11.41599 9.94378  1.000 50.31184  ? 154 PHE A CD1 1 
ATOM   1235 C  CD2 . PHE A 1 159 ? 15.48598 -10.42894 9.03875  1.000 53.57743  ? 154 PHE A CD2 1 
ATOM   1236 C  CE1 . PHE A 1 159 ? 12.78896 -10.96827 8.85889  1.000 52.97627  ? 154 PHE A CE1 1 
ATOM   1237 C  CE2 . PHE A 1 159 ? 14.76510 -9.97617  7.95202  1.000 52.13413  ? 154 PHE A CE2 1 
ATOM   1238 C  CZ  . PHE A 1 159 ? 13.41426 -10.24862 7.86153  1.000 56.46694  ? 154 PHE A CZ  1 
ATOM   1239 N  N   . TRP A 1 160 ? 17.16148 -14.42096 12.76475 1.000 43.10847  ? 155 TRP A N   1 
ATOM   1240 C  CA  . TRP A 1 160 ? 18.15609 -14.84417 13.74228 1.000 45.12028  ? 155 TRP A CA  1 
ATOM   1241 C  C   . TRP A 1 160 ? 19.23110 -15.66764 13.04926 1.000 42.68246  ? 155 TRP A C   1 
ATOM   1242 O  O   . TRP A 1 160 ? 18.90405 -16.64309 12.36114 1.000 41.49509  ? 155 TRP A O   1 
ATOM   1243 C  CB  . TRP A 1 160 ? 17.51650 -15.66715 14.85031 1.000 41.90802  ? 155 TRP A CB  1 
ATOM   1244 C  CG  . TRP A 1 160 ? 16.62530 -14.87359 15.75299 1.000 43.24018  ? 155 TRP A CG  1 
ATOM   1245 C  CD1 . TRP A 1 160 ? 15.61659 -14.03423 15.37906 1.000 41.29597  ? 155 TRP A CD1 1 
ATOM   1246 C  CD2 . TRP A 1 160 ? 16.64913 -14.85869 17.18422 1.000 36.46733  ? 155 TRP A CD2 1 
ATOM   1247 N  NE1 . TRP A 1 160 ? 15.01945 -13.48804 16.48824 1.000 38.16329  ? 155 TRP A NE1 1 
ATOM   1248 C  CE2 . TRP A 1 160 ? 15.63188 -13.98129 17.60946 1.000 38.87770  ? 155 TRP A CE2 1 
ATOM   1249 C  CE3 . TRP A 1 160 ? 17.43309 -15.49949 18.14754 1.000 40.40024  ? 155 TRP A CE3 1 
ATOM   1250 C  CZ2 . TRP A 1 160 ? 15.37828 -13.72917 18.95338 1.000 38.36409  ? 155 TRP A CZ2 1 
ATOM   1251 C  CZ3 . TRP A 1 160 ? 17.17875 -15.24887 19.48197 1.000 37.47313  ? 155 TRP A CZ3 1 
ATOM   1252 C  CH2 . TRP A 1 160 ? 16.16052 -14.37057 19.87297 1.000 41.88399  ? 155 TRP A CH2 1 
ATOM   1253 N  N   . PRO A 1 161 ? 20.50212 -15.30024 13.19126 1.000 41.64244  ? 156 PRO A N   1 
ATOM   1254 C  CA  . PRO A 1 161 ? 21.57312 -16.06947 12.54823 1.000 46.58390  ? 156 PRO A CA  1 
ATOM   1255 C  C   . PRO A 1 161 ? 21.51591 -17.54180 12.92561 1.000 49.41849  ? 156 PRO A C   1 
ATOM   1256 O  O   . PRO A 1 161 ? 21.34006 -17.89870 14.09302 1.000 50.97682  ? 156 PRO A O   1 
ATOM   1257 C  CB  . PRO A 1 161 ? 22.84597 -15.39945 13.07424 1.000 46.96995  ? 156 PRO A CB  1 
ATOM   1258 C  CG  . PRO A 1 161 ? 22.43060 -14.00234 13.36118 1.000 42.56844  ? 156 PRO A CG  1 
ATOM   1259 C  CD  . PRO A 1 161 ? 21.01346 -14.09327 13.86214 1.000 46.28564  ? 156 PRO A CD  1 
ATOM   1260 N  N   . ASP A 1 162 ? 21.63831 -18.40030 11.91517 1.000 52.83791  ? 157 ASP A N   1 
ATOM   1261 C  CA  . ASP A 1 162 ? 21.72311 -19.83783 12.12466 1.000 55.16004  ? 157 ASP A CA  1 
ATOM   1262 C  C   . ASP A 1 162 ? 23.15713 -20.32292 12.28259 1.000 56.85050  ? 157 ASP A C   1 
ATOM   1263 O  O   . ASP A 1 162 ? 23.36640 -21.47979 12.66490 1.000 50.16161  ? 157 ASP A O   1 
ATOM   1264 C  CB  . ASP A 1 162 ? 21.04918 -20.58414 10.96879 1.000 61.67639  ? 157 ASP A CB  1 
ATOM   1265 C  CG  . ASP A 1 162 ? 21.26494 -19.90490 9.63295  1.000 70.36485  ? 157 ASP A CG  1 
ATOM   1266 O  OD1 . ASP A 1 162 ? 22.38067 -19.39711 9.39308  1.000 65.75136  ? 157 ASP A OD1 1 
ATOM   1267 O  OD2 . ASP A 1 162 ? 20.31905 -19.88780 8.81764  1.000 80.63653  ? 157 ASP A OD2 1 
ATOM   1268 N  N   . HIS A 1 163 ? 24.14229 -19.47409 11.99034 1.000 46.59237  ? 158 HIS A N   1 
ATOM   1269 C  CA  . HIS A 1 163 ? 25.53154 -19.74726 12.31466 1.000 55.40095  ? 158 HIS A CA  1 
ATOM   1270 C  C   . HIS A 1 163 ? 26.13791 -18.49421 12.93593 1.000 53.91154  ? 158 HIS A C   1 
ATOM   1271 O  O   . HIS A 1 163 ? 25.99565 -17.39507 12.37282 1.000 56.90438  ? 158 HIS A O   1 
ATOM   1272 C  CB  . HIS A 1 163 ? 26.33154 -20.18818 11.08679 1.000 63.00091  ? 158 HIS A CB  1 
ATOM   1273 C  CG  . HIS A 1 163 ? 26.39603 -21.67373 10.92096 1.000 71.92061  ? 158 HIS A CG  1 
ATOM   1274 N  ND1 . HIS A 1 163 ? 25.43081 -22.39073 10.24735 1.000 79.41896  ? 158 HIS A ND1 1 
ATOM   1275 C  CD2 . HIS A 1 163 ? 27.29758 -22.58111 11.36536 1.000 72.85814  ? 158 HIS A CD2 1 
ATOM   1276 C  CE1 . HIS A 1 163 ? 25.74347 -23.67423 10.26912 1.000 86.40405  ? 158 HIS A CE1 1 
ATOM   1277 N  NE2 . HIS A 1 163 ? 26.87111 -23.81688 10.94237 1.000 98.71462  ? 158 HIS A NE2 1 
ATOM   1278 N  N   . PRO A 1 164 ? 26.80939 -18.60387 14.09257 1.000 49.76826  ? 159 PRO A N   1 
ATOM   1279 C  CA  . PRO A 1 164 ? 27.08158 -19.81959 14.88418 1.000 53.56396  ? 159 PRO A CA  1 
ATOM   1280 C  C   . PRO A 1 164 ? 25.81155 -20.51666 15.36986 1.000 54.14046  ? 159 PRO A C   1 
ATOM   1281 O  O   . PRO A 1 164 ? 24.82338 -19.86478 15.70066 1.000 49.47669  ? 159 PRO A O   1 
ATOM   1282 C  CB  . PRO A 1 164 ? 27.92846 -19.28878 16.05186 1.000 45.44791  ? 159 PRO A CB  1 
ATOM   1283 C  CG  . PRO A 1 164 ? 27.57982 -17.83170 16.15193 1.000 49.47710  ? 159 PRO A CG  1 
ATOM   1284 C  CD  . PRO A 1 164 ? 27.36493 -17.40108 14.73467 1.000 52.09454  ? 159 PRO A CD  1 
ATOM   1285 N  N   . GLU A 1 165 ? 25.83501 -21.85372 15.39884 1.000 47.78755  ? 160 GLU A N   1 
ATOM   1286 C  CA  . GLU A 1 165 ? 24.61948 -22.63024 15.62942 1.000 51.40560  ? 160 GLU A CA  1 
ATOM   1287 C  C   . GLU A 1 165 ? 23.93570 -22.26267 16.93990 1.000 47.61542  ? 160 GLU A C   1 
ATOM   1288 O  O   . GLU A 1 165 ? 22.70225 -22.27728 17.01871 1.000 51.19541  ? 160 GLU A O   1 
ATOM   1289 C  CB  . GLU A 1 165 ? 24.94174 -24.12611 15.61651 1.000 50.48074  ? 160 GLU A CB  1 
ATOM   1290 C  CG  . GLU A 1 165 ? 25.69512 -24.60261 14.38558 1.000 68.65230  ? 160 GLU A CG  1 
ATOM   1291 C  CD  . GLU A 1 165 ? 26.03449 -26.08305 14.44981 1.000 74.73582  ? 160 GLU A CD  1 
ATOM   1292 O  OE1 . GLU A 1 165 ? 25.53867 -26.76714 15.37006 1.000 66.86869  ? 160 GLU A OE1 1 
ATOM   1293 O  OE2 . GLU A 1 165 ? 26.79721 -26.56245 13.58259 1.000 87.36913  ? 160 GLU A OE2 1 
ATOM   1294 N  N   . SER A 1 166 ? 24.70511 -21.93396 17.97267 1.000 43.60124  ? 161 SER A N   1 
ATOM   1295 C  CA  . SER A 1 166 ? 24.14924 -21.71096 19.29954 1.000 47.35450  ? 161 SER A CA  1 
ATOM   1296 C  C   . SER A 1 166 ? 23.67868 -20.27852 19.51959 1.000 43.28552  ? 161 SER A C   1 
ATOM   1297 O  O   . SER A 1 166 ? 23.31718 -19.93091 20.64823 1.000 39.40671  ? 161 SER A O   1 
ATOM   1298 C  CB  . SER A 1 166 ? 25.17724 -22.08672 20.36956 1.000 46.92765  ? 161 SER A CB  1 
ATOM   1299 O  OG  . SER A 1 166 ? 26.32118 -21.25542 20.29204 1.000 55.67162  ? 161 SER A OG  1 
ATOM   1300 N  N   . PHE A 1 167 ? 23.66293 -19.44993 18.47121 1.000 37.82159  ? 162 PHE A N   1 
ATOM   1301 C  CA  . PHE A 1 167 ? 23.32371 -18.03807 18.63461 1.000 43.88416  ? 162 PHE A CA  1 
ATOM   1302 C  C   . PHE A 1 167 ? 21.95361 -17.86896 19.27908 1.000 38.13290  ? 162 PHE A C   1 
ATOM   1303 O  O   . PHE A 1 167 ? 21.80078 -17.11746 20.25053 1.000 38.40651  ? 162 PHE A O   1 
ATOM   1304 C  CB  . PHE A 1 167 ? 23.37551 -17.32561 17.28085 1.000 46.18800  ? 162 PHE A CB  1 
ATOM   1305 C  CG  . PHE A 1 167 ? 23.17407 -15.83384 17.37026 1.000 42.64255  ? 162 PHE A CG  1 
ATOM   1306 C  CD1 . PHE A 1 167 ? 21.90157 -15.28645 17.31716 1.000 38.57246  ? 162 PHE A CD1 1 
ATOM   1307 C  CD2 . PHE A 1 167 ? 24.25812 -14.97987 17.50587 1.000 44.81584  ? 162 PHE A CD2 1 
ATOM   1308 C  CE1 . PHE A 1 167 ? 21.71352 -13.91608 17.39973 1.000 37.75717  ? 162 PHE A CE1 1 
ATOM   1309 C  CE2 . PHE A 1 167 ? 24.07580 -13.60747 17.59067 1.000 49.85639  ? 162 PHE A CE2 1 
ATOM   1310 C  CZ  . PHE A 1 167 ? 22.80188 -13.07653 17.53810 1.000 38.85581  ? 162 PHE A CZ  1 
ATOM   1311 N  N   . ARG A 1 168 ? 20.94608 -18.57172 18.75542 1.000 42.20846  ? 163 ARG A N   1 
ATOM   1312 C  CA  . ARG A 1 168 ? 19.59009 -18.43560 19.27861 1.000 43.26388  ? 163 ARG A CA  1 
ATOM   1313 C  C   . ARG A 1 168 ? 19.51945 -18.83736 20.74548 1.000 40.78630  ? 163 ARG A C   1 
ATOM   1314 O  O   . ARG A 1 168 ? 19.01858 -18.07871 21.58316 1.000 37.02591  ? 163 ARG A O   1 
ATOM   1315 C  CB  . ARG A 1 168 ? 18.61829 -19.27439 18.44926 1.000 48.81297  ? 163 ARG A CB  1 
ATOM   1316 C  CG  . ARG A 1 168 ? 18.38777 -18.75713 17.03842 1.000 63.87681  ? 163 ARG A CG  1 
ATOM   1317 C  CD  . ARG A 1 168 ? 19.05144 -19.64492 15.99289 1.000 68.40141  ? 163 ARG A CD  1 
ATOM   1318 N  NE  . ARG A 1 168 ? 18.69290 -19.23440 14.64027 1.000 61.42032  ? 163 ARG A NE  1 
ATOM   1319 C  CZ  . ARG A 1 168 ? 17.65408 -19.70506 13.96263 1.000 66.25381  ? 163 ARG A CZ  1 
ATOM   1320 N  NH1 . ARG A 1 168 ? 16.85468 -20.62836 14.47342 1.000 70.72692  ? 163 ARG A NH1 1 
ATOM   1321 N  NH2 . ARG A 1 168 ? 17.41010 -19.23662 12.74168 1.000 67.14505  ? 163 ARG A NH2 1 
ATOM   1322 N  N   . ASP A 1 169 ? 20.02382 -20.02878 21.07567 1.000 35.96787  ? 164 ASP A N   1 
ATOM   1323 C  CA  . ASP A 1 169 ? 19.93227 -20.51969 22.44914 1.000 39.53866  ? 164 ASP A CA  1 
ATOM   1324 C  C   . ASP A 1 169 ? 20.65085 -19.59435 23.42279 1.000 35.34006  ? 164 ASP A C   1 
ATOM   1325 O  O   . ASP A 1 169 ? 20.14550 -19.31855 24.51708 1.000 36.89158  ? 164 ASP A O   1 
ATOM   1326 C  CB  . ASP A 1 169 ? 20.50791 -21.93436 22.54625 1.000 39.15601  ? 164 ASP A CB  1 
ATOM   1327 C  CG  . ASP A 1 169 ? 19.57763 -22.98508 21.97680 1.000 51.58491  ? 164 ASP A CG  1 
ATOM   1328 O  OD1 . ASP A 1 169 ? 18.34841 -22.76651 21.99495 1.000 48.24707  ? 164 ASP A OD1 1 
ATOM   1329 O  OD2 . ASP A 1 169 ? 20.07716 -24.03081 21.51707 1.000 56.70595  ? 164 ASP A OD2 1 
ATOM   1330 N  N   . VAL A 1 170 ? 21.83005 -19.10201 23.04205 1.000 34.15744  ? 165 VAL A N   1 
ATOM   1331 C  CA  . VAL A 1 170 ? 22.61222 -18.27318 23.95217 1.000 34.24615  ? 165 VAL A CA  1 
ATOM   1332 C  C   . VAL A 1 170 ? 21.95342 -16.91256 24.14963 1.000 29.78681  ? 165 VAL A C   1 
ATOM   1333 O  O   . VAL A 1 170 ? 21.86913 -16.41261 25.27641 1.000 31.09110  ? 165 VAL A O   1 
ATOM   1334 C  CB  . VAL A 1 170 ? 24.05802 -18.14990 23.44137 1.000 33.69855  ? 165 VAL A CB  1 
ATOM   1335 C  CG1 . VAL A 1 170 ? 24.81243 -17.09248 24.21623 1.000 31.39799  ? 165 VAL A CG1 1 
ATOM   1336 C  CG2 . VAL A 1 170 ? 24.76152 -19.48903 23.57072 1.000 37.17231  ? 165 VAL A CG2 1 
ATOM   1337 N  N   . LEU A 1 171 ? 21.47081 -16.29106 23.06784 1.000 33.61946  ? 166 LEU A N   1 
ATOM   1338 C  CA  . LEU A 1 171 ? 20.80727 -14.99688 23.20499 1.000 36.32957  ? 166 LEU A CA  1 
ATOM   1339 C  C   . LEU A 1 171 ? 19.54957 -15.10773 24.05966 1.000 30.00290  ? 166 LEU A C   1 
ATOM   1340 O  O   . LEU A 1 171 ? 19.29358 -14.24936 24.91229 1.000 30.18953  ? 166 LEU A O   1 
ATOM   1341 C  CB  . LEU A 1 171 ? 20.47542 -14.41463 21.82775 1.000 31.59621  ? 166 LEU A CB  1 
ATOM   1342 C  CG  . LEU A 1 171 ? 19.68831 -13.09241 21.82192 1.000 30.23851  ? 166 LEU A CG  1 
ATOM   1343 C  CD1 . LEU A 1 171 ? 20.34243 -12.02575 22.70424 1.000 30.29654  ? 166 LEU A CD1 1 
ATOM   1344 C  CD2 . LEU A 1 171 ? 19.51680 -12.57069 20.39553 1.000 33.50904  ? 166 LEU A CD2 1 
ATOM   1345 N  N   . ASN A 1 172 ? 18.75131 -16.15532 23.85031 1.000 31.76275  ? 167 ASN A N   1 
ATOM   1346 C  CA  . ASN A 1 172 ? 17.55873 -16.32552 24.67552 1.000 35.63184  ? 167 ASN A CA  1 
ATOM   1347 C  C   . ASN A 1 172 ? 17.92620 -16.51954 26.14061 1.000 35.56846  ? 167 ASN A C   1 
ATOM   1348 O  O   . ASN A 1 172 ? 17.27260 -15.96131 27.03016 1.000 34.29044  ? 167 ASN A O   1 
ATOM   1349 C  CB  . ASN A 1 172 ? 16.72194 -17.49657 24.16775 1.000 39.38571  ? 167 ASN A CB  1 
ATOM   1350 C  CG  . ASN A 1 172 ? 15.81742 -17.10331 23.02303 1.000 39.85531  ? 167 ASN A CG  1 
ATOM   1351 O  OD1 . ASN A 1 172 ? 15.29442 -15.98972 22.98776 1.000 42.59928  ? 167 ASN A OD1 1 
ATOM   1352 N  ND2 . ASN A 1 172 ? 15.63219 -18.00999 22.07598 1.000 41.66521  ? 167 ASN A ND2 1 
ATOM   1353 N  N   . LYS A 1 173 ? 18.97855 -17.29506 26.41377 1.000 33.54678  ? 168 LYS A N   1 
ATOM   1354 C  CA  . LYS A 1 173 ? 19.40198 -17.47861 27.79784 1.000 31.99272  ? 168 LYS A CA  1 
ATOM   1355 C  C   . LYS A 1 173 ? 19.92597 -16.17526 28.38566 1.000 31.51874  ? 168 LYS A C   1 
ATOM   1356 O  O   . LYS A 1 173 ? 19.62729 -15.84176 29.53876 1.000 29.32200  ? 168 LYS A O   1 
ATOM   1357 C  CB  . LYS A 1 173 ? 20.45846 -18.58117 27.88711 1.000 38.04526  ? 168 LYS A CB  1 
ATOM   1358 C  CG  . LYS A 1 173 ? 20.59188 -19.18604 29.28034 1.000 50.07875  ? 168 LYS A CG  1 
ATOM   1359 C  CD  . LYS A 1 173 ? 21.59769 -20.32499 29.31260 1.000 61.91739  ? 168 LYS A CD  1 
ATOM   1360 C  CE  . LYS A 1 173 ? 21.69614 -20.92801 30.70798 1.000 71.53109  ? 168 LYS A CE  1 
ATOM   1361 N  NZ  . LYS A 1 173 ? 22.65400 -22.06857 30.75915 1.000 76.83447  ? 168 LYS A NZ  1 
ATOM   1362 N  N   . TYR A 1 174 ? 20.69736 -15.41703 27.60186 1.000 30.77549  ? 169 TYR A N   1 
ATOM   1363 C  CA  . TYR A 1 174 ? 21.17764 -14.12105 28.06728 1.000 27.88140  ? 169 TYR A CA  1 
ATOM   1364 C  C   . TYR A 1 174 ? 20.01209 -13.17870 28.34673 1.000 27.30514  ? 169 TYR A C   1 
ATOM   1365 O  O   . TYR A 1 174 ? 19.96830 -12.51374 29.39036 1.000 31.38501  ? 169 TYR A O   1 
ATOM   1366 C  CB  . TYR A 1 174 ? 22.13486 -13.51497 27.03421 1.000 29.24378  ? 169 TYR A CB  1 
ATOM   1367 C  CG  . TYR A 1 174 ? 22.64863 -12.16112 27.44597 1.000 27.58330  ? 169 TYR A CG  1 
ATOM   1368 C  CD1 . TYR A 1 174 ? 23.55558 -12.03203 28.49158 1.000 27.71295  ? 169 TYR A CD1 1 
ATOM   1369 C  CD2 . TYR A 1 174 ? 22.21661 -11.00538 26.80462 1.000 24.19249  ? 169 TYR A CD2 1 
ATOM   1370 C  CE1 . TYR A 1 174 ? 24.01682 -10.78203 28.89062 1.000 27.47117  ? 169 TYR A CE1 1 
ATOM   1371 C  CE2 . TYR A 1 174 ? 22.66742 -9.75730  27.19743 1.000 20.72628  ? 169 TYR A CE2 1 
ATOM   1372 C  CZ  . TYR A 1 174 ? 23.56811 -9.65458  28.23854 1.000 23.96431  ? 169 TYR A CZ  1 
ATOM   1373 O  OH  . TYR A 1 174 ? 24.02727 -8.41090  28.61929 1.000 25.35045  ? 169 TYR A OH  1 
ATOM   1374 N  N   . ALA A 1 175 ? 19.04174 -13.12661 27.42740 1.000 30.43663  ? 170 ALA A N   1 
ATOM   1375 C  CA  . ALA A 1 175 ? 17.91296 -12.21489 27.58338 1.000 31.16239  ? 170 ALA A CA  1 
ATOM   1376 C  C   . ALA A 1 175 ? 17.06221 -12.57152 28.79509 1.000 30.33107  ? 170 ALA A C   1 
ATOM   1377 O  O   . ALA A 1 175 ? 16.45611 -11.68463 29.40772 1.000 29.63119  ? 170 ALA A O   1 
ATOM   1378 C  CB  . ALA A 1 175 ? 17.05411 -12.21565 26.31992 1.000 31.98104  ? 170 ALA A CB  1 
ATOM   1379 N  N   . SER A 1 176 ? 16.99350 -13.85650 29.15040 1.000 33.16460  ? 171 SER A N   1 
ATOM   1380 C  CA  . SER A 1 176 ? 16.28178 -14.23520 30.36706 1.000 29.40780  ? 171 SER A CA  1 
ATOM   1381 C  C   . SER A 1 176 ? 16.94067 -13.62067 31.59293 1.000 35.92089  ? 171 SER A C   1 
ATOM   1382 O  O   . SER A 1 176 ? 16.25351 -13.16630 32.51426 1.000 31.72024  ? 171 SER A O   1 
ATOM   1383 C  CB  . SER A 1 176 ? 16.21501 -15.75797 30.49995 1.000 33.60881  ? 171 SER A CB  1 
ATOM   1384 O  OG  . SER A 1 176 ? 15.47183 -16.32907 29.43962 1.000 48.20525  ? 171 SER A OG  1 
ATOM   1385 N  N   . GLY A 1 177 ? 18.27380 -13.58542 31.61722 1.000 32.00774  ? 172 GLY A N   1 
ATOM   1386 C  CA  . GLY A 1 177 ? 18.96106 -12.98088 32.74558 1.000 31.97065  ? 172 GLY A CA  1 
ATOM   1387 C  C   . GLY A 1 177 ? 18.78564 -11.47507 32.80548 1.000 31.13274  ? 172 GLY A C   1 
ATOM   1388 O  O   . GLY A 1 177 ? 18.56978 -10.91020 33.88048 1.000 27.46694  ? 172 GLY A O   1 
ATOM   1389 N  N   . THR A 1 178 ? 18.88280 -10.79745 31.65793 1.000 28.32209  ? 173 THR A N   1 
ATOM   1390 C  CA  . THR A 1 178 ? 18.73120 -9.34729  31.68484 1.000 24.62410  ? 173 THR A CA  1 
ATOM   1391 C  C   . THR A 1 178 ? 17.29440 -8.94772  32.00702 1.000 23.50277  ? 173 THR A C   1 
ATOM   1392 O  O   . THR A 1 178 ? 17.07121 -7.89700  32.60966 1.000 24.40461  ? 173 THR A O   1 
ATOM   1393 C  CB  . THR A 1 178 ? 19.21463 -8.71779  30.36962 1.000 30.93354  ? 173 THR A CB  1 
ATOM   1394 O  OG1 . THR A 1 178 ? 18.47291 -9.22074  29.25550 1.000 25.69176  ? 173 THR A OG1 1 
ATOM   1395 C  CG2 . THR A 1 178 ? 20.69051 -9.01890  30.15152 1.000 24.22447  ? 173 THR A CG2 1 
ATOM   1396 N  N   . LYS A 1 179 ? 16.31459 -9.78386  31.66080 1.000 24.49859  ? 174 LYS A N   1 
ATOM   1397 C  CA  . LYS A 1 179 ? 14.93484 -9.47214  32.02863 1.000 28.65485  ? 174 LYS A CA  1 
ATOM   1398 C  C   . LYS A 1 179 ? 14.73926 -9.54672  33.53716 1.000 29.66322  ? 174 LYS A C   1 
ATOM   1399 O  O   . LYS A 1 179 ? 13.99584 -8.74176  34.11600 1.000 31.89977  ? 174 LYS A O   1 
ATOM   1400 C  CB  . LYS A 1 179 ? 13.96959 -10.41821 31.31501 1.000 31.75868  ? 174 LYS A CB  1 
ATOM   1401 C  CG  . LYS A 1 179 ? 12.50409 -10.05919 31.50620 1.000 37.55328  ? 174 LYS A CG  1 
ATOM   1402 C  CD  . LYS A 1 179 ? 11.61062 -11.03719 30.76579 1.000 43.03288  ? 174 LYS A CD  1 
ATOM   1403 C  CE  . LYS A 1 179 ? 10.14215 -10.73778 31.00847 1.000 46.12028  ? 174 LYS A CE  1 
ATOM   1404 N  NZ  . LYS A 1 179 ? 9.27881  -11.72260 30.30476 1.000 46.59509  ? 174 LYS A NZ  1 
ATOM   1405 N  N   . ARG A 1 180 ? 15.39468 -10.50709 34.19181 1.000 29.36659  ? 175 ARG A N   1 
ATOM   1406 C  CA  . ARG A 1 180 ? 15.34437 -10.56647 35.65076 1.000 28.79779  ? 175 ARG A CA  1 
ATOM   1407 C  C   . ARG A 1 180 ? 15.99385 -9.33297  36.26490 1.000 30.31645  ? 175 ARG A C   1 
ATOM   1408 O  O   . ARG A 1 180 ? 15.48891 -8.77569  37.24881 1.000 27.08882  ? 175 ARG A O   1 
ATOM   1409 C  CB  . ARG A 1 180 ? 16.02496 -11.84673 36.14703 1.000 32.26929  ? 175 ARG A CB  1 
ATOM   1410 C  CG  . ARG A 1 180 ? 16.29697 -11.87232 37.64695 1.000 34.74293  ? 175 ARG A CG  1 
ATOM   1411 C  CD  . ARG A 1 180 ? 17.15785 -13.06700 38.05806 1.000 43.08763  ? 175 ARG A CD  1 
ATOM   1412 N  NE  . ARG A 1 180 ? 18.40016 -13.12652 37.29575 1.000 44.16892  ? 175 ARG A NE  1 
ATOM   1413 C  CZ  . ARG A 1 180 ? 19.44572 -12.33733 37.50743 1.000 42.27370  ? 175 ARG A CZ  1 
ATOM   1414 N  NH1 . ARG A 1 180 ? 19.44622 -11.43309 38.47631 1.000 39.08738  ? 175 ARG A NH1 1 
ATOM   1415 N  NH2 . ARG A 1 180 ? 20.50932 -12.44274 36.71494 1.000 33.48544  ? 175 ARG A NH2 1 
ATOM   1416 N  N   . ILE A 1 181 ? 17.10956 -8.88231  35.68715 1.000 29.03647  ? 176 ILE A N   1 
ATOM   1417 C  CA  . ILE A 1 181 ? 17.75543 -7.65642  36.15330 1.000 26.40923  ? 176 ILE A CA  1 
ATOM   1418 C  C   . ILE A 1 181 ? 16.83267 -6.46171  35.96177 1.000 26.89527  ? 176 ILE A C   1 
ATOM   1419 O  O   . ILE A 1 181 ? 16.69973 -5.61069  36.85006 1.000 26.07407  ? 176 ILE A O   1 
ATOM   1420 C  CB  . ILE A 1 181 ? 19.09512 -7.44836  35.42457 1.000 23.86938  ? 176 ILE A CB  1 
ATOM   1421 C  CG1 . ILE A 1 181 ? 20.04821 -8.60038  35.74769 1.000 25.61575  ? 176 ILE A CG1 1 
ATOM   1422 C  CG2 . ILE A 1 181 ? 19.69635 -6.08786  35.79044 1.000 24.93496  ? 176 ILE A CG2 1 
ATOM   1423 C  CD1 . ILE A 1 181 ? 21.33454 -8.55701  34.94633 1.000 26.40189  ? 176 ILE A CD1 1 
ATOM   1424 N  N   . ARG A 1 182 ? 16.20218 -6.36673  34.78581 1.000 24.29476  ? 177 ARG A N   1 
ATOM   1425 C  CA  . ARG A 1 182 ? 15.24452 -5.29281  34.53890 1.000 26.91952  ? 177 ARG A CA  1 
ATOM   1426 C  C   . ARG A 1 182 ? 14.20884 -5.21787  35.65557 1.000 25.12622  ? 177 ARG A C   1 
ATOM   1427 O  O   . ARG A 1 182 ? 13.93585 -4.14090  36.19726 1.000 24.77491  ? 177 ARG A O   1 
ATOM   1428 C  CB  . ARG A 1 182 ? 14.55367 -5.50130  33.19088 1.000 23.83271  ? 177 ARG A CB  1 
ATOM   1429 C  CG  . ARG A 1 182 ? 13.45745 -4.48023  32.89593 1.000 25.68351  ? 177 ARG A CG  1 
ATOM   1430 C  CD  . ARG A 1 182 ? 12.45229 -5.02415  31.88590 1.000 27.41662  ? 177 ARG A CD  1 
ATOM   1431 N  NE  . ARG A 1 182 ? 11.56413 -6.02357  32.46895 1.000 29.80578  ? 177 ARG A NE  1 
ATOM   1432 C  CZ  . ARG A 1 182 ? 10.58177 -6.62228  31.80777 1.000 31.96802  ? 177 ARG A CZ  1 
ATOM   1433 N  NH1 . ARG A 1 182 ? 10.35048 -6.36552  30.52928 1.000 34.28225  ? 177 ARG A NH1 1 
ATOM   1434 N  NH2 . ARG A 1 182 ? 9.81094  -7.49823  32.44366 1.000 32.32700  ? 177 ARG A NH2 1 
ATOM   1435 N  N   . ASP A 1 183 ? 13.63136 -6.36168  36.01870 1.000 26.88852  ? 178 ASP A N   1 
ATOM   1436 C  CA  . ASP A 1 183 ? 12.60566 -6.37494  37.06203 1.000 27.83962  ? 178 ASP A CA  1 
ATOM   1437 C  C   . ASP A 1 183 ? 13.16445 -5.91198  38.40252 1.000 31.71646  ? 178 ASP A C   1 
ATOM   1438 O  O   . ASP A 1 183 ? 12.51426 -5.13558  39.11621 1.000 31.52995  ? 178 ASP A O   1 
ATOM   1439 C  CB  . ASP A 1 183 ? 11.99831 -7.77337  37.18586 1.000 31.63969  ? 178 ASP A CB  1 
ATOM   1440 C  CG  . ASP A 1 183 ? 11.11487 -8.13690  36.00455 1.000 37.66131  ? 178 ASP A CG  1 
ATOM   1441 O  OD1 . ASP A 1 183 ? 10.84149 -7.25457  35.16502 1.000 36.82198  ? 178 ASP A OD1 1 
ATOM   1442 O  OD2 . ASP A 1 183 ? 10.69813 -9.31037  35.91333 1.000 38.60191  ? 178 ASP A OD2 1 
ATOM   1443 N  N   . ASP A 1 184 ? 14.36315 -6.38102  38.77034 1.000 26.52119  ? 179 ASP A N   1 
ATOM   1444 C  CA  . ASP A 1 184 ? 14.94725 -5.97781  40.04918 1.000 31.26775  ? 179 ASP A CA  1 
ATOM   1445 C  C   . ASP A 1 184 ? 15.20720 -4.47789  40.09145 1.000 32.20107  ? 179 ASP A C   1 
ATOM   1446 O  O   . ASP A 1 184 ? 14.96638 -3.82378  41.11588 1.000 27.54387  ? 179 ASP A O   1 
ATOM   1447 C  CB  . ASP A 1 184 ? 16.24821 -6.73670  40.30605 1.000 29.34678  ? 179 ASP A CB  1 
ATOM   1448 C  CG  . ASP A 1 184 ? 16.01998 -8.17473  40.71869 1.000 37.83274  ? 179 ASP A CG  1 
ATOM   1449 O  OD1 . ASP A 1 184 ? 14.85598 -8.55837  40.94130 1.000 37.32397  ? 179 ASP A OD1 1 
ATOM   1450 O  OD2 . ASP A 1 184 ? 17.01528 -8.91983  40.81454 1.000 46.04429  ? 179 ASP A OD2 1 
ATOM   1451 N  N   . ILE A 1 185 ? 15.71320 -3.91433  38.99146 1.000 27.57416  ? 180 ILE A N   1 
ATOM   1452 C  CA  . ILE A 1 185 ? 16.00092 -2.48377  38.96543 1.000 24.40553  ? 180 ILE A CA  1 
ATOM   1453 C  C   . ILE A 1 185 ? 14.71906 -1.66621  39.04565 1.000 27.68322  ? 180 ILE A C   1 
ATOM   1454 O  O   . ILE A 1 185 ? 14.64704 -0.67219  39.78175 1.000 25.88114  ? 180 ILE A O   1 
ATOM   1455 C  CB  . ILE A 1 185 ? 16.81801 -2.12115  37.71126 1.000 22.43160  ? 180 ILE A CB  1 
ATOM   1456 C  CG1 . ILE A 1 185 ? 18.20094 -2.77014  37.77337 1.000 25.85874  ? 180 ILE A CG1 1 
ATOM   1457 C  CG2 . ILE A 1 185 ? 16.94631 -0.60622  37.58838 1.000 23.54158  ? 180 ILE A CG2 1 
ATOM   1458 C  CD1 . ILE A 1 185 ? 19.01775 -2.32694  38.96334 1.000 28.72006  ? 180 ILE A CD1 1 
ATOM   1459 N  N   . ILE A 1 186 ? 13.68730 -2.05655  38.29409 1.000 27.17225  ? 181 ILE A N   1 
ATOM   1460 C  CA  . ILE A 1 186 ? 12.48073 -1.23379  38.28495 1.000 32.84589  ? 181 ILE A CA  1 
ATOM   1461 C  C   . ILE A 1 186 ? 11.74814 -1.32322  39.61832 1.000 30.88917  ? 181 ILE A C   1 
ATOM   1462 O  O   . ILE A 1 186 ? 11.04118 -0.38600  40.00314 1.000 28.90720  ? 181 ILE A O   1 
ATOM   1463 C  CB  . ILE A 1 186 ? 11.55723 -1.62367  37.12063 1.000 34.48060  ? 181 ILE A CB  1 
ATOM   1464 C  CG1 . ILE A 1 186 ? 11.15336 -3.08284  37.25597 1.000 48.25115  ? 181 ILE A CG1 1 
ATOM   1465 C  CG2 . ILE A 1 186 ? 12.22405 -1.33716  35.77899 1.000 38.73141  ? 181 ILE A CG2 1 
ATOM   1466 C  CD1 . ILE A 1 186 ? 10.32951 -3.58381  36.13631 1.000 65.68064  ? 181 ILE A CD1 1 
ATOM   1467 N  N   . GLN A 1 187 ? 11.88592 -2.43985  40.33837 1.000 28.92628  ? 182 GLN A N   1 
ATOM   1468 C  CA  . GLN A 1 187 ? 11.30753 -2.51590  41.67937 1.000 29.14096  ? 182 GLN A CA  1 
ATOM   1469 C  C   . GLN A 1 187 ? 12.01382 -1.56449  42.63581 1.000 32.41644  ? 182 GLN A C   1 
ATOM   1470 O  O   . GLN A 1 187 ? 11.36528 -0.90476  43.45611 1.000 29.79843  ? 182 GLN A O   1 
ATOM   1471 C  CB  . GLN A 1 187 ? 11.37696 -3.94630  42.21128 1.000 31.71516  ? 182 GLN A CB  1 
ATOM   1472 C  CG  . GLN A 1 187 ? 10.51395 -4.93489  41.46295 1.000 39.18735  ? 182 GLN A CG  1 
ATOM   1473 C  CD  . GLN A 1 187 ? 10.59588 -6.32632  42.05397 1.000 52.98930  ? 182 GLN A CD  1 
ATOM   1474 O  OE1 . GLN A 1 187 ? 11.56198 -7.05620  41.82701 1.000 51.90766  ? 182 GLN A OE1 1 
ATOM   1475 N  NE2 . GLN A 1 187 ? 9.58275  -6.69968  42.82409 1.000 52.03912  ? 182 GLN A NE2 1 
ATOM   1476 N  N   . ALA A 1 188 ? 13.34424 -1.49169  42.55295 1.000 27.47428  ? 183 ALA A N   1 
ATOM   1477 C  CA  . ALA A 1 188 ? 14.09691 -0.54958  43.37646 1.000 27.61082  ? 183 ALA A CA  1 
ATOM   1478 C  C   . ALA A 1 188 ? 13.77789 0.89149   43.00551 1.000 29.68751  ? 183 ALA A C   1 
ATOM   1479 O  O   . ALA A 1 188 ? 13.71361 1.76398   43.88073 1.000 29.10264  ? 183 ALA A O   1 
ATOM   1480 C  CB  . ALA A 1 188 ? 15.59883 -0.81390  43.24212 1.000 28.50289  ? 183 ALA A CB  1 
ATOM   1481 N  N   . MET A 1 189 ? 13.58585 1.16881   41.71106 1.000 24.98166  ? 184 MET A N   1 
ATOM   1482 C  CA  . MET A 1 189 ? 13.23339 2.52698   41.30428 1.000 24.63271  ? 184 MET A CA  1 
ATOM   1483 C  C   . MET A 1 189 ? 11.84290 2.91420   41.80190 1.000 28.73419  ? 184 MET A C   1 
ATOM   1484 O  O   . MET A 1 189 ? 11.62280 4.05987   42.21515 1.000 27.36307  ? 184 MET A O   1 
ATOM   1485 C  CB  . MET A 1 189 ? 13.32250 2.65933   39.78588 1.000 27.17231  ? 184 MET A CB  1 
ATOM   1486 C  CG  . MET A 1 189 ? 14.72485 2.48003   39.25356 1.000 23.75343  ? 184 MET A CG  1 
ATOM   1487 S  SD  . MET A 1 189 ? 14.79252 2.73386   37.48201 1.000 29.50633  ? 184 MET A SD  1 
ATOM   1488 C  CE  . MET A 1 189 ? 14.22396 4.42246   37.38036 1.000 32.60231  ? 184 MET A CE  1 
ATOM   1489 N  N   . ALA A 1 190 ? 10.89179 1.97776   41.77611 1.000 28.09689  ? 185 ALA A N   1 
ATOM   1490 C  CA  . ALA A 1 190 ? 9.56365  2.28453   42.30209 1.000 34.04607  ? 185 ALA A CA  1 
ATOM   1491 C  C   . ALA A 1 190 ? 9.62807  2.63288   43.78358 1.000 36.61855  ? 185 ALA A C   1 
ATOM   1492 O  O   . ALA A 1 190 ? 8.93587  3.54666   44.24590 1.000 35.82168  ? 185 ALA A O   1 
ATOM   1493 C  CB  . ALA A 1 190 ? 8.61278  1.11024   42.06848 1.000 36.96649  ? 185 ALA A CB  1 
ATOM   1494 N  N   . LYS A 1 191 ? 10.46080 1.92171   44.54374 1.000 33.63518  ? 186 LYS A N   1 
ATOM   1495 C  CA  . LYS A 1 191 ? 10.60574 2.23261   45.96211 1.000 36.64574  ? 186 LYS A CA  1 
ATOM   1496 C  C   . LYS A 1 191 ? 11.25248 3.59627   46.16382 1.000 38.00019  ? 186 LYS A C   1 
ATOM   1497 O  O   . LYS A 1 191 ? 10.86312 4.34408   47.06689 1.000 34.24022  ? 186 LYS A O   1 
ATOM   1498 C  CB  . LYS A 1 191 ? 11.42265 1.14612   46.66305 1.000 35.16680  ? 186 LYS A CB  1 
ATOM   1499 C  CG  . LYS A 1 191 ? 10.75780 -0.21401  46.72473 1.000 47.76196  ? 186 LYS A CG  1 
ATOM   1500 C  CD  . LYS A 1 191 ? 11.72105 -1.23992  47.30858 1.000 49.54035  ? 186 LYS A CD  1 
ATOM   1501 C  CE  . LYS A 1 191 ? 11.09427 -2.61768  47.41484 1.000 54.29322  ? 186 LYS A CE  1 
ATOM   1502 N  NZ  . LYS A 1 191 ? 12.12073 -3.63788  47.76989 1.000 64.57885  ? 186 LYS A NZ  1 
ATOM   1503 N  N   . LEU A 1 192 ? 12.24652 3.93771   45.33822 1.000 31.20160  ? 187 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 192 ? 12.85791 5.25886   45.43795 1.000 28.85797  ? 187 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 192 ? 11.84664 6.36064   45.16745 1.000 33.19297  ? 187 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 192 ? 11.92495 7.43910   45.76804 1.000 35.53276  ? 187 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 192 ? 14.02669 5.38308   44.46025 1.000 27.54101  ? 187 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 192 ? 15.29466 4.58156   44.74422 1.000 26.92797  ? 187 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 192 ? 16.29371 4.85266   43.64432 1.000 24.58733  ? 187 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 192 ? 15.89450 4.95794   46.06948 1.000 32.41719  ? 187 LEU A CD2 1 
ATOM   1511 N  N   . LEU A 1 193 ? 10.89676 6.10860   44.27182 1.000 30.14785  ? 188 LEU A N   1 
ATOM   1512 C  CA  . LEU A 1 193 ? 9.87938  7.07845   43.89899 1.000 35.25479  ? 188 LEU A CA  1 
ATOM   1513 C  C   . LEU A 1 193 ? 8.64552  7.00821   44.78382 1.000 32.74034  ? 188 LEU A C   1 
ATOM   1514 O  O   . LEU A 1 193 ? 7.71234  7.79265   44.57929 1.000 32.78798  ? 188 LEU A O   1 
ATOM   1515 C  CB  . LEU A 1 193 ? 9.47923  6.87081   42.43756 1.000 33.61419  ? 188 LEU A CB  1 
ATOM   1516 C  CG  . LEU A 1 193 ? 10.61431 7.07998   41.43354 1.000 28.28748  ? 188 LEU A CG  1 
ATOM   1517 C  CD1 . LEU A 1 193 ? 10.27024 6.45006   40.09856 1.000 26.63529  ? 188 LEU A CD1 1 
ATOM   1518 C  CD2 . LEU A 1 193 ? 10.91365 8.56781   41.27472 1.000 30.49964  ? 188 LEU A CD2 1 
ATOM   1519 N  N   . GLU A 1 194 ? 8.62512  6.09614   45.75873 1.000 35.64230  ? 189 GLU A N   1 
ATOM   1520 C  CA  . GLU A 1 194 ? 7.47286  5.89110   46.63748 1.000 41.18733  ? 189 GLU A CA  1 
ATOM   1521 C  C   . GLU A 1 194 ? 6.21199  5.60392   45.82861 1.000 41.07959  ? 189 GLU A C   1 
ATOM   1522 O  O   . GLU A 1 194 ? 5.11774  6.06237   46.16161 1.000 37.77732  ? 189 GLU A O   1 
ATOM   1523 C  CB  . GLU A 1 194 ? 7.26452  7.08016   47.57795 1.000 40.65257  ? 189 GLU A CB  1 
ATOM   1524 C  CG  . GLU A 1 194 ? 8.48766  7.41514   48.42367 1.000 49.50945  ? 189 GLU A CG  1 
ATOM   1525 C  CD  . GLU A 1 194 ? 8.17417  8.36401   49.56516 1.000 57.04241  ? 189 GLU A CD  1 
ATOM   1526 O  OE1 . GLU A 1 194 ? 7.21774  8.09317   50.32070 1.000 64.10467  ? 189 GLU A OE1 1 
ATOM   1527 O  OE2 . GLU A 1 194 ? 8.88191  9.38449   49.70311 1.000 70.92786  ? 189 GLU A OE2 1 
ATOM   1528 N  N   . LEU A 1 195 ? 6.37507  4.85060   44.74696 1.000 35.63523  ? 190 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 195 ? 5.27360  4.30566   43.97217 1.000 36.57261  ? 190 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 195 ? 5.16539  2.81721   44.26264 1.000 47.81200  ? 190 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 195 ? 6.11576  2.19675   44.74732 1.000 45.09950  ? 190 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 195 ? 5.48236  4.53824   42.47232 1.000 35.91913  ? 190 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 195 ? 5.66165  5.99416   42.03684 1.000 30.02589  ? 190 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 195 ? 6.14448  6.04905   40.59505 1.000 37.55892  ? 190 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 195 ? 4.35915  6.77008   42.19490 1.000 34.07463  ? 190 LEU A CD2 1 
ATOM   1536 N  N   . ASP A 1 196 ? 3.99421  2.24988   43.97037 1.000 38.95592  ? 191 ASP A N   1 
ATOM   1537 C  CA  . ASP A 1 196 ? 3.78798  0.82053   44.17777 1.000 56.79776  ? 191 ASP A CA  1 
ATOM   1538 C  C   . ASP A 1 196 ? 4.90390  0.03162   43.51033 1.000 63.93020  ? 191 ASP A C   1 
ATOM   1539 O  O   . ASP A 1 196 ? 5.21324  0.25067   42.33746 1.000 59.72834  ? 191 ASP A O   1 
ATOM   1540 C  CB  . ASP A 1 196 ? 2.42943  0.38607   43.62249 1.000 51.16884  ? 191 ASP A CB  1 
ATOM   1541 C  CG  . ASP A 1 196 ? 2.29091  -1.12875  43.53702 1.000 73.37564  ? 191 ASP A CG  1 
ATOM   1542 O  OD1 . ASP A 1 196 ? 2.28418  -1.79069  44.59662 1.000 81.05262  ? 191 ASP A OD1 1 
ATOM   1543 O  OD2 . ASP A 1 196 ? 2.19141  -1.65959  42.40962 1.000 74.12499  ? 191 ASP A OD2 1 
ATOM   1544 N  N   . GLU A 1 197 ? 5.51530  -0.88149  44.27418 1.000 70.01200  ? 192 GLU A N   1 
ATOM   1545 C  CA  . GLU A 1 197 ? 6.70043  -1.59186  43.80211 1.000 73.31790  ? 192 GLU A CA  1 
ATOM   1546 C  C   . GLU A 1 197 ? 6.47932  -2.27179  42.45757 1.000 69.00940  ? 192 GLU A C   1 
ATOM   1547 O  O   . GLU A 1 197 ? 7.45182  -2.53550  41.74242 1.000 67.50843  ? 192 GLU A O   1 
ATOM   1548 C  CB  . GLU A 1 197 ? 7.14902  -2.62551  44.84154 1.000 80.27935  ? 192 GLU A CB  1 
ATOM   1549 C  CG  . GLU A 1 197 ? 6.19187  -3.79612  45.01863 1.000 90.26644  ? 192 GLU A CG  1 
ATOM   1550 C  CD  . GLU A 1 197 ? 6.76595  -4.89588  45.89527 1.000 95.80471  ? 192 GLU A CD  1 
ATOM   1551 O  OE1 . GLU A 1 197 ? 7.19246  -4.59415  47.03019 1.000 100.57328 ? 192 GLU A OE1 1 
ATOM   1552 O  OE2 . GLU A 1 197 ? 6.79838  -6.06204  45.44574 1.000 94.63712  ? 192 GLU A OE2 1 
ATOM   1553 N  N   . ASP A 1 198 ? 5.22644  -2.54738  42.09200 1.000 67.90142  ? 193 ASP A N   1 
ATOM   1554 C  CA  . ASP A 1 198 ? 4.88422  -3.13301  40.80422 1.000 73.38968  ? 193 ASP A CA  1 
ATOM   1555 C  C   . ASP A 1 198 ? 4.27804  -2.11737  39.83743 1.000 62.00398  ? 193 ASP A C   1 
ATOM   1556 O  O   . ASP A 1 198 ? 3.58493  -2.51435  38.89551 1.000 68.66763  ? 193 ASP A O   1 
ATOM   1557 C  CB  . ASP A 1 198 ? 3.91740  -4.30592  40.99817 1.000 75.91760  ? 193 ASP A CB  1 
ATOM   1558 C  CG  . ASP A 1 198 ? 4.51563  -5.43750  41.82226 1.000 77.26184  ? 193 ASP A CG  1 
ATOM   1559 O  OD1 . ASP A 1 198 ? 5.72786  -5.38726  42.11713 1.000 72.00605  ? 193 ASP A OD1 1 
ATOM   1560 O  OD2 . ASP A 1 198 ? 3.77026  -6.37850  42.17394 1.000 68.77316  ? 193 ASP A OD2 1 
ATOM   1561 N  N   . TYR A 1 199 ? 4.51111  -0.81762  40.05226 1.000 72.54720  ? 194 TYR A N   1 
ATOM   1562 C  CA  . TYR A 1 199 ? 3.89924  0.18876   39.18499 1.000 57.54076  ? 194 TYR A CA  1 
ATOM   1563 C  C   . TYR A 1 199 ? 4.38315  0.04995   37.74678 1.000 43.56936  ? 194 TYR A C   1 
ATOM   1564 O  O   . TYR A 1 199 ? 3.61225  0.23619   36.79726 1.000 44.66485  ? 194 TYR A O   1 
ATOM   1565 C  CB  . TYR A 1 199 ? 4.19435  1.59983   39.69864 1.000 58.72533  ? 194 TYR A CB  1 
ATOM   1566 C  CG  . TYR A 1 199 ? 3.72879  2.67199   38.73936 1.000 47.30778  ? 194 TYR A CG  1 
ATOM   1567 C  CD1 . TYR A 1 199 ? 2.38885  3.00745   38.65779 1.000 56.81301  ? 194 TYR A CD1 1 
ATOM   1568 C  CD2 . TYR A 1 199 ? 4.62477  3.33357   37.89927 1.000 47.57469  ? 194 TYR A CD2 1 
ATOM   1569 C  CE1 . TYR A 1 199 ? 1.94360  3.97203   37.78268 1.000 53.57538  ? 194 TYR A CE1 1 
ATOM   1570 C  CE2 . TYR A 1 199 ? 4.18499  4.30688   37.01058 1.000 44.43995  ? 194 TYR A CE2 1 
ATOM   1571 C  CZ  . TYR A 1 199 ? 2.83409  4.62033   36.96439 1.000 53.30376  ? 194 TYR A CZ  1 
ATOM   1572 O  OH  . TYR A 1 199 ? 2.35040  5.57716   36.10344 1.000 43.19624  ? 194 TYR A OH  1 
ATOM   1573 N  N   . PHE A 1 200 ? 5.65796  -0.26342  37.56418 1.000 51.75851  ? 195 PHE A N   1 
ATOM   1574 C  CA  . PHE A 1 200 ? 6.17674  -0.40324  36.21347 1.000 42.53695  ? 195 PHE A CA  1 
ATOM   1575 C  C   . PHE A 1 200 ? 5.91469  -1.79333  35.65253 1.000 46.21312  ? 195 PHE A C   1 
ATOM   1576 O  O   . PHE A 1 200 ? 5.85349  -1.96255  34.42966 1.000 48.42552  ? 195 PHE A O   1 
ATOM   1577 C  CB  . PHE A 1 200 ? 7.66751  -0.07818  36.20601 1.000 43.92432  ? 195 PHE A CB  1 
ATOM   1578 C  CG  . PHE A 1 200 ? 7.97868  1.31467   36.67174 1.000 40.60718  ? 195 PHE A CG  1 
ATOM   1579 C  CD1 . PHE A 1 200 ? 7.84896  2.38884   35.80769 1.000 34.52311  ? 195 PHE A CD1 1 
ATOM   1580 C  CD2 . PHE A 1 200 ? 8.39466  1.55378   37.97222 1.000 47.90191  ? 195 PHE A CD2 1 
ATOM   1581 C  CE1 . PHE A 1 200 ? 8.12851  3.67681   36.22857 1.000 36.42602  ? 195 PHE A CE1 1 
ATOM   1582 C  CE2 . PHE A 1 200 ? 8.68093  2.84147   38.39755 1.000 47.22324  ? 195 PHE A CE2 1 
ATOM   1583 C  CZ  . PHE A 1 200 ? 8.54700  3.90339   37.52121 1.000 35.06010  ? 195 PHE A CZ  1 
ATOM   1584 N  N   . LEU A 1 201 ? 5.73067  -2.78718  36.52451 1.000 55.78900  ? 196 LEU A N   1 
ATOM   1585 C  CA  . LEU A 1 201 ? 5.51547  -4.15385  36.05900 1.000 54.34679  ? 196 LEU A CA  1 
ATOM   1586 C  C   . LEU A 1 201 ? 4.22215  -4.28702  35.26506 1.000 49.34313  ? 196 LEU A C   1 
ATOM   1587 O  O   . LEU A 1 201 ? 4.15074  -5.09351  34.33163 1.000 48.22407  ? 196 LEU A O   1 
ATOM   1588 C  CB  . LEU A 1 201 ? 5.51780  -5.11431  37.24779 1.000 53.04246  ? 196 LEU A CB  1 
ATOM   1589 C  CG  . LEU A 1 201 ? 6.88140  -5.32908  37.90928 1.000 56.84226  ? 196 LEU A CG  1 
ATOM   1590 C  CD1 . LEU A 1 201 ? 6.74622  -6.17430  39.16199 1.000 63.54899  ? 196 LEU A CD1 1 
ATOM   1591 C  CD2 . LEU A 1 201 ? 7.83904  -5.98722  36.93312 1.000 57.98029  ? 196 LEU A CD2 1 
ATOM   1592 N  N   . ASP A 1 202 ? 3.19754  -3.50273  35.60757 1.000 52.30979  ? 197 ASP A N   1 
ATOM   1593 C  CA  . ASP A 1 202 ? 1.93751  -3.57135  34.87276 1.000 44.21167  ? 197 ASP A CA  1 
ATOM   1594 C  C   . ASP A 1 202 ? 2.12085  -3.17355  33.41385 1.000 48.04524  ? 197 ASP A C   1 
ATOM   1595 O  O   . ASP A 1 202 ? 1.55719  -3.80738  32.51373 1.000 47.40957  ? 197 ASP A O   1 
ATOM   1596 C  CB  . ASP A 1 202 ? 0.89004  -2.67964  35.53739 1.000 52.63191  ? 197 ASP A CB  1 
ATOM   1597 C  CG  . ASP A 1 202 ? -0.16371 -3.47588  36.27831 1.000 58.32444  ? 197 ASP A CG  1 
ATOM   1598 O  OD1 . ASP A 1 202 ? 0.05149  -4.68781  36.48622 1.000 56.76729  ? 197 ASP A OD1 1 
ATOM   1599 O  OD2 . ASP A 1 202 ? -1.20912 -2.89515  36.64138 1.000 60.86620  ? 197 ASP A OD2 1 
ATOM   1600 N  N   . ARG A 1 203 ? 2.90066  -2.12633  33.15883 1.000 39.73928  ? 198 ARG A N   1 
ATOM   1601 C  CA  . ARG A 1 203 ? 3.13406  -1.66050  31.79786 1.000 42.30259  ? 198 ARG A CA  1 
ATOM   1602 C  C   . ARG A 1 203 ? 4.19934  -2.46991  31.07237 1.000 40.48566  ? 198 ARG A C   1 
ATOM   1603 O  O   . ARG A 1 203 ? 4.52861  -2.15041  29.92428 1.000 38.24663  ? 198 ARG A O   1 
ATOM   1604 C  CB  . ARG A 1 203 ? 3.51424  -0.17788  31.81354 1.000 41.50040  ? 198 ARG A CB  1 
ATOM   1605 C  CG  . ARG A 1 203 ? 2.31342  0.73605   32.03424 1.000 45.89627  ? 198 ARG A CG  1 
ATOM   1606 C  CD  . ARG A 1 203 ? 2.71287  2.08322   32.61206 1.000 49.43405  ? 198 ARG A CD  1 
ATOM   1607 N  NE  . ARG A 1 203 ? 1.54449  2.90114   32.91778 1.000 50.13481  ? 198 ARG A NE  1 
ATOM   1608 C  CZ  . ARG A 1 203 ? 0.82130  2.78749   34.02329 1.000 52.49034  ? 198 ARG A CZ  1 
ATOM   1609 N  NH1 . ARG A 1 203 ? 1.13481  1.91522   34.96664 1.000 57.16377  ? 198 ARG A NH1 1 
ATOM   1610 N  NH2 . ARG A 1 203 ? -0.24792 3.56344   34.18274 1.000 63.24684  ? 198 ARG A NH2 1 
ATOM   1611 N  N   . LEU A 1 204 ? 4.73859  -3.50671  31.70538 1.000 41.00480  ? 199 LEU A N   1 
ATOM   1612 C  CA  . LEU A 1 204 ? 5.70292  -4.38867  31.06870 1.000 40.17128  ? 199 LEU A CA  1 
ATOM   1613 C  C   . LEU A 1 204 ? 5.11312  -5.74057  30.70339 1.000 43.42870  ? 199 LEU A C   1 
ATOM   1614 O  O   . LEU A 1 204 ? 5.82865  -6.58745  30.15889 1.000 38.81426  ? 199 LEU A O   1 
ATOM   1615 C  CB  . LEU A 1 204 ? 6.91753  -4.57160  31.97816 1.000 41.13432  ? 199 LEU A CB  1 
ATOM   1616 C  CG  . LEU A 1 204 ? 7.70815  -3.27322  32.10186 1.000 40.13016  ? 199 LEU A CG  1 
ATOM   1617 C  CD1 . LEU A 1 204 ? 8.83429  -3.43460  33.07433 1.000 40.10767  ? 199 LEU A CD1 1 
ATOM   1618 C  CD2 . LEU A 1 204 ? 8.23492  -2.87257  30.73762 1.000 36.86152  ? 199 LEU A CD2 1 
ATOM   1619 N  N   . ASN A 1 205 ? 3.83047  -5.96289  30.98072 1.000 45.18842  ? 200 ASN A N   1 
ATOM   1620 C  CA  . ASN A 1 205 ? 3.18745  -7.21340  30.60641 1.000 43.55262  ? 200 ASN A CA  1 
ATOM   1621 C  C   . ASN A 1 205 ? 3.15705  -7.35368  29.08856 1.000 43.03856  ? 200 ASN A C   1 
ATOM   1622 O  O   . ASN A 1 205 ? 2.61760  -6.49141  28.38627 1.000 43.69209  ? 200 ASN A O   1 
ATOM   1623 C  CB  . ASN A 1 205 ? 1.77502  -7.26368  31.18698 1.000 50.03684  ? 200 ASN A CB  1 
ATOM   1624 C  CG  . ASN A 1 205 ? 1.00793  -8.48709  30.74172 1.000 53.39940  ? 200 ASN A CG  1 
ATOM   1625 O  OD1 . ASN A 1 205 ? 1.44865  -9.61847  30.94471 1.000 60.99871  ? 200 ASN A OD1 1 
ATOM   1626 N  ND2 . ASN A 1 205 ? -0.15453 -8.26813  30.13767 1.000 62.55292  ? 200 ASN A ND2 1 
ATOM   1627 N  N   . GLU A 1 206 ? 3.75619  -8.43573  28.58741 1.000 38.29205  ? 201 GLU A N   1 
ATOM   1628 C  CA  . GLU A 1 206 ? 3.84712  -8.70049  27.15008 1.000 38.93066  ? 201 GLU A CA  1 
ATOM   1629 C  C   . GLU A 1 206 ? 4.48334  -7.52574  26.40979 1.000 40.28442  ? 201 GLU A C   1 
ATOM   1630 O  O   . GLU A 1 206 ? 4.11926  -7.20408  25.27726 1.000 46.45712  ? 201 GLU A O   1 
ATOM   1631 C  CB  . GLU A 1 206 ? 2.47453  -9.03148  26.56252 1.000 53.91293  ? 201 GLU A CB  1 
ATOM   1632 C  CG  . GLU A 1 206 ? 1.77282  -10.20416 27.22427 1.000 55.35340  ? 201 GLU A CG  1 
ATOM   1633 C  CD  . GLU A 1 206 ? 0.46173  -10.54839 26.54415 1.000 71.35554  ? 201 GLU A CD  1 
ATOM   1634 O  OE1 . GLU A 1 206 ? 0.08889  -9.84563  25.58014 1.000 76.19640  ? 201 GLU A OE1 1 
ATOM   1635 O  OE2 . GLU A 1 206 ? -0.19533 -11.52217 26.97007 1.000 81.03271  ? 201 GLU A OE2 1 
ATOM   1636 N  N   . ALA A 1 207 ? 5.43876  -6.87695  27.05765 1.000 37.67437  ? 202 ALA A N   1 
ATOM   1637 C  CA  . ALA A 1 207 ? 6.03884  -5.69513  26.46372 1.000 39.44179  ? 202 ALA A CA  1 
ATOM   1638 C  C   . ALA A 1 207 ? 7.13027  -6.08431  25.46905 1.000 39.59937  ? 202 ALA A C   1 
ATOM   1639 O  O   . ALA A 1 207 ? 7.79021  -7.11441  25.63099 1.000 34.29814  ? 202 ALA A O   1 
ATOM   1640 C  CB  . ALA A 1 207 ? 6.62325  -4.79500  27.54498 1.000 39.88467  ? 202 ALA A CB  1 
ATOM   1641 N  N   . PRO A 1 208 ? 7.33218  -5.27981  24.42741 1.000 36.63977  ? 203 PRO A N   1 
ATOM   1642 C  CA  . PRO A 1 208 ? 8.40480  -5.57637  23.47145 1.000 34.67568  ? 203 PRO A CA  1 
ATOM   1643 C  C   . PRO A 1 208 ? 9.77857  -5.31413  24.07101 1.000 36.38184  ? 203 PRO A C   1 
ATOM   1644 O  O   . PRO A 1 208 ? 9.97893  -4.36573  24.83416 1.000 32.43538  ? 203 PRO A O   1 
ATOM   1645 C  CB  . PRO A 1 208 ? 8.11292  -4.62768  22.30408 1.000 40.21360  ? 203 PRO A CB  1 
ATOM   1646 C  CG  . PRO A 1 208 ? 7.32696  -3.51014  22.91455 1.000 40.77088  ? 203 PRO A CG  1 
ATOM   1647 C  CD  . PRO A 1 208 ? 6.51099  -4.13074  24.00738 1.000 39.05213  ? 203 PRO A CD  1 
ATOM   1648 N  N   . ALA A 1 209 ? 10.72455 -6.18178  23.72138 1.000 35.16098  ? 204 ALA A N   1 
ATOM   1649 C  CA  . ALA A 1 209 ? 12.12401 -6.03458  24.08931 1.000 28.80316  ? 204 ALA A CA  1 
ATOM   1650 C  C   . ALA A 1 209 ? 12.97130 -6.43155  22.89098 1.000 30.17812  ? 204 ALA A C   1 
ATOM   1651 O  O   . ALA A 1 209 ? 12.59053 -7.31098  22.11717 1.000 31.15935  ? 204 ALA A O   1 
ATOM   1652 C  CB  . ALA A 1 209 ? 12.49521 -6.89457  25.30219 1.000 33.95708  ? 204 ALA A CB  1 
ATOM   1653 N  N   . PHE A 1 210 ? 14.11956 -5.77579  22.73757 1.000 31.65610  ? 205 PHE A N   1 
ATOM   1654 C  CA  . PHE A 1 210 ? 14.95041 -5.96847  21.55794 1.000 27.16468  ? 205 PHE A CA  1 
ATOM   1655 C  C   . PHE A 1 210 ? 16.40212 -6.17550  21.95397 1.000 27.95705  ? 205 PHE A C   1 
ATOM   1656 O  O   . PHE A 1 210 ? 16.85405 -5.70701  22.99925 1.000 24.57661  ? 205 PHE A O   1 
ATOM   1657 C  CB  . PHE A 1 210 ? 14.85135 -4.77141  20.60179 1.000 27.14727  ? 205 PHE A CB  1 
ATOM   1658 C  CG  . PHE A 1 210 ? 13.44424 -4.40265  20.24171 1.000 30.83136  ? 205 PHE A CG  1 
ATOM   1659 C  CD1 . PHE A 1 210 ? 12.70836 -3.55026  21.05465 1.000 32.20549  ? 205 PHE A CD1 1 
ATOM   1660 C  CD2 . PHE A 1 210 ? 12.85172 -4.91187  19.09933 1.000 34.62619  ? 205 PHE A CD2 1 
ATOM   1661 C  CE1 . PHE A 1 210 ? 11.41119 -3.21199  20.72821 1.000 34.87975  ? 205 PHE A CE1 1 
ATOM   1662 C  CE2 . PHE A 1 210 ? 11.55536 -4.57109  18.76671 1.000 38.66797  ? 205 PHE A CE2 1 
ATOM   1663 C  CZ  . PHE A 1 210 ? 10.83551 -3.72219  19.58241 1.000 35.84108  ? 205 PHE A CZ  1 
ATOM   1664 N  N   . ALA A 1 211 ? 17.12463 -6.89501  21.10113 1.000 28.27123  ? 206 ALA A N   1 
ATOM   1665 C  CA  . ALA A 1 211 ? 18.56859 -7.05356  21.20829 1.000 24.45815  ? 206 ALA A CA  1 
ATOM   1666 C  C   . ALA A 1 211 ? 19.18481 -6.30946  20.03207 1.000 32.13305  ? 206 ALA A C   1 
ATOM   1667 O  O   . ALA A 1 211 ? 18.95508 -6.67922  18.87573 1.000 31.68821  ? 206 ALA A O   1 
ATOM   1668 C  CB  . ALA A 1 211 ? 18.96126 -8.52972  21.19055 1.000 27.33942  ? 206 ALA A CB  1 
ATOM   1669 N  N   . ARG A 1 212 ? 19.94459 -5.25279  20.31947 1.000 25.25406  ? 207 ARG A N   1 
ATOM   1670 C  CA  . ARG A 1 212 ? 20.63663 -4.48684  19.28612 1.000 22.78851  ? 207 ARG A CA  1 
ATOM   1671 C  C   . ARG A 1 212 ? 22.12278 -4.80784  19.37768 1.000 24.37607  ? 207 ARG A C   1 
ATOM   1672 O  O   . ARG A 1 212 ? 22.81083 -4.33717  20.28905 1.000 24.73832  ? 207 ARG A O   1 
ATOM   1673 C  CB  . ARG A 1 212 ? 20.38776 -2.98410  19.43319 1.000 21.88776  ? 207 ARG A CB  1 
ATOM   1674 C  CG  . ARG A 1 212 ? 21.01152 -2.13777  18.31174 1.000 21.42264  ? 207 ARG A CG  1 
ATOM   1675 C  CD  . ARG A 1 212 ? 20.74971 -0.62991  18.50617 1.000 23.32687  ? 207 ARG A CD  1 
ATOM   1676 N  NE  . ARG A 1 212 ? 21.47283 0.14812   17.50346 1.000 22.26555  ? 207 ARG A NE  1 
ATOM   1677 C  CZ  . ARG A 1 212 ? 20.91156 0.78771   16.48595 1.000 31.36254  ? 207 ARG A CZ  1 
ATOM   1678 N  NH1 . ARG A 1 212 ? 19.59623 0.85818   16.34967 1.000 24.93255  ? 207 ARG A NH1 1 
ATOM   1679 N  NH2 . ARG A 1 212 ? 21.69136 1.37146   15.57935 1.000 27.90628  ? 207 ARG A NH2 1 
ATOM   1680 N  N   . PHE A 1 213 ? 22.60908 -5.61620  18.44124 1.000 26.59611  ? 208 PHE A N   1 
ATOM   1681 C  CA  . PHE A 1 213 ? 24.03175 -5.91607  18.32280 1.000 26.34928  ? 208 PHE A CA  1 
ATOM   1682 C  C   . PHE A 1 213 ? 24.66735 -4.84670  17.44518 1.000 25.57317  ? 208 PHE A C   1 
ATOM   1683 O  O   . PHE A 1 213 ? 24.49053 -4.86370  16.22418 1.000 27.56723  ? 208 PHE A O   1 
ATOM   1684 C  CB  . PHE A 1 213 ? 24.25747 -7.29529  17.70718 1.000 25.21870  ? 208 PHE A CB  1 
ATOM   1685 C  CG  . PHE A 1 213 ? 23.79401 -8.44204  18.56062 1.000 27.61411  ? 208 PHE A CG  1 
ATOM   1686 C  CD1 . PHE A 1 213 ? 22.48400 -8.89670  18.49034 1.000 27.71600  ? 208 PHE A CD1 1 
ATOM   1687 C  CD2 . PHE A 1 213 ? 24.68590 -9.10284  19.39155 1.000 27.10505  ? 208 PHE A CD2 1 
ATOM   1688 C  CE1 . PHE A 1 213 ? 22.06455 -9.97611  19.26036 1.000 28.51005  ? 208 PHE A CE1 1 
ATOM   1689 C  CE2 . PHE A 1 213 ? 24.27339 -10.18161 20.16459 1.000 31.66720  ? 208 PHE A CE2 1 
ATOM   1690 C  CZ  . PHE A 1 213 ? 22.96134 -10.61855 20.09578 1.000 28.82432  ? 208 PHE A CZ  1 
ATOM   1691 N  N   . ASN A 1 214 ? 25.40972 -3.92900  18.05807 1.000 25.84342  ? 209 ASN A N   1 
ATOM   1692 C  CA  . ASN A 1 214 ? 26.11236 -2.88632  17.31754 1.000 26.24960  ? 209 ASN A CA  1 
ATOM   1693 C  C   . ASN A 1 214 ? 27.49104 -3.36407  16.88083 1.000 27.80299  ? 209 ASN A C   1 
ATOM   1694 O  O   . ASN A 1 214 ? 28.20823 -4.00815  17.65168 1.000 27.04176  ? 209 ASN A O   1 
ATOM   1695 C  CB  . ASN A 1 214 ? 26.26520 -1.62995  18.17123 1.000 23.97516  ? 209 ASN A CB  1 
ATOM   1696 C  CG  . ASN A 1 214 ? 24.94267 -1.02499  18.55218 1.000 25.33988  ? 209 ASN A CG  1 
ATOM   1697 O  OD1 . ASN A 1 214 ? 24.22983 -0.48558  17.69866 1.000 26.63118  ? 209 ASN A OD1 1 
ATOM   1698 N  ND2 . ASN A 1 214 ? 24.60280 -1.09612  19.84087 1.000 22.39711  ? 209 ASN A ND2 1 
ATOM   1699 N  N   . TYR A 1 215 ? 27.86593 -3.02119  15.64554 1.000 26.66639  ? 210 TYR A N   1 
ATOM   1700 C  CA  . TYR A 1 215 ? 29.20946 -3.26469  15.12859 1.000 24.07498  ? 210 TYR A CA  1 
ATOM   1701 C  C   . TYR A 1 215 ? 29.77396 -1.95807  14.59301 1.000 27.93017  ? 210 TYR A C   1 
ATOM   1702 O  O   . TYR A 1 215 ? 29.25393 -1.41066  13.61670 1.000 27.14220  ? 210 TYR A O   1 
ATOM   1703 C  CB  . TYR A 1 215 ? 29.20521 -4.32907  14.02720 1.000 27.03750  ? 210 TYR A CB  1 
ATOM   1704 C  CG  . TYR A 1 215 ? 30.58906 -4.72816  13.54744 1.000 30.74751  ? 210 TYR A CG  1 
ATOM   1705 C  CD1 . TYR A 1 215 ? 31.23507 -4.01614  12.53892 1.000 26.96521  ? 210 TYR A CD1 1 
ATOM   1706 C  CD2 . TYR A 1 215 ? 31.25014 -5.81801  14.10238 1.000 30.27737  ? 210 TYR A CD2 1 
ATOM   1707 C  CE1 . TYR A 1 215 ? 32.49588 -4.38369  12.09599 1.000 32.72421  ? 210 TYR A CE1 1 
ATOM   1708 C  CE2 . TYR A 1 215 ? 32.51124 -6.19301  13.66199 1.000 33.64287  ? 210 TYR A CE2 1 
ATOM   1709 C  CZ  . TYR A 1 215 ? 33.12734 -5.47081  12.66304 1.000 31.37331  ? 210 TYR A CZ  1 
ATOM   1710 O  OH  . TYR A 1 215 ? 34.38170 -5.83372  12.22780 1.000 33.14048  ? 210 TYR A OH  1 
ATOM   1711 N  N   . TYR A 1 216 ? 30.84387 -1.47308  15.21908 1.000 25.18023  ? 211 TYR A N   1 
ATOM   1712 C  CA  . TYR A 1 216 ? 31.49822 -0.23129  14.81970 1.000 29.48201  ? 211 TYR A CA  1 
ATOM   1713 C  C   . TYR A 1 216 ? 32.81245 -0.57065  14.13190 1.000 28.22682  ? 211 TYR A C   1 
ATOM   1714 O  O   . TYR A 1 216 ? 33.79969 -0.89210  14.81291 1.000 30.33099  ? 211 TYR A O   1 
ATOM   1715 C  CB  . TYR A 1 216 ? 31.74416 0.66247   16.04121 1.000 24.88379  ? 211 TYR A CB  1 
ATOM   1716 C  CG  . TYR A 1 216 ? 30.50663 0.88981   16.88631 1.000 25.52291  ? 211 TYR A CG  1 
ATOM   1717 C  CD1 . TYR A 1 216 ? 29.63702 1.93716   16.60927 1.000 28.18123  ? 211 TYR A CD1 1 
ATOM   1718 C  CD2 . TYR A 1 216 ? 30.20882 0.05927   17.95964 1.000 25.80609  ? 211 TYR A CD2 1 
ATOM   1719 C  CE1 . TYR A 1 216 ? 28.50364 2.14720   17.36393 1.000 24.62086  ? 211 TYR A CE1 1 
ATOM   1720 C  CE2 . TYR A 1 216 ? 29.07247 0.26954   18.73589 1.000 24.09734  ? 211 TYR A CE2 1 
ATOM   1721 C  CZ  . TYR A 1 216 ? 28.22429 1.31082   18.42805 1.000 25.15702  ? 211 TYR A CZ  1 
ATOM   1722 O  OH  . TYR A 1 216 ? 27.09221 1.53801   19.16820 1.000 26.60597  ? 211 TYR A OH  1 
ATOM   1723 N  N   . PRO A 1 217 ? 32.88340 -0.54137  12.80308 1.000 32.39529  ? 212 PRO A N   1 
ATOM   1724 C  CA  . PRO A 1 217 ? 34.15346 -0.81668  12.12489 1.000 32.95512  ? 212 PRO A CA  1 
ATOM   1725 C  C   . PRO A 1 217 ? 35.15701 0.28154   12.42012 1.000 31.72057  ? 212 PRO A C   1 
ATOM   1726 O  O   . PRO A 1 217 ? 34.77312 1.38764   12.83385 1.000 31.28779  ? 212 PRO A O   1 
ATOM   1727 C  CB  . PRO A 1 217 ? 33.77465 -0.83795  10.63101 1.000 31.09838  ? 212 PRO A CB  1 
ATOM   1728 C  CG  . PRO A 1 217 ? 32.27693 -0.95312  10.59771 1.000 29.58284  ? 212 PRO A CG  1 
ATOM   1729 C  CD  . PRO A 1 217 ? 31.79198 -0.27590  11.85135 1.000 28.84055  ? 212 PRO A CD  1 
ATOM   1730 N  N   . PRO A 1 218 ? 36.44906 0.02019   12.23649 1.000 37.00732  ? 213 PRO A N   1 
ATOM   1731 C  CA  . PRO A 1 218 ? 37.41906 1.11231   12.31621 1.000 36.79599  ? 213 PRO A CA  1 
ATOM   1732 C  C   . PRO A 1 218 ? 37.07910 2.17112   11.28228 1.000 37.59183  ? 213 PRO A C   1 
ATOM   1733 O  O   . PRO A 1 218 ? 36.52127 1.87743   10.22207 1.000 31.41315  ? 213 PRO A O   1 
ATOM   1734 C  CB  . PRO A 1 218 ? 38.75887 0.42934   12.01771 1.000 41.38941  ? 213 PRO A CB  1 
ATOM   1735 C  CG  . PRO A 1 218 ? 38.39380 -0.82734  11.29943 1.000 44.23191  ? 213 PRO A CG  1 
ATOM   1736 C  CD  . PRO A 1 218 ? 37.08510 -1.25579  11.87054 1.000 30.97364  ? 213 PRO A CD  1 
ATOM   1737 N  N   . CYS A 1 219 ? 37.37909 3.42079   11.62093 1.000 39.75535  ? 214 CYS A N   1 
ATOM   1738 C  CA  . CYS A 1 219 ? 37.14106 4.52968   10.71739 1.000 37.99787  ? 214 CYS A CA  1 
ATOM   1739 C  C   . CYS A 1 219 ? 38.44625 5.26241   10.45781 1.000 38.47054  ? 214 CYS A C   1 
ATOM   1740 O  O   . CYS A 1 219 ? 39.15533 5.60625   11.41477 1.000 42.63772  ? 214 CYS A O   1 
ATOM   1741 C  CB  . CYS A 1 219 ? 36.10274 5.50484   11.29986 1.000 37.86292  ? 214 CYS A CB  1 
ATOM   1742 S  SG  . CYS A 1 219 ? 35.72352 6.88732   10.20143 1.000 39.74829  ? 214 CYS A SG  1 
ATOM   1743 N  N   . PRO A 1 220 ? 38.79915 5.52958   9.19629  1.000 37.44813  ? 215 PRO A N   1 
ATOM   1744 C  CA  . PRO A 1 220 ? 40.06474 6.22536   8.92255  1.000 38.37158  ? 215 PRO A CA  1 
ATOM   1745 C  C   . PRO A 1 220 ? 40.08314 7.66242   9.41152  1.000 49.18679  ? 215 PRO A C   1 
ATOM   1746 O  O   . PRO A 1 220 ? 41.17064 8.23352   9.54501  1.000 46.74771  ? 215 PRO A O   1 
ATOM   1747 C  CB  . PRO A 1 220 ? 40.18406 6.14961   7.39570  1.000 47.50505  ? 215 PRO A CB  1 
ATOM   1748 C  CG  . PRO A 1 220 ? 38.78017 5.99285   6.91653  1.000 43.13827  ? 215 PRO A CG  1 
ATOM   1749 C  CD  . PRO A 1 220 ? 38.07592 5.17774   7.96139  1.000 34.39819  ? 215 PRO A CD  1 
ATOM   1750 N  N   . ARG A 1 221 ? 38.92402 8.25991   9.68965  1.000 39.77581  ? 216 ARG A N   1 
ATOM   1751 C  CA  . ARG A 1 221 ? 38.82729 9.62267   10.21223 1.000 40.05467  ? 216 ARG A CA  1 
ATOM   1752 C  C   . ARG A 1 221 ? 37.84124 9.63153   11.37350 1.000 42.65303  ? 216 ARG A C   1 
ATOM   1753 O  O   . ARG A 1 221 ? 36.70697 10.10443  11.24063 1.000 38.20220  ? 216 ARG A O   1 
ATOM   1754 C  CB  . ARG A 1 221 ? 38.39641 10.60615  9.12262  1.000 39.79360  ? 216 ARG A CB  1 
ATOM   1755 C  CG  . ARG A 1 221 ? 39.42744 10.81856  8.03493  1.000 52.89646  ? 216 ARG A CG  1 
ATOM   1756 C  CD  . ARG A 1 221 ? 40.69212 11.42613  8.61181  1.000 51.13809  ? 216 ARG A CD  1 
ATOM   1757 N  NE  . ARG A 1 221 ? 40.42642 12.68958  9.29068  1.000 54.26553  ? 216 ARG A NE  1 
ATOM   1758 C  CZ  . ARG A 1 221 ? 40.51336 13.88142  8.71547  1.000 56.09936  ? 216 ARG A CZ  1 
ATOM   1759 N  NH1 . ARG A 1 221 ? 40.84805 14.01134  7.44192  1.000 48.44987  ? 216 ARG A NH1 1 
ATOM   1760 N  NH2 . ARG A 1 221 ? 40.26326 14.97030  9.43728  1.000 51.56052  ? 216 ARG A NH2 1 
ATOM   1761 N  N   . PRO A 1 222 ? 38.24785 9.11513   12.53647 1.000 43.83143  ? 217 PRO A N   1 
ATOM   1762 C  CA  . PRO A 1 222 ? 37.31753 9.06013   13.67589 1.000 42.16036  ? 217 PRO A CA  1 
ATOM   1763 C  C   . PRO A 1 222 ? 36.90191 10.43148  14.18622 1.000 36.00400  ? 217 PRO A C   1 
ATOM   1764 O  O   . PRO A 1 222 ? 35.92631 10.52133  14.93971 1.000 39.70467  ? 217 PRO A O   1 
ATOM   1765 C  CB  . PRO A 1 222 ? 38.09972 8.27385   14.73579 1.000 42.80237  ? 217 PRO A CB  1 
ATOM   1766 C  CG  . PRO A 1 222 ? 39.52063 8.40450   14.35852 1.000 43.72045  ? 217 PRO A CG  1 
ATOM   1767 C  CD  . PRO A 1 222 ? 39.57567 8.56378   12.86151 1.000 41.26501  ? 217 PRO A CD  1 
ATOM   1768 N  N   . ASP A 1 223 ? 37.59301 11.49867  13.78531 1.000 39.37568  ? 218 ASP A N   1 
ATOM   1769 C  CA  . ASP A 1 223 ? 37.19609 12.85018  14.15560 1.000 43.05641  ? 218 ASP A CA  1 
ATOM   1770 C  C   . ASP A 1 223 ? 36.03622 13.38297  13.32544 1.000 40.41951  ? 218 ASP A C   1 
ATOM   1771 O  O   . ASP A 1 223 ? 35.50054 14.44579  13.65614 1.000 46.06856  ? 218 ASP A O   1 
ATOM   1772 C  CB  . ASP A 1 223 ? 38.38679 13.80386  14.01922 1.000 43.07563  ? 218 ASP A CB  1 
ATOM   1773 C  CG  . ASP A 1 223 ? 38.92326 13.86677  12.59784 1.000 48.04922  ? 218 ASP A CG  1 
ATOM   1774 O  OD1 . ASP A 1 223 ? 39.04378 12.80036  11.95902 1.000 46.98160  ? 218 ASP A OD1 1 
ATOM   1775 O  OD2 . ASP A 1 223 ? 39.22129 14.98176  12.11637 1.000 54.32029  ? 218 ASP A OD2 1 
ATOM   1776 N  N   . LEU A 1 224 ? 35.63278 12.68315  12.26606 1.000 37.26006  ? 219 LEU A N   1 
ATOM   1777 C  CA  . LEU A 1 224 ? 34.67867 13.22146  11.30664 1.000 37.01644  ? 219 LEU A CA  1 
ATOM   1778 C  C   . LEU A 1 224 ? 33.32455 12.52676  11.32844 1.000 35.31026  ? 219 LEU A C   1 
ATOM   1779 O  O   . LEU A 1 224 ? 32.42055 12.95327  10.60375 1.000 39.64300  ? 219 LEU A O   1 
ATOM   1780 C  CB  . LEU A 1 224 ? 35.26157 13.15478  9.88937  1.000 34.12515  ? 219 LEU A CB  1 
ATOM   1781 C  CG  . LEU A 1 224 ? 36.52672 13.97261  9.62196  1.000 46.11295  ? 219 LEU A CG  1 
ATOM   1782 C  CD1 . LEU A 1 224 ? 36.86880 13.95258  8.14321  1.000 44.77290  ? 219 LEU A CD1 1 
ATOM   1783 C  CD2 . LEU A 1 224 ? 36.36601 15.40346  10.11340 1.000 50.34924  ? 219 LEU A CD2 1 
ATOM   1784 N  N   . VAL A 1 225 ? 33.15194 11.47284  12.13009 1.000 37.22883  ? 220 VAL A N   1 
ATOM   1785 C  CA  . VAL A 1 225 ? 31.91504 10.70139  12.16459 1.000 31.23055  ? 220 VAL A CA  1 
ATOM   1786 C  C   . VAL A 1 225 ? 31.59109 10.35423  13.61269 1.000 32.82144  ? 220 VAL A C   1 
ATOM   1787 O  O   . VAL A 1 225 ? 32.38805 10.58001  14.52410 1.000 33.25845  ? 220 VAL A O   1 
ATOM   1788 C  CB  . VAL A 1 225 ? 32.00426 9.40361   11.32840 1.000 29.88408  ? 220 VAL A CB  1 
ATOM   1789 C  CG1 . VAL A 1 225 ? 32.53717 9.67845   9.92146  1.000 35.15209  ? 220 VAL A CG1 1 
ATOM   1790 C  CG2 . VAL A 1 225 ? 32.85744 8.36185   12.06192 1.000 31.80574  ? 220 VAL A CG2 1 
ATOM   1791 N  N   . PHE A 1 226 ? 30.39412 9.80662   13.81640 1.000 34.11803  ? 221 PHE A N   1 
ATOM   1792 C  CA  . PHE A 1 226 ? 30.04236 9.10230   15.04035 1.000 29.06685  ? 221 PHE A CA  1 
ATOM   1793 C  C   . PHE A 1 226 ? 29.78205 7.63598   14.72474 1.000 30.99339  ? 221 PHE A C   1 
ATOM   1794 O  O   . PHE A 1 226 ? 29.18105 7.31353   13.69521 1.000 29.57392  ? 221 PHE A O   1 
ATOM   1795 C  CB  . PHE A 1 226 ? 28.79475 9.70074   15.71467 1.000 25.85386  ? 221 PHE A CB  1 
ATOM   1796 C  CG  . PHE A 1 226 ? 29.03858 11.03082  16.37924 1.000 29.37195  ? 221 PHE A CG  1 
ATOM   1797 C  CD1 . PHE A 1 226 ? 30.08961 11.19442  17.26805 1.000 32.08558  ? 221 PHE A CD1 1 
ATOM   1798 C  CD2 . PHE A 1 226 ? 28.22292 12.11614  16.10957 1.000 37.42256  ? 221 PHE A CD2 1 
ATOM   1799 C  CE1 . PHE A 1 226 ? 30.31678 12.41725  17.88577 1.000 35.25052  ? 221 PHE A CE1 1 
ATOM   1800 C  CE2 . PHE A 1 226 ? 28.44943 13.34877  16.71937 1.000 38.15368  ? 221 PHE A CE2 1 
ATOM   1801 C  CZ  . PHE A 1 226 ? 29.49900 13.49503  17.60510 1.000 33.17681  ? 221 PHE A CZ  1 
ATOM   1802 N  N   . GLY A 1 227 ? 30.23300 6.75179   15.61838 1.000 27.89365  ? 222 GLY A N   1 
ATOM   1803 C  CA  . GLY A 1 227 ? 29.84194 5.35310   15.51580 1.000 27.60064  ? 222 GLY A CA  1 
ATOM   1804 C  C   . GLY A 1 227 ? 28.34732 5.17563   15.69039 1.000 27.99298  ? 222 GLY A C   1 
ATOM   1805 O  O   . GLY A 1 227 ? 27.69306 4.47591   14.91372 1.000 27.77420  ? 222 GLY A O   1 
ATOM   1806 N  N   . ILE A 1 228 ? 27.78808 5.80435   16.72221 1.000 26.89674  ? 223 ILE A N   1 
ATOM   1807 C  CA  . ILE A 1 228 ? 26.35219 6.03513   16.81159 1.000 28.38316  ? 223 ILE A CA  1 
ATOM   1808 C  C   . ILE A 1 228 ? 26.15417 7.45408   17.32452 1.000 26.30124  ? 223 ILE A C   1 
ATOM   1809 O  O   . ILE A 1 228 ? 26.87226 7.91332   18.22081 1.000 26.19011  ? 223 ILE A O   1 
ATOM   1810 C  CB  . ILE A 1 228 ? 25.62931 4.98281   17.68654 1.000 33.36122  ? 223 ILE A CB  1 
ATOM   1811 C  CG1 . ILE A 1 228 ? 24.10675 5.12796   17.54962 1.000 25.95249  ? 223 ILE A CG1 1 
ATOM   1812 C  CG2 . ILE A 1 228 ? 26.05003 5.06102   19.14948 1.000 25.45804  ? 223 ILE A CG2 1 
ATOM   1813 C  CD1 . ILE A 1 228 ? 23.32937 3.98437   18.19409 1.000 30.25404  ? 223 ILE A CD1 1 
ATOM   1814 N  N   . ARG A 1 229 ? 25.20964 8.16305   16.71091 1.000 25.30237  ? 224 ARG A N   1 
ATOM   1815 C  CA  . ARG A 1 229 ? 25.02234 9.58225   16.96333 1.000 26.87282  ? 224 ARG A CA  1 
ATOM   1816 C  C   . ARG A 1 229 ? 24.61003 9.82398   18.41487 1.000 25.40260  ? 224 ARG A C   1 
ATOM   1817 O  O   . ARG A 1 229 ? 24.08098 8.92886   19.07577 1.000 27.87229  ? 224 ARG A O   1 
ATOM   1818 C  CB  . ARG A 1 229 ? 23.95009 10.13292  16.02589 1.000 24.95273  ? 224 ARG A CB  1 
ATOM   1819 C  CG  . ARG A 1 229 ? 22.55396 9.59827   16.34483 1.000 30.55861  ? 224 ARG A CG  1 
ATOM   1820 C  CD  . ARG A 1 229 ? 21.63701 9.76061   15.15759 1.000 38.19701  ? 224 ARG A CD  1 
ATOM   1821 N  NE  . ARG A 1 229 ? 22.24420 9.17018   13.97303 1.000 34.09763  ? 224 ARG A NE  1 
ATOM   1822 C  CZ  . ARG A 1 229 ? 21.90232 9.46551   12.72714 1.000 37.09845  ? 224 ARG A CZ  1 
ATOM   1823 N  NH1 . ARG A 1 229 ? 20.93018 10.32287  12.46041 1.000 37.15987  ? 224 ARG A NH1 1 
ATOM   1824 N  NH2 . ARG A 1 229 ? 22.55309 8.88653   11.72414 1.000 34.17863  ? 224 ARG A NH2 1 
ATOM   1825 N  N   . PRO A 1 230 ? 24.84442 11.03037  18.93176 1.000 24.67325  ? 225 PRO A N   1 
ATOM   1826 C  CA  . PRO A 1 230 ? 24.29340 11.38015  20.24524 1.000 22.97331  ? 225 PRO A CA  1 
ATOM   1827 C  C   . PRO A 1 230 ? 22.79781 11.13018  20.27562 1.000 27.12732  ? 225 PRO A C   1 
ATOM   1828 O  O   . PRO A 1 230 ? 22.05581 11.56682  19.39273 1.000 27.09883  ? 225 PRO A O   1 
ATOM   1829 C  CB  . PRO A 1 230 ? 24.62311 12.87029  20.38434 1.000 26.42341  ? 225 PRO A CB  1 
ATOM   1830 C  CG  . PRO A 1 230 ? 25.81806 13.06190  19.54031 1.000 33.63586  ? 225 PRO A CG  1 
ATOM   1831 C  CD  . PRO A 1 230 ? 25.65918 12.12160  18.37664 1.000 30.56703  ? 225 PRO A CD  1 
ATOM   1832 N  N   . HIS A 1 231 ? 22.35990 10.40365  21.29642 1.000 25.98009  ? 226 HIS A N   1 
ATOM   1833 C  CA  . HIS A 1 231 ? 20.95652 10.06106  21.42576 1.000 27.02449  ? 226 HIS A CA  1 
ATOM   1834 C  C   . HIS A 1 231 ? 20.69671 9.66297   22.86598 1.000 28.27095  ? 226 HIS A C   1 
ATOM   1835 O  O   . HIS A 1 231 ? 21.60968 9.26815   23.59793 1.000 26.73236  ? 226 HIS A O   1 
ATOM   1836 C  CB  . HIS A 1 231 ? 20.56648 8.91555   20.48571 1.000 27.70064  ? 226 HIS A CB  1 
ATOM   1837 C  CG  . HIS A 1 231 ? 21.14847 7.59473   20.88320 1.000 29.62150  ? 226 HIS A CG  1 
ATOM   1838 N  ND1 . HIS A 1 231 ? 22.44650 7.23176   20.58829 1.000 26.33990  ? 226 HIS A ND1 1 
ATOM   1839 C  CD2 . HIS A 1 231 ? 20.61135 6.55216   21.56071 1.000 25.16946  ? 226 HIS A CD2 1 
ATOM   1840 C  CE1 . HIS A 1 231 ? 22.68249 6.02364   21.06844 1.000 26.75276  ? 226 HIS A CE1 1 
ATOM   1841 N  NE2 . HIS A 1 231 ? 21.58658 5.59187   21.67052 1.000 23.51940  ? 226 HIS A NE2 1 
ATOM   1842 N  N   . SER A 1 232 ? 19.44085 9.79333   23.26731 1.000 23.78738  ? 227 SER A N   1 
ATOM   1843 C  CA  . SER A 1 232 ? 18.93652 9.07612   24.42335 1.000 26.58974  ? 227 SER A CA  1 
ATOM   1844 C  C   . SER A 1 232 ? 18.11559 7.90138   23.91850 1.000 27.07861  ? 227 SER A C   1 
ATOM   1845 O  O   . SER A 1 232 ? 17.50176 7.97290   22.85122 1.000 27.38283  ? 227 SER A O   1 
ATOM   1846 C  CB  . SER A 1 232 ? 18.08540 9.98007   25.31953 1.000 31.24285  ? 227 SER A CB  1 
ATOM   1847 O  OG  . SER A 1 232 ? 16.97896 10.50234  24.60730 1.000 31.31437  ? 227 SER A OG  1 
ATOM   1848 N  N   . ASP A 1 233 ? 18.13812 6.80144   24.66662 1.000 25.18452  ? 228 ASP A N   1 
ATOM   1849 C  CA  . ASP A 1 233 ? 17.30666 5.66791   24.29636 1.000 22.40591  ? 228 ASP A CA  1 
ATOM   1850 C  C   . ASP A 1 233 ? 15.83800 6.00162   24.54224 1.000 26.22386  ? 228 ASP A C   1 
ATOM   1851 O  O   . ASP A 1 233 ? 15.49232 6.74861   25.46432 1.000 29.11361  ? 228 ASP A O   1 
ATOM   1852 C  CB  . ASP A 1 233 ? 17.70333 4.41953   25.09060 1.000 22.95455  ? 228 ASP A CB  1 
ATOM   1853 C  CG  . ASP A 1 233 ? 19.10238 3.91787   24.75015 1.000 27.64945  ? 228 ASP A CG  1 
ATOM   1854 O  OD1 . ASP A 1 233 ? 19.68227 4.35976   23.73092 1.000 25.62436  ? 228 ASP A OD1 1 
ATOM   1855 O  OD2 . ASP A 1 233 ? 19.61685 3.06810   25.50459 1.000 25.19043  ? 228 ASP A OD2 1 
ATOM   1856 N  N   . GLY A 1 234 ? 14.96516 5.44296   23.70521 1.000 25.42000  ? 229 GLY A N   1 
ATOM   1857 C  CA  . GLY A 1 234 ? 13.54236 5.63513   23.90194 1.000 28.12860  ? 229 GLY A CA  1 
ATOM   1858 C  C   . GLY A 1 234 ? 12.89545 4.65112   24.85423 1.000 26.82977  ? 229 GLY A C   1 
ATOM   1859 O  O   . GLY A 1 234 ? 11.68408 4.71946   25.08416 1.000 26.42352  ? 229 GLY A O   1 
ATOM   1860 N  N   . THR A 1 235 ? 13.68613 3.74919   25.42997 1.000 25.22065  ? 230 THR A N   1 
ATOM   1861 C  CA  . THR A 1 235 ? 13.18804 2.62010   26.19967 1.000 22.56599  ? 230 THR A CA  1 
ATOM   1862 C  C   . THR A 1 235 ? 12.65683 3.07070   27.55470 1.000 23.28638  ? 230 THR A C   1 
ATOM   1863 O  O   . THR A 1 235 ? 12.73132 4.24216   27.93016 1.000 24.94232  ? 230 THR A O   1 
ATOM   1864 C  CB  . THR A 1 235 ? 14.31051 1.62250   26.43509 1.000 24.55696  ? 230 THR A CB  1 
ATOM   1865 O  OG1 . THR A 1 235 ? 15.41381 2.33400   27.01640 1.000 22.13075  ? 230 THR A OG1 1 
ATOM   1866 C  CG2 . THR A 1 235 ? 14.74887 0.96939   25.11860 1.000 25.67978  ? 230 THR A CG2 1 
ATOM   1867 N  N   . LEU A 1 236 ? 12.13208 2.10289   28.30936 1.000 22.73676  ? 231 LEU A N   1 
ATOM   1868 C  CA  . LEU A 1 236 ? 12.01571 2.28306   29.75199 1.000 23.53165  ? 231 LEU A CA  1 
ATOM   1869 C  C   . LEU A 1 236 ? 13.38192 2.11129   30.40577 1.000 24.76111  ? 231 LEU A C   1 
ATOM   1870 O  O   . LEU A 1 236 ? 13.84814 2.98428   31.14836 1.000 25.46496  ? 231 LEU A O   1 
ATOM   1871 C  CB  . LEU A 1 236 ? 11.00465 1.28693   30.32883 1.000 22.88834  ? 231 LEU A CB  1 
ATOM   1872 C  CG  . LEU A 1 236 ? 10.61653 1.46253   31.79952 1.000 26.85473  ? 231 LEU A CG  1 
ATOM   1873 C  CD1 . LEU A 1 236 ? 9.72780  2.69675   31.98508 1.000 26.76208  ? 231 LEU A CD1 1 
ATOM   1874 C  CD2 . LEU A 1 236 ? 9.93273  0.20706   32.36615 1.000 26.34834  ? 231 LEU A CD2 1 
ATOM   1875 N  N   . LEU A 1 237 ? 14.06239 1.01185   30.08710 1.000 25.59449  ? 232 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 237 ? 15.38135 0.69844   30.61301 1.000 22.94700  ? 232 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 237 ? 16.20124 0.04279   29.50802 1.000 22.39454  ? 232 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 237 ? 15.65893 -0.71465  28.70044 1.000 23.97249  ? 232 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 237 ? 15.26314 -0.24846  31.81632 1.000 26.91518  ? 232 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 237 ? 16.42718 -0.37409  32.78937 1.000 33.66357  ? 232 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 237 ? 16.48399 0.84577   33.69372 1.000 31.81087  ? 232 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 237 ? 16.30016 -1.65005  33.61272 1.000 33.16572  ? 232 LEU A CD2 1 
ATOM   1883 N  N   . THR A 1 238 ? 17.49982 0.33172   29.47098 1.000 20.84034  ? 233 THR A N   1 
ATOM   1884 C  CA  . THR A 1 238 ? 18.42277 -0.35876  28.57573 1.000 22.47361  ? 233 THR A CA  1 
ATOM   1885 C  C   . THR A 1 238 ? 19.50299 -1.03181  29.41146 1.000 19.97110  ? 233 THR A C   1 
ATOM   1886 O  O   . THR A 1 238 ? 20.02697 -0.44069  30.36047 1.000 22.46769  ? 233 THR A O   1 
ATOM   1887 C  CB  . THR A 1 238 ? 19.05484 0.60230   27.56561 1.000 21.73288  ? 233 THR A CB  1 
ATOM   1888 O  OG1 . THR A 1 238 ? 18.02959 1.20461   26.76134 1.000 24.97028  ? 233 THR A OG1 1 
ATOM   1889 C  CG2 . THR A 1 238 ? 20.05069 -0.13629  26.65060 1.000 24.08849  ? 233 THR A CG2 1 
ATOM   1890 N  N   . ILE A 1 239 ? 19.82361 -2.27550  29.07496 1.000 23.01195  ? 234 ILE A N   1 
ATOM   1891 C  CA  . ILE A 1 239 ? 20.87797 -3.01996  29.75120 1.000 21.85867  ? 234 ILE A CA  1 
ATOM   1892 C  C   . ILE A 1 239 ? 21.95119 -3.31190  28.70979 1.000 23.75378  ? 234 ILE A C   1 
ATOM   1893 O  O   . ILE A 1 239 ? 21.72264 -4.09094  27.77365 1.000 23.08614  ? 234 ILE A O   1 
ATOM   1894 C  CB  . ILE A 1 239 ? 20.34505 -4.30187  30.39918 1.000 23.10780  ? 234 ILE A CB  1 
ATOM   1895 C  CG1 . ILE A 1 239 ? 19.30232 -3.93780  31.47140 1.000 21.58150  ? 234 ILE A CG1 1 
ATOM   1896 C  CG2 . ILE A 1 239 ? 21.49127 -5.13098  30.96837 1.000 26.05910  ? 234 ILE A CG2 1 
ATOM   1897 C  CD1 . ILE A 1 239 ? 18.66157 -5.13434  32.14013 1.000 23.67634  ? 234 ILE A CD1 1 
ATOM   1898 N  N   . LEU A 1 240 ? 23.11822 -2.69167  28.87120 1.000 20.24580  ? 235 LEU A N   1 
ATOM   1899 C  CA  . LEU A 1 240 ? 24.13014 -2.61876  27.81934 1.000 21.83172  ? 235 LEU A CA  1 
ATOM   1900 C  C   . LEU A 1 240 ? 25.37275 -3.40590  28.21045 1.000 23.43359  ? 235 LEU A C   1 
ATOM   1901 O  O   . LEU A 1 240 ? 25.87817 -3.26519  29.32993 1.000 22.58199  ? 235 LEU A O   1 
ATOM   1902 C  CB  . LEU A 1 240 ? 24.50568 -1.16138  27.53904 1.000 21.14514  ? 235 LEU A CB  1 
ATOM   1903 C  CG  . LEU A 1 240 ? 25.57310 -0.86902  26.48184 1.000 24.03639  ? 235 LEU A CG  1 
ATOM   1904 C  CD1 . LEU A 1 240 ? 25.04719 -1.21484  25.10891 1.000 24.04025  ? 235 LEU A CD1 1 
ATOM   1905 C  CD2 . LEU A 1 240 ? 26.00010 0.60217   26.54201 1.000 21.61714  ? 235 LEU A CD2 1 
ATOM   1906 N  N   . LEU A 1 241 ? 25.87357 -4.21243  27.27435 1.000 22.97847  ? 236 LEU A N   1 
ATOM   1907 C  CA  . LEU A 1 241 ? 27.11256 -4.96652  27.43579 1.000 21.89095  ? 236 LEU A CA  1 
ATOM   1908 C  C   . LEU A 1 241 ? 28.08722 -4.47012  26.37549 1.000 26.23541  ? 236 LEU A C   1 
ATOM   1909 O  O   . LEU A 1 241 ? 27.85191 -4.65831  25.17592 1.000 25.47639  ? 236 LEU A O   1 
ATOM   1910 C  CB  . LEU A 1 241 ? 26.85602 -6.46673  27.29673 1.000 24.37041  ? 236 LEU A CB  1 
ATOM   1911 C  CG  . LEU A 1 241 ? 28.05077 -7.41424  27.42615 1.000 29.28036  ? 236 LEU A CG  1 
ATOM   1912 C  CD1 . LEU A 1 241 ? 28.86682 -7.10808  28.68494 1.000 31.83835  ? 236 LEU A CD1 1 
ATOM   1913 C  CD2 . LEU A 1 241 ? 27.56253 -8.86291  27.41951 1.000 25.97961  ? 236 LEU A CD2 1 
ATOM   1914 N  N   . VAL A 1 242 ? 29.16831 -3.82499  26.80597 1.000 27.14137  ? 237 VAL A N   1 
ATOM   1915 C  CA  . VAL A 1 242 ? 30.08405 -3.17315  25.87922 1.000 27.76320  ? 237 VAL A CA  1 
ATOM   1916 C  C   . VAL A 1 242 ? 31.27901 -4.07409  25.61087 1.000 33.18602  ? 237 VAL A C   1 
ATOM   1917 O  O   . VAL A 1 242 ? 31.61639 -4.97271  26.38933 1.000 24.14366  ? 237 VAL A O   1 
ATOM   1918 C  CB  . VAL A 1 242 ? 30.55770 -1.78640  26.38269 1.000 25.72459  ? 237 VAL A CB  1 
ATOM   1919 C  CG1 . VAL A 1 242 ? 29.38574 -0.82767  26.51017 1.000 27.74399  ? 237 VAL A CG1 1 
ATOM   1920 C  CG2 . VAL A 1 242 ? 31.28972 -1.91578  27.70489 1.000 33.69969  ? 237 VAL A CG2 1 
ATOM   1921 N  N   . ASP A 1 243 ? 31.90487 -3.83858  24.45890 1.000 27.89444  ? 238 ASP A N   1 
ATOM   1922 C  CA  . ASP A 1 243 ? 33.20418 -4.39373  24.11714 1.000 29.61694  ? 238 ASP A CA  1 
ATOM   1923 C  C   . ASP A 1 243 ? 34.14533 -4.31228  25.30721 1.000 30.05646  ? 238 ASP A C   1 
ATOM   1924 O  O   . ASP A 1 243 ? 34.29645 -3.25305  25.92103 1.000 27.94242  ? 238 ASP A O   1 
ATOM   1925 C  CB  . ASP A 1 243 ? 33.77771 -3.59970  22.93993 1.000 28.01404  ? 238 ASP A CB  1 
ATOM   1926 C  CG  . ASP A 1 243 ? 34.83634 -4.35463  22.17027 1.000 37.88030  ? 238 ASP A CG  1 
ATOM   1927 O  OD1 . ASP A 1 243 ? 35.85763 -4.76846  22.76378 1.000 32.40775  ? 238 ASP A OD1 1 
ATOM   1928 O  OD2 . ASP A 1 243 ? 34.64419 -4.51237  20.94888 1.000 32.02442  ? 238 ASP A OD2 1 
ATOM   1929 N  N   . LYS A 1 244 ? 34.77567 -5.43588  25.64157 1.000 31.66332  ? 239 LYS A N   1 
ATOM   1930 C  CA  . LYS A 1 244 ? 35.66286 -5.40959  26.79430 1.000 31.76773  ? 239 LYS A CA  1 
ATOM   1931 C  C   . LYS A 1 244 ? 37.04788 -4.87597  26.46239 1.000 32.72445  ? 239 LYS A C   1 
ATOM   1932 O  O   . LYS A 1 244 ? 37.79701 -4.54970  27.38718 1.000 32.58537  ? 239 LYS A O   1 
ATOM   1933 C  CB  . LYS A 1 244 ? 35.78386 -6.80276  27.41257 1.000 33.87619  ? 239 LYS A CB  1 
ATOM   1934 C  CG  . LYS A 1 244 ? 36.50749 -7.82061  26.56138 1.000 35.65985  ? 239 LYS A CG  1 
ATOM   1935 C  CD  . LYS A 1 244 ? 36.66067 -9.13587  27.31517 1.000 39.34645  ? 239 LYS A CD  1 
ATOM   1936 C  CE  . LYS A 1 244 ? 37.37026 -10.18321 26.46790 1.000 39.81738  ? 239 LYS A CE  1 
ATOM   1937 N  NZ  . LYS A 1 244 ? 38.79815 -9.84148  26.21039 1.000 35.78288  ? 239 LYS A NZ  1 
ATOM   1938 N  N   . ASP A 1 245 ? 37.39854 -4.76338  25.17758 1.000 28.82353  ? 240 ASP A N   1 
ATOM   1939 C  CA  . ASP A 1 245 ? 38.73656 -4.36193  24.76117 1.000 34.10806  ? 240 ASP A CA  1 
ATOM   1940 C  C   . ASP A 1 245 ? 38.81919 -2.96073  24.18053 1.000 34.99822  ? 240 ASP A C   1 
ATOM   1941 O  O   . ASP A 1 245 ? 39.85384 -2.31015  24.33134 1.000 41.31530  ? 240 ASP A O   1 
ATOM   1942 C  CB  . ASP A 1 245 ? 39.28661 -5.33307  23.70743 1.000 33.37151  ? 240 ASP A CB  1 
ATOM   1943 C  CG  . ASP A 1 245 ? 39.26804 -6.77243  24.17111 1.000 44.97441  ? 240 ASP A CG  1 
ATOM   1944 O  OD1 . ASP A 1 245 ? 39.61364 -7.02318  25.34571 1.000 43.05550  ? 240 ASP A OD1 1 
ATOM   1945 O  OD2 . ASP A 1 245 ? 38.90266 -7.64803  23.35792 1.000 51.90648  ? 240 ASP A OD2 1 
ATOM   1946 N  N   . VAL A 1 246 ? 37.77263 -2.48813  23.50938 1.000 31.30111  ? 241 VAL A N   1 
ATOM   1947 C  CA  . VAL A 1 246 ? 37.83477 -1.27834  22.69527 1.000 29.86627  ? 241 VAL A CA  1 
ATOM   1948 C  C   . VAL A 1 246 ? 36.86088 -0.25658  23.26022 1.000 32.99546  ? 241 VAL A C   1 
ATOM   1949 O  O   . VAL A 1 246 ? 35.65148 -0.51187  23.31729 1.000 30.55425  ? 241 VAL A O   1 
ATOM   1950 C  CB  . VAL A 1 246 ? 37.51833 -1.57627  21.22177 1.000 34.57301  ? 241 VAL A CB  1 
ATOM   1951 C  CG1 . VAL A 1 246 ? 37.62150 -0.30301  20.38885 1.000 37.61042  ? 241 VAL A CG1 1 
ATOM   1952 C  CG2 . VAL A 1 246 ? 38.46155 -2.64914  20.68633 1.000 37.54634  ? 241 VAL A CG2 1 
ATOM   1953 N  N   . SER A 1 247 ? 37.38279 0.90516   23.65479 1.000 29.07811  ? 242 SER A N   1 
ATOM   1954 C  CA  . SER A 1 247 ? 36.55424 1.96052   24.21537 1.000 32.09673  ? 242 SER A CA  1 
ATOM   1955 C  C   . SER A 1 247 ? 35.79063 2.68319   23.10724 1.000 31.25627  ? 242 SER A C   1 
ATOM   1956 O  O   . SER A 1 247 ? 36.00582 2.45870   21.91216 1.000 29.57219  ? 242 SER A O   1 
ATOM   1957 C  CB  . SER A 1 247 ? 37.40969 2.95980   24.99355 1.000 38.98002  ? 242 SER A CB  1 
ATOM   1958 O  OG  . SER A 1 247 ? 38.17836 2.31103   25.99241 1.000 45.24870  ? 242 SER A OG  1 
ATOM   1959 N  N   . GLY A 1 248 ? 34.89886 3.58100   23.51469 1.000 30.14263  ? 243 GLY A N   1 
ATOM   1960 C  CA  . GLY A 1 248 ? 34.18283 4.39092   22.54713 1.000 26.15877  ? 243 GLY A CA  1 
ATOM   1961 C  C   . GLY A 1 248 ? 32.89100 4.98983   23.06142 1.000 27.49488  ? 243 GLY A C   1 
ATOM   1962 O  O   . GLY A 1 248 ? 32.42811 6.00652   22.54521 1.000 26.53000  ? 243 GLY A O   1 
ATOM   1963 N  N   . LEU A 1 249 ? 32.28351 4.36180   24.06061 1.000 24.80856  ? 244 LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 249 ? 31.05274 4.89944   24.62746 1.000 25.82538  ? 244 LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 249 ? 31.33812 6.17529   25.40887 1.000 26.31830  ? 244 LEU A C   1 
ATOM   1966 O  O   . LEU A 1 249 ? 32.28502 6.23921   26.19796 1.000 27.92058  ? 244 LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 249 ? 30.39451 3.86897   25.54338 1.000 23.74965  ? 244 LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 249 ? 29.11751 4.29424   26.27307 1.000 24.13670  ? 244 LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 249 ? 28.01222 4.65066   25.28985 1.000 24.01869  ? 244 LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 249 ? 28.66083 3.18596   27.22294 1.000 25.94810  ? 244 LEU A CD2 1 
ATOM   1971 N  N   . GLN A 1 250 ? 30.50230 7.19202   25.19769 1.000 21.79756  ? 245 GLN A N   1 
ATOM   1972 C  CA  . GLN A 1 250 ? 30.61422 8.45444   25.92103 1.000 25.00070  ? 245 GLN A CA  1 
ATOM   1973 C  C   . GLN A 1 250 ? 29.22835 8.92114   26.34160 1.000 25.74886  ? 245 GLN A C   1 
ATOM   1974 O  O   . GLN A 1 250 ? 28.23457 8.64005   25.66956 1.000 25.77782  ? 245 GLN A O   1 
ATOM   1975 C  CB  . GLN A 1 250 ? 31.30961 9.52945   25.06021 1.000 25.21681  ? 245 GLN A CB  1 
ATOM   1976 C  CG  . GLN A 1 250 ? 32.74595 9.17218   24.69071 1.000 29.22755  ? 245 GLN A CG  1 
ATOM   1977 C  CD  . GLN A 1 250 ? 33.41257 10.20634  23.79319 1.000 30.09977  ? 245 GLN A CD  1 
ATOM   1978 O  OE1 . GLN A 1 250 ? 32.76965 11.13625  23.30779 1.000 30.45182  ? 245 GLN A OE1 1 
ATOM   1979 N  NE2 . GLN A 1 250 ? 34.70936 10.03920  23.56514 1.000 33.44377  ? 245 GLN A NE2 1 
ATOM   1980 N  N   . VAL A 1 251 ? 29.16528 9.63304   27.46806 1.000 24.56648  ? 246 VAL A N   1 
ATOM   1981 C  CA  . VAL A 1 251 ? 27.90443 10.13972  27.98882 1.000 26.78822  ? 246 VAL A CA  1 
ATOM   1982 C  C   . VAL A 1 251 ? 28.01821 11.64198  28.21196 1.000 30.79016  ? 246 VAL A C   1 
ATOM   1983 O  O   . VAL A 1 251 ? 29.08655 12.16811  28.53941 1.000 31.70461  ? 246 VAL A O   1 
ATOM   1984 C  CB  . VAL A 1 251 ? 27.49573 9.41701   29.29367 1.000 27.10913  ? 246 VAL A CB  1 
ATOM   1985 C  CG1 . VAL A 1 251 ? 28.49647 9.71142   30.40249 1.000 34.01704  ? 246 VAL A CG1 1 
ATOM   1986 C  CG2 . VAL A 1 251 ? 26.09464 9.81830   29.71514 1.000 29.72622  ? 246 VAL A CG2 1 
ATOM   1987 N  N   . GLN A 1 252 ? 26.90929 12.33986  28.00950 1.000 27.11418  ? 247 GLN A N   1 
ATOM   1988 C  CA  . GLN A 1 252 ? 26.86545 13.78383  28.17209 1.000 26.92505  ? 247 GLN A CA  1 
ATOM   1989 C  C   . GLN A 1 252 ? 26.34571 14.10754  29.56753 1.000 26.62718  ? 247 GLN A C   1 
ATOM   1990 O  O   . GLN A 1 252 ? 25.32753 13.55869  30.00263 1.000 33.50333  ? 247 GLN A O   1 
ATOM   1991 C  CB  . GLN A 1 252 ? 25.98422 14.42252  27.09824 1.000 30.64199  ? 247 GLN A CB  1 
ATOM   1992 C  CG  . GLN A 1 252 ? 26.20574 15.90527  26.91435 1.000 37.94652  ? 247 GLN A CG  1 
ATOM   1993 C  CD  . GLN A 1 252 ? 25.33223 16.47845  25.82061 1.000 40.79979  ? 247 GLN A CD  1 
ATOM   1994 O  OE1 . GLN A 1 252 ? 24.17568 16.08532  25.66405 1.000 42.50961  ? 247 GLN A OE1 1 
ATOM   1995 N  NE2 . GLN A 1 252 ? 25.88230 17.40679  25.05238 1.000 45.41401  ? 247 GLN A NE2 1 
ATOM   1996 N  N   . ARG A 1 253 ? 27.06519 14.97192  30.27397 1.000 30.74273  ? 248 ARG A N   1 
ATOM   1997 C  CA  . ARG A 1 253 ? 26.66861 15.39580  31.60957 1.000 42.63323  ? 248 ARG A CA  1 
ATOM   1998 C  C   . ARG A 1 253 ? 27.09085 16.84532  31.78260 1.000 51.02550  ? 248 ARG A C   1 
ATOM   1999 O  O   . ARG A 1 253 ? 28.28758 17.14864  31.75363 1.000 50.19875  ? 248 ARG A O   1 
ATOM   2000 C  CB  . ARG A 1 253 ? 27.29713 14.49551  32.67747 1.000 40.92433  ? 248 ARG A CB  1 
ATOM   2001 C  CG  . ARG A 1 253 ? 26.77290 14.72336  34.07938 1.000 56.21173  ? 248 ARG A CG  1 
ATOM   2002 C  CD  . ARG A 1 253 ? 26.90028 13.46171  34.91509 1.000 41.88678  ? 248 ARG A CD  1 
ATOM   2003 N  NE  . ARG A 1 253 ? 26.94102 13.76473  36.34006 1.000 58.34788  ? 248 ARG A NE  1 
ATOM   2004 C  CZ  . ARG A 1 253 ? 28.05694 14.00047  37.01854 1.000 57.11809  ? 248 ARG A CZ  1 
ATOM   2005 N  NH1 . ARG A 1 253 ? 29.24603 13.96047  36.43360 1.000 49.81127  ? 248 ARG A NH1 1 
ATOM   2006 N  NH2 . ARG A 1 253 ? 27.98021 14.28068  38.31653 1.000 69.70350  ? 248 ARG A NH2 1 
ATOM   2007 N  N   . ASP A 1 254 ? 26.10625 17.73634  31.92499 1.000 54.36301  ? 249 ASP A N   1 
ATOM   2008 C  CA  . ASP A 1 254 ? 26.34654 19.17575  32.05306 1.000 54.58784  ? 249 ASP A CA  1 
ATOM   2009 C  C   . ASP A 1 254 ? 27.12637 19.71265  30.85290 1.000 61.47839  ? 249 ASP A C   1 
ATOM   2010 O  O   . ASP A 1 254 ? 28.09289 20.46577  30.99182 1.000 64.04386  ? 249 ASP A O   1 
ATOM   2011 C  CB  . ASP A 1 254 ? 27.05987 19.49966  33.36802 1.000 64.22725  ? 249 ASP A CB  1 
ATOM   2012 C  CG  . ASP A 1 254 ? 26.20542 19.18868  34.58492 1.000 69.06293  ? 249 ASP A CG  1 
ATOM   2013 O  OD1 . ASP A 1 254 ? 25.01901 19.58148  34.59484 1.000 69.53971  ? 249 ASP A OD1 1 
ATOM   2014 O  OD2 . ASP A 1 254 ? 26.71615 18.54154  35.52606 1.000 69.28764  ? 249 ASP A OD2 1 
ATOM   2015 N  N   . GLY A 1 255 ? 26.70058 19.30188  29.65878 1.000 60.46320  ? 250 GLY A N   1 
ATOM   2016 C  CA  . GLY A 1 255 ? 27.27202 19.79792  28.42462 1.000 57.12002  ? 250 GLY A CA  1 
ATOM   2017 C  C   . GLY A 1 255 ? 28.64270 19.26749  28.06961 1.000 55.05136  ? 250 GLY A C   1 
ATOM   2018 O  O   . GLY A 1 255 ? 29.15329 19.60108  26.99514 1.000 63.72725  ? 250 GLY A O   1 
ATOM   2019 N  N   . LYS A 1 256 ? 29.26148 18.46511  28.92744 1.000 43.60784  ? 251 LYS A N   1 
ATOM   2020 C  CA  . LYS A 1 256 ? 30.56539 17.88579  28.65298 1.000 49.08975  ? 251 LYS A CA  1 
ATOM   2021 C  C   . LYS A 1 256 ? 30.41124 16.39780  28.36671 1.000 40.63512  ? 251 LYS A C   1 
ATOM   2022 O  O   . LYS A 1 256 ? 29.54807 15.72740  28.93805 1.000 36.37991  ? 251 LYS A O   1 
ATOM   2023 C  CB  . LYS A 1 256 ? 31.51938 18.09765  29.83215 1.000 46.90494  ? 251 LYS A CB  1 
ATOM   2024 C  CG  . LYS A 1 256 ? 31.52315 19.52216  30.36596 1.000 66.50227  ? 251 LYS A CG  1 
ATOM   2025 C  CD  . LYS A 1 256 ? 32.36904 19.65232  31.62428 1.000 71.31006  ? 251 LYS A CD  1 
ATOM   2026 C  CE  . LYS A 1 256 ? 32.12645 20.99063  32.31271 1.000 82.33341  ? 251 LYS A CE  1 
ATOM   2027 N  NZ  . LYS A 1 256 ? 33.14127 21.28520  33.36550 1.000 77.30622  ? 251 LYS A NZ  1 
ATOM   2028 N  N   . TRP A 1 257 ? 31.24633 15.88834  27.46589 1.000 35.54583  ? 252 TRP A N   1 
ATOM   2029 C  CA  . TRP A 1 257 ? 31.27732 14.46669  27.14988 1.000 38.72931  ? 252 TRP A CA  1 
ATOM   2030 C  C   . TRP A 1 257 ? 32.40687 13.80596  27.92719 1.000 36.14475  ? 252 TRP A C   1 
ATOM   2031 O  O   . TRP A 1 257 ? 33.51907 14.33813  27.98710 1.000 47.50094  ? 252 TRP A O   1 
ATOM   2032 C  CB  . TRP A 1 257 ? 31.45860 14.23495  25.64583 1.000 41.89941  ? 252 TRP A CB  1 
ATOM   2033 C  CG  . TRP A 1 257 ? 30.25619 14.62012  24.82948 1.000 36.76002  ? 252 TRP A CG  1 
ATOM   2034 C  CD1 . TRP A 1 257 ? 30.03847 15.81292  24.20671 1.000 36.38053  ? 252 TRP A CD1 1 
ATOM   2035 C  CD2 . TRP A 1 257 ? 29.09933 13.81258  24.56578 1.000 29.86303  ? 252 TRP A CD2 1 
ATOM   2036 N  NE1 . TRP A 1 257 ? 28.81983 15.79976  23.57272 1.000 38.09315  ? 252 TRP A NE1 1 
ATOM   2037 C  CE2 . TRP A 1 257 ? 28.22668 14.58175  23.77236 1.000 34.71910  ? 252 TRP A CE2 1 
ATOM   2038 C  CE3 . TRP A 1 257 ? 28.72160 12.51411  24.91857 1.000 26.87283  ? 252 TRP A CE3 1 
ATOM   2039 C  CZ2 . TRP A 1 257 ? 26.99852 14.09672  23.32734 1.000 31.70411  ? 252 TRP A CZ2 1 
ATOM   2040 C  CZ3 . TRP A 1 257 ? 27.50227 12.03347  24.47589 1.000 30.06456  ? 252 TRP A CZ3 1 
ATOM   2041 C  CH2 . TRP A 1 257 ? 26.65747 12.82292  23.68348 1.000 28.78857  ? 252 TRP A CH2 1 
ATOM   2042 N  N   . SER A 1 258 ? 32.11533 12.65458  28.52548 1.000 38.34808  ? 253 SER A N   1 
ATOM   2043 C  CA  . SER A 1 258 ? 33.10227 11.87787  29.25693 1.000 35.30916  ? 253 SER A CA  1 
ATOM   2044 C  C   . SER A 1 258 ? 33.02983 10.42394  28.81138 1.000 34.17764  ? 253 SER A C   1 
ATOM   2045 O  O   . SER A 1 258 ? 31.96817 9.93068   28.42339 1.000 29.34155  ? 253 SER A O   1 
ATOM   2046 C  CB  . SER A 1 258 ? 32.87989 11.98336  30.77218 1.000 38.91022  ? 253 SER A CB  1 
ATOM   2047 O  OG  . SER A 1 258 ? 31.50574 11.85758  31.08762 1.000 45.43101  ? 253 SER A OG  1 
ATOM   2048 N  N   . ASN A 1 259 ? 34.17217 9.74600   28.86586 1.000 36.08802  ? 254 ASN A N   1 
ATOM   2049 C  CA  . ASN A 1 259 ? 34.23464 8.34526   28.47358 1.000 35.90333  ? 254 ASN A CA  1 
ATOM   2050 C  C   . ASN A 1 259 ? 33.59173 7.46162   29.53262 1.000 35.76239  ? 254 ASN A C   1 
ATOM   2051 O  O   . ASN A 1 259 ? 33.67411 7.73881   30.73205 1.000 40.99422  ? 254 ASN A O   1 
ATOM   2052 C  CB  . ASN A 1 259 ? 35.68480 7.91381   28.26311 1.000 39.66687  ? 254 ASN A CB  1 
ATOM   2053 C  CG  . ASN A 1 259 ? 36.33544 8.61368   27.09915 1.000 48.22806  ? 254 ASN A CG  1 
ATOM   2054 O  OD1 . ASN A 1 259 ? 35.68869 8.89747   26.09332 1.000 48.15675  ? 254 ASN A OD1 1 
ATOM   2055 N  ND2 . ASN A 1 259 ? 37.62546 8.89623   27.22503 1.000 54.73202  ? 254 ASN A ND2 1 
ATOM   2056 N  N   . VAL A 1 260 ? 32.95204 6.38773   29.08723 1.000 27.76207  ? 255 VAL A N   1 
ATOM   2057 C  CA  . VAL A 1 260 ? 32.39035 5.38577   29.98357 1.000 28.35736  ? 255 VAL A CA  1 
ATOM   2058 C  C   . VAL A 1 260 ? 33.20759 4.11837   29.80048 1.000 41.93903  ? 255 VAL A C   1 
ATOM   2059 O  O   . VAL A 1 260 ? 33.21314 3.52421   28.71493 1.000 38.20810  ? 255 VAL A O   1 
ATOM   2060 C  CB  . VAL A 1 260 ? 30.90164 5.14018   29.71518 1.000 32.41083  ? 255 VAL A CB  1 
ATOM   2061 C  CG1 . VAL A 1 260 ? 30.38921 3.98583   30.57282 1.000 35.52096  ? 255 VAL A CG1 1 
ATOM   2062 C  CG2 . VAL A 1 260 ? 30.11092 6.40532   30.00604 1.000 35.30662  ? 255 VAL A CG2 1 
ATOM   2063 N  N   . GLU A 1 261 ? 33.92045 3.72156   30.85212 1.000 36.15106  ? 256 GLU A N   1 
ATOM   2064 C  CA  . GLU A 1 261 ? 34.76807 2.53642   30.84241 1.000 34.42358  ? 256 GLU A CA  1 
ATOM   2065 C  C   . GLU A 1 261 ? 34.20542 1.52862   31.83503 1.000 40.25018  ? 256 GLU A C   1 
ATOM   2066 O  O   . GLU A 1 261 ? 33.99853 1.85901   33.00833 1.000 46.39262  ? 256 GLU A O   1 
ATOM   2067 C  CB  . GLU A 1 261 ? 36.21450 2.89286   31.18979 1.000 36.93296  ? 256 GLU A CB  1 
ATOM   2068 C  CG  . GLU A 1 261 ? 36.83719 3.95427   30.28236 1.000 37.23363  ? 256 GLU A CG  1 
ATOM   2069 C  CD  . GLU A 1 261 ? 36.87978 3.53311   28.82613 1.000 57.14497  ? 256 GLU A CD  1 
ATOM   2070 O  OE1 . GLU A 1 261 ? 36.99770 2.31787   28.55998 1.000 57.63405  ? 256 GLU A OE1 1 
ATOM   2071 O  OE2 . GLU A 1 261 ? 36.79352 4.42033   27.94636 1.000 53.28962  ? 256 GLU A OE2 1 
ATOM   2072 N  N   . ALA A 1 262 ? 33.94522 0.31410   31.35657 1.000 44.13631  ? 257 ALA A N   1 
ATOM   2073 C  CA  . ALA A 1 262 ? 33.40758 -0.77364  32.16123 1.000 41.36031  ? 257 ALA A CA  1 
ATOM   2074 C  C   . ALA A 1 262 ? 34.36304 -1.95713  32.12414 1.000 45.42080  ? 257 ALA A C   1 
ATOM   2075 O  O   . ALA A 1 262 ? 34.93979 -2.26885  31.07705 1.000 50.23697  ? 257 ALA A O   1 
ATOM   2076 C  CB  . ALA A 1 262 ? 32.03066 -1.21824  31.65094 1.000 34.56423  ? 257 ALA A CB  1 
ATOM   2077 N  N   . THR A 1 263 ? 34.51839 -2.62096  33.26057 1.000 29.01188  ? 258 THR A N   1 
ATOM   2078 C  CA  . THR A 1 263 ? 35.31158 -3.83495  33.30148 1.000 26.14542  ? 258 THR A CA  1 
ATOM   2079 C  C   . THR A 1 263 ? 34.53934 -4.96902  32.63978 1.000 29.34896  ? 258 THR A C   1 
ATOM   2080 O  O   . THR A 1 263 ? 33.31439 -4.89325  32.49650 1.000 27.43661  ? 258 THR A O   1 
ATOM   2081 C  CB  . THR A 1 263 ? 35.64983 -4.19340  34.74406 1.000 33.14692  ? 258 THR A CB  1 
ATOM   2082 O  OG1 . THR A 1 263 ? 34.43638 -4.34835  35.48781 1.000 28.75494  ? 258 THR A OG1 1 
ATOM   2083 C  CG2 . THR A 1 263 ? 36.50725 -3.10408  35.38285 1.000 31.02803  ? 258 THR A CG2 1 
ATOM   2084 N  N   . PRO A 1 264 ? 35.22653 -6.02827  32.21374 1.000 25.11851  ? 259 PRO A N   1 
ATOM   2085 C  CA  . PRO A 1 264 ? 34.50775 -7.16221  31.62748 1.000 30.34357  ? 259 PRO A CA  1 
ATOM   2086 C  C   . PRO A 1 264 ? 33.49607 -7.71408  32.61895 1.000 31.60824  ? 259 PRO A C   1 
ATOM   2087 O  O   . PRO A 1 264 ? 33.75290 -7.78902  33.82487 1.000 38.56980  ? 259 PRO A O   1 
ATOM   2088 C  CB  . PRO A 1 264 ? 35.61560 -8.17696  31.32735 1.000 33.86417  ? 259 PRO A CB  1 
ATOM   2089 C  CG  . PRO A 1 264 ? 36.86021 -7.37018  31.22891 1.000 38.60286  ? 259 PRO A CG  1 
ATOM   2090 C  CD  . PRO A 1 264 ? 36.68426 -6.24617  32.21394 1.000 33.11812  ? 259 PRO A CD  1 
ATOM   2091 N  N   . HIS A 1 265 ? 32.32279 -8.05251  32.09926 1.000 35.04925  ? 260 HIS A N   1 
ATOM   2092 C  CA  . HIS A 1 265 ? 31.23129 -8.71441  32.79852 1.000 27.41123  ? 260 HIS A CA  1 
ATOM   2093 C  C   . HIS A 1 265 ? 30.48261 -7.77239  33.72801 1.000 27.64493  ? 260 HIS A C   1 
ATOM   2094 O  O   . HIS A 1 265 ? 29.53800 -8.20930  34.37689 1.000 24.79426  ? 260 HIS A O   1 
ATOM   2095 C  CB  . HIS A 1 265 ? 31.71568 -9.94951  33.57152 1.000 26.67218  ? 260 HIS A CB  1 
ATOM   2096 C  CG  . HIS A 1 265 ? 32.54338 -10.86982 32.73207 1.000 27.49889  ? 260 HIS A CG  1 
ATOM   2097 N  ND1 . HIS A 1 265 ? 33.84062 -11.20804 33.04821 1.000 30.08366  ? 260 HIS A ND1 1 
ATOM   2098 C  CD2 . HIS A 1 265 ? 32.26424 -11.49665 31.56502 1.000 28.15391  ? 260 HIS A CD2 1 
ATOM   2099 C  CE1 . HIS A 1 265 ? 34.31891 -12.01821 32.12010 1.000 36.74934  ? 260 HIS A CE1 1 
ATOM   2100 N  NE2 . HIS A 1 265 ? 33.38286 -12.20634 31.20780 1.000 29.98299  ? 260 HIS A NE2 1 
ATOM   2101 N  N   . THR A 1 266 ? 30.86608 -6.50196  33.80597 1.000 21.55759  ? 261 THR A N   1 
ATOM   2102 C  CA  . THR A 1 266 ? 30.02520 -5.48564  34.41807 1.000 22.20819  ? 261 THR A CA  1 
ATOM   2103 C  C   . THR A 1 266 ? 29.00758 -5.00089  33.39607 1.000 24.17546  ? 261 THR A C   1 
ATOM   2104 O  O   . THR A 1 266 ? 29.33274 -4.81120  32.22151 1.000 31.30845  ? 261 THR A O   1 
ATOM   2105 C  CB  . THR A 1 266 ? 30.88518 -4.31943  34.90609 1.000 25.34041  ? 261 THR A CB  1 
ATOM   2106 O  OG1 . THR A 1 266 ? 31.84013 -4.80608  35.85641 1.000 33.67127  ? 261 THR A OG1 1 
ATOM   2107 C  CG2 . THR A 1 266 ? 30.02770 -3.25440  35.56875 1.000 29.68330  ? 261 THR A CG2 1 
ATOM   2108 N  N   . LEU A 1 267 ? 27.77252 -4.81261  33.82929 1.000 22.06500  ? 262 LEU A N   1 
ATOM   2109 C  CA  . LEU A 1 267 ? 26.74269 -4.31206  32.93339 1.000 23.28293  ? 262 LEU A CA  1 
ATOM   2110 C  C   . LEU A 1 267 ? 26.56329 -2.81460  33.13051 1.000 25.58551  ? 262 LEU A C   1 
ATOM   2111 O  O   . LEU A 1 267 ? 26.79070 -2.28605  34.22066 1.000 27.43418  ? 262 LEU A O   1 
ATOM   2112 C  CB  . LEU A 1 267 ? 25.41682 -5.03590  33.16879 1.000 24.62812  ? 262 LEU A CB  1 
ATOM   2113 C  CG  . LEU A 1 267 ? 25.37895 -6.46158  32.61978 1.000 25.79758  ? 262 LEU A CG  1 
ATOM   2114 C  CD1 . LEU A 1 267 ? 24.12402 -7.16539  33.12398 1.000 26.68200  ? 262 LEU A CD1 1 
ATOM   2115 C  CD2 . LEU A 1 267 ? 25.43726 -6.46911  31.09627 1.000 26.79476  ? 262 LEU A CD2 1 
ATOM   2116 N  N   . LEU A 1 268 ? 26.17213 -2.12983  32.05867 1.000 21.44924  ? 263 LEU A N   1 
ATOM   2117 C  CA  . LEU A 1 268 ? 25.76700 -0.73031  32.12236 1.000 21.19920  ? 263 LEU A CA  1 
ATOM   2118 C  C   . LEU A 1 268 ? 24.25600 -0.63574  31.97958 1.000 24.14961  ? 263 LEU A C   1 
ATOM   2119 O  O   . LEU A 1 268 ? 23.68805 -1.16461  31.02061 1.000 26.39261  ? 263 LEU A O   1 
ATOM   2120 C  CB  . LEU A 1 268 ? 26.45145 0.08741   31.02502 1.000 23.06284  ? 263 LEU A CB  1 
ATOM   2121 C  CG  . LEU A 1 268 ? 27.90758 0.44837   31.27543 1.000 26.34486  ? 263 LEU A CG  1 
ATOM   2122 C  CD1 . LEU A 1 268 ? 28.63255 0.69446   29.94651 1.000 30.57406  ? 263 LEU A CD1 1 
ATOM   2123 C  CD2 . LEU A 1 268 ? 27.93755 1.70136   32.12037 1.000 34.61072  ? 263 LEU A CD2 1 
ATOM   2124 N  N   . ILE A 1 269 ? 23.60866 0.03305   32.93255 1.000 22.23725  ? 264 ILE A N   1 
ATOM   2125 C  CA  . ILE A 1 269 ? 22.16251 0.21989   32.93243 1.000 22.28980  ? 264 ILE A CA  1 
ATOM   2126 C  C   . ILE A 1 269 ? 21.87877 1.70221   32.76368 1.000 25.97827  ? 264 ILE A C   1 
ATOM   2127 O  O   . ILE A 1 269 ? 22.41867 2.51970   33.51173 1.000 24.71700  ? 264 ILE A O   1 
ATOM   2128 C  CB  . ILE A 1 269 ? 21.51643 -0.27761  34.23940 1.000 25.90130  ? 264 ILE A CB  1 
ATOM   2129 C  CG1 . ILE A 1 269 ? 22.09496 -1.62594  34.68745 1.000 33.44471  ? 264 ILE A CG1 1 
ATOM   2130 C  CG2 . ILE A 1 269 ? 20.00706 -0.32031  34.08616 1.000 31.18947  ? 264 ILE A CG2 1 
ATOM   2131 C  CD1 . ILE A 1 269 ? 21.87834 -2.73952  33.71659 1.000 28.14035  ? 264 ILE A CD1 1 
ATOM   2132 N  N   . ASN A 1 270 ? 21.02455 2.05238   31.80447 1.000 24.81154  ? 265 ASN A N   1 
ATOM   2133 C  CA  . ASN A 1 270 ? 20.58827 3.43570   31.66918 1.000 23.47192  ? 265 ASN A CA  1 
ATOM   2134 C  C   . ASN A 1 270 ? 19.07822 3.47729   31.51226 1.000 28.57889  ? 265 ASN A C   1 
ATOM   2135 O  O   . ASN A 1 270 ? 18.46909 2.57502   30.93374 1.000 24.06367  ? 265 ASN A O   1 
ATOM   2136 C  CB  . ASN A 1 270 ? 21.26414 4.16725   30.47738 1.000 25.19166  ? 265 ASN A CB  1 
ATOM   2137 C  CG  . ASN A 1 270 ? 20.94256 3.54095   29.13456 1.000 29.89830  ? 265 ASN A CG  1 
ATOM   2138 O  OD1 . ASN A 1 270 ? 21.54003 2.53891   28.74983 1.000 31.90028  ? 265 ASN A OD1 1 
ATOM   2139 N  ND2 . ASN A 1 270 ? 20.01850 4.15561   28.39320 1.000 26.12020  ? 265 ASN A ND2 1 
ATOM   2140 N  N   . LEU A 1 271 ? 18.47551 4.52463   32.06070 1.000 27.18417  ? 266 LEU A N   1 
ATOM   2141 C  CA  . LEU A 1 271 ? 17.07168 4.77601   31.79447 1.000 23.43169  ? 266 LEU A CA  1 
ATOM   2142 C  C   . LEU A 1 271 ? 16.89342 5.27686   30.37249 1.000 25.11657  ? 266 LEU A C   1 
ATOM   2143 O  O   . LEU A 1 271 ? 17.79271 5.88803   29.78449 1.000 28.57537  ? 266 LEU A O   1 
ATOM   2144 C  CB  . LEU A 1 271 ? 16.52141 5.82065   32.75651 1.000 27.13123  ? 266 LEU A CB  1 
ATOM   2145 C  CG  . LEU A 1 271 ? 16.92267 5.60083   34.20225 1.000 35.06206  ? 266 LEU A CG  1 
ATOM   2146 C  CD1 . LEU A 1 271 ? 16.26926 6.66030   35.02284 1.000 36.02868  ? 266 LEU A CD1 1 
ATOM   2147 C  CD2 . LEU A 1 271 ? 16.46431 4.23696   34.63532 1.000 36.55417  ? 266 LEU A CD2 1 
ATOM   2148 N  N   . GLY A 1 272 ? 15.70823 5.02771   29.82149 1.000 24.52932  ? 267 GLY A N   1 
ATOM   2149 C  CA  . GLY A 1 272 ? 15.31805 5.58396   28.54802 1.000 22.27077  ? 267 GLY A CA  1 
ATOM   2150 C  C   . GLY A 1 272 ? 14.25997 6.66638   28.70868 1.000 24.44525  ? 267 GLY A C   1 
ATOM   2151 O  O   . GLY A 1 272 ? 13.78144 6.96376   29.80526 1.000 24.87372  ? 267 GLY A O   1 
ATOM   2152 N  N   . ASP A 1 273 ? 13.88149 7.24003   27.56358 1.000 23.87439  ? 268 ASP A N   1 
ATOM   2153 C  CA  . ASP A 1 273 ? 12.99152 8.39683   27.57386 1.000 27.09794  ? 268 ASP A CA  1 
ATOM   2154 C  C   . ASP A 1 273 ? 11.62166 8.04422   28.13336 1.000 23.25382  ? 268 ASP A C   1 
ATOM   2155 O  O   . ASP A 1 273 ? 10.94891 8.90799   28.70908 1.000 25.24848  ? 268 ASP A O   1 
ATOM   2156 C  CB  . ASP A 1 273 ? 12.86069 8.97383   26.16257 1.000 24.28463  ? 268 ASP A CB  1 
ATOM   2157 C  CG  . ASP A 1 273 ? 14.13491 9.63474   25.68582 1.000 27.91414  ? 268 ASP A CG  1 
ATOM   2158 O  OD1 . ASP A 1 273 ? 15.03384 9.86637   26.51989 1.000 28.51910  ? 268 ASP A OD1 1 
ATOM   2159 O  OD2 . ASP A 1 273 ? 14.24026 9.92173   24.47878 1.000 31.19838  ? 268 ASP A OD2 1 
ATOM   2160 N  N   . THR A 1 274 ? 11.19093 6.78760   27.97732 1.000 23.57753  ? 269 THR A N   1 
ATOM   2161 C  CA  . THR A 1 274 ? 9.93062  6.36435   28.57551 1.000 23.70570  ? 269 THR A CA  1 
ATOM   2162 C  C   . THR A 1 274 ? 9.97743  6.51450   30.08705 1.000 28.46794  ? 269 THR A C   1 
ATOM   2163 O  O   . THR A 1 274 ? 9.02505  7.00557   30.69919 1.000 25.31562  ? 269 THR A O   1 
ATOM   2164 C  CB  . THR A 1 274 ? 9.59950  4.91486   28.21569 1.000 29.00025  ? 269 THR A CB  1 
ATOM   2165 O  OG1 . THR A 1 274 ? 9.54057  4.75376   26.79105 1.000 28.38898  ? 269 THR A OG1 1 
ATOM   2166 C  CG2 . THR A 1 274 ? 8.25460  4.52909   28.82977 1.000 24.00464  ? 269 THR A CG2 1 
ATOM   2167 N  N   . MET A 1 275 ? 11.08257 6.09233   30.71026 1.000 24.07351  ? 270 MET A N   1 
ATOM   2168 C  CA  . MET A 1 275 ? 11.17850 6.20067   32.16276 1.000 26.32263  ? 270 MET A CA  1 
ATOM   2169 C  C   . MET A 1 275 ? 11.29644 7.65515   32.60307 1.000 25.92666  ? 270 MET A C   1 
ATOM   2170 O  O   . MET A 1 275 ? 10.72307 8.04324   33.62586 1.000 22.07838  ? 270 MET A O   1 
ATOM   2171 C  CB  . MET A 1 275 ? 12.36074 5.39162   32.69698 1.000 24.21530  ? 270 MET A CB  1 
ATOM   2172 C  CG  . MET A 1 275 ? 12.53920 5.52135   34.20931 1.000 29.15531  ? 270 MET A CG  1 
ATOM   2173 S  SD  . MET A 1 275 ? 11.14710 4.83547   35.14596 1.000 29.84871  ? 270 MET A SD  1 
ATOM   2174 C  CE  . MET A 1 275 ? 11.58860 3.10274   35.07600 1.000 26.83259  ? 270 MET A CE  1 
ATOM   2175 N  N   . GLU A 1 276 ? 12.03620 8.47919   31.85698 1.000 24.10699  ? 271 GLU A N   1 
ATOM   2176 C  CA  . GLU A 1 276 ? 12.13464 9.88259   32.24848 1.000 24.37215  ? 271 GLU A CA  1 
ATOM   2177 C  C   . GLU A 1 276 ? 10.76165 10.53258  32.28734 1.000 24.21311  ? 271 GLU A C   1 
ATOM   2178 O  O   . GLU A 1 276 ? 10.45999 11.30355  33.20437 1.000 24.53798  ? 271 GLU A O   1 
ATOM   2179 C  CB  . GLU A 1 276 ? 13.05677 10.66689  31.31151 1.000 27.20220  ? 271 GLU A CB  1 
ATOM   2180 C  CG  . GLU A 1 276 ? 13.10478 12.15773  31.69403 1.000 22.35965  ? 271 GLU A CG  1 
ATOM   2181 C  CD  . GLU A 1 276 ? 14.14751 12.95646  30.93596 1.000 30.80870  ? 271 GLU A CD  1 
ATOM   2182 O  OE1 . GLU A 1 276 ? 15.12566 12.35853  30.44450 1.000 30.50217  ? 271 GLU A OE1 1 
ATOM   2183 O  OE2 . GLU A 1 276 ? 13.98430 14.18856  30.84146 1.000 26.95680  ? 271 GLU A OE2 1 
ATOM   2184 N  N   . VAL A 1 277 ? 9.90913  10.22722  31.30897 1.000 23.26331  ? 272 VAL A N   1 
ATOM   2185 C  CA  . VAL A 1 277 ? 8.55988  10.78195  31.32050 1.000 23.43500  ? 272 VAL A CA  1 
ATOM   2186 C  C   . VAL A 1 277 ? 7.77182  10.22027  32.49700 1.000 25.10259  ? 272 VAL A C   1 
ATOM   2187 O  O   . VAL A 1 277 ? 7.13696  10.96479  33.25282 1.000 23.98019  ? 272 VAL A O   1 
ATOM   2188 C  CB  . VAL A 1 277 ? 7.85126  10.50914  29.98133 1.000 25.16973  ? 272 VAL A CB  1 
ATOM   2189 C  CG1 . VAL A 1 277 ? 6.40198  10.98695  30.03911 1.000 28.50530  ? 272 VAL A CG1 1 
ATOM   2190 C  CG2 . VAL A 1 277 ? 8.58400  11.21020  28.85015 1.000 24.78027  ? 272 VAL A CG2 1 
ATOM   2191 N  N   . MET A 1 278 ? 7.82833  8.89944   32.68842 1.000 24.91868  ? 273 MET A N   1 
ATOM   2192 C  CA  . MET A 1 278 ? 6.99818  8.27049   33.71137 1.000 24.49645  ? 273 MET A CA  1 
ATOM   2193 C  C   . MET A 1 278 ? 7.40225  8.69347   35.11737 1.000 26.21826  ? 273 MET A C   1 
ATOM   2194 O  O   . MET A 1 278 ? 6.54373  8.76951   36.00332 1.000 26.69318  ? 273 MET A O   1 
ATOM   2195 C  CB  . MET A 1 278 ? 7.04854  6.74769   33.56355 1.000 23.70781  ? 273 MET A CB  1 
ATOM   2196 C  CG  . MET A 1 278 ? 6.28538  6.23915   32.34776 1.000 26.35571  ? 273 MET A CG  1 
ATOM   2197 S  SD  . MET A 1 278 ? 6.43701  4.46033   32.09200 1.000 32.29326  ? 273 MET A SD  1 
ATOM   2198 C  CE  . MET A 1 278 ? 5.61746  3.84716   33.55491 1.000 34.80512  ? 273 MET A CE  1 
ATOM   2199 N  N   . CYS A 1 279 ? 8.68397  8.97876   35.35234 1.000 24.16689  ? 274 CYS A N   1 
ATOM   2200 C  CA  . CYS A 1 279 ? 9.11411  9.46552   36.65588 1.000 23.79587  ? 274 CYS A CA  1 
ATOM   2201 C  C   . CYS A 1 279 ? 9.15306  10.99234  36.72811 1.000 26.59342  ? 274 CYS A C   1 
ATOM   2202 O  O   . CYS A 1 279 ? 9.77131  11.54983  37.64566 1.000 25.60720  ? 274 CYS A O   1 
ATOM   2203 C  CB  . CYS A 1 279 ? 10.47197 8.87015   37.03090 1.000 25.39319  ? 274 CYS A CB  1 
ATOM   2204 S  SG  . CYS A 1 279 ? 11.89292 9.60495   36.22972 1.000 28.58812  ? 274 CYS A SG  1 
ATOM   2205 N  N   . ASN A 1 280 ? 8.49712  11.67073  35.78558 1.000 20.92906  ? 275 ASN A N   1 
ATOM   2206 C  CA  . ASN A 1 280 ? 8.35758  13.12800  35.78139 1.000 23.29077  ? 275 ASN A CA  1 
ATOM   2207 C  C   . ASN A 1 280 ? 9.70452  13.84358  35.81858 1.000 26.75254  ? 275 ASN A C   1 
ATOM   2208 O  O   . ASN A 1 280 ? 9.82741  14.92731  36.39231 1.000 24.51816  ? 275 ASN A O   1 
ATOM   2209 C  CB  . ASN A 1 280 ? 7.47410  13.60994  36.93725 1.000 21.06590  ? 275 ASN A CB  1 
ATOM   2210 C  CG  . ASN A 1 280 ? 6.80097  14.92114  36.62817 1.000 26.00028  ? 275 ASN A CG  1 
ATOM   2211 O  OD1 . ASN A 1 280 ? 6.50347  15.21202  35.46763 1.000 27.73323  ? 275 ASN A OD1 1 
ATOM   2212 N  ND2 . ASN A 1 280 ? 6.56824  15.73467  37.65717 1.000 23.60873  ? 275 ASN A ND2 1 
ATOM   2213 N  N   . GLY A 1 281 ? 10.72513 13.25602  35.20129 1.000 26.63165  ? 276 GLY A N   1 
ATOM   2214 C  CA  . GLY A 1 281 ? 12.01456 13.90917  35.15971 1.000 25.28736  ? 276 GLY A CA  1 
ATOM   2215 C  C   . GLY A 1 281 ? 12.78337 13.91291  36.45814 1.000 27.26056  ? 276 GLY A C   1 
ATOM   2216 O  O   . GLY A 1 281 ? 13.82619 14.56857  36.53339 1.000 26.81490  ? 276 GLY A O   1 
ATOM   2217 N  N   . ILE A 1 282 ? 12.29308 13.22663  37.49623 1.000 25.26015  ? 277 ILE A N   1 
ATOM   2218 C  CA  . ILE A 1 282 ? 13.08504 13.07576  38.71288 1.000 26.36529  ? 277 ILE A CA  1 
ATOM   2219 C  C   . ILE A 1 282 ? 14.38450 12.34253  38.40291 1.000 27.88681  ? 277 ILE A C   1 
ATOM   2220 O  O   . ILE A 1 282 ? 15.44265 12.64568  38.96619 1.000 27.11513  ? 277 ILE A O   1 
ATOM   2221 C  CB  . ILE A 1 282 ? 12.26785 12.34699  39.79522 1.000 31.62963  ? 277 ILE A CB  1 
ATOM   2222 C  CG1 . ILE A 1 282 ? 11.04235 13.17966  40.19596 1.000 27.46534  ? 277 ILE A CG1 1 
ATOM   2223 C  CG2 . ILE A 1 282 ? 13.14428 12.03670  40.99948 1.000 33.13071  ? 277 ILE A CG2 1 
ATOM   2224 C  CD1 . ILE A 1 282 ? 10.09438 12.43919  41.13500 1.000 31.76770  ? 277 ILE A CD1 1 
ATOM   2225 N  N   . PHE A 1 283 ? 14.31540 11.35324  37.52108 1.000 26.87675  ? 278 PHE A N   1 
ATOM   2226 C  CA  . PHE A 1 283 ? 15.47654 10.67660  36.96948 1.000 26.39575  ? 278 PHE A CA  1 
ATOM   2227 C  C   . PHE A 1 283 ? 15.57384 11.03269  35.49389 1.000 29.51694  ? 278 PHE A C   1 
ATOM   2228 O  O   . PHE A 1 283 ? 14.56077 11.27932  34.83515 1.000 28.29992  ? 278 PHE A O   1 
ATOM   2229 C  CB  . PHE A 1 283 ? 15.37329 9.15651   37.12214 1.000 25.68486  ? 278 PHE A CB  1 
ATOM   2230 C  CG  . PHE A 1 283 ? 15.08693 8.68739   38.52275 1.000 27.17451  ? 278 PHE A CG  1 
ATOM   2231 C  CD1 . PHE A 1 283 ? 15.67678 9.29467   39.61568 1.000 31.43529  ? 278 PHE A CD1 1 
ATOM   2232 C  CD2 . PHE A 1 283 ? 14.22899 7.62623   38.73620 1.000 26.41336  ? 278 PHE A CD2 1 
ATOM   2233 C  CE1 . PHE A 1 283 ? 15.40743 8.84720   40.90696 1.000 30.87752  ? 278 PHE A CE1 1 
ATOM   2234 C  CE2 . PHE A 1 283 ? 13.96061 7.16875   40.01786 1.000 32.40015  ? 278 PHE A CE2 1 
ATOM   2235 C  CZ  . PHE A 1 283 ? 14.55278 7.78313   41.10082 1.000 28.33926  ? 278 PHE A CZ  1 
ATOM   2236 N  N   . ARG A 1 284 ? 16.79369 11.03623  34.97457 1.000 30.66988  ? 279 ARG A N   1 
ATOM   2237 C  CA  . ARG A 1 284 ? 17.06619 11.52504  33.63293 1.000 30.28114  ? 279 ARG A CA  1 
ATOM   2238 C  C   . ARG A 1 284 ? 17.43484 10.37769  32.69996 1.000 31.74767  ? 279 ARG A C   1 
ATOM   2239 O  O   . ARG A 1 284 ? 18.04890 9.38673   33.11094 1.000 32.47511  ? 279 ARG A O   1 
ATOM   2240 C  CB  . ARG A 1 284 ? 18.19947 12.54916  33.65967 1.000 45.64720  ? 279 ARG A CB  1 
ATOM   2241 C  CG  . ARG A 1 284 ? 19.47279 12.01341  34.30349 1.000 48.66819  ? 279 ARG A CG  1 
ATOM   2242 C  CD  . ARG A 1 284 ? 20.62094 13.01089  34.18145 1.000 55.72965  ? 279 ARG A CD  1 
ATOM   2243 N  NE  . ARG A 1 284 ? 20.51594 14.09484  35.15124 1.000 56.58656  ? 279 ARG A NE  1 
ATOM   2244 C  CZ  . ARG A 1 284 ? 21.32111 15.14825  35.18140 1.000 65.81421  ? 279 ARG A CZ  1 
ATOM   2245 N  NH1 . ARG A 1 284 ? 22.28823 15.30416  34.29122 1.000 61.04087  ? 279 ARG A NH1 1 
ATOM   2246 N  NH2 . ARG A 1 284 ? 21.15325 16.06692  36.12875 1.000 60.62500  ? 279 ARG A NH2 1 
ATOM   2247 N  N   . SER A 1 285 ? 17.02887 10.51244  31.43849 1.000 22.93152  ? 280 SER A N   1 
ATOM   2248 C  CA  . SER A 1 285 ? 17.46183 9.59018   30.39475 1.000 26.39053  ? 280 SER A CA  1 
ATOM   2249 C  C   . SER A 1 285 ? 18.70936 10.16268  29.73250 1.000 24.36111  ? 280 SER A C   1 
ATOM   2250 O  O   . SER A 1 285 ? 18.63580 11.24418  29.13553 1.000 26.65474  ? 280 SER A O   1 
ATOM   2251 C  CB  . SER A 1 285 ? 16.35719 9.38619   29.37181 1.000 28.14084  ? 280 SER A CB  1 
ATOM   2252 O  OG  . SER A 1 285 ? 16.81753 8.65091   28.24648 1.000 27.35779  ? 280 SER A OG  1 
ATOM   2253 N  N   . PRO A 1 286 ? 19.86318 9.50332   29.83371 1.000 25.01649  ? 281 PRO A N   1 
ATOM   2254 C  CA  . PRO A 1 286 ? 21.12079 10.16190  29.46613 1.000 23.57717  ? 281 PRO A CA  1 
ATOM   2255 C  C   . PRO A 1 286 ? 21.37482 10.12733  27.96970 1.000 21.78988  ? 281 PRO A C   1 
ATOM   2256 O  O   . PRO A 1 286 ? 21.12173 9.12623   27.29348 1.000 23.32074  ? 281 PRO A O   1 
ATOM   2257 C  CB  . PRO A 1 286 ? 22.17458 9.34674   30.22555 1.000 21.55649  ? 281 PRO A CB  1 
ATOM   2258 C  CG  . PRO A 1 286 ? 21.58853 7.96789   30.26980 1.000 24.66599  ? 281 PRO A CG  1 
ATOM   2259 C  CD  . PRO A 1 286 ? 20.08898 8.18217   30.44853 1.000 26.56376  ? 281 PRO A CD  1 
ATOM   2260 N  N   . VAL A 1 287 ? 21.87050 11.24593  27.45689 1.000 22.89565  ? 282 VAL A N   1 
ATOM   2261 C  CA  . VAL A 1 287 ? 22.32454 11.31399  26.07317 1.000 22.70645  ? 282 VAL A CA  1 
ATOM   2262 C  C   . VAL A 1 287 ? 23.72119 10.71951  25.99039 1.000 23.01493  ? 282 VAL A C   1 
ATOM   2263 O  O   . VAL A 1 287 ? 24.61968 11.11372  26.74404 1.000 25.02540  ? 282 VAL A O   1 
ATOM   2264 C  CB  . VAL A 1 287 ? 22.31347 12.76464  25.56542 1.000 26.82598  ? 282 VAL A CB  1 
ATOM   2265 C  CG1 . VAL A 1 287 ? 22.90619 12.83718  24.15895 1.000 26.99604  ? 282 VAL A CG1 1 
ATOM   2266 C  CG2 . VAL A 1 287 ? 20.90062 13.31461  25.58815 1.000 30.68865  ? 282 VAL A CG2 1 
ATOM   2267 N  N   . HIS A 1 288 ? 23.91805 9.79029   25.05492 1.000 25.03485  ? 283 HIS A N   1 
ATOM   2268 C  CA  . HIS A 1 288 ? 25.19366 9.10566   24.91260 1.000 23.12708  ? 283 HIS A CA  1 
ATOM   2269 C  C   . HIS A 1 288 ? 25.51759 8.95050   23.43413 1.000 24.34471  ? 283 HIS A C   1 
ATOM   2270 O  O   . HIS A 1 288 ? 24.67119 9.16842   22.56394 1.000 26.32221  ? 283 HIS A O   1 
ATOM   2271 C  CB  . HIS A 1 288 ? 25.17692 7.73917   25.60790 1.000 23.53014  ? 283 HIS A CB  1 
ATOM   2272 C  CG  . HIS A 1 288 ? 24.00243 6.88775   25.23679 1.000 27.52073  ? 283 HIS A CG  1 
ATOM   2273 N  ND1 . HIS A 1 288 ? 22.73955 7.08870   25.75420 1.000 21.54115  ? 283 HIS A ND1 1 
ATOM   2274 C  CD2 . HIS A 1 288 ? 23.90177 5.82774   24.40253 1.000 26.59138  ? 283 HIS A CD2 1 
ATOM   2275 C  CE1 . HIS A 1 288 ? 21.91296 6.19066   25.25121 1.000 23.83226  ? 283 HIS A CE1 1 
ATOM   2276 N  NE2 . HIS A 1 288 ? 22.59259 5.41375   24.42432 1.000 23.84856  ? 283 HIS A NE2 1 
ATOM   2277 N  N   . ARG A 1 289 ? 26.76480 8.58206   23.15556 1.000 24.95151  ? 284 ARG A N   1 
ATOM   2278 C  CA  . ARG A 1 289 ? 27.22281 8.38940   21.78337 1.000 24.85523  ? 284 ARG A CA  1 
ATOM   2279 C  C   . ARG A 1 289 ? 28.38677 7.40888   21.79523 1.000 26.16500  ? 284 ARG A C   1 
ATOM   2280 O  O   . ARG A 1 289 ? 28.91800 7.05831   22.84825 1.000 25.22471  ? 284 ARG A O   1 
ATOM   2281 C  CB  . ARG A 1 289 ? 27.64447 9.72012   21.14178 1.000 23.23192  ? 284 ARG A CB  1 
ATOM   2282 C  CG  . ARG A 1 289 ? 28.94806 10.26509  21.70283 1.000 24.90199  ? 284 ARG A CG  1 
ATOM   2283 C  CD  . ARG A 1 289 ? 29.22622 11.68503  21.24701 1.000 28.49966  ? 284 ARG A CD  1 
ATOM   2284 N  NE  . ARG A 1 289 ? 30.52662 12.14735  21.71772 1.000 29.04801  ? 284 ARG A NE  1 
ATOM   2285 C  CZ  . ARG A 1 289 ? 30.99195 13.37664  21.53973 1.000 35.73631  ? 284 ARG A CZ  1 
ATOM   2286 N  NH1 . ARG A 1 289 ? 30.28718 14.29642  20.90058 1.000 35.17178  ? 284 ARG A NH1 1 
ATOM   2287 N  NH2 . ARG A 1 289 ? 32.19295 13.69263  22.01809 1.000 33.98777  ? 284 ARG A NH2 1 
ATOM   2288 N  N   . VAL A 1 290 ? 28.79228 6.96662   20.60829 1.000 23.71437  ? 285 VAL A N   1 
ATOM   2289 C  CA  . VAL A 1 290 ? 29.99608 6.16078   20.46643 1.000 23.74399  ? 285 VAL A CA  1 
ATOM   2290 C  C   . VAL A 1 290 ? 30.88416 6.83175   19.43817 1.000 30.32853  ? 285 VAL A C   1 
ATOM   2291 O  O   . VAL A 1 290 ? 30.42161 7.17489   18.34593 1.000 26.18974  ? 285 VAL A O   1 
ATOM   2292 C  CB  . VAL A 1 290 ? 29.68516 4.70790   20.05688 1.000 24.51828  ? 285 VAL A CB  1 
ATOM   2293 C  CG1 . VAL A 1 290 ? 30.97198 3.96398   19.70548 1.000 24.59583  ? 285 VAL A CG1 1 
ATOM   2294 C  CG2 . VAL A 1 290 ? 28.96201 4.00022   21.19363 1.000 23.05323  ? 285 VAL A CG2 1 
ATOM   2295 N  N   . VAL A 1 291 ? 32.14052 7.04402   19.79673 1.000 25.11199  ? 286 VAL A N   1 
ATOM   2296 C  CA  . VAL A 1 291 ? 33.13993 7.51946   18.85495 1.000 26.90829  ? 286 VAL A CA  1 
ATOM   2297 C  C   . VAL A 1 291 ? 33.93689 6.32308   18.36037 1.000 31.73487  ? 286 VAL A C   1 
ATOM   2298 O  O   . VAL A 1 291 ? 34.15981 5.34891   19.08908 1.000 32.34881  ? 286 VAL A O   1 
ATOM   2299 C  CB  . VAL A 1 291 ? 34.05697 8.58884   19.48537 1.000 34.75131  ? 286 VAL A CB  1 
ATOM   2300 C  CG1 . VAL A 1 291 ? 33.24390 9.80674   19.87553 1.000 30.13598  ? 286 VAL A CG1 1 
ATOM   2301 C  CG2 . VAL A 1 291 ? 34.80360 8.02356   20.68758 1.000 37.46437  ? 286 VAL A CG2 1 
ATOM   2302 N  N   . THR A 1 292 ? 34.35420 6.38550   17.09974 1.000 27.53871  ? 287 THR A N   1 
ATOM   2303 C  CA  . THR A 1 292 ? 35.11148 5.30455   16.49316 1.000 31.97515  ? 287 THR A CA  1 
ATOM   2304 C  C   . THR A 1 292 ? 36.60503 5.49580   16.74177 1.000 31.50977  ? 287 THR A C   1 
ATOM   2305 O  O   . THR A 1 292 ? 37.04023 6.45311   17.38562 1.000 35.21575  ? 287 THR A O   1 
ATOM   2306 C  CB  . THR A 1 292 ? 34.82464 5.22229   14.99418 1.000 32.95470  ? 287 THR A CB  1 
ATOM   2307 O  OG1 . THR A 1 292 ? 35.19581 6.45480   14.36854 1.000 35.18447  ? 287 THR A OG1 1 
ATOM   2308 C  CG2 . THR A 1 292 ? 33.33885 4.96453   14.75776 1.000 31.67754  ? 287 THR A CG2 1 
ATOM   2309 N  N   . ASN A 1 293 ? 37.40069 4.56080   16.22779 1.000 33.05222  ? 288 ASN A N   1 
ATOM   2310 C  CA  . ASN A 1 293 ? 38.85018 4.68534   16.20838 1.000 34.13351  ? 288 ASN A CA  1 
ATOM   2311 C  C   . ASN A 1 293 ? 39.35419 4.10472   14.89359 1.000 39.70676  ? 288 ASN A C   1 
ATOM   2312 O  O   . ASN A 1 293 ? 38.62518 3.41301   14.17916 1.000 37.07540  ? 288 ASN A O   1 
ATOM   2313 C  CB  . ASN A 1 293 ? 39.49971 3.99069   17.41263 1.000 37.78950  ? 288 ASN A CB  1 
ATOM   2314 C  CG  . ASN A 1 293 ? 39.43206 2.48465   17.32273 1.000 33.72624  ? 288 ASN A CG  1 
ATOM   2315 O  OD1 . ASN A 1 293 ? 40.36488 1.83787   16.83836 1.000 36.72834  ? 288 ASN A OD1 1 
ATOM   2316 N  ND2 . ASN A 1 293 ? 38.32664 1.91285   17.79046 1.000 33.60684  ? 288 ASN A ND2 1 
ATOM   2317 N  N   . ALA A 1 294 ? 40.61319 4.38923   14.56966 1.000 35.66714  ? 289 ALA A N   1 
ATOM   2318 C  CA  . ALA A 1 294 ? 41.14702 4.01924   13.26679 1.000 34.55332  ? 289 ALA A CA  1 
ATOM   2319 C  C   . ALA A 1 294 ? 41.70838 2.60469   13.20947 1.000 34.65189  ? 289 ALA A C   1 
ATOM   2320 O  O   . ALA A 1 294 ? 42.07258 2.15076   12.12121 1.000 39.02656  ? 289 ALA A O   1 
ATOM   2321 C  CB  . ALA A 1 294 ? 42.23618 5.01255   12.83729 1.000 40.66438  ? 289 ALA A CB  1 
ATOM   2322 N  N   . GLU A 1 295 ? 41.78174 1.88890   14.32687 1.000 36.75851  ? 290 GLU A N   1 
ATOM   2323 C  CA  . GLU A 1 295 ? 42.54980 0.64892   14.35354 1.000 49.61766  ? 290 GLU A CA  1 
ATOM   2324 C  C   . GLU A 1 295 ? 41.72498 -0.61095  14.57205 1.000 44.03295  ? 290 GLU A C   1 
ATOM   2325 O  O   . GLU A 1 295 ? 42.03866 -1.64558  13.97407 1.000 44.06025  ? 290 GLU A O   1 
ATOM   2326 C  CB  . GLU A 1 295 ? 43.64419 0.73634   15.42405 1.000 50.41057  ? 290 GLU A CB  1 
ATOM   2327 C  CG  . GLU A 1 295 ? 44.80778 1.62616   15.00060 1.000 54.57834  ? 290 GLU A CG  1 
ATOM   2328 C  CD  . GLU A 1 295 ? 45.86666 1.78739   16.07581 1.000 77.14947  ? 290 GLU A CD  1 
ATOM   2329 O  OE1 . GLU A 1 295 ? 45.67276 1.26758   17.19537 1.000 75.11141  ? 290 GLU A OE1 1 
ATOM   2330 O  OE2 . GLU A 1 295 ? 46.89690 2.44011   15.79745 1.000 82.54657  ? 290 GLU A OE2 1 
ATOM   2331 N  N   . LYS A 1 296 ? 40.67792 -0.57418  15.39491 1.000 39.41755  ? 291 LYS A N   1 
ATOM   2332 C  CA  . LYS A 1 296 ? 39.98537 -1.79871  15.77237 1.000 36.68383  ? 291 LYS A CA  1 
ATOM   2333 C  C   . LYS A 1 296 ? 38.47450 -1.61348  15.72364 1.000 33.78726  ? 291 LYS A C   1 
ATOM   2334 O  O   . LYS A 1 296 ? 37.94611 -0.54563  16.04704 1.000 34.47945  ? 291 LYS A O   1 
ATOM   2335 C  CB  . LYS A 1 296 ? 40.40005 -2.26404  17.17669 1.000 37.58966  ? 291 LYS A CB  1 
ATOM   2336 C  CG  . LYS A 1 296 ? 41.87188 -2.61337  17.30518 1.000 51.77805  ? 291 LYS A CG  1 
ATOM   2337 C  CD  . LYS A 1 296 ? 42.17375 -3.30702  18.62383 1.000 52.79300  ? 291 LYS A CD  1 
ATOM   2338 C  CE  . LYS A 1 296 ? 41.96654 -2.37687  19.80985 1.000 72.95775  ? 291 LYS A CE  1 
ATOM   2339 N  NZ  . LYS A 1 296 ? 42.08095 -3.08546  21.12415 1.000 63.75142  ? 291 LYS A NZ  1 
ATOM   2340 N  N   . GLU A 1 297 ? 37.78132 -2.67997  15.32997 1.000 30.34476  ? 292 GLU A N   1 
ATOM   2341 C  CA  . GLU A 1 297 ? 36.33169 -2.70217  15.43406 1.000 25.19137  ? 292 GLU A CA  1 
ATOM   2342 C  C   . GLU A 1 297 ? 35.91338 -2.79410  16.89549 1.000 26.68691  ? 292 GLU A C   1 
ATOM   2343 O  O   . GLU A 1 297 ? 36.69171 -3.18385  17.76805 1.000 33.50380  ? 292 GLU A O   1 
ATOM   2344 C  CB  . GLU A 1 297 ? 35.74197 -3.87586  14.65067 1.000 29.58160  ? 292 GLU A CB  1 
ATOM   2345 C  CG  . GLU A 1 297 ? 35.85361 -5.23351  15.33803 1.000 33.51431  ? 292 GLU A CG  1 
ATOM   2346 C  CD  . GLU A 1 297 ? 37.24413 -5.84250  15.27692 1.000 39.46269  ? 292 GLU A CD  1 
ATOM   2347 O  OE1 . GLU A 1 297 ? 38.14270 -5.24959  14.64418 1.000 37.27152  ? 292 GLU A OE1 1 
ATOM   2348 O  OE2 . GLU A 1 297 ? 37.43662 -6.93249  15.86030 1.000 44.29557  ? 292 GLU A OE2 1 
ATOM   2349 N  N   . ARG A 1 298 ? 34.65945 -2.43035  17.14921 1.000 25.40392  ? 293 ARG A N   1 
ATOM   2350 C  CA  . ARG A 1 298 ? 34.07027 -2.44914  18.48078 1.000 25.08477  ? 293 ARG A CA  1 
ATOM   2351 C  C   . ARG A 1 298 ? 32.66330 -3.01353  18.37543 1.000 24.34449  ? 293 ARG A C   1 
ATOM   2352 O  O   . ARG A 1 298 ? 31.94254 -2.70618  17.42504 1.000 26.95345  ? 293 ARG A O   1 
ATOM   2353 C  CB  . ARG A 1 298 ? 34.02821 -1.03673  19.09531 1.000 24.79628  ? 293 ARG A CB  1 
ATOM   2354 C  CG  . ARG A 1 298 ? 33.39199 -0.95710  20.49025 1.000 25.65212  ? 293 ARG A CG  1 
ATOM   2355 C  CD  . ARG A 1 298 ? 33.35020 0.48488   21.01383 1.000 26.07578  ? 293 ARG A CD  1 
ATOM   2356 N  NE  . ARG A 1 298 ? 32.73334 0.57446   22.33680 1.000 24.10334  ? 293 ARG A NE  1 
ATOM   2357 C  CZ  . ARG A 1 298 ? 31.42629 0.65139   22.54812 1.000 28.03134  ? 293 ARG A CZ  1 
ATOM   2358 N  NH1 . ARG A 1 298 ? 30.56705 0.68896   21.54347 1.000 25.15532  ? 293 ARG A NH1 1 
ATOM   2359 N  NH2 . ARG A 1 298 ? 30.96757 0.67600   23.80028 1.000 24.56287  ? 293 ARG A NH2 1 
ATOM   2360 N  N   . ILE A 1 299 ? 32.26144 -3.82647  19.35429 1.000 26.41899  ? 294 ILE A N   1 
ATOM   2361 C  CA  . ILE A 1 299 ? 30.91133 -4.37241  19.37134 1.000 23.09217  ? 294 ILE A CA  1 
ATOM   2362 C  C   . ILE A 1 299 ? 30.25469 -4.03660  20.70240 1.000 26.71226  ? 294 ILE A C   1 
ATOM   2363 O  O   . ILE A 1 299 ? 30.92917 -3.81487  21.71200 1.000 30.11365  ? 294 ILE A O   1 
ATOM   2364 C  CB  . ILE A 1 299 ? 30.88751 -5.89955  19.13632 1.000 24.49929  ? 294 ILE A CB  1 
ATOM   2365 C  CG1 . ILE A 1 299 ? 31.74427 -6.61130  20.18508 1.000 32.90122  ? 294 ILE A CG1 1 
ATOM   2366 C  CG2 . ILE A 1 299 ? 31.34637 -6.23952  17.71889 1.000 29.81449  ? 294 ILE A CG2 1 
ATOM   2367 C  CD1 . ILE A 1 299 ? 31.32239 -8.04611  20.44585 1.000 40.82413  ? 294 ILE A CD1 1 
ATOM   2368 N  N   . SER A 1 300 ? 28.92507 -3.98268  20.69362 1.000 25.44674  ? 295 SER A N   1 
ATOM   2369 C  CA  . SER A 1 300 ? 28.15522 -3.89247  21.92719 1.000 22.58443  ? 295 SER A CA  1 
ATOM   2370 C  C   . SER A 1 300 ? 26.82591 -4.58903  21.70088 1.000 24.48716  ? 295 SER A C   1 
ATOM   2371 O  O   . SER A 1 300 ? 26.40635 -4.80731  20.56137 1.000 25.84351  ? 295 SER A O   1 
ATOM   2372 C  CB  . SER A 1 300 ? 27.92665 -2.43871  22.36073 1.000 24.97938  ? 295 SER A CB  1 
ATOM   2373 O  OG  . SER A 1 300 ? 27.05727 -1.79276  21.44733 1.000 27.14331  ? 295 SER A OG  1 
ATOM   2374 N  N   . LEU A 1 301 ? 26.17224 -4.94779  22.80284 1.000 23.75826  ? 296 LEU A N   1 
ATOM   2375 C  CA  . LEU A 1 301 ? 24.83908 -5.54257  22.77842 1.000 21.52177  ? 296 LEU A CA  1 
ATOM   2376 C  C   . LEU A 1 301 ? 23.96272 -4.75281  23.74063 1.000 24.69581  ? 296 LEU A C   1 
ATOM   2377 O  O   . LEU A 1 301 ? 24.20032 -4.76157  24.95288 1.000 23.39959  ? 296 LEU A O   1 
ATOM   2378 C  CB  . LEU A 1 301 ? 24.86605 -7.02174  23.16644 1.000 24.73732  ? 296 LEU A CB  1 
ATOM   2379 C  CG  . LEU A 1 301 ? 23.49821 -7.66227  23.41914 1.000 25.04974  ? 296 LEU A CG  1 
ATOM   2380 C  CD1 . LEU A 1 301 ? 22.56358 -7.47833  22.22011 1.000 25.96757  ? 296 LEU A CD1 1 
ATOM   2381 C  CD2 . LEU A 1 301 ? 23.64063 -9.14852  23.77182 1.000 27.33282  ? 296 LEU A CD2 1 
ATOM   2382 N  N   . ALA A 1 302 ? 22.95550 -4.07634  23.20325 1.000 25.21906  ? 297 ALA A N   1 
ATOM   2383 C  CA  . ALA A 1 302 ? 21.98874 -3.33872  24.00520 1.000 23.68276  ? 297 ALA A CA  1 
ATOM   2384 C  C   . ALA A 1 302 ? 20.69277 -4.13015  24.06935 1.000 22.81428  ? 297 ALA A C   1 
ATOM   2385 O  O   . ALA A 1 302 ? 20.09806 -4.43219  23.02827 1.000 25.04734  ? 297 ALA A O   1 
ATOM   2386 C  CB  . ALA A 1 302 ? 21.73854 -1.95167  23.41375 1.000 21.18184  ? 297 ALA A CB  1 
ATOM   2387 N  N   . MET A 1 303 ? 20.27047 -4.48913  25.28463 1.000 24.20118  ? 298 MET A N   1 
ATOM   2388 C  CA  . MET A 1 303 ? 18.94341 -5.04765  25.50585 1.000 22.85513  ? 298 MET A CA  1 
ATOM   2389 C  C   . MET A 1 303 ? 17.99923 -3.88675  25.79704 1.000 25.56811  ? 298 MET A C   1 
ATOM   2390 O  O   . MET A 1 303 ? 18.13662 -3.21039  26.82251 1.000 24.88063  ? 298 MET A O   1 
ATOM   2391 C  CB  . MET A 1 303 ? 18.93220 -6.05619  26.65701 1.000 20.51336  ? 298 MET A CB  1 
ATOM   2392 C  CG  . MET A 1 303 ? 19.79284 -7.29489  26.44737 1.000 22.79194  ? 298 MET A CG  1 
ATOM   2393 S  SD  . MET A 1 303 ? 19.47146 -8.17165  24.89648 1.000 29.10188  ? 298 MET A SD  1 
ATOM   2394 C  CE  . MET A 1 303 ? 17.77580 -8.68415  25.12146 1.000 28.23694  ? 298 MET A CE  1 
ATOM   2395 N  N   . LEU A 1 304 ? 17.04767 -3.66368  24.89627 1.000 25.73087  ? 299 LEU A N   1 
ATOM   2396 C  CA  . LEU A 1 304 ? 16.19388 -2.48070  24.88862 1.000 22.85712  ? 299 LEU A CA  1 
ATOM   2397 C  C   . LEU A 1 304 ? 14.81210 -2.89095  25.37366 1.000 23.42140  ? 299 LEU A C   1 
ATOM   2398 O  O   . LEU A 1 304 ? 14.10167 -3.61954  24.67401 1.000 26.29917  ? 299 LEU A O   1 
ATOM   2399 C  CB  . LEU A 1 304 ? 16.12594 -1.89212  23.47934 1.000 24.30763  ? 299 LEU A CB  1 
ATOM   2400 C  CG  . LEU A 1 304 ? 17.47764 -1.50018  22.88581 1.000 25.45007  ? 299 LEU A CG  1 
ATOM   2401 C  CD1 . LEU A 1 304 ? 17.39910 -1.40891  21.36287 1.000 24.71248  ? 299 LEU A CD1 1 
ATOM   2402 C  CD2 . LEU A 1 304 ? 17.95111 -0.17471  23.47930 1.000 27.22884  ? 299 LEU A CD2 1 
ATOM   2403 N  N   . TYR A 1 305 ? 14.42479 -2.41798  26.55801 1.000 23.66026  ? 300 TYR A N   1 
ATOM   2404 C  CA  . TYR A 1 305 ? 13.16714 -2.81419  27.18669 1.000 25.69665  ? 300 TYR A CA  1 
ATOM   2405 C  C   . TYR A 1 305 ? 12.15648 -1.67849  27.12116 1.000 26.75947  ? 300 TYR A C   1 
ATOM   2406 O  O   . TYR A 1 305 ? 12.34504 -0.63689  27.75957 1.000 27.57939  ? 300 TYR A O   1 
ATOM   2407 C  CB  . TYR A 1 305 ? 13.39797 -3.24719  28.63465 1.000 27.99319  ? 300 TYR A CB  1 
ATOM   2408 C  CG  . TYR A 1 305 ? 14.09749 -4.58006  28.71696 1.000 25.77701  ? 300 TYR A CG  1 
ATOM   2409 C  CD1 . TYR A 1 305 ? 13.40311 -5.75474  28.47243 1.000 27.12730  ? 300 TYR A CD1 1 
ATOM   2410 C  CD2 . TYR A 1 305 ? 15.45597 -4.66644  29.00942 1.000 26.64571  ? 300 TYR A CD2 1 
ATOM   2411 C  CE1 . TYR A 1 305 ? 14.03466 -6.98753  28.51820 1.000 31.06632  ? 300 TYR A CE1 1 
ATOM   2412 C  CE2 . TYR A 1 305 ? 16.09946 -5.90124  29.06353 1.000 28.42542  ? 300 TYR A CE2 1 
ATOM   2413 C  CZ  . TYR A 1 305 ? 15.38022 -7.05547  28.81645 1.000 27.91094  ? 300 TYR A CZ  1 
ATOM   2414 O  OH  . TYR A 1 305 ? 15.98899 -8.29016  28.86400 1.000 29.73872  ? 300 TYR A OH  1 
ATOM   2415 N  N   . SER A 1 306 ? 11.07409 -1.89634  26.37756 1.000 26.02195  ? 301 SER A N   1 
ATOM   2416 C  CA  . SER A 1 306 ? 10.00440 -0.92122  26.21541 1.000 29.54002  ? 301 SER A CA  1 
ATOM   2417 C  C   . SER A 1 306 ? 8.79295  -1.30746  27.06046 1.000 34.07072  ? 301 SER A C   1 
ATOM   2418 O  O   . SER A 1 306 ? 8.71396  -2.40655  27.60976 1.000 34.47450  ? 301 SER A O   1 
ATOM   2419 C  CB  . SER A 1 306 ? 9.60152  -0.81137  24.74297 1.000 32.21703  ? 301 SER A CB  1 
ATOM   2420 O  OG  . SER A 1 306 ? 10.68056 -0.33504  23.95965 1.000 44.70608  ? 301 SER A OG  1 
ATOM   2421 N  N   . VAL A 1 307 ? 7.83581  -0.37852  27.16280 1.000 33.28281  ? 302 VAL A N   1 
ATOM   2422 C  CA  . VAL A 1 307 ? 6.54702  -0.68139  27.77593 1.000 33.05160  ? 302 VAL A CA  1 
ATOM   2423 C  C   . VAL A 1 307 ? 5.60049  -1.19204  26.69579 1.000 36.13332  ? 302 VAL A C   1 
ATOM   2424 O  O   . VAL A 1 307 ? 5.83709  -1.02411  25.49603 1.000 36.88060  ? 302 VAL A O   1 
ATOM   2425 C  CB  . VAL A 1 307 ? 5.94121  0.54014   28.50392 1.000 32.66310  ? 302 VAL A CB  1 
ATOM   2426 C  CG1 . VAL A 1 307 ? 6.86045  1.02029   29.61264 1.000 30.18460  ? 302 VAL A CG1 1 
ATOM   2427 C  CG2 . VAL A 1 307 ? 5.65288  1.65574   27.51520 1.000 31.40551  ? 302 VAL A CG2 1 
ATOM   2428 N  N   . ASN A 1 308 ? 4.50963  -1.82629  27.12145 1.000 36.14307  ? 303 ASN A N   1 
ATOM   2429 C  CA  . ASN A 1 308 ? 3.50603  -2.26816  26.16557 1.000 36.43280  ? 303 ASN A CA  1 
ATOM   2430 C  C   . ASN A 1 308 ? 2.65986  -1.07455  25.72023 1.000 44.44715  ? 303 ASN A C   1 
ATOM   2431 O  O   . ASN A 1 308 ? 2.82978  0.05388   26.19198 1.000 42.34482  ? 303 ASN A O   1 
ATOM   2432 C  CB  . ASN A 1 308 ? 2.65310  -3.39402  26.75626 1.000 38.48385  ? 303 ASN A CB  1 
ATOM   2433 C  CG  . ASN A 1 308 ? 1.85183  -2.96350  27.97876 1.000 42.27974  ? 303 ASN A CG  1 
ATOM   2434 O  OD1 . ASN A 1 308 ? 1.36373  -1.83900  28.05866 1.000 38.84681  ? 303 ASN A OD1 1 
ATOM   2435 N  ND2 . ASN A 1 308 ? 1.70409  -3.87507  28.93577 1.000 36.36727  ? 303 ASN A ND2 1 
ATOM   2436 N  N   . ASP A 1 309 ? 1.72349  -1.32445  24.80470 1.000 39.53692  ? 304 ASP A N   1 
ATOM   2437 C  CA  . ASP A 1 309 ? 0.90026  -0.27172  24.22175 1.000 49.78486  ? 304 ASP A CA  1 
ATOM   2438 C  C   . ASP A 1 309 ? -0.46514 -0.15220  24.89420 1.000 47.88431  ? 304 ASP A C   1 
ATOM   2439 O  O   . ASP A 1 309 ? -1.41617 0.33829   24.27727 1.000 57.78555  ? 304 ASP A O   1 
ATOM   2440 C  CB  . ASP A 1 309 ? 0.73277  -0.50553  22.72015 1.000 56.21156  ? 304 ASP A CB  1 
ATOM   2441 C  CG  . ASP A 1 309 ? 0.07516  -1.84073  22.40284 1.000 68.31186  ? 304 ASP A CG  1 
ATOM   2442 O  OD1 . ASP A 1 309 ? -0.14818 -2.64716  23.33337 1.000 69.26129  ? 304 ASP A OD1 1 
ATOM   2443 O  OD2 . ASP A 1 309 ? -0.22080 -2.08437  21.21451 1.000 76.81494  ? 304 ASP A OD2 1 
ATOM   2444 N  N   . GLU A 1 310 ? -0.58092 -0.58282  26.15303 1.000 45.35039  ? 305 GLU A N   1 
ATOM   2445 C  CA  . GLU A 1 310 ? -1.87850 -0.57479  26.82297 1.000 47.69429  ? 305 GLU A CA  1 
ATOM   2446 C  C   . GLU A 1 310 ? -2.25910 0.80353   27.35018 1.000 46.23535  ? 305 GLU A C   1 
ATOM   2447 O  O   . GLU A 1 310 ? -3.44466 1.15471   27.34297 1.000 41.50543  ? 305 GLU A O   1 
ATOM   2448 C  CB  . GLU A 1 310 ? -1.88863 -1.58522  27.97126 1.000 46.22628  ? 305 GLU A CB  1 
ATOM   2449 C  CG  . GLU A 1 310 ? -1.85951 -3.03718  27.52257 1.000 60.51353  ? 305 GLU A CG  1 
ATOM   2450 C  CD  . GLU A 1 310 ? -1.82509 -4.00481  28.69008 1.000 76.27515  ? 305 GLU A CD  1 
ATOM   2451 O  OE1 . GLU A 1 310 ? -1.91216 -3.54293  29.84874 1.000 73.05248  ? 305 GLU A OE1 1 
ATOM   2452 O  OE2 . GLU A 1 310 ? -1.70814 -5.22623  28.44943 1.000 80.65225  ? 305 GLU A OE2 1 
ATOM   2453 N  N   . LYS A 1 311 ? -1.28838 1.58533   27.81841 1.000 42.15958  ? 306 LYS A N   1 
ATOM   2454 C  CA  . LYS A 1 311 ? -1.54614 2.89380   28.40132 1.000 42.41520  ? 306 LYS A CA  1 
ATOM   2455 C  C   . LYS A 1 311 ? -0.71537 3.95217   27.69145 1.000 47.32070  ? 306 LYS A C   1 
ATOM   2456 O  O   . LYS A 1 311 ? 0.37103  3.67202   27.18002 1.000 40.14855  ? 306 LYS A O   1 
ATOM   2457 C  CB  . LYS A 1 311 ? -1.21306 2.92176   29.90012 1.000 45.96183  ? 306 LYS A CB  1 
ATOM   2458 C  CG  . LYS A 1 311 ? -1.94472 1.89222   30.73786 1.000 49.29038  ? 306 LYS A CG  1 
ATOM   2459 C  CD  . LYS A 1 311 ? -3.35050 2.34632   31.07937 1.000 57.25443  ? 306 LYS A CD  1 
ATOM   2460 C  CE  . LYS A 1 311 ? -3.93472 1.50387   32.20554 1.000 65.57638  ? 306 LYS A CE  1 
ATOM   2461 N  NZ  . LYS A 1 311 ? -3.14391 1.63817   33.46416 1.000 61.57921  ? 306 LYS A NZ  1 
ATOM   2462 N  N   . ASP A 1 312 ? -1.23614 5.17588   27.66803 1.000 39.22216  ? 307 ASP A N   1 
ATOM   2463 C  CA  . ASP A 1 312 ? -0.44394 6.30259   27.20051 1.000 32.73116  ? 307 ASP A CA  1 
ATOM   2464 C  C   . ASP A 1 312 ? 0.76588  6.49319   28.10742 1.000 32.83866  ? 307 ASP A C   1 
ATOM   2465 O  O   . ASP A 1 312 ? 0.74489  6.14432   29.28941 1.000 38.08161  ? 307 ASP A O   1 
ATOM   2466 C  CB  . ASP A 1 312 ? -1.28594 7.57979   27.17671 1.000 36.74854  ? 307 ASP A CB  1 
ATOM   2467 C  CG  . ASP A 1 312 ? -2.29797 7.60101   26.04478 1.000 42.86005  ? 307 ASP A CG  1 
ATOM   2468 O  OD1 . ASP A 1 312 ? -2.32876 6.64548   25.24355 1.000 44.53271  ? 307 ASP A OD1 1 
ATOM   2469 O  OD2 . ASP A 1 312 ? -3.06651 8.58354   25.95669 1.000 43.59887  ? 307 ASP A OD2 1 
ATOM   2470 N  N   . ILE A 1 313 ? 1.83540  7.03860   27.54513 1.000 32.91646  ? 308 ILE A N   1 
ATOM   2471 C  CA  . ILE A 1 313 ? 3.03361  7.34163   28.31578 1.000 25.11179  ? 308 ILE A CA  1 
ATOM   2472 C  C   . ILE A 1 313 ? 2.87860  8.73791   28.90880 1.000 27.94346  ? 308 ILE A C   1 
ATOM   2473 O  O   . ILE A 1 313 ? 2.59712  9.70177   28.18838 1.000 29.27860  ? 308 ILE A O   1 
ATOM   2474 C  CB  . ILE A 1 313 ? 4.29189  7.22883   27.43864 1.000 32.12820  ? 308 ILE A CB  1 
ATOM   2475 C  CG1 . ILE A 1 313 ? 4.45514  5.78541   26.94931 1.000 29.31347  ? 308 ILE A CG1 1 
ATOM   2476 C  CG2 . ILE A 1 313 ? 5.53181  7.66395   28.20514 1.000 28.91116  ? 308 ILE A CG2 1 
ATOM   2477 C  CD1 . ILE A 1 313 ? 5.61112  5.59490   25.99321 1.000 38.36934  ? 308 ILE A CD1 1 
ATOM   2478 N  N   . GLU A 1 314 ? 3.02835  8.84245   30.22316 1.000 30.83300  ? 309 GLU A N   1 
ATOM   2479 C  CA  . GLU A 1 314 ? 2.79544  10.08645  30.94374 1.000 28.97711  ? 309 GLU A CA  1 
ATOM   2480 C  C   . GLU A 1 314 ? 3.40244  9.95318   32.33544 1.000 25.70106  ? 309 GLU A C   1 
ATOM   2481 O  O   . GLU A 1 314 ? 3.65567  8.83690   32.79415 1.000 25.43555  ? 309 GLU A O   1 
ATOM   2482 C  CB  . GLU A 1 314 ? 1.29335  10.40261  31.04823 1.000 33.39301  ? 309 GLU A CB  1 
ATOM   2483 C  CG  . GLU A 1 314 ? 0.52605  9.40560   31.89411 1.000 33.62745  ? 309 GLU A CG  1 
ATOM   2484 C  CD  . GLU A 1 314 ? -0.94504 9.74675   31.99268 1.000 38.61876  ? 309 GLU A CD  1 
ATOM   2485 O  OE1 . GLU A 1 314 ? -1.26565 10.92650  32.24618 1.000 42.69779  ? 309 GLU A OE1 1 
ATOM   2486 O  OE2 . GLU A 1 314 ? -1.77769 8.83915   31.79536 1.000 40.48169  ? 309 GLU A OE2 1 
ATOM   2487 N  N   . PRO A 1 315 ? 3.63963  11.07198  33.01969 1.000 29.64813  ? 310 PRO A N   1 
ATOM   2488 C  CA  . PRO A 1 315 ? 4.14294  10.99731  34.39568 1.000 24.67030  ? 310 PRO A CA  1 
ATOM   2489 C  C   . PRO A 1 315 ? 3.20441  10.21321  35.29856 1.000 29.12178  ? 310 PRO A C   1 
ATOM   2490 O  O   . PRO A 1 315 ? 1.98003  10.29021  35.17448 1.000 30.63563  ? 310 PRO A O   1 
ATOM   2491 C  CB  . PRO A 1 315 ? 4.23299  12.46668  34.81806 1.000 24.76991  ? 310 PRO A CB  1 
ATOM   2492 C  CG  . PRO A 1 315 ? 4.44428  13.20159  33.53238 1.000 29.88379  ? 310 PRO A CG  1 
ATOM   2493 C  CD  . PRO A 1 315 ? 3.60372  12.45926  32.52538 1.000 27.10774  ? 310 PRO A CD  1 
ATOM   2494 N  N   . ALA A 1 316 ? 3.79672  9.45354   36.21474 1.000 30.00925  ? 311 ALA A N   1 
ATOM   2495 C  CA  . ALA A 1 316 ? 3.01333  8.66529   37.15847 1.000 33.08169  ? 311 ALA A CA  1 
ATOM   2496 C  C   . ALA A 1 316 ? 2.13822  9.56516   38.02496 1.000 28.55477  ? 311 ALA A C   1 
ATOM   2497 O  O   . ALA A 1 316 ? 2.59448  10.58763  38.54146 1.000 25.92827  ? 311 ALA A O   1 
ATOM   2498 C  CB  . ALA A 1 316 ? 3.94066  7.82902   38.03558 1.000 31.32321  ? 311 ALA A CB  1 
ATOM   2499 N  N   . ALA A 1 317 ? 0.87578  9.16306   38.19462 1.000 32.82712  ? 312 ALA A N   1 
ATOM   2500 C  CA  . ALA A 1 317 ? -0.07936 9.97791   38.94122 1.000 39.38334  ? 312 ALA A CA  1 
ATOM   2501 C  C   . ALA A 1 317 ? 0.38203  10.22290  40.37383 1.000 27.68233  ? 312 ALA A C   1 
ATOM   2502 O  O   . ALA A 1 317 ? 0.12451  11.29061  40.94021 1.000 29.24209  ? 312 ALA A O   1 
ATOM   2503 C  CB  . ALA A 1 317 ? -1.45494 9.31137   38.92803 1.000 38.19454  ? 312 ALA A CB  1 
ATOM   2504 N  N   . GLY A 1 318 ? 1.06060  9.24822   40.98062 1.000 31.18831  ? 313 GLY A N   1 
ATOM   2505 C  CA  . GLY A 1 318 ? 1.53877  9.41114   42.34394 1.000 28.62940  ? 313 GLY A CA  1 
ATOM   2506 C  C   . GLY A 1 318 ? 2.59267  10.48779  42.51348 1.000 37.46595  ? 313 GLY A C   1 
ATOM   2507 O  O   . GLY A 1 318 ? 2.84644  10.91970  43.64243 1.000 31.42879  ? 313 GLY A O   1 
ATOM   2508 N  N   . LEU A 1 319 ? 3.21372  10.93157  41.42041 1.000 26.63209  ? 314 LEU A N   1 
ATOM   2509 C  CA  . LEU A 1 319 ? 4.20969  11.99497  41.47312 1.000 24.98602  ? 314 LEU A CA  1 
ATOM   2510 C  C   . LEU A 1 319 ? 3.61861  13.37915  41.25706 1.000 28.26935  ? 314 LEU A C   1 
ATOM   2511 O  O   . LEU A 1 319 ? 4.34463  14.37244  41.38469 1.000 29.99242  ? 314 LEU A O   1 
ATOM   2512 C  CB  . LEU A 1 319 ? 5.29898  11.74924  40.42085 1.000 22.47602  ? 314 LEU A CB  1 
ATOM   2513 C  CG  . LEU A 1 319 ? 6.01541  10.40760  40.55807 1.000 26.19428  ? 314 LEU A CG  1 
ATOM   2514 C  CD1 . LEU A 1 319 ? 7.00082  10.22185  39.41318 1.000 23.75143  ? 314 LEU A CD1 1 
ATOM   2515 C  CD2 . LEU A 1 319 ? 6.72372  10.33432  41.89784 1.000 35.18254  ? 314 LEU A CD2 1 
ATOM   2516 N  N   . LEU A 1 320 ? 2.33085  13.47040  40.94048 1.000 24.49370  ? 315 LEU A N   1 
ATOM   2517 C  CA  . LEU A 1 320 ? 1.67574  14.72247  40.60456 1.000 24.16637  ? 315 LEU A CA  1 
ATOM   2518 C  C   . LEU A 1 320 ? 0.68107  15.10887  41.69131 1.000 32.57942  ? 315 LEU A C   1 
ATOM   2519 O  O   . LEU A 1 320 ? -0.08721 14.26978  42.16587 1.000 34.50565  ? 315 LEU A O   1 
ATOM   2520 C  CB  . LEU A 1 320 ? 0.94224  14.61001  39.26681 1.000 26.00703  ? 315 LEU A CB  1 
ATOM   2521 C  CG  . LEU A 1 320 ? 1.78101  14.14709  38.07508 1.000 23.76825  ? 315 LEU A CG  1 
ATOM   2522 C  CD1 . LEU A 1 320 ? 0.92573  14.07108  36.82415 1.000 27.20776  ? 315 LEU A CD1 1 
ATOM   2523 C  CD2 . LEU A 1 320 ? 2.97631  15.07561  37.86009 1.000 27.12204  ? 315 LEU A CD2 1 
ATOM   2524 N  N   . ASP A 1 321 ? 0.68876  16.38308  42.06992 1.000 28.38730  ? 316 ASP A N   1 
ATOM   2525 C  CA  . ASP A 1 321 ? -0.28908 16.92609  43.00509 1.000 29.64183  ? 316 ASP A CA  1 
ATOM   2526 C  C   . ASP A 1 321 ? -0.33268 18.43937  42.80407 1.000 29.85716  ? 316 ASP A C   1 
ATOM   2527 O  O   . ASP A 1 321 ? 0.28932  18.97615  41.87940 1.000 28.10283  ? 316 ASP A O   1 
ATOM   2528 C  CB  . ASP A 1 321 ? 0.02823  16.50119  44.44853 1.000 41.63306  ? 316 ASP A CB  1 
ATOM   2529 C  CG  . ASP A 1 321 ? 1.05981  17.39622  45.13733 1.000 53.02299  ? 316 ASP A CG  1 
ATOM   2530 O  OD1 . ASP A 1 321 ? 1.89069  18.02699  44.45672 1.000 49.64401  ? 316 ASP A OD1 1 
ATOM   2531 O  OD2 . ASP A 1 321 ? 1.04487  17.46040  46.38547 1.000 44.00860  ? 316 ASP A OD2 1 
ATOM   2532 N  N   . GLU A 1 322 ? -1.04818 19.13758  43.68705 1.000 25.42866  ? 317 GLU A N   1 
ATOM   2533 C  CA  . GLU A 1 322 ? -1.33201 20.54720  43.43999 1.000 26.31669  ? 317 GLU A CA  1 
ATOM   2534 C  C   . GLU A 1 322 ? -0.07098 21.40582  43.37292 1.000 30.21151  ? 317 GLU A C   1 
ATOM   2535 O  O   . GLU A 1 322 ? -0.11275 22.48755  42.77946 1.000 33.20208  ? 317 GLU A O   1 
ATOM   2536 C  CB  . GLU A 1 322 ? -2.28211 21.10036  44.50191 1.000 38.55019  ? 317 GLU A CB  1 
ATOM   2537 C  CG  . GLU A 1 322 ? -1.82462 20.91104  45.92463 1.000 36.41710  ? 317 GLU A CG  1 
ATOM   2538 C  CD  . GLU A 1 322 ? -2.90760 21.29190  46.92629 1.000 34.07455  ? 317 GLU A CD  1 
ATOM   2539 O  OE1 . GLU A 1 322 ? -3.26821 22.48297  46.99799 1.000 32.38075  ? 317 GLU A OE1 1 
ATOM   2540 O  OE2 . GLU A 1 322 ? -3.41318 20.38030  47.61761 1.000 42.48077  ? 317 GLU A OE2 1 
ATOM   2541 N  N   . ASN A 1 323 ? 1.03147  20.96887  43.97870 1.000 28.91430  ? 318 ASN A N   1 
ATOM   2542 C  CA  . ASN A 1 323 ? 2.27506  21.73177  43.98131 1.000 40.45743  ? 318 ASN A CA  1 
ATOM   2543 C  C   . ASN A 1 323 ? 3.33508  21.11410  43.08225 1.000 34.50034  ? 318 ASN A C   1 
ATOM   2544 O  O   . ASN A 1 323 ? 4.47566  21.58998  43.07014 1.000 27.03718  ? 318 ASN A O   1 
ATOM   2545 C  CB  . ASN A 1 323 ? 2.84033  21.85874  45.40310 1.000 40.41854  ? 318 ASN A CB  1 
ATOM   2546 C  CG  . ASN A 1 323 ? 1.85517  22.46059  46.38907 1.000 43.93214  ? 318 ASN A CG  1 
ATOM   2547 O  OD1 . ASN A 1 323 ? 1.73382  21.98098  47.53156 1.000 41.74108  ? 318 ASN A OD1 1 
ATOM   2548 N  ND2 . ASN A 1 323 ? 1.16104  23.52522  45.97379 1.000 34.49198  ? 318 ASN A ND2 1 
ATOM   2549 N  N   . ARG A 1 324 ? 2.99628  20.05421  42.34892 1.000 24.96772  ? 319 ARG A N   1 
ATOM   2550 C  CA  . ARG A 1 324 ? 3.97451  19.27771  41.59113 1.000 23.89924  ? 319 ARG A CA  1 
ATOM   2551 C  C   . ARG A 1 324 ? 3.42130  19.01690  40.20106 1.000 27.14343  ? 319 ARG A C   1 
ATOM   2552 O  O   . ARG A 1 324 ? 2.79383  17.98220  39.94574 1.000 27.78452  ? 319 ARG A O   1 
ATOM   2553 C  CB  . ARG A 1 324 ? 4.31807  17.96366  42.29916 1.000 33.74914  ? 319 ARG A CB  1 
ATOM   2554 C  CG  . ARG A 1 324 ? 4.93676  18.14707  43.68491 1.000 28.62077  ? 319 ARG A CG  1 
ATOM   2555 C  CD  . ARG A 1 324 ? 5.65611  16.88753  44.15786 1.000 39.76088  ? 319 ARG A CD  1 
ATOM   2556 N  NE  . ARG A 1 324 ? 4.72714  15.83205  44.53827 1.000 47.94573  ? 319 ARG A NE  1 
ATOM   2557 C  CZ  . ARG A 1 324 ? 5.06772  14.55974  44.70164 1.000 48.32600  ? 319 ARG A CZ  1 
ATOM   2558 N  NH1 . ARG A 1 324 ? 6.30996  14.14532  44.50720 1.000 60.08949  ? 319 ARG A NH1 1 
ATOM   2559 N  NH2 . ARG A 1 324 ? 4.13708  13.68051  45.06189 1.000 52.19382  ? 319 ARG A NH2 1 
ATOM   2560 N  N   . PRO A 1 325 ? 3.64910  19.93222  39.26837 1.000 26.25275  ? 320 PRO A N   1 
ATOM   2561 C  CA  . PRO A 1 325 ? 3.08554  19.78300  37.92442 1.000 25.88303  ? 320 PRO A CA  1 
ATOM   2562 C  C   . PRO A 1 325 ? 3.82448  18.74782  37.08843 1.000 25.43208  ? 320 PRO A C   1 
ATOM   2563 O  O   . PRO A 1 325 ? 4.98853  18.40934  37.32431 1.000 22.47855  ? 320 PRO A O   1 
ATOM   2564 C  CB  . PRO A 1 325 ? 3.25099  21.18215  37.32102 1.000 28.48365  ? 320 PRO A CB  1 
ATOM   2565 C  CG  . PRO A 1 325 ? 4.44104  21.74150  38.03045 1.000 29.37815  ? 320 PRO A CG  1 
ATOM   2566 C  CD  . PRO A 1 325 ? 4.34990  21.21587  39.44056 1.000 30.53374  ? 320 PRO A CD  1 
ATOM   2567 N  N   . ALA A 1 326 ? 3.11038  18.24851  36.08381 1.000 24.57729  ? 321 ALA A N   1 
ATOM   2568 C  CA  . ALA A 1 326 ? 3.72299  17.38745  35.08581 1.000 27.55304  ? 321 ALA A CA  1 
ATOM   2569 C  C   . ALA A 1 326 ? 4.74867  18.17461  34.28205 1.000 20.92790  ? 321 ALA A C   1 
ATOM   2570 O  O   . ALA A 1 326 ? 4.51458  19.32689  33.90003 1.000 24.34433  ? 321 ALA A O   1 
ATOM   2571 C  CB  . ALA A 1 326 ? 2.65976  16.81488  34.15273 1.000 27.42373  ? 321 ALA A CB  1 
ATOM   2572 N  N   A ARG A 1 327 ? 5.89546  17.54509  34.03302 0.500 26.54598  ? 322 ARG A N   1 
ATOM   2573 N  N   B ARG A 1 327 ? 5.89587  17.55230  34.02837 0.500 26.55776  ? 322 ARG A N   1 
ATOM   2574 C  CA  A ARG A 1 327 ? 6.95438  18.14964  33.23699 0.500 29.88897  ? 322 ARG A CA  1 
ATOM   2575 C  CA  B ARG A 1 327 ? 6.93085  18.18300  33.22154 0.500 29.87594  ? 322 ARG A CA  1 
ATOM   2576 C  C   A ARG A 1 327 ? 6.91921  17.72039  31.77706 0.500 29.68680  ? 322 ARG A C   1 
ATOM   2577 C  C   B ARG A 1 327 ? 6.90223  17.73780  31.76644 0.500 29.69249  ? 322 ARG A C   1 
ATOM   2578 O  O   A ARG A 1 327 ? 7.62356  18.31703  30.95571 0.500 27.71708  ? 322 ARG A O   1 
ATOM   2579 O  O   B ARG A 1 327 ? 7.59102  18.34205  30.93743 0.500 27.69573  ? 322 ARG A O   1 
ATOM   2580 C  CB  A ARG A 1 327 ? 8.32413  17.81448  33.84255 0.500 28.56616  ? 322 ARG A CB  1 
ATOM   2581 C  CB  B ARG A 1 327 ? 8.31216  17.90617  33.82738 0.500 28.66221  ? 322 ARG A CB  1 
ATOM   2582 C  CG  A ARG A 1 327 ? 8.57250  18.50655  35.18122 0.500 34.27000  ? 322 ARG A CG  1 
ATOM   2583 C  CG  B ARG A 1 327 ? 8.50438  18.57111  35.19052 0.500 34.22695  ? 322 ARG A CG  1 
ATOM   2584 C  CD  A ARG A 1 327 ? 9.89076  18.08860  35.81964 0.500 39.05724  ? 322 ARG A CD  1 
ATOM   2585 C  CD  B ARG A 1 327 ? 9.76436  18.09103  35.89518 0.500 39.07690  ? 322 ARG A CD  1 
ATOM   2586 N  NE  A ARG A 1 327 ? 11.03810 18.34244  34.95728 0.500 41.56581  ? 322 ARG A NE  1 
ATOM   2587 N  NE  B ARG A 1 327 ? 9.58355  18.05731  37.34245 0.500 44.74281  ? 322 ARG A NE  1 
ATOM   2588 C  CZ  A ARG A 1 327 ? 12.30055 18.30346  35.36224 0.500 49.17849  ? 322 ARG A CZ  1 
ATOM   2589 C  CZ  B ARG A 1 327 ? 10.37709 17.41140  38.18600 0.500 37.59225  ? 322 ARG A CZ  1 
ATOM   2590 N  NH1 A ARG A 1 327 ? 12.61530 18.03762  36.62032 0.500 48.47724  ? 322 ARG A NH1 1 
ATOM   2591 N  NH1 B ARG A 1 327 ? 11.44185 16.74996  37.76466 0.500 39.70780  ? 322 ARG A NH1 1 
ATOM   2592 N  NH2 A ARG A 1 327 ? 13.27119 18.54188  34.48442 0.500 48.51720  ? 322 ARG A NH2 1 
ATOM   2593 N  NH2 B ARG A 1 327 ? 10.09200 17.42625  39.48487 0.500 52.89753  ? 322 ARG A NH2 1 
ATOM   2594 N  N   . TYR A 1 328 ? 6.11291  16.71727  31.43739 1.000 25.10019  ? 323 TYR A N   1 
ATOM   2595 C  CA  . TYR A 1 328 ? 6.00819  16.19606  30.08136 1.000 27.39540  ? 323 TYR A CA  1 
ATOM   2596 C  C   . TYR A 1 328 ? 4.54475  15.92220  29.78723 1.000 37.29608  ? 323 TYR A C   1 
ATOM   2597 O  O   . TYR A 1 328 ? 3.79963  15.47743  30.66794 1.000 30.44203  ? 323 TYR A O   1 
ATOM   2598 C  CB  . TYR A 1 328 ? 6.80860  14.89744  29.89800 1.000 28.17448  ? 323 TYR A CB  1 
ATOM   2599 C  CG  . TYR A 1 328 ? 8.21915  14.97039  30.41297 1.000 26.67216  ? 323 TYR A CG  1 
ATOM   2600 C  CD1 . TYR A 1 328 ? 8.49476  14.72892  31.74848 1.000 27.12364  ? 323 TYR A CD1 1 
ATOM   2601 C  CD2 . TYR A 1 328 ? 9.27972  15.27696  29.56594 1.000 31.03274  ? 323 TYR A CD2 1 
ATOM   2602 C  CE1 . TYR A 1 328 ? 9.77644  14.80061  32.23960 1.000 35.59559  ? 323 TYR A CE1 1 
ATOM   2603 C  CE2 . TYR A 1 328 ? 10.58196 15.34365  30.05100 1.000 33.10175  ? 323 TYR A CE2 1 
ATOM   2604 C  CZ  . TYR A 1 328 ? 10.81894 15.10252  31.38878 1.000 30.23332  ? 323 TYR A CZ  1 
ATOM   2605 O  OH  . TYR A 1 328 ? 12.09101 15.17156  31.90851 1.000 32.05848  ? 323 TYR A OH  1 
ATOM   2606 N  N   . ARG A 1 329 ? 4.13261  16.17776  28.55266 1.000 27.71988  ? 324 ARG A N   1 
ATOM   2607 C  CA  . ARG A 1 329 ? 2.73743  15.92755  28.25589 1.000 29.82886  ? 324 ARG A CA  1 
ATOM   2608 C  C   . ARG A 1 329 ? 2.53023  14.47006  27.85972 1.000 34.27695  ? 324 ARG A C   1 
ATOM   2609 O  O   . ARG A 1 329 ? 3.46973  13.74448  27.52053 1.000 33.13912  ? 324 ARG A O   1 
ATOM   2610 C  CB  . ARG A 1 329 ? 2.23103  16.86345  27.16270 1.000 43.28598  ? 324 ARG A CB  1 
ATOM   2611 C  CG  . ARG A 1 329 ? 2.67580  16.49235  25.77918 1.000 40.04792  ? 324 ARG A CG  1 
ATOM   2612 C  CD  . ARG A 1 329 ? 1.89079  17.27064  24.73566 1.000 45.14859  ? 324 ARG A CD  1 
ATOM   2613 N  NE  . ARG A 1 329 ? 2.42238  17.02945  23.39808 1.000 44.16607  ? 324 ARG A NE  1 
ATOM   2614 C  CZ  . ARG A 1 329 ? 2.00724  16.06059  22.59200 1.000 57.48484  ? 324 ARG A CZ  1 
ATOM   2615 N  NH1 . ARG A 1 329 ? 1.00261  15.26306  22.92777 1.000 50.61607  ? 324 ARG A NH1 1 
ATOM   2616 N  NH2 . ARG A 1 329 ? 2.61850  15.88143  21.42296 1.000 52.33396  ? 324 ARG A NH2 1 
ATOM   2617 N  N   . LYS A 1 330 ? 1.27253  14.04853  27.92404 1.000 29.17960  ? 325 LYS A N   1 
ATOM   2618 C  CA  . LYS A 1 330 ? 0.90381  12.66088  27.68556 1.000 33.28636  ? 325 LYS A CA  1 
ATOM   2619 C  C   . LYS A 1 330 ? 0.81079  12.37528  26.19025 1.000 28.21534  ? 325 LYS A C   1 
ATOM   2620 O  O   . LYS A 1 330 ? 0.25260  13.16844  25.42631 1.000 32.52348  ? 325 LYS A O   1 
ATOM   2621 C  CB  . LYS A 1 330 ? -0.43172 12.36329  28.37043 1.000 34.31805  ? 325 LYS A CB  1 
ATOM   2622 C  CG  . LYS A 1 330 ? -1.05193 11.04036  27.99012 1.000 37.43813  ? 325 LYS A CG  1 
ATOM   2623 C  CD  . LYS A 1 330 ? -2.24619 10.69648  28.87346 1.000 42.91903  ? 325 LYS A CD  1 
ATOM   2624 C  CE  . LYS A 1 330 ? -3.45630 11.54531  28.54775 1.000 41.27941  ? 325 LYS A CE  1 
ATOM   2625 N  NZ  . LYS A 1 330 ? -4.66237 11.03737  29.26520 1.000 54.67516  ? 325 LYS A NZ  1 
ATOM   2626 N  N   . VAL A 1 331 ? 1.37372  11.23942  25.77082 1.000 32.83473  ? 326 VAL A N   1 
ATOM   2627 C  CA  . VAL A 1 331 ? 1.33545  10.81799  24.37571 1.000 31.28631  ? 326 VAL A CA  1 
ATOM   2628 C  C   . VAL A 1 331 ? 1.03986  9.32718   24.30823 1.000 33.40689  ? 326 VAL A C   1 
ATOM   2629 O  O   . VAL A 1 331 ? 1.43818  8.55268   25.18335 1.000 32.93563  ? 326 VAL A O   1 
ATOM   2630 C  CB  . VAL A 1 331 ? 2.65436  11.12115  23.62965 1.000 41.53258  ? 326 VAL A CB  1 
ATOM   2631 C  CG1 . VAL A 1 331 ? 2.78593  12.60216  23.35500 1.000 39.88613  ? 326 VAL A CG1 1 
ATOM   2632 C  CG2 . VAL A 1 331 ? 3.84381  10.60844  24.42732 1.000 36.29252  ? 326 VAL A CG2 1 
ATOM   2633 N  N   . SER A 1 332 ? 0.35121  8.92340   23.24558 1.000 35.33414  ? 327 SER A N   1 
ATOM   2634 C  CA  . SER A 1 332 ? 0.14959  7.50456   23.01150 1.000 39.24112  ? 327 SER A CA  1 
ATOM   2635 C  C   . SER A 1 332 ? 1.48185  6.83146   22.70062 1.000 37.91087  ? 327 SER A C   1 
ATOM   2636 O  O   . SER A 1 332 ? 2.45251  7.47428   22.28935 1.000 34.36577  ? 327 SER A O   1 
ATOM   2637 C  CB  . SER A 1 332 ? -0.83173 7.28017   21.86230 1.000 46.64466  ? 327 SER A CB  1 
ATOM   2638 O  OG  . SER A 1 332 ? -0.26377 7.68749   20.63007 1.000 43.75488  ? 327 SER A OG  1 
ATOM   2639 N  N   . VAL A 1 333 ? 1.51869  5.51217   22.90463 1.000 37.69004  ? 328 VAL A N   1 
ATOM   2640 C  CA  . VAL A 1 333 ? 2.73241  4.75084   22.62145 1.000 36.23656  ? 328 VAL A CA  1 
ATOM   2641 C  C   . VAL A 1 333 ? 3.06342  4.80640   21.13520 1.000 40.25921  ? 328 VAL A C   1 
ATOM   2642 O  O   . VAL A 1 333 ? 4.23712  4.85582   20.74640 1.000 38.89706  ? 328 VAL A O   1 
ATOM   2643 C  CB  . VAL A 1 333 ? 2.57866  3.30043   23.11386 1.000 44.31634  ? 328 VAL A CB  1 
ATOM   2644 C  CG1 . VAL A 1 333 ? 3.84104  2.50628   22.82740 1.000 46.69833  ? 328 VAL A CG1 1 
ATOM   2645 C  CG2 . VAL A 1 333 ? 2.26899  3.27665   24.59778 1.000 36.49235  ? 328 VAL A CG2 1 
ATOM   2646 N  N   . GLU A 1 334 ? 2.03549  4.80541   20.28302 1.000 38.27269  ? 329 GLU A N   1 
ATOM   2647 C  CA  . GLU A 1 334 ? 2.25341  4.88508   18.84167 1.000 45.18150  ? 329 GLU A CA  1 
ATOM   2648 C  C   . GLU A 1 334 ? 2.90007  6.21008   18.45375 1.000 44.68474  ? 329 GLU A C   1 
ATOM   2649 O  O   . GLU A 1 334 ? 3.85170  6.24678   17.66345 1.000 41.38407  ? 329 GLU A O   1 
ATOM   2650 C  CB  . GLU A 1 334 ? 0.92433  4.69774   18.10977 1.000 49.30004  ? 329 GLU A CB  1 
ATOM   2651 C  CG  . GLU A 1 334 ? 0.99145  4.95662   16.61659 1.000 65.32633  ? 329 GLU A CG  1 
ATOM   2652 C  CD  . GLU A 1 334 ? -0.37838 4.94531   15.96597 1.000 75.47288  ? 329 GLU A CD  1 
ATOM   2653 O  OE1 . GLU A 1 334 ? -1.34324 4.47888   16.61042 1.000 70.82990  ? 329 GLU A OE1 1 
ATOM   2654 O  OE2 . GLU A 1 334 ? -0.49100 5.40923   14.81172 1.000 82.11206  ? 329 GLU A OE2 1 
ATOM   2655 N  N   . GLU A 1 335 ? 2.38613  7.31627   18.99366 1.000 40.14321  ? 330 GLU A N   1 
ATOM   2656 C  CA  . GLU A 1 335 ? 2.97795  8.61758   18.70570 1.000 42.68111  ? 330 GLU A CA  1 
ATOM   2657 C  C   . GLU A 1 335 ? 4.36305  8.74066   19.33005 1.000 39.62914  ? 330 GLU A C   1 
ATOM   2658 O  O   . GLU A 1 335 ? 5.27385  9.32289   18.72915 1.000 35.88415  ? 330 GLU A O   1 
ATOM   2659 C  CB  . GLU A 1 335 ? 2.05109  9.72281   19.20747 1.000 45.05365  ? 330 GLU A CB  1 
ATOM   2660 C  CG  . GLU A 1 335 ? 2.55181  11.12474  18.95836 1.000 44.01933  ? 330 GLU A CG  1 
ATOM   2661 C  CD  . GLU A 1 335 ? 1.58256  12.17856  19.45887 1.000 55.45135  ? 330 GLU A CD  1 
ATOM   2662 O  OE1 . GLU A 1 335 ? 0.38185  11.86136  19.61495 1.000 55.23358  ? 330 GLU A OE1 1 
ATOM   2663 O  OE2 . GLU A 1 335 ? 2.02364  13.32117  19.70029 1.000 51.73927  ? 330 GLU A OE2 1 
ATOM   2664 N  N   . PHE A 1 336 ? 4.53562  8.19818   20.53664 1.000 34.10189  ? 331 PHE A N   1 
ATOM   2665 C  CA  . PHE A 1 336 ? 5.84442  8.18722   21.18277 1.000 34.37236  ? 331 PHE A CA  1 
ATOM   2666 C  C   . PHE A 1 336 ? 6.85726  7.43063   20.33243 1.000 36.96012  ? 331 PHE A C   1 
ATOM   2667 O  O   . PHE A 1 336 ? 7.98086  7.89958   20.11421 1.000 31.76400  ? 331 PHE A O   1 
ATOM   2668 C  CB  . PHE A 1 336 ? 5.71124  7.55595   22.57082 1.000 32.00837  ? 331 PHE A CB  1 
ATOM   2669 C  CG  . PHE A 1 336 ? 6.89238  7.77917   23.47462 1.000 32.40194  ? 331 PHE A CG  1 
ATOM   2670 C  CD1 . PHE A 1 336 ? 6.93939  8.88318   24.31073 1.000 32.81213  ? 331 PHE A CD1 1 
ATOM   2671 C  CD2 . PHE A 1 336 ? 7.93223  6.86499   23.52037 1.000 33.23503  ? 331 PHE A CD2 1 
ATOM   2672 C  CE1 . PHE A 1 336 ? 8.00804  9.08530   25.15895 1.000 30.39341  ? 331 PHE A CE1 1 
ATOM   2673 C  CE2 . PHE A 1 336 ? 9.00591  7.06269   24.36744 1.000 33.31488  ? 331 PHE A CE2 1 
ATOM   2674 C  CZ  . PHE A 1 336 ? 9.04287  8.17475   25.18522 1.000 29.32698  ? 331 PHE A CZ  1 
ATOM   2675 N  N   . ARG A 1 337 ? 6.46161  6.25653   19.83293 1.000 31.17376  ? 332 ARG A N   1 
ATOM   2676 C  CA  . ARG A 1 337 ? 7.33565  5.45462   18.97971 1.000 34.24142  ? 332 ARG A CA  1 
ATOM   2677 C  C   . ARG A 1 337 ? 7.75918  6.22489   17.73932 1.000 35.06249  ? 332 ARG A C   1 
ATOM   2678 O  O   . ARG A 1 337 ? 8.94768  6.28650   17.40884 1.000 32.61474  ? 332 ARG A O   1 
ATOM   2679 C  CB  . ARG A 1 337 ? 6.62649  4.16776   18.56574 1.000 39.42660  ? 332 ARG A CB  1 
ATOM   2680 C  CG  . ARG A 1 337 ? 6.65617  3.06338   19.58952 1.000 52.01035  ? 332 ARG A CG  1 
ATOM   2681 C  CD  . ARG A 1 337 ? 6.37341  1.73092   18.91398 1.000 60.96568  ? 332 ARG A CD  1 
ATOM   2682 N  NE  . ARG A 1 337 ? 4.99656  1.62248   18.45065 1.000 62.40590  ? 332 ARG A NE  1 
ATOM   2683 C  CZ  . ARG A 1 337 ? 4.06519  0.89188   19.04709 1.000 63.64252  ? 332 ARG A CZ  1 
ATOM   2684 N  NH1 . ARG A 1 337 ? 4.33795  0.16797   20.12064 1.000 62.73528  ? 332 ARG A NH1 1 
ATOM   2685 N  NH2 . ARG A 1 337 ? 2.83036  0.88546   18.55270 1.000 60.92016  ? 332 ARG A NH2 1 
ATOM   2686 N  N   . ALA A 1 338 ? 6.78823  6.79544   17.02216 1.000 34.15238  ? 333 ALA A N   1 
ATOM   2687 C  CA  . ALA A 1 338 ? 7.09868  7.54253   15.80985 1.000 41.28753  ? 333 ALA A CA  1 
ATOM   2688 C  C   . ALA A 1 338 ? 8.03073  8.70790   16.10541 1.000 42.05407  ? 333 ALA A C   1 
ATOM   2689 O  O   . ALA A 1 338 ? 8.90880  9.03026   15.29711 1.000 38.94577  ? 333 ALA A O   1 
ATOM   2690 C  CB  . ALA A 1 338 ? 5.80914  8.03952   15.15646 1.000 39.38467  ? 333 ALA A CB  1 
ATOM   2691 N  N   . GLY A 1 339 ? 7.86348  9.34616   17.26573 1.000 36.59634  ? 334 GLY A N   1 
ATOM   2692 C  CA  . GLY A 1 339 ? 8.72644  10.46392  17.60805 1.000 36.49734  ? 334 GLY A CA  1 
ATOM   2693 C  C   . GLY A 1 339 ? 10.14850 10.03319  17.91248 1.000 33.93535  ? 334 GLY A C   1 
ATOM   2694 O  O   . GLY A 1 339 ? 11.10586 10.66319  17.45662 1.000 34.20600  ? 334 GLY A O   1 
ATOM   2695 N  N   . ILE A 1 340 ? 10.30830 8.96105   18.69255 1.000 28.39686  ? 335 ILE A N   1 
ATOM   2696 C  CA  . ILE A 1 340 ? 11.64557 8.46438   19.01198 1.000 27.18191  ? 335 ILE A CA  1 
ATOM   2697 C  C   . ILE A 1 340 ? 12.37740 8.05940   17.73832 1.000 30.15789  ? 335 ILE A C   1 
ATOM   2698 O  O   . ILE A 1 340 ? 13.54391 8.41469   17.52785 1.000 32.83267  ? 335 ILE A O   1 
ATOM   2699 C  CB  . ILE A 1 340 ? 11.56276 7.28846   20.00013 1.000 29.36291  ? 335 ILE A CB  1 
ATOM   2700 C  CG1 . ILE A 1 340 ? 11.02401 7.75701   21.35363 1.000 34.12968  ? 335 ILE A CG1 1 
ATOM   2701 C  CG2 . ILE A 1 340 ? 12.93376 6.64721   20.16885 1.000 35.92776  ? 335 ILE A CG2 1 
ATOM   2702 C  CD1 . ILE A 1 340 ? 11.93747 8.71516   22.06211 1.000 28.73012  ? 335 ILE A CD1 1 
ATOM   2703 N  N   . PHE A 1 341 ? 11.69895 7.31166   16.86765 1.000 32.45335  ? 336 PHE A N   1 
ATOM   2704 C  CA  . PHE A 1 341 ? 12.35252 6.82263   15.65575 1.000 34.89481  ? 336 PHE A CA  1 
ATOM   2705 C  C   . PHE A 1 341 ? 12.63013 7.96059   14.68055 1.000 40.26091  ? 336 PHE A C   1 
ATOM   2706 O  O   . PHE A 1 341 ? 13.71645 8.03162   14.09332 1.000 39.42803  ? 336 PHE A O   1 
ATOM   2707 C  CB  . PHE A 1 341 ? 11.49470 5.74310   14.98934 1.000 39.50449  ? 336 PHE A CB  1 
ATOM   2708 C  CG  . PHE A 1 341 ? 11.25994 4.52372   15.84811 1.000 40.80359  ? 336 PHE A CG  1 
ATOM   2709 C  CD1 . PHE A 1 341 ? 12.07765 4.24702   16.93161 1.000 38.91115  ? 336 PHE A CD1 1 
ATOM   2710 C  CD2 . PHE A 1 341 ? 10.21750 3.65450   15.56610 1.000 44.54572  ? 336 PHE A CD2 1 
ATOM   2711 C  CE1 . PHE A 1 341 ? 11.85796 3.12926   17.71954 1.000 42.41043  ? 336 PHE A CE1 1 
ATOM   2712 C  CE2 . PHE A 1 341 ? 9.99424  2.53290   16.34691 1.000 44.07762  ? 336 PHE A CE2 1 
ATOM   2713 C  CZ  . PHE A 1 341 ? 10.81441 2.27109   17.42577 1.000 44.96284  ? 336 PHE A CZ  1 
ATOM   2714 N  N   . GLY A 1 342 ? 11.66370 8.86379   14.50083 1.000 33.31697  ? 337 GLY A N   1 
ATOM   2715 C  CA  . GLY A 1 342 ? 11.82002 9.91441   13.50944 1.000 34.81941  ? 337 GLY A CA  1 
ATOM   2716 C  C   . GLY A 1 342 ? 12.83554 10.96549  13.91340 1.000 35.87629  ? 337 GLY A C   1 
ATOM   2717 O  O   . GLY A 1 342 ? 13.60712 11.44579  13.08065 1.000 38.74667  ? 337 GLY A O   1 
ATOM   2718 N  N   . LYS A 1 343 ? 12.84973 11.34355  15.19275 1.000 35.60799  ? 338 LYS A N   1 
ATOM   2719 C  CA  . LYS A 1 343 ? 13.80631 12.34916  15.64223 1.000 35.52269  ? 338 LYS A CA  1 
ATOM   2720 C  C   . LYS A 1 343 ? 15.22731 11.80350  15.68384 1.000 34.54587  ? 338 LYS A C   1 
ATOM   2721 O  O   . LYS A 1 343 ? 16.18293 12.56499  15.49993 1.000 36.18427  ? 338 LYS A O   1 
ATOM   2722 C  CB  . LYS A 1 343 ? 13.40547 12.88450  17.01575 1.000 34.47024  ? 338 LYS A CB  1 
ATOM   2723 C  CG  . LYS A 1 343 ? 12.12215 13.69400  17.01058 1.000 36.40257  ? 338 LYS A CG  1 
ATOM   2724 C  CD  . LYS A 1 343 ? 12.36566 15.13511  16.59266 1.000 49.32825  ? 338 LYS A CD  1 
ATOM   2725 C  CE  . LYS A 1 343 ? 11.11499 15.98834  16.78097 1.000 50.80830  ? 338 LYS A CE  1 
ATOM   2726 N  NZ  . LYS A 1 343 ? 11.32197 17.39801  16.33951 1.000 77.43481  ? 338 LYS A NZ  1 
ATOM   2727 N  N   . PHE A 1 344 ? 15.39094 10.50264  15.93687 1.000 34.52825  ? 339 PHE A N   1 
ATOM   2728 C  CA  . PHE A 1 344 ? 16.72027 9.90565   15.86889 1.000 35.41201  ? 339 PHE A CA  1 
ATOM   2729 C  C   . PHE A 1 344 ? 17.31401 10.06172  14.47647 1.000 30.37752  ? 339 PHE A C   1 
ATOM   2730 O  O   . PHE A 1 344 ? 18.50978 10.33986  14.33161 1.000 31.69909  ? 339 PHE A O   1 
ATOM   2731 C  CB  . PHE A 1 344 ? 16.66438 8.42563   16.25213 1.000 33.36030  ? 339 PHE A CB  1 
ATOM   2732 C  CG  . PHE A 1 344 ? 18.00359 7.73743   16.20264 1.000 30.26534  ? 339 PHE A CG  1 
ATOM   2733 C  CD1 . PHE A 1 344 ? 18.84666 7.76213   17.30190 1.000 33.63049  ? 339 PHE A CD1 1 
ATOM   2734 C  CD2 . PHE A 1 344 ? 18.41824 7.06435   15.05891 1.000 32.44748  ? 339 PHE A CD2 1 
ATOM   2735 C  CE1 . PHE A 1 344 ? 20.07911 7.13599   17.26470 1.000 29.82247  ? 339 PHE A CE1 1 
ATOM   2736 C  CE2 . PHE A 1 344 ? 19.64894 6.43151   15.01534 1.000 30.95887  ? 339 PHE A CE2 1 
ATOM   2737 C  CZ  . PHE A 1 344 ? 20.48084 6.46739   16.11751 1.000 29.49103  ? 339 PHE A CZ  1 
ATOM   2738 N  N   . SER A 1 345 ? 16.48778 9.88476   13.44033 1.000 29.65026  ? 340 SER A N   1 
ATOM   2739 C  CA  . SER A 1 345 ? 16.96807 10.00336  12.06704 1.000 34.95251  ? 340 SER A CA  1 
ATOM   2740 C  C   . SER A 1 345 ? 17.48277 11.40477  11.77308 1.000 42.10640  ? 340 SER A C   1 
ATOM   2741 O  O   . SER A 1 345 ? 18.38946 11.57244  10.94827 1.000 39.42087  ? 340 SER A O   1 
ATOM   2742 C  CB  . SER A 1 345 ? 15.84937 9.63899   11.09396 1.000 38.34183  ? 340 SER A CB  1 
ATOM   2743 O  OG  . SER A 1 345 ? 15.28890 8.37863   11.41679 1.000 45.07784  ? 340 SER A OG  1 
ATOM   2744 N  N   . ARG A 1 346 ? 16.92226 12.41782  12.43267 1.000 34.77294  ? 341 ARG A N   1 
ATOM   2745 C  CA  . ARG A 1 346 ? 17.33511 13.80203  12.24450 1.000 41.28996  ? 341 ARG A CA  1 
ATOM   2746 C  C   . ARG A 1 346 ? 18.38808 14.24358  13.24869 1.000 39.25320  ? 341 ARG A C   1 
ATOM   2747 O  O   . ARG A 1 346 ? 18.84195 15.39036  13.18404 1.000 42.18281  ? 341 ARG A O   1 
ATOM   2748 C  CB  . ARG A 1 346 ? 16.12865 14.73997  12.34564 1.000 39.76532  ? 341 ARG A CB  1 
ATOM   2749 C  CG  . ARG A 1 346 ? 14.93223 14.33773  11.50740 1.000 48.74789  ? 341 ARG A CG  1 
ATOM   2750 C  CD  . ARG A 1 346 ? 13.84205 15.39825  11.58689 1.000 55.37889  ? 341 ARG A CD  1 
ATOM   2751 N  NE  . ARG A 1 346 ? 12.52705 14.85246  11.27151 1.000 80.54977  ? 341 ARG A NE  1 
ATOM   2752 C  CZ  . ARG A 1 346 ? 11.67017 14.39435  12.17510 1.000 67.04600  ? 341 ARG A CZ  1 
ATOM   2753 N  NH1 . ARG A 1 346 ? 11.95331 14.41051  13.46698 1.000 72.94403  ? 341 ARG A NH1 1 
ATOM   2754 N  NH2 . ARG A 1 346 ? 10.49901 13.90888  11.77257 1.000 66.46738  ? 341 ARG A NH2 1 
ATOM   2755 N  N   . GLY A 1 347 ? 18.78490 13.37111  14.16948 1.000 36.01597  ? 342 GLY A N   1 
ATOM   2756 C  CA  . GLY A 1 347 ? 19.70536 13.77080  15.21553 1.000 42.29318  ? 342 GLY A CA  1 
ATOM   2757 C  C   . GLY A 1 347 ? 19.12130 14.75055  16.20883 1.000 44.61706  ? 342 GLY A C   1 
ATOM   2758 O  O   . GLY A 1 347 ? 19.84755 15.60559  16.72563 1.000 49.04324  ? 342 GLY A O   1 
ATOM   2759 N  N   . GLU A 1 348 ? 17.82451 14.65345  16.48682 1.000 42.11295  ? 343 GLU A N   1 
ATOM   2760 C  CA  . GLU A 1 348 ? 17.13603 15.54735  17.40756 1.000 35.24474  ? 343 GLU A CA  1 
ATOM   2761 C  C   . GLU A 1 348 ? 16.61686 14.76067  18.60517 1.000 38.60830  ? 343 GLU A C   1 
ATOM   2762 O  O   . GLU A 1 348 ? 16.54252 13.53034  18.58389 1.000 39.28248  ? 343 GLU A O   1 
ATOM   2763 C  CB  . GLU A 1 348 ? 15.98791 16.27998  16.70046 1.000 38.59249  ? 343 GLU A CB  1 
ATOM   2764 C  CG  . GLU A 1 348 ? 16.45745 17.22016  15.60697 1.000 43.31672  ? 343 GLU A CG  1 
ATOM   2765 C  CD  . GLU A 1 348 ? 15.34328 17.62711  14.66584 1.000 48.13917  ? 343 GLU A CD  1 
ATOM   2766 O  OE1 . GLU A 1 348 ? 14.18102 17.24382  14.91570 1.000 57.98718  ? 343 GLU A OE1 1 
ATOM   2767 O  OE2 . GLU A 1 348 ? 15.63087 18.32637  13.67172 1.000 57.74615  ? 343 GLU A OE2 1 
ATOM   2768 N  N   . ARG A 1 349 ? 16.25426 15.49082  19.66286 1.000 33.93641  ? 344 ARG A N   1 
ATOM   2769 C  CA  . ARG A 1 349 ? 15.80384 14.89303  20.91869 1.000 39.31980  ? 344 ARG A CA  1 
ATOM   2770 C  C   . ARG A 1 349 ? 14.28425 14.99578  20.98781 1.000 32.42400  ? 344 ARG A C   1 
ATOM   2771 O  O   . ARG A 1 349 ? 13.73672 16.08741  21.17143 1.000 35.69248  ? 344 ARG A O   1 
ATOM   2772 C  CB  . ARG A 1 349 ? 16.45895 15.58086  22.11590 1.000 39.88757  ? 344 ARG A CB  1 
ATOM   2773 C  CG  . ARG A 1 349 ? 16.14195 14.92792  23.46085 1.000 48.26731  ? 344 ARG A CG  1 
ATOM   2774 C  CD  . ARG A 1 349 ? 17.38228 14.31554  24.10282 1.000 41.04644  ? 344 ARG A CD  1 
ATOM   2775 N  NE  . ARG A 1 349 ? 17.04116 13.30524  25.09825 1.000 35.66824  ? 344 ARG A NE  1 
ATOM   2776 C  CZ  . ARG A 1 349 ? 17.04859 13.50552  26.40814 1.000 42.58518  ? 344 ARG A CZ  1 
ATOM   2777 N  NH1 . ARG A 1 349 ? 17.36599 14.68121  26.92505 1.000 55.49281  ? 344 ARG A NH1 1 
ATOM   2778 N  NH2 . ARG A 1 349 ? 16.72899 12.50085  27.21961 1.000 41.18954  ? 344 ARG A NH2 1 
ATOM   2779 N  N   . TYR A 1 350 ? 13.60424 13.85606  20.84900 1.000 32.22911  ? 345 TYR A N   1 
ATOM   2780 C  CA  . TYR A 1 350 ? 12.14514 13.87340  20.81355 1.000 33.65737  ? 345 TYR A CA  1 
ATOM   2781 C  C   . TYR A 1 350 ? 11.55411 14.32626  22.14255 1.000 28.92599  ? 345 TYR A C   1 
ATOM   2782 O  O   . TYR A 1 350 ? 10.56855 15.07165  22.16702 1.000 35.27348  ? 345 TYR A O   1 
ATOM   2783 C  CB  . TYR A 1 350 ? 11.61010 12.49383  20.45240 1.000 28.29035  ? 345 TYR A CB  1 
ATOM   2784 C  CG  . TYR A 1 350 ? 10.11302 12.37012  20.62291 1.000 33.28364  ? 345 TYR A CG  1 
ATOM   2785 C  CD1 . TYR A 1 350 ? 9.24156  13.14399  19.86675 1.000 34.20869  ? 345 TYR A CD1 1 
ATOM   2786 C  CD2 . TYR A 1 350 ? 9.57048  11.47319  21.53230 1.000 32.55905  ? 345 TYR A CD2 1 
ATOM   2787 C  CE1 . TYR A 1 350 ? 7.86687  13.03281  20.01844 1.000 36.49620  ? 345 TYR A CE1 1 
ATOM   2788 C  CE2 . TYR A 1 350 ? 8.19867  11.35132  21.68744 1.000 32.29816  ? 345 TYR A CE2 1 
ATOM   2789 C  CZ  . TYR A 1 350 ? 7.35438  12.13230  20.93217 1.000 34.67319  ? 345 TYR A CZ  1 
ATOM   2790 O  OH  . TYR A 1 350 ? 5.99163  12.00913  21.08917 1.000 39.94521  ? 345 TYR A OH  1 
ATOM   2791 N  N   . ILE A 1 351 ? 12.13726 13.87878  23.25680 1.000 31.45970  ? 346 ILE A N   1 
ATOM   2792 C  CA  . ILE A 1 351 ? 11.55429 14.15862  24.56842 1.000 33.13129  ? 346 ILE A CA  1 
ATOM   2793 C  C   . ILE A 1 351 ? 11.48408 15.65885  24.82142 1.000 37.17958  ? 346 ILE A C   1 
ATOM   2794 O  O   . ILE A 1 351 ? 10.60657 16.13214  25.55427 1.000 29.70381  ? 346 ILE A O   1 
ATOM   2795 C  CB  . ILE A 1 351 ? 12.34415 13.42247  25.67232 1.000 32.27954  ? 346 ILE A CB  1 
ATOM   2796 C  CG1 . ILE A 1 351 ? 11.51795 13.33156  26.95380 1.000 31.35058  ? 346 ILE A CG1 1 
ATOM   2797 C  CG2 . ILE A 1 351 ? 13.65673 14.12800  25.97383 1.000 40.43152  ? 346 ILE A CG2 1 
ATOM   2798 C  CD1 . ILE A 1 351 ? 12.21185 12.56816  28.06433 1.000 29.11096  ? 346 ILE A CD1 1 
ATOM   2799 N  N   . ASP A 1 352 ? 12.38274 16.43381  24.20470 1.000 30.88424  ? 347 ASP A N   1 
ATOM   2800 C  CA  . ASP A 1 352 ? 12.34225 17.88309  24.35628 1.000 33.78798  ? 347 ASP A CA  1 
ATOM   2801 C  C   . ASP A 1 352 ? 11.03212 18.46242  23.84415 1.000 31.31466  ? 347 ASP A C   1 
ATOM   2802 O  O   . ASP A 1 352 ? 10.55186 19.47238  24.37190 1.000 37.75127  ? 347 ASP A O   1 
ATOM   2803 C  CB  . ASP A 1 352 ? 13.52047 18.52586  23.62049 1.000 43.46416  ? 347 ASP A CB  1 
ATOM   2804 C  CG  . ASP A 1 352 ? 14.83110 18.37816  24.36928 1.000 47.67787  ? 347 ASP A CG  1 
ATOM   2805 O  OD1 . ASP A 1 352 ? 14.80789 17.90968  25.52403 1.000 44.35679  ? 347 ASP A OD1 1 
ATOM   2806 O  OD2 . ASP A 1 352 ? 15.88515 18.74061  23.80177 1.000 45.82769  ? 347 ASP A OD2 1 
ATOM   2807 N  N   . SER A 1 353 ? 10.44179 17.84225  22.82074 1.000 30.10819  ? 348 SER A N   1 
ATOM   2808 C  CA  . SER A 1 353 ? 9.18830  18.33878  22.27154 1.000 30.97943  ? 348 SER A CA  1 
ATOM   2809 C  C   . SER A 1 353 ? 8.01499  18.06251  23.19805 1.000 35.01160  ? 348 SER A C   1 
ATOM   2810 O  O   . SER A 1 353 ? 6.95346  18.66711  23.02499 1.000 35.55369  ? 348 SER A O   1 
ATOM   2811 C  CB  . SER A 1 353 ? 8.91745  17.71566  20.90025 1.000 32.25622  ? 348 SER A CB  1 
ATOM   2812 O  OG  . SER A 1 353 ? 8.63645  16.33092  21.01083 1.000 34.78612  ? 348 SER A OG  1 
ATOM   2813 N  N   . LEU A 1 354 ? 8.18536  17.16342  24.16544 1.000 30.59151  ? 349 LEU A N   1 
ATOM   2814 C  CA  . LEU A 1 354 ? 7.14499  16.82831  25.12715 1.000 29.37041  ? 349 LEU A CA  1 
ATOM   2815 C  C   . LEU A 1 354 ? 7.18813  17.69567  26.37502 1.000 34.28426  ? 349 LEU A C   1 
ATOM   2816 O  O   . LEU A 1 354 ? 6.22820  17.66998  27.15708 1.000 28.91116  ? 349 LEU A O   1 
ATOM   2817 C  CB  . LEU A 1 354 ? 7.26217  15.35593  25.54004 1.000 24.10850  ? 349 LEU A CB  1 
ATOM   2818 C  CG  . LEU A 1 354 ? 7.09112  14.34227  24.40922 1.000 29.48494  ? 349 LEU A CG  1 
ATOM   2819 C  CD1 . LEU A 1 354 ? 7.15776  12.92477  24.94525 1.000 35.16385  ? 349 LEU A CD1 1 
ATOM   2820 C  CD2 . LEU A 1 354 ? 5.78726  14.60148  23.66229 1.000 30.60980  ? 349 LEU A CD2 1 
ATOM   2821 N  N   . ARG A 1 355 ? 8.26466  18.45713  26.58096 1.000 28.60640  ? 350 ARG A N   1 
ATOM   2822 C  CA  . ARG A 1 355 ? 8.39877  19.24244  27.80337 1.000 32.18929  ? 350 ARG A CA  1 
ATOM   2823 C  C   . ARG A 1 355 ? 7.34566  20.34169  27.86414 1.000 32.88225  ? 350 ARG A C   1 
ATOM   2824 O  O   . ARG A 1 355 ? 7.06284  21.02142  26.87312 1.000 32.56633  ? 350 ARG A O   1 
ATOM   2825 C  CB  . ARG A 1 355 ? 9.80540  19.84083  27.90101 1.000 37.49554  ? 350 ARG A CB  1 
ATOM   2826 C  CG  . ARG A 1 355 ? 10.89391 18.78809  28.09227 1.000 37.10335  ? 350 ARG A CG  1 
ATOM   2827 C  CD  . ARG A 1 355 ? 12.30224 19.38791  28.15524 1.000 46.44959  ? 350 ARG A CD  1 
ATOM   2828 N  NE  . ARG A 1 355 ? 13.33768 18.36282  28.03779 1.000 49.47414  ? 350 ARG A NE  1 
ATOM   2829 C  CZ  . ARG A 1 355 ? 13.80800 17.64710  29.05177 1.000 57.47237  ? 350 ARG A CZ  1 
ATOM   2830 N  NH1 . ARG A 1 355 ? 13.36467 17.82162  30.28611 1.000 51.90949  ? 350 ARG A NH1 1 
ATOM   2831 N  NH2 . ARG A 1 355 ? 14.74265 16.72842  28.82081 1.000 54.99192  ? 350 ARG A NH2 1 
ATOM   2832 N  N   . ILE A 1 356 ? 6.75822  20.51341  29.04267 1.000 28.97833  ? 351 ILE A N   1 
ATOM   2833 C  CA  . ILE A 1 356 ? 5.70342  21.49223  29.21551 1.000 30.46126  ? 351 ILE A CA  1 
ATOM   2834 C  C   . ILE A 1 356 ? 6.30468  22.83701  29.58833 1.000 27.89532  ? 351 ILE A C   1 
ATOM   2835 O  O   . ILE A 1 356 ? 7.16209  22.92683  30.46983 1.000 37.93589  ? 351 ILE A O   1 
ATOM   2836 C  CB  . ILE A 1 356 ? 4.68841  21.01032  30.26278 1.000 34.03772  ? 351 ILE A CB  1 
ATOM   2837 C  CG1 . ILE A 1 356 ? 3.93164  19.79912  29.70254 1.000 30.81475  ? 351 ILE A CG1 1 
ATOM   2838 C  CG2 . ILE A 1 356 ? 3.74339  22.14516  30.66389 1.000 37.39889  ? 351 ILE A CG2 1 
ATOM   2839 C  CD1 . ILE A 1 356 ? 3.06623  19.09940  30.69515 1.000 38.52052  ? 351 ILE A CD1 1 
ATOM   2840 O  OXT . ILE A 1 356 ? 5.95020  23.85525  29.00303 1.000 31.86612  ? 351 ILE A OXT 1 
HETATM 2841 MN MN  . MN  B 2 .   ? 21.70998 3.99189   23.10455 1.000 23.26549  ? 401 MN  A MN  1 
HETATM 2842 C  C1  . AKG C 3 .   ? 22.38344 1.75289   21.66061 1.000 27.72843  ? 402 AKG A C1  1 
HETATM 2843 O  O1  . AKG C 3 .   ? 21.33261 2.35997   21.86515 1.000 28.25373  ? 402 AKG A O1  1 
HETATM 2844 O  O2  . AKG C 3 .   ? 22.47880 0.62266   21.00792 1.000 25.01346  ? 402 AKG A O2  1 
HETATM 2845 C  C2  . AKG C 3 .   ? 23.70259 2.30380   22.17149 1.000 28.52199  ? 402 AKG A C2  1 
HETATM 2846 O  O5  . AKG C 3 .   ? 23.71553 3.42463   22.66154 1.000 30.68898  ? 402 AKG A O5  1 
HETATM 2847 C  C3  . AKG C 3 .   ? 24.93824 1.45175   22.05028 1.000 27.30366  ? 402 AKG A C3  1 
HETATM 2848 C  C4  . AKG C 3 .   ? 26.10478 2.00048   22.85309 1.000 23.69112  ? 402 AKG A C4  1 
HETATM 2849 C  C5  . AKG C 3 .   ? 27.39378 1.25417   22.65136 1.000 30.45271  ? 402 AKG A C5  1 
HETATM 2850 O  O3  . AKG C 3 .   ? 27.72085 0.73397   21.60092 1.000 27.09837  ? 402 AKG A O3  1 
HETATM 2851 O  O4  . AKG C 3 .   ? 28.13602 1.23760   23.73065 1.000 22.98320  ? 402 AKG A O4  1 
HETATM 2852 O  O1  . PE8 D 4 .   ? 18.89211 2.04531   20.57379 1.000 33.97170  ? 403 PE8 A O1  1 
HETATM 2853 C  C2  . PE8 D 4 .   ? 18.73390 3.43805   20.64226 1.000 36.33503  ? 403 PE8 A C2  1 
HETATM 2854 C  C3  . PE8 D 4 .   ? 18.97142 4.03210   19.25926 1.000 38.27112  ? 403 PE8 A C3  1 
HETATM 2855 O  O4  . PE8 D 4 .   ? 17.86324 3.74079   18.45946 1.000 36.99488  ? 403 PE8 A O4  1 
HETATM 2856 C  C5  . PE8 D 4 .   ? 18.09016 3.99821   17.10459 1.000 40.55106  ? 403 PE8 A C5  1 
HETATM 2857 C  C6  . PE8 D 4 .   ? 16.75053 3.97569   16.37834 1.000 42.77271  ? 403 PE8 A C6  1 
HETATM 2858 O  O7  . PE8 D 4 .   ? 16.24984 2.67657   16.46317 1.000 37.08046  ? 403 PE8 A O7  1 
HETATM 2859 C  C8  . PE8 D 4 .   ? 14.93663 2.55391   15.99871 1.000 37.81548  ? 403 PE8 A C8  1 
HETATM 2860 C  C9  . PE8 D 4 .   ? 14.49001 1.11335   16.21968 1.000 40.42024  ? 403 PE8 A C9  1 
HETATM 2861 O  O10 . PE8 D 4 .   ? 14.29457 0.93471   17.59475 1.000 36.67783  ? 403 PE8 A O10 1 
HETATM 2862 C  C11 . PE8 D 4 .   ? 13.45887 -0.13316  17.93535 1.000 38.04481  ? 403 PE8 A C11 1 
HETATM 2863 C  C12 . PE8 D 4 .   ? 13.63418 -0.39155  19.43078 1.000 43.30558  ? 403 PE8 A C12 1 
HETATM 2864 O  O13 . PE8 D 4 .   ? 13.18311 0.74759   20.11190 1.000 40.79598  ? 403 PE8 A O13 1 
HETATM 2865 C  C14 . PE8 D 4 .   ? 13.13670 0.62727   21.50454 1.000 33.13037  ? 403 PE8 A C14 1 
HETATM 2866 C  C15 . PE8 D 4 .   ? 12.73577 1.99603   22.05308 1.000 40.93174  ? 403 PE8 A C15 1 
HETATM 2867 O  O16 . PE8 D 4 .   ? 11.34588 2.07718   21.95547 1.000 40.64016  ? 403 PE8 A O16 1 
HETATM 2868 C  C17 . PE8 D 4 .   ? 10.82808 3.35037   22.20911 1.000 41.66235  ? 403 PE8 A C17 1 
HETATM 2869 C  C18 . PE8 D 4 .   ? 9.31366  3.26463   22.04287 1.000 43.12103  ? 403 PE8 A C18 1 
HETATM 2870 O  O19 . PE8 D 4 .   ? 8.82374  2.39395   23.02723 1.000 51.69670  ? 403 PE8 A O19 1 
HETATM 2871 C  C20 . PE8 D 4 .   ? 7.43819  2.18276   22.99021 1.000 48.61080  ? 403 PE8 A C20 1 
HETATM 2872 C  C21 . PE8 D 4 .   ? 7.15684  0.79375   22.41373 1.000 56.36475  ? 403 PE8 A C21 1 
HETATM 2873 O  O22 . PE8 D 4 .   ? 8.33963  0.28866   21.85638 1.000 60.74527  ? 403 PE8 A O22 1 
HETATM 2874 C  C23 . PE8 D 4 .   ? 8.14447  -0.62699  20.81813 1.000 60.87965  ? 403 PE8 A C23 1 
HETATM 2875 C  C24 . PE8 D 4 .   ? 9.14979  -0.31941  19.70815 1.000 50.19111  ? 403 PE8 A C24 1 
HETATM 2876 O  O25 . PE8 D 4 .   ? 8.62604  -0.79651  18.49792 1.000 64.41643  ? 403 PE8 A O25 1 
HETATM 2877 O  O   . HOH E 5 .   ? 15.69213 7.05879   49.39861 1.000 59.71465  ? 501 HOH A O   1 
HETATM 2878 O  O   . HOH E 5 .   ? 41.05767 14.87745  33.48981 1.000 54.69962  ? 502 HOH A O   1 
HETATM 2879 O  O   . HOH E 5 .   ? 7.71091  -5.45094  42.80303 1.000 67.51664  ? 503 HOH A O   1 
HETATM 2880 O  O   . HOH E 5 .   ? 34.80134 -8.66571  12.25359 1.000 44.10478  ? 504 HOH A O   1 
HETATM 2881 O  O   . HOH E 5 .   ? -1.51668 12.74560  41.56033 0.50  31.32978  ? 505 HOH A O   1 
HETATM 2882 O  O   . HOH E 5 .   ? -1.51668 23.64678  41.56033 0.50  32.60379  ? 506 HOH A O   1 
HETATM 2883 O  O   . HOH E 5 .   ? 1.59413  -3.05167  39.68396 1.000 50.54474  ? 507 HOH A O   1 
HETATM 2884 O  O   . HOH E 5 .   ? 48.25866 12.24657  34.12236 1.000 59.80667  ? 508 HOH A O   1 
HETATM 2885 O  O   . HOH E 5 .   ? 1.29301  24.93578  44.16834 1.000 27.97703  ? 509 HOH A O   1 
HETATM 2886 O  O   . HOH E 5 .   ? 12.17984 -9.10442  40.97394 1.000 46.91512  ? 510 HOH A O   1 
HETATM 2887 O  O   . HOH E 5 .   ? 2.62203  6.60691   34.03546 1.000 42.74758  ? 511 HOH A O   1 
HETATM 2888 O  O   . HOH E 5 .   ? 17.80132 7.42877   49.11067 1.000 49.50658  ? 512 HOH A O   1 
HETATM 2889 O  O   . HOH E 5 .   ? 17.85457 -11.12221 40.71174 1.000 43.13817  ? 513 HOH A O   1 
HETATM 2890 O  O   . HOH E 5 .   ? 31.25251 -5.81941  -0.29390 1.000 48.27148  ? 514 HOH A O   1 
HETATM 2891 O  O   . HOH E 5 .   ? 34.08573 -0.49072  25.15039 1.000 39.59074  ? 515 HOH A O   1 
HETATM 2892 O  O   . HOH E 5 .   ? 31.54453 -7.79033  6.33032  1.000 34.82873  ? 516 HOH A O   1 
HETATM 2893 O  O   . HOH E 5 .   ? 21.39300 -4.98978  4.84436  1.000 37.24024  ? 517 HOH A O   1 
HETATM 2894 O  O   . HOH E 5 .   ? 32.31912 -16.06113 11.48772 1.000 48.92968  ? 518 HOH A O   1 
HETATM 2895 O  O   . HOH E 5 .   ? 28.58641 -5.19232  10.27529 1.000 32.02548  ? 519 HOH A O   1 
HETATM 2896 O  O   . HOH E 5 .   ? 15.17717 8.57259   22.33351 1.000 41.25084  ? 520 HOH A O   1 
HETATM 2897 O  O   . HOH E 5 .   ? -3.547   11.838    32.261   1.000 42.46337  ? 521 HOH A O   1 
HETATM 2898 O  O   . HOH E 5 .   ? 33.35912 4.13667   40.60847 1.000 42.10928  ? 522 HOH A O   1 
HETATM 2899 O  O   . HOH E 5 .   ? 30.11168 -5.13857  45.13468 1.000 39.26505  ? 523 HOH A O   1 
HETATM 2900 O  O   . HOH E 5 .   ? 9.39415  -7.17134  15.66812 1.000 52.54709  ? 524 HOH A O   1 
HETATM 2901 O  O   . HOH E 5 .   ? -3.121   17.942    47.187   1.000 40.63306  ? 525 HOH A O   1 
HETATM 2902 O  O   . HOH E 5 .   ? 45.45296 9.27951   33.40660 1.000 50.10707  ? 526 HOH A O   1 
HETATM 2903 O  O   . HOH E 5 .   ? 14.20173 11.95168  23.01393 1.000 39.09036  ? 527 HOH A O   1 
HETATM 2904 O  O   . HOH E 5 .   ? 35.68775 -4.28267  10.75843 1.000 30.28092  ? 528 HOH A O   1 
HETATM 2905 O  O   . HOH E 5 .   ? 4.51207  13.55716  19.54529 1.000 46.48920  ? 529 HOH A O   1 
HETATM 2906 O  O   . HOH E 5 .   ? 13.69500 -10.25949 39.49920 1.000 46.57141  ? 530 HOH A O   1 
HETATM 2907 O  O   . HOH E 5 .   ? 14.60907 -10.09226 27.74051 1.000 37.73823  ? 531 HOH A O   1 
HETATM 2908 O  O   . HOH E 5 .   ? 36.12210 7.28777   24.17559 1.000 46.62878  ? 532 HOH A O   1 
HETATM 2909 O  O   . HOH E 5 .   ? 35.42107 8.50207   32.41437 1.000 48.57604  ? 533 HOH A O   1 
HETATM 2910 O  O   . HOH E 5 .   ? 22.06288 13.75424  12.47007 1.000 47.21853  ? 534 HOH A O   1 
HETATM 2911 O  O   . HOH E 5 .   ? 40.72808 -2.50593  -1.43103 1.000 33.10134  ? 535 HOH A O   1 
HETATM 2912 O  O   . HOH E 5 .   ? 2.22560  20.44740  33.63246 1.000 36.71572  ? 536 HOH A O   1 
HETATM 2913 O  O   . HOH E 5 .   ? 9.55300  -7.24678  27.50632 1.000 47.91848  ? 537 HOH A O   1 
HETATM 2914 O  O   . HOH E 5 .   ? 34.31904 -15.43167 32.02911 1.000 34.62202  ? 538 HOH A O   1 
HETATM 2915 O  O   . HOH E 5 .   ? 10.15732 -4.49220  28.11954 1.000 33.88325  ? 539 HOH A O   1 
HETATM 2916 O  O   . HOH E 5 .   ? 16.57616 -21.00658 22.67299 1.000 54.33685  ? 540 HOH A O   1 
HETATM 2917 O  O   . HOH E 5 .   ? 8.23237  21.27817  32.16193 1.000 37.23080  ? 541 HOH A O   1 
HETATM 2918 O  O   . HOH E 5 .   ? 33.710   -17.784   29.089   1.000 33.18856  ? 542 HOH A O   1 
HETATM 2919 O  O   . HOH E 5 .   ? -2.12233 7.76938   18.81543 1.000 52.20264  ? 543 HOH A O   1 
HETATM 2920 O  O   . HOH E 5 .   ? 2.36761  5.72714   31.27809 1.000 45.48493  ? 544 HOH A O   1 
HETATM 2921 O  O   . HOH E 5 .   ? 12.97242 7.24585   11.02030 1.000 45.88090  ? 545 HOH A O   1 
HETATM 2922 O  O   . HOH E 5 .   ? 34.10356 8.77284   15.59304 1.000 32.60993  ? 546 HOH A O   1 
HETATM 2923 O  O   . HOH E 5 .   ? 24.61385 1.18521   15.73159 1.000 32.23695  ? 547 HOH A O   1 
HETATM 2924 O  O   . HOH E 5 .   ? 12.57976 17.86533  19.65082 1.000 42.38677  ? 548 HOH A O   1 
HETATM 2925 O  O   . HOH E 5 .   ? 22.05490 2.46235   24.78185 1.000 29.19083  ? 549 HOH A O   1 
HETATM 2926 O  O   . HOH E 5 .   ? 33.77991 -9.68351  14.53278 1.000 43.45125  ? 550 HOH A O   1 
HETATM 2927 O  O   . HOH E 5 .   ? 38.95488 5.88397   28.12050 1.000 48.07712  ? 551 HOH A O   1 
HETATM 2928 O  O   . HOH E 5 .   ? 7.94631  -8.08686  29.81574 1.000 45.25795  ? 552 HOH A O   1 
HETATM 2929 O  O   . HOH E 5 .   ? 34.10130 9.81433   34.62012 1.000 40.86057  ? 553 HOH A O   1 
HETATM 2930 O  O   . HOH E 5 .   ? -2.744   24.733    45.746   1.000 43.01265  ? 554 HOH A O   1 
HETATM 2931 O  O   . HOH E 5 .   ? 16.33597 0.92238   13.27511 1.000 30.65322  ? 555 HOH A O   1 
HETATM 2932 O  O   . HOH E 5 .   ? 36.57426 -5.43970  19.41190 1.000 32.63963  ? 556 HOH A O   1 
HETATM 2933 O  O   . HOH E 5 .   ? 16.48514 12.52643  7.62488  1.000 42.38686  ? 557 HOH A O   1 
HETATM 2934 O  O   . HOH E 5 .   ? 25.62691 3.02705   6.17813  1.000 32.48055  ? 558 HOH A O   1 
HETATM 2935 O  O   . HOH E 5 .   ? 11.67995 -11.44254 37.12240 1.000 50.80400  ? 559 HOH A O   1 
HETATM 2936 O  O   . HOH E 5 .   ? 16.59876 19.84714  21.50546 1.000 46.17368  ? 560 HOH A O   1 
HETATM 2937 O  O   . HOH E 5 .   ? 24.57617 -16.56274 10.15249 1.000 55.62726  ? 561 HOH A O   1 
HETATM 2938 O  O   . HOH E 5 .   ? 39.74411 -11.73722 24.60788 1.000 46.84453  ? 562 HOH A O   1 
HETATM 2939 O  O   . HOH E 5 .   ? 35.74886 -8.88090  16.51794 1.000 37.40001  ? 563 HOH A O   1 
HETATM 2940 O  O   . HOH E 5 .   ? -0.19969 11.81947  34.51503 1.000 42.17273  ? 564 HOH A O   1 
HETATM 2941 O  O   . HOH E 5 .   ? 5.14116  -6.45249  21.00191 1.000 52.76804  ? 565 HOH A O   1 
HETATM 2942 O  O   . HOH E 5 .   ? 9.74204  -10.19196 14.74195 1.000 41.23488  ? 566 HOH A O   1 
HETATM 2943 O  O   . HOH E 5 .   ? 24.68565 -0.45645  7.28056  1.000 36.48052  ? 567 HOH A O   1 
HETATM 2944 O  O   . HOH E 5 .   ? 40.34179 9.38792   -0.94936 1.000 42.37202  ? 568 HOH A O   1 
HETATM 2945 O  O   . HOH E 5 .   ? 15.90497 14.80958  40.49109 1.000 42.35433  ? 569 HOH A O   1 
HETATM 2946 O  O   . HOH E 5 .   ? 27.66559 -20.09548 30.15266 1.000 46.33178  ? 570 HOH A O   1 
HETATM 2947 O  O   . HOH E 5 .   ? 15.90149 -1.03030  47.09218 1.000 35.09487  ? 571 HOH A O   1 
HETATM 2948 O  O   . HOH E 5 .   ? -1.12044 6.24944   31.46780 1.000 50.43157  ? 572 HOH A O   1 
HETATM 2949 O  O   . HOH E 5 .   ? 23.37289 3.07782   26.85296 1.000 35.43056  ? 573 HOH A O   1 
HETATM 2950 O  O   . HOH E 5 .   ? 15.20466 9.28016   19.46454 1.000 33.20197  ? 574 HOH A O   1 
HETATM 2951 O  O   . HOH E 5 .   ? 27.40710 -6.56577  18.77889 1.000 37.03373  ? 575 HOH A O   1 
HETATM 2952 O  O   . HOH E 5 .   ? 41.935   4.335     -2.483   1.000 39.86843  ? 576 HOH A O   1 
HETATM 2953 O  O   . HOH E 5 .   ? 22.00791 5.12428   12.66456 1.000 31.60536  ? 577 HOH A O   1 
HETATM 2954 O  O   . HOH E 5 .   ? 22.32461 13.35094  17.38020 1.000 36.98247  ? 578 HOH A O   1 
HETATM 2955 O  O   . HOH E 5 .   ? 23.18629 -12.97550 -0.00526 1.000 59.33035  ? 579 HOH A O   1 
HETATM 2956 O  O   . HOH E 5 .   ? 4.89466  -1.01715  22.49572 1.000 52.97124  ? 580 HOH A O   1 
HETATM 2957 O  O   . HOH E 5 .   ? -0.31244 12.47283  44.18647 1.000 44.31367  ? 581 HOH A O   1 
HETATM 2958 O  O   . HOH E 5 .   ? 36.22640 3.36557   19.36140 1.000 29.25305  ? 582 HOH A O   1 
HETATM 2959 O  O   . HOH E 5 .   ? 28.26670 -0.42181  44.90473 1.000 29.77621  ? 583 HOH A O   1 
HETATM 2960 O  O   . HOH E 5 .   ? 8.95546  2.16608   25.74785 1.000 30.29622  ? 584 HOH A O   1 
HETATM 2961 O  O   . HOH E 5 .   ? 15.57295 4.74881   21.12748 1.000 44.56445  ? 585 HOH A O   1 
HETATM 2962 O  O   . HOH E 5 .   ? 23.13236 -6.33106  27.06752 1.000 22.40324  ? 586 HOH A O   1 
HETATM 2963 O  O   . HOH E 5 .   ? 35.68194 -4.41320  8.06858  1.000 35.69961  ? 587 HOH A O   1 
HETATM 2964 O  O   . HOH E 5 .   ? 15.25351 11.73926  20.28598 1.000 43.43020  ? 588 HOH A O   1 
HETATM 2965 O  O   . HOH E 5 .   ? 31.78102 -18.66615 27.12572 1.000 37.11067  ? 589 HOH A O   1 
HETATM 2966 O  O   . HOH E 5 .   ? 11.75887 4.40631   4.65633  1.000 52.48883  ? 590 HOH A O   1 
HETATM 2967 O  O   . HOH E 5 .   ? 17.33143 6.53493   11.45479 1.000 31.04617  ? 591 HOH A O   1 
HETATM 2968 O  O   . HOH E 5 .   ? 12.74492 -11.84053 16.30351 1.000 34.86569  ? 592 HOH A O   1 
HETATM 2969 O  O   . HOH E 5 .   ? -3.22842 17.70110  44.58330 1.000 31.93619  ? 593 HOH A O   1 
HETATM 2970 O  O   . HOH E 5 .   ? 6.78240  15.26233  40.43689 1.000 29.54577  ? 594 HOH A O   1 
HETATM 2971 O  O   . HOH E 5 .   ? 6.94114  18.76675  39.24853 1.000 46.79009  ? 595 HOH A O   1 
HETATM 2972 O  O   . HOH E 5 .   ? 34.89568 5.16361   26.06715 1.000 35.91250  ? 596 HOH A O   1 
HETATM 2973 O  O   . HOH E 5 .   ? 15.26727 -4.69797  43.73084 1.000 39.28194  ? 597 HOH A O   1 
HETATM 2974 O  O   . HOH E 5 .   ? 24.00639 1.47001   12.44218 1.000 34.10124  ? 598 HOH A O   1 
HETATM 2975 O  O   . HOH E 5 .   ? 25.58386 -1.55121  50.31149 1.000 29.39065  ? 599 HOH A O   1 
HETATM 2976 O  O   . HOH E 5 .   ? 28.50012 9.84125   11.28819 1.000 28.30303  ? 600 HOH A O   1 
HETATM 2977 O  O   . HOH E 5 .   ? 35.65712 2.03816   15.39887 1.000 32.06926  ? 601 HOH A O   1 
HETATM 2978 O  O   . HOH E 5 .   ? 19.70607 -0.98716  6.44051  1.000 35.55295  ? 602 HOH A O   1 
HETATM 2979 O  O   . HOH E 5 .   ? 28.13925 15.71852  19.82318 1.000 42.24749  ? 603 HOH A O   1 
HETATM 2980 O  O   . HOH E 5 .   ? 34.64595 -4.90998  1.37236  1.000 41.23879  ? 604 HOH A O   1 
HETATM 2981 O  O   . HOH E 5 .   ? 25.21237 3.14066   8.77359  1.000 29.61664  ? 605 HOH A O   1 
HETATM 2982 O  O   . HOH E 5 .   ? 13.60188 -13.97169 32.91847 1.000 45.15251  ? 606 HOH A O   1 
HETATM 2983 O  O   . HOH E 5 .   ? 16.22720 -10.27323 4.51844  1.000 50.66394  ? 607 HOH A O   1 
HETATM 2984 O  O   . HOH E 5 .   ? 13.82588 4.70327   3.31285  1.000 59.96280  ? 608 HOH A O   1 
HETATM 2985 O  O   . HOH E 5 .   ? 29.34303 17.74396  36.11898 1.000 54.13183  ? 609 HOH A O   1 
HETATM 2986 O  O   . HOH E 5 .   ? 26.37207 10.64999  13.04463 1.000 32.95122  ? 610 HOH A O   1 
HETATM 2987 O  O   . HOH E 5 .   ? 23.89971 12.48599  32.33805 1.000 41.14037  ? 611 HOH A O   1 
HETATM 2988 O  O   . HOH E 5 .   ? 32.66862 -5.06614  29.00884 1.000 37.51206  ? 612 HOH A O   1 
HETATM 2989 O  O   . HOH E 5 .   ? 28.19085 4.19319   43.32967 1.000 27.79842  ? 613 HOH A O   1 
HETATM 2990 O  O   . HOH E 5 .   ? 8.92130  8.22972   12.58324 1.000 50.82734  ? 614 HOH A O   1 
HETATM 2991 O  O   . HOH E 5 .   ? 40.64072 -6.46615  14.10927 1.000 53.94082  ? 615 HOH A O   1 
HETATM 2992 O  O   . HOH E 5 .   ? 20.70970 -21.94880 19.11216 1.000 46.68273  ? 616 HOH A O   1 
HETATM 2993 O  O   . HOH E 5 .   ? 0.129    15.852    48.530   1.000 31.11978  ? 617 HOH A O   1 
HETATM 2994 O  O   . HOH E 5 .   ? 1.05289  15.22877  31.31892 1.000 39.26450  ? 618 HOH A O   1 
HETATM 2995 O  O   . HOH E 5 .   ? 22.53385 -17.25859 36.43515 1.000 56.26428  ? 619 HOH A O   1 
HETATM 2996 O  O   . HOH E 5 .   ? 28.84347 -7.44217  47.76046 1.000 33.90408  ? 620 HOH A O   1 
HETATM 2997 O  O   . HOH E 5 .   ? 14.91728 3.05896   19.37211 1.000 41.71570  ? 621 HOH A O   1 
HETATM 2998 O  O   . HOH E 5 .   ? 32.15141 10.93344  40.59358 1.000 35.25889  ? 622 HOH A O   1 
HETATM 2999 O  O   . HOH E 5 .   ? 23.08277 5.20115   10.16062 1.000 32.56949  ? 623 HOH A O   1 
HETATM 3000 O  O   . HOH E 5 .   ? -0.08751 6.57600   37.16918 1.000 46.19382  ? 624 HOH A O   1 
HETATM 3001 O  O   . HOH E 5 .   ? 17.33833 16.04471  1.70947  1.000 56.92829  ? 625 HOH A O   1 
HETATM 3002 O  O   . HOH E 5 .   ? 19.12954 7.09824   27.33583 1.000 24.95201  ? 626 HOH A O   1 
HETATM 3003 O  O   . HOH E 5 .   ? 0.91310  6.48450   40.32904 1.000 40.68201  ? 627 HOH A O   1 
HETATM 3004 O  O   . HOH E 5 .   ? 39.05507 1.94329   5.77225  1.000 48.01419  ? 628 HOH A O   1 
HETATM 3005 O  O   . HOH E 5 .   ? 33.04873 -10.25982 6.74483  1.000 41.70699  ? 629 HOH A O   1 
HETATM 3006 O  O   . HOH E 5 .   ? 30.03388 -20.39305 35.08981 1.000 42.94620  ? 630 HOH A O   1 
HETATM 3007 O  O   . HOH E 5 .   ? 37.12052 -3.87272  30.07587 1.000 37.53225  ? 631 HOH A O   1 
HETATM 3008 O  O   . HOH E 5 .   ? 17.44094 0.73200   18.49183 1.000 29.15347  ? 632 HOH A O   1 
HETATM 3009 O  O   . HOH E 5 .   ? 32.89684 1.79289   25.58959 1.000 36.25878  ? 633 HOH A O   1 
HETATM 3010 O  O   . HOH E 5 .   ? 32.95190 17.64019  25.97760 1.000 48.25650  ? 634 HOH A O   1 
HETATM 3011 O  O   . HOH E 5 .   ? 24.16930 2.03104   29.76463 1.000 40.59419  ? 635 HOH A O   1 
HETATM 3012 O  O   . HOH E 5 .   ? 16.69240 6.72080   20.40458 1.000 49.16349  ? 636 HOH A O   1 
HETATM 3013 O  O   . HOH E 5 .   ? 26.29720 6.21383   43.00159 1.000 27.33174  ? 637 HOH A O   1 
HETATM 3014 O  O   . HOH E 5 .   ? 6.34243  21.45905  34.50120 1.000 36.99747  ? 638 HOH A O   1 
HETATM 3015 O  O   . HOH E 5 .   ? 28.97303 -3.41217  29.73627 1.000 35.85237  ? 639 HOH A O   1 
HETATM 3016 O  O   . HOH E 5 .   ? 41.93865 -0.35387  22.03431 1.000 60.79594  ? 640 HOH A O   1 
HETATM 3017 O  O   . HOH E 5 .   ? 14.10352 -5.62741  15.78925 1.000 35.09684  ? 641 HOH A O   1 
HETATM 3018 O  O   . HOH E 5 .   ? 41.00551 3.05563   9.59770  1.000 38.48512  ? 642 HOH A O   1 
HETATM 3019 O  O   . HOH E 5 .   ? 19.92638 15.12057  42.34953 1.000 46.36891  ? 643 HOH A O   1 
HETATM 3020 O  O   . HOH E 5 .   ? 0.11380  -12.06452 30.18316 1.000 58.44325  ? 644 HOH A O   1 
HETATM 3021 O  O   . HOH E 5 .   ? 9.80778  2.41200   11.73935 1.000 56.50133  ? 645 HOH A O   1 
HETATM 3022 O  O   . HOH E 5 .   ? 19.31153 -0.95339  55.04229 1.000 41.66727  ? 646 HOH A O   1 
HETATM 3023 O  O   . HOH E 5 .   ? 15.13013 1.25043   46.35877 1.000 33.02983  ? 647 HOH A O   1 
HETATM 3024 O  O   . HOH E 5 .   ? 38.472   7.465     37.727   1.000 30.03680  ? 648 HOH A O   1 
HETATM 3025 O  O   . HOH E 5 .   ? 26.02593 -9.93086  48.47225 1.000 28.08203  ? 649 HOH A O   1 
HETATM 3026 O  O   . HOH E 5 .   ? 42.25865 6.05374   16.28795 1.000 41.93100  ? 650 HOH A O   1 
HETATM 3027 O  O   . HOH E 5 .   ? 22.51593 13.54833  29.10487 1.000 30.91719  ? 651 HOH A O   1 
HETATM 3028 O  O   . HOH E 5 .   ? 17.45247 14.36103  37.45272 1.000 48.83513  ? 652 HOH A O   1 
HETATM 3029 O  O   . HOH E 5 .   ? 17.77017 -20.76348 25.37813 1.000 43.94386  ? 653 HOH A O   1 
HETATM 3030 O  O   . HOH E 5 .   ? 8.68887  12.45481  13.52929 1.000 62.07036  ? 654 HOH A O   1 
HETATM 3031 O  O   . HOH E 5 .   ? 36.477   6.618     36.357   1.000 32.52307  ? 655 HOH A O   1 
HETATM 3032 O  O   . HOH E 5 .   ? 23.28719 -16.71036 34.02459 1.000 37.85370  ? 656 HOH A O   1 
HETATM 3033 O  O   . HOH E 5 .   ? 15.68457 -0.13770  50.35039 1.000 51.60733  ? 657 HOH A O   1 
HETATM 3034 O  O   . HOH E 5 .   ? 19.73436 -6.83676  48.73903 1.000 38.30508  ? 658 HOH A O   1 
HETATM 3035 O  O   . HOH E 5 .   ? 22.38418 15.90495  27.96735 1.000 46.85332  ? 659 HOH A O   1 
HETATM 3036 O  O   . HOH E 5 .   ? 9.29944  3.62195   49.43164 1.000 43.75408  ? 660 HOH A O   1 
HETATM 3037 O  O   . HOH E 5 .   ? 15.40668 5.72622   13.47022 1.000 33.96976  ? 661 HOH A O   1 
HETATM 3038 O  O   . HOH E 5 .   ? 21.972   -10.855   48.433   1.000 49.81877  ? 662 HOH A O   1 
HETATM 3039 O  O   . HOH E 5 .   ? 16.45710 2.86545   4.99471  1.000 38.79621  ? 663 HOH A O   1 
HETATM 3040 O  O   . HOH E 5 .   ? 17.97226 11.52874  21.41721 1.000 42.15501  ? 664 HOH A O   1 
HETATM 3041 O  O   . HOH E 5 .   ? 38.21648 -4.59854  11.78228 1.000 39.50612  ? 665 HOH A O   1 
HETATM 3042 O  O   . HOH E 5 .   ? 20.61503 5.64888   9.02255  1.000 35.82298  ? 666 HOH A O   1 
HETATM 3043 O  O   . HOH E 5 .   ? -5.478   23.668    48.544   1.000 36.50002  ? 667 HOH A O   1 
HETATM 3044 O  O   . HOH E 5 .   ? 22.64868 -1.05574  5.32914  1.000 36.94312  ? 668 HOH A O   1 
HETATM 3045 O  O   . HOH E 5 .   ? 10.93310 -4.85109  12.18108 1.000 38.31008  ? 669 HOH A O   1 
HETATM 3046 O  O   . HOH E 5 .   ? 21.78731 -15.92158 39.31163 1.000 48.86447  ? 670 HOH A O   1 
HETATM 3047 O  O   . HOH E 5 .   ? 33.44613 -1.57090  35.89009 1.000 38.49865  ? 671 HOH A O   1 
HETATM 3048 O  O   . HOH E 5 .   ? 35.48203 -13.01961 26.69132 1.000 40.39124  ? 672 HOH A O   1 
HETATM 3049 O  O   . HOH E 5 .   ? 20.77748 13.40430  9.97586  1.000 41.99850  ? 673 HOH A O   1 
HETATM 3050 O  O   . HOH E 5 .   ? 17.26189 13.99534  46.02908 1.000 48.43057  ? 674 HOH A O   1 
HETATM 3051 O  O   . HOH E 5 .   ? 7.17013  -8.89188  32.68172 1.000 50.00686  ? 675 HOH A O   1 
HETATM 3052 O  O   . HOH E 5 .   ? 12.41455 11.91042  10.37077 1.000 55.74267  ? 676 HOH A O   1 
HETATM 3053 O  O   . HOH E 5 .   ? 38.93496 1.75090   8.44367  1.000 38.88169  ? 677 HOH A O   1 
HETATM 3054 O  O   . HOH E 5 .   ? 36.90168 11.34993  28.97461 1.000 48.28273  ? 678 HOH A O   1 
HETATM 3055 O  O   . HOH E 5 .   ? 18.74561 1.49727   6.40677  1.000 40.96717  ? 679 HOH A O   1 
HETATM 3056 O  O   . HOH E 5 .   ? 25.61636 5.14831   50.23859 1.000 33.00679  ? 680 HOH A O   1 
HETATM 3057 O  O   . HOH E 5 .   ? 22.324   -11.249   42.107   1.000 37.74678  ? 681 HOH A O   1 
HETATM 3058 O  O   . HOH E 5 .   ? 27.36671 12.33504  41.52483 1.000 43.52425  ? 682 HOH A O   1 
HETATM 3059 O  O   . HOH E 5 .   ? 39.10194 7.24520   19.44802 1.000 52.38825  ? 683 HOH A O   1 
HETATM 3060 O  O   . HOH E 5 .   ? 20.11048 -14.95006 35.06828 1.000 58.64968  ? 684 HOH A O   1 
HETATM 3061 O  O   . HOH E 5 .   ? 1.58605  3.82899   43.03979 1.000 47.57444  ? 685 HOH A O   1 
HETATM 3062 O  O   . HOH E 5 .   ? 8.21472  -9.72672  34.22651 1.000 44.75032  ? 686 HOH A O   1 
HETATM 3063 O  O   . HOH E 5 .   ? 35.43868 -7.25522  7.82102  1.000 38.92337  ? 687 HOH A O   1 
HETATM 3064 O  O   . HOH E 5 .   ? 5.34032  11.94882  17.19990 1.000 53.64373  ? 688 HOH A O   1 
HETATM 3065 O  O   . HOH E 5 .   ? 14.88814 3.37021   12.17754 1.000 32.99332  ? 689 HOH A O   1 
HETATM 3066 O  O   . HOH E 5 .   ? 14.44029 -3.45186  45.80199 1.000 45.25152  ? 690 HOH A O   1 
HETATM 3067 O  O   . HOH E 5 .   ? 26.175   -3.956    51.612   1.000 28.10063  ? 691 HOH A O   1 
HETATM 3068 O  O   . HOH E 5 .   ? 19.11704 11.90182  18.29046 1.000 44.76067  ? 692 HOH A O   1 
HETATM 3069 O  O   . HOH E 5 .   ? 34.09867 -8.17282  24.18039 1.000 38.93001  ? 693 HOH A O   1 
HETATM 3070 O  O   . HOH E 5 .   ? 23.14620 -1.32314  51.48198 1.000 33.29060  ? 694 HOH A O   1 
HETATM 3071 O  O   . HOH E 5 .   ? 40.32235 1.23336   22.83202 1.000 43.46300  ? 695 HOH A O   1 
HETATM 3072 O  O   . HOH E 5 .   ? 35.297   4.651     37.759   1.000 31.84532  ? 696 HOH A O   1 
HETATM 3073 O  O   . HOH E 5 .   ? 32.86473 -10.50704 3.49669  1.000 50.09747  ? 697 HOH A O   1 
HETATM 3074 O  O   . HOH E 5 .   ? 38.48452 15.43402  17.28035 1.000 53.11033  ? 698 HOH A O   1 
HETATM 3075 O  O   . HOH E 5 .   ? 27.48296 -20.52994 27.30736 1.000 47.96294  ? 699 HOH A O   1 
HETATM 3076 O  O   . HOH E 5 .   ? 34.87504 -0.30440  28.45216 1.000 48.73821  ? 700 HOH A O   1 
HETATM 3077 O  O   . HOH E 5 .   ? -1.45872 4.13896   23.61265 1.000 51.65256  ? 701 HOH A O   1 
HETATM 3078 O  O   . HOH E 5 .   ? 9.95949  24.31364  30.35503 1.000 48.19815  ? 702 HOH A O   1 
HETATM 3079 O  O   . HOH E 5 .   ? 38.577   13.016    39.057   1.000 49.93014  ? 703 HOH A O   1 
HETATM 3080 O  O   . HOH E 5 .   ? 32.86634 10.55196  -0.23477 1.000 55.66682  ? 704 HOH A O   1 
HETATM 3081 O  O   . HOH E 5 .   ? 38.75584 -6.87328  20.28768 1.000 39.88960  ? 705 HOH A O   1 
HETATM 3082 O  O   . HOH E 5 .   ? 22.454   -4.553    51.738   1.000 36.15366  ? 706 HOH A O   1 
HETATM 3083 O  O   . HOH E 5 .   ? 22.33399 5.84021   52.94834 1.000 44.04522  ? 707 HOH A O   1 
HETATM 3084 O  O   . HOH E 5 .   ? 16.23078 2.87830   22.10366 1.000 38.43237  ? 708 HOH A O   1 
HETATM 3085 O  O   . HOH E 5 .   ? 32.33198 -7.82170  36.74906 1.000 46.30970  ? 709 HOH A O   1 
HETATM 3086 O  O   . HOH E 5 .   ? 12.24028 3.55317   11.74229 1.000 38.80152  ? 710 HOH A O   1 
HETATM 3087 O  O   . HOH E 5 .   ? 9.71987  -2.32653  11.49553 1.000 49.76728  ? 711 HOH A O   1 
HETATM 3088 O  O   . HOH E 5 .   ? 8.88145  16.00429  42.12135 1.000 55.77904  ? 712 HOH A O   1 
HETATM 3089 O  O   . HOH E 5 .   ? 0.90938  -5.24906  41.12965 1.000 58.86715  ? 713 HOH A O   1 
HETATM 3090 O  O   . HOH E 5 .   ? 34.28675 -8.78670  1.62482  1.000 54.56920  ? 714 HOH A O   1 
HETATM 3091 O  O   . HOH E 5 .   ? 25.54355 -20.49211 30.95349 1.000 52.42040  ? 715 HOH A O   1 
HETATM 3092 O  O   . HOH E 5 .   ? 19.83904 6.97577   11.48234 1.000 42.30018  ? 716 HOH A O   1 
HETATM 3093 O  O   . HOH E 5 .   ? 27.53116 -0.05795  51.31021 1.000 42.66005  ? 717 HOH A O   1 
HETATM 3094 O  O   . HOH E 5 .   ? 16.88069 18.80103  19.37496 1.000 52.78846  ? 718 HOH A O   1 
HETATM 3095 O  O   . HOH E 5 .   ? 17.55103 5.07409   50.48549 1.000 48.03691  ? 719 HOH A O   1 
HETATM 3096 O  O   . HOH E 5 .   ? 13.92184 13.16086  8.59483  1.000 51.08538  ? 720 HOH A O   1 
HETATM 3097 O  O   . HOH E 5 .   ? 10.07180 19.02655  42.55569 1.000 49.65697  ? 721 HOH A O   1 
HETATM 3098 O  O   . HOH E 5 .   ? -0.47010 7.48906   35.35626 1.000 50.92481  ? 722 HOH A O   1 
HETATM 3099 O  O   . HOH E 5 .   ? 29.87691 13.58781  41.35402 1.000 57.16803  ? 723 HOH A O   1 
HETATM 3100 O  O   . HOH E 5 .   ? 7.90754  19.85553  41.08850 1.000 43.44011  ? 724 HOH A O   1 
HETATM 3101 O  O   . HOH E 5 .   ? 0.19991  14.16017  33.12751 1.000 41.41493  ? 725 HOH A O   1 
HETATM 3102 O  O   . HOH E 5 .   ? 33.408   -17.244   34.021   1.000 35.99662  ? 726 HOH A O   1 
HETATM 3103 O  O   . HOH E 5 .   ? 32.34592 -8.65308  28.33519 1.000 61.85490  ? 727 HOH A O   1 
HETATM 3104 O  O   . HOH E 5 .   ? 34.46079 -1.75957  38.29320 1.000 48.08325  ? 728 HOH A O   1 
HETATM 3105 O  O   . HOH E 5 .   ? 18.09686 14.80867  8.54544  1.000 51.51827  ? 729 HOH A O   1 
HETATM 3106 O  O   . HOH E 5 .   ? 12.48234 -14.48953 31.06166 1.000 51.96593  ? 730 HOH A O   1 
HETATM 3107 O  O   . HOH E 5 .   ? 7.72174  2.20528   48.26633 1.000 44.52295  ? 731 HOH A O   1 
HETATM 3108 O  O   . HOH E 5 .   ? 20.955   -6.808    51.502   1.000 45.05684  ? 732 HOH A O   1 
HETATM 3109 O  O   . HOH E 5 .   ? 24.82908 12.85619  13.42939 1.000 41.74497  ? 733 HOH A O   1 
HETATM 3110 O  O   . HOH E 5 .   ? 11.48083 -5.39873  15.03877 1.000 40.64178  ? 734 HOH A O   1 
HETATM 3111 O  O   . HOH E 5 .   ? 43.00036 -1.79505  0.51922  1.000 51.07009  ? 735 HOH A O   1 
HETATM 3112 O  O   . HOH E 5 .   ? 24.74840 4.86796   28.87291 1.000 50.66529  ? 736 HOH A O   1 
HETATM 3113 O  O   . HOH E 5 .   ? 32.05933 -6.21664  43.36872 1.000 50.12763  ? 737 HOH A O   1 
HETATM 3114 O  O   . HOH E 5 .   ? 40.31209 -1.54050  8.56832  1.000 52.69111  ? 738 HOH A O   1 
HETATM 3115 O  O   . HOH E 5 .   ? 42.04376 -1.05100  9.55395  1.000 60.11373  ? 739 HOH A O   1 
HETATM 3116 O  O   . HOH E 5 .   ? 20.756   -10.536   43.335   1.000 47.47908  ? 740 HOH A O   1 
HETATM 3117 O  O   . HOH E 5 .   ? 38.86888 -4.23157  8.00505  1.000 48.24854  ? 741 HOH A O   1 
HETATM 3118 O  O   . HOH E 5 .   ? 14.59760 2.86946   48.62049 1.000 39.37238  ? 742 HOH A O   1 
HETATM 3119 O  O   . HOH E 5 .   ? -2.31186 12.04071  36.14135 1.000 46.43465  ? 743 HOH A O   1 
HETATM 3120 O  O   . HOH E 5 .   ? 0.80130  5.99589   43.65546 1.000 45.67350  ? 744 HOH A O   1 
HETATM 3121 O  O   . HOH E 5 .   ? 15.89987 1.62213   50.85234 1.000 53.15297  ? 745 HOH A O   1 
HETATM 3122 O  O   . HOH E 5 .   ? 38.27293 -13.53152 10.79649 1.000 59.76951  ? 746 HOH A O   1 
HETATM 3123 O  O   . HOH E 5 .   ? 10.70213 10.02478  9.90789  1.000 55.76182  ? 747 HOH A O   1 
HETATM 3124 O  O   . HOH E 5 .   ? 24.53489 6.09965   52.37631 1.000 44.29192  ? 748 HOH A O   1 
HETATM 3125 O  O   . HOH E 5 .   ? 33.14326 -9.62683  26.04548 1.000 47.05699  ? 749 HOH A O   1 
HETATM 3126 O  O   . HOH E 5 .   ? 43.79406 7.69947   14.94243 1.000 57.83225  ? 750 HOH A O   1 
HETATM 3127 O  O   . HOH E 5 .   ? 37.066   5.927     33.810   1.000 38.90242  ? 751 HOH A O   1 
HETATM 3128 O  O   . HOH E 5 .   ? -1.51668 -4.78424  41.56033 0.50  56.64445  ? 752 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   . ALA A 7   ? 1.65734 1.48668 0.96637 0.20562  -0.09733 0.02200  2   ALA A N   
2    C  CA  . ALA A 7   ? 1.63559 1.46936 0.93285 0.20388  -0.09162 0.01314  2   ALA A CA  
3    C  C   . ALA A 7   ? 1.55918 1.40977 0.88782 0.19359  -0.09793 -0.00434 2   ALA A C   
4    O  O   . ALA A 7   ? 1.54656 1.40655 0.90420 0.18931  -0.10906 -0.01054 2   ALA A O   
5    C  CB  . ALA A 7   ? 1.61960 1.44060 0.90144 0.19804  -0.06706 0.02734  2   ALA A CB  
6    N  N   . ASP A 8   ? 1.54432 1.39821 0.86692 0.18997  -0.09038 -0.01225 3   ASP A N   
7    C  CA  . ASP A 8   ? 1.49801 1.36520 0.84858 0.18001  -0.09394 -0.02820 3   ASP A CA  
8    C  C   . ASP A 8   ? 1.45541 1.32334 0.83504 0.16683  -0.08397 -0.02193 3   ASP A C   
9    O  O   . ASP A 8   ? 1.48767 1.34803 0.86327 0.16069  -0.06478 -0.01016 3   ASP A O   
10   C  CB  . ASP A 8   ? 1.50296 1.37075 0.83895 0.17933  -0.08471 -0.03571 3   ASP A CB  
11   C  CG  . ASP A 8   ? 1.48912 1.36950 0.85001 0.17215  -0.09248 -0.05519 3   ASP A CG  
12   O  OD1 . ASP A 8   ? 1.53450 1.42128 0.92739 0.16232  -0.09438 -0.05825 3   ASP A OD1 
13   O  OD2 . ASP A 8   ? 1.58066 1.46351 0.92849 0.17648  -0.09648 -0.06754 3   ASP A OD2 
14   N  N   . GLU A 9   ? 1.39837 1.27611 0.80799 0.16231  -0.09682 -0.03001 4   GLU A N   
15   C  CA  . GLU A 9   ? 1.20662 1.08485 0.64315 0.15122  -0.08967 -0.02419 4   GLU A CA  
16   C  C   . GLU A 9   ? 1.14643 1.02894 0.59750 0.14004  -0.07760 -0.02991 4   GLU A C   
17   O  O   . GLU A 9   ? 1.05467 0.94571 0.53459 0.13200  -0.08215 -0.03845 4   GLU A O   
18   C  CB  . GLU A 9   ? 1.22913 1.11768 0.69309 0.15053  -0.10735 -0.03209 4   GLU A CB  
19   C  CG  . GLU A 9   ? 1.28521 1.17194 0.73805 0.16247  -0.12056 -0.02779 4   GLU A CG  
20   C  CD  . GLU A 9   ? 1.40659 1.30772 0.88875 0.16219  -0.13905 -0.03866 4   GLU A CD  
21   O  OE1 . GLU A 9   ? 1.40504 1.31896 0.90949 0.15554  -0.14610 -0.05424 4   GLU A OE1 
22   O  OE2 . GLU A 9   ? 1.46237 1.36196 0.94627 0.16848  -0.14594 -0.03160 4   GLU A OE2 
23   N  N   . SER A 10  ? 1.03405 0.91096 0.46582 0.13979  -0.06179 -0.02516 5   SER A N   
24   C  CA  . SER A 10  ? 1.09745 0.97886 0.54263 0.13028  -0.04914 -0.02993 5   SER A CA  
25   C  C   . SER A 10  ? 0.95989 0.84055 0.42758 0.11961  -0.03875 -0.02088 5   SER A C   
26   O  O   . SER A 10  ? 0.94618 0.83314 0.43317 0.11143  -0.03285 -0.02727 5   SER A O   
27   C  CB  . SER A 10  ? 1.04655 0.92320 0.46671 0.13292  -0.03329 -0.02546 5   SER A CB  
28   O  OG  . SER A 10  ? 1.08967 0.95609 0.49598 0.13255  -0.01866 -0.00668 5   SER A OG  
29   N  N   . TRP A 11  ? 0.94414 0.81644 0.40947 0.11992  -0.03649 -0.00641 6   TRP A N   
30   C  CA  . TRP A 11  ? 0.99716 0.86803 0.48409 0.10996  -0.02834 0.00149  6   TRP A CA  
31   C  C   . TRP A 11  ? 0.88554 0.76575 0.40132 0.10568  -0.04166 -0.00980 6   TRP A C   
32   O  O   . TRP A 11  ? 0.78563 0.66674 0.32117 0.09680  -0.03506 -0.00690 6   TRP A O   
33   C  CB  . TRP A 11  ? 0.91029 0.76804 0.38769 0.11179  -0.02405 0.01875  6   TRP A CB  
34   C  CG  . TRP A 11  ? 0.94353 0.79840 0.41250 0.12243  -0.04125 0.01839  6   TRP A CG  
35   C  CD1 . TRP A 11  ? 1.04292 0.89157 0.48442 0.13382  -0.04559 0.02162  6   TRP A CD1 
36   C  CD2 . TRP A 11  ? 0.85559 0.71467 0.34425 0.12328  -0.05618 0.01460  6   TRP A CD2 
37   N  NE1 . TRP A 11  ? 1.07031 0.91967 0.51384 0.14195  -0.06262 0.01981  6   TRP A NE1 
38   C  CE2 . TRP A 11  ? 0.95736 0.81373 0.43057 0.13552  -0.06920 0.01543  6   TRP A CE2 
39   C  CE3 . TRP A 11  ? 0.88680 0.75216 0.40459 0.11533  -0.05965 0.01051  6   TRP A CE3 
40   C  CZ2 . TRP A 11  ? 0.93167 0.79301 0.41975 0.13986  -0.08521 0.01206  6   TRP A CZ2 
41   C  CZ3 . TRP A 11  ? 0.88844 0.75792 0.42012 0.11941  -0.07530 0.00741  6   TRP A CZ3 
42   C  CH2 . TRP A 11  ? 0.90493 0.77319 0.42284 0.13148  -0.08776 0.00806  6   TRP A CH2 
43   N  N   . ARG A 12  ? 0.82850 0.71605 0.34796 0.11146  -0.06003 -0.02270 7   ARG A N   
44   C  CA  . ARG A 12  ? 0.88990 0.78768 0.43888 0.10668  -0.07246 -0.03460 7   ARG A CA  
45   C  C   . ARG A 12  ? 0.81942 0.72425 0.38368 0.09937  -0.06838 -0.04706 7   ARG A C   
46   O  O   . ARG A 12  ? 0.86708 0.77862 0.45779 0.09322  -0.07456 -0.05513 7   ARG A O   
47   C  CB  . ARG A 12  ? 0.83601 0.74106 0.38726 0.11432  -0.09307 -0.04466 7   ARG A CB  
48   C  CG  . ARG A 12  ? 1.00883 0.90800 0.54873 0.12265  -0.09902 -0.03346 7   ARG A CG  
49   C  CD  . ARG A 12  ? 1.07751 0.98786 0.62947 0.12863  -0.12001 -0.04416 7   ARG A CD  
50   N  NE  . ARG A 12  ? 1.19469 1.10051 0.74381 0.13539  -0.12506 -0.03328 7   ARG A NE  
51   C  CZ  . ARG A 12  ? 1.26272 1.17860 0.82459 0.14119  -0.14200 -0.03949 7   ARG A CZ  
52   N  NH1 . ARG A 12  ? 1.42510 1.35662 1.00465 0.14010  -0.15585 -0.05656 7   ARG A NH1 
53   N  NH2 . ARG A 12  ? 1.18328 1.09345 0.74139 0.14799  -0.14464 -0.02848 7   ARG A NH2 
54   N  N   . ALA A 13  ? 0.77256 0.67565 0.32121 0.10026  -0.05779 -0.04875 8   ALA A N   
55   C  CA  . ALA A 13  ? 0.75931 0.66752 0.32035 0.09469  -0.05224 -0.05996 8   ALA A CA  
56   C  C   . ALA A 13  ? 0.81833 0.72321 0.37467 0.09015  -0.03102 -0.04930 8   ALA A C   
57   O  O   . ALA A 13  ? 0.76124 0.66435 0.29882 0.09338  -0.02074 -0.04749 8   ALA A O   
58   C  CB  . ALA A 13  ? 0.75919 0.66974 0.30830 0.10028  -0.05911 -0.07362 8   ALA A CB  
59   N  N   . PRO A 14  ? 0.72843 0.63329 0.30229 0.08258  -0.02385 -0.04232 9   PRO A N   
60   C  CA  . PRO A 14  ? 0.73306 0.63672 0.30576 0.07738  -0.00361 -0.03180 9   PRO A CA  
61   C  C   . PRO A 14  ? 0.74542 0.65602 0.32635 0.07514  0.00463  -0.04172 9   PRO A C   
62   O  O   . PRO A 14  ? 0.69224 0.60662 0.28371 0.07583  -0.00490 -0.05645 9   PRO A O   
63   C  CB  . PRO A 14  ? 0.71494 0.61680 0.30614 0.07008  -0.00159 -0.02382 9   PRO A CB  
64   C  CG  . PRO A 14  ? 0.74437 0.65000 0.35308 0.07008  -0.01907 -0.03563 9   PRO A CG  
65   C  CD  . PRO A 14  ? 0.67595 0.58263 0.27233 0.07831  -0.03393 -0.04393 9   PRO A CD  
66   N  N   . ALA A 15  ? 0.71872 0.63111 0.29655 0.07214  0.02301  -0.03331 10  ALA A N   
67   C  CA  . ALA A 15  ? 0.60750 0.52733 0.19219 0.07134  0.03284  -0.04119 10  ALA A CA  
68   C  C   . ALA A 15  ? 0.61472 0.53977 0.22709 0.06552  0.03266  -0.04755 10  ALA A C   
69   O  O   . ALA A 15  ? 0.61615 0.53975 0.24214 0.06031  0.03022  -0.04233 10  ALA A O   
70   C  CB  . ALA A 15  ? 0.74823 0.67137 0.32575 0.06924  0.05290  -0.02990 10  ALA A CB  
71   N  N   . ILE A 16  ? 0.58702 0.51710 0.20682 0.06705  0.03559  -0.05886 11  ILE A N   
72   C  CA  . ILE A 16  ? 0.59665 0.53211 0.24145 0.06264  0.03985  -0.06331 11  ILE A CA  
73   C  C   . ILE A 16  ? 0.53199 0.47547 0.18350 0.05825  0.05878  -0.05166 11  ILE A C   
74   O  O   . ILE A 16  ? 0.57060 0.51963 0.21419 0.06047  0.07057  -0.04997 11  ILE A O   
75   C  CB  . ILE A 16  ? 0.61199 0.54840 0.26254 0.06653  0.03674  -0.07900 11  ILE A CB  
76   C  CG1 . ILE A 16  ? 0.58810 0.51765 0.23877 0.06817  0.01753  -0.09113 11  ILE A CG1 
77   C  CG2 . ILE A 16  ? 0.56906 0.51120 0.24400 0.06356  0.04416  -0.08166 11  ILE A CG2 
78   C  CD1 . ILE A 16  ? 0.58376 0.51175 0.25436 0.06276  0.00729  -0.09186 11  ILE A CD1 
79   N  N   . VAL A 17  ? 0.57741 0.52202 0.24443 0.05151  0.06171  -0.04380 12  VAL A N   
80   C  CA  . VAL A 17  ? 0.61206 0.56494 0.28770 0.04542  0.07887  -0.03189 12  VAL A CA  
81   C  C   . VAL A 17  ? 0.56125 0.52763 0.25210 0.04649  0.09007  -0.03742 12  VAL A C   
82   O  O   . VAL A 17  ? 0.53458 0.51118 0.22784 0.04413  0.10461  -0.03075 12  VAL A O   
83   C  CB  . VAL A 17  ? 0.58250 0.53665 0.28341 0.03481  0.07611  -0.02320 12  VAL A CB  
84   C  CG1 . VAL A 17  ? 0.53602 0.49871 0.24674 0.02721  0.09291  -0.01168 12  VAL A CG1 
85   C  CG2 . VAL A 17  ? 0.53355 0.47450 0.22076 0.03522  0.06420  -0.01844 12  VAL A CG2 
86   N  N   . GLN A 18  ? 0.51422 0.48213 0.21993 0.04921  0.08279  -0.04938 13  GLN A N   
87   C  CA  . GLN A 18  ? 0.55519 0.53414 0.27203 0.05303  0.09297  -0.05533 13  GLN A CA  
88   C  C   . GLN A 18  ? 0.55855 0.54029 0.25848 0.05829  0.10006  -0.05760 13  GLN A C   
89   O  O   . GLN A 18  ? 0.56978 0.56460 0.27901 0.05883  0.11320  -0.05647 13  GLN A O   
90   C  CB  . GLN A 18  ? 0.51317 0.48893 0.24686 0.05545  0.08222  -0.06777 13  GLN A CB  
91   C  CG  . GLN A 18  ? 0.54432 0.52987 0.29049 0.06086  0.09176  -0.07389 13  GLN A CG  
92   C  CD  . GLN A 18  ? 0.53508 0.51403 0.29743 0.06304  0.08189  -0.08468 13  GLN A CD  
93   O  OE1 . GLN A 18  ? 0.50131 0.46994 0.26818 0.05917  0.06855  -0.08749 13  GLN A OE1 
94   N  NE2 . GLN A 18  ? 0.53468 0.51931 0.30600 0.06961  0.08911  -0.09057 13  GLN A NE2 
95   N  N   . GLU A 19  ? 0.55511 0.52567 0.23089 0.06228  0.09145  -0.06074 14  GLU A N   
96   C  CA  . GLU A 19  ? 0.61657 0.58816 0.27335 0.06776  0.09786  -0.06286 14  GLU A CA  
97   C  C   . GLU A 19  ? 0.54818 0.52584 0.19644 0.06391  0.11158  -0.04867 14  GLU A C   
98   O  O   . GLU A 19  ? 0.60103 0.58686 0.24506 0.06612  0.12403  -0.04811 14  GLU A O   
99   C  CB  . GLU A 19  ? 0.68574 0.64401 0.32008 0.07355  0.08327  -0.07132 14  GLU A CB  
100  C  CG  . GLU A 19  ? 0.61969 0.57227 0.26286 0.07690  0.07174  -0.08707 14  GLU A CG  
101  C  CD  . GLU A 19  ? 0.59707 0.55431 0.24437 0.08193  0.08072  -0.09536 14  GLU A CD  
102  O  OE1 . GLU A 19  ? 0.69872 0.65572 0.32680 0.08710  0.08596  -0.09713 14  GLU A OE1 
103  O  OE2 . GLU A 19  ? 0.68205 0.64282 0.35131 0.08139  0.08274  -0.09981 14  GLU A OE2 
104  N  N   . LEU A 20  ? 0.60870 0.58166 0.25474 0.05802  0.10977  -0.03718 15  LEU A N   
105  C  CA  . LEU A 20  ? 0.69812 0.67545 0.33967 0.05267  0.12339  -0.02285 15  LEU A CA  
106  C  C   . LEU A 20  ? 0.65034 0.64608 0.31690 0.04693  0.13922  -0.01973 15  LEU A C   
107  O  O   . LEU A 20  ? 0.58077 0.58549 0.24420 0.04600  0.15287  -0.01510 15  LEU A O   
108  C  CB  . LEU A 20  ? 0.62094 0.58838 0.26047 0.04672  0.11821  -0.01151 15  LEU A CB  
109  C  CG  . LEU A 20  ? 0.63899 0.59009 0.25426 0.05222  0.10330  -0.01175 15  LEU A CG  
110  C  CD1 . LEU A 20  ? 0.73243 0.67457 0.35053 0.04620  0.09940  -0.00036 15  LEU A CD1 
111  C  CD2 . LEU A 20  ? 0.62539 0.57255 0.21313 0.05836  0.10764  -0.00917 15  LEU A CD2 
112  N  N   . ALA A 21  ? 0.58135 0.58388 0.27372 0.04321  0.13734  -0.02242 16  ALA A N   
113  C  CA  . ALA A 21  ? 0.59012 0.61258 0.30975 0.03819  0.15040  -0.02038 16  ALA A CA  
114  C  C   . ALA A 21  ? 0.62619 0.65939 0.34761 0.04540  0.15737  -0.02971 16  ALA A C   
115  O  O   . ALA A 21  ? 0.64446 0.69419 0.37714 0.04244  0.17145  -0.02615 16  ALA A O   
116  C  CB  . ALA A 21  ? 0.55558 0.58150 0.30032 0.03457  0.14495  -0.02230 16  ALA A CB  
117  N  N   . ALA A 22  ? 0.55414 0.57791 0.26553 0.05457  0.14760  -0.04209 17  ALA A N   
118  C  CA  . ALA A 22  ? 0.56715 0.59753 0.27844 0.06226  0.15361  -0.05155 17  ALA A CA  
119  C  C   . ALA A 22  ? 0.58604 0.61687 0.27481 0.06463  0.16311  -0.04847 17  ALA A C   
120  O  O   . ALA A 22  ? 0.63106 0.67432 0.32529 0.06743  0.17509  -0.05102 17  ALA A O   
121  C  CB  . ALA A 22  ? 0.61403 0.63103 0.31920 0.07055  0.14005  -0.06549 17  ALA A CB  
122  N  N   . ALA A 23  ? 0.60588 0.62325 0.26901 0.06430  0.15800  -0.04300 18  ALA A N   
123  C  CA  . ALA A 23  ? 0.62179 0.63867 0.26177 0.06673  0.16746  -0.03843 18  ALA A CA  
124  C  C   . ALA A 23  ? 0.66678 0.69902 0.31912 0.05811  0.18470  -0.02590 18  ALA A C   
125  O  O   . ALA A 23  ? 0.72507 0.76221 0.36498 0.05991  0.19670  -0.02310 18  ALA A O   
126  C  CB  . ALA A 23  ? 0.68236 0.68076 0.29252 0.06928  0.15662  -0.03496 18  ALA A CB  
127  N  N   . GLY A 24  ? 0.65890 0.69897 0.33574 0.04848  0.18622  -0.01860 19  GLY A N   
128  C  CA  . GLY A 24  ? 0.71828 0.77530 0.41248 0.03895  0.20182  -0.00824 19  GLY A CA  
129  C  C   . GLY A 24  ? 0.69198 0.74005 0.37387 0.03149  0.20499  0.00659  19  GLY A C   
130  O  O   . GLY A 24  ? 0.68649 0.74354 0.36874 0.02650  0.21928  0.01485  19  GLY A O   
131  N  N   . VAL A 25  ? 0.63133 0.66130 0.30288 0.03069  0.19216  0.01029  20  VAL A N   
132  C  CA  . VAL A 25  ? 0.85039 0.86996 0.51290 0.02360  0.19496  0.02491  20  VAL A CA  
133  C  C   . VAL A 25  ? 0.66907 0.70442 0.36267 0.01066  0.20613  0.03334  20  VAL A C   
134  O  O   . VAL A 25  ? 0.70911 0.75597 0.43082 0.00649  0.20350  0.02917  20  VAL A O   
135  C  CB  . VAL A 25  ? 0.83272 0.83124 0.48240 0.02549  0.17837  0.02625  20  VAL A CB  
136  C  CG1 . VAL A 25  ? 0.80003 0.78451 0.41846 0.03769  0.16727  0.01879  20  VAL A CG1 
137  C  CG2 . VAL A 25  ? 0.73735 0.73953 0.41168 0.02255  0.16925  0.02011  20  VAL A CG2 
138  N  N   . GLU A 26  ? 0.81477 0.85117 0.50397 0.00438  0.21874  0.04502  21  GLU A N   
139  C  CA  . GLU A 26  ? 0.72893 0.78126 0.44859 -0.00867 0.22969  0.05285  21  GLU A CA  
140  C  C   . GLU A 26  ? 0.72803 0.76652 0.45637 -0.01762 0.22331  0.06156  21  GLU A C   
141  O  O   . GLU A 26  ? 0.68237 0.73327 0.44065 -0.02866 0.22853  0.06550  21  GLU A O   
142  C  CB  . GLU A 26  ? 0.75546 0.81446 0.46822 -0.01248 0.24668  0.06158  21  GLU A CB  
143  C  CG  . GLU A 26  ? 0.91509 0.98882 0.62079 -0.00431 0.25501  0.05295  21  GLU A CG  
144  C  CD  . GLU A 26  ? 0.95024 1.01661 0.62825 -0.00225 0.26678  0.06095  21  GLU A CD  
145  O  OE1 . GLU A 26  ? 1.13941 1.18315 0.79395 -0.00245 0.26380  0.07088  21  GLU A OE1 
146  O  OE2 . GLU A 26  ? 0.97377 1.05652 0.65285 0.00020  0.27919  0.05733  21  GLU A OE2 
147  N  N   . GLU A 27  ? 0.73103 0.74449 0.43455 -0.01281 0.21176  0.06401  22  GLU A N   
148  C  CA  . GLU A 27  ? 0.67648 0.67315 0.38394 -0.01955 0.20463  0.07147  22  GLU A CA  
149  C  C   . GLU A 27  ? 0.63258 0.61115 0.32000 -0.00992 0.18731  0.06572  22  GLU A C   
150  O  O   . GLU A 27  ? 0.66884 0.64391 0.33352 0.00137  0.18205  0.05898  22  GLU A O   
151  C  CB  . GLU A 27  ? 0.67243 0.65468 0.36669 -0.02523 0.21294  0.08604  22  GLU A CB  
152  C  CG  . GLU A 27  ? 1.05187 1.05095 0.76624 -0.03606 0.23037  0.09267  22  GLU A CG  
153  C  CD  . GLU A 27  ? 1.14308 1.12682 0.83588 -0.03829 0.24015  0.10600  22  GLU A CD  
154  O  OE1 . GLU A 27  ? 1.24567 1.20424 0.91158 -0.03265 0.23230  0.11128  22  GLU A OE1 
155  O  OE2 . GLU A 27  ? 1.15062 1.14780 0.85343 -0.04522 0.25570  0.11126  22  GLU A OE2 
156  N  N   . PRO A 28  ? 0.62401 0.59121 0.31982 -0.01416 0.17780  0.06749  23  PRO A N   
157  C  CA  . PRO A 28  ? 0.61867 0.56933 0.29604 -0.00526 0.16108  0.06260  23  PRO A CA  
158  C  C   . PRO A 28  ? 0.70735 0.63882 0.35174 0.00181  0.15765  0.06981  23  PRO A C   
159  O  O   . PRO A 28  ? 0.64712 0.56869 0.28713 -0.00364 0.16478  0.08197  23  PRO A O   
160  C  CB  . PRO A 28  ? 0.61732 0.56129 0.31391 -0.01351 0.15478  0.06469  23  PRO A CB  
161  C  CG  . PRO A 28  ? 0.65877 0.62020 0.38756 -0.02576 0.16661  0.06649  23  PRO A CG  
162  C  CD  . PRO A 28  ? 0.67440 0.64405 0.39823 -0.02737 0.18118  0.07285  23  PRO A CD  
163  N  N   . PRO A 29  ? 0.73984 0.66559 0.36108 0.01407  0.14661  0.06230  24  PRO A N   
164  C  CA  . PRO A 29  ? 0.82444 0.73228 0.41451 0.02206  0.14096  0.06849  24  PRO A CA  
165  C  C   . PRO A 29  ? 0.77422 0.66462 0.36406 0.01933  0.13336  0.07694  24  PRO A C   
166  O  O   . PRO A 29  ? 0.70787 0.59872 0.31836 0.01333  0.12846  0.07507  24  PRO A O   
167  C  CB  . PRO A 29  ? 0.67686 0.58497 0.25056 0.03450  0.12683  0.05532  24  PRO A CB  
168  C  CG  . PRO A 29  ? 0.70875 0.63568 0.29931 0.03337  0.13242  0.04424  24  PRO A CG  
169  C  CD  . PRO A 29  ? 0.71276 0.64907 0.33553 0.02140  0.13967  0.04733  24  PRO A CD  
170  N  N   . SER A 30  ? 0.73012 0.60427 0.29532 0.02454  0.13247  0.08625  25  SER A N   
171  C  CA  . SER A 30  ? 0.77219 0.62891 0.33808 0.02082  0.12994  0.09691  25  SER A CA  
172  C  C   . SER A 30  ? 0.77590 0.62680 0.34801 0.02418  0.11246  0.09099  25  SER A C   
173  O  O   . SER A 30  ? 0.70145 0.54326 0.28653 0.01763  0.11151  0.09662  25  SER A O   
174  C  CB  . SER A 30  ? 0.89101 0.73074 0.42695 0.02798  0.13173  0.10753  25  SER A CB  
175  O  OG  . SER A 30  ? 1.03070 0.86519 0.54294 0.04229  0.11637  0.10148  25  SER A OG  
176  N  N   . ARG A 31  ? 0.73514 0.59125 0.29945 0.03387  0.09854  0.07914  26  ARG A N   
177  C  CA  . ARG A 31  ? 0.69242 0.54413 0.26306 0.03720  0.08168  0.07343  26  ARG A CA  
178  C  C   . ARG A 31  ? 0.70390 0.56408 0.30357 0.02756  0.08248  0.06830  26  ARG A C   
179  O  O   . ARG A 31  ? 0.75525 0.61096 0.36223 0.02860  0.07030  0.06499  26  ARG A O   
180  C  CB  . ARG A 31  ? 0.79519 0.65121 0.35165 0.04943  0.06587  0.06124  26  ARG A CB  
181  C  CG  . ARG A 31  ? 0.98566 0.83060 0.51369 0.06070  0.05908  0.06576  26  ARG A CG  
182  C  CD  . ARG A 31  ? 1.11951 0.97118 0.63687 0.07156  0.04311  0.05187  26  ARG A CD  
183  N  NE  . ARG A 31  ? 0.99421 0.84709 0.52376 0.07416  0.02541  0.04431  26  ARG A NE  
184  C  CZ  . ARG A 31  ? 0.94522 0.80807 0.47995 0.07863  0.01142  0.02918  26  ARG A CZ  
185  N  NH1 . ARG A 31  ? 0.83513 0.70646 0.36388 0.08111  0.01266  0.01917  26  ARG A NH1 
186  N  NH2 . ARG A 31  ? 1.11582 0.98020 0.66356 0.08025  -0.00398 0.02354  26  ARG A NH2 
187  N  N   . TYR A 32  ? 0.71708 0.59008 0.33377 0.01867  0.09622  0.06739  27  TYR A N   
188  C  CA  . TYR A 32  ? 0.62625 0.50748 0.27082 0.00916  0.09815  0.06326  27  TYR A CA  
189  C  C   . TYR A 32  ? 0.61681 0.49311 0.27826 -0.00336 0.10831  0.07360  27  TYR A C   
190  O  O   . TYR A 32  ? 0.63510 0.51610 0.31964 -0.01181 0.10846  0.07075  27  TYR A O   
191  C  CB  . TYR A 32  ? 0.61491 0.51576 0.27190 0.00768  0.10557  0.05410  27  TYR A CB  
192  C  CG  . TYR A 32  ? 0.63599 0.54135 0.27912 0.01916  0.09559  0.04195  27  TYR A CG  
193  C  CD1 . TYR A 32  ? 0.62236 0.52827 0.24383 0.02695  0.09774  0.04140  27  TYR A CD1 
194  C  CD2 . TYR A 32  ? 0.63130 0.53974 0.28349 0.02172  0.08395  0.03040  27  TYR A CD2 
195  C  CE1 . TYR A 32  ? 0.65876 0.56824 0.26899 0.03667  0.08781  0.02893  27  TYR A CE1 
196  C  CE2 . TYR A 32  ? 0.53137 0.44341 0.17362 0.03125  0.07406  0.01804  27  TYR A CE2 
197  C  CZ  . TYR A 32  ? 0.60784 0.52046 0.22968 0.03846  0.07574  0.01699  27  TYR A CZ  
198  O  OH  . TYR A 32  ? 0.65674 0.57223 0.27012 0.04694  0.06537  0.00364  27  TYR A OH  
199  N  N   . LEU A 33  ? 0.63515 0.50165 0.28590 -0.00498 0.11643  0.08488  28  LEU A N   
200  C  CA  . LEU A 33  ? 0.65130 0.51322 0.31962 -0.01768 0.12640  0.09362  28  LEU A CA  
201  C  C   . LEU A 33  ? 0.75879 0.60390 0.43099 -0.01917 0.11657  0.09632  28  LEU A C   
202  O  O   . LEU A 33  ? 0.79209 0.62206 0.44426 -0.00945 0.10639  0.09911  28  LEU A O   
203  C  CB  . LEU A 33  ? 0.59349 0.44820 0.24802 -0.01882 0.13826  0.10485  28  LEU A CB  
204  C  CG  . LEU A 33  ? 0.66197 0.53260 0.31124 -0.01741 0.14964  0.10347  28  LEU A CG  
205  C  CD1 . LEU A 33  ? 0.76420 0.62628 0.40192 -0.02064 0.16271  0.11592  28  LEU A CD1 
206  C  CD2 . LEU A 33  ? 0.70060 0.59494 0.37960 -0.02604 0.15697  0.09607  28  LEU A CD2 
207  N  N   . LEU A 34  ? 0.67871 0.52749 0.37746 -0.03089 0.11922  0.09494  29  LEU A N   
208  C  CA  . LEU A 34  ? 0.74564 0.57831 0.45019 -0.03366 0.11178  0.09758  29  LEU A CA  
209  C  C   . LEU A 34  ? 0.75153 0.56484 0.44567 -0.03491 0.11686  0.10938  29  LEU A C   
210  O  O   . LEU A 34  ? 0.82190 0.63599 0.51024 -0.03757 0.12849  0.11596  29  LEU A O   
211  C  CB  . LEU A 34  ? 0.74105 0.58351 0.47691 -0.04660 0.11404  0.09240  29  LEU A CB  
212  C  CG  . LEU A 34  ? 0.59903 0.46114 0.34682 -0.04637 0.11090  0.08116  29  LEU A CG  
213  C  CD1 . LEU A 34  ? 0.66601 0.54090 0.44629 -0.05948 0.11423  0.07642  29  LEU A CD1 
214  C  CD2 . LEU A 34  ? 0.69107 0.55050 0.43232 -0.03528 0.09360  0.07448  29  LEU A CD2 
215  N  N   . ARG A 35  ? 1.15440 0.94994 0.84662 -0.03289 0.10839  0.11198  30  ARG A N   
216  C  CA  . ARG A 35  ? 1.25865 1.03233 0.93824 -0.03148 0.11090  0.12264  30  ARG A CA  
217  C  C   . ARG A 35  ? 1.30903 1.07465 1.01115 -0.04422 0.11469  0.12403  30  ARG A C   
218  O  O   . ARG A 35  ? 1.43008 1.18508 1.13683 -0.04247 0.10538  0.12184  30  ARG A O   
219  C  CB  . ARG A 35  ? 1.27202 1.03137 0.92905 -0.01611 0.09701  0.12405  30  ARG A CB  
220  C  CG  . ARG A 35  ? 1.22962 0.99513 0.89451 -0.01136 0.08277  0.11443  30  ARG A CG  
221  C  CD  . ARG A 35  ? 1.30082 1.05906 0.94447 0.00515  0.06822  0.11412  30  ARG A CD  
222  N  NE  . ARG A 35  ? 1.28239 1.05283 0.93242 0.00994  0.05557  0.10355  30  ARG A NE  
223  C  CZ  . ARG A 35  ? 1.32940 1.09718 0.99315 0.00925  0.04710  0.09971  30  ARG A CZ  
224  N  NH1 . ARG A 35  ? 1.31906 1.07235 0.99166 0.00467  0.04918  0.10457  30  ARG A NH1 
225  N  NH2 . ARG A 35  ? 1.07121 0.85278 0.74271 0.01320  0.03599  0.08964  30  ARG A NH2 
226  N  N   . GLU A 36  ? 1.34323 1.11489 1.05999 -0.05685 0.12811  0.12699  31  GLU A N   
227  C  CA  . GLU A 36  ? 1.31584 1.07907 1.05257 -0.06967 0.13293  0.12879  31  GLU A CA  
228  C  C   . GLU A 36  ? 1.22890 0.99368 0.98584 -0.07385 0.12346  0.11979  31  GLU A C   
229  O  O   . GLU A 36  ? 1.18832 0.96790 0.97153 -0.08577 0.12676  0.11339  31  GLU A O   
230  C  CB  . GLU A 36  ? 1.26712 1.00307 0.98599 -0.06629 0.13489  0.13971  31  GLU A CB  
231  C  CG  . GLU A 36  ? 1.38476 1.11741 1.09078 -0.06830 0.14846  0.14987  31  GLU A CG  
232  C  CD  . GLU A 36  ? 1.46197 1.19893 1.14063 -0.05472 0.14727  0.15240  31  GLU A CD  
233  O  OE1 . GLU A 36  ? 1.46039 1.19744 1.12662 -0.04233 0.13441  0.14771  31  GLU A OE1 
234  O  OE2 . GLU A 36  ? 1.48793 1.22862 1.15770 -0.05644 0.15896  0.15864  31  GLU A OE2 
235  N  N   . LYS A 37  ? 1.21001 0.96027 0.95514 -0.06368 0.11149  0.11916  32  LYS A N   
236  C  CA  . LYS A 37  ? 1.20334 0.95325 0.96510 -0.06627 0.10235  0.11111  32  LYS A CA  
237  C  C   . LYS A 37  ? 1.19319 0.96770 0.97377 -0.07163 0.10089  0.10089  32  LYS A C   
238  O  O   . LYS A 37  ? 1.16000 0.94158 0.96384 -0.08146 0.10021  0.09419  32  LYS A O   
239  C  CB  . LYS A 37  ? 1.14878 0.88428 0.89339 -0.05182 0.08946  0.11171  32  LYS A CB  
240  C  CG  . LYS A 37  ? 1.44771 1.15839 1.17520 -0.04541 0.08959  0.12110  32  LYS A CG  
241  C  CD  . LYS A 37  ? 1.38480 1.08641 1.09423 -0.02855 0.07643  0.12166  32  LYS A CD  
242  C  CE  . LYS A 37  ? 1.26899 0.97423 0.95399 -0.01684 0.07485  0.12593  32  LYS A CE  
243  N  NZ  . LYS A 37  ? 1.33035 1.05824 1.01835 -0.01763 0.07434  0.11915  32  LYS A NZ  
244  N  N   . ASP A 38  ? 1.17593 0.96373 0.94615 -0.06475 0.10001  0.09905  33  ASP A N   
245  C  CA  . ASP A 38  ? 1.09033 0.90143 0.87704 -0.06919 0.09980  0.08980  33  ASP A CA  
246  C  C   . ASP A 38  ? 1.05912 0.88898 0.86276 -0.07982 0.11236  0.08899  33  ASP A C   
247  O  O   . ASP A 38  ? 0.99777 0.84728 0.82313 -0.08657 0.11285  0.08087  33  ASP A O   
248  C  CB  . ASP A 38  ? 1.03839 0.85575 0.80749 -0.05713 0.09318  0.08682  33  ASP A CB  
249  C  CG  . ASP A 38  ? 1.12219 0.94033 0.89723 -0.04873 0.07660  0.07969  33  ASP A CG  
250  O  OD1 . ASP A 38  ? 0.88774 0.70909 0.68414 -0.05451 0.07252  0.07442  33  ASP A OD1 
251  O  OD2 . ASP A 38  ? 1.09360 0.91046 0.85285 -0.03623 0.06755  0.07878  33  ASP A OD2 
252  N  N   . ARG A 39  ? 1.05635 0.88156 0.85132 -0.08111 0.12237  0.09728  34  ARG A N   
253  C  CA  . ARG A 39  ? 1.04031 0.88494 0.85229 -0.09064 0.13465  0.09692  34  ARG A CA  
254  C  C   . ARG A 39  ? 1.06191 0.91368 0.90468 -0.10494 0.13653  0.09245  34  ARG A C   
255  O  O   . ARG A 39  ? 0.96946 0.84543 0.83508 -0.11209 0.14079  0.08622  34  ARG A O   
256  C  CB  . ARG A 39  ? 1.05826 0.89436 0.85350 -0.08932 0.14522  0.10773  34  ARG A CB  
257  C  CG  . ARG A 39  ? 0.98223 0.82341 0.75333 -0.07737 0.14672  0.10955  34  ARG A CG  
258  C  CD  . ARG A 39  ? 1.11931 0.96147 0.88243 -0.07976 0.16059  0.11839  34  ARG A CD  
259  N  NE  . ARG A 39  ? 1.08294 0.92653 0.81880 -0.06712 0.16111  0.12028  34  ARG A NE  
260  C  CZ  . ARG A 39  ? 1.04299 0.89078 0.76836 -0.06674 0.17282  0.12651  34  ARG A CZ  
261  N  NH1 . ARG A 39  ? 1.05055 0.90255 0.79135 -0.07870 0.18580  0.13206  34  ARG A NH1 
262  N  NH2 . ARG A 39  ? 0.87753 0.72566 0.57641 -0.05417 0.17125  0.12666  34  ARG A NH2 
263  N  N   . SER A 40  ? 1.04776 0.87936 0.89170 -0.10850 0.13272  0.09480  35  SER A N   
264  C  CA  . SER A 40  ? 1.06949 0.90599 0.94101 -0.12171 0.13318  0.08960  35  SER A CA  
265  C  C   . SER A 40  ? 1.07495 0.92738 0.96549 -0.12370 0.12402  0.07754  35  SER A C   
266  O  O   . SER A 40  ? 1.08854 0.95179 1.00410 -0.13428 0.12375  0.07113  35  SER A O   
267  C  CB  . SER A 40  ? 0.95788 0.76640 0.82310 -0.12350 0.13088  0.09452  35  SER A CB  
268  O  OG  . SER A 40  ? 1.11498 0.90815 0.96689 -0.11368 0.11922  0.09268  35  SER A OG  
269  N  N   . ASP A 41  ? 1.02255 0.87707 0.90187 -0.11387 0.11625  0.07415  36  ASP A N   
270  C  CA  . ASP A 41  ? 0.90979 0.77567 0.80391 -0.11486 0.10706  0.06384  36  ASP A CA  
271  C  C   . ASP A 41  ? 0.92029 0.81255 0.82228 -0.11295 0.10817  0.05778  36  ASP A C   
272  O  O   . ASP A 41  ? 0.72962 0.63474 0.64391 -0.10882 0.09765  0.04893  36  ASP A O   
273  C  CB  . ASP A 41  ? 0.97710 0.82295 0.85469 -0.10564 0.09618  0.06421  36  ASP A CB  
274  C  CG  . ASP A 41  ? 0.98054 0.82817 0.87506 -0.10926 0.08716  0.05545  36  ASP A CG  
275  O  OD1 . ASP A 41  ? 0.95400 0.81506 0.87100 -0.11980 0.08919  0.04950  36  ASP A OD1 
276  O  OD2 . ASP A 41  ? 1.05809 0.89735 0.94563 -0.09935 0.07642  0.05344  36  ASP A OD2 
277  N  N   . VAL A 42  ? 0.91062 0.81469 0.80893 -0.11161 0.11761  0.06108  37  VAL A N   
278  C  CA  . VAL A 42  ? 0.84013 0.77008 0.74681 -0.10794 0.11871  0.05464  37  VAL A CA  
279  C  C   . VAL A 42  ? 0.86598 0.82059 0.80481 -0.11862 0.12161  0.04745  37  VAL A C   
280  O  O   . VAL A 42  ? 0.84677 0.80946 0.79819 -0.12577 0.12997  0.04994  37  VAL A O   
281  C  CB  . VAL A 42  ? 0.86353 0.79638 0.75276 -0.10209 0.12860  0.06024  37  VAL A CB  
282  C  CG1 . VAL A 42  ? 0.55566 0.51366 0.45295 -0.09506 0.12720  0.05209  37  VAL A CG1 
283  C  CG2 . VAL A 42  ? 0.75641 0.66420 0.61272 -0.09192 0.12526  0.06761  37  VAL A CG2 
284  N  N   . LYS A 43  ? 0.65373 0.62327 0.60876 -0.11495 0.11016  0.03778  38  LYS A N   
285  C  CA  . LYS A 43  ? 0.78814 0.78303 0.77290 -0.12256 0.11006  0.02980  38  LYS A CA  
286  C  C   . LYS A 43  ? 0.71179 0.73316 0.70479 -0.11485 0.11172  0.02505  38  LYS A C   
287  O  O   . LYS A 43  ? 0.55846 0.58199 0.54510 -0.10279 0.10292  0.02124  38  LYS A O   
288  C  CB  . LYS A 43  ? 0.65085 0.64443 0.64618 -0.12215 0.09635  0.02244  38  LYS A CB  
289  C  CG  . LYS A 43  ? 0.78453 0.80130 0.80901 -0.13114 0.09497  0.01415  38  LYS A CG  
290  C  CD  . LYS A 43  ? 0.57727 0.59168 0.60745 -0.12842 0.08100  0.00681  38  LYS A CD  
291  C  CE  . LYS A 43  ? 0.66132 0.68244 0.68558 -0.11335 0.07198  0.00358  38  LYS A CE  
292  N  NZ  . LYS A 43  ? 0.65328 0.70283 0.69167 -0.10890 0.07395  -0.00065 38  LYS A NZ  
293  N  N   . LEU A 44  ? 0.58952 0.63052 0.59726 -0.12179 0.12360  0.02523  39  LEU A N   
294  C  CA  . LEU A 44  ? 0.73806 0.80551 0.75570 -0.11429 0.12629  0.02035  39  LEU A CA  
295  C  C   . LEU A 44  ? 0.81109 0.90772 0.86090 -0.11820 0.12252  0.01136  39  LEU A C   
296  O  O   . LEU A 44  ? 0.78208 0.89998 0.84081 -0.10923 0.12120  0.00609  39  LEU A O   
297  C  CB  . LEU A 44  ? 0.75788 0.82984 0.76853 -0.11493 0.14185  0.02672  39  LEU A CB  
298  C  CG  . LEU A 44  ? 0.66074 0.70830 0.63700 -0.10800 0.14622  0.03511  39  LEU A CG  
299  C  CD1 . LEU A 44  ? 0.61151 0.66732 0.58367 -0.10589 0.15924  0.04064  39  LEU A CD1 
300  C  CD2 . LEU A 44  ? 0.69648 0.73848 0.65625 -0.09365 0.13570  0.03085  39  LEU A CD2 
301  N  N   . VAL A 45  ? 0.76080 0.85860 0.82763 -0.13064 0.12020  0.00899  40  VAL A N   
302  C  CA  . VAL A 45  ? 0.72884 0.85503 0.82638 -0.13404 0.11496  -0.00002 40  VAL A CA  
303  C  C   . VAL A 45  ? 0.74086 0.86362 0.83986 -0.12944 0.09887  -0.00685 40  VAL A C   
304  O  O   . VAL A 45  ? 0.73945 0.83606 0.82288 -0.13018 0.09286  -0.00449 40  VAL A O   
305  C  CB  . VAL A 45  ? 0.79532 0.92427 0.91055 -0.14647 0.11891  0.00133  40  VAL A CB  
306  C  CG1 . VAL A 45  ? 0.75941 0.86004 0.86600 -0.15473 0.11388  0.00342  40  VAL A CG1 
307  C  CG2 . VAL A 45  ? 0.69913 0.86152 0.84664 -0.14855 0.11401  -0.00810 40  VAL A CG2 
308  N  N   . ALA A 46  ? 0.68442 0.83265 0.80050 -0.12252 0.09153  -0.01481 41  ALA A N   
309  C  CA  . ALA A 46  ? 0.74193 0.88816 0.85871 -0.11650 0.07637  -0.02092 41  ALA A CA  
310  C  C   . ALA A 46  ? 0.54477 0.69277 0.67724 -0.12967 0.07147  -0.02632 41  ALA A C   
311  O  O   . ALA A 46  ? 0.60854 0.76838 0.75943 -0.14328 0.07895  -0.02750 41  ALA A O   
312  C  CB  . ALA A 46  ? 0.67026 0.84162 0.79806 -0.10370 0.07041  -0.02684 41  ALA A CB  
313  N  N   . ALA A 47  ? 0.53440 0.67052 0.65974 -0.12565 0.05903  -0.03014 42  ALA A N   
314  C  CA  . ALA A 47  ? 0.65985 0.78940 0.79327 -0.13719 0.05344  -0.03544 42  ALA A CA  
315  C  C   . ALA A 47  ? 0.72367 0.88445 0.88539 -0.14212 0.04717  -0.04626 42  ALA A C   
316  O  O   . ALA A 47  ? 0.88350 1.04073 1.05477 -0.15339 0.04321  -0.05171 42  ALA A O   
317  C  CB  . ALA A 47  ? 0.53828 0.64387 0.65217 -0.12979 0.04291  -0.03596 42  ALA A CB  
318  N  N   . GLU A 48  ? 0.66865 0.85817 0.84269 -0.13243 0.04511  -0.04960 43  GLU A N   
319  C  CA  . GLU A 48  ? 0.64248 0.86643 0.84458 -0.13446 0.03836  -0.06000 43  GLU A CA  
320  C  C   . GLU A 48  ? 0.60520 0.82956 0.80420 -0.12749 0.02175  -0.06816 43  GLU A C   
321  O  O   . GLU A 48  ? 0.52348 0.77485 0.73576 -0.11897 0.01333  -0.07495 43  GLU A O   
322  C  CB  . GLU A 48  ? 0.73773 0.96450 0.95686 -0.14841 0.04325  -0.06035 43  GLU A CB  
323  C  CG  . GLU A 48  ? 0.72778 0.98818 0.97417 -0.14759 0.03664  -0.06877 43  GLU A CG  
324  C  CD  . GLU A 48  ? 0.93541 1.20127 1.20037 -0.16096 0.04476  -0.06705 43  GLU A CD  
325  O  OE1 . GLU A 48  ? 0.94162 1.18390 1.19687 -0.17026 0.05560  -0.05882 43  GLU A OE1 
326  O  OE2 . GLU A 48  ? 1.01041 1.30429 1.29957 -0.16173 0.04025  -0.07356 43  GLU A OE2 
327  N  N   . LEU A 49  ? 0.41261 0.60765 0.59327 -0.12979 0.01698  -0.06754 44  LEU A N   
328  C  CA  . LEU A 49  ? 0.47166 0.66278 0.64330 -0.12111 0.00252  -0.07403 44  LEU A CA  
329  C  C   . LEU A 49  ? 0.40988 0.56763 0.55150 -0.11238 0.00209  -0.06679 44  LEU A C   
330  O  O   . LEU A 49  ? 0.40840 0.54468 0.53916 -0.11640 -0.00212 -0.06881 44  LEU A O   
331  C  CB  . LEU A 49  ? 0.39920 0.59354 0.58444 -0.13434 -0.00501 -0.08483 44  LEU A CB  
332  C  CG  . LEU A 49  ? 0.45390 0.68001 0.66699 -0.13852 -0.00853 -0.09218 44  LEU A CG  
333  C  CD1 . LEU A 49  ? 0.54393 0.76217 0.76243 -0.14807 -0.01663 -0.09998 44  LEU A CD1 
334  C  CD2 . LEU A 49  ? 0.38477 0.64140 0.60509 -0.12314 -0.01772 -0.09726 44  LEU A CD2 
335  N  N   . PRO A 50  ? 0.33602 0.48925 0.46461 -0.10007 0.00620  -0.05902 45  PRO A N   
336  C  CA  . PRO A 50  ? 0.31318 0.43743 0.41648 -0.09236 0.00600  -0.05255 45  PRO A CA  
337  C  C   . PRO A 50  ? 0.35189 0.47156 0.44521 -0.08284 -0.00522 -0.05707 45  PRO A C   
338  O  O   . PRO A 50  ? 0.34547 0.48552 0.44699 -0.07646 -0.01301 -0.06324 45  PRO A O   
339  C  CB  . PRO A 50  ? 0.38632 0.51284 0.48311 -0.08196 0.01214  -0.04547 45  PRO A CB  
340  C  CG  . PRO A 50  ? 0.31094 0.46900 0.42635 -0.07768 0.01073  -0.05006 45  PRO A CG  
341  C  CD  . PRO A 50  ? 0.37187 0.54640 0.50910 -0.09246 0.01114  -0.05654 45  PRO A CD  
342  N  N   . GLU A 51  ? 0.38187 0.47479 0.45677 -0.08122 -0.00579 -0.05383 46  GLU A N   
343  C  CA  . GLU A 51  ? 0.35471 0.44058 0.41683 -0.07099 -0.01418 -0.05657 46  GLU A CA  
344  C  C   . GLU A 51  ? 0.34422 0.43328 0.39790 -0.05590 -0.01378 -0.05125 46  GLU A C   
345  O  O   . GLU A 51  ? 0.28611 0.37119 0.33734 -0.05380 -0.00663 -0.04442 46  GLU A O   
346  C  CB  . GLU A 51  ? 0.47662 0.53379 0.52274 -0.07306 -0.01356 -0.05442 46  GLU A CB  
347  C  CG  . GLU A 51  ? 0.60257 0.65136 0.65277 -0.08532 -0.01633 -0.06128 46  GLU A CG  
348  C  CD  . GLU A 51  ? 0.84675 0.86705 0.87925 -0.08357 -0.01648 -0.05949 46  GLU A CD  
349  O  OE1 . GLU A 51  ? 0.80493 0.81654 0.82380 -0.07208 -0.01595 -0.05431 46  GLU A OE1 
350  O  OE2 . GLU A 51  ? 1.00738 1.01386 1.04046 -0.09363 -0.01671 -0.06335 46  GLU A OE2 
351  N  N   . PRO A 52  ? 0.34022 0.43512 0.38827 -0.04509 -0.02124 -0.05434 47  PRO A N   
352  C  CA  . PRO A 52  ? 0.32335 0.41627 0.36148 -0.03095 -0.01985 -0.04834 47  PRO A CA  
353  C  C   . PRO A 52  ? 0.34893 0.41770 0.37307 -0.02933 -0.01381 -0.04087 47  PRO A C   
354  O  O   . PRO A 52  ? 0.34661 0.39874 0.36268 -0.03341 -0.01409 -0.04114 47  PRO A O   
355  C  CB  . PRO A 52  ? 0.32244 0.42044 0.35302 -0.02096 -0.02882 -0.05280 47  PRO A CB  
356  C  CG  . PRO A 52  ? 0.34532 0.46105 0.38977 -0.02889 -0.03622 -0.06292 47  PRO A CG  
357  C  CD  . PRO A 52  ? 0.32393 0.42983 0.37549 -0.04515 -0.03134 -0.06390 47  PRO A CD  
358  N  N   . LEU A 53  ? 0.30669 0.37413 0.32888 -0.02320 -0.00873 -0.03495 48  LEU A N   
359  C  CA  . LEU A 53  ? 0.25183 0.29963 0.26345 -0.02143 -0.00377 -0.02873 48  LEU A CA  
360  C  C   . LEU A 53  ? 0.33192 0.37122 0.33215 -0.01064 -0.00535 -0.02635 48  LEU A C   
361  O  O   . LEU A 53  ? 0.30804 0.35675 0.30711 -0.00217 -0.00878 -0.02748 48  LEU A O   
362  C  CB  . LEU A 53  ? 0.30714 0.35669 0.32205 -0.02051 0.00231  -0.02457 48  LEU A CB  
363  C  CG  . LEU A 53  ? 0.38322 0.43801 0.40609 -0.03055 0.00653  -0.02498 48  LEU A CG  
364  C  CD1 . LEU A 53  ? 0.50623 0.56083 0.52838 -0.02730 0.01224  -0.02138 48  LEU A CD1 
365  C  CD2 . LEU A 53  ? 0.42857 0.46774 0.44625 -0.03958 0.00755  -0.02398 48  LEU A CD2 
366  N  N   . PRO A 54  ? 0.31631 0.33838 0.30796 -0.01007 -0.00256 -0.02268 49  PRO A N   
367  C  CA  . PRO A 54  ? 0.32296 0.33739 0.30487 -0.00029 -0.00201 -0.01963 49  PRO A CA  
368  C  C   . PRO A 54  ? 0.34169 0.35745 0.32439 0.00703  0.00191  -0.01490 49  PRO A C   
369  O  O   . PRO A 54  ? 0.32018 0.33427 0.30784 0.00421  0.00571  -0.01283 49  PRO A O   
370  C  CB  . PRO A 54  ? 0.39057 0.38864 0.36709 -0.00303 0.00072  -0.01743 49  PRO A CB  
371  C  CG  . PRO A 54  ? 0.46732 0.46304 0.44964 -0.01197 0.00242  -0.01719 49  PRO A CG  
372  C  CD  . PRO A 54  ? 0.38186 0.39123 0.37241 -0.01774 0.00033  -0.02102 49  PRO A CD  
373  N  N   . VAL A 55  ? 0.31492 0.33265 0.29133 0.01701  0.00085  -0.01340 50  VAL A N   
374  C  CA  . VAL A 55  ? 0.25798 0.27398 0.23337 0.02527  0.00480  -0.00850 50  VAL A CA  
375  C  C   . VAL A 55  ? 0.30843 0.31125 0.27269 0.03241  0.00845  -0.00340 50  VAL A C   
376  O  O   . VAL A 55  ? 0.34113 0.34370 0.29607 0.03658  0.00555  -0.00447 50  VAL A O   
377  C  CB  . VAL A 55  ? 0.31959 0.35102 0.29766 0.03232  0.00083  -0.01036 50  VAL A CB  
378  C  CG1 . VAL A 55  ? 0.27554 0.30197 0.25196 0.04133  0.00559  -0.00500 50  VAL A CG1 
379  C  CG2 . VAL A 55  ? 0.44282 0.49016 0.43395 0.02441  -0.00200 -0.01591 50  VAL A CG2 
380  N  N   . VAL A 56  ? 0.28314 0.27501 0.24851 0.03340  0.01512  0.00168  51  VAL A N   
381  C  CA  . VAL A 56  ? 0.30355 0.28277 0.26100 0.03910  0.02093  0.00749  51  VAL A CA  
382  C  C   . VAL A 56  ? 0.34117 0.31522 0.29759 0.04646  0.02560  0.01267  51  VAL A C   
383  O  O   . VAL A 56  ? 0.32463 0.29886 0.28943 0.04374  0.02688  0.01192  51  VAL A O   
384  C  CB  . VAL A 56  ? 0.31841 0.28828 0.28082 0.03215  0.02533  0.00851  51  VAL A CB  
385  C  CG1 . VAL A 56  ? 0.32734 0.28578 0.28487 0.03728  0.03317  0.01486  51  VAL A CG1 
386  C  CG2 . VAL A 56  ? 0.35009 0.32245 0.31188 0.02635  0.02092  0.00385  51  VAL A CG2 
387  N  N   . ASP A 57  ? 0.31167 0.27975 0.25628 0.05636  0.02840  0.01794  52  ASP A N   
388  C  CA  . ASP A 57  ? 0.33519 0.29428 0.27607 0.06468  0.03388  0.02430  52  ASP A CA  
389  C  C   . ASP A 57  ? 0.36771 0.31039 0.30929 0.06234  0.04391  0.03029  52  ASP A C   
390  O  O   . ASP A 57  ? 0.33862 0.27547 0.27097 0.06560  0.04800  0.03431  52  ASP A O   
391  C  CB  . ASP A 57  ? 0.35845 0.32061 0.28435 0.07799  0.03085  0.02721  52  ASP A CB  
392  C  CG  . ASP A 57  ? 0.38337 0.33400 0.30300 0.08847  0.03662  0.03486  52  ASP A CG  
393  O  OD1 . ASP A 57  ? 0.35022 0.28446 0.27209 0.08626  0.04607  0.04040  52  ASP A OD1 
394  O  OD2 . ASP A 57  ? 0.37800 0.33576 0.29068 0.09936  0.03155  0.03526  52  ASP A OD2 
395  N  N   . LEU A 58  ? 0.32503 0.26105 0.27814 0.05655  0.04798  0.03026  53  LEU A N   
396  C  CA  . LEU A 58  ? 0.33013 0.25292 0.28872 0.05215  0.05700  0.03445  53  LEU A CA  
397  C  C   . LEU A 58  ? 0.33494 0.24444 0.28175 0.06118  0.06572  0.04381  53  LEU A C   
398  O  O   . LEU A 58  ? 0.41861 0.32113 0.36547 0.05929  0.07336  0.04807  53  LEU A O   
399  C  CB  . LEU A 58  ? 0.33235 0.24971 0.30412 0.04577  0.05880  0.03187  53  LEU A CB  
400  C  CG  . LEU A 58  ? 0.39840 0.30593 0.38099 0.03841  0.06631  0.03364  53  LEU A CG  
401  C  CD1 . LEU A 58  ? 0.44165 0.35877 0.43148 0.03064  0.06267  0.02913  53  LEU A CD1 
402  C  CD2 . LEU A 58  ? 0.37883 0.27808 0.37228 0.03372  0.06825  0.03096  53  LEU A CD2 
403  N  N   . SER A 59  ? 0.36149 0.26738 0.29778 0.07177  0.06529  0.04758  54  SER A N   
404  C  CA  . SER A 59  ? 0.42551 0.31580 0.34812 0.08142  0.07445  0.05791  54  SER A CA  
405  C  C   . SER A 59  ? 0.46164 0.35440 0.36801 0.08794  0.07505  0.06136  54  SER A C   
406  O  O   . SER A 59  ? 0.44240 0.32125 0.33672 0.09463  0.08485  0.07075  54  SER A O   
407  C  CB  . SER A 59  ? 0.42204 0.30734 0.33577 0.09310  0.07301  0.06133  54  SER A CB  
408  O  OG  . SER A 59  ? 0.41373 0.31441 0.31691 0.10209  0.06276  0.05833  54  SER A OG  
409  N  N   . ARG A 60  ? 0.38815 0.29678 0.29299 0.08623  0.06552  0.05404  55  ARG A N   
410  C  CA  . ARG A 60  ? 0.43554 0.34661 0.32393 0.09259  0.06479  0.05523  55  ARG A CA  
411  C  C   . ARG A 60  ? 0.45149 0.36427 0.34689 0.08362  0.06774  0.05220  55  ARG A C   
412  O  O   . ARG A 60  ? 0.43249 0.34736 0.31478 0.08818  0.06700  0.05157  55  ARG A O   
413  C  CB  . ARG A 60  ? 0.42529 0.35236 0.30561 0.09816  0.05128  0.04818  55  ARG A CB  
414  C  CG  . ARG A 60  ? 0.44008 0.37095 0.31633 0.10771  0.04599  0.04929  55  ARG A CG  
415  C  CD  . ARG A 60  ? 0.42169 0.33513 0.28264 0.12014  0.05508  0.06107  55  ARG A CD  
416  N  NE  . ARG A 60  ? 0.42473 0.33303 0.26255 0.13067  0.05758  0.06640  55  ARG A NE  
417  C  CZ  . ARG A 60  ? 0.49441 0.38571 0.31441 0.14225  0.06691  0.07807  55  ARG A CZ  
418  N  NH1 . ARG A 60  ? 0.52232 0.39877 0.34584 0.14442  0.07462  0.08557  55  ARG A NH1 
419  N  NH2 . ARG A 60  ? 0.48158 0.36916 0.27835 0.15223  0.06898  0.08240  55  ARG A NH2 
420  N  N   . LEU A 61  ? 0.40940 0.32128 0.32443 0.07201  0.07077  0.04995  56  LEU A N   
421  C  CA  . LEU A 61  ? 0.40757 0.32502 0.33205 0.06355  0.07002  0.04489  56  LEU A CA  
422  C  C   . LEU A 61  ? 0.47151 0.38237 0.39020 0.06625  0.08044  0.05031  56  LEU A C   
423  O  O   . LEU A 61  ? 0.51295 0.42903 0.43544 0.06248  0.07927  0.04599  56  LEU A O   
424  C  CB  . LEU A 61  ? 0.48520 0.40416 0.43131 0.05198  0.06958  0.04112  56  LEU A CB  
425  C  CG  . LEU A 61  ? 0.47404 0.40118 0.43108 0.04343  0.06469  0.03424  56  LEU A CG  
426  C  CD1 . LEU A 61  ? 0.41462 0.35002 0.36150 0.04548  0.05542  0.02858  56  LEU A CD1 
427  C  CD2 . LEU A 61  ? 0.40866 0.33857 0.38190 0.03461  0.06081  0.02978  56  LEU A CD2 
428  N  N   . ASP A 62  ? 0.49727 0.39628 0.40649 0.07313  0.09131  0.05993  57  ASP A N   
429  C  CA  . ASP A 62  ? 0.49314 0.38670 0.39492 0.07668  0.10260  0.06565  57  ASP A CA  
430  C  C   . ASP A 62  ? 0.60999 0.50728 0.48870 0.08661  0.09803  0.06365  57  ASP A C   
431  O  O   . ASP A 62  ? 0.61938 0.51569 0.49255 0.08879  0.10496  0.06496  57  ASP A O   
432  C  CB  . ASP A 62  ? 0.64867 0.52662 0.54548 0.08107  0.11709  0.07761  57  ASP A CB  
433  C  CG  . ASP A 62  ? 0.72469 0.59770 0.64654 0.06963  0.12409  0.07890  57  ASP A CG  
434  O  OD1 . ASP A 62  ? 0.72724 0.61004 0.66956 0.05915  0.11994  0.07140  57  ASP A OD1 
435  O  OD2 . ASP A 62  ? 0.84562 0.70421 0.76617 0.07140  0.13346  0.08718  57  ASP A OD2 
436  N  N   . GLY A 63  ? 0.50049 0.40285 0.36637 0.09282  0.08644  0.05977  58  GLY A N   
437  C  CA  . GLY A 63  ? 0.51678 0.42291 0.36042 0.10231  0.08056  0.05646  58  GLY A CA  
438  C  C   . GLY A 63  ? 0.52106 0.43692 0.37091 0.09570  0.07204  0.04541  58  GLY A C   
439  O  O   . GLY A 63  ? 0.43335 0.35578 0.30236 0.08497  0.06603  0.03924  58  GLY A O   
440  N  N   . ALA A 64  ? 0.48823 0.40341 0.31959 0.10299  0.07180  0.04302  59  ALA A N   
441  C  CA  . ALA A 64  ? 0.55747 0.47842 0.39240 0.09780  0.06466  0.03259  59  ALA A CA  
442  C  C   . ALA A 64  ? 0.41098 0.34206 0.25214 0.09226  0.04907  0.02274  59  ALA A C   
443  O  O   . ALA A 64  ? 0.43225 0.36714 0.28857 0.08217  0.04432  0.01617  59  ALA A O   
444  C  CB  . ALA A 64  ? 0.52528 0.44232 0.33609 0.10822  0.06679  0.03095  59  ALA A CB  
445  N  N   . GLU A 65  ? 0.46456 0.40045 0.29447 0.09906  0.04130  0.02188  60  GLU A N   
446  C  CA  . GLU A 65  ? 0.41737 0.36535 0.25472 0.09372  0.02705  0.01213  60  GLU A CA  
447  C  C   . GLU A 65  ? 0.45311 0.40534 0.31493 0.08191  0.02643  0.01198  60  GLU A C   
448  O  O   . GLU A 65  ? 0.40039 0.35952 0.27380 0.07262  0.01880  0.00404  60  GLU A O   
449  C  CB  . GLU A 65  ? 0.49959 0.45451 0.32275 0.10438  0.01912  0.01175  60  GLU A CB  
450  C  CG  . GLU A 65  ? 0.64579 0.59857 0.44176 0.11699  0.01628  0.00961  60  GLU A CG  
451  C  CD  . GLU A 65  ? 0.83098 0.76998 0.60831 0.12834  0.02997  0.02173  60  GLU A CD  
452  O  OE1 . GLU A 65  ? 0.64715 0.57873 0.43365 0.12662  0.04093  0.03199  60  GLU A OE1 
453  O  OE2 . GLU A 65  ? 0.88105 0.81608 0.63411 0.13886  0.03014  0.02078  60  GLU A OE2 
454  N  N   . GLU A 66  ? 0.44327 0.39027 0.31228 0.08210  0.03480  0.02060  61  GLU A N   
455  C  CA  . GLU A 66  ? 0.37348 0.32394 0.26344 0.07195  0.03402  0.01979  61  GLU A CA  
456  C  C   . GLU A 66  ? 0.40405 0.35137 0.30766 0.06183  0.03763  0.01799  61  GLU A C   
457  O  O   . GLU A 66  ? 0.38424 0.33669 0.30137 0.05269  0.03269  0.01323  61  GLU A O   
458  C  CB  . GLU A 66  ? 0.36502 0.30943 0.25779 0.07555  0.04108  0.02825  61  GLU A CB  
459  C  CG  . GLU A 66  ? 0.32231 0.27263 0.23197 0.06834  0.03729  0.02562  61  GLU A CG  
460  C  CD  . GLU A 66  ? 0.37564 0.33926 0.28377 0.07134  0.02671  0.02019  61  GLU A CD  
461  O  OE1 . GLU A 66  ? 0.37998 0.34738 0.27339 0.08069  0.02218  0.01958  61  GLU A OE1 
462  O  OE2 . GLU A 66  ? 0.35486 0.32629 0.27668 0.06467  0.02284  0.01620  61  GLU A OE2 
463  N  N   . ALA A 67  ? 0.40812 0.34761 0.30812 0.06405  0.04646  0.02198  62  ALA A N   
464  C  CA  . ALA A 67  ? 0.36493 0.30330 0.27759 0.05632  0.04881  0.01962  62  ALA A CA  
465  C  C   . ALA A 67  ? 0.36589 0.30796 0.27690 0.05249  0.03962  0.01069  62  ALA A C   
466  O  O   . ALA A 67  ? 0.39337 0.33607 0.31678 0.04461  0.03759  0.00762  62  ALA A O   
467  C  CB  . ALA A 67  ? 0.40327 0.33494 0.31233 0.06085  0.06035  0.02506  62  ALA A CB  
468  N  N   . THR A 68  ? 0.40828 0.35185 0.30349 0.05818  0.03385  0.00630  63  THR A N   
469  C  CA  . THR A 68  ? 0.40583 0.35132 0.29991 0.05354  0.02489  -0.00302 63  THR A CA  
470  C  C   . THR A 68  ? 0.36094 0.31391 0.26818 0.04420  0.01730  -0.00690 63  THR A C   
471  O  O   . THR A 68  ? 0.34764 0.29930 0.26203 0.03630  0.01366  -0.01164 63  THR A O   
472  C  CB  . THR A 68  ? 0.39834 0.34447 0.27286 0.06158  0.01954  -0.00809 63  THR A CB  
473  O  OG1 . THR A 68  ? 0.43106 0.36904 0.29203 0.06990  0.02739  -0.00534 63  THR A OG1 
474  C  CG2 . THR A 68  ? 0.53056 0.47858 0.40594 0.05511  0.00929  -0.01890 63  THR A CG2 
475  N  N   . LYS A 69  ? 0.33331 0.29354 0.24314 0.04565  0.01548  -0.00461 64  LYS A N   
476  C  CA  . LYS A 69  ? 0.34625 0.31471 0.26934 0.03731  0.01016  -0.00767 64  LYS A CA  
477  C  C   . LYS A 69  ? 0.34084 0.30523 0.27738 0.02954  0.01441  -0.00504 64  LYS A C   
478  O  O   . LYS A 69  ? 0.32425 0.29116 0.26897 0.02120  0.01063  -0.00865 64  LYS A O   
479  C  CB  . LYS A 69  ? 0.33717 0.31414 0.26082 0.04226  0.00866  -0.00520 64  LYS A CB  
480  C  CG  . LYS A 69  ? 0.39744 0.38150 0.30847 0.05076  0.00220  -0.00847 64  LYS A CG  
481  C  CD  . LYS A 69  ? 0.38084 0.37205 0.29240 0.05783  0.00171  -0.00451 64  LYS A CD  
482  C  CE  . LYS A 69  ? 0.47002 0.46555 0.36488 0.07029  -0.00321 -0.00509 64  LYS A CE  
483  N  NZ  . LYS A 69  ? 0.44474 0.44249 0.33754 0.07984  -0.00139 0.00143  64  LYS A NZ  
484  N  N   . LEU A 70  ? 0.34510 0.30339 0.28404 0.03217  0.02234  0.00123  65  LEU A N   
485  C  CA  . LEU A 70  ? 0.34328 0.29860 0.29482 0.02561  0.02529  0.00268  65  LEU A CA  
486  C  C   . LEU A 70  ? 0.35010 0.30123 0.30227 0.02183  0.02339  -0.00085 65  LEU A C   
487  O  O   . LEU A 70  ? 0.33893 0.28992 0.29871 0.01516  0.02073  -0.00253 65  LEU A O   
488  C  CB  . LEU A 70  ? 0.33609 0.28657 0.29171 0.02876  0.03405  0.00903  65  LEU A CB  
489  C  CG  . LEU A 70  ? 0.37653 0.32574 0.34652 0.02245  0.03613  0.00948  65  LEU A CG  
490  C  CD1 . LEU A 70  ? 0.33563 0.28881 0.31281 0.01656  0.03151  0.00722  65  LEU A CD1 
491  C  CD2 . LEU A 70  ? 0.35486 0.30018 0.33137 0.02443  0.04511  0.01485  65  LEU A CD2 
492  N  N   . ARG A 71  ? 0.34309 0.28964 0.28578 0.02703  0.02506  -0.00180 66  ARG A N   
493  C  CA  . ARG A 71  ? 0.30993 0.25073 0.25231 0.02491  0.02350  -0.00537 66  ARG A CA  
494  C  C   . ARG A 71  ? 0.32034 0.26100 0.26232 0.01809  0.01563  -0.01113 66  ARG A C   
495  O  O   . ARG A 71  ? 0.38902 0.32533 0.33642 0.01288  0.01410  -0.01198 66  ARG A O   
496  C  CB  . ARG A 71  ? 0.33640 0.27205 0.26649 0.03282  0.02678  -0.00642 66  ARG A CB  
497  C  CG  . ARG A 71  ? 0.40137 0.32947 0.32973 0.03189  0.02483  -0.01100 66  ARG A CG  
498  C  CD  . ARG A 71  ? 0.47682 0.39956 0.39280 0.04092  0.02942  -0.01229 66  ARG A CD  
499  N  NE  . ARG A 71  ? 0.57241 0.49464 0.49672 0.04425  0.03765  -0.00796 66  ARG A NE  
500  C  CZ  . ARG A 71  ? 0.53518 0.46012 0.45922 0.05015  0.04699  -0.00249 66  ARG A CZ  
501  N  NH1 . ARG A 71  ? 0.86481 0.79074 0.77719 0.05490  0.04952  0.00010  66  ARG A NH1 
502  N  NH2 . ARG A 71  ? 0.64301 0.56996 0.57902 0.05161  0.05421  0.00068  66  ARG A NH2 
503  N  N   . VAL A 72  ? 0.36709 0.31281 0.30319 0.01805  0.01068  -0.01494 67  VAL A N   
504  C  CA  . VAL A 72  ? 0.38633 0.33316 0.32461 0.01013  0.00407  -0.02068 67  VAL A CA  
505  C  C   . VAL A 72  ? 0.40769 0.35777 0.35750 0.00258  0.00432  -0.01811 67  VAL A C   
506  O  O   . VAL A 72  ? 0.38308 0.32783 0.33557 -0.00428 0.00256  -0.01977 67  VAL A O   
507  C  CB  . VAL A 72  ? 0.38259 0.33849 0.31593 0.01155  -0.00169 -0.02570 67  VAL A CB  
508  C  CG1 . VAL A 72  ? 0.41364 0.37402 0.35438 0.00136  -0.00750 -0.03135 67  VAL A CG1 
509  C  CG2 . VAL A 72  ? 0.38077 0.33181 0.29949 0.01911  -0.00310 -0.02966 67  VAL A CG2 
510  N  N   . ALA A 73  ? 0.33542 0.29265 0.29067 0.00428  0.00700  -0.01386 68  ALA A N   
511  C  CA  . ALA A 73  ? 0.37942 0.33964 0.34362 -0.00170 0.00750  -0.01197 68  ALA A CA  
512  C  C   . ALA A 73  ? 0.37181 0.32332 0.33857 -0.00391 0.00936  -0.00975 68  ALA A C   
513  O  O   . ALA A 73  ? 0.35854 0.30767 0.32737 -0.00992 0.00784  -0.01007 68  ALA A O   
514  C  CB  . ALA A 73  ? 0.29354 0.26065 0.26183 0.00191  0.01030  -0.00853 68  ALA A CB  
515  N  N   . LEU A 74  ? 0.34341 0.29060 0.31001 0.00135  0.01284  -0.00732 69  LEU A N   
516  C  CA  . LEU A 74  ? 0.35940 0.30177 0.33102 0.00041  0.01383  -0.00545 69  LEU A CA  
517  C  C   . LEU A 74  ? 0.39956 0.33270 0.36634 -0.00094 0.01123  -0.00756 69  LEU A C   
518  O  O   . LEU A 74  ? 0.35456 0.28348 0.32325 -0.00350 0.00966  -0.00646 69  LEU A O   
519  C  CB  . LEU A 74  ? 0.36892 0.31197 0.34539 0.00583  0.01888  -0.00258 69  LEU A CB  
520  C  CG  . LEU A 74  ? 0.34615 0.29473 0.32865 0.00636  0.02222  0.00012  69  LEU A CG  
521  C  CD1 . LEU A 74  ? 0.47705 0.42533 0.46599 0.01026  0.02847  0.00312  69  LEU A CD1 
522  C  CD2 . LEU A 74  ? 0.36947 0.32067 0.35796 0.00119  0.01954  -0.00034 69  LEU A CD2 
523  N  N   . GLN A 75  ? 0.38742 0.31606 0.34653 0.00147  0.01055  -0.01073 70  GLN A N   
524  C  CA  . GLN A 75  ? 0.39131 0.30827 0.34499 0.00070  0.00841  -0.01330 70  GLN A CA  
525  C  C   . GLN A 75  ? 0.42369 0.33656 0.37549 -0.00771 0.00469  -0.01551 70  GLN A C   
526  O  O   . GLN A 75  ? 0.51198 0.41406 0.46175 -0.01022 0.00372  -0.01478 70  GLN A O   
527  C  CB  . GLN A 75  ? 0.40631 0.31858 0.35134 0.00658  0.00913  -0.01707 70  GLN A CB  
528  C  CG  . GLN A 75  ? 0.44349 0.35832 0.39001 0.01502  0.01478  -0.01426 70  GLN A CG  
529  C  CD  . GLN A 75  ? 0.48419 0.39298 0.41955 0.02187  0.01629  -0.01809 70  GLN A CD  
530  O  OE1 . GLN A 75  ? 0.56316 0.46504 0.48942 0.02021  0.01197  -0.02388 70  GLN A OE1 
531  N  NE2 . GLN A 75  ? 0.46225 0.37362 0.39847 0.02939  0.02283  -0.01530 70  GLN A NE2 
532  N  N   . ASN A 76  ? 0.42060 0.34202 0.37350 -0.01191 0.00300  -0.01789 71  ASN A N   
533  C  CA  . ASN A 76  ? 0.42138 0.34056 0.37464 -0.02082 0.00039  -0.02081 71  ASN A CA  
534  C  C   . ASN A 76  ? 0.45090 0.37758 0.41073 -0.02677 0.00164  -0.01751 71  ASN A C   
535  O  O   . ASN A 76  ? 0.42873 0.35126 0.38922 -0.03470 0.00153  -0.01800 71  ASN A O   
536  C  CB  . ASN A 76  ? 0.47074 0.39633 0.42251 -0.02215 -0.00319 -0.02737 71  ASN A CB  
537  C  CG  . ASN A 76  ? 0.56730 0.48228 0.50971 -0.01782 -0.00508 -0.03244 71  ASN A CG  
538  O  OD1 . ASN A 76  ? 0.52011 0.42181 0.45801 -0.01471 -0.00329 -0.03108 71  ASN A OD1 
539  N  ND2 . ASN A 76  ? 0.55409 0.47523 0.49299 -0.01668 -0.00909 -0.03879 71  ASN A ND2 
540  N  N   . TRP A 77  ? 0.35258 0.28905 0.31681 -0.02330 0.00353  -0.01428 72  TRP A N   
541  C  CA  . TRP A 77  ? 0.35887 0.30246 0.32788 -0.02780 0.00500  -0.01201 72  TRP A CA  
542  C  C   . TRP A 77  ? 0.39321 0.33461 0.36267 -0.02498 0.00671  -0.00770 72  TRP A C   
543  O  O   . TRP A 77  ? 0.38664 0.32690 0.35523 -0.02885 0.00763  -0.00561 72  TRP A O   
544  C  CB  . TRP A 77  ? 0.39260 0.35164 0.36705 -0.02665 0.00492  -0.01374 72  TRP A CB  
545  C  CG  . TRP A 77  ? 0.37862 0.34384 0.35394 -0.02858 0.00162  -0.01908 72  TRP A CG  
546  C  CD1 . TRP A 77  ? 0.43745 0.40013 0.40742 -0.02403 -0.00115 -0.02244 72  TRP A CD1 
547  C  CD2 . TRP A 77  ? 0.37685 0.35358 0.35931 -0.03512 0.00043  -0.02240 72  TRP A CD2 
548  N  NE1 . TRP A 77  ? 0.49680 0.46829 0.46944 -0.02735 -0.00530 -0.02832 72  TRP A NE1 
549  C  CE2 . TRP A 77  ? 0.43524 0.41642 0.41725 -0.03456 -0.00439 -0.02843 72  TRP A CE2 
550  C  CE3 . TRP A 77  ? 0.41054 0.39521 0.40005 -0.04120 0.00323  -0.02117 72  TRP A CE3 
551  C  CZ2 . TRP A 77  ? 0.39092 0.38567 0.38176 -0.04052 -0.00739 -0.03380 72  TRP A CZ2 
552  C  CZ3 . TRP A 77  ? 0.40837 0.40649 0.40700 -0.04711 0.00179  -0.02568 72  TRP A CZ3 
553  C  CH2 . TRP A 77  ? 0.49002 0.49381 0.49050 -0.04707 -0.00392 -0.03219 72  TRP A CH2 
554  N  N   . GLY A 78  ? 0.32110 0.26234 0.29199 -0.01847 0.00729  -0.00661 73  GLY A N   
555  C  CA  . GLY A 78  ? 0.29721 0.23899 0.27133 -0.01622 0.00796  -0.00411 73  GLY A CA  
556  C  C   . GLY A 78  ? 0.34708 0.29815 0.32625 -0.01560 0.00962  -0.00399 73  GLY A C   
557  O  O   . GLY A 78  ? 0.31349 0.26510 0.29611 -0.01416 0.00975  -0.00321 73  GLY A O   
558  N  N   . PHE A 79  ? 0.27778 0.23616 0.25780 -0.01626 0.01040  -0.00534 74  PHE A N   
559  C  CA  . PHE A 79  ? 0.30430 0.27025 0.28836 -0.01450 0.01221  -0.00528 74  PHE A CA  
560  C  C   . PHE A 79  ? 0.38233 0.35513 0.36680 -0.01128 0.01245  -0.00631 74  PHE A C   
561  O  O   . PHE A 79  ? 0.34369 0.31690 0.32525 -0.01180 0.01042  -0.00805 74  PHE A O   
562  C  CB  . PHE A 79  ? 0.27634 0.24600 0.26005 -0.01876 0.01260  -0.00573 74  PHE A CB  
563  C  CG  . PHE A 79  ? 0.35141 0.32761 0.33540 -0.02319 0.01262  -0.00723 74  PHE A CG  
564  C  CD1 . PHE A 79  ? 0.33285 0.30344 0.31362 -0.02874 0.01167  -0.00725 74  PHE A CD1 
565  C  CD2 . PHE A 79  ? 0.36249 0.35055 0.35119 -0.02182 0.01369  -0.00884 74  PHE A CD2 
566  C  CE1 . PHE A 79  ? 0.29016 0.26738 0.27394 -0.03442 0.01205  -0.00926 74  PHE A CE1 
567  C  CE2 . PHE A 79  ? 0.33771 0.33492 0.33006 -0.02642 0.01349  -0.01099 74  PHE A CE2 
568  C  CZ  . PHE A 79  ? 0.33955 0.33161 0.33022 -0.03354 0.01279  -0.01140 74  PHE A CZ  
569  N  N   . PHE A 80  ? 0.30846 0.28600 0.29578 -0.00734 0.01444  -0.00563 75  PHE A N   
570  C  CA  . PHE A 80  ? 0.30883 0.29364 0.29559 -0.00254 0.01411  -0.00612 75  PHE A CA  
571  C  C   . PHE A 80  ? 0.28022 0.27011 0.27052 0.00069  0.01623  -0.00574 75  PHE A C   
572  O  O   . PHE A 80  ? 0.28322 0.26802 0.27554 0.00038  0.01858  -0.00497 75  PHE A O   
573  C  CB  . PHE A 80  ? 0.30676 0.28637 0.28887 0.00372  0.01529  -0.00397 75  PHE A CB  
574  C  CG  . PHE A 80  ? 0.30793 0.27898 0.29214 0.00578  0.01971  -0.00059 75  PHE A CG  
575  C  CD1 . PHE A 80  ? 0.32840 0.29339 0.31449 0.00271  0.02006  -0.00036 75  PHE A CD1 
576  C  CD2 . PHE A 80  ? 0.29146 0.26050 0.27670 0.01091  0.02361  0.00227  75  PHE A CD2 
577  C  CE1 . PHE A 80  ? 0.33014 0.29014 0.32157 0.00385  0.02392  0.00191  75  PHE A CE1 
578  C  CE2 . PHE A 80  ? 0.33886 0.30008 0.32849 0.01122  0.02826  0.00492  75  PHE A CE2 
579  C  CZ  . PHE A 80  ? 0.35741 0.31554 0.35129 0.00727  0.02826  0.00437  75  PHE A CZ  
580  N  N   . LEU A 81  ? 0.24946 0.24992 0.24086 0.00404  0.01479  -0.00714 76  LEU A N   
581  C  CA  . LEU A 81  ? 0.26498 0.26928 0.25844 0.01044  0.01687  -0.00637 76  LEU A CA  
582  C  C   . LEU A 81  ? 0.31965 0.31497 0.30825 0.01837  0.01922  -0.00233 76  LEU A C   
583  O  O   . LEU A 81  ? 0.31753 0.31088 0.30059 0.02105  0.01799  -0.00100 76  LEU A O   
584  C  CB  . LEU A 81  ? 0.28230 0.30284 0.27964 0.01274  0.01403  -0.00920 76  LEU A CB  
585  C  CG  . LEU A 81  ? 0.35259 0.38454 0.35681 0.00491  0.01343  -0.01280 76  LEU A CG  
586  C  CD1 . LEU A 81  ? 0.44783 0.49779 0.45829 0.00651  0.00946  -0.01631 76  LEU A CD1 
587  C  CD2 . LEU A 81  ? 0.47045 0.50277 0.47719 0.00538  0.01771  -0.01281 76  LEU A CD2 
588  N  N   . LEU A 82  ? 0.26029 0.24906 0.25010 0.02223  0.02317  -0.00041 77  LEU A N   
589  C  CA  . LEU A 82  ? 0.25931 0.23661 0.24496 0.02872  0.02732  0.00448  77  LEU A CA  
590  C  C   . LEU A 82  ? 0.28064 0.25829 0.26473 0.03783  0.02892  0.00609  77  LEU A C   
591  O  O   . LEU A 82  ? 0.30771 0.28613 0.29628 0.03764  0.02996  0.00368  77  LEU A O   
592  C  CB  . LEU A 82  ? 0.25188 0.21678 0.24165 0.02400  0.03146  0.00553  77  LEU A CB  
593  C  CG  . LEU A 82  ? 0.29110 0.24333 0.27861 0.02865  0.03757  0.01115  77  LEU A CG  
594  C  CD1 . LEU A 82  ? 0.34499 0.29717 0.32625 0.03040  0.03796  0.01413  77  LEU A CD1 
595  C  CD2 . LEU A 82  ? 0.31574 0.25821 0.31172 0.02297  0.04135  0.01056  77  LEU A CD2 
596  N  N   . THR A 83  ? 0.31176 0.28810 0.28808 0.04685  0.02913  0.01015  78  THR A N   
597  C  CA  . THR A 83  ? 0.28459 0.25942 0.25733 0.05784  0.03052  0.01290  78  THR A CA  
598  C  C   . THR A 83  ? 0.30776 0.26330 0.27339 0.06340  0.03765  0.02030  78  THR A C   
599  O  O   . THR A 83  ? 0.31575 0.26300 0.27920 0.05952  0.04108  0.02321  78  THR A O   
600  C  CB  . THR A 83  ? 0.30348 0.29389 0.27185 0.06573  0.02410  0.01180  78  THR A CB  
601  O  OG1 . THR A 83  ? 0.34751 0.33470 0.30555 0.06853  0.02303  0.01479  78  THR A OG1 
602  C  CG2 . THR A 83  ? 0.38233 0.39214 0.36020 0.05837  0.01814  0.00449  78  THR A CG2 
603  N  N   . ASN A 84  ? 0.33535 0.28340 0.29776 0.07280  0.04065  0.02355  79  ASN A N   
604  C  CA  . ASN A 84  ? 0.40584 0.33348 0.36014 0.07929  0.04853  0.03185  79  ASN A CA  
605  C  C   . ASN A 84  ? 0.35287 0.26632 0.31421 0.06877  0.05532  0.03278  79  ASN A C   
606  O  O   . ASN A 84  ? 0.39177 0.29355 0.34845 0.06919  0.06177  0.03914  79  ASN A O   
607  C  CB  . ASN A 84  ? 0.36307 0.29109 0.30277 0.08861  0.04791  0.03787  79  ASN A CB  
608  C  CG  . ASN A 84  ? 0.41272 0.34912 0.34407 0.10292  0.04271  0.03901  79  ASN A CG  
609  O  OD1 . ASN A 84  ? 0.40968 0.34638 0.34534 0.10772  0.04241  0.03762  79  ASN A OD1 
610  N  ND2 . ASN A 84  ? 0.44917 0.39288 0.36822 0.11066  0.03820  0.04102  79  ASN A ND2 
611  N  N   . HIS A 85  ? 0.34627 0.26194 0.31920 0.05956  0.05388  0.02612  80  HIS A N   
612  C  CA  . HIS A 85  ? 0.34020 0.24805 0.32284 0.04851  0.05732  0.02427  80  HIS A CA  
613  C  C   . HIS A 85  ? 0.35952 0.24802 0.34652 0.04799  0.06450  0.02588  80  HIS A C   
614  O  O   . HIS A 85  ? 0.43610 0.31845 0.43333 0.03861  0.06718  0.02363  80  HIS A O   
615  C  CB  . HIS A 85  ? 0.30461 0.22502 0.29529 0.03975  0.05089  0.01583  80  HIS A CB  
616  C  CG  . HIS A 85  ? 0.27599 0.20227 0.26692 0.04306  0.04778  0.01104  80  HIS A CG  
617  N  ND1 . HIS A 85  ? 0.34548 0.25971 0.33776 0.04618  0.05133  0.00982  80  HIS A ND1 
618  C  CD2 . HIS A 85  ? 0.26440 0.20737 0.25484 0.04401  0.04226  0.00711  80  HIS A CD2 
619  C  CE1 . HIS A 85  ? 0.36703 0.29092 0.35886 0.04989  0.04817  0.00528  80  HIS A CE1 
620  N  NE2 . HIS A 85  ? 0.31730 0.25952 0.30888 0.04820  0.04298  0.00379  80  HIS A NE2 
621  N  N   . GLY A 86  ? 0.32452 0.20325 0.30484 0.05783  0.06729  0.02914  81  GLY A N   
622  C  CA  . GLY A 86  ? 0.39830 0.25454 0.38105 0.05804  0.07528  0.03178  81  GLY A CA  
623  C  C   . GLY A 86  ? 0.36122 0.21245 0.35171 0.05426  0.07372  0.02334  81  GLY A C   
624  O  O   . GLY A 86  ? 0.40606 0.23671 0.39778 0.05546  0.07995  0.02458  81  GLY A O   
625  N  N   . VAL A 87  ? 0.38667 0.25437 0.38141 0.04979  0.06620  0.01479  82  VAL A N   
626  C  CA  . VAL A 87  ? 0.36405 0.22739 0.36325 0.04749  0.06468  0.00621  82  VAL A CA  
627  C  C   . VAL A 87  ? 0.47358 0.33774 0.46521 0.06009  0.06430  0.00611  82  VAL A C   
628  O  O   . VAL A 87  ? 0.40681 0.28924 0.39442 0.06588  0.05993  0.00682  82  VAL A O   
629  C  CB  . VAL A 87  ? 0.37644 0.25600 0.38103 0.03835  0.05773  -0.00208 82  VAL A CB  
630  C  CG1 . VAL A 87  ? 0.37595 0.25147 0.38170 0.03764  0.05607  -0.01133 82  VAL A CG1 
631  C  CG2 . VAL A 87  ? 0.40242 0.28167 0.41549 0.02740  0.05757  -0.00224 82  VAL A CG2 
632  N  N   . GLU A 88  ? 0.39468 0.23934 0.38554 0.06431  0.06883  0.00465  83  GLU A N   
633  C  CA  . GLU A 88  ? 0.40862 0.25223 0.39270 0.07796  0.06917  0.00453  83  GLU A CA  
634  C  C   . GLU A 88  ? 0.46049 0.32760 0.44605 0.07865  0.06296  -0.00312 83  GLU A C   
635  O  O   . GLU A 88  ? 0.41105 0.28301 0.40117 0.06945  0.06035  -0.01115 83  GLU A O   
636  C  CB  . GLU A 88  ? 0.48690 0.30392 0.47075 0.08057  0.07477  0.00175  83  GLU A CB  
637  C  CG  . GLU A 88  ? 0.60480 0.39781 0.58423 0.08465  0.08232  0.01166  83  GLU A CG  
638  C  CD  . GLU A 88  ? 0.68382 0.45800 0.66214 0.08667  0.08460  0.00882  83  GLU A CD  
639  O  OE1 . GLU A 88  ? 0.67962 0.45691 0.65558 0.09431  0.08205  0.00230  83  GLU A OE1 
640  O  OE2 . GLU A 88  ? 0.94913 0.70576 0.92925 0.08072  0.08942  0.01301  83  GLU A OE2 
641  N  N   . ALA A 89  ? 0.42953 0.31200 0.41130 0.08976  0.06070  -0.00048 84  ALA A N   
642  C  CA  . ALA A 89  ? 0.41076 0.31714 0.39581 0.09023  0.05632  -0.00702 84  ALA A CA  
643  C  C   . ALA A 89  ? 0.38727 0.28668 0.37282 0.09128  0.05838  -0.01566 84  ALA A C   
644  O  O   . ALA A 89  ? 0.41562 0.32849 0.40365 0.08508  0.05615  -0.02246 84  ALA A O   
645  C  CB  . ALA A 89  ? 0.41215 0.33630 0.39575 0.10287  0.05379  -0.00336 84  ALA A CB  
646  N  N   . SER A 90  ? 0.39555 0.27223 0.37737 0.09923  0.06303  -0.01554 85  SER A N   
647  C  CA  . SER A 90  ? 0.40995 0.27820 0.39077 0.10121  0.06493  -0.02494 85  SER A CA  
648  C  C   . SER A 90  ? 0.41573 0.27564 0.39885 0.08680  0.06365  -0.03243 85  SER A C   
649  O  O   . SER A 90  ? 0.41656 0.27925 0.39789 0.08575  0.06285  -0.04176 85  SER A O   
650  C  CB  . SER A 90  ? 0.43998 0.28252 0.41575 0.11332  0.07029  -0.02330 85  SER A CB  
651  O  OG  . SER A 90  ? 0.51117 0.32805 0.48648 0.10791  0.07389  -0.01810 85  SER A OG  
652  N  N   . LEU A 91  ? 0.40271 0.25330 0.38955 0.07642  0.06338  -0.02881 86  LEU A N   
653  C  CA  . LEU A 91  ? 0.44457 0.29161 0.43551 0.06293  0.06054  -0.03613 86  LEU A CA  
654  C  C   . LEU A 91  ? 0.39066 0.26245 0.38155 0.05696  0.05506  -0.03916 86  LEU A C   
655  O  O   . LEU A 91  ? 0.42269 0.29593 0.41203 0.05142  0.05214  -0.04778 86  LEU A O   
656  C  CB  . LEU A 91  ? 0.46450 0.29871 0.46203 0.05390  0.06218  -0.03106 86  LEU A CB  
657  C  CG  . LEU A 91  ? 0.46891 0.30142 0.47379 0.03998  0.05839  -0.03837 86  LEU A CG  
658  C  CD1 . LEU A 91  ? 0.49978 0.31679 0.50387 0.03900  0.05793  -0.04998 86  LEU A CD1 
659  C  CD2 . LEU A 91  ? 0.47657 0.29983 0.49069 0.03188  0.06135  -0.03229 86  LEU A CD2 
660  N  N   . MET A 92  ? 0.33277 0.22311 0.32424 0.05835  0.05359  -0.03231 87  MET A N   
661  C  CA  . MET A 92  ? 0.37080 0.28299 0.36200 0.05306  0.04955  -0.03432 87  MET A CA  
662  C  C   . MET A 92  ? 0.36599 0.28773 0.35295 0.05875  0.05059  -0.04072 87  MET A C   
663  O  O   . MET A 92  ? 0.38239 0.31123 0.36613 0.05318  0.04868  -0.04608 87  MET A O   
664  C  CB  . MET A 92  ? 0.37900 0.30729 0.37234 0.05378  0.04802  -0.02652 87  MET A CB  
665  C  CG  . MET A 92  ? 0.36276 0.28179 0.35842 0.04993  0.04819  -0.01987 87  MET A CG  
666  S  SD  . MET A 92  ? 0.36262 0.29945 0.35818 0.05172  0.04560  -0.01243 87  MET A SD  
667  C  CE  . MET A 92  ? 0.40622 0.35754 0.40392 0.03972  0.04097  -0.01578 87  MET A CE  
668  N  N   . ASP A 93  ? 0.33361 0.25587 0.31979 0.07082  0.05401  -0.03989 88  ASP A N   
669  C  CA  . ASP A 93  ? 0.35243 0.28371 0.33544 0.07761  0.05639  -0.04632 88  ASP A CA  
670  C  C   . ASP A 93  ? 0.43680 0.35267 0.41335 0.07464  0.05677  -0.05587 88  ASP A C   
671  O  O   . ASP A 93  ? 0.43299 0.35889 0.40444 0.07350  0.05708  -0.06173 88  ASP A O   
672  C  CB  . ASP A 93  ? 0.42603 0.35674 0.40985 0.09273  0.05993  -0.04440 88  ASP A CB  
673  C  CG  . ASP A 93  ? 0.42280 0.37302 0.41253 0.09734  0.05823  -0.03673 88  ASP A CG  
674  O  OD1 . ASP A 93  ? 0.41990 0.38907 0.41362 0.08921  0.05530  -0.03501 88  ASP A OD1 
675  O  OD2 . ASP A 93  ? 0.46984 0.41553 0.45958 0.10954  0.05948  -0.03272 88  ASP A OD2 
676  N  N   . SER A 94  ? 0.42297 0.31411 0.39930 0.07322  0.05696  -0.05778 89  SER A N   
677  C  CA  . SER A 94  ? 0.50289 0.37801 0.47350 0.07136  0.05657  -0.06865 89  SER A CA  
678  C  C   . SER A 94  ? 0.44545 0.32700 0.41360 0.05964  0.05113  -0.07344 89  SER A C   
679  O  O   . SER A 94  ? 0.46078 0.34341 0.42015 0.06025  0.05022  -0.08229 89  SER A O   
680  C  CB  . SER A 94  ? 0.50731 0.35388 0.48069 0.07116  0.05825  -0.06971 89  SER A CB  
681  O  OG  . SER A 94  ? 0.57303 0.40939 0.54473 0.08445  0.06362  -0.06694 89  SER A OG  
682  N  N   . VAL A 95  ? 0.42003 0.30578 0.39452 0.05006  0.04748  -0.06774 90  VAL A N   
683  C  CA  . VAL A 95  ? 0.42402 0.31481 0.39598 0.04035  0.04164  -0.07216 90  VAL A CA  
684  C  C   . VAL A 95  ? 0.50050 0.41109 0.46412 0.04156  0.04162  -0.07204 90  VAL A C   
685  O  O   . VAL A 95  ? 0.45077 0.36267 0.40531 0.03877  0.03849  -0.07863 90  VAL A O   
686  C  CB  . VAL A 95  ? 0.44690 0.33805 0.42835 0.03096  0.03821  -0.06612 90  VAL A CB  
687  C  CG1 . VAL A 95  ? 0.36309 0.27200 0.34684 0.03053  0.03875  -0.05599 90  VAL A CG1 
688  C  CG2 . VAL A 95  ? 0.41627 0.30646 0.39680 0.02226  0.03131  -0.07313 90  VAL A CG2 
689  N  N   . MET A 96  ? 0.37581 0.30184 0.34201 0.04599  0.04533  -0.06491 91  MET A N   
690  C  CA  . MET A 96  ? 0.41573 0.36049 0.37607 0.04621  0.04704  -0.06444 91  MET A CA  
691  C  C   . MET A 96  ? 0.42377 0.36882 0.37514 0.05457  0.05164  -0.07199 91  MET A C   
692  O  O   . MET A 96  ? 0.50420 0.45604 0.44526 0.05319  0.05238  -0.07544 91  MET A O   
693  C  CB  . MET A 96  ? 0.37406 0.33650 0.34270 0.04728  0.04922  -0.05579 91  MET A CB  
694  C  CG  . MET A 96  ? 0.37897 0.34244 0.35380 0.03930  0.04497  -0.04895 91  MET A CG  
695  S  SD  . MET A 96  ? 0.45859 0.42354 0.42684 0.02850  0.04022  -0.04954 91  MET A SD  
696  C  CE  . MET A 96  ? 0.43379 0.42060 0.40185 0.02689  0.04382  -0.04467 91  MET A CE  
697  N  N   A ASN A 97  ? 0.41201 0.34882 0.36575 0.06416  0.05528  -0.07438 92  ASN A N   
698  N  N   B ASN A 97  ? 0.41182 0.34871 0.36568 0.06416  0.05529  -0.07428 92  ASN A N   
699  C  CA  A ASN A 97  ? 0.47269 0.40962 0.41791 0.07357  0.06030  -0.08206 92  ASN A CA  
700  C  CA  B ASN A 97  ? 0.47315 0.40951 0.41862 0.07373  0.06028  -0.08204 92  ASN A CA  
701  C  C   A ASN A 97  ? 0.51695 0.43693 0.44964 0.07162  0.05732  -0.09297 92  ASN A C   
702  C  C   B ASN A 97  ? 0.51624 0.43657 0.44901 0.07136  0.05722  -0.09279 92  ASN A C   
703  O  O   A ASN A 97  ? 0.52674 0.45077 0.44733 0.07613  0.06036  -0.09956 92  ASN A O   
704  O  O   B ASN A 97  ? 0.52778 0.45296 0.44838 0.07530  0.06009  -0.09905 92  ASN A O   
705  C  CB  A ASN A 97  ? 0.52335 0.45436 0.47409 0.08575  0.06462  -0.08171 92  ASN A CB  
706  C  CB  B ASN A 97  ? 0.52160 0.44972 0.47237 0.08555  0.06423  -0.08196 92  ASN A CB  
707  C  CG  A ASN A 97  ? 0.58365 0.53711 0.54484 0.09079  0.06755  -0.07343 92  ASN A CG  
708  C  CG  B ASN A 97  ? 0.56255 0.48781 0.50468 0.09685  0.06967  -0.09088 92  ASN A CG  
709  O  OD1 A ASN A 97  ? 0.61475 0.56553 0.58398 0.09376  0.06635  -0.06706 92  ASN A OD1 
710  O  OD1 B ASN A 97  ? 0.47801 0.42339 0.42047 0.10311  0.07502  -0.09035 92  ASN A OD1 
711  N  ND2 A ASN A 97  ? 0.55806 0.53424 0.51912 0.09170  0.07148  -0.07362 92  ASN A ND2 
712  N  ND2 B ASN A 97  ? 0.52070 0.42096 0.45592 0.09938  0.06872  -0.09961 92  ASN A ND2 
713  N  N   . LEU A 98  ? 0.47180 0.37349 0.40733 0.06510  0.05154  -0.09554 93  LEU A N   
714  C  CA  . LEU A 98  ? 0.55598 0.44378 0.48122 0.06189  0.04667  -0.10704 93  LEU A CA  
715  C  C   . LEU A 98  ? 0.52511 0.42531 0.44112 0.05513  0.04218  -0.10711 93  LEU A C   
716  O  O   . LEU A 98  ? 0.58438 0.48039 0.48570 0.05630  0.03962  -0.11661 93  LEU A O   
717  C  CB  . LEU A 98  ? 0.55825 0.42535 0.49276 0.05553  0.04189  -0.10991 93  LEU A CB  
718  C  CG  . LEU A 98  ? 0.54390 0.39291 0.48505 0.06237  0.04691  -0.10975 93  LEU A CG  
719  C  CD1 . LEU A 98  ? 0.64954 0.47859 0.60129 0.05374  0.04347  -0.11127 93  LEU A CD1 
720  C  CD2 . LEU A 98  ? 0.59188 0.43072 0.52188 0.07354  0.05104  -0.11992 93  LEU A CD2 
721  N  N   . SER A 99  ? 0.45019 0.36442 0.37302 0.04890  0.04114  -0.09668 94  SER A N   
722  C  CA  . SER A 99  ? 0.51335 0.43961 0.42634 0.04416  0.03872  -0.09445 94  SER A CA  
723  C  C   . SER A 99  ? 0.52179 0.45936 0.42151 0.05097  0.04600  -0.09566 94  SER A C   
724  O  O   . SER A 99  ? 0.48129 0.41770 0.36380 0.05187  0.04463  -0.10135 94  SER A O   
725  C  CB  . SER A 99  ? 0.41230 0.34976 0.33612 0.03718  0.03761  -0.08283 94  SER A CB  
726  O  OG  . SER A 99  ? 0.62624 0.57518 0.54025 0.03402  0.03774  -0.07895 94  SER A OG  
727  N  N   . ARG A 100 ? 0.45866 0.40825 0.36615 0.05633  0.05396  -0.09041 95  ARG A N   
728  C  CA  . ARG A 100 ? 0.49294 0.45540 0.39115 0.06302  0.06257  -0.09162 95  ARG A CA  
729  C  C   . ARG A 100 ? 0.57473 0.52492 0.45702 0.07104  0.06379  -0.10383 95  ARG A C   
730  O  O   . ARG A 100 ? 0.51812 0.47373 0.38383 0.07393  0.06790  -0.10691 95  ARG A O   
731  C  CB  . ARG A 100 ? 0.54635 0.52388 0.45931 0.06882  0.06988  -0.08620 95  ARG A CB  
732  C  CG  . ARG A 100 ? 0.57538 0.56835 0.50224 0.06147  0.06936  -0.07532 95  ARG A CG  
733  C  CD  . ARG A 100 ? 0.59940 0.61050 0.54077 0.06792  0.07558  -0.07159 95  ARG A CD  
734  N  NE  . ARG A 100 ? 0.57550 0.59879 0.53070 0.06086  0.07306  -0.06284 95  ARG A NE  
735  C  CZ  . ARG A 100 ? 0.56212 0.60187 0.52024 0.05365  0.07586  -0.05766 95  ARG A CZ  
736  N  NH1 . ARG A 100 ? 0.45040 0.49720 0.39853 0.05258  0.08239  -0.05888 95  ARG A NH1 
737  N  NH2 . ARG A 100 ? 0.48567 0.53379 0.45610 0.04736  0.07248  -0.05115 95  ARG A NH2 
738  N  N   . GLU A 101 ? 0.47598 0.40820 0.36196 0.07484  0.06075  -0.11100 96  GLU A N   
739  C  CA  . GLU A 101 ? 0.50324 0.42145 0.37421 0.08267  0.06151  -0.12412 96  GLU A CA  
740  C  C   . GLU A 101 ? 0.48390 0.39460 0.33713 0.07778  0.05394  -0.13165 96  GLU A C   
741  O  O   . GLU A 101 ? 0.56404 0.47250 0.39779 0.08431  0.05628  -0.14034 96  GLU A O   
742  C  CB  . GLU A 101 ? 0.52715 0.42457 0.40693 0.08647  0.05972  -0.12983 96  GLU A CB  
743  C  CG  . GLU A 101 ? 0.82683 0.71087 0.69515 0.09532  0.06239  -0.14213 96  GLU A CG  
744  C  CD  . GLU A 101 ? 0.92073 0.78534 0.80108 0.09833  0.06254  -0.14458 96  GLU A CD  
745  O  OE1 . GLU A 101 ? 0.73118 0.59469 0.62510 0.09919  0.06368  -0.13640 96  GLU A OE1 
746  O  OE2 . GLU A 101 ? 1.03336 0.88304 0.90870 0.09988  0.06187  -0.15426 96  GLU A OE2 
747  N  N   . PHE A 102 ? 0.52731 0.43500 0.38627 0.06729  0.04471  -0.12863 97  PHE A N   
748  C  CA  . PHE A 102 ? 0.59200 0.49486 0.43489 0.06351  0.03602  -0.13554 97  PHE A CA  
749  C  C   . PHE A 102 ? 0.56041 0.47756 0.38483 0.06546  0.04040  -0.13070 97  PHE A C   
750  O  O   . PHE A 102 ? 0.57737 0.49070 0.37920 0.07064  0.03954  -0.13914 97  PHE A O   
751  C  CB  . PHE A 102 ? 0.56623 0.46607 0.42165 0.05266  0.02570  -0.13245 97  PHE A CB  
752  C  CG  . PHE A 102 ? 0.57253 0.47267 0.41236 0.04956  0.01625  -0.13711 97  PHE A CG  
753  C  CD1 . PHE A 102 ? 0.68012 0.56785 0.50773 0.05171  0.00845  -0.15225 97  PHE A CD1 
754  C  CD2 . PHE A 102 ? 0.53813 0.45037 0.37427 0.04538  0.01487  -0.12682 97  PHE A CD2 
755  C  CE1 . PHE A 102 ? 0.66424 0.55346 0.47619 0.05036  -0.00154 -0.15704 97  PHE A CE1 
756  C  CE2 . PHE A 102 ? 0.57796 0.48993 0.39793 0.04444  0.00581  -0.13052 97  PHE A CE2 
757  C  CZ  . PHE A 102 ? 0.59139 0.49285 0.39913 0.04728  -0.00283 -0.14561 97  PHE A CZ  
758  N  N   . PHE A 103 ? 0.51066 0.44325 0.34342 0.06123  0.04528  -0.11718 98  PHE A N   
759  C  CA  . PHE A 103 ? 0.47414 0.41837 0.29025 0.06161  0.05050  -0.11113 98  PHE A CA  
760  C  C   . PHE A 103 ? 0.56638 0.51658 0.36891 0.07148  0.06224  -0.11469 98  PHE A C   
761  O  O   . PHE A 103 ? 0.55811 0.51227 0.33915 0.07398  0.06638  -0.11381 98  PHE A O   
762  C  CB  . PHE A 103 ? 0.43990 0.39788 0.27025 0.05417  0.05389  -0.09666 98  PHE A CB  
763  C  CG  . PHE A 103 ? 0.46069 0.41389 0.29979 0.04534  0.04327  -0.09259 98  PHE A CG  
764  C  CD1 . PHE A 103 ? 0.44856 0.39682 0.27193 0.04302  0.03541  -0.09356 98  PHE A CD1 
765  C  CD2 . PHE A 103 ? 0.38466 0.33863 0.24682 0.04053  0.04118  -0.08787 98  PHE A CD2 
766  C  CE1 . PHE A 103 ? 0.44713 0.39256 0.27992 0.03597  0.02584  -0.09014 98  PHE A CE1 
767  C  CE2 . PHE A 103 ? 0.44673 0.39714 0.31708 0.03310  0.03250  -0.08431 98  PHE A CE2 
768  C  CZ  . PHE A 103 ? 0.43682 0.38352 0.29359 0.03080  0.02488  -0.08565 98  PHE A CZ  
769  N  N   . ASN A 104 ? 0.53724 0.48776 0.35093 0.07805  0.06817  -0.11848 99  ASN A N   
770  C  CA  . ASN A 104 ? 0.56823 0.52533 0.37347 0.08726  0.07909  -0.12201 99  ASN A CA  
771  C  C   . ASN A 104 ? 0.64758 0.59031 0.43685 0.09069  0.07481  -0.13365 99  ASN A C   
772  O  O   . ASN A 104 ? 0.59630 0.54374 0.37903 0.09674  0.08302  -0.13616 99  ASN A O   
773  C  CB  . ASN A 104 ? 0.63785 0.60161 0.46410 0.09290  0.08577  -0.12065 99  ASN A CB  
774  C  CG  . ASN A 104 ? 0.62850 0.61393 0.47114 0.08978  0.09270  -0.10848 99  ASN A CG  
775  O  OD1 . ASN A 104 ? 0.92159 0.91029 0.78552 0.08832  0.09082  -0.10395 99  ASN A OD1 
776  N  ND2 . ASN A 104 ? 0.85813 0.85839 0.69246 0.08721  0.10040  -0.10225 99  ASN A ND2 
777  N  N   . GLN A 105 ? 0.54614 0.47259 0.33006 0.08676  0.06223  -0.14120 100 GLN A N   
778  C  CA  . GLN A 105 ? 0.61184 0.52546 0.38166 0.08927  0.05742  -0.15292 100 GLN A CA  
779  C  C   . GLN A 105 ? 0.64923 0.56917 0.39478 0.09026  0.05886  -0.15149 100 GLN A C   
780  O  O   . GLN A 105 ? 0.62390 0.55403 0.36363 0.08690  0.06048  -0.14165 100 GLN A O   
781  C  CB  . GLN A 105 ? 0.66432 0.56102 0.43920 0.08323  0.04326  -0.16131 100 GLN A CB  
782  C  CG  . GLN A 105 ? 0.74971 0.63635 0.54706 0.08240  0.04287  -0.16298 100 GLN A CG  
783  C  CD  . GLN A 105 ? 0.96937 0.83857 0.77354 0.07531  0.03067  -0.17190 100 GLN A CD  
784  O  OE1 . GLN A 105 ? 0.89962 0.76870 0.69748 0.06928  0.02045  -0.17431 100 GLN A OE1 
785  N  NE2 . GLN A 105 ? 1.04040 0.89514 0.85856 0.07584  0.03197  -0.17631 100 GLN A NE2 
786  N  N   . PRO A 106 ? 0.66260 0.57563 0.39292 0.09515  0.05885  -0.16080 101 PRO A N   
787  C  CA  . PRO A 106 ? 0.65041 0.56763 0.35552 0.09692  0.05968  -0.15968 101 PRO A CA  
788  C  C   . PRO A 106 ? 0.66579 0.57989 0.36172 0.09095  0.04689  -0.15796 101 PRO A C   
789  O  O   . PRO A 106 ? 0.70414 0.60894 0.40994 0.08599  0.03454  -0.16368 101 PRO A O   
790  C  CB  . PRO A 106 ? 0.64672 0.55294 0.33955 0.10298  0.05862  -0.17299 101 PRO A CB  
791  C  CG  . PRO A 106 ? 0.71726 0.61915 0.42917 0.10638  0.06418  -0.17714 101 PRO A CG  
792  C  CD  . PRO A 106 ? 0.69778 0.59866 0.43244 0.10016  0.05958  -0.17209 101 PRO A CD  
793  N  N   . ILE A 107 ? 0.69526 0.61737 0.37283 0.09150  0.05029  -0.14959 102 ILE A N   
794  C  CA  . ILE A 107 ? 0.65724 0.57775 0.32566 0.08708  0.03891  -0.14575 102 ILE A CA  
795  C  C   . ILE A 107 ? 0.71604 0.62506 0.37573 0.08741  0.02357  -0.15882 102 ILE A C   
796  O  O   . ILE A 107 ? 0.78441 0.69039 0.44960 0.08242  0.01024  -0.16021 102 ILE A O   
797  C  CB  . ILE A 107 ? 0.67428 0.60335 0.32289 0.08852  0.04694  -0.13347 102 ILE A CB  
798  C  CG1 . ILE A 107 ? 0.64315 0.57003 0.28351 0.08482  0.03532  -0.12786 102 ILE A CG1 
799  C  CG2 . ILE A 107 ? 0.73384 0.66189 0.35926 0.09576  0.05251  -0.13795 102 ILE A CG2 
800  C  CD1 . ILE A 107 ? 0.64040 0.56901 0.30165 0.07796  0.03114  -0.12211 102 ILE A CD1 
801  N  N   . GLU A 108 ? 0.75547 0.65876 0.40301 0.09312  0.02515  -0.16903 103 GLU A N   
802  C  CA  . GLU A 108 ? 0.78052 0.67309 0.42093 0.09310  0.01089  -0.18279 103 GLU A CA  
803  C  C   . GLU A 108 ? 0.80485 0.68954 0.47044 0.08578  0.00048  -0.19005 103 GLU A C   
804  O  O   . GLU A 108 ? 0.88011 0.76112 0.54738 0.08153  -0.01416 -0.19621 103 GLU A O   
805  C  CB  . GLU A 108 ? 0.81134 0.69774 0.43747 0.10036  0.01618  -0.19327 103 GLU A CB  
806  C  CG  . GLU A 108 ? 0.90361 0.79656 0.50237 0.10773  0.02534  -0.18785 103 GLU A CG  
807  C  CD  . GLU A 108 ? 0.92506 0.82857 0.52818 0.11058  0.04426  -0.17748 103 GLU A CD  
808  O  OE1 . GLU A 108 ? 0.74540 0.65185 0.37238 0.10767  0.04962  -0.17448 103 GLU A OE1 
809  O  OE2 . GLU A 108 ? 1.02571 0.93525 0.60893 0.11579  0.05392  -0.17227 103 GLU A OE2 
810  N  N   . ARG A 109 ? 0.77687 0.65959 0.46324 0.08430  0.00815  -0.18889 104 ARG A N   
811  C  CA  . ARG A 109 ? 0.74689 0.62053 0.45774 0.07729  0.00053  -0.19457 104 ARG A CA  
812  C  C   . ARG A 109 ? 0.79247 0.67249 0.51714 0.07016  -0.00598 -0.18606 104 ARG A C   
813  O  O   . ARG A 109 ? 0.74850 0.62387 0.48596 0.06329  -0.01812 -0.19138 104 ARG A O   
814  C  CB  . ARG A 109 ? 0.77372 0.64222 0.50020 0.07970  0.01159  -0.19499 104 ARG A CB  
815  C  CG  . ARG A 109 ? 1.02921 0.88297 0.77697 0.07384  0.00569  -0.20286 104 ARG A CG  
816  C  CD  . ARG A 109 ? 1.11185 0.96098 0.87392 0.07784  0.01738  -0.20054 104 ARG A CD  
817  N  NE  . ARG A 109 ? 1.29201 1.12373 1.07223 0.07266  0.01340  -0.20733 104 ARG A NE  
818  C  CZ  . ARG A 109 ? 1.16920 0.98496 0.94689 0.07430  0.01349  -0.21858 104 ARG A CZ  
819  N  NH1 . ARG A 109 ? 1.10120 0.91671 0.85917 0.08161  0.01677  -0.22536 104 ARG A NH1 
820  N  NH2 . ARG A 109 ? 1.15868 0.95738 0.95352 0.06832  0.01087  -0.22286 104 ARG A NH2 
821  N  N   . LYS A 110 ? 0.67313 0.56430 0.39644 0.07137  0.00238  -0.17289 105 LYS A N   
822  C  CA  . LYS A 110 ? 0.64513 0.54172 0.38041 0.06526  -0.00295 -0.16466 105 LYS A CA  
823  C  C   . LYS A 110 ? 0.62765 0.52611 0.35272 0.06290  -0.01661 -0.16571 105 LYS A C   
824  O  O   . LYS A 110 ? 0.67968 0.57843 0.42021 0.05656  -0.02680 -0.16601 105 LYS A O   
825  C  CB  . LYS A 110 ? 0.66275 0.57043 0.39580 0.06718  0.00949  -0.15053 105 LYS A CB  
826  C  CG  . LYS A 110 ? 0.58611 0.49540 0.33483 0.06928  0.02153  -0.14829 105 LYS A CG  
827  C  CD  . LYS A 110 ? 0.55629 0.47843 0.30789 0.06892  0.03178  -0.13428 105 LYS A CD  
828  C  CE  . LYS A 110 ? 0.55502 0.48655 0.28604 0.07256  0.04156  -0.12699 105 LYS A CE  
829  N  NZ  . LYS A 110 ? 0.63412 0.57825 0.37114 0.07024  0.05233  -0.11311 105 LYS A NZ  
830  N  N   . GLN A 111 ? 0.71416 0.61438 0.41399 0.06845  -0.01707 -0.16628 106 GLN A N   
831  C  CA  . GLN A 111 ? 0.76696 0.67011 0.45510 0.06821  -0.02960 -0.16550 106 GLN A CA  
832  C  C   . GLN A 111 ? 0.76011 0.65855 0.45954 0.06391  -0.04549 -0.17864 106 GLN A C   
833  O  O   . GLN A 111 ? 0.69639 0.59933 0.39297 0.06304  -0.05766 -0.17834 106 GLN A O   
834  C  CB  . GLN A 111 ? 0.81973 0.72483 0.47683 0.07610  -0.02541 -0.16243 106 GLN A CB  
835  C  CG  . GLN A 111 ? 0.72252 0.63432 0.36853 0.07855  -0.01100 -0.14669 106 GLN A CG  
836  C  CD  . GLN A 111 ? 0.92539 0.84142 0.57009 0.07599  -0.01565 -0.13474 106 GLN A CD  
837  O  OE1 . GLN A 111 ? 0.86946 0.78634 0.53409 0.07024  -0.02226 -0.13382 106 GLN A OE1 
838  N  NE2 . GLN A 111 ? 0.89206 0.80981 0.51296 0.08051  -0.01164 -0.12518 106 GLN A NE2 
839  N  N   . LYS A 112 ? 0.71187 0.60151 0.42493 0.06119  -0.04540 -0.18974 107 LYS A N   
840  C  CA  . LYS A 112 ? 0.68357 0.56897 0.41298 0.05462  -0.05918 -0.20122 107 LYS A CA  
841  C  C   . LYS A 112 ? 0.67985 0.57037 0.43529 0.04635  -0.06538 -0.19644 107 LYS A C   
842  O  O   . LYS A 112 ? 0.70133 0.59275 0.47174 0.04035  -0.07758 -0.20378 107 LYS A O   
843  C  CB  . LYS A 112 ? 0.71583 0.58802 0.45494 0.05273  -0.05553 -0.21248 107 LYS A CB  
844  C  CG  . LYS A 112 ? 0.77203 0.63848 0.48684 0.06117  -0.04919 -0.21869 107 LYS A CG  
845  C  CD  . LYS A 112 ? 1.09209 0.94351 0.81703 0.05960  -0.04528 -0.22954 107 LYS A CD  
846  C  CE  . LYS A 112 ? 0.96846 0.81603 0.71327 0.05772  -0.03387 -0.22257 107 LYS A CE  
847  N  NZ  . LYS A 112 ? 1.21073 1.04248 0.96012 0.05926  -0.02726 -0.23121 107 LYS A NZ  
848  N  N   . PHE A 113 ? 0.63355 0.52824 0.39537 0.04586  -0.05700 -0.18458 108 PHE A N   
849  C  CA  . PHE A 113 ? 0.60261 0.50240 0.38767 0.03883  -0.06150 -0.17908 108 PHE A CA  
850  C  C   . PHE A 113 ? 0.61320 0.52308 0.38669 0.04157  -0.06403 -0.16782 108 PHE A C   
851  O  O   . PHE A 113 ? 0.58890 0.50322 0.37839 0.03718  -0.06535 -0.16123 108 PHE A O   
852  C  CB  . PHE A 113 ? 0.61263 0.50759 0.41591 0.03591  -0.05050 -0.17486 108 PHE A CB  
853  C  CG  . PHE A 113 ? 0.65659 0.53897 0.46889 0.03468  -0.04615 -0.18400 108 PHE A CG  
854  C  CD1 . PHE A 113 ? 0.71564 0.59132 0.54969 0.02652  -0.05320 -0.19197 108 PHE A CD1 
855  C  CD2 . PHE A 113 ? 0.60254 0.47970 0.40191 0.04174  -0.03435 -0.18411 108 PHE A CD2 
856  C  CE1 . PHE A 113 ? 0.68557 0.54666 0.52610 0.02539  -0.04858 -0.19956 108 PHE A CE1 
857  C  CE2 . PHE A 113 ? 0.68640 0.55029 0.49297 0.04163  -0.03030 -0.19221 108 PHE A CE2 
858  C  CZ  . PHE A 113 ? 0.63508 0.48947 0.46117 0.03341  -0.03742 -0.19979 108 PHE A CZ  
859  N  N   . SER A 114 ? 0.65162 0.56393 0.39709 0.04894  -0.06426 -0.16510 109 SER A N   
860  C  CA  . SER A 114 ? 0.64784 0.56675 0.37902 0.05234  -0.06556 -0.15314 109 SER A CA  
861  C  C   . SER A 114 ? 0.56743 0.49273 0.31519 0.04817  -0.07965 -0.15342 109 SER A C   
862  O  O   . SER A 114 ? 0.66570 0.59280 0.42581 0.04520  -0.09128 -0.16413 109 SER A O   
863  C  CB  . SER A 114 ? 0.67863 0.59736 0.37797 0.06081  -0.06536 -0.15192 109 SER A CB  
864  O  OG  . SER A 114 ? 0.71848 0.64139 0.40397 0.06424  -0.06774 -0.14016 109 SER A OG  
865  N  N   . ASN A 115 ? 0.56241 0.49156 0.31126 0.04790  -0.07819 -0.14159 110 ASN A N   
866  C  CA  . ASN A 115 ? 0.58489 0.52127 0.34778 0.04563  -0.09084 -0.14039 110 ASN A CA  
867  C  C   . ASN A 115 ? 0.71225 0.65211 0.45267 0.05346  -0.09930 -0.13691 110 ASN A C   
868  O  O   . ASN A 115 ? 0.68755 0.63415 0.43650 0.05385  -0.10961 -0.13448 110 ASN A O   
869  C  CB  . ASN A 115 ? 0.56090 0.49850 0.33600 0.04209  -0.08610 -0.12989 110 ASN A CB  
870  C  CG  . ASN A 115 ? 0.59824 0.53297 0.34911 0.04710  -0.07614 -0.11454 110 ASN A CG  
871  O  OD1 . ASN A 115 ? 0.62645 0.55690 0.35222 0.05251  -0.06827 -0.11233 110 ASN A OD1 
872  N  ND2 . ASN A 115 ? 0.57676 0.51466 0.34004 0.04370  -0.07406 -0.10179 110 ASN A ND2 
873  N  N   . LEU A 116 ? 0.64857 0.58404 0.36084 0.06032  -0.09484 -0.13646 111 LEU A N   
874  C  CA  . LEU A 116 ? 0.67351 0.61073 0.36261 0.06869  -0.10284 -0.13424 111 LEU A CA  
875  C  C   . LEU A 116 ? 0.75142 0.69053 0.44228 0.06943  -0.11380 -0.15014 111 LEU A C   
876  O  O   . LEU A 116 ? 0.75631 0.68988 0.43137 0.07227  -0.10881 -0.15595 111 LEU A O   
877  C  CB  . LEU A 116 ? 0.81683 0.74767 0.47374 0.07549  -0.09001 -0.12267 111 LEU A CB  
878  C  CG  . LEU A 116 ? 0.75709 0.68542 0.41072 0.07449  -0.07946 -0.10596 111 LEU A CG  
879  C  CD1 . LEU A 116 ? 0.92069 0.84315 0.54796 0.07848  -0.06323 -0.09570 111 LEU A CD1 
880  C  CD2 . LEU A 116 ? 0.78141 0.71204 0.43393 0.07784  -0.08980 -0.09844 111 LEU A CD2 
881  N  N   . ILE A 117 ? 0.77713 0.72458 0.48857 0.06663  -0.12860 -0.15747 112 ILE A N   
882  C  CA  . ILE A 117 ? 0.83301 0.78313 0.55009 0.06581  -0.13991 -0.17327 112 ILE A CA  
883  C  C   . ILE A 117 ? 0.91228 0.86056 0.59566 0.07660  -0.14410 -0.17421 112 ILE A C   
884  O  O   . ILE A 117 ? 0.93255 0.88285 0.59780 0.08450  -0.14672 -0.16420 112 ILE A O   
885  C  CB  . ILE A 117 ? 0.82152 0.78355 0.56914 0.06058  -0.15416 -0.17938 112 ILE A CB  
886  C  CG1 . ILE A 117 ? 0.82088 0.78455 0.59980 0.05073  -0.14839 -0.17563 112 ILE A CG1 
887  C  CG2 . ILE A 117 ? 0.79906 0.76351 0.55704 0.05729  -0.16459 -0.19657 112 ILE A CG2 
888  C  CD1 . ILE A 117 ? 1.06372 1.04077 0.87324 0.04607  -0.15996 -0.17849 112 ILE A CD1 
889  N  N   . ASP A 118 ? 0.95945 0.90254 0.63332 0.07741  -0.14427 -0.18602 113 ASP A N   
890  C  CA  . ASP A 118 ? 0.94617 0.88615 0.58662 0.08766  -0.14699 -0.18851 113 ASP A CA  
891  C  C   . ASP A 118 ? 1.00430 0.93796 0.61418 0.09525  -0.13298 -0.17319 113 ASP A C   
892  O  O   . ASP A 118 ? 1.04529 0.97658 0.62523 0.10485  -0.13441 -0.17149 113 ASP A O   
893  C  CB  . ASP A 118 ? 1.05143 1.00074 0.68939 0.09317  -0.16515 -0.19308 113 ASP A CB  
894  C  CG  . ASP A 118 ? 1.07137 1.02912 0.74223 0.08481  -0.17875 -0.20801 113 ASP A CG  
895  O  OD1 . ASP A 118 ? 0.98100 0.93360 0.66279 0.07810  -0.17700 -0.22004 113 ASP A OD1 
896  O  OD2 . ASP A 118 ? 1.09687 1.06620 0.78336 0.08490  -0.19056 -0.20746 113 ASP A OD2 
897  N  N   . GLY A 119 ? 0.91488 0.84576 0.53181 0.09096  -0.11907 -0.16196 114 GLY A N   
898  C  CA  . GLY A 119 ? 0.87918 0.80489 0.47143 0.09620  -0.10443 -0.14666 114 GLY A CA  
899  C  C   . GLY A 119 ? 1.00186 0.92912 0.58625 0.10007  -0.10617 -0.13171 114 GLY A C   
900  O  O   . GLY A 119 ? 1.01837 0.94019 0.58083 0.10429  -0.09395 -0.11814 114 GLY A O   
901  N  N   . LYS A 120 ? 0.96722 0.90152 0.56990 0.09860  -0.12015 -0.13343 115 LYS A N   
902  C  CA  . LYS A 120 ? 0.97918 0.91389 0.57236 0.10423  -0.12332 -0.12006 115 LYS A CA  
903  C  C   . LYS A 120 ? 0.93646 0.87881 0.55949 0.09900  -0.13191 -0.11910 115 LYS A C   
904  O  O   . LYS A 120 ? 1.06161 1.00152 0.68256 0.10034  -0.12811 -0.10539 115 LYS A O   
905  C  CB  . LYS A 120 ? 1.02112 0.95669 0.59075 0.11521  -0.13482 -0.12268 115 LYS A CB  
906  C  CG  . LYS A 120 ? 1.05845 1.00370 0.64394 0.11463  -0.15295 -0.14062 115 LYS A CG  
907  C  CD  . LYS A 120 ? 1.18402 1.12992 0.74308 0.12647  -0.16389 -0.14383 115 LYS A CD  
908  C  CE  . LYS A 120 ? 1.14337 1.07942 0.66944 0.13211  -0.15366 -0.14349 115 LYS A CE  
909  N  NZ  . LYS A 120 ? 1.32729 1.26361 0.82646 0.14406  -0.16491 -0.14785 115 LYS A NZ  
910  N  N   . ASN A 121 ? 0.93604 0.88715 0.58736 0.09279  -0.14279 -0.13330 116 ASN A N   
911  C  CA  . ASN A 121 ? 0.86793 0.82905 0.54858 0.08883  -0.15293 -0.13413 116 ASN A CA  
912  C  C   . ASN A 121 ? 0.80999 0.77003 0.51487 0.07864  -0.14352 -0.13093 116 ASN A C   
913  O  O   . ASN A 121 ? 0.75135 0.71122 0.47404 0.07055  -0.14056 -0.14061 116 ASN A O   
914  C  CB  . ASN A 121 ? 0.95647 0.92875 0.65695 0.08674  -0.16887 -0.15072 116 ASN A CB  
915  C  CG  . ASN A 121 ? 1.07653 1.05089 0.75303 0.09766  -0.17983 -0.15446 116 ASN A CG  
916  O  OD1 . ASN A 121 ? 1.03717 1.00868 0.69100 0.10740  -0.18023 -0.14311 116 ASN A OD1 
917  N  ND2 . ASN A 121 ? 0.95559 0.93372 0.63617 0.09625  -0.18857 -0.17033 116 ASN A ND2 
918  N  N   . PHE A 122 ? 0.84999 0.80829 0.55533 0.07936  -0.13905 -0.11745 117 PHE A N   
919  C  CA  . PHE A 122 ? 0.78168 0.73763 0.50523 0.07091  -0.12934 -0.11307 117 PHE A CA  
920  C  C   . PHE A 122 ? 0.69205 0.65856 0.45421 0.06265  -0.13773 -0.12234 117 PHE A C   
921  O  O   . PHE A 122 ? 0.73699 0.71393 0.51320 0.06449  -0.15016 -0.12512 117 PHE A O   
922  C  CB  . PHE A 122 ? 0.69513 0.64477 0.40661 0.07405  -0.12225 -0.09589 117 PHE A CB  
923  C  CG  . PHE A 122 ? 0.67116 0.61939 0.40250 0.06586  -0.11475 -0.09189 117 PHE A CG  
924  C  CD1 . PHE A 122 ? 0.69740 0.63744 0.42155 0.06181  -0.09953 -0.08769 117 PHE A CD1 
925  C  CD2 . PHE A 122 ? 0.61865 0.57463 0.37647 0.06260  -0.12275 -0.09267 117 PHE A CD2 
926  C  CE1 . PHE A 122 ? 0.59653 0.53770 0.34775 0.05225  -0.08942 -0.08123 117 PHE A CE1 
927  C  CE2 . PHE A 122 ? 0.60098 0.55683 0.38377 0.05327  -0.11209 -0.08636 117 PHE A CE2 
928  C  CZ  . PHE A 122 ? 0.55525 0.50362 0.33499 0.04796  -0.09549 -0.08034 117 PHE A CZ  
929  N  N   . GLN A 123 ? 0.66696 0.63089 0.44707 0.05367  -0.12982 -0.12658 118 GLN A N   
930  C  CA  . GLN A 123 ? 0.60435 0.57521 0.42074 0.04472  -0.13229 -0.13047 118 GLN A CA  
931  C  C   . GLN A 123 ? 0.55500 0.51762 0.37466 0.03966  -0.11848 -0.12385 118 GLN A C   
932  O  O   . GLN A 123 ? 0.57351 0.52708 0.37265 0.04162  -0.10672 -0.11869 118 GLN A O   
933  C  CB  . GLN A 123 ? 0.62267 0.59896 0.46382 0.03756  -0.13815 -0.14561 118 GLN A CB  
934  C  CG  . GLN A 123 ? 0.66489 0.63064 0.50122 0.03384  -0.12868 -0.15187 118 GLN A CG  
935  C  CD  . GLN A 123 ? 0.76227 0.73030 0.62536 0.02542  -0.13299 -0.16529 118 GLN A CD  
936  O  OE1 . GLN A 123 ? 0.80888 0.78680 0.68470 0.02449  -0.14485 -0.17251 118 GLN A OE1 
937  N  NE2 . GLN A 123 ? 0.67855 0.63701 0.55060 0.01939  -0.12290 -0.16830 118 GLN A NE2 
938  N  N   . ILE A 124 ? 0.58709 0.55515 0.43902 0.03175  -0.11531 -0.11966 119 ILE A N   
939  C  CA  . ILE A 124 ? 0.53507 0.49773 0.39726 0.02560  -0.09862 -0.10862 119 ILE A CA  
940  C  C   . ILE A 124 ? 0.52551 0.48182 0.39204 0.02110  -0.09080 -0.11606 119 ILE A C   
941  O  O   . ILE A 124 ? 0.51283 0.46250 0.36730 0.02174  -0.07820 -0.10953 119 ILE A O   
942  C  CB  . ILE A 124 ? 0.49678 0.46643 0.39026 0.01939  -0.09753 -0.10306 119 ILE A CB  
943  C  CG1 . ILE A 124 ? 0.51846 0.49227 0.40517 0.02539  -0.10334 -0.09414 119 ILE A CG1 
944  C  CG2 . ILE A 124 ? 0.48368 0.44806 0.38747 0.01341  -0.08174 -0.09371 119 ILE A CG2 
945  C  CD1 . ILE A 124 ? 0.51120 0.49271 0.42723 0.02093  -0.10281 -0.08949 119 ILE A CD1 
946  N  N   . GLN A 125 ? 0.48895 0.44718 0.37329 0.01670  -0.09816 -0.13013 120 GLN A N   
947  C  CA  . GLN A 125 ? 0.52986 0.48001 0.42327 0.01182  -0.09027 -0.13659 120 GLN A CA  
948  C  C   . GLN A 125 ? 0.55770 0.49946 0.42191 0.01841  -0.08796 -0.14270 120 GLN A C   
949  O  O   . GLN A 125 ? 0.59076 0.53382 0.43819 0.02347  -0.09741 -0.15037 120 GLN A O   
950  C  CB  . GLN A 125 ? 0.53913 0.49167 0.45999 0.00450  -0.09860 -0.15017 120 GLN A CB  
951  C  CG  . GLN A 125 ? 0.61457 0.55544 0.54425 -0.00018 -0.09094 -0.15738 120 GLN A CG  
952  C  CD  . GLN A 125 ? 0.62579 0.56799 0.59080 -0.01053 -0.09064 -0.16042 120 GLN A CD  
953  O  OE1 . GLN A 125 ? 0.49098 0.42895 0.47210 -0.01513 -0.08033 -0.15335 120 GLN A OE1 
954  N  NE2 . GLN A 125 ? 0.54026 0.48914 0.51724 -0.01411 -0.10029 -0.16855 120 GLN A NE2 
955  N  N   . GLY A 126 ? 0.50706 0.44187 0.36734 0.01836  -0.07372 -0.13724 121 GLY A N   
956  C  CA  . GLY A 126 ? 0.54393 0.47127 0.37986 0.02463  -0.06926 -0.14330 121 GLY A CA  
957  C  C   . GLY A 126 ? 0.52869 0.45598 0.34895 0.02842  -0.05497 -0.12964 121 GLY A C   
958  O  O   . GLY A 126 ? 0.47175 0.40321 0.30364 0.02477  -0.04785 -0.11645 121 GLY A O   
959  N  N   . TYR A 127 ? 0.54954 0.47257 0.34334 0.03573  -0.05082 -0.13362 122 TYR A N   
960  C  CA  . TYR A 127 ? 0.61418 0.53799 0.39389 0.03930  -0.03580 -0.12311 122 TYR A CA  
961  C  C   . TYR A 127 ? 0.52350 0.44899 0.27386 0.04534  -0.03622 -0.11588 122 TYR A C   
962  O  O   . TYR A 127 ? 0.56844 0.49153 0.29743 0.05133  -0.04399 -0.12337 122 TYR A O   
963  C  CB  . TYR A 127 ? 0.59391 0.51177 0.36533 0.04399  -0.02856 -0.13242 122 TYR A CB  
964  C  CG  . TYR A 127 ? 0.55350 0.47474 0.31194 0.04833  -0.01262 -0.12344 122 TYR A CG  
965  C  CD1 . TYR A 127 ? 0.53634 0.46465 0.31107 0.04369  -0.00210 -0.10994 122 TYR A CD1 
966  C  CD2 . TYR A 127 ? 0.61163 0.53051 0.34405 0.05649  -0.00780 -0.12861 122 TYR A CD2 
967  C  CE1 . TYR A 127 ? 0.53972 0.47370 0.30612 0.04681  0.01233  -0.10266 122 TYR A CE1 
968  C  CE2 . TYR A 127 ? 0.61671 0.54070 0.33960 0.06022  0.00774  -0.12081 122 TYR A CE2 
969  C  CZ  . TYR A 127 ? 0.56191 0.49403 0.30264 0.05515  0.01764  -0.10813 122 TYR A CZ  
970  O  OH  . TYR A 127 ? 0.56764 0.50739 0.30209 0.05808  0.03307  -0.10109 122 TYR A OH  
971  N  N   . GLY A 128 ? 0.50118 0.43053 0.25218 0.04310  -0.02722 -0.10034 123 GLY A N   
972  C  CA  . GLY A 128 ? 0.55126 0.47969 0.27552 0.04796  -0.02570 -0.09096 123 GLY A CA  
973  C  C   . GLY A 128 ? 0.51166 0.44298 0.24796 0.04208  -0.01908 -0.07520 123 GLY A C   
974  O  O   . GLY A 128 ? 0.48877 0.42400 0.24343 0.03652  -0.00862 -0.06992 123 GLY A O   
975  N  N   . THR A 129 ? 0.48999 0.41908 0.21616 0.04377  -0.02561 -0.06811 124 THR A N   
976  C  CA  . THR A 129 ? 0.52743 0.45716 0.26655 0.03806  -0.02126 -0.05477 124 THR A CA  
977  C  C   . THR A 129 ? 0.50540 0.43491 0.25047 0.03916  -0.03592 -0.05533 124 THR A C   
978  O  O   . THR A 129 ? 0.54812 0.47953 0.29289 0.04277  -0.04923 -0.06667 124 THR A O   
979  C  CB  . THR A 129 ? 0.55404 0.47933 0.27169 0.03928  -0.00849 -0.04146 124 THR A CB  
980  O  OG1 . THR A 129 ? 0.49193 0.41681 0.22483 0.03244  -0.00373 -0.02990 124 THR A OG1 
981  C  CG2 . THR A 129 ? 0.54552 0.46302 0.22869 0.04860  -0.01413 -0.03934 124 THR A CG2 
982  N  N   . ASP A 130 ? 0.50529 0.43303 0.25685 0.03613  -0.03364 -0.04371 125 ASP A N   
983  C  CA  . ASP A 130 ? 0.48785 0.41657 0.24815 0.03764  -0.04623 -0.04344 125 ASP A CA  
984  C  C   . ASP A 130 ? 0.55483 0.47766 0.28486 0.04776  -0.05449 -0.04097 125 ASP A C   
985  O  O   . ASP A 130 ? 0.55182 0.46796 0.25273 0.05284  -0.04840 -0.03707 125 ASP A O   
986  C  CB  . ASP A 130 ? 0.46827 0.39611 0.24658 0.03136  -0.04028 -0.03283 125 ASP A CB  
987  C  CG  . ASP A 130 ? 0.53328 0.46658 0.33695 0.02282  -0.03165 -0.03444 125 ASP A CG  
988  O  OD1 . ASP A 130 ? 0.46728 0.40653 0.29071 0.02055  -0.03709 -0.04384 125 ASP A OD1 
989  O  OD2 . ASP A 130 ? 0.47110 0.40277 0.27467 0.01855  -0.01941 -0.02657 125 ASP A OD2 
990  N  N   . ARG A 131 ? 0.55127 0.47716 0.28801 0.05148  -0.06831 -0.04307 126 ARG A N   
991  C  CA  . ARG A 131 ? 0.57126 0.49386 0.28053 0.06300  -0.07989 -0.04363 126 ARG A CA  
992  C  C   . ARG A 131 ? 0.60665 0.51531 0.28550 0.06806  -0.07080 -0.02794 126 ARG A C   
993  O  O   . ARG A 131 ? 0.58355 0.48602 0.26971 0.06328  -0.06169 -0.01602 126 ARG A O   
994  C  CB  . ARG A 131 ? 0.56880 0.49942 0.29496 0.06626  -0.09590 -0.04771 126 ARG A CB  
995  C  CG  . ARG A 131 ? 0.68301 0.61408 0.38443 0.07911  -0.11095 -0.05134 126 ARG A CG  
996  C  CD  . ARG A 131 ? 0.76496 0.70490 0.48408 0.08332  -0.12507 -0.05243 126 ARG A CD  
997  N  NE  . ARG A 131 ? 0.71571 0.67150 0.47053 0.07662  -0.13395 -0.06645 126 ARG A NE  
998  C  CZ  . ARG A 131 ? 0.67484 0.64341 0.44138 0.07768  -0.14599 -0.07992 126 ARG A CZ  
999  N  NH1 . ARG A 131 ? 0.63824 0.60644 0.38408 0.08549  -0.15108 -0.08178 126 ARG A NH1 
1000 N  NH2 . ARG A 131 ? 0.71031 0.69203 0.51162 0.06994  -0.15193 -0.09135 126 ARG A NH2 
1001 N  N   . VAL A 132 ? 0.65681 0.56051 0.30406 0.07687  -0.07225 -0.02787 127 VAL A N   
1002 C  CA  . VAL A 132 ? 0.68787 0.57925 0.31047 0.08139  -0.06327 -0.01252 127 VAL A CA  
1003 C  C   . VAL A 132 ? 0.68995 0.58111 0.30707 0.09108  -0.07729 -0.01067 127 VAL A C   
1004 O  O   . VAL A 132 ? 0.70399 0.60202 0.31480 0.09793  -0.08819 -0.01930 127 VAL A O   
1005 C  CB  . VAL A 132 ? 0.64697 0.53605 0.24815 0.08308  -0.05262 -0.01173 127 VAL A CB  
1006 C  CG1 . VAL A 132 ? 0.73267 0.60876 0.31043 0.08722  -0.04349 0.00430  127 VAL A CG1 
1007 C  CG2 . VAL A 132 ? 0.76119 0.65264 0.37055 0.07432  -0.03845 -0.01397 127 VAL A CG2 
1008 N  N   . VAL A 133 ? 0.67001 0.55307 0.28979 0.09202  -0.07697 0.00031  128 VAL A N   
1009 C  CA  . VAL A 133 ? 0.71384 0.59762 0.33195 0.10195  -0.09039 0.00187  128 VAL A CA  
1010 C  C   . VAL A 133 ? 0.69905 0.56919 0.28783 0.10999  -0.08488 0.01406  128 VAL A C   
1011 O  O   . VAL A 133 ? 0.78814 0.66137 0.36682 0.12033  -0.09623 0.01132  128 VAL A O   
1012 C  CB  . VAL A 133 ? 0.70307 0.58537 0.34087 0.10014  -0.09390 0.00628  128 VAL A CB  
1013 C  CG1 . VAL A 133 ? 0.80533 0.69161 0.44542 0.11119  -0.10842 0.00616  128 VAL A CG1 
1014 C  CG2 . VAL A 133 ? 0.71629 0.61128 0.38231 0.09163  -0.09799 -0.00525 128 VAL A CG2 
1015 N  N   . THR A 134 ? 0.79748 0.65270 0.37326 0.10514  -0.06741 0.02741  129 THR A N   
1016 C  CA  . THR A 134 ? 0.81932 0.65970 0.36874 0.11144  -0.06024 0.04023  129 THR A CA  
1017 C  C   . THR A 134 ? 0.83558 0.67162 0.36947 0.10617  -0.04350 0.04438  129 THR A C   
1018 O  O   . THR A 134 ? 0.82372 0.66496 0.36928 0.09622  -0.03414 0.04108  129 THR A O   
1019 C  CB  . THR A 134 ? 0.85756 0.68172 0.40822 0.11056  -0.05423 0.05450  129 THR A CB  
1020 O  OG1 . THR A 134 ? 0.81769 0.63673 0.38086 0.09745  -0.03969 0.05957  129 THR A OG1 
1021 C  CG2 . THR A 134 ? 0.81540 0.64491 0.38250 0.11672  -0.07020 0.05037  129 THR A CG2 
1022 N  N   . GLN A 135 ? 0.83846 0.66534 0.34591 0.11349  -0.03950 0.05179  130 GLN A N   
1023 C  CA  . GLN A 135 ? 0.88331 0.70679 0.37554 0.10933  -0.02303 0.05637  130 GLN A CA  
1024 C  C   . GLN A 135 ? 0.79917 0.61286 0.29912 0.09747  -0.00407 0.06875  130 GLN A C   
1025 O  O   . GLN A 135 ? 0.91582 0.73334 0.41684 0.08973  0.01007  0.06925  130 GLN A O   
1026 C  CB  . GLN A 135 ? 0.91079 0.72576 0.37182 0.12052  -0.02331 0.06206  130 GLN A CB  
1027 C  CG  . GLN A 135 ? 0.96825 0.78440 0.41240 0.11892  -0.01013 0.06241  130 GLN A CG  
1028 C  CD  . GLN A 135 ? 1.08639 0.89343 0.49762 0.13098  -0.01106 0.06795  130 GLN A CD  
1029 O  OE1 . GLN A 135 ? 1.10874 0.90670 0.50908 0.14024  -0.01989 0.07349  130 GLN A OE1 
1030 N  NE2 . GLN A 135 ? 1.05175 0.86115 0.44645 0.13165  -0.00182 0.06636  130 GLN A NE2 
1031 N  N   . ASP A 136 ? 0.90558 0.70751 0.41269 0.09571  -0.00359 0.07801  131 ASP A N   
1032 C  CA  . ASP A 136 ? 0.94966 0.74172 0.46683 0.08354  0.01321  0.08886  131 ASP A CA  
1033 C  C   . ASP A 136 ? 0.90478 0.70511 0.45034 0.07294  0.01357  0.08287  131 ASP A C   
1034 O  O   . ASP A 136 ? 0.91251 0.70475 0.47047 0.06292  0.02422  0.09050  131 ASP A O   
1035 C  CB  . ASP A 136 ? 0.97867 0.75093 0.48793 0.08674  0.01470  0.10198  131 ASP A CB  
1036 C  CG  . ASP A 136 ? 1.11035 0.88106 0.63426 0.09047  0.00081  0.09917  131 ASP A CG  
1037 O  OD1 . ASP A 136 ? 1.09809 0.88344 0.63194 0.09499  -0.01396 0.08700  131 ASP A OD1 
1038 O  OD2 . ASP A 136 ? 1.12665 0.88156 0.65303 0.08880  0.00486  0.10881  131 ASP A OD2 
1039 N  N   . GLN A 137 ? 0.80938 0.62510 0.36569 0.07467  0.00214  0.06903  132 GLN A N   
1040 C  CA  . GLN A 137 ? 0.80539 0.62825 0.38665 0.06554  0.00204  0.06322  132 GLN A CA  
1041 C  C   . GLN A 137 ? 0.68044 0.50903 0.26946 0.05420  0.01877  0.06343  132 GLN A C   
1042 O  O   . GLN A 137 ? 0.73244 0.56793 0.31122 0.05556  0.02460  0.06038  132 GLN A O   
1043 C  CB  . GLN A 137 ? 0.74620 0.58356 0.33716 0.07083  -0.01540 0.04794  132 GLN A CB  
1044 C  CG  . GLN A 137 ? 0.72290 0.56738 0.33808 0.06244  -0.01669 0.04113  132 GLN A CG  
1045 C  CD  . GLN A 137 ? 0.67316 0.53386 0.30493 0.06640  -0.03398 0.02551  132 GLN A CD  
1046 O  OE1 . GLN A 137 ? 0.69061 0.55156 0.31511 0.07646  -0.04888 0.02291  132 GLN A OE1 
1047 N  NE2 . GLN A 137 ? 0.63765 0.51258 0.29348 0.05844  -0.03195 0.01487  132 GLN A NE2 
1048 N  N   . ILE A 138 ? 0.72687 0.55332 0.33496 0.04320  0.02644  0.06666  133 ILE A N   
1049 C  CA  . ILE A 138 ? 0.70073 0.53587 0.32162 0.03206  0.04119  0.06554  133 ILE A CA  
1050 C  C   . ILE A 138 ? 0.66120 0.51349 0.29603 0.03232  0.03411  0.05069  133 ILE A C   
1051 O  O   . ILE A 138 ? 0.63144 0.49054 0.28491 0.03370  0.02017  0.04237  133 ILE A O   
1052 C  CB  . ILE A 138 ? 0.77515 0.60368 0.41507 0.01956  0.05056  0.07272  133 ILE A CB  
1053 C  CG1 . ILE A 138 ? 0.79047 0.60085 0.42214 0.02014  0.05324  0.08517  133 ILE A CG1 
1054 C  CG2 . ILE A 138 ? 0.76666 0.60603 0.42034 0.00816  0.06715  0.07296  133 ILE A CG2 
1055 C  CD1 . ILE A 138 ? 0.73711 0.54346 0.35445 0.01956  0.06593  0.09376  133 ILE A CD1 
1056 N  N   . LEU A 139 ? 0.62439 0.48654 0.25715 0.03044  0.04381  0.04656  134 LEU A N   
1057 C  CA  . LEU A 139 ? 0.54732 0.42693 0.19886 0.02999  0.03870  0.03204  134 LEU A CA  
1058 C  C   . LEU A 139 ? 0.55037 0.44187 0.23296 0.01808  0.04911  0.03106  134 LEU A C   
1059 O  O   . LEU A 139 ? 0.55644 0.44626 0.23982 0.01095  0.06389  0.03999  134 LEU A O   
1060 C  CB  . LEU A 139 ? 0.58945 0.47178 0.21593 0.03824  0.04147  0.02656  134 LEU A CB  
1061 C  CG  . LEU A 139 ? 0.63674 0.51327 0.24025 0.04930  0.03040  0.02631  134 LEU A CG  
1062 C  CD1 . LEU A 139 ? 0.69550 0.57856 0.28434 0.05455  0.03480  0.02087  134 LEU A CD1 
1063 C  CD2 . LEU A 139 ? 0.72511 0.60278 0.33335 0.05511  0.01017  0.01631  134 LEU A CD2 
1064 N  N   . ASP A 140 ? 0.51383 0.41751 0.22236 0.01600  0.04126  0.02018  135 ASP A N   
1065 C  CA  . ASP A 140 ? 0.49936 0.41547 0.23622 0.00682  0.04928  0.01822  135 ASP A CA  
1066 C  C   . ASP A 140 ? 0.44086 0.36793 0.17523 0.00853  0.05853  0.01272  135 ASP A C   
1067 O  O   . ASP A 140 ? 0.50190 0.42833 0.21824 0.01699  0.05494  0.00607  135 ASP A O   
1068 C  CB  . ASP A 140 ? 0.46082 0.38375 0.22486 0.00469  0.03820  0.01021  135 ASP A CB  
1069 C  CG  . ASP A 140 ? 0.46916 0.38373 0.24061 0.00208  0.03149  0.01563  135 ASP A CG  
1070 O  OD1 . ASP A 140 ? 0.57640 0.48079 0.33888 -0.00108 0.03778  0.02601  135 ASP A OD1 
1071 O  OD2 . ASP A 140 ? 0.48141 0.39897 0.26778 0.00323  0.02064  0.00948  135 ASP A OD2 
1072 N  N   . TRP A 141 ? 0.48085 0.41881 0.23428 0.00086  0.07006  0.01468  136 TRP A N   
1073 C  CA  . TRP A 141 ? 0.51264 0.46327 0.26748 0.00271  0.08014  0.00979  136 TRP A CA  
1074 C  C   . TRP A 141 ? 0.44344 0.40447 0.21985 0.00454  0.07285  -0.00192 136 TRP A C   
1075 O  O   . TRP A 141 ? 0.47124 0.44503 0.27101 0.00008  0.07797  -0.00352 136 TRP A O   
1076 C  CB  . TRP A 141 ? 0.46191 0.42130 0.22770 -0.00592 0.09638  0.01757  136 TRP A CB  
1077 C  CG  . TRP A 141 ? 0.52324 0.49514 0.28501 -0.00248 0.10902  0.01448  136 TRP A CG  
1078 C  CD1 . TRP A 141 ? 0.46579 0.45528 0.24917 -0.00228 0.11259  0.00709  136 TRP A CD1 
1079 C  CD2 . TRP A 141 ? 0.51214 0.47969 0.24546 0.00251  0.12012  0.01888  136 TRP A CD2 
1080 N  NE1 . TRP A 141 ? 0.47985 0.47708 0.25144 0.00261  0.12529  0.00606  136 TRP A NE1 
1081 C  CE2 . TRP A 141 ? 0.50798 0.49205 0.24846 0.00531  0.13059  0.01327  136 TRP A CE2 
1082 C  CE3 . TRP A 141 ? 0.53002 0.48236 0.23424 0.00570  0.12116  0.02712  136 TRP A CE3 
1083 C  CZ2 . TRP A 141 ? 0.52817 0.51707 0.25353 0.00989  0.13973  0.01489  136 TRP A CZ2 
1084 C  CZ3 . TRP A 141 ? 0.56115 0.51863 0.25164 0.00999  0.12945  0.02888  136 TRP A CZ3 
1085 C  CH2 . TRP A 141 ? 0.61705 0.59261 0.31792 0.01159  0.13883  0.02265  136 TRP A CH2 
1086 N  N   . SER A 142 ? 0.50363 0.45858 0.27179 0.01143  0.06038  -0.01022 137 SER A N   
1087 C  CA  . SER A 142 ? 0.41758 0.37829 0.20374 0.01331  0.05338  -0.02114 137 SER A CA  
1088 C  C   . SER A 142 ? 0.50966 0.46230 0.28044 0.02087  0.04148  -0.03049 137 SER A C   
1089 O  O   . SER A 142 ? 0.48706 0.43074 0.23842 0.02403  0.03497  -0.02816 137 SER A O   
1090 C  CB  . SER A 142 ? 0.37623 0.33926 0.18913 0.00688  0.04737  -0.02000 137 SER A CB  
1091 O  OG  . SER A 142 ? 0.46409 0.41748 0.27328 0.00646  0.03662  -0.01785 137 SER A OG  
1092 N  N   . ASP A 143 ? 0.41631 0.37197 0.19624 0.02397  0.03838  -0.04141 138 ASP A N   
1093 C  CA  . ASP A 143 ? 0.42126 0.37034 0.19634 0.02856  0.02540  -0.05260 138 ASP A CA  
1094 C  C   . ASP A 143 ? 0.40160 0.35200 0.20491 0.02382  0.01850  -0.05632 138 ASP A C   
1095 O  O   . ASP A 143 ? 0.42282 0.37929 0.24585 0.01915  0.02445  -0.05160 138 ASP A O   
1096 C  CB  . ASP A 143 ? 0.45798 0.40628 0.21898 0.03602  0.02821  -0.06314 138 ASP A CB  
1097 C  CG  . ASP A 143 ? 0.52895 0.47810 0.26379 0.04073  0.03934  -0.05823 138 ASP A CG  
1098 O  OD1 . ASP A 143 ? 0.51044 0.45357 0.22364 0.04266  0.03674  -0.05263 138 ASP A OD1 
1099 O  OD2 . ASP A 143 ? 0.54076 0.49672 0.27685 0.04295  0.05120  -0.05940 138 ASP A OD2 
1100 N  N   . ARG A 144 ? 0.46361 0.40877 0.26888 0.02511  0.00600  -0.06502 139 ARG A N   
1101 C  CA  . ARG A 144 ? 0.39184 0.33740 0.22344 0.02063  0.00122  -0.06872 139 ARG A CA  
1102 C  C   . ARG A 144 ? 0.50066 0.44061 0.33296 0.02280  -0.00925 -0.08228 139 ARG A C   
1103 O  O   . ARG A 144 ? 0.46302 0.39994 0.27800 0.02672  -0.01765 -0.08802 139 ARG A O   
1104 C  CB  . ARG A 144 ? 0.40175 0.34890 0.24716 0.01507  -0.00272 -0.06038 139 ARG A CB  
1105 C  CG  . ARG A 144 ? 0.40340 0.34777 0.24821 0.01551  -0.01597 -0.06416 139 ARG A CG  
1106 C  CD  . ARG A 144 ? 0.47035 0.41174 0.28839 0.02087  -0.02003 -0.06199 139 ARG A CD  
1107 N  NE  . ARG A 144 ? 0.45733 0.39852 0.27754 0.02212  -0.03373 -0.06534 139 ARG A NE  
1108 C  CZ  . ARG A 144 ? 0.48939 0.43097 0.31102 0.02424  -0.04478 -0.07783 139 ARG A CZ  
1109 N  NH1 . ARG A 144 ? 0.45059 0.38993 0.26896 0.02564  -0.04382 -0.08839 139 ARG A NH1 
1110 N  NH2 . ARG A 144 ? 0.48786 0.43244 0.31524 0.02509  -0.05729 -0.08046 139 ARG A NH2 
1111 N  N   . LEU A 145 ? 0.45688 0.39496 0.30892 0.02037  -0.00855 -0.08751 140 LEU A N   
1112 C  CA  . LEU A 145 ? 0.45071 0.38249 0.31089 0.01957  -0.01781 -0.09999 140 LEU A CA  
1113 C  C   . LEU A 145 ? 0.39352 0.32715 0.27767 0.01273  -0.02305 -0.09684 140 LEU A C   
1114 O  O   . LEU A 145 ? 0.41439 0.34924 0.31537 0.00935  -0.01652 -0.09020 140 LEU A O   
1115 C  CB  . LEU A 145 ? 0.48387 0.40926 0.34862 0.02187  -0.01203 -0.10764 140 LEU A CB  
1116 C  CG  . LEU A 145 ? 0.48495 0.40103 0.36175 0.01935  -0.01977 -0.12044 140 LEU A CG  
1117 C  CD1 . LEU A 145 ? 0.49741 0.41071 0.35757 0.02206  -0.03111 -0.13270 140 LEU A CD1 
1118 C  CD2 . LEU A 145 ? 0.53523 0.44257 0.41754 0.02201  -0.01194 -0.12513 140 LEU A CD2 
1119 N  N   . HIS A 146 ? 0.46875 0.40367 0.35388 0.01147  -0.03474 -0.10155 141 HIS A N   
1120 C  CA  . HIS A 146 ? 0.39537 0.33466 0.30174 0.00590  -0.03972 -0.09793 141 HIS A CA  
1121 C  C   . HIS A 146 ? 0.45054 0.38722 0.37390 0.00194  -0.04778 -0.11038 141 HIS A C   
1122 O  O   . HIS A 146 ? 0.47730 0.41397 0.39230 0.00395  -0.05816 -0.12129 141 HIS A O   
1123 C  CB  . HIS A 146 ? 0.40086 0.34578 0.29655 0.00823  -0.04662 -0.09244 141 HIS A CB  
1124 C  CG  . HIS A 146 ? 0.41783 0.36761 0.33048 0.00433  -0.04586 -0.08296 141 HIS A CG  
1125 N  ND1 . HIS A 146 ? 0.46073 0.41400 0.39800 -0.00051 -0.05046 -0.08619 141 HIS A ND1 
1126 C  CD2 . HIS A 146 ? 0.40333 0.35457 0.31160 0.00460  -0.04067 -0.07081 141 HIS A CD2 
1127 C  CE1 . HIS A 146 ? 0.43008 0.38711 0.37621 -0.00205 -0.04796 -0.07642 141 HIS A CE1 
1128 N  NE2 . HIS A 146 ? 0.40441 0.35954 0.33306 0.00091  -0.04254 -0.06738 141 HIS A NE2 
1129 N  N   . LEU A 147 ? 0.40777 0.34196 0.35456 -0.00375 -0.04295 -0.10895 142 LEU A N   
1130 C  CA  . LEU A 147 ? 0.41529 0.34482 0.38062 -0.00906 -0.04773 -0.12009 142 LEU A CA  
1131 C  C   . LEU A 147 ? 0.44993 0.38511 0.44153 -0.01578 -0.04805 -0.11531 142 LEU A C   
1132 O  O   . LEU A 147 ? 0.40979 0.34576 0.40833 -0.01671 -0.03928 -0.10384 142 LEU A O   
1133 C  CB  . LEU A 147 ? 0.39746 0.31416 0.36498 -0.00906 -0.03922 -0.12382 142 LEU A CB  
1134 C  CG  . LEU A 147 ? 0.42308 0.33357 0.36680 -0.00172 -0.03638 -0.12891 142 LEU A CG  
1135 C  CD1 . LEU A 147 ? 0.49924 0.39691 0.44912 -0.00109 -0.02733 -0.13102 142 LEU A CD1 
1136 C  CD2 . LEU A 147 ? 0.47399 0.38350 0.40452 0.00031  -0.04813 -0.14323 142 LEU A CD2 
1137 N  N   . ARG A 148 ? 0.47852 0.41854 0.48509 -0.02025 -0.05806 -0.12467 143 ARG A N   
1138 C  CA  . ARG A 148 ? 0.45920 0.40491 0.49404 -0.02728 -0.05705 -0.12173 143 ARG A CA  
1139 C  C   . ARG A 148 ? 0.42251 0.35592 0.47372 -0.03324 -0.04808 -0.12354 143 ARG A C   
1140 O  O   . ARG A 148 ? 0.44217 0.36683 0.49622 -0.03605 -0.05116 -0.13565 143 ARG A O   
1141 C  CB  . ARG A 148 ? 0.50842 0.46605 0.55671 -0.03020 -0.07081 -0.13176 143 ARG A CB  
1142 C  CG  . ARG A 148 ? 0.55461 0.51988 0.63542 -0.03807 -0.06876 -0.12985 143 ARG A CG  
1143 C  CD  . ARG A 148 ? 0.57316 0.55126 0.67188 -0.04205 -0.08222 -0.14237 143 ARG A CD  
1144 N  NE  . ARG A 148 ? 0.59759 0.59078 0.68879 -0.03545 -0.09338 -0.14125 143 ARG A NE  
1145 C  CZ  . ARG A 148 ? 0.60546 0.61100 0.71067 -0.03490 -0.09271 -0.13319 143 ARG A CZ  
1146 N  NH1 . ARG A 148 ? 0.58723 0.59285 0.71426 -0.04080 -0.08140 -0.12590 143 ARG A NH1 
1147 N  NH2 . ARG A 148 ? 0.66034 0.67757 0.75607 -0.02732 -0.10333 -0.13224 143 ARG A NH2 
1148 N  N   . VAL A 149 ? 0.42941 0.36057 0.48969 -0.03460 -0.03698 -0.11164 144 VAL A N   
1149 C  CA  . VAL A 149 ? 0.45279 0.37038 0.52613 -0.03893 -0.02721 -0.11090 144 VAL A CA  
1150 C  C   . VAL A 149 ? 0.43739 0.35916 0.53965 -0.04774 -0.02621 -0.11124 144 VAL A C   
1151 O  O   . VAL A 149 ? 0.44857 0.35926 0.56527 -0.05379 -0.02140 -0.11498 144 VAL A O   
1152 C  CB  . VAL A 149 ? 0.45082 0.36225 0.51428 -0.03379 -0.01524 -0.09787 144 VAL A CB  
1153 C  CG1 . VAL A 149 ? 0.44814 0.35692 0.48648 -0.02579 -0.01511 -0.09848 144 VAL A CG1 
1154 C  CG2 . VAL A 149 ? 0.61554 0.53819 0.68266 -0.03306 -0.01247 -0.08588 144 VAL A CG2 
1155 N  N   . GLU A 150 ? 0.42058 0.35815 0.53123 -0.04821 -0.02988 -0.10665 145 GLU A N   
1156 C  CA  . GLU A 150 ? 0.52742 0.47161 0.66662 -0.05590 -0.02720 -0.10576 145 GLU A CA  
1157 C  C   . GLU A 150 ? 0.49449 0.45827 0.64490 -0.05691 -0.03956 -0.11181 145 GLU A C   
1158 O  O   . GLU A 150 ? 0.48124 0.45344 0.61466 -0.04973 -0.04706 -0.11005 145 GLU A O   
1159 C  CB  . GLU A 150 ? 0.47628 0.41958 0.61817 -0.05437 -0.01467 -0.09069 145 GLU A CB  
1160 C  CG  . GLU A 150 ? 0.53855 0.46316 0.67582 -0.05411 -0.00224 -0.08492 145 GLU A CG  
1161 C  CD  . GLU A 150 ? 0.69654 0.61966 0.84515 -0.05565 0.00992  -0.07319 145 GLU A CD  
1162 O  OE1 . GLU A 150 ? 0.69744 0.62775 0.83721 -0.05024 0.01225  -0.06370 145 GLU A OE1 
1163 O  OE2 . GLU A 150 ? 0.73144 0.64576 0.89631 -0.06199 0.01742  -0.07322 145 GLU A OE2 
1164 N  N   . PRO A 151 ? 0.52909 0.50119 0.70550 -0.06432 -0.04101 -0.11675 146 PRO A N   
1165 C  CA  . PRO A 151 ? 0.56029 0.52315 0.75209 -0.07155 -0.03093 -0.11537 146 PRO A CA  
1166 C  C   . PRO A 151 ? 0.64411 0.59139 0.82361 -0.07230 -0.03271 -0.12327 146 PRO A C   
1167 O  O   . PRO A 151 ? 0.59213 0.54205 0.75854 -0.06917 -0.04438 -0.13300 146 PRO A O   
1168 C  CB  . PRO A 151 ? 0.62283 0.60427 0.84168 -0.07723 -0.03517 -0.11928 146 PRO A CB  
1169 C  CG  . PRO A 151 ? 0.68317 0.68100 0.89635 -0.07227 -0.05156 -0.12729 146 PRO A CG  
1170 C  CD  . PRO A 151 ? 0.49810 0.49160 0.68770 -0.06417 -0.05269 -0.12199 146 PRO A CD  
1171 N  N   . LYS A 152 ? 0.66373 0.59380 0.84533 -0.07540 -0.02098 -0.11871 147 LYS A N   
1172 C  CA  . LYS A 152 ? 0.65485 0.56686 0.82264 -0.07471 -0.02108 -0.12497 147 LYS A CA  
1173 C  C   . LYS A 152 ? 0.63183 0.54914 0.80397 -0.07865 -0.03317 -0.13913 147 LYS A C   
1174 O  O   . LYS A 152 ? 0.65749 0.56633 0.81120 -0.07497 -0.03924 -0.14744 147 LYS A O   
1175 C  CB  . LYS A 152 ? 0.65340 0.54723 0.82701 -0.07797 -0.00704 -0.11746 147 LYS A CB  
1176 C  CG  . LYS A 152 ? 0.83528 0.70754 0.99380 -0.07589 -0.00553 -0.12236 147 LYS A CG  
1177 C  CD  . LYS A 152 ? 0.78962 0.65074 0.92556 -0.06603 -0.00025 -0.11619 147 LYS A CD  
1178 C  CE  . LYS A 152 ? 0.83363 0.67462 0.95393 -0.06229 0.00039  -0.12230 147 LYS A CE  
1179 N  NZ  . LYS A 152 ? 0.84006 0.66274 0.96870 -0.06646 0.00943  -0.11879 147 LYS A NZ  
1180 N  N   . GLU A 153 ? 0.68287 0.61497 0.87903 -0.08561 -0.03675 -0.14234 148 GLU A N   
1181 C  CA  . GLU A 153 ? 0.66592 0.60434 0.86923 -0.09003 -0.04831 -0.15603 148 GLU A CA  
1182 C  C   . GLU A 153 ? 0.69919 0.65078 0.88702 -0.08317 -0.06384 -0.16433 148 GLU A C   
1183 O  O   . GLU A 153 ? 0.69282 0.64707 0.87931 -0.08467 -0.07439 -0.17642 148 GLU A O   
1184 C  CB  . GLU A 153 ? 0.73391 0.68689 0.96928 -0.09902 -0.04738 -0.15686 148 GLU A CB  
1185 C  CG  . GLU A 153 ? 0.81857 0.75776 1.06929 -0.10667 -0.03221 -0.14983 148 GLU A CG  
1186 C  CD  . GLU A 153 ? 0.90154 0.83847 1.15282 -0.10380 -0.01844 -0.13413 148 GLU A CD  
1187 O  OE1 . GLU A 153 ? 0.81199 0.76061 1.05660 -0.09738 -0.02112 -0.12943 148 GLU A OE1 
1188 O  OE2 . GLU A 153 ? 0.73481 0.65751 0.99209 -0.10766 -0.00501 -0.12644 148 GLU A OE2 
1189 N  N   . GLU A 154 ? 0.72083 0.67998 0.89593 -0.07550 -0.06559 -0.15814 149 GLU A N   
1190 C  CA  . GLU A 154 ? 0.65644 0.62715 0.81433 -0.06791 -0.07972 -0.16429 149 GLU A CA  
1191 C  C   . GLU A 154 ? 0.61838 0.57535 0.74341 -0.05976 -0.07998 -0.16503 149 GLU A C   
1192 O  O   . GLU A 154 ? 0.66398 0.62833 0.76968 -0.05206 -0.08959 -0.16761 149 GLU A O   
1193 C  CB  . GLU A 154 ? 0.73451 0.72355 0.89934 -0.06424 -0.08301 -0.15769 149 GLU A CB  
1194 C  CG  . GLU A 154 ? 0.73683 0.74455 0.93269 -0.07008 -0.08611 -0.15963 149 GLU A CG  
1195 C  CD  . GLU A 154 ? 0.73776 0.76334 0.93962 -0.06500 -0.08983 -0.15358 149 GLU A CD  
1196 O  OE1 . GLU A 154 ? 0.82398 0.84670 1.00476 -0.05729 -0.09110 -0.14826 149 GLU A OE1 
1197 O  OE2 . GLU A 154 ? 0.76443 0.80673 0.99231 -0.06859 -0.09125 -0.15427 149 GLU A OE2 
1198 N  N   . GLN A 155 ? 0.61800 0.55524 0.73559 -0.06048 -0.06923 -0.16238 150 GLN A N   
1199 C  CA  . GLN A 155 ? 0.60416 0.52892 0.69214 -0.05255 -0.06869 -0.16441 150 GLN A CA  
1200 C  C   . GLN A 155 ? 0.69665 0.62050 0.77097 -0.05063 -0.07951 -0.17753 150 GLN A C   
1201 O  O   . GLN A 155 ? 0.68056 0.60247 0.76856 -0.05735 -0.08268 -0.18548 150 GLN A O   
1202 C  CB  . GLN A 155 ? 0.58851 0.49272 0.67408 -0.05305 -0.05496 -0.15929 150 GLN A CB  
1203 C  CG  . GLN A 155 ? 0.53714 0.44034 0.63195 -0.05341 -0.04349 -0.14583 150 GLN A CG  
1204 C  CD  . GLN A 155 ? 0.59191 0.47472 0.68286 -0.05221 -0.03066 -0.14048 150 GLN A CD  
1205 O  OE1 . GLN A 155 ? 0.63084 0.49935 0.71466 -0.05189 -0.03005 -0.14701 150 GLN A OE1 
1206 N  NE2 . GLN A 155 ? 0.53422 0.41513 0.62894 -0.05071 -0.02052 -0.12848 150 GLN A NE2 
1207 N  N   . ASP A 156 ? 0.60755 0.53255 0.65398 -0.04137 -0.08478 -0.17967 151 ASP A N   
1208 C  CA  . ASP A 156 ? 0.61762 0.53966 0.64495 -0.03752 -0.09340 -0.19116 151 ASP A CA  
1209 C  C   . ASP A 156 ? 0.62355 0.52702 0.62891 -0.03212 -0.08447 -0.19155 151 ASP A C   
1210 O  O   . ASP A 156 ? 0.68983 0.59309 0.67324 -0.02370 -0.08132 -0.18667 151 ASP A O   
1211 C  CB  . ASP A 156 ? 0.68097 0.61813 0.69090 -0.02981 -0.10523 -0.19246 151 ASP A CB  
1212 C  CG  . ASP A 156 ? 0.67981 0.61506 0.67008 -0.02558 -0.11456 -0.20425 151 ASP A CG  
1213 O  OD1 . ASP A 156 ? 0.63223 0.55364 0.62100 -0.02847 -0.11167 -0.21203 151 ASP A OD1 
1214 O  OD2 . ASP A 156 ? 0.74208 0.68882 0.71732 -0.01881 -0.12473 -0.20549 151 ASP A OD2 
1215 N  N   . LEU A 157 ? 0.58471 0.47253 0.59613 -0.03667 -0.08002 -0.19729 152 LEU A N   
1216 C  CA  . LEU A 157 ? 0.64743 0.51667 0.64141 -0.03116 -0.07034 -0.19727 152 LEU A CA  
1217 C  C   . LEU A 157 ? 0.72904 0.59652 0.69246 -0.02205 -0.07475 -0.20495 152 LEU A C   
1218 O  O   . LEU A 157 ? 0.74206 0.59708 0.68886 -0.01551 -0.06629 -0.20458 152 LEU A O   
1219 C  CB  . LEU A 157 ? 0.70240 0.55339 0.71049 -0.03805 -0.06461 -0.20092 152 LEU A CB  
1220 C  CG  . LEU A 157 ? 0.76698 0.61558 0.80136 -0.04551 -0.05605 -0.19076 152 LEU A CG  
1221 C  CD1 . LEU A 157 ? 0.75516 0.58338 0.79994 -0.05163 -0.05037 -0.19399 152 LEU A CD1 
1222 C  CD2 . LEU A 157 ? 0.69932 0.54702 0.72820 -0.03930 -0.04581 -0.17820 152 LEU A CD2 
1223 N  N   . ALA A 158 ? 0.62877 0.50889 0.58400 -0.02056 -0.08718 -0.21139 153 ALA A N   
1224 C  CA  . ALA A 158 ? 0.66538 0.54466 0.58914 -0.01093 -0.09032 -0.21678 153 ALA A CA  
1225 C  C   . ALA A 158 ? 0.63882 0.52245 0.54205 -0.00165 -0.08361 -0.20657 153 ALA A C   
1226 O  O   . ALA A 158 ? 0.68156 0.56187 0.55803 0.00691  -0.08117 -0.20865 153 ALA A O   
1227 C  CB  . ALA A 158 ? 0.66047 0.55273 0.57959 -0.01050 -0.10551 -0.22479 153 ALA A CB  
1228 N  N   . PHE A 159 ? 0.63565 0.52670 0.55082 -0.00329 -0.07998 -0.19563 154 PHE A N   
1229 C  CA  . PHE A 159 ? 0.64291 0.53788 0.54040 0.00441  -0.07329 -0.18580 154 PHE A CA  
1230 C  C   . PHE A 159 ? 0.63289 0.51892 0.53739 0.00480  -0.05968 -0.17926 154 PHE A C   
1231 O  O   . PHE A 159 ? 0.59142 0.48090 0.48302 0.01093  -0.05295 -0.17146 154 PHE A O   
1232 C  CB  . PHE A 159 ? 0.61817 0.52815 0.51963 0.00397  -0.07985 -0.17826 154 PHE A CB  
1233 C  CG  . PHE A 159 ? 0.67598 0.59563 0.56461 0.00727  -0.09270 -0.18271 154 PHE A CG  
1234 C  CD1 . PHE A 159 ? 0.69212 0.61918 0.60032 0.00121  -0.10384 -0.18941 154 PHE A CD1 
1235 C  CD2 . PHE A 159 ? 0.75243 0.67393 0.60935 0.01690  -0.09298 -0.17985 154 PHE A CD2 
1236 C  CE1 . PHE A 159 ? 0.72654 0.66326 0.62306 0.00555  -0.11632 -0.19384 154 PHE A CE1 
1237 C  CE2 . PHE A 159 ? 0.73599 0.66529 0.57958 0.02116  -0.10464 -0.18314 154 PHE A CE2 
1238 C  CZ  . PHE A 159 ? 0.78165 0.71878 0.64505 0.01593  -0.11696 -0.19056 154 PHE A CZ  
1239 N  N   . TRP A 160 ? 0.61314 0.48769 0.53709 -0.00111 -0.05524 -0.18175 155 TRP A N   
1240 C  CA  . TRP A 160 ? 0.64021 0.50482 0.56934 0.00102  -0.04239 -0.17572 155 TRP A CA  
1241 C  C   . TRP A 160 ? 0.61962 0.47277 0.52935 0.00903  -0.03605 -0.18105 155 TRP A C   
1242 O  O   . TRP A 160 ? 0.60887 0.45220 0.51554 0.00751  -0.03948 -0.19080 155 TRP A O   
1243 C  CB  . TRP A 160 ? 0.59337 0.44893 0.55001 -0.00789 -0.03915 -0.17382 155 TRP A CB  
1244 C  CG  . TRP A 160 ? 0.59933 0.46646 0.57714 -0.01505 -0.04167 -0.16653 155 TRP A CG  
1245 C  CD1 . TRP A 160 ? 0.56824 0.45052 0.55030 -0.01838 -0.05229 -0.16776 155 TRP A CD1 
1246 C  CD2 . TRP A 160 ? 0.50793 0.37248 0.50519 -0.01890 -0.03294 -0.15654 155 TRP A CD2 
1247 N  NE1 . TRP A 160 ? 0.51892 0.40853 0.52258 -0.02416 -0.05042 -0.15958 155 TRP A NE1 
1248 C  CE2 . TRP A 160 ? 0.52854 0.40726 0.54137 -0.02493 -0.03829 -0.15244 155 TRP A CE2 
1249 C  CE3 . TRP A 160 ? 0.56041 0.41213 0.56248 -0.01686 -0.02093 -0.15012 155 TRP A CE3 
1250 C  CZ2 . TRP A 160 ? 0.51507 0.39553 0.54706 -0.02944 -0.03110 -0.14168 155 TRP A CZ2 
1251 C  CZ3 . TRP A 160 ? 0.51684 0.37019 0.53678 -0.02112 -0.01430 -0.13873 155 TRP A CZ3 
1252 C  CH2 . TRP A 160 ? 0.56321 0.43100 0.59719 -0.02750 -0.01895 -0.13411 155 TRP A CH2 
1253 N  N   . PRO A 161 ? 0.61006 0.46513 0.50703 0.01769  -0.02673 -0.17529 156 PRO A N   
1254 C  CA  . PRO A 161 ? 0.68121 0.52758 0.56118 0.02624  -0.01941 -0.17975 156 PRO A CA  
1255 C  C   . PRO A 161 ? 0.71978 0.54676 0.61114 0.02399  -0.01566 -0.18485 156 PRO A C   
1256 O  O   . PRO A 161 ? 0.73537 0.55530 0.64621 0.01984  -0.01173 -0.17943 156 PRO A O   
1257 C  CB  . PRO A 161 ? 0.68536 0.53986 0.55943 0.03425  -0.00889 -0.17011 156 PRO A CB  
1258 C  CG  . PRO A 161 ? 0.62335 0.49393 0.50012 0.02993  -0.01252 -0.15976 156 PRO A CG  
1259 C  CD  . PRO A 161 ? 0.66439 0.53257 0.56169 0.01970  -0.02196 -0.16261 156 PRO A CD  
1260 N  N   . ASP A 162 ? 0.77079 0.58806 0.64875 0.02682  -0.01666 -0.19497 157 ASP A N   
1261 C  CA  . ASP A 162 ? 0.80538 0.60138 0.68908 0.02623  -0.01219 -0.20036 157 ASP A CA  
1262 C  C   . ASP A 162 ? 0.83179 0.62144 0.70683 0.03751  0.00052  -0.19768 157 ASP A C   
1263 O  O   . ASP A 162 ? 0.75175 0.52228 0.63188 0.03870  0.00606  -0.19965 157 ASP A O   
1264 C  CB  . ASP A 162 ? 0.89362 0.68124 0.76856 0.02297  -0.02027 -0.21407 157 ASP A CB  
1265 C  CG  . ASP A 162 ? 1.00699 0.80793 0.85862 0.02874  -0.02509 -0.21896 157 ASP A CG  
1266 O  OD1 . ASP A 162 ? 0.95079 0.75975 0.78771 0.03824  -0.01737 -0.21406 157 ASP A OD1 
1267 O  OD2 . ASP A 162 ? 1.13730 0.94118 0.98535 0.02405  -0.03642 -0.22725 157 ASP A OD2 
1268 N  N   . HIS A 163 ? 0.70080 0.50637 0.56313 0.04601  0.00550  -0.19278 158 HIS A N   
1269 C  CA  . HIS A 163 ? 0.81310 0.61936 0.67252 0.05676  0.01780  -0.18803 158 HIS A CA  
1270 C  C   . HIS A 163 ? 0.78703 0.61297 0.64839 0.05996  0.02164  -0.17622 158 HIS A C   
1271 O  O   . HIS A 163 ? 0.82359 0.66439 0.67413 0.05884  0.01767  -0.17423 158 HIS A O   
1272 C  CB  . HIS A 163 ? 0.91577 0.72226 0.75571 0.06527  0.02199  -0.19561 158 HIS A CB  
1273 C  CG  . HIS A 163 ? 1.03549 0.82037 0.87679 0.06701  0.02497  -0.20460 158 HIS A CG  
1274 N  ND1 . HIS A 163 ? 1.13672 0.90663 0.97421 0.06032  0.01704  -0.21606 158 HIS A ND1 
1275 C  CD2 . HIS A 163 ? 1.04865 0.82424 0.89538 0.07476  0.03485  -0.20378 158 HIS A CD2 
1276 C  CE1 . HIS A 163 ? 1.23131 0.98150 1.07015 0.06345  0.02268  -0.22205 158 HIS A CE1 
1277 N  NE2 . HIS A 163 ? 1.38422 1.13748 1.22901 0.07254  0.03358  -0.21466 158 HIS A NE2 
1278 N  N   . PRO A 164 ? 0.73029 0.55646 0.60422 0.06419  0.02923  -0.16779 159 PRO A N   
1279 C  CA  . PRO A 164 ? 0.78014 0.58895 0.66610 0.06720  0.03508  -0.16730 159 PRO A CA  
1280 C  C   . PRO A 164 ? 0.79006 0.57865 0.68839 0.05671  0.02930  -0.17005 159 PRO A C   
1281 O  O   . PRO A 164 ? 0.72634 0.51988 0.63366 0.04721  0.02197  -0.16773 159 PRO A O   
1282 C  CB  . PRO A 164 ? 0.67049 0.49080 0.56553 0.07340  0.04176  -0.15480 159 PRO A CB  
1283 C  CG  . PRO A 164 ? 0.71457 0.55503 0.61031 0.06632  0.03758  -0.14680 159 PRO A CG  
1284 C  CD  . PRO A 164 ? 0.75250 0.59792 0.62893 0.06632  0.03266  -0.15620 159 PRO A CD  
1285 N  N   . GLU A 165 ? 0.71678 0.48298 0.61595 0.05825  0.03299  -0.17451 160 GLU A N   
1286 C  CA  . GLU A 165 ? 0.76728 0.51243 0.67347 0.04841  0.02661  -0.17760 160 GLU A CA  
1287 C  C   . GLU A 165 ? 0.71208 0.45904 0.63805 0.04151  0.02419  -0.16701 160 GLU A C   
1288 O  O   . GLU A 165 ? 0.75434 0.49915 0.69171 0.02933  0.01712  -0.16885 160 GLU A O   
1289 C  CB  . GLU A 165 ? 0.76643 0.48429 0.66732 0.05363  0.03207  -0.18159 160 GLU A CB  
1290 C  CG  . GLU A 165 ? 1.00066 0.71936 0.88845 0.05998  0.03721  -0.19301 160 GLU A CG  
1291 C  CD  . GLU A 165 ? 1.08572 0.78026 0.97364 0.06446  0.04390  -0.19650 160 GLU A CD  
1292 O  OE1 . GLU A 165 ? 0.99277 0.66505 0.88288 0.06355  0.04038  -0.18899 160 GLU A OE1 
1293 O  OE2 . GLU A 165 ? 1.24672 0.94377 1.12914 0.07160  0.04879  -0.20639 160 GLU A OE2 
1294 N  N   . SER A 166 ? 0.65664 0.41050 0.58951 0.04849  0.03070  -0.15607 161 SER A N   
1295 C  CA  . SER A 166 ? 0.69716 0.45227 0.64982 0.04171  0.03200  -0.14491 161 SER A CA  
1296 C  C   . SER A 166 ? 0.63595 0.41262 0.59608 0.03407  0.02944  -0.14058 161 SER A C   
1297 O  O   . SER A 166 ? 0.58126 0.36056 0.55546 0.02927  0.03237  -0.13015 161 SER A O   
1298 C  CB  . SER A 166 ? 0.69132 0.44383 0.64789 0.05241  0.04097  -0.13419 161 SER A CB  
1299 O  OG  . SER A 166 ? 0.79813 0.56969 0.74745 0.06161  0.04607  -0.13092 161 SER A OG  
1300 N  N   . PHE A 167 ? 0.56531 0.35684 0.51489 0.03349  0.02382  -0.14788 162 PHE A N   
1301 C  CA  . PHE A 167 ? 0.63356 0.44760 0.58624 0.02799  0.01995  -0.14021 162 PHE A CA  
1302 C  C   . PHE A 167 ? 0.55498 0.36744 0.52646 0.01552  0.01524  -0.13797 162 PHE A C   
1303 O  O   . PHE A 167 ? 0.55171 0.37489 0.53267 0.01238  0.01744  -0.12537 162 PHE A O   
1304 C  CB  . PHE A 167 ? 0.66431 0.49108 0.59955 0.02951  0.01341  -0.14781 162 PHE A CB  
1305 C  CG  . PHE A 167 ? 0.61234 0.46083 0.54706 0.02553  0.01021  -0.13815 162 PHE A CG  
1306 C  CD1 . PHE A 167 ? 0.55643 0.40962 0.49953 0.01608  0.00121  -0.13958 162 PHE A CD1 
1307 C  CD2 . PHE A 167 ? 0.63725 0.50136 0.56419 0.03130  0.01628  -0.12800 162 PHE A CD2 
1308 C  CE1 . PHE A 167 ? 0.54072 0.41151 0.48237 0.01352  -0.00154 -0.13064 162 PHE A CE1 
1309 C  CE2 . PHE A 167 ? 0.69571 0.57672 0.62188 0.02724  0.01378  -0.11931 162 PHE A CE2 
1310 C  CZ  . PHE A 167 ? 0.55356 0.43675 0.48604 0.01889  0.00492  -0.12043 162 PHE A CZ  
1311 N  N   . ARG A 168 ? 0.60870 0.41023 0.58479 0.00828  0.00862  -0.14777 163 ARG A N   
1312 C  CA  . ARG A 168 ? 0.61484 0.41887 0.61013 -0.00388 0.00409  -0.14508 163 ARG A CA  
1313 C  C   . ARG A 168 ? 0.58122 0.37654 0.59194 -0.00599 0.01309  -0.13295 163 ARG A C   
1314 O  O   . ARG A 168 ? 0.52602 0.33137 0.54943 -0.01107 0.01441  -0.12455 163 ARG A O   
1315 C  CB  . ARG A 168 ? 0.68728 0.48305 0.68435 -0.01093 -0.00383 -0.15592 163 ARG A CB  
1316 C  CG  . ARG A 168 ? 0.87910 0.68607 0.86186 -0.01023 -0.01430 -0.16680 163 ARG A CG  
1317 C  CD  . ARG A 168 ? 0.94741 0.74124 0.91029 -0.00340 -0.01406 -0.17685 163 ARG A CD  
1318 N  NE  . ARG A 168 ? 0.86031 0.66426 0.80912 -0.00327 -0.02414 -0.18686 163 ARG A NE  
1319 C  CZ  . ARG A 168 ? 0.92075 0.72295 0.87364 -0.01049 -0.03332 -0.19650 163 ARG A CZ  
1320 N  NH1 . ARG A 168 ? 0.97515 0.76571 0.94644 -0.01940 -0.03336 -0.19804 163 ARG A NH1 
1321 N  NH2 . ARG A 168 ? 0.93345 0.74635 0.87140 -0.00846 -0.04258 -0.20448 163 ARG A NH2 
1322 N  N   . ASP A 169 ? 0.52748 0.30360 0.53554 -0.00122 0.01941  -0.13137 164 ASP A N   
1323 C  CA  . ASP A 169 ? 0.57209 0.33840 0.59180 -0.00224 0.02778  -0.11907 164 ASP A CA  
1324 C  C   . ASP A 169 ? 0.51532 0.29255 0.53489 0.00359  0.03454  -0.10693 164 ASP A C   
1325 O  O   . ASP A 169 ? 0.53040 0.30985 0.56146 -0.00090 0.03852  -0.09643 164 ASP A O   
1326 C  CB  . ASP A 169 ? 0.57696 0.32048 0.59030 0.00443  0.03259  -0.11962 164 ASP A CB  
1327 C  CG  . ASP A 169 ? 0.73783 0.46640 0.75576 -0.00401 0.02779  -0.12888 164 ASP A CG  
1328 O  OD1 . ASP A 169 ? 0.68851 0.42382 0.72084 -0.01632 0.02349  -0.13042 164 ASP A OD1 
1329 O  OD2 . ASP A 169 ? 0.81207 0.52270 0.81981 0.00193  0.02836  -0.13488 164 ASP A OD2 
1330 N  N   . VAL A 170 ? 0.50229 0.28708 0.50846 0.01370  0.03644  -0.10823 165 VAL A N   
1331 C  CA  . VAL A 170 ? 0.49930 0.29925 0.50265 0.01982  0.04082  -0.09420 165 VAL A CA  
1332 C  C   . VAL A 170 ? 0.43401 0.25485 0.44290 0.01217  0.03576  -0.08888 165 VAL A C   
1333 O  O   . VAL A 170 ? 0.44659 0.27323 0.46150 0.01143  0.03923  -0.07732 165 VAL A O   
1334 C  CB  . VAL A 170 ? 0.49449 0.30337 0.48254 0.03210  0.04263  -0.09484 165 VAL A CB  
1335 C  CG1 . VAL A 170 ? 0.45886 0.28848 0.44564 0.03627  0.04471  -0.08238 165 VAL A CG1 
1336 C  CG2 . VAL A 170 ? 0.54687 0.33470 0.53082 0.04195  0.04912  -0.09716 165 VAL A CG2 
1337 N  N   . LEU A 171 ? 0.48011 0.31163 0.48565 0.00736  0.02741  -0.09725 166 LEU A N   
1338 C  CA  . LEU A 171 ? 0.50687 0.35647 0.51702 0.00114  0.02234  -0.09239 166 LEU A CA  
1339 C  C   . LEU A 171 ? 0.42190 0.26718 0.45089 -0.00805 0.02291  -0.08909 166 LEU A C   
1340 O  O   . LEU A 171 ? 0.41888 0.27482 0.45337 -0.00994 0.02433  -0.07924 166 LEU A O   
1341 C  CB  . LEU A 171 ? 0.44665 0.30593 0.44794 -0.00093 0.01295  -0.10214 166 LEU A CB  
1342 C  CG  . LEU A 171 ? 0.42260 0.29863 0.42770 -0.00648 0.00662  -0.09815 166 LEU A CG  
1343 C  CD1 . LEU A 171 ? 0.42001 0.30828 0.42285 -0.00358 0.01128  -0.08459 166 LEU A CD1 
1344 C  CD2 . LEU A 171 ? 0.46594 0.34966 0.45759 -0.00583 -0.00240 -0.10703 166 LEU A CD2 
1345 N  N   . ASN A 172 ? 0.44581 0.27554 0.48549 -0.01410 0.02234  -0.09760 167 ASN A N   
1346 C  CA  . ASN A 172 ? 0.48921 0.31538 0.54926 -0.02357 0.02467  -0.09428 167 ASN A CA  
1347 C  C   . ASN A 172 ? 0.49000 0.30888 0.55256 -0.02003 0.03582  -0.07994 167 ASN A C   
1348 O  O   . ASN A 172 ? 0.46794 0.29416 0.54078 -0.02428 0.03851  -0.07160 167 ASN A O   
1349 C  CB  . ASN A 172 ? 0.53769 0.35309 0.60570 -0.03034 0.02139  -0.10252 167 ASN A CB  
1350 C  CG  . ASN A 172 ? 0.53824 0.36611 0.60997 -0.03667 0.00918  -0.11426 167 ASN A CG  
1351 O  OD1 . ASN A 172 ? 0.56547 0.41040 0.64271 -0.03942 0.00411  -0.11350 167 ASN A OD1 
1352 N  ND2 . ASN A 172 ? 0.56546 0.38457 0.63306 -0.03820 0.00395  -0.12517 167 ASN A ND2 
1353 N  N   . LYS A 173 ? 0.47258 0.27738 0.52467 -0.01105 0.04231  -0.07690 168 LYS A N   
1354 C  CA  . LYS A 173 ? 0.45545 0.25344 0.50668 -0.00557 0.05196  -0.06301 168 LYS A CA  
1355 C  C   . LYS A 173 ? 0.44469 0.26387 0.48902 -0.00089 0.05086  -0.05327 168 LYS A C   
1356 O  O   . LYS A 173 ? 0.41481 0.23588 0.46341 -0.00141 0.05574  -0.04283 168 LYS A O   
1357 C  CB  . LYS A 173 ? 0.54123 0.32338 0.58093 0.00495  0.05672  -0.06151 168 LYS A CB  
1358 C  CG  . LYS A 173 ? 0.69733 0.46878 0.73666 0.00944  0.06535  -0.04780 168 LYS A CG  
1359 C  CD  . LYS A 173 ? 0.85610 0.61203 0.88445 0.02054  0.06873  -0.04685 168 LYS A CD  
1360 C  CE  . LYS A 173 ? 0.98211 0.72743 1.00831 0.02551  0.07669  -0.03294 168 LYS A CE  
1361 N  NZ  . LYS A 173 ? 1.05779 0.78787 1.07370 0.03701  0.07932  -0.03180 168 LYS A NZ  
1362 N  N   . TYR A 174 ? 0.43378 0.26843 0.46712 0.00342  0.04490  -0.05679 169 TYR A N   
1363 C  CA  . TYR A 174 ? 0.39236 0.24660 0.42040 0.00621  0.04335  -0.04893 169 TYR A CA  
1364 C  C   . TYR A 174 ? 0.37833 0.24279 0.41635 -0.00251 0.04014  -0.04669 169 TYR A C   
1365 O  O   . TYR A 174 ? 0.42745 0.29846 0.46658 -0.00162 0.04291  -0.03740 169 TYR A O   
1366 C  CB  . TYR A 174 ? 0.40919 0.27677 0.42517 0.01063  0.03854  -0.05377 169 TYR A CB  
1367 C  CG  . TYR A 174 ? 0.38327 0.26977 0.39500 0.01204  0.03707  -0.04654 169 TYR A CG  
1368 C  CD1 . TYR A 174 ? 0.38452 0.27513 0.39332 0.01900  0.04138  -0.03795 169 TYR A CD1 
1369 C  CD2 . TYR A 174 ? 0.33644 0.23591 0.34686 0.00664  0.03096  -0.04855 169 TYR A CD2 
1370 C  CE1 . TYR A 174 ? 0.37677 0.28416 0.38286 0.01923  0.03951  -0.03261 169 TYR A CE1 
1371 C  CE2 . TYR A 174 ? 0.28887 0.20288 0.29576 0.00716  0.03007  -0.04217 169 TYR A CE2 
1372 C  CZ  . TYR A 174 ? 0.32905 0.24701 0.33447 0.01281  0.03431  -0.03478 169 TYR A CZ  
1373 O  OH  . TYR A 174 ? 0.34281 0.27476 0.34563 0.01239  0.03287  -0.02987 169 TYR A OH  
1374 N  N   . ALA A 175 ? 0.41500 0.28119 0.46027 -0.01024 0.03389  -0.05576 170 ALA A N   
1375 C  CA  . ALA A 175 ? 0.41684 0.29461 0.47258 -0.01736 0.02998  -0.05457 170 ALA A CA  
1376 C  C   . ALA A 175 ? 0.40370 0.27485 0.47389 -0.02159 0.03730  -0.04776 170 ALA A C   
1377 O  O   . ALA A 175 ? 0.38934 0.27112 0.46539 -0.02392 0.03742  -0.04227 170 ALA A O   
1378 C  CB  . ALA A 175 ? 0.42422 0.30563 0.48528 -0.02357 0.02083  -0.06663 170 ALA A CB  
1379 N  N   . SER A 176 ? 0.44399 0.29663 0.51949 -0.02237 0.04423  -0.04779 171 SER A N   
1380 C  CA  . SER A 176 ? 0.39524 0.23976 0.48236 -0.02574 0.05356  -0.03945 171 SER A CA  
1381 C  C   . SER A 176 ? 0.47991 0.32869 0.55624 -0.01777 0.05905  -0.02657 171 SER A C   
1382 O  O   . SER A 176 ? 0.42300 0.27618 0.50605 -0.02011 0.06358  -0.01949 171 SER A O   
1383 C  CB  . SER A 176 ? 0.45429 0.27784 0.54485 -0.02688 0.05991  -0.04021 171 SER A CB  
1384 O  OG  . SER A 176 ? 0.63600 0.45942 0.73616 -0.03478 0.05322  -0.05197 171 SER A OG  
1385 N  N   . GLY A 177 ? 0.43583 0.28460 0.49572 -0.00801 0.05849  -0.02406 172 GLY A N   
1386 C  CA  . GLY A 177 ? 0.43686 0.29144 0.48644 -0.00020 0.06182  -0.01347 172 GLY A CA  
1387 C  C   . GLY A 177 ? 0.41996 0.29440 0.46854 -0.00200 0.05615  -0.01238 172 GLY A C   
1388 O  O   . GLY A 177 ? 0.37262 0.25093 0.42007 -0.00037 0.05966  -0.00462 172 GLY A O   
1389 N  N   . THR A 178 ? 0.38097 0.26680 0.42833 -0.00473 0.04766  -0.01999 173 THR A N   
1390 C  CA  . THR A 178 ? 0.32946 0.23129 0.37486 -0.00611 0.04264  -0.01854 173 THR A CA  
1391 C  C   . THR A 178 ? 0.30966 0.21475 0.36859 -0.01280 0.04311  -0.01785 173 THR A C   
1392 O  O   . THR A 178 ? 0.31854 0.23251 0.37621 -0.01215 0.04267  -0.01337 173 THR A O   
1393 C  CB  . THR A 178 ? 0.40848 0.31974 0.44712 -0.00666 0.03457  -0.02547 173 THR A CB  
1394 O  OG1 . THR A 178 ? 0.34101 0.24895 0.38621 -0.01192 0.03027  -0.03448 173 THR A OG1 
1395 C  CG2 . THR A 178 ? 0.32744 0.23869 0.35429 0.00041  0.03550  -0.02546 173 THR A CG2 
1396 N  N   . LYS A 179 ? 0.31988 0.21810 0.39286 -0.01916 0.04436  -0.02259 174 LYS A N   
1397 C  CA  . LYS A 179 ? 0.36529 0.26890 0.45457 -0.02547 0.04580  -0.02194 174 LYS A CA  
1398 C  C   . LYS A 179 ? 0.37932 0.27819 0.46956 -0.02306 0.05636  -0.01138 174 LYS A C   
1399 O  O   . LYS A 179 ? 0.40265 0.31059 0.49881 -0.02421 0.05779  -0.00798 174 LYS A O   
1400 C  CB  . LYS A 179 ? 0.40049 0.29899 0.50721 -0.03379 0.04466  -0.03044 174 LYS A CB  
1401 C  CG  . LYS A 179 ? 0.46357 0.37223 0.59105 -0.04090 0.04474  -0.03167 174 LYS A CG  
1402 C  CD  . LYS A 179 ? 0.52776 0.43270 0.67460 -0.05006 0.04261  -0.04162 174 LYS A CD  
1403 C  CE  . LYS A 179 ? 0.55438 0.47218 0.72580 -0.05735 0.04328  -0.04306 174 LYS A CE  
1404 N  NZ  . LYS A 179 ? 0.55464 0.47281 0.74296 -0.06535 0.03977  -0.05260 174 LYS A NZ  
1405 N  N   . ARG A 180 ? 0.38286 0.26698 0.46595 -0.01863 0.06407  -0.00594 175 ARG A N   
1406 C  CA  . ARG A 180 ? 0.37895 0.25747 0.45776 -0.01425 0.07413  0.00506  175 ARG A CA  
1407 C  C   . ARG A 180 ? 0.39922 0.28913 0.46354 -0.00723 0.07096  0.00956  175 ARG A C   
1408 O  O   . ARG A 180 ? 0.35725 0.25067 0.42134 -0.00586 0.07578  0.01553  175 ARG A O   
1409 C  CB  . ARG A 180 ? 0.43207 0.29110 0.50292 -0.00901 0.08196  0.01025  175 ARG A CB  
1410 C  CG  . ARG A 180 ? 0.46951 0.32216 0.52841 -0.00095 0.09108  0.02246  175 ARG A CG  
1411 C  CD  . ARG A 180 ? 0.58549 0.41890 0.63274 0.00700  0.09704  0.02793  175 ARG A CD  
1412 N  NE  . ARG A 180 ? 0.60142 0.43781 0.63899 0.01287  0.08871  0.02245  175 ARG A NE  
1413 C  CZ  . ARG A 180 ? 0.57760 0.42666 0.60194 0.02083  0.08263  0.02346  175 ARG A CZ  
1414 N  NH1 . ARG A 180 ? 0.53658 0.39485 0.55371 0.02442  0.08296  0.02919  175 ARG A NH1 
1415 N  NH2 . ARG A 180 ? 0.46672 0.31988 0.48569 0.02497  0.07619  0.01789  175 ARG A NH2 
1416 N  N   . ILE A 181 ? 0.38491 0.28079 0.43755 -0.00305 0.06322  0.00624  176 ILE A N   
1417 C  CA  . ILE A 181 ? 0.35181 0.25886 0.39276 0.00185  0.05920  0.00881  176 ILE A CA  
1418 C  C   . ILE A 181 ? 0.35187 0.27020 0.39983 -0.00300 0.05523  0.00648  176 ILE A C   
1419 O  O   . ILE A 181 ? 0.34157 0.26446 0.38467 -0.00016 0.05668  0.01068  176 ILE A O   
1420 C  CB  . ILE A 181 ? 0.32125 0.23358 0.35210 0.00543  0.05241  0.00493  176 ILE A CB  
1421 C  CG1 . ILE A 181 ? 0.34913 0.25132 0.37284 0.01254  0.05649  0.00776  176 ILE A CG1 
1422 C  CG2 . ILE A 181 ? 0.33368 0.25811 0.35563 0.00800  0.04771  0.00616  176 ILE A CG2 
1423 C  CD1 . ILE A 181 ? 0.35920 0.26783 0.37612 0.01615  0.05102  0.00324  176 ILE A CD1 
1424 N  N   . ARG A 182 ? 0.31403 0.23677 0.37228 -0.00935 0.04959  -0.00071 177 ARG A N   
1425 C  CA  . ARG A 182 ? 0.34131 0.27447 0.40704 -0.01278 0.04534  -0.00294 177 ARG A CA  
1426 C  C   . ARG A 182 ? 0.31550 0.24893 0.39025 -0.01314 0.05321  0.00229  177 ARG A C   
1427 O  O   . ARG A 182 ? 0.30987 0.24987 0.38159 -0.01070 0.05279  0.00461  177 ARG A O   
1428 C  CB  . ARG A 182 ? 0.29724 0.23403 0.37426 -0.01880 0.03864  -0.01137 177 ARG A CB  
1429 C  CG  . ARG A 182 ? 0.31383 0.26190 0.40013 -0.02115 0.03363  -0.01377 177 ARG A CG  
1430 C  CD  . ARG A 182 ? 0.32900 0.28085 0.43185 -0.02727 0.02871  -0.02185 177 ARG A CD  
1431 N  NE  . ARG A 182 ? 0.35421 0.30268 0.47559 -0.03219 0.03661  -0.02129 177 ARG A NE  
1432 C  CZ  . ARG A 182 ? 0.37397 0.32620 0.51447 -0.03896 0.03366  -0.02866 177 ARG A CZ  
1433 N  NH1 . ARG A 182 ? 0.40043 0.35992 0.54222 -0.04044 0.02204  -0.03751 177 ARG A NH1 
1434 N  NH2 . ARG A 182 ? 0.37368 0.32230 0.53230 -0.04442 0.04263  -0.02725 177 ARG A NH2 
1435 N  N   . ASP A 183 ? 0.33687 0.26225 0.42252 -0.01612 0.06132  0.00422  178 ASP A N   
1436 C  CA  . ASP A 183 ? 0.34548 0.27136 0.44094 -0.01697 0.07091  0.00974  178 ASP A CA  
1437 C  C   . ASP A 183 ? 0.40129 0.32417 0.47962 -0.00868 0.07671  0.01814  178 ASP A C   
1438 O  O   . ASP A 183 ? 0.39640 0.32549 0.47611 -0.00687 0.08010  0.02093  178 ASP A O   
1439 C  CB  . ASP A 183 ? 0.39228 0.30767 0.50221 -0.02258 0.07991  0.01088  178 ASP A CB  
1440 C  CG  . ASP A 183 ? 0.45954 0.38059 0.59082 -0.03193 0.07424  0.00125  178 ASP A CG  
1441 O  OD1 . ASP A 183 ? 0.44343 0.37766 0.57798 -0.03297 0.06376  -0.00527 178 ASP A OD1 
1442 O  OD2 . ASP A 183 ? 0.47030 0.38184 0.61455 -0.03803 0.08000  0.00002  178 ASP A OD2 
1443 N  N   . ASP A 184 ? 0.34397 0.25792 0.40579 -0.00274 0.07757  0.02171  179 ASP A N   
1444 C  CA  . ASP A 184 ? 0.41068 0.32248 0.45488 0.00597  0.08152  0.02876  179 ASP A CA  
1445 C  C   . ASP A 184 ? 0.42137 0.34451 0.45762 0.00837  0.07372  0.02584  179 ASP A C   
1446 O  O   . ASP A 184 ? 0.36434 0.28905 0.39315 0.01294  0.07741  0.02956  179 ASP A O   
1447 C  CB  . ASP A 184 ? 0.39440 0.29709 0.42355 0.01271  0.08156  0.03188  179 ASP A CB  
1448 C  CG  . ASP A 184 ? 0.50641 0.39310 0.53796 0.01332  0.09209  0.03784  179 ASP A CG  
1449 O  OD1 . ASP A 184 ? 0.49678 0.37961 0.54175 0.00783  0.10064  0.04023  179 ASP A OD1 
1450 O  OD2 . ASP A 184 ? 0.61696 0.49485 0.63766 0.01940  0.09212  0.04019  179 ASP A OD2 
1451 N  N   . ILE A 185 ? 0.36048 0.29022 0.39699 0.00554  0.06347  0.01923  180 ILE A N   
1452 C  CA  . ILE A 185 ? 0.32015 0.25797 0.34917 0.00695  0.05651  0.01663  180 ILE A CA  
1453 C  C   . ILE A 185 ? 0.35661 0.29991 0.39532 0.00484  0.05748  0.01569  180 ILE A C   
1454 O  O   . ILE A 185 ? 0.33568 0.28107 0.36661 0.00876  0.05759  0.01680  180 ILE A O   
1455 C  CB  . ILE A 185 ? 0.29439 0.23656 0.32135 0.00402  0.04704  0.01087  180 ILE A CB  
1456 C  CG1 . ILE A 185 ? 0.34197 0.28148 0.35907 0.00776  0.04633  0.01171  180 ILE A CG1 
1457 C  CG2 . ILE A 185 ? 0.30836 0.25653 0.32958 0.00393  0.04083  0.00850  180 ILE A CG2 
1458 C  CD1 . ILE A 185 ? 0.38241 0.32292 0.38591 0.01447  0.04679  0.01509  180 ILE A CD1 
1459 N  N   . ILE A 186 ? 0.34330 0.28958 0.39955 -0.00088 0.05773  0.01287  181 ILE A N   
1460 C  CA  . ILE A 186 ? 0.40882 0.36306 0.47612 -0.00190 0.05752  0.01132  181 ILE A CA  
1461 C  C   . ILE A 186 ? 0.38360 0.33688 0.45317 0.00147  0.06877  0.01707  181 ILE A C   
1462 O  O   . ILE A 186 ? 0.35577 0.31493 0.42764 0.00411  0.06965  0.01689  181 ILE A O   
1463 C  CB  . ILE A 186 ? 0.42089 0.38135 0.50787 -0.00850 0.05352  0.00580  181 ILE A CB  
1464 C  CG1 . ILE A 186 ? 0.59263 0.54811 0.69258 -0.01306 0.06131  0.00708  181 ILE A CG1 
1465 C  CG2 . ILE A 186 ? 0.47629 0.43790 0.55742 -0.01036 0.04230  0.00016  181 ILE A CG2 
1466 C  CD1 . ILE A 186 ? 0.80485 0.76619 0.92453 -0.02024 0.05658  0.00012  181 ILE A CD1 
1467 N  N   . GLN A 187 ? 0.36199 0.30703 0.43005 0.00216  0.07819  0.02257  182 GLN A N   
1468 C  CA  . GLN A 187 ? 0.36628 0.30889 0.43206 0.00651  0.09028  0.02934  182 GLN A CA  
1469 C  C   . GLN A 187 ? 0.41589 0.35675 0.45904 0.01523  0.08902  0.03139  182 GLN A C   
1470 O  O   . GLN A 187 ? 0.38250 0.32623 0.42347 0.01945  0.09445  0.03323  182 GLN A O   
1471 C  CB  . GLN A 187 ? 0.40253 0.33369 0.46881 0.00585  0.10109  0.03590  182 GLN A CB  
1472 C  CG  . GLN A 187 ? 0.48894 0.42035 0.57965 -0.00367 0.10449  0.03366  182 GLN A CG  
1473 C  CD  . GLN A 187 ? 0.66900 0.58540 0.75895 -0.00433 0.11647  0.04094  182 GLN A CD  
1474 O  OE1 . GLN A 187 ? 0.66244 0.56786 0.74196 -0.00270 0.11408  0.04170  182 GLN A OE1 
1475 N  NE2 . GLN A 187 ? 0.65367 0.56897 0.75461 -0.00627 0.13023  0.04675  182 GLN A NE2 
1476 N  N   . ALA A 188 ? 0.36009 0.29693 0.38688 0.01812  0.08191  0.03039  183 ALA A N   
1477 C  CA  . ALA A 188 ? 0.36867 0.30505 0.37537 0.02530  0.07854  0.03030  183 ALA A CA  
1478 C  C   . ALA A 188 ? 0.39226 0.33521 0.40051 0.02439  0.07146  0.02452  183 ALA A C   
1479 O  O   . ALA A 188 ? 0.38882 0.33120 0.38574 0.03001  0.07250  0.02437  183 ALA A O   
1480 C  CB  . ALA A 188 ? 0.38524 0.31900 0.37875 0.02747  0.07163  0.02939  183 ALA A CB  
1481 N  N   . MET A 189 ? 0.32698 0.27479 0.34742 0.01810  0.06413  0.01964  184 MET A N   
1482 C  CA  . MET A 189 ? 0.32098 0.27277 0.34218 0.01801  0.05776  0.01514  184 MET A CA  
1483 C  C   . MET A 189 ? 0.36824 0.32418 0.39934 0.02059  0.06432  0.01611  184 MET A C   
1484 O  O   . MET A 189 ? 0.35324 0.30890 0.37753 0.02503  0.06295  0.01425  184 MET A O   
1485 C  CB  . MET A 189 ? 0.34915 0.30434 0.37894 0.01193  0.04892  0.01075  184 MET A CB  
1486 C  CG  . MET A 189 ? 0.31004 0.26259 0.32989 0.00987  0.04292  0.00932  184 MET A CG  
1487 S  SD  . MET A 189 ? 0.37975 0.33542 0.40594 0.00394  0.03381  0.00468  184 MET A SD  
1488 C  CE  . MET A 189 ? 0.42004 0.37560 0.44309 0.00600  0.02928  0.00282  184 MET A CE  
1489 N  N   . ALA A 190 ? 0.35317 0.31304 0.40134 0.01779  0.07189  0.01861  185 ALA A N   
1490 C  CA  . ALA A 190 ? 0.42228 0.38874 0.48257 0.02027  0.07960  0.01971  185 ALA A CA  
1491 C  C   . ALA A 190 ? 0.46201 0.42347 0.50585 0.02847  0.08820  0.02373  185 ALA A C   
1492 O  O   . ALA A 190 ? 0.45077 0.41573 0.49456 0.03359  0.09064  0.02245  185 ALA A O   
1493 C  CB  . ALA A 190 ? 0.44969 0.42170 0.53317 0.01434  0.08726  0.02165  185 ALA A CB  
1494 N  N   . LYS A 191 ? 0.43221 0.38519 0.46059 0.03094  0.09259  0.02835  186 LYS A N   
1495 C  CA  . LYS A 191 ? 0.47864 0.42628 0.48746 0.03991  0.09974  0.03186  186 LYS A CA  
1496 C  C   . LYS A 191 ? 0.50229 0.44769 0.49385 0.04465  0.09039  0.02610  186 LYS A C   
1497 O  O   . LYS A 191 ? 0.45841 0.40259 0.43997 0.05176  0.09464  0.02552  186 LYS A O   
1498 C  CB  . LYS A 191 ? 0.46769 0.40641 0.46208 0.04266  0.10489  0.03820  186 LYS A CB  
1499 C  CG  . LYS A 191 ? 0.62326 0.55983 0.63164 0.03885  0.11698  0.04514  186 LYS A CG  
1500 C  CD  . LYS A 191 ? 0.65529 0.58037 0.64664 0.04279  0.12027  0.05154  186 LYS A CD  
1501 C  CE  . LYS A 191 ? 0.71343 0.63231 0.71715 0.03886  0.13348  0.05919  186 LYS A CE  
1502 N  NZ  . LYS A 191 ? 0.85345 0.75941 0.84084 0.04307  0.13476  0.06509  186 LYS A NZ  
1503 N  N   . LEU A 192 ? 0.41779 0.36204 0.40568 0.04064  0.07825  0.02154  187 LEU A N   
1504 C  CA  . LEU A 192 ? 0.39371 0.33486 0.36790 0.04314  0.06951  0.01563  187 LEU A CA  
1505 C  C   . LEU A 192 ? 0.44523 0.38860 0.42735 0.04443  0.06882  0.01209  187 LEU A C   
1506 O  O   . LEU A 192 ? 0.48081 0.41924 0.45003 0.04970  0.06698  0.00836  187 LEU A O   
1507 C  CB  . LEU A 192 ? 0.37763 0.31833 0.35047 0.03703  0.05824  0.01203  187 LEU A CB  
1508 C  CG  . LEU A 192 ? 0.37377 0.31303 0.33634 0.03738  0.05624  0.01369  187 LEU A CG  
1509 C  CD1 . LEU A 192 ? 0.34266 0.28387 0.30767 0.03086  0.04617  0.00957  187 LEU A CD1 
1510 C  CD2 . LEU A 192 ? 0.45137 0.38690 0.39344 0.04508  0.05638  0.01287  187 LEU A CD2 
1511 N  N   . LEU A 193 ? 0.39726 0.34787 0.40035 0.04028  0.06970  0.01260  188 LEU A N   
1512 C  CA  . LEU A 193 ? 0.45735 0.41186 0.47031 0.04252  0.06828  0.00953  188 LEU A CA  
1513 C  C   . LEU A 193 ? 0.42097 0.38127 0.44174 0.04854  0.08019  0.01202  188 LEU A C   
1514 O  O   . LEU A 193 ? 0.41675 0.38198 0.44706 0.05211  0.08001  0.00950  188 LEU A O   
1515 C  CB  . LEU A 193 ? 0.42800 0.38949 0.45970 0.03597  0.06169  0.00805  188 LEU A CB  
1516 C  CG  . LEU A 193 ? 0.36491 0.32106 0.38882 0.03054  0.05068  0.00561  188 LEU A CG  
1517 C  CD1 . LEU A 193 ? 0.33613 0.29936 0.37652 0.02434  0.04607  0.00494  188 LEU A CD1 
1518 C  CD2 . LEU A 193 ? 0.39954 0.34779 0.41152 0.03337  0.04372  0.00189  188 LEU A CD2 
1519 N  N   . GLU A 194 ? 0.45933 0.41902 0.47589 0.05043  0.09104  0.01731  189 GLU A N   
1520 C  CA  . GLU A 194 ? 0.52502 0.49061 0.54930 0.05556  0.10501  0.02095  189 GLU A CA  
1521 C  C   . GLU A 194 ? 0.50854 0.48840 0.56390 0.05093  0.10744  0.02065  189 GLU A C   
1522 O  O   . GLU A 194 ? 0.46010 0.44859 0.52668 0.05585  0.11419  0.02011  189 GLU A O   
1523 C  CB  . GLU A 194 ? 0.52512 0.48639 0.53311 0.06592  0.10742  0.01798  189 GLU A CB  
1524 C  CG  . GLU A 194 ? 0.65174 0.60010 0.62929 0.07060  0.10372  0.01654  189 GLU A CG  
1525 C  CD  . GLU A 194 ? 0.75462 0.69803 0.71470 0.08161  0.10883  0.01371  189 GLU A CD  
1526 O  OE1 . GLU A 194 ? 0.84112 0.78953 0.80503 0.08727  0.12257  0.01771  189 GLU A OE1 
1527 O  OE2 . GLU A 194 ? 0.93930 0.87354 0.88209 0.08440  0.09958  0.00712  189 GLU A OE2 
1528 N  N   . LEU A 195 ? 0.43367 0.41696 0.50335 0.04184  0.10139  0.02018  190 LEU A N   
1529 C  CA  . LEU A 195 ? 0.43065 0.42811 0.53083 0.03591  0.10296  0.01929  190 LEU A CA  
1530 C  C   . LEU A 195 ? 0.56976 0.56697 0.67990 0.02948  0.11356  0.02483  190 LEU A C   
1531 O  O   . LEU A 195 ? 0.54546 0.53039 0.63773 0.02936  0.11613  0.02903  190 LEU A O   
1532 C  CB  . LEU A 195 ? 0.41867 0.41921 0.52688 0.03055  0.08778  0.01370  190 LEU A CB  
1533 C  CG  . LEU A 195 ? 0.34869 0.34620 0.44595 0.03624  0.07697  0.00914  190 LEU A CG  
1534 C  CD1 . LEU A 195 ? 0.44385 0.44060 0.54262 0.03073  0.06323  0.00549  190 LEU A CD1 
1535 C  CD2 . LEU A 195 ? 0.39120 0.40021 0.50327 0.04296  0.07996  0.00720  190 LEU A CD2 
1536 N  N   . ASP A 196 ? 0.44329 0.45404 0.58282 0.02429  0.11969  0.02469  191 ASP A N   
1537 C  CA  . ASP A 196 ? 0.66552 0.67477 0.81776 0.01666  0.13054  0.02969  191 ASP A CA  
1538 C  C   . ASP A 196 ? 0.76313 0.76031 0.90561 0.01076  0.12248  0.02930  191 ASP A C   
1539 O  O   . ASP A 196 ? 0.70792 0.70759 0.85390 0.00717  0.10850  0.02296  191 ASP A O   
1540 C  CB  . ASP A 196 ? 0.57556 0.60315 0.76548 0.00934  0.13408  0.02670  191 ASP A CB  
1541 C  CG  . ASP A 196 ? 0.85273 0.87676 1.05845 -0.00138 0.14249  0.02996  191 ASP A CG  
1542 O  OD1 . ASP A 196 ? 0.95525 0.97026 1.15412 -0.00066 0.15798  0.03834  191 ASP A OD1 
1543 O  OD2 . ASP A 196 ? 0.85493 0.88347 1.07800 -0.01014 0.13327  0.02400  191 ASP A OD2 
1544 N  N   . GLU A 197 ? 0.84924 0.83288 0.97801 0.01092  0.13177  0.03645  192 GLU A N   
1545 C  CA  . GLU A 197 ? 0.89959 0.87064 1.01551 0.00792  0.12495  0.03662  192 GLU A CA  
1546 C  C   . GLU A 197 ? 0.83628 0.81188 0.97388 -0.00233 0.11725  0.03066  192 GLU A C   
1547 O  O   . GLU A 197 ? 0.82294 0.79140 0.95067 -0.00408 0.10766  0.02789  192 GLU A O   
1548 C  CB  . GLU A 197 ? 0.99727 0.95365 1.09933 0.01018  0.13791  0.04607  192 GLU A CB  
1549 C  CG  . GLU A 197 ? 1.11630 1.07239 1.24103 0.00268  0.15232  0.05081  192 GLU A CG  
1550 C  CD  . GLU A 197 ? 1.19838 1.13583 1.30593 0.00546  0.16280  0.06027  192 GLU A CD  
1551 O  OE1 . GLU A 197 ? 1.26963 1.19987 1.35183 0.01577  0.16787  0.06631  192 GLU A OE1 
1552 O  OE2 . GLU A 197 ? 1.18314 1.11274 1.29989 -0.00116 0.16264  0.05989  192 GLU A OE2 
1553 N  N   . ASP A 198 ? 0.80810 0.79651 0.97533 -0.00888 0.12096  0.02789  193 ASP A N   
1554 C  CA  . ASP A 198 ? 0.86820 0.86291 1.05737 -0.01848 0.11244  0.02041  193 ASP A CA  
1555 C  C   . ASP A 198 ? 0.71421 0.72585 0.91581 -0.01784 0.09926  0.01188  193 ASP A C   
1556 O  O   . ASP A 198 ? 0.78707 0.80944 1.01255 -0.02513 0.09345  0.00506  193 ASP A O   
1557 C  CB  . ASP A 198 ? 0.89022 0.88756 1.10674 -0.02778 0.12494  0.02218  193 ASP A CB  
1558 C  CG  . ASP A 198 ? 0.91832 0.89550 1.12178 -0.02851 0.13772  0.03117  193 ASP A CG  
1559 O  OD1 . ASP A 198 ? 0.86602 0.82900 1.04088 -0.02190 0.13508  0.03496  193 ASP A OD1 
1560 O  OD2 . ASP A 198 ? 0.80783 0.78260 1.02264 -0.03281 0.14525  0.03268  193 ASP A OD2 
1561 N  N   . TYR A 199 ? 0.85246 0.86600 1.03800 -0.00889 0.09412  0.01185  194 TYR A N   
1562 C  CA  . TYR A 199 ? 0.65437 0.68196 0.84996 -0.00660 0.08235  0.00499  194 TYR A CA  
1563 C  C   . TYR A 199 ? 0.47814 0.50487 0.67242 -0.01089 0.06717  -0.00172 194 TYR A C   
1564 O  O   . TYR A 199 ? 0.48151 0.52183 0.69372 -0.01285 0.05820  -0.00836 194 TYR A O   
1565 C  CB  . TYR A 199 ? 0.67714 0.70186 0.85229 0.00393  0.08008  0.00654  194 TYR A CB  
1566 C  CG  . TYR A 199 ? 0.52739 0.56207 0.70801 0.00760  0.06715  0.00046  194 TYR A CG  
1567 C  CD1 . TYR A 199 ? 0.63353 0.68631 0.83880 0.00966  0.06815  -0.00242 194 TYR A CD1 
1568 C  CD2 . TYR A 199 ? 0.53996 0.56619 0.70147 0.00938  0.05434  -0.00203 194 TYR A CD2 
1569 C  CE1 . TYR A 199 ? 0.58830 0.64972 0.79760 0.01467  0.05588  -0.00745 194 TYR A CE1 
1570 C  CE2 . TYR A 199 ? 0.49706 0.53010 0.66136 0.01363  0.04308  -0.00639 194 TYR A CE2 
1571 C  CZ  . TYR A 199 ? 0.59580 0.64610 0.78340 0.01689  0.04347  -0.00902 194 TYR A CZ  
1572 O  OH  . TYR A 199 ? 0.46474 0.52182 0.65470 0.02286  0.03198  -0.01289 194 TYR A OH  
1573 N  N   . PHE A 200 ? 0.59403 0.60584 0.76672 -0.01153 0.06397  -0.00029 195 PHE A N   
1574 C  CA  . PHE A 200 ? 0.47894 0.48930 0.64797 -0.01487 0.05095  -0.00635 195 PHE A CA  
1575 C  C   . PHE A 200 ? 0.51969 0.53023 0.70596 -0.02404 0.05178  -0.01023 195 PHE A C   
1576 O  O   . PHE A 200 ? 0.54463 0.55927 0.73605 -0.02739 0.04073  -0.01757 195 PHE A O   
1577 C  CB  . PHE A 200 ? 0.51079 0.50714 0.65100 -0.01143 0.04734  -0.00381 195 PHE A CB  
1578 C  CG  . PHE A 200 ? 0.47493 0.46948 0.59848 -0.00376 0.04539  -0.00145 195 PHE A CG  
1579 C  CD1 . PHE A 200 ? 0.39776 0.39622 0.51774 -0.00086 0.03477  -0.00509 195 PHE A CD1 
1580 C  CD2 . PHE A 200 ? 0.57406 0.56164 0.68435 0.00093  0.05402  0.00421  195 PHE A CD2 
1581 C  CE1 . PHE A 200 ? 0.42837 0.42243 0.53323 0.00567  0.03336  -0.00321 195 PHE A CE1 
1582 C  CE2 . PHE A 200 ? 0.57150 0.55618 0.66659 0.00748  0.05167  0.00492  195 PHE A CE2 
1583 C  CZ  . PHE A 200 ? 0.41727 0.40449 0.51036 0.00938  0.04160  0.00116  195 PHE A CZ  
1584 N  N   . LEU A 201 ? 0.64005 0.64510 0.83458 -0.02795 0.06491  -0.00556 196 LEU A N   
1585 C  CA  . LEU A 201 ? 0.61756 0.61915 0.82822 -0.03732 0.06686  -0.00918 196 LEU A CA  
1586 C  C   . LEU A 201 ? 0.53795 0.55740 0.77946 -0.04387 0.06114  -0.01791 196 LEU A C   
1587 O  O   . LEU A 201 ? 0.52056 0.53942 0.77232 -0.05098 0.05469  -0.02551 196 LEU A O   
1588 C  CB  . LEU A 201 ? 0.60422 0.59440 0.81675 -0.03960 0.08376  -0.00084 196 LEU A CB  
1589 C  CG  . LEU A 201 ? 0.66843 0.63992 0.85141 -0.03359 0.08799  0.00661  196 LEU A CG  
1590 C  CD1 . LEU A 201 ? 0.75701 0.71738 0.94018 -0.03388 0.10522  0.01615  196 LEU A CD1 
1591 C  CD2 . LEU A 201 ? 0.68933 0.65070 0.86295 -0.03594 0.07941  0.00178  196 LEU A CD2 
1592 N  N   . ASP A 202 ? 0.56486 0.60101 0.82167 -0.04104 0.06277  -0.01778 197 ASP A N   
1593 C  CA  . ASP A 202 ? 0.44486 0.50167 0.73331 -0.04629 0.05626  -0.02664 197 ASP A CA  
1594 C  C   . ASP A 202 ? 0.49359 0.55553 0.77639 -0.04479 0.03716  -0.03594 197 ASP A C   
1595 O  O   . ASP A 202 ? 0.47600 0.54684 0.77851 -0.05187 0.02930  -0.04541 197 ASP A O   
1596 C  CB  . ASP A 202 ? 0.54043 0.61510 0.84424 -0.04099 0.06141  -0.02435 197 ASP A CB  
1597 C  CG  . ASP A 202 ? 0.59876 0.68320 0.93410 -0.04887 0.07628  -0.02271 197 ASP A CG  
1598 O  OD1 . ASP A 202 ? 0.58436 0.65440 0.91814 -0.05629 0.08325  -0.02083 197 ASP A OD1 
1599 O  OD2 . ASP A 202 ? 0.61881 0.72167 0.97216 -0.04556 0.07953  -0.02294 197 ASP A OD2 
1600 N  N   . ARG A 203 ? 0.39946 0.45543 0.65502 -0.03571 0.02963  -0.03359 198 ARG A N   
1601 C  CA  . ARG A 203 ? 0.43427 0.49306 0.67998 -0.03296 0.01284  -0.04062 198 ARG A CA  
1602 C  C   . ARG A 203 ? 0.42180 0.46540 0.65107 -0.03700 0.00867  -0.04347 198 ARG A C   
1603 O  O   . ARG A 203 ? 0.39748 0.44117 0.61454 -0.03447 -0.00410 -0.04876 198 ARG A O   
1604 C  CB  . ARG A 203 ? 0.43208 0.48901 0.65574 -0.02208 0.00789  -0.03626 198 ARG A CB  
1605 C  CG  . ARG A 203 ? 0.47611 0.55088 0.71686 -0.01616 0.00636  -0.03694 198 ARG A CG  
1606 C  CD  . ARG A 203 ? 0.53045 0.59799 0.74982 -0.00596 0.00813  -0.03020 198 ARG A CD  
1607 N  NE  . ARG A 203 ? 0.52833 0.61202 0.76454 0.00076  0.00818  -0.03076 198 ARG A NE  
1608 C  CZ  . ARG A 203 ? 0.54961 0.64162 0.80317 0.00084  0.02077  -0.02782 198 ARG A CZ  
1609 N  NH1 . ARG A 203 ? 0.61104 0.69527 0.86565 -0.00525 0.03456  -0.02322 198 ARG A NH1 
1610 N  NH2 . ARG A 203 ? 0.67502 0.78342 0.94465 0.00803  0.01996  -0.02918 198 ARG A NH2 
1611 N  N   . LEU A 204 ? 0.43339 0.46353 0.66107 -0.04226 0.01951  -0.03986 199 LEU A N   
1612 C  CA  . LEU A 204 ? 0.43207 0.44778 0.64647 -0.04557 0.01674  -0.04298 199 LEU A CA  
1613 C  C   . LEU A 204 ? 0.46572 0.48141 0.70297 -0.05584 0.01774  -0.05062 199 LEU A C   
1614 O  O   . LEU A 204 ? 0.41469 0.41740 0.64267 -0.05869 0.01583  -0.05439 199 LEU A O   
1615 C  CB  . LEU A 204 ? 0.45744 0.45561 0.64987 -0.04234 0.02693  -0.03357 199 LEU A CB  
1616 C  CG  . LEU A 204 ? 0.45335 0.45000 0.62142 -0.03350 0.02339  -0.02848 199 LEU A CG  
1617 C  CD1 . LEU A 204 ? 0.46392 0.44668 0.61331 -0.03024 0.03248  -0.02024 199 LEU A CD1 
1618 C  CD2 . LEU A 204 ? 0.41646 0.41342 0.57069 -0.03155 0.01021  -0.03442 199 LEU A CD2 
1619 N  N   . ASN A 205 ? 0.47307 0.50302 0.74086 -0.06162 0.02094  -0.05352 200 ASN A N   
1620 C  CA  . ASN A 205 ? 0.44415 0.47476 0.73589 -0.07255 0.02142  -0.06178 200 ASN A CA  
1621 C  C   . ASN A 205 ? 0.43681 0.47229 0.72618 -0.07344 0.00396  -0.07473 200 ASN A C   
1622 O  O   . ASN A 205 ? 0.43732 0.49036 0.73242 -0.06984 -0.00873 -0.08070 200 ASN A O   
1623 C  CB  . ASN A 205 ? 0.51184 0.55901 0.83033 -0.07560 0.02755  -0.06106 200 ASN A CB  
1624 C  CG  . ASN A 205 ? 0.54892 0.59684 0.88318 -0.08388 0.02643  -0.06853 200 ASN A CG  
1625 O  OD1 . ASN A 205 ? 0.65352 0.68315 0.98101 -0.08814 0.03365  -0.06667 200 ASN A OD1 
1626 N  ND2 . ASN A 205 ? 0.65059 0.71985 1.00628 -0.08584 0.01716  -0.07709 200 ASN A ND2 
1627 N  N   . GLU A 206 ? 0.38577 0.40512 0.66403 -0.07668 0.00331  -0.07865 201 GLU A N   
1628 C  CA  . GLU A 206 ? 0.39572 0.41645 0.66702 -0.07685 -0.01196 -0.09086 201 GLU A CA  
1629 C  C   . GLU A 206 ? 0.41782 0.44268 0.67012 -0.06893 -0.02405 -0.09288 201 GLU A C   
1630 O  O   . GLU A 206 ? 0.49272 0.52852 0.74391 -0.06673 -0.03910 -0.10252 201 GLU A O   
1631 C  CB  . GLU A 206 ? 0.57182 0.61008 0.86655 -0.08155 -0.01977 -0.10039 201 GLU A CB  
1632 C  CG  . GLU A 206 ? 0.58495 0.61926 0.89897 -0.09015 -0.00822 -0.09901 201 GLU A CG  
1633 C  CD  . GLU A 206 ? 0.77393 0.82583 1.11143 -0.09552 -0.01703 -0.10982 201 GLU A CD  
1634 O  OE1 . GLU A 206 ? 0.82990 0.89766 1.16756 -0.09131 -0.03241 -0.11789 201 GLU A OE1 
1635 O  OE2 . GLU A 206 ? 0.89132 0.94102 1.24653 -0.10365 -0.00877 -0.11014 201 GLU A OE2 
1636 N  N   . ALA A 207 ? 0.39585 0.41102 0.62459 -0.06156 -0.01677 -0.08098 202 ALA A N   
1637 C  CA  . ALA A 207 ? 0.42610 0.44336 0.62915 -0.05171 -0.02534 -0.07843 202 ALA A CA  
1638 C  C   . ALA A 207 ? 0.44052 0.44500 0.61907 -0.04959 -0.03096 -0.08292 202 ALA A C   
1639 O  O   . ALA A 207 ? 0.37944 0.36931 0.55442 -0.05317 -0.02433 -0.08348 202 ALA A O   
1640 C  CB  . ALA A 207 ? 0.43786 0.45059 0.62698 -0.04551 -0.01581 -0.06514 202 ALA A CB  
1641 N  N   . PRO A 208 ? 0.40743 0.41657 0.56814 -0.04304 -0.04254 -0.08583 203 PRO A N   
1642 C  CA  . PRO A 208 ? 0.39472 0.39247 0.53032 -0.04013 -0.04651 -0.08941 203 PRO A CA  
1643 C  C   . PRO A 208 ? 0.42772 0.41260 0.54202 -0.03616 -0.03632 -0.07869 203 PRO A C   
1644 O  O   . PRO A 208 ? 0.37878 0.36536 0.48826 -0.03255 -0.03142 -0.06886 203 PRO A O   
1645 C  CB  . PRO A 208 ? 0.46606 0.47341 0.58847 -0.03340 -0.06050 -0.09343 203 PRO A CB  
1646 C  CG  . PRO A 208 ? 0.46564 0.48516 0.59831 -0.03009 -0.06086 -0.08685 203 PRO A CG  
1647 C  CD  . PRO A 208 ? 0.43185 0.45685 0.59510 -0.03754 -0.05262 -0.08654 203 PRO A CD  
1648 N  N   . ALA A 209 ? 0.42037 0.39281 0.52277 -0.03664 -0.03350 -0.08154 204 ALA A N   
1649 C  CA  . ALA A 209 ? 0.34980 0.31224 0.43235 -0.03238 -0.02550 -0.07344 204 ALA A CA  
1650 C  C   . ALA A 209 ? 0.37580 0.33194 0.43889 -0.02937 -0.02986 -0.07998 204 ALA A C   
1651 O  O   . ALA A 209 ? 0.38760 0.34131 0.45501 -0.03207 -0.03545 -0.09096 204 ALA A O   
1652 C  CB  . ALA A 209 ? 0.41550 0.36808 0.50663 -0.03512 -0.01321 -0.06800 204 ALA A CB  
1653 N  N   . PHE A 210 ? 0.40230 0.35611 0.44438 -0.02397 -0.02701 -0.07374 205 PHE A N   
1654 C  CA  . PHE A 210 ? 0.35358 0.30330 0.37525 -0.02006 -0.03006 -0.07884 205 PHE A CA  
1655 C  C   . PHE A 210 ? 0.36963 0.31274 0.37987 -0.01705 -0.02031 -0.07292 205 PHE A C   
1656 O  O   . PHE A 210 ? 0.32569 0.26977 0.33834 -0.01668 -0.01347 -0.06356 205 PHE A O   
1657 C  CB  . PHE A 210 ? 0.35669 0.31303 0.36175 -0.01559 -0.03785 -0.07790 205 PHE A CB  
1658 C  CG  . PHE A 210 ? 0.39678 0.36211 0.41256 -0.01652 -0.04855 -0.08282 205 PHE A CG  
1659 C  CD1 . PHE A 210 ? 0.40754 0.38012 0.43600 -0.01719 -0.04839 -0.07624 205 PHE A CD1 
1660 C  CD2 . PHE A 210 ? 0.44489 0.41234 0.45841 -0.01605 -0.05919 -0.09475 205 PHE A CD2 
1661 C  CE1 . PHE A 210 ? 0.43398 0.41705 0.47424 -0.01700 -0.05834 -0.08098 205 PHE A CE1 
1662 C  CE2 . PHE A 210 ? 0.48856 0.46698 0.51366 -0.01625 -0.07025 -0.09996 205 PHE A CE2 
1663 C  CZ  . PHE A 210 ? 0.44519 0.43208 0.48453 -0.01657 -0.06965 -0.09281 205 PHE A CZ  
1664 N  N   . ALA A 211 ? 0.37967 0.31689 0.37762 -0.01432 -0.02015 -0.07928 206 ALA A N   
1665 C  CA  . ALA A 211 ? 0.33650 0.27036 0.32244 -0.01001 -0.01197 -0.07509 206 ALA A CA  
1666 C  C   . ALA A 211 ? 0.43957 0.37746 0.40388 -0.00568 -0.01445 -0.07557 206 ALA A C   
1667 O  O   . ALA A 211 ? 0.43808 0.37373 0.39219 -0.00381 -0.02031 -0.08458 206 ALA A O   
1668 C  CB  . ALA A 211 ? 0.37565 0.29860 0.36453 -0.00909 -0.00804 -0.08172 206 ALA A CB  
1669 N  N   . ARG A 212 ? 0.35312 0.29642 0.31000 -0.00429 -0.00987 -0.06610 207 ARG A N   
1670 C  CA  . ARG A 212 ? 0.32777 0.27394 0.26415 -0.00081 -0.00953 -0.06443 207 ARG A CA  
1671 C  C   . ARG A 212 ? 0.34932 0.29662 0.28024 0.00210  0.00011  -0.06200 207 ARG A C   
1672 O  O   . ARG A 212 ? 0.35035 0.30222 0.28738 0.00098  0.00605  -0.05424 207 ARG A O   
1673 C  CB  . ARG A 212 ? 0.31620 0.26683 0.24861 -0.00206 -0.01111 -0.05577 207 ARG A CB  
1674 C  CG  . ARG A 212 ? 0.31760 0.26882 0.22754 0.00112  -0.00997 -0.05285 207 ARG A CG  
1675 C  CD  . ARG A 212 ? 0.34275 0.29488 0.24869 -0.00021 -0.01097 -0.04366 207 ARG A CD  
1676 N  NE  . ARG A 212 ? 0.33705 0.28764 0.22130 0.00225  -0.00739 -0.03928 207 ARG A NE  
1677 C  CZ  . ARG A 212 ? 0.45930 0.40620 0.32614 0.00590  -0.01316 -0.03864 207 ARG A CZ  
1678 N  NH1 . ARG A 212 ? 0.37692 0.32335 0.24705 0.00766  -0.02407 -0.04232 207 ARG A NH1 
1679 N  NH2 . ARG A 212 ? 0.42349 0.36767 0.26915 0.00826  -0.00761 -0.03397 207 ARG A NH2 
1680 N  N   . PHE A 213 ? 0.38220 0.32620 0.30214 0.00628  0.00126  -0.06941 208 PHE A N   
1681 C  CA  . PHE A 213 ? 0.38007 0.32713 0.29395 0.01044  0.01047  -0.06809 208 PHE A CA  
1682 C  C   . PHE A 213 ? 0.37409 0.32715 0.27042 0.01177  0.01366  -0.06339 208 PHE A C   
1683 O  O   . PHE A 213 ? 0.40621 0.35631 0.28490 0.01501  0.01088  -0.06839 208 PHE A O   
1684 C  CB  . PHE A 213 ? 0.36972 0.30933 0.27914 0.01529  0.01115  -0.07865 208 PHE A CB  
1685 C  CG  . PHE A 213 ? 0.39743 0.32830 0.32348 0.01404  0.01026  -0.08260 208 PHE A CG  
1686 C  CD1 . PHE A 213 ? 0.39879 0.32210 0.33219 0.00992  0.00214  -0.08931 208 PHE A CD1 
1687 C  CD2 . PHE A 213 ? 0.38850 0.31860 0.32277 0.01736  0.01781  -0.07976 208 PHE A CD2 
1688 C  CE1 . PHE A 213 ? 0.40691 0.32043 0.35592 0.00787  0.00296  -0.09235 208 PHE A CE1 
1689 C  CE2 . PHE A 213 ? 0.44560 0.36474 0.39287 0.01687  0.01809  -0.08223 208 PHE A CE2 
1690 C  CZ  . PHE A 213 ? 0.41020 0.32018 0.36482 0.01154  0.01136  -0.08826 208 PHE A CZ  
1691 N  N   . ASN A 214 ? 0.37355 0.33433 0.27405 0.00923  0.01968  -0.05400 209 ASN A N   
1692 C  CA  . ASN A 214 ? 0.38192 0.34755 0.26789 0.00911  0.02493  -0.04825 209 ASN A CA  
1693 C  C   . ASN A 214 ? 0.40081 0.37332 0.28225 0.01322  0.03492  -0.04961 209 ASN A C   
1694 O  O   . ASN A 214 ? 0.38475 0.36276 0.27996 0.01460  0.03926  -0.05026 209 ASN A O   
1695 C  CB  . ASN A 214 ? 0.34891 0.31901 0.24302 0.00326  0.02685  -0.03837 209 ASN A CB  
1696 C  CG  . ASN A 214 ? 0.36710 0.33115 0.26455 0.00032  0.01803  -0.03649 209 ASN A CG  
1697 O  OD1 . ASN A 214 ? 0.38975 0.34866 0.27345 0.00148  0.01292  -0.03638 209 ASN A OD1 
1698 N  ND2 . ASN A 214 ? 0.32364 0.28867 0.23868 -0.00252 0.01630  -0.03483 209 ASN A ND2 
1699 N  N   . TYR A 215 ? 0.39300 0.36568 0.25453 0.01600  0.03891  -0.04959 210 TYR A N   
1700 C  CA  . TYR A 215 ? 0.35901 0.34034 0.21539 0.01978  0.05025  -0.04970 210 TYR A CA  
1701 C  C   . TYR A 215 ? 0.40985 0.39589 0.25548 0.01621  0.05780  -0.04049 210 TYR A C   
1702 O  O   . TYR A 215 ? 0.40944 0.38772 0.23412 0.01742  0.05575  -0.03897 210 TYR A O   
1703 C  CB  . TYR A 215 ? 0.40384 0.37950 0.24396 0.02796  0.05019  -0.05991 210 TYR A CB  
1704 C  CG  . TYR A 215 ? 0.44881 0.43424 0.28521 0.03339  0.06266  -0.06107 210 TYR A CG  
1705 C  CD1 . TYR A 215 ? 0.40523 0.39541 0.22392 0.03450  0.07176  -0.05660 210 TYR A CD1 
1706 C  CD2 . TYR A 215 ? 0.43668 0.42653 0.28720 0.03807  0.06603  -0.06620 210 TYR A CD2 
1707 C  CE1 . TYR A 215 ? 0.47510 0.47623 0.29205 0.03961  0.08432  -0.05778 210 TYR A CE1 
1708 C  CE2 . TYR A 215 ? 0.47635 0.47694 0.32498 0.04421  0.07749  -0.06770 210 TYR A CE2 
1709 C  CZ  . TYR A 215 ? 0.45066 0.45792 0.28346 0.04466  0.08681  -0.06371 210 TYR A CZ  
1710 O  OH  . TYR A 215 ? 0.46887 0.48883 0.30149 0.05079  0.09938  -0.06518 210 TYR A OH  
1711 N  N   . TYR A 216 ? 0.36616 0.36463 0.22595 0.01199  0.06647  -0.03448 211 TYR A N   
1712 C  CA  . TYR A 216 ? 0.42113 0.42424 0.27481 0.00671  0.07543  -0.02541 211 TYR A CA  
1713 C  C   . TYR A 216 ? 0.40214 0.41760 0.25275 0.01026  0.08871  -0.02630 211 TYR A C   
1714 O  O   . TYR A 216 ? 0.41706 0.44769 0.28769 0.00964  0.09428  -0.02705 211 TYR A O   
1715 C  CB  . TYR A 216 ? 0.35407 0.36322 0.22818 -0.00217 0.07545  -0.01880 211 TYR A CB  
1716 C  CG  . TYR A 216 ? 0.36365 0.36253 0.24357 -0.00465 0.06335  -0.01858 211 TYR A CG  
1717 C  CD1 . TYR A 216 ? 0.40516 0.39223 0.27337 -0.00778 0.05891  -0.01316 211 TYR A CD1 
1718 C  CD2 . TYR A 216 ? 0.36106 0.36179 0.25767 -0.00309 0.05713  -0.02330 211 TYR A CD2 
1719 C  CE1 . TYR A 216 ? 0.36052 0.33990 0.23506 -0.00922 0.04861  -0.01326 211 TYR A CE1 
1720 C  CE2 . TYR A 216 ? 0.34032 0.33264 0.24263 -0.00530 0.04763  -0.02278 211 TYR A CE2 
1721 C  CZ  . TYR A 216 ? 0.36037 0.34306 0.25242 -0.00833 0.04342  -0.01816 211 TYR A CZ  
1722 O  OH  . TYR A 216 ? 0.37883 0.35474 0.27733 -0.00976 0.03469  -0.01787 211 TYR A OH  
1723 N  N   . PRO A 217 ? 0.46472 0.47538 0.29078 0.01498  0.09417  -0.02655 212 PRO A N   
1724 C  CA  . PRO A 217 ? 0.46857 0.49205 0.29152 0.01866  0.10864  -0.02696 212 PRO A CA  
1725 C  C   . PRO A 217 ? 0.44418 0.48069 0.28036 0.00940  0.12030  -0.01723 212 PRO A C   
1726 O  O   . PRO A 217 ? 0.43977 0.47024 0.27878 0.00073  0.11758  -0.00960 212 PRO A O   
1727 C  CB  . PRO A 217 ? 0.46029 0.47212 0.24919 0.02551  0.11069  -0.02826 212 PRO A CB  
1728 C  CG  . PRO A 217 ? 0.45056 0.44517 0.22828 0.02725  0.09439  -0.03217 212 PRO A CG  
1729 C  CD  . PRO A 217 ? 0.43418 0.42826 0.23337 0.01825  0.08711  -0.02680 212 PRO A CD  
1730 N  N   . PRO A 218 ? 0.50180 0.55652 0.34779 0.01075  0.13344  -0.01771 213 PRO A N   
1731 C  CA  . PRO A 218 ? 0.49090 0.55848 0.34869 0.00084  0.14601  -0.00873 213 PRO A CA  
1732 C  C   . PRO A 218 ? 0.51476 0.56766 0.34591 -0.00266 0.15219  0.00038  213 PRO A C   
1733 O  O   . PRO A 218 ? 0.45071 0.49036 0.25248 0.00549  0.15135  -0.00120 213 PRO A O   
1734 C  CB  . PRO A 218 ? 0.53790 0.62784 0.40687 0.00593  0.15935  -0.01257 213 PRO A CB  
1735 C  CG  . PRO A 218 ? 0.58293 0.66497 0.43272 0.01971  0.15624  -0.02189 213 PRO A CG  
1736 C  CD  . PRO A 218 ? 0.42206 0.48628 0.26852 0.02153  0.13821  -0.02663 213 PRO A CD  
1737 N  N   . CYS A 219 ? 0.53873 0.59246 0.37933 -0.01459 0.15761  0.00979  214 CYS A N   
1738 C  CA  . CYS A 219 ? 0.52885 0.56794 0.34696 -0.01827 0.16332  0.02031  214 CYS A CA  
1739 C  C   . CYS A 219 ? 0.52366 0.57975 0.35830 -0.02616 0.17679  0.02774  214 CYS A C   
1740 O  O   . CYS A 219 ? 0.56160 0.63227 0.42617 -0.03534 0.17946  0.02825  214 CYS A O   
1741 C  CB  . CYS A 219 ? 0.53504 0.55448 0.34910 -0.02499 0.15352  0.02584  214 CYS A CB  
1742 S  SG  . CYS A 219 ? 0.57472 0.57382 0.36172 -0.02725 0.15744  0.03938  214 CYS A SG  
1743 N  N   . PRO A 220 ? 0.51691 0.57225 0.33369 -0.02339 0.18496  0.03307  215 PRO A N   
1744 C  CA  . PRO A 220 ? 0.51760 0.58965 0.35069 -0.03153 0.19869  0.04031  215 PRO A CA  
1745 C  C   . PRO A 220 ? 0.65392 0.71716 0.49780 -0.04499 0.20015  0.05047  215 PRO A C   
1746 O  O   . PRO A 220 ? 0.61032 0.68930 0.47658 -0.05397 0.20989  0.05497  215 PRO A O   
1747 C  CB  . PRO A 220 ? 0.64406 0.71202 0.44890 -0.02494 0.20582  0.04309  215 PRO A CB  
1748 C  CG  . PRO A 220 ? 0.60823 0.65035 0.38047 -0.01662 0.19404  0.04153  215 PRO A CG  
1749 C  CD  . PRO A 220 ? 0.49515 0.53522 0.27660 -0.01292 0.18165  0.03186  215 PRO A CD  
1750 N  N   . ARG A 221 ? 0.54766 0.58639 0.37725 -0.04652 0.19045  0.05364  216 ARG A N   
1751 C  CA  . ARG A 221 ? 0.55217 0.57898 0.39074 -0.05861 0.19031  0.06208  216 ARG A CA  
1752 C  C   . ARG A 221 ? 0.58738 0.60235 0.43089 -0.06043 0.17698  0.05750  216 ARG A C   
1753 O  O   . ARG A 221 ? 0.54603 0.53722 0.36826 -0.05784 0.16905  0.06115  216 ARG A O   
1754 C  CB  . ARG A 221 ? 0.56548 0.57051 0.37598 -0.05800 0.19362  0.07327  216 ARG A CB  
1755 C  CG  . ARG A 221 ? 0.72915 0.74485 0.53582 -0.05906 0.20830  0.07931  216 ARG A CG  
1756 C  CD  . ARG A 221 ? 0.68931 0.72344 0.53027 -0.07257 0.21815  0.08219  216 ARG A CD  
1757 N  NE  . ARG A 221 ? 0.73123 0.74917 0.58144 -0.08385 0.21520  0.08833  216 ARG A NE  
1758 C  CZ  . ARG A 221 ? 0.76287 0.76520 0.60345 -0.09010 0.22199  0.09945  216 ARG A CZ  
1759 N  NH1 . ARG A 221 ? 0.67319 0.67390 0.49379 -0.08664 0.23251  0.10648  216 ARG A NH1 
1760 N  NH2 . ARG A 221 ? 0.70709 0.69428 0.55769 -0.09991 0.21829  0.10327  216 ARG A NH2 
1761 N  N   . PRO A 222 ? 0.58722 0.61935 0.45882 -0.06446 0.17390  0.04937  217 PRO A N   
1762 C  CA  . PRO A 222 ? 0.56778 0.59033 0.44379 -0.06647 0.16147  0.04444  217 PRO A CA  
1763 C  C   . PRO A 222 ? 0.49495 0.49980 0.37324 -0.07644 0.15805  0.05132  217 PRO A C   
1764 O  O   . PRO A 222 ? 0.54690 0.53916 0.42253 -0.07630 0.14680  0.04891  217 PRO A O   
1765 C  CB  . PRO A 222 ? 0.55652 0.60554 0.46423 -0.06895 0.16052  0.03481  217 PRO A CB  
1766 C  CG  . PRO A 222 ? 0.55475 0.62547 0.48096 -0.07241 0.17226  0.03691  217 PRO A CG  
1767 C  CD  . PRO A 222 ? 0.53506 0.59720 0.43562 -0.06668 0.18115  0.04433  217 PRO A CD  
1768 N  N   . ASP A 223 ? 0.53654 0.53959 0.41996 -0.08424 0.16666  0.05959  218 ASP A N   
1769 C  CA  . ASP A 223 ? 0.58991 0.57287 0.47317 -0.09267 0.16387  0.06612  218 ASP A CA  
1770 C  C   . ASP A 223 ? 0.57747 0.53164 0.42664 -0.08535 0.16017  0.07397  218 ASP A C   
1771 O  O   . ASP A 223 ? 0.65661 0.59109 0.50270 -0.08978 0.15612  0.07888  218 ASP A O   
1772 C  CB  . ASP A 223 ? 0.58133 0.57215 0.48320 -0.10406 0.17464  0.07172  218 ASP A CB  
1773 C  CG  . ASP A 223 ? 0.64901 0.64145 0.53519 -0.10040 0.18694  0.07961  218 ASP A CG  
1774 O  OD1 . ASP A 223 ? 0.63476 0.63914 0.51118 -0.09069 0.18953  0.07627  218 ASP A OD1 
1775 O  OD2 . ASP A 223 ? 0.73329 0.71449 0.61615 -0.10708 0.19409  0.08889  218 ASP A OD2 
1776 N  N   . LEU A 224 ? 0.54686 0.49830 0.37055 -0.07348 0.16056  0.07457  219 LEU A N   
1777 C  CA  . LEU A 224 ? 0.56265 0.48993 0.35387 -0.06553 0.15732  0.08230  219 LEU A CA  
1778 C  C   . LEU A 224 ? 0.55139 0.46771 0.32252 -0.05401 0.14372  0.07717  219 LEU A C   
1779 O  O   . LEU A 224 ? 0.62122 0.51863 0.36641 -0.04613 0.13834  0.08251  219 LEU A O   
1780 C  CB  . LEU A 224 ? 0.53045 0.46153 0.30462 -0.06067 0.16788  0.08787  219 LEU A CB  
1781 C  CG  . LEU A 224 ? 0.67456 0.61371 0.46381 -0.07156 0.18235  0.09515  219 LEU A CG  
1782 C  CD1 . LEU A 224 ? 0.66554 0.60411 0.43152 -0.06543 0.19192  0.10155  219 LEU A CD1 
1783 C  CD2 . LEU A 224 ? 0.73220 0.65286 0.52798 -0.08135 0.18189  0.10257  219 LEU A CD2 
1784 N  N   . VAL A 225 ? 0.56791 0.49599 0.35063 -0.05256 0.13761  0.06681  220 VAL A N   
1785 C  CA  . VAL A 225 ? 0.49866 0.42027 0.26769 -0.04159 0.12302  0.06022  220 VAL A CA  
1786 C  C   . VAL A 225 ? 0.50602 0.43703 0.30402 -0.04480 0.11096  0.05173  220 VAL A C   
1787 O  O   . VAL A 225 ? 0.49919 0.44167 0.32280 -0.05462 0.11513  0.05038  220 VAL A O   
1788 C  CB  . VAL A 225 ? 0.48208 0.41451 0.23887 -0.03090 0.12301  0.05294  220 VAL A CB  
1789 C  CG1 . VAL A 225 ? 0.55664 0.48687 0.29211 -0.02709 0.13392  0.05986  220 VAL A CG1 
1790 C  CG2 . VAL A 225 ? 0.48854 0.44572 0.27421 -0.03331 0.12467  0.04313  220 VAL A CG2 
1791 N  N   . PHE A 226 ? 0.52547 0.45187 0.31899 -0.03625 0.09587  0.04586  221 PHE A N   
1792 C  CA  . PHE A 226 ? 0.44989 0.38700 0.26752 -0.03637 0.08509  0.03669  221 PHE A CA  
1793 C  C   . PHE A 226 ? 0.47162 0.41858 0.28741 -0.02719 0.07935  0.02706  221 PHE A C   
1794 O  O   . PHE A 226 ? 0.46370 0.40319 0.25679 -0.01876 0.07601  0.02620  221 PHE A O   
1795 C  CB  . PHE A 226 ? 0.41349 0.33701 0.23184 -0.03525 0.07279  0.03755  221 PHE A CB  
1796 C  CG  . PHE A 226 ? 0.45863 0.37272 0.28465 -0.04472 0.07663  0.04431  221 PHE A CG  
1797 C  CD1 . PHE A 226 ? 0.48111 0.40740 0.33059 -0.05484 0.08274  0.04264  221 PHE A CD1 
1798 C  CD2 . PHE A 226 ? 0.57311 0.46591 0.38286 -0.04303 0.07363  0.05170  221 PHE A CD2 
1799 C  CE1 . PHE A 226 ? 0.52189 0.43864 0.37882 -0.06427 0.08564  0.04734  221 PHE A CE1 
1800 C  CE2 . PHE A 226 ? 0.58404 0.46538 0.40025 -0.05178 0.07741  0.05731  221 PHE A CE2 
1801 C  CZ  . PHE A 226 ? 0.50919 0.40226 0.34912 -0.06298 0.08341  0.05468  221 PHE A CZ  
1802 N  N   . GLY A 227 ? 0.41937 0.38211 0.25836 -0.02844 0.07781  0.01956  222 GLY A N   
1803 C  CA  . GLY A 227 ? 0.41353 0.38206 0.25311 -0.02016 0.07103  0.01000  222 GLY A CA  
1804 C  C   . GLY A 227 ? 0.42360 0.38141 0.25859 -0.01534 0.05685  0.00669  222 GLY A C   
1805 O  O   . GLY A 227 ? 0.42674 0.38070 0.24785 -0.00784 0.05108  0.00151  222 GLY A O   
1806 N  N   . ILE A 228 ? 0.40688 0.36068 0.25440 -0.01958 0.05103  0.00888  223 ILE A N   
1807 C  CA  . ILE A 228 ? 0.43098 0.37406 0.27339 -0.01581 0.03933  0.00830  223 ILE A CA  
1808 C  C   . ILE A 228 ? 0.40756 0.34085 0.25092 -0.02104 0.03980  0.01633  223 ILE A C   
1809 O  O   . ILE A 228 ? 0.39970 0.33727 0.25813 -0.02839 0.04477  0.01836  223 ILE A O   
1810 C  CB  . ILE A 228 ? 0.48640 0.43517 0.34601 -0.01350 0.03033  -0.00007 223 ILE A CB  
1811 C  CG1 . ILE A 228 ? 0.39705 0.33746 0.25157 -0.00900 0.01866  -0.00162 223 ILE A CG1 
1812 C  CG2 . ILE A 228 ? 0.37649 0.33212 0.25868 -0.01917 0.03187  0.00014  223 ILE A CG2 
1813 C  CD1 . ILE A 228 ? 0.44452 0.39011 0.31489 -0.00702 0.01097  -0.01011 223 ILE A CD1 
1814 N  N   . ARG A 229 ? 0.40511 0.32485 0.23141 -0.01668 0.03443  0.02053  224 ARG A N   
1815 C  CA  . ARG A 229 ? 0.43089 0.33720 0.25295 -0.02013 0.03578  0.02899  224 ARG A CA  
1816 C  C   . ARG A 229 ? 0.40465 0.31256 0.24798 -0.02381 0.03070  0.02668  224 ARG A C   
1817 O  O   . ARG A 229 ? 0.42829 0.34517 0.28556 -0.02145 0.02399  0.01951  224 ARG A O   
1818 C  CB  . ARG A 229 ? 0.41897 0.31102 0.21810 -0.01177 0.02900  0.03310  224 ARG A CB  
1819 C  CG  . ARG A 229 ? 0.48664 0.38169 0.29275 -0.00494 0.01489  0.02621  224 ARG A CG  
1820 C  CD  . ARG A 229 ? 0.59385 0.48084 0.37662 0.00513  0.00714  0.02750  224 ARG A CD  
1821 N  NE  . ARG A 229 ? 0.54743 0.43655 0.31158 0.00821  0.01165  0.02637  224 ARG A NE  
1822 C  CZ  . ARG A 229 ? 0.59775 0.47787 0.33395 0.01652  0.00914  0.02988  224 ARG A CZ  
1823 N  NH1 . ARG A 229 ? 0.60645 0.47512 0.33033 0.02327  0.00124  0.03489  224 ARG A NH1 
1824 N  NH2 . ARG A 229 ? 0.56565 0.44825 0.28473 0.01921  0.01465  0.02830  224 ARG A NH2 
1825 N  N   . PRO A 230 ? 0.39802 0.29614 0.24331 -0.02959 0.03437  0.03263  225 PRO A N   
1826 C  CA  . PRO A 230 ? 0.37165 0.26855 0.23268 -0.03128 0.02880  0.03035  225 PRO A CA  
1827 C  C   . PRO A 230 ? 0.42571 0.31994 0.28506 -0.02246 0.01760  0.02754  225 PRO A C   
1828 O  O   . PRO A 230 ? 0.43436 0.31838 0.27689 -0.01599 0.01359  0.03123  225 PRO A O   
1829 C  CB  . PRO A 230 ? 0.42249 0.30343 0.27805 -0.03713 0.03411  0.03783  225 PRO A CB  
1830 C  CG  . PRO A 230 ? 0.51648 0.39759 0.36394 -0.04287 0.04540  0.04261  225 PRO A CG  
1831 C  CD  . PRO A 230 ? 0.48026 0.36723 0.31391 -0.03538 0.04465  0.04138  225 PRO A CD  
1832 N  N   . HIS A 231 ? 0.40186 0.30617 0.27910 -0.02187 0.01270  0.02105  226 HIS A N   
1833 C  CA  . HIS A 231 ? 0.41359 0.31884 0.29437 -0.01475 0.00303  0.01751  226 HIS A CA  
1834 C  C   . HIS A 231 ? 0.42006 0.33290 0.32120 -0.01660 0.00149  0.01304  226 HIS A C   
1835 O  O   . HIS A 231 ? 0.39481 0.31489 0.30600 -0.02176 0.00638  0.01115  226 HIS A O   
1836 C  CB  . HIS A 231 ? 0.42115 0.33400 0.29735 -0.00964 -0.00151 0.01238  226 HIS A CB  
1837 C  CG  . HIS A 231 ? 0.43685 0.36253 0.32610 -0.01235 0.00102  0.00594  226 HIS A CG  
1838 N  ND1 . HIS A 231 ? 0.39459 0.32494 0.28126 -0.01607 0.00905  0.00616  226 HIS A ND1 
1839 C  CD2 . HIS A 231 ? 0.37237 0.30647 0.27748 -0.01143 -0.00280 -0.00047 226 HIS A CD2 
1840 C  CE1 . HIS A 231 ? 0.39215 0.33266 0.29167 -0.01630 0.00930  0.00004  226 HIS A CE1 
1841 N  NE2 . HIS A 231 ? 0.34721 0.28895 0.25747 -0.01388 0.00247  -0.00371 226 HIS A NE2 
1842 N  N   . SER A 232 ? 0.36182 0.27347 0.26852 -0.01162 -0.00520 0.01162  227 SER A N   
1843 C  CA  . SER A 232 ? 0.38825 0.30891 0.31313 -0.01147 -0.00693 0.00677  227 SER A CA  
1844 C  C   . SER A 232 ? 0.38965 0.31909 0.32013 -0.00764 -0.01241 0.00128  227 SER A C   
1845 O  O   . SER A 232 ? 0.39718 0.32486 0.31838 -0.00312 -0.01796 0.00091  227 SER A O   
1846 C  CB  . SER A 232 ? 0.44744 0.36229 0.37736 -0.00889 -0.00922 0.00830  227 SER A CB  
1847 O  OG  . SER A 232 ? 0.45212 0.36209 0.37559 -0.00210 -0.01562 0.00978  227 SER A OG  
1848 N  N   . ASP A 233 ? 0.35789 0.29612 0.30288 -0.00942 -0.01095 -0.00318 228 ASP A N   
1849 C  CA  . ASP A 233 ? 0.31765 0.26289 0.27078 -0.00718 -0.01574 -0.00911 228 ASP A CA  
1850 C  C   . ASP A 233 ? 0.36229 0.30951 0.32459 -0.00324 -0.02190 -0.01016 228 ASP A C   
1851 O  O   . ASP A 233 ? 0.39791 0.34289 0.36538 -0.00245 -0.02044 -0.00717 228 ASP A O   
1852 C  CB  . ASP A 233 ? 0.31827 0.26957 0.28433 -0.01007 -0.01141 -0.01259 228 ASP A CB  
1853 C  CG  . ASP A 233 ? 0.37985 0.33187 0.33883 -0.01238 -0.00609 -0.01277 228 ASP A CG  
1854 O  OD1 . ASP A 233 ? 0.35993 0.30910 0.30458 -0.01222 -0.00559 -0.01117 228 ASP A OD1 
1855 O  OD2 . ASP A 233 ? 0.34464 0.30025 0.31223 -0.01368 -0.00196 -0.01421 228 ASP A OD2 
1856 N  N   . GLY A 234 ? 0.34953 0.30192 0.31439 -0.00041 -0.02907 -0.01519 229 GLY A N   
1857 C  CA  . GLY A 234 ? 0.37767 0.33590 0.35519 0.00334  -0.03533 -0.01733 229 GLY A CA  
1858 C  C   . GLY A 234 ? 0.35059 0.31766 0.35116 0.00035  -0.03316 -0.02156 229 GLY A C   
1859 O  O   . GLY A 234 ? 0.33810 0.31272 0.35315 0.00271  -0.03720 -0.02381 229 GLY A O   
1860 N  N   . THR A 235 ? 0.32917 0.29546 0.33364 -0.00441 -0.02624 -0.02219 230 THR A N   
1861 C  CA  . THR A 235 ? 0.28726 0.25912 0.31102 -0.00760 -0.02298 -0.02567 230 THR A CA  
1862 C  C   . THR A 235 ? 0.29208 0.26563 0.32706 -0.00690 -0.01797 -0.02172 230 THR A C   
1863 O  O   . THR A 235 ? 0.31672 0.28659 0.34438 -0.00392 -0.01738 -0.01715 230 THR A O   
1864 C  CB  . THR A 235 ? 0.31477 0.28266 0.33562 -0.01103 -0.01661 -0.02608 230 THR A CB  
1865 O  OG1 . THR A 235 ? 0.28942 0.25232 0.29913 -0.01079 -0.01125 -0.02009 230 THR A OG1 
1866 C  CG2 . THR A 235 ? 0.33257 0.29925 0.34390 -0.01129 -0.02069 -0.03144 230 THR A CG2 
1867 N  N   . LEU A 236 ? 0.27795 0.25580 0.33014 -0.00966 -0.01351 -0.02354 231 LEU A N   
1868 C  CA  . LEU A 236 ? 0.28614 0.26335 0.34461 -0.00914 -0.00552 -0.01889 231 LEU A CA  
1869 C  C   . LEU A 236 ? 0.30828 0.27787 0.35466 -0.00997 0.00077  -0.01504 231 LEU A C   
1870 O  O   . LEU A 236 ? 0.32119 0.28720 0.35917 -0.00785 0.00343  -0.01093 231 LEU A O   
1871 C  CB  . LEU A 236 ? 0.26861 0.25220 0.34883 -0.01191 -0.00136 -0.02108 231 LEU A CB  
1872 C  CG  . LEU A 236 ? 0.31626 0.30044 0.40366 -0.01039 0.00763  -0.01617 231 LEU A CG  
1873 C  CD1 . LEU A 236 ? 0.31204 0.30195 0.40285 -0.00543 0.00502  -0.01521 231 LEU A CD1 
1874 C  CD2 . LEU A 236 ? 0.30241 0.28966 0.40904 -0.01468 0.01475  -0.01701 231 LEU A CD2 
1875 N  N   . LEU A 237 ? 0.32002 0.28727 0.36519 -0.01259 0.00240  -0.01711 232 LEU A N   
1876 C  CA  . LEU A 237 ? 0.29135 0.25367 0.32686 -0.01243 0.00750  -0.01423 232 LEU A CA  
1877 C  C   . LEU A 237 ? 0.28727 0.24796 0.31565 -0.01368 0.00511  -0.01786 232 LEU A C   
1878 O  O   . LEU A 237 ? 0.30502 0.26648 0.33935 -0.01531 0.00189  -0.02309 232 LEU A O   
1879 C  CB  . LEU A 237 ? 0.33947 0.29977 0.38342 -0.01235 0.01527  -0.01180 232 LEU A CB  
1880 C  CG  . LEU A 237 ? 0.42927 0.38592 0.46388 -0.00980 0.02047  -0.00756 232 LEU A CG  
1881 C  CD1 . LEU A 237 ? 0.40762 0.36499 0.43607 -0.00724 0.02112  -0.00410 232 LEU A CD1 
1882 C  CD2 . LEU A 237 ? 0.42225 0.37446 0.46344 -0.00913 0.02767  -0.00544 232 LEU A CD2 
1883 N  N   . THR A 238 ? 0.27209 0.23129 0.28846 -0.01290 0.00671  -0.01581 233 THR A N   
1884 C  CA  . THR A 238 ? 0.29528 0.25371 0.30491 -0.01308 0.00657  -0.01882 233 THR A CA  
1885 C  C   . THR A 238 ? 0.26407 0.22176 0.27298 -0.01137 0.01245  -0.01663 233 THR A C   
1886 O  O   . THR A 238 ? 0.29593 0.25522 0.30252 -0.01026 0.01478  -0.01257 233 THR A O   
1887 C  CB  . THR A 238 ? 0.29003 0.24937 0.28635 -0.01328 0.00356  -0.01845 233 THR A CB  
1888 O  OG1 . THR A 238 ? 0.33158 0.29073 0.32645 -0.01310 -0.00265 -0.02001 233 THR A OG1 
1889 C  CG2 . THR A 238 ? 0.32222 0.28186 0.31117 -0.01273 0.00488  -0.02161 233 THR A CG2 
1890 N  N   . ILE A 239 ? 0.30294 0.25788 0.31353 -0.01045 0.01430  -0.01981 234 ILE A N   
1891 C  CA  . ILE A 239 ? 0.28910 0.24310 0.29834 -0.00703 0.01932  -0.01789 234 ILE A CA  
1892 C  C   . ILE A 239 ? 0.31485 0.27126 0.31642 -0.00562 0.01909  -0.02131 234 ILE A C   
1893 O  O   . ILE A 239 ? 0.30788 0.26033 0.30895 -0.00572 0.01785  -0.02663 234 ILE A O   
1894 C  CB  . ILE A 239 ? 0.30470 0.25092 0.32238 -0.00584 0.02342  -0.01772 234 ILE A CB  
1895 C  CG1 . ILE A 239 ? 0.28323 0.22848 0.30829 -0.00706 0.02537  -0.01357 234 ILE A CG1 
1896 C  CG2 . ILE A 239 ? 0.34405 0.28800 0.35807 -0.00035 0.02800  -0.01558 234 ILE A CG2 
1897 C  CD1 . ILE A 239 ? 0.30961 0.24628 0.34371 -0.00699 0.03111  -0.01217 234 ILE A CD1 
1898 N  N   . LEU A 240 ? 0.26986 0.23332 0.26607 -0.00442 0.02045  -0.01889 235 LEU A N   
1899 C  CA  . LEU A 240 ? 0.29059 0.25919 0.27972 -0.00392 0.02111  -0.02134 235 LEU A CA  
1900 C  C   . LEU A 240 ? 0.30889 0.28214 0.29934 0.00118  0.02525  -0.02137 235 LEU A C   
1901 O  O   . LEU A 240 ? 0.29550 0.27315 0.28937 0.00331  0.02642  -0.01789 235 LEU A O   
1902 C  CB  . LEU A 240 ? 0.28178 0.25615 0.26549 -0.00770 0.02004  -0.01866 235 LEU A CB  
1903 C  CG  . LEU A 240 ? 0.31879 0.29932 0.29516 -0.00829 0.02252  -0.01969 235 LEU A CG  
1904 C  CD1 . LEU A 240 ? 0.32340 0.29866 0.29136 -0.00777 0.02073  -0.02368 235 LEU A CD1 
1905 C  CD2 . LEU A 240 ? 0.28775 0.27232 0.26128 -0.01311 0.02294  -0.01570 235 LEU A CD2 
1906 N  N   . LEU A 241 ? 0.30445 0.27719 0.29144 0.00406  0.02702  -0.02572 236 LEU A N   
1907 C  CA  . LEU A 241 ? 0.28844 0.26677 0.27654 0.01030  0.03104  -0.02647 236 LEU A CA  
1908 C  C   . LEU A 241 ? 0.34181 0.33047 0.32454 0.00965  0.03326  -0.02835 236 LEU A C   
1909 O  O   . LEU A 241 ? 0.33607 0.32071 0.31120 0.00919  0.03328  -0.03243 236 LEU A O   
1910 C  CB  . LEU A 241 ? 0.32342 0.29027 0.31227 0.01539  0.03264  -0.03026 236 LEU A CB  
1911 C  CG  . LEU A 241 ? 0.38436 0.35438 0.37378 0.02404  0.03680  -0.03137 236 LEU A CG  
1912 C  CD1 . LEU A 241 ? 0.41164 0.39204 0.40604 0.02785  0.03747  -0.02588 236 LEU A CD1 
1913 C  CD2 . LEU A 241 ? 0.34800 0.30125 0.33786 0.02836  0.03836  -0.03455 236 LEU A CD2 
1914 N  N   . VAL A 242 ? 0.34743 0.34978 0.33404 0.00946  0.03527  -0.02565 237 VAL A N   
1915 C  CA  . VAL A 242 ? 0.35265 0.36604 0.33618 0.00704  0.03886  -0.02624 237 VAL A CA  
1916 C  C   . VAL A 242 ? 0.41708 0.44016 0.40368 0.01434  0.04377  -0.02928 237 VAL A C   
1917 O  O   . VAL A 242 ? 0.30033 0.32418 0.29283 0.02139  0.04373  -0.02974 237 VAL A O   
1918 C  CB  . VAL A 242 ? 0.32196 0.34543 0.31003 0.00042  0.03864  -0.02221 237 VAL A CB  
1919 C  CG1 . VAL A 242 ? 0.35263 0.36540 0.33612 -0.00575 0.03434  -0.01943 237 VAL A CG1 
1920 C  CG2 . VAL A 242 ? 0.41589 0.44974 0.41480 0.00356  0.03757  -0.02118 237 VAL A CG2 
1921 N  N   . ASP A 243 ? 0.34956 0.37938 0.33092 0.01353  0.04859  -0.03107 238 ASP A N   
1922 C  CA  . ASP A 243 ? 0.36528 0.40904 0.35098 0.01971  0.05473  -0.03363 238 ASP A CA  
1923 C  C   . ASP A 243 ? 0.36055 0.42023 0.36122 0.02206  0.05428  -0.03169 238 ASP A C   
1924 O  O   . ASP A 243 ? 0.32908 0.39651 0.33610 0.01516  0.05225  -0.02843 238 ASP A O   
1925 C  CB  . ASP A 243 ? 0.34410 0.39641 0.32390 0.01511  0.06101  -0.03319 238 ASP A CB  
1926 C  CG  . ASP A 243 ? 0.46556 0.52847 0.44524 0.02260  0.06863  -0.03725 238 ASP A CG  
1927 O  OD1 . ASP A 243 ? 0.38664 0.46498 0.37972 0.02801  0.07096  -0.03809 238 ASP A OD1 
1928 O  OD2 . ASP A 243 ? 0.39832 0.45468 0.36378 0.02380  0.07217  -0.03986 238 ASP A OD2 
1929 N  N   . LYS A 244 ? 0.37777 0.44175 0.38354 0.03245  0.05558  -0.03415 239 LYS A N   
1930 C  CA  . LYS A 244 ? 0.36923 0.44937 0.38843 0.03646  0.05370  -0.03265 239 LYS A CA  
1931 C  C   . LYS A 244 ? 0.36883 0.47486 0.39970 0.03523  0.05864  -0.03389 239 LYS A C   
1932 O  O   . LYS A 244 ? 0.35699 0.48011 0.40100 0.03593  0.05582  -0.03330 239 LYS A O   
1933 C  CB  . LYS A 244 ? 0.39779 0.47169 0.41766 0.04946  0.05260  -0.03372 239 LYS A CB  
1934 C  CG  . LYS A 244 ? 0.41966 0.49671 0.43855 0.05918  0.05850  -0.03832 239 LYS A CG  
1935 C  CD  . LYS A 244 ? 0.46879 0.53782 0.48838 0.07274  0.05719  -0.03841 239 LYS A CD  
1936 C  CE  . LYS A 244 ? 0.47490 0.54508 0.49290 0.08371  0.06322  -0.04365 239 LYS A CE  
1937 N  NZ  . LYS A 244 ? 0.40974 0.50963 0.44022 0.08729  0.06745  -0.04543 239 LYS A NZ  
1938 N  N   . ASP A 245 ? 0.31950 0.42956 0.34610 0.03331  0.06598  -0.03582 240 ASP A N   
1939 C  CA  . ASP A 245 ? 0.37380 0.50937 0.41278 0.03230  0.07296  -0.03698 240 ASP A CA  
1940 C  C   . ASP A 245 ? 0.38329 0.52411 0.42238 0.01857  0.07714  -0.03399 240 ASP A C   
1941 O  O   . ASP A 245 ? 0.45050 0.61377 0.50552 0.01378  0.08074  -0.03385 240 ASP A O   
1942 C  CB  . ASP A 245 ? 0.36498 0.50357 0.39941 0.04191  0.08092  -0.04121 240 ASP A CB  
1943 C  CG  . ASP A 245 ? 0.51486 0.64564 0.54832 0.05629  0.07804  -0.04431 240 ASP A CG  
1944 O  OD1 . ASP A 245 ? 0.48428 0.62281 0.52882 0.06158  0.07270  -0.04322 240 ASP A OD1 
1945 O  OD2 . ASP A 245 ? 0.61202 0.72769 0.63250 0.06259  0.08099  -0.04793 240 ASP A OD2 
1946 N  N   . VAL A 246 ? 0.34872 0.46954 0.37104 0.01232  0.07686  -0.03166 241 VAL A N   
1947 C  CA  . VAL A 246 ? 0.33190 0.45348 0.34941 0.00134  0.08270  -0.02805 241 VAL A CA  
1948 C  C   . VAL A 246 ? 0.37773 0.48496 0.39098 -0.00786 0.07572  -0.02401 241 VAL A C   
1949 O  O   . VAL A 246 ? 0.35752 0.44497 0.35843 -0.00601 0.06954  -0.02371 241 VAL A O   
1950 C  CB  . VAL A 246 ? 0.40166 0.51230 0.39966 0.00403  0.08916  -0.02870 241 VAL A CB  
1951 C  CG1 . VAL A 246 ? 0.44270 0.55278 0.43354 -0.00644 0.09620  -0.02343 241 VAL A CG1 
1952 C  CG2 . VAL A 246 ? 0.43389 0.55759 0.43511 0.01460  0.09639  -0.03361 241 VAL A CG2 
1953 N  N   . SER A 247 ? 0.32107 0.43838 0.34539 -0.01788 0.07699  -0.02141 242 SER A N   
1954 C  CA  . SER A 247 ? 0.36502 0.46876 0.38575 -0.02629 0.07100  -0.01801 242 SER A CA  
1955 C  C   . SER A 247 ? 0.36663 0.45239 0.36857 -0.03145 0.07447  -0.01351 242 SER A C   
1956 O  O   . SER A 247 ? 0.34891 0.43421 0.34049 -0.02944 0.08198  -0.01283 242 SER A O   
1957 C  CB  . SER A 247 ? 0.44102 0.56022 0.47982 -0.03549 0.07098  -0.01794 242 SER A CB  
1958 O  OG  . SER A 247 ? 0.50849 0.64659 0.56417 -0.02958 0.06684  -0.02243 242 SER A OG  
1959 N  N   . GLY A 248 ? 0.35939 0.43012 0.35578 -0.03720 0.06892  -0.01037 243 GLY A N   
1960 C  CA  . GLY A 248 ? 0.32061 0.37412 0.29919 -0.04136 0.07130  -0.00537 243 GLY A CA  
1961 C  C   . GLY A 248 ? 0.34622 0.38118 0.31728 -0.04288 0.06273  -0.00326 243 GLY A C   
1962 O  O   . GLY A 248 ? 0.34217 0.36384 0.30201 -0.04779 0.06403  0.00168  243 GLY A O   
1963 N  N   . LEU A 249 ? 0.31095 0.34427 0.28739 -0.03796 0.05460  -0.00652 244 LEU A N   
1964 C  CA  . LEU A 249 ? 0.33068 0.34858 0.30199 -0.03877 0.04721  -0.00487 244 LEU A CA  
1965 C  C   . LEU A 249 ? 0.33474 0.35212 0.31312 -0.04711 0.04661  -0.00289 244 LEU A C   
1966 O  O   . LEU A 249 ? 0.34556 0.37697 0.33833 -0.04998 0.04713  -0.00542 244 LEU A O   
1967 C  CB  . LEU A 249 ? 0.30307 0.32012 0.27919 -0.03171 0.04056  -0.00840 244 LEU A CB  
1968 C  CG  . LEU A 249 ? 0.31317 0.31718 0.28673 -0.03163 0.03376  -0.00719 244 LEU A CG  
1969 C  CD1 . LEU A 249 ? 0.32099 0.31083 0.28078 -0.03119 0.03194  -0.00498 244 LEU A CD1 
1970 C  CD2 . LEU A 249 ? 0.33375 0.33868 0.31349 -0.02510 0.02974  -0.00999 244 LEU A CD2 
1971 N  N   . GLN A 250 ? 0.28638 0.28726 0.25457 -0.05044 0.04485  0.00104  245 GLN A N   
1972 C  CA  . GLN A 250 ? 0.32719 0.32281 0.29991 -0.05805 0.04385  0.00240  245 GLN A CA  
1973 C  C   . GLN A 250 ? 0.34510 0.32361 0.30963 -0.05516 0.03707  0.00376  245 GLN A C   
1974 O  O   . GLN A 250 ? 0.35237 0.32146 0.30562 -0.04973 0.03484  0.00556  245 GLN A O   
1975 C  CB  . GLN A 250 ? 0.33248 0.32423 0.30141 -0.06697 0.05210  0.00710  245 GLN A CB  
1976 C  CG  . GLN A 250 ? 0.37293 0.38438 0.35321 -0.07081 0.06020  0.00566  245 GLN A CG  
1977 C  CD  . GLN A 250 ? 0.38656 0.39376 0.36334 -0.08034 0.07041  0.01122  245 GLN A CD  
1978 O  OE1 . GLN A 250 ? 0.40259 0.38951 0.36493 -0.08288 0.07157  0.01702  245 GLN A OE1 
1979 N  NE2 . GLN A 250 ? 0.41801 0.44440 0.40830 -0.08522 0.07845  0.00986  245 GLN A NE2 
1980 N  N   . VAL A 251 ? 0.32901 0.30461 0.29980 -0.05838 0.03349  0.00215  246 VAL A N   
1981 C  CA  . VAL A 251 ? 0.36422 0.32488 0.32873 -0.05516 0.02783  0.00299  246 VAL A CA  
1982 C  C   . VAL A 251 ? 0.41991 0.36787 0.38211 -0.06249 0.02878  0.00479  246 VAL A C   
1983 O  O   . VAL A 251 ? 0.42665 0.38055 0.39743 -0.07055 0.03160  0.00290  246 VAL A O   
1984 C  CB  . VAL A 251 ? 0.36377 0.33053 0.33572 -0.04945 0.02236  -0.00133 246 VAL A CB  
1985 C  CG1 . VAL A 251 ? 0.44440 0.42111 0.42699 -0.05369 0.02148  -0.00549 246 VAL A CG1 
1986 C  CG2 . VAL A 251 ? 0.40348 0.35653 0.36945 -0.04504 0.01787  -0.00028 246 VAL A CG2 
1987 N  N   . GLN A 252 ? 0.38288 0.31315 0.33419 -0.05964 0.02631  0.00811  247 GLN A N   
1988 C  CA  . GLN A 252 ? 0.38757 0.30114 0.33432 -0.06521 0.02721  0.01020  247 GLN A CA  
1989 C  C   . GLN A 252 ? 0.38349 0.29353 0.33469 -0.06289 0.02146  0.00543  247 GLN A C   
1990 O  O   . GLN A 252 ? 0.47075 0.38132 0.42090 -0.05446 0.01699  0.00432  247 GLN A O   
1991 C  CB  . GLN A 252 ? 0.44630 0.34126 0.37669 -0.06178 0.02798  0.01709  247 GLN A CB  
1992 C  CG  . GLN A 252 ? 0.54770 0.42294 0.47115 -0.06854 0.03173  0.02123  247 GLN A CG  
1993 C  CD  . GLN A 252 ? 0.59628 0.45267 0.50126 -0.06298 0.03216  0.02900  247 GLN A CD  
1994 O  OE1 . GLN A 252 ? 0.62022 0.47537 0.51957 -0.05288 0.02618  0.02930  247 GLN A OE1 
1995 N  NE2 . GLN A 252 ? 0.66261 0.50457 0.55834 -0.06938 0.03932  0.03547  247 GLN A NE2 
1996 N  N   . ARG A 253 ? 0.43476 0.34191 0.39141 -0.07060 0.02193  0.00209  248 ARG A N   
1997 C  CA  . ARG A 253 ? 0.58628 0.48876 0.54483 -0.06850 0.01669  -0.00332 248 ARG A CA  
1998 C  C   . ARG A 253 ? 0.69844 0.58477 0.65553 -0.07750 0.01818  -0.00447 248 ARG A C   
1999 O  O   . ARG A 253 ? 0.68277 0.57573 0.64882 -0.08785 0.02112  -0.00689 248 ARG A O   
2000 C  CB  . ARG A 253 ? 0.55416 0.47692 0.52386 -0.06709 0.01345  -0.00987 248 ARG A CB  
2001 C  CG  . ARG A 253 ? 0.74941 0.66852 0.71786 -0.06225 0.00806  -0.01523 248 ARG A CG  
2002 C  CD  . ARG A 253 ? 0.56025 0.49722 0.53404 -0.05541 0.00528  -0.01830 248 ARG A CD  
2003 N  NE  . ARG A 253 ? 0.76888 0.70607 0.74200 -0.05311 0.00058  -0.02473 248 ARG A NE  
2004 C  CZ  . ARG A 253 ? 0.74775 0.69487 0.72761 -0.05829 -0.00252 -0.03131 248 ARG A CZ  
2005 N  NH1 . ARG A 253 ? 0.64761 0.60692 0.63807 -0.06660 -0.00074 -0.03217 248 ARG A NH1 
2006 N  NH2 . ARG A 253 ? 0.90876 0.85474 0.88491 -0.05475 -0.00758 -0.03762 248 ARG A NH2 
2007 N  N   . ASP A 254 ? 0.75121 0.61632 0.69802 -0.07361 0.01649  -0.00288 249 ASP A N   
2008 C  CA  . ASP A 254 ? 0.76228 0.60640 0.70540 -0.08120 0.01809  -0.00367 249 ASP A CA  
2009 C  C   . ASP A 254 ? 0.85252 0.68932 0.79405 -0.09117 0.02580  0.00270  249 ASP A C   
2010 O  O   . ASP A 254 ? 0.88410 0.71682 0.83246 -0.10324 0.02904  0.00003  249 ASP A O   
2011 C  CB  . ASP A 254 ? 0.87941 0.72893 0.83200 -0.08696 0.01427  -0.01387 249 ASP A CB  
2012 C  CG  . ASP A 254 ? 0.94098 0.79243 0.89067 -0.07636 0.00790  -0.01932 249 ASP A CG  
2013 O  OD1 . ASP A 254 ? 0.95571 0.79139 0.89510 -0.06798 0.00703  -0.01660 249 ASP A OD1 
2014 O  OD2 . ASP A 254 ? 0.93533 0.80459 0.89270 -0.07566 0.00409  -0.02600 249 ASP A OD2 
2015 N  N   . GLY A 255 ? 0.84311 0.67866 0.77555 -0.08618 0.02899  0.01099  250 GLY A N   
2016 C  CA  . GLY A 255 ? 0.80597 0.63216 0.73217 -0.09327 0.03735  0.01882  250 GLY A CA  
2017 C  C   . GLY A 255 ? 0.76873 0.61534 0.70763 -0.10303 0.04344  0.01779  250 GLY A C   
2018 O  O   . GLY A 255 ? 0.88240 0.72297 0.81597 -0.10882 0.05205  0.02490  250 GLY A O   
2019 N  N   . LYS A 256 ? 0.61045 0.48103 0.56542 -0.10431 0.03974  0.00959  251 LYS A N   
2020 C  CA  . LYS A 256 ? 0.66750 0.56088 0.63681 -0.11191 0.04485  0.00778  251 LYS A CA  
2021 C  C   . LYS A 256 ? 0.55349 0.46695 0.52351 -0.10214 0.04306  0.00777  251 LYS A C   
2022 O  O   . LYS A 256 ? 0.49973 0.41568 0.46687 -0.09196 0.03596  0.00527  251 LYS A O   
2023 C  CB  . LYS A 256 ? 0.62899 0.53601 0.61718 -0.12039 0.04138  -0.00219 251 LYS A CB  
2024 C  CG  . LYS A 256 ? 0.88454 0.77002 0.87222 -0.12915 0.04074  -0.00497 251 LYS A CG  
2025 C  CD  . LYS A 256 ? 0.93450 0.83494 0.94002 -0.13606 0.03477  -0.01690 251 LYS A CD  
2026 C  CE  . LYS A 256 ? 1.08333 0.95952 1.08545 -0.14214 0.03190  -0.02162 251 LYS A CE  
2027 N  NZ  . LYS A 256 ? 1.00827 0.90003 1.02898 -0.14976 0.02604  -0.03343 251 LYS A NZ  
2028 N  N   . TRP A 257 ? 0.48330 0.41015 0.45714 -0.10537 0.05036  0.01058  252 TRP A N   
2029 C  CA  . TRP A 257 ? 0.51687 0.46241 0.49226 -0.09692 0.04957  0.00964  252 TRP A CA  
2030 C  C   . TRP A 257 ? 0.46858 0.44037 0.46439 -0.09978 0.04835  0.00216  252 TRP A C   
2031 O  O   . TRP A 257 ? 0.60494 0.58573 0.61415 -0.11051 0.05300  0.00013  252 TRP A O   
2032 C  CB  . TRP A 257 ? 0.56109 0.50519 0.52571 -0.09634 0.05823  0.01678  252 TRP A CB  
2033 C  CG  . TRP A 257 ? 0.51095 0.43228 0.45348 -0.08986 0.05735  0.02380  252 TRP A CG  
2034 C  CD1 . TRP A 257 ? 0.51801 0.41692 0.44736 -0.09400 0.06209  0.03110  252 TRP A CD1 
2035 C  CD2 . TRP A 257 ? 0.42794 0.34701 0.35970 -0.07770 0.05081  0.02394  252 TRP A CD2 
2036 N  NE1 . TRP A 257 ? 0.55106 0.43501 0.46130 -0.08386 0.05810  0.03581  252 TRP A NE1 
2037 C  CE2 . TRP A 257 ? 0.50312 0.40029 0.41576 -0.07437 0.05095  0.03097  252 TRP A CE2 
2038 C  CE3 . TRP A 257 ? 0.38370 0.31669 0.32066 -0.06950 0.04498  0.01876  252 TRP A CE3 
2039 C  CZ2 . TRP A 257 ? 0.47074 0.36262 0.37125 -0.06328 0.04442  0.03195  252 TRP A CZ2 
2040 C  CZ3 . TRP A 257 ? 0.43023 0.35632 0.35576 -0.05993 0.03955  0.01982  252 TRP A CZ3 
2041 C  CH2 . TRP A 257 ? 0.42610 0.33331 0.33443 -0.05696 0.03883  0.02588  252 TRP A CH2 
2042 N  N   . SER A 258 ? 0.49144 0.47545 0.49016 -0.09007 0.04212  -0.00186 253 SER A N   
2043 C  CA  . SER A 258 ? 0.43904 0.44782 0.45472 -0.08941 0.03993  -0.00834 253 SER A CA  
2044 C  C   . SER A 258 ? 0.42153 0.44172 0.43534 -0.07924 0.04060  -0.00777 253 SER A C   
2045 O  O   . SER A 258 ? 0.36844 0.37721 0.36920 -0.07157 0.03894  -0.00478 253 SER A O   
2046 C  CB  . SER A 258 ? 0.48258 0.49272 0.50312 -0.08695 0.03060  -0.01472 253 SER A CB  
2047 O  OG  . SER A 258 ? 0.57515 0.56896 0.58207 -0.07863 0.02593  -0.01276 253 SER A OG  
2048 N  N   . ASN A 259 ? 0.43340 0.47643 0.46135 -0.07918 0.04288  -0.01125 254 ASN A N   
2049 C  CA  . ASN A 259 ? 0.42793 0.48134 0.45489 -0.06924 0.04396  -0.01149 254 ASN A CA  
2050 C  C   . ASN A 259 ? 0.42670 0.47981 0.45230 -0.05905 0.03565  -0.01434 254 ASN A C   
2051 O  O   . ASN A 259 ? 0.48995 0.54625 0.52140 -0.05924 0.02949  -0.01796 254 ASN A O   
2052 C  CB  . ASN A 259 ? 0.46166 0.54034 0.50516 -0.07107 0.04912  -0.01449 254 ASN A CB  
2053 C  CG  . ASN A 259 ? 0.56925 0.64934 0.61386 -0.08050 0.05990  -0.01072 254 ASN A CG  
2054 O  OD1 . ASN A 259 ? 0.57958 0.64251 0.60764 -0.08096 0.06461  -0.00493 254 ASN A OD1 
2055 N  ND2 . ASN A 259 ? 0.63803 0.73926 0.70228 -0.08785 0.06407  -0.01389 254 ASN A ND2 
2056 N  N   . VAL A 260 ? 0.32969 0.37824 0.34691 -0.05019 0.03582  -0.01285 255 VAL A N   
2057 C  CA  . VAL A 260 ? 0.33780 0.38556 0.35409 -0.04053 0.03014  -0.01457 255 VAL A CA  
2058 C  C   . VAL A 260 ? 0.50250 0.56558 0.52541 -0.03336 0.03248  -0.01670 255 VAL A C   
2059 O  O   . VAL A 260 ? 0.45720 0.51922 0.47532 -0.03095 0.03735  -0.01575 255 VAL A O   
2060 C  CB  . VAL A 260 ? 0.39976 0.42859 0.40311 -0.03650 0.02821  -0.01175 255 VAL A CB  
2061 C  CG1 . VAL A 260 ? 0.43923 0.46738 0.44302 -0.02726 0.02457  -0.01290 255 VAL A CG1 
2062 C  CG2 . VAL A 260 ? 0.44308 0.45769 0.44073 -0.04179 0.02557  -0.00988 255 VAL A CG2 
2063 N  N   . GLU A 261 ? 0.42115 0.49832 0.45410 -0.02911 0.02875  -0.01992 256 GLU A N   
2064 C  CA  . GLU A 261 ? 0.39180 0.48420 0.43194 -0.02056 0.03020  -0.02204 256 GLU A CA  
2065 C  C   . GLU A 261 ? 0.46927 0.55531 0.50474 -0.00975 0.02530  -0.02169 256 GLU A C   
2066 O  O   . GLU A 261 ? 0.54757 0.63241 0.58273 -0.00874 0.01961  -0.02217 256 GLU A O   
2067 C  CB  . GLU A 261 ? 0.40968 0.52674 0.46687 -0.02355 0.03004  -0.02595 256 GLU A CB  
2068 C  CG  . GLU A 261 ? 0.40907 0.53267 0.47297 -0.03589 0.03646  -0.02578 256 GLU A CG  
2069 C  CD  . GLU A 261 ? 0.66409 0.78520 0.72195 -0.03525 0.04552  -0.02317 256 GLU A CD  
2070 O  OE1 . GLU A 261 ? 0.66968 0.79435 0.72581 -0.02501 0.04699  -0.02406 256 GLU A OE1 
2071 O  OE2 . GLU A 261 ? 0.61906 0.73328 0.67242 -0.04446 0.05133  -0.02020 256 GLU A OE2 
2072 N  N   . ALA A 262 ? 0.52192 0.60238 0.55267 -0.00176 0.02803  -0.02088 257 ALA A N   
2073 C  CA  . ALA A 262 ? 0.49132 0.56296 0.51723 0.00838  0.02546  -0.01957 257 ALA A CA  
2074 C  C   . ALA A 262 ? 0.53720 0.62011 0.56848 0.01875  0.02728  -0.02122 257 ALA A C   
2075 O  O   . ALA A 262 ? 0.59493 0.68465 0.62920 0.01903  0.03226  -0.02310 257 ALA A O   
2076 C  CB  . ALA A 262 ? 0.41584 0.46615 0.43129 0.00834  0.02702  -0.01734 257 ALA A CB  
2077 N  N   . THR A 263 ? 0.32905 0.41312 0.36015 0.02831  0.02359  -0.02026 258 THR A N   
2078 C  CA  . THR A 263 ? 0.28923 0.38058 0.32359 0.04045  0.02499  -0.02105 258 THR A CA  
2079 C  C   . THR A 263 ? 0.33936 0.41073 0.36504 0.04503  0.02962  -0.01969 258 THR A C   
2080 O  O   . THR A 263 ? 0.32394 0.37672 0.34180 0.04003  0.03015  -0.01772 258 THR A O   
2081 C  CB  . THR A 263 ? 0.37647 0.47263 0.41033 0.05051  0.01928  -0.01954 258 THR A CB  
2082 O  OG1 . THR A 263 ? 0.33191 0.40688 0.35376 0.05146  0.01827  -0.01507 258 THR A OG1 
2083 C  CG2 . THR A 263 ? 0.33903 0.45708 0.38281 0.04604  0.01335  -0.02297 258 THR A CG2 
2084 N  N   . PRO A 264 ? 0.28383 0.35890 0.31166 0.05454  0.03287  -0.02142 259 PRO A N   
2085 C  CA  . PRO A 264 ? 0.35974 0.41385 0.37932 0.05889  0.03687  -0.02131 259 PRO A CA  
2086 C  C   . PRO A 264 ? 0.38506 0.41890 0.39701 0.06234  0.03527  -0.01658 259 PRO A C   
2087 O  O   . PRO A 264 ? 0.47236 0.50938 0.48374 0.06890  0.03209  -0.01314 259 PRO A O   
2088 C  CB  . PRO A 264 ? 0.39989 0.46313 0.42367 0.07107  0.03987  -0.02393 259 PRO A CB  
2089 C  CG  . PRO A 264 ? 0.44611 0.53830 0.48232 0.06918  0.03916  -0.02653 259 PRO A CG  
2090 C  CD  . PRO A 264 ? 0.37354 0.47236 0.41244 0.06188  0.03311  -0.02432 259 PRO A CD  
2091 N  N   . HIS A 265 ? 0.43729 0.45103 0.44340 0.05752  0.03755  -0.01653 260 HIS A N   
2092 C  CA  . HIS A 265 ? 0.34948 0.34196 0.35006 0.05920  0.03840  -0.01241 260 HIS A CA  
2093 C  C   . HIS A 265 ? 0.35320 0.34482 0.35237 0.05315  0.03542  -0.00836 260 HIS A C   
2094 O  O   . HIS A 265 ? 0.32368 0.29935 0.31903 0.05384  0.03714  -0.00431 260 HIS A O   
2095 C  CB  . HIS A 265 ? 0.34351 0.32869 0.34122 0.07299  0.04028  -0.00913 260 HIS A CB  
2096 C  CG  . HIS A 265 ? 0.35311 0.33954 0.35219 0.08084  0.04328  -0.01346 260 HIS A CG  
2097 N  ND1 . HIS A 265 ? 0.37982 0.38116 0.38206 0.09262  0.04255  -0.01360 260 HIS A ND1 
2098 C  CD2 . HIS A 265 ? 0.36550 0.34105 0.36317 0.07913  0.04675  -0.01863 260 HIS A CD2 
2099 C  CE1 . HIS A 265 ? 0.46485 0.46380 0.46765 0.09824  0.04636  -0.01821 260 HIS A CE1 
2100 N  NE2 . HIS A 265 ? 0.38583 0.36845 0.38493 0.09011  0.04894  -0.02156 260 HIS A NE2 
2101 N  N   . THR A 266 ? 0.26978 0.27723 0.27209 0.04715  0.03176  -0.00949 261 THR A N   
2102 C  CA  . THR A 266 ? 0.27963 0.28423 0.27995 0.04004  0.02924  -0.00722 261 THR A CA  
2103 C  C   . THR A 266 ? 0.30722 0.30384 0.30750 0.02996  0.03006  -0.00915 261 THR A C   
2104 O  O   . THR A 266 ? 0.39544 0.39701 0.39714 0.02613  0.03074  -0.01287 261 THR A O   
2105 C  CB  . THR A 266 ? 0.31202 0.33504 0.31576 0.03762  0.02468  -0.00858 261 THR A CB  
2106 O  OG1 . THR A 266 ? 0.41426 0.44679 0.41831 0.04812  0.02242  -0.00759 261 THR A OG1 
2107 C  CG2 . THR A 266 ? 0.36974 0.38799 0.37009 0.03124  0.02214  -0.00692 261 THR A CG2 
2108 N  N   . LEU A 267 ? 0.28505 0.26998 0.28333 0.02647  0.03015  -0.00658 262 LEU A N   
2109 C  CA  . LEU A 267 ? 0.30225 0.28119 0.30120 0.01806  0.02962  -0.00851 262 LEU A CA  
2110 C  C   . LEU A 267 ? 0.32960 0.31463 0.32790 0.01177  0.02634  -0.00798 262 LEU A C   
2111 O  O   . LEU A 267 ? 0.35208 0.34108 0.34922 0.01344  0.02483  -0.00586 262 LEU A O   
2112 C  CB  . LEU A 267 ? 0.32396 0.28762 0.32418 0.01757  0.03197  -0.00684 262 LEU A CB  
2113 C  CG  . LEU A 267 ? 0.34174 0.29530 0.34315 0.02101  0.03518  -0.00899 262 LEU A CG  
2114 C  CD1 . LEU A 267 ? 0.35667 0.29544 0.36168 0.01974  0.03848  -0.00656 262 LEU A CD1 
2115 C  CD2 . LEU A 267 ? 0.35395 0.30908 0.35505 0.01713  0.03354  -0.01530 262 LEU A CD2 
2116 N  N   . LEU A 268 ? 0.27756 0.26221 0.27521 0.00520  0.02505  -0.01015 263 LEU A N   
2117 C  CA  . LEU A 268 ? 0.27460 0.26019 0.27068 -0.00068 0.02237  -0.00929 263 LEU A CA  
2118 C  C   . LEU A 268 ? 0.31520 0.29064 0.31173 -0.00299 0.02148  -0.00867 263 LEU A C   
2119 O  O   . LEU A 268 ? 0.34491 0.31585 0.34204 -0.00410 0.02128  -0.01096 263 LEU A O   
2120 C  CB  . LEU A 268 ? 0.29679 0.28877 0.29072 -0.00572 0.02200  -0.01103 263 LEU A CB  
2121 C  CG  . LEU A 268 ? 0.33291 0.33831 0.32977 -0.00596 0.02270  -0.01175 263 LEU A CG  
2122 C  CD1 . LEU A 268 ? 0.38492 0.39626 0.38049 -0.00954 0.02542  -0.01331 263 LEU A CD1 
2123 C  CD2 . LEU A 268 ? 0.43697 0.44394 0.43414 -0.01000 0.01997  -0.01081 263 LEU A CD2 
2124 N  N   . ILE A 269 ? 0.29180 0.26464 0.28847 -0.00333 0.02070  -0.00631 264 ILE A N   
2125 C  CA  . ILE A 269 ? 0.29381 0.25982 0.29328 -0.00492 0.02018  -0.00566 264 ILE A CA  
2126 C  C   . ILE A 269 ? 0.34167 0.30765 0.33773 -0.00844 0.01703  -0.00542 264 ILE A C   
2127 O  O   . ILE A 269 ? 0.32611 0.29413 0.31889 -0.00856 0.01649  -0.00458 264 ILE A O   
2128 C  CB  . ILE A 269 ? 0.34000 0.30185 0.34228 -0.00116 0.02359  -0.00258 264 ILE A CB  
2129 C  CG1 . ILE A 269 ? 0.43605 0.39607 0.43863 0.00377  0.02737  -0.00123 264 ILE A CG1 
2130 C  CG2 . ILE A 269 ? 0.40619 0.36344 0.41543 -0.00315 0.02415  -0.00257 264 ILE A CG2 
2131 C  CD1 . ILE A 269 ? 0.36886 0.32440 0.37595 0.00283  0.02854  -0.00384 264 ILE A CD1 
2132 N  N   . ASN A 270 ? 0.32778 0.29075 0.32419 -0.01080 0.01452  -0.00650 265 ASN A N   
2133 C  CA  . ASN A 270 ? 0.31306 0.27321 0.30556 -0.01267 0.01173  -0.00549 265 ASN A CA  
2134 C  C   . ASN A 270 ? 0.37685 0.33417 0.37485 -0.01153 0.00980  -0.00578 265 ASN A C   
2135 O  O   . ASN A 270 ? 0.31738 0.27565 0.32127 -0.01145 0.00906  -0.00796 265 ASN A O   
2136 C  CB  . ASN A 270 ? 0.33756 0.29741 0.32219 -0.01602 0.01000  -0.00569 265 ASN A CB  
2137 C  CG  . ASN A 270 ? 0.39782 0.35749 0.38069 -0.01591 0.00829  -0.00777 265 ASN A CG  
2138 O  OD1 . ASN A 270 ? 0.42185 0.38483 0.40538 -0.01533 0.01010  -0.00989 265 ASN A OD1 
2139 N  ND2 . ASN A 270 ? 0.35246 0.30804 0.33195 -0.01560 0.00430  -0.00759 265 ASN A ND2 
2140 N  N   . LEU A 271 ? 0.36045 0.31484 0.35758 -0.01049 0.00888  -0.00428 266 LEU A N   
2141 C  CA  . LEU A 271 ? 0.31112 0.26495 0.31422 -0.00874 0.00639  -0.00473 266 LEU A CA  
2142 C  C   . LEU A 271 ? 0.33490 0.28709 0.33233 -0.00945 0.00104  -0.00562 266 LEU A C   
2143 O  O   . LEU A 271 ? 0.38346 0.33216 0.37011 -0.01138 0.00042  -0.00442 266 LEU A O   
2144 C  CB  . LEU A 271 ? 0.35926 0.30987 0.36174 -0.00601 0.00720  -0.00306 266 LEU A CB  
2145 C  CG  . LEU A 271 ? 0.45980 0.41051 0.46188 -0.00442 0.01217  -0.00193 266 LEU A CG  
2146 C  CD1 . LEU A 271 ? 0.47397 0.42080 0.47416 -0.00099 0.01273  -0.00134 266 LEU A CD1 
2147 C  CD2 . LEU A 271 ? 0.47416 0.42882 0.48592 -0.00343 0.01651  -0.00152 266 LEU A CD2 
2148 N  N   . GLY A 272 ? 0.32399 0.27918 0.32883 -0.00771 -0.00273 -0.00769 267 GLY A N   
2149 C  CA  . GLY A 272 ? 0.29808 0.25181 0.29630 -0.00625 -0.00906 -0.00840 267 GLY A CA  
2150 C  C   . GLY A 272 ? 0.32560 0.27771 0.32550 -0.00180 -0.01239 -0.00689 267 GLY A C   
2151 O  O   . GLY A 272 ? 0.32843 0.28114 0.33552 -0.00003 -0.00930 -0.00586 267 GLY A O   
2152 N  N   . ASP A 273 ? 0.32176 0.27164 0.31371 0.00115  -0.01875 -0.00675 268 ASP A N   
2153 C  CA  . ASP A 273 ? 0.36419 0.31067 0.35474 0.00699  -0.02250 -0.00465 268 ASP A CA  
2154 C  C   . ASP A 273 ? 0.30535 0.26276 0.31543 0.01029  -0.02398 -0.00770 268 ASP A C   
2155 O  O   . ASP A 273 ? 0.33010 0.28604 0.34318 0.01523  -0.02382 -0.00603 268 ASP A O   
2156 C  CB  . ASP A 273 ? 0.33490 0.27657 0.31124 0.01083  -0.02945 -0.00336 268 ASP A CB  
2157 C  CG  . ASP A 273 ? 0.39165 0.32069 0.34827 0.00788  -0.02606 0.00136  268 ASP A CG  
2158 O  OD1 . ASP A 273 ? 0.40114 0.32560 0.35685 0.00316  -0.01949 0.00319  268 ASP A OD1 
2159 O  OD2 . ASP A 273 ? 0.43966 0.36391 0.38182 0.01029  -0.02985 0.00313  268 ASP A OD2 
2160 N  N   . THR A 274 ? 0.30110 0.26931 0.32543 0.00749  -0.02483 -0.01244 269 THR A N   
2161 C  CA  . THR A 274 ? 0.29150 0.27148 0.33773 0.00884  -0.02442 -0.01532 269 THR A CA  
2162 C  C   . THR A 274 ? 0.35065 0.32884 0.40217 0.00866  -0.01516 -0.01222 269 THR A C   
2163 O  O   . THR A 274 ? 0.30567 0.28883 0.36738 0.01313  -0.01390 -0.01185 269 THR A O   
2164 C  CB  . THR A 274 ? 0.35044 0.33988 0.41156 0.00380  -0.02548 -0.02112 269 THR A CB  
2165 O  OG1 . THR A 274 ? 0.34432 0.33556 0.39878 0.00466  -0.03494 -0.02529 269 THR A OG1 
2166 C  CG2 . THR A 274 ? 0.27428 0.27694 0.36085 0.00404  -0.02403 -0.02390 269 THR A CG2 
2167 N  N   . MET A 275 ? 0.29959 0.27138 0.34371 0.00447  -0.00871 -0.01020 270 MET A N   
2168 C  CA  . MET A 275 ? 0.32812 0.29786 0.37417 0.00525  -0.00052 -0.00750 270 MET A CA  
2169 C  C   . MET A 275 ? 0.32979 0.29112 0.36419 0.00990  -0.00075 -0.00494 270 MET A C   
2170 O  O   . MET A 275 ? 0.27926 0.24138 0.31823 0.01376  0.00369  -0.00413 270 MET A O   
2171 C  CB  . MET A 275 ? 0.30482 0.27046 0.34479 0.00101  0.00500  -0.00623 270 MET A CB  
2172 C  CG  . MET A 275 ? 0.36889 0.33184 0.40704 0.00304  0.01260  -0.00343 270 MET A CG  
2173 S  SD  . MET A 275 ? 0.36836 0.33979 0.42596 0.00489  0.01992  -0.00293 270 MET A SD  
2174 C  CE  . MET A 275 ? 0.32782 0.29984 0.39186 -0.00069 0.02409  -0.00300 270 MET A CE  
2175 N  N   . GLU A 276 ? 0.31501 0.26710 0.33385 0.00959  -0.00509 -0.00369 271 GLU A N   
2176 C  CA  . GLU A 276 ? 0.32560 0.26686 0.33357 0.01336  -0.00516 -0.00163 271 GLU A CA  
2177 C  C   . GLU A 276 ? 0.31988 0.26426 0.33585 0.02104  -0.00762 -0.00204 271 GLU A C   
2178 O  O   . GLU A 276 ? 0.32610 0.26562 0.34061 0.02552  -0.00441 -0.00158 271 GLU A O   
2179 C  CB  . GLU A 276 ? 0.37088 0.30063 0.36205 0.01113  -0.00867 0.00047  271 GLU A CB  
2180 C  CG  . GLU A 276 ? 0.31789 0.23340 0.29827 0.01451  -0.00853 0.00241  271 GLU A CG  
2181 C  CD  . GLU A 276 ? 0.43481 0.33679 0.39899 0.01051  -0.00960 0.00524  271 GLU A CD  
2182 O  OE1 . GLU A 276 ? 0.43107 0.33577 0.39211 0.00420  -0.00851 0.00547  271 GLU A OE1 
2183 O  OE2 . GLU A 276 ? 0.39376 0.28182 0.34865 0.01384  -0.01077 0.00738  271 GLU A OE2 
2184 N  N   . VAL A 277 ? 0.30197 0.25526 0.32667 0.02335  -0.01369 -0.00360 272 VAL A N   
2185 C  CA  . VAL A 277 ? 0.29841 0.25826 0.33376 0.03155  -0.01674 -0.00451 272 VAL A CA  
2186 C  C   . VAL A 277 ? 0.30937 0.28095 0.36346 0.03236  -0.00958 -0.00614 272 VAL A C   
2187 O  O   . VAL A 277 ? 0.29438 0.26543 0.35134 0.03900  -0.00652 -0.00567 272 VAL A O   
2188 C  CB  . VAL A 277 ? 0.31525 0.28453 0.35655 0.03397  -0.02628 -0.00681 272 VAL A CB  
2189 C  CG1 . VAL A 277 ? 0.34879 0.32911 0.40517 0.04310  -0.02998 -0.00850 272 VAL A CG1 
2190 C  CG2 . VAL A 277 ? 0.32230 0.27785 0.34140 0.03492  -0.03210 -0.00384 272 VAL A CG2 
2191 N  N   . MET A 278 ? 0.29995 0.28085 0.36600 0.02585  -0.00580 -0.00777 273 MET A N   
2192 C  CA  . MET A 278 ? 0.28456 0.27672 0.36947 0.02604  0.00217  -0.00845 273 MET A CA  
2193 C  C   . MET A 278 ? 0.31230 0.29600 0.38787 0.02831  0.01126  -0.00560 273 MET A C   
2194 O  O   . MET A 278 ? 0.31240 0.30291 0.39891 0.03261  0.01784  -0.00539 273 MET A O   
2195 C  CB  . MET A 278 ? 0.26760 0.26769 0.36549 0.01800  0.00474  -0.01026 273 MET A CB  
2196 C  CG  . MET A 278 ? 0.29205 0.30440 0.40495 0.01631  -0.00394 -0.01518 273 MET A CG  
2197 S  SD  . MET A 278 ? 0.36106 0.37850 0.48744 0.00610  -0.00143 -0.01857 273 MET A SD  
2198 C  CE  . MET A 278 ? 0.38328 0.40857 0.53059 0.00454  0.01233  -0.01632 273 MET A CE  
2199 N  N   . CYS A 279 ? 0.29746 0.26748 0.35329 0.02580  0.01180  -0.00389 274 CYS A N   
2200 C  CA  . CYS A 279 ? 0.29917 0.26093 0.34403 0.02852  0.01845  -0.00252 274 CYS A CA  
2201 C  C   . CYS A 279 ? 0.34294 0.29285 0.37464 0.03443  0.01522  -0.00296 274 CYS A C   
2202 O  O   . CYS A 279 ? 0.33826 0.27805 0.35665 0.03572  0.01843  -0.00319 274 CYS A O   
2203 C  CB  . CYS A 279 ? 0.32542 0.28095 0.35846 0.02278  0.02073  -0.00142 274 CYS A CB  
2204 S  SG  . CYS A 279 ? 0.37614 0.31936 0.39072 0.01856  0.01363  -0.00172 274 CYS A SG  
2205 N  N   . ASN A 280 ? 0.27015 0.22033 0.30473 0.03850  0.00858  -0.00338 275 ASN A N   
2206 C  CA  . ASN A 280 ? 0.30823 0.24538 0.33134 0.04542  0.00573  -0.00332 275 ASN A CA  
2207 C  C   . ASN A 280 ? 0.36521 0.28386 0.36741 0.04105  0.00448  -0.00271 275 ASN A C   
2208 O  O   . ASN A 280 ? 0.34509 0.25015 0.33634 0.04507  0.00548  -0.00364 275 ASN A O   
2209 C  CB  . ASN A 280 ? 0.27769 0.21689 0.30583 0.05391  0.01202  -0.00463 275 ASN A CB  
2210 C  CG  . ASN A 280 ? 0.34424 0.27523 0.36843 0.06364  0.00790  -0.00498 275 ASN A CG  
2211 O  OD1 . ASN A 280 ? 0.36579 0.29686 0.39109 0.06570  0.00018  -0.00384 275 ASN A OD1 
2212 N  ND2 . ASN A 280 ? 0.31889 0.24152 0.33661 0.07066  0.01283  -0.00663 275 ASN A ND2 
2213 N  N   . GLY A 281 ? 0.36542 0.28356 0.36289 0.03266  0.00245  -0.00174 276 GLY A N   
2214 C  CA  . GLY A 281 ? 0.35873 0.26218 0.33990 0.02741  0.00154  -0.00140 276 GLY A CA  
2215 C  C   . GLY A 281 ? 0.38688 0.28684 0.36205 0.02515  0.00622  -0.00373 276 GLY A C   
2216 O  O   . GLY A 281 ? 0.38890 0.27745 0.35250 0.02057  0.00510  -0.00470 276 GLY A O   
2217 N  N   . ILE A 282 ? 0.35597 0.26537 0.33843 0.02834  0.01152  -0.00474 277 ILE A N   
2218 C  CA  . ILE A 282 ? 0.37330 0.28058 0.34788 0.02704  0.01526  -0.00677 277 ILE A CA  
2219 C  C   . ILE A 282 ? 0.39239 0.30281 0.36437 0.01884  0.01370  -0.00632 277 ILE A C   
2220 O  O   . ILE A 282 ? 0.38743 0.29289 0.34994 0.01582  0.01293  -0.00873 277 ILE A O   
2221 C  CB  . ILE A 282 ? 0.43441 0.35124 0.41613 0.03262  0.02246  -0.00638 277 ILE A CB  
2222 C  CG1 . ILE A 282 ? 0.38152 0.29616 0.36588 0.04164  0.02490  -0.00749 277 ILE A CG1 
2223 C  CG2 . ILE A 282 ? 0.45749 0.37273 0.42859 0.03224  0.02568  -0.00783 277 ILE A CG2 
2224 C  CD1 . ILE A 282 ? 0.42895 0.35499 0.42308 0.04695  0.03370  -0.00626 277 ILE A CD1 
2225 N  N   . PHE A 283 ? 0.37350 0.29310 0.35459 0.01554  0.01295  -0.00401 278 PHE A N   
2226 C  CA  . PHE A 283 ? 0.36689 0.28965 0.34637 0.00868  0.01134  -0.00355 278 PHE A CA  
2227 C  C   . PHE A 283 ? 0.40779 0.32744 0.38627 0.00533  0.00667  -0.00228 278 PHE A C   
2228 O  O   . PHE A 283 ? 0.39093 0.31062 0.37372 0.00885  0.00445  -0.00130 278 PHE A O   
2229 C  CB  . PHE A 283 ? 0.35115 0.28492 0.33984 0.00819  0.01487  -0.00220 278 PHE A CB  
2230 C  CG  . PHE A 283 ? 0.36909 0.30536 0.35805 0.01270  0.02086  -0.00175 278 PHE A CG  
2231 C  CD1 . PHE A 283 ? 0.42867 0.35967 0.40606 0.01503  0.02155  -0.00360 278 PHE A CD1 
2232 C  CD2 . PHE A 283 ? 0.35329 0.29672 0.35358 0.01446  0.02603  0.00042  278 PHE A CD2 
2233 C  CE1 . PHE A 283 ? 0.42202 0.35472 0.39647 0.02046  0.02738  -0.00273 278 PHE A CE1 
2234 C  CE2 . PHE A 283 ? 0.42923 0.37372 0.42811 0.01888  0.03315  0.00216  278 PHE A CE2 
2235 C  CZ  . PHE A 283 ? 0.38440 0.32340 0.36896 0.02255  0.03381  0.00087  278 PHE A CZ  
2236 N  N   . ARG A 284 ? 0.42485 0.34287 0.39760 -0.00085 0.00533  -0.00223 279 ARG A N   
2237 C  CA  . ARG A 284 ? 0.42339 0.33607 0.39109 -0.00407 0.00223  -0.00035 279 ARG A CA  
2238 C  C   . ARG A 284 ? 0.43760 0.35950 0.40916 -0.00711 0.00191  0.00024  279 ARG A C   
2239 O  O   . ARG A 284 ? 0.44274 0.37267 0.41850 -0.00900 0.00424  -0.00092 279 ARG A O   
2240 C  CB  . ARG A 284 ? 0.62450 0.52717 0.58271 -0.00956 0.00227  -0.00069 279 ARG A CB  
2241 C  CG  . ARG A 284 ? 0.65973 0.56996 0.61948 -0.01457 0.00404  -0.00316 279 ARG A CG  
2242 C  CD  . ARG A 284 ? 0.75360 0.65631 0.70756 -0.02179 0.00393  -0.00420 279 ARG A CD  
2243 N  NE  . ARG A 284 ? 0.76964 0.66146 0.71893 -0.02099 0.00309  -0.00735 279 ARG A NE  
2244 C  CZ  . ARG A 284 ? 0.89125 0.77318 0.83621 -0.02754 0.00278  -0.00927 279 ARG A CZ  
2245 N  NH1 . ARG A 284 ? 0.83053 0.71282 0.77592 -0.03566 0.00420  -0.00744 279 ARG A NH1 
2246 N  NH2 . ARG A 284 ? 0.83067 0.70180 0.77100 -0.02615 0.00157  -0.01344 279 ARG A NH2 
2247 N  N   . SER A 285 ? 0.32751 0.24744 0.29634 -0.00644 -0.00126 0.00188  280 SER A N   
2248 C  CA  . SER A 285 ? 0.36920 0.29545 0.33807 -0.00912 -0.00195 0.00172  280 SER A CA  
2249 C  C   . SER A 285 ? 0.34896 0.26953 0.30712 -0.01445 -0.00045 0.00369  280 SER A C   
2250 O  O   . SER A 285 ? 0.38485 0.29453 0.33338 -0.01433 -0.00160 0.00666  280 SER A O   
2251 C  CB  . SER A 285 ? 0.39018 0.31841 0.36063 -0.00499 -0.00679 0.00158  280 SER A CB  
2252 O  OG  . SER A 285 ? 0.38030 0.31222 0.34696 -0.00711 -0.00798 0.00078  280 SER A OG  
2253 N  N   . PRO A 286 ? 0.35443 0.28179 0.31430 -0.01888 0.00269  0.00248  281 PRO A N   
2254 C  CA  . PRO A 286 ? 0.33953 0.26353 0.29277 -0.02495 0.00551  0.00400  281 PRO A CA  
2255 C  C   . PRO A 286 ? 0.32044 0.24257 0.26491 -0.02606 0.00611  0.00657  281 PRO A C   
2256 O  O   . PRO A 286 ? 0.33742 0.26602 0.28264 -0.02348 0.00491  0.00515  281 PRO A O   
2257 C  CB  . PRO A 286 ? 0.30756 0.24306 0.26843 -0.02755 0.00815  0.00109  281 PRO A CB  
2258 C  CG  . PRO A 286 ? 0.34221 0.28546 0.30953 -0.02297 0.00741  -0.00061 281 PRO A CG  
2259 C  CD  . PRO A 286 ? 0.36736 0.30555 0.33639 -0.01823 0.00440  -0.00019 281 PRO A CD  
2260 N  N   . VAL A 287 ? 0.34100 0.25286 0.27607 -0.02990 0.00835  0.01030  282 VAL A N   
2261 C  CA  . VAL A 287 ? 0.34318 0.25232 0.26725 -0.03139 0.01092  0.01380  282 VAL A CA  
2262 C  C   . VAL A 287 ? 0.34163 0.26223 0.27060 -0.03715 0.01657  0.01226  282 VAL A C   
2263 O  O   . VAL A 287 ? 0.36378 0.28730 0.29978 -0.04311 0.01956  0.01116  282 VAL A O   
2264 C  CB  . VAL A 287 ? 0.40548 0.29702 0.31676 -0.03323 0.01265  0.01969  282 VAL A CB  
2265 C  CG1 . VAL A 287 ? 0.41319 0.30147 0.31106 -0.03490 0.01719  0.02439  282 VAL A CG1 
2266 C  CG2 . VAL A 287 ? 0.45945 0.34066 0.36592 -0.02544 0.00654  0.02114  282 VAL A CG2 
2267 N  N   . HIS A 288 ? 0.36602 0.29369 0.29150 -0.03501 0.01772  0.01152  283 HIS A N   
2268 C  CA  . HIS A 288 ? 0.33595 0.27608 0.26669 -0.03861 0.02329  0.00965  283 HIS A CA  
2269 C  C   . HIS A 288 ? 0.35619 0.29510 0.27370 -0.03777 0.02724  0.01220  283 HIS A C   
2270 O  O   . HIS A 288 ? 0.38887 0.31832 0.29293 -0.03329 0.02411  0.01455  283 HIS A O   
2271 C  CB  . HIS A 288 ? 0.33300 0.28548 0.27555 -0.03494 0.02112  0.00413  283 HIS A CB  
2272 C  CG  . HIS A 288 ? 0.38480 0.33555 0.32531 -0.02846 0.01595  0.00181  283 HIS A CG  
2273 N  ND1 . HIS A 288 ? 0.31006 0.25522 0.25318 -0.02530 0.01047  0.00155  283 HIS A ND1 
2274 C  CD2 . HIS A 288 ? 0.37281 0.32732 0.31022 -0.02490 0.01544  -0.00119 283 HIS A CD2 
2275 C  CE1 . HIS A 288 ? 0.33840 0.28516 0.28195 -0.02095 0.00666  -0.00151 283 HIS A CE1 
2276 N  NE2 . HIS A 288 ? 0.33846 0.28985 0.27782 -0.02071 0.00919  -0.00355 283 HIS A NE2 
2277 N  N   . ARG A 289 ? 0.35921 0.30863 0.28021 -0.04138 0.03416  0.01155  284 ARG A N   
2278 C  CA  . ARG A 289 ? 0.36229 0.31192 0.27018 -0.04034 0.03980  0.01378  284 ARG A CA  
2279 C  C   . ARG A 289 ? 0.36988 0.33659 0.28768 -0.04095 0.04537  0.00974  284 ARG A C   
2280 O  O   . ARG A 289 ? 0.34883 0.32649 0.28310 -0.04277 0.04486  0.00627  284 ARG A O   
2281 C  CB  . ARG A 289 ? 0.34920 0.28771 0.24579 -0.04606 0.04653  0.02142  284 ARG A CB  
2282 C  CG  . ARG A 289 ? 0.36315 0.30962 0.27339 -0.05593 0.05420  0.02220  284 ARG A CG  
2283 C  CD  . ARG A 289 ? 0.41669 0.34840 0.31776 -0.06310 0.06083  0.02994  284 ARG A CD  
2284 N  NE  . ARG A 289 ? 0.41507 0.35657 0.33205 -0.07396 0.06845  0.02951  284 ARG A NE  
2285 C  CZ  . ARG A 289 ? 0.50415 0.43447 0.41919 -0.08323 0.07552  0.03517  284 ARG A CZ  
2286 N  NH1 . ARG A 289 ? 0.51124 0.41823 0.40689 -0.08199 0.07644  0.04276  284 ARG A NH1 
2287 N  NH2 . ARG A 289 ? 0.47174 0.41438 0.40526 -0.09389 0.08167  0.03303  284 ARG A NH2 
2288 N  N   . VAL A 290 ? 0.34178 0.31087 0.24838 -0.03830 0.05066  0.01011  285 VAL A N   
2289 C  CA  . VAL A 290 ? 0.33400 0.31930 0.24886 -0.03827 0.05768  0.00687  285 VAL A CA  
2290 C  C   . VAL A 290 ? 0.42040 0.40621 0.32573 -0.04260 0.06884  0.01233  285 VAL A C   
2291 O  O   . VAL A 290 ? 0.37895 0.35270 0.26344 -0.03995 0.07036  0.01642  285 VAL A O   
2292 C  CB  . VAL A 290 ? 0.34369 0.33269 0.25521 -0.02947 0.05453  0.00040  285 VAL A CB  
2293 C  CG1 . VAL A 290 ? 0.33774 0.34210 0.25469 -0.02800 0.06314  -0.00240 285 VAL A CG1 
2294 C  CG2 . VAL A 290 ? 0.32086 0.31019 0.24487 -0.02652 0.04582  -0.00424 285 VAL A CG2 
2295 N  N   . VAL A 291 ? 0.34451 0.34455 0.26508 -0.04912 0.07666  0.01256  286 VAL A N   
2296 C  CA  . VAL A 291 ? 0.36745 0.37192 0.28302 -0.05382 0.08959  0.01732  286 VAL A CA  
2297 C  C   . VAL A 291 ? 0.42185 0.44328 0.34065 -0.04776 0.09525  0.01234  286 VAL A C   
2298 O  O   . VAL A 291 ? 0.42051 0.45453 0.35406 -0.04341 0.09078  0.00561  286 VAL A O   
2299 C  CB  . VAL A 291 ? 0.45898 0.46971 0.39170 -0.06615 0.09564  0.02032  286 VAL A CB  
2300 C  CG1 . VAL A 291 ? 0.40940 0.39973 0.33590 -0.07130 0.09071  0.02510  286 VAL A CG1 
2301 C  CG2 . VAL A 291 ? 0.47742 0.50941 0.43665 -0.06750 0.09233  0.01316  286 VAL A CG2 
2302 N  N   . THR A 292 ? 0.37421 0.39472 0.27741 -0.04642 0.10556  0.01592  287 THR A N   
2303 C  CA  . THR A 292 ? 0.42541 0.46069 0.32882 -0.03967 0.11232  0.01118  287 THR A CA  
2304 C  C   . THR A 292 ? 0.40462 0.46249 0.33011 -0.04647 0.12389  0.01158  287 THR A C   
2305 O  O   . THR A 292 ? 0.44508 0.50690 0.38606 -0.05727 0.12596  0.01488  287 THR A O   
2306 C  CB  . THR A 292 ? 0.45138 0.47544 0.32531 -0.03350 0.11799  0.01403  287 THR A CB  
2307 O  OG1 . THR A 292 ? 0.48519 0.50240 0.34926 -0.04120 0.12894  0.02397  287 THR A OG1 
2308 C  CG2 . THR A 292 ? 0.44795 0.45293 0.30273 -0.02632 0.10478  0.01195  287 THR A CG2 
2309 N  N   . ASN A 293 ? 0.41809 0.49165 0.34610 -0.03991 0.13128  0.00732  288 ASN A N   
2310 C  CA  . ASN A 293 ? 0.41708 0.51477 0.36508 -0.04498 0.14414  0.00763  288 ASN A CA  
2311 C  C   . ASN A 293 ? 0.49124 0.59383 0.42361 -0.03747 0.15657  0.00750  288 ASN A C   
2312 O  O   . ASN A 293 ? 0.47032 0.55939 0.37899 -0.02725 0.15280  0.00485  288 ASN A O   
2313 C  CB  . ASN A 293 ? 0.44624 0.56595 0.42364 -0.04311 0.13845  0.00020  288 ASN A CB  
2314 C  CG  . ASN A 293 ? 0.39438 0.51848 0.36858 -0.02875 0.13457  -0.00747 288 ASN A CG  
2315 O  OD1 . ASN A 293 ? 0.42475 0.56612 0.40465 -0.02306 0.14386  -0.01054 288 ASN A OD1 
2316 N  ND2 . ASN A 293 ? 0.40103 0.50913 0.36675 -0.02279 0.12145  -0.01072 288 ASN A ND2 
2317 N  N   . ALA A 294 ? 0.42873 0.55142 0.37503 -0.04250 0.17143  0.00982  289 ALA A N   
2318 C  CA  . ALA A 294 ? 0.41817 0.54460 0.35011 -0.03421 0.18177  0.01199  289 ALA A CA  
2319 C  C   . ALA A 294 ? 0.41140 0.55479 0.35042 -0.02144 0.18313  0.00269  289 ALA A C   
2320 O  O   . ALA A 294 ? 0.47068 0.61683 0.39532 -0.01273 0.19078  0.00290  289 ALA A O   
2321 C  CB  . ALA A 294 ? 0.48719 0.62577 0.43210 -0.04285 0.19355  0.02092  289 ALA A CB  
2322 N  N   . GLU A 295 ? 0.42736 0.58240 0.38689 -0.01919 0.17529  -0.00552 290 GLU A N   
2323 C  CA  . GLU A 295 ? 0.58042 0.75310 0.55172 -0.00694 0.17722  -0.01312 290 GLU A CA  
2324 C  C   . GLU A 295 ? 0.51743 0.67852 0.47710 0.00530  0.16613  -0.02192 290 GLU A C   
2325 O  O   . GLU A 295 ? 0.51924 0.68334 0.47151 0.01746  0.17045  -0.02780 290 GLU A O   
2326 C  CB  . GLU A 295 ? 0.56897 0.76845 0.57795 -0.01099 0.17649  -0.01465 290 GLU A CB  
2327 C  CG  . GLU A 295 ? 0.61151 0.82605 0.63617 -0.01901 0.18862  -0.00741 290 GLU A CG  
2328 C  CD  . GLU A 295 ? 0.87572 1.11719 0.93842 -0.02403 0.18616  -0.00994 290 GLU A CD  
2329 O  OE1 . GLU A 295 ? 0.84350 1.09152 0.91888 -0.02094 0.17442  -0.01657 290 GLU A OE1 
2330 O  OE2 . GLU A 295 ? 0.93333 1.19002 1.01304 -0.03066 0.19561  -0.00518 290 GLU A OE2 
2331 N  N   . LYS A 296 ? 0.46505 0.60944 0.42320 0.00332  0.15092  -0.02232 291 LYS A N   
2332 C  CA  . LYS A 296 ? 0.43587 0.56890 0.38905 0.01428  0.13952  -0.02971 291 LYS A CA  
2333 C  C   . LYS A 296 ? 0.41507 0.52047 0.34823 0.01239  0.12784  -0.02865 291 LYS A C   
2334 O  O   . LYS A 296 ? 0.42662 0.52420 0.35924 0.00247  0.12391  -0.02248 291 LYS A O   
2335 C  CB  . LYS A 296 ? 0.43371 0.58067 0.41386 0.01627  0.13220  -0.03283 291 LYS A CB  
2336 C  CG  . LYS A 296 ? 0.59597 0.77282 0.59853 0.02062  0.14151  -0.03542 291 LYS A CG  
2337 C  CD  . LYS A 296 ? 0.59810 0.78577 0.62202 0.02678  0.13239  -0.03935 291 LYS A CD  
2338 C  CE  . LYS A 296 ? 0.84775 1.03795 0.88637 0.01578  0.12363  -0.03549 291 LYS A CE  
2339 N  NZ  . LYS A 296 ? 0.72406 0.92047 0.77773 0.02321  0.11330  -0.03882 291 LYS A NZ  
2340 N  N   . GLU A 297 ? 0.38135 0.47231 0.29931 0.02217  0.12214  -0.03540 292 GLU A N   
2341 C  CA  . GLU A 297 ? 0.32814 0.39624 0.23277 0.02114  0.10951  -0.03627 292 GLU A CA  
2342 C  C   . GLU A 297 ? 0.34097 0.40822 0.26479 0.01817  0.09912  -0.03601 292 GLU A C   
2343 O  O   . GLU A 297 ? 0.41574 0.49759 0.35966 0.02035  0.10008  -0.03721 292 GLU A O   
2344 C  CB  . GLU A 297 ? 0.39462 0.44863 0.28072 0.03151  0.10597  -0.04505 292 GLU A CB  
2345 C  CG  . GLU A 297 ? 0.44028 0.49437 0.33873 0.03991  0.10172  -0.05271 292 GLU A CG  
2346 C  CD  . GLU A 297 ? 0.50563 0.57866 0.41511 0.04760  0.11233  -0.05548 292 GLU A CD  
2347 O  OE1 . GLU A 297 ? 0.47325 0.56114 0.38175 0.04598  0.12391  -0.05205 292 GLU A OE1 
2348 O  OE2 . GLU A 297 ? 0.56357 0.63647 0.48299 0.05572  0.10957  -0.06089 292 GLU A OE2 
2349 N  N   . ARG A 298 ? 0.33271 0.38315 0.24938 0.01405  0.08914  -0.03441 293 ARG A N   
2350 C  CA  . ARG A 298 ? 0.32507 0.37189 0.25615 0.01124  0.07965  -0.03362 293 ARG A CA  
2351 C  C   . ARG A 298 ? 0.32580 0.35304 0.24615 0.01376  0.06977  -0.03760 293 ARG A C   
2352 O  O   . ARG A 298 ? 0.36842 0.38483 0.27086 0.01315  0.06774  -0.03792 293 ARG A O   
2353 C  CB  . ARG A 298 ? 0.31800 0.36766 0.25648 0.00060  0.07870  -0.02604 293 ARG A CB  
2354 C  CG  . ARG A 298 ? 0.32595 0.37161 0.27710 -0.00192 0.06934  -0.02517 293 ARG A CG  
2355 C  CD  . ARG A 298 ? 0.32932 0.37588 0.28556 -0.01204 0.06857  -0.01881 293 ARG A CD  
2356 N  NE  . ARG A 298 ? 0.30238 0.34492 0.26851 -0.01348 0.06015  -0.01842 293 ARG A NE  
2357 C  CZ  . ARG A 298 ? 0.35955 0.38659 0.31893 -0.01364 0.05271  -0.01795 293 ARG A CZ  
2358 N  NH1 . ARG A 298 ? 0.33254 0.34716 0.27609 -0.01264 0.05101  -0.01818 293 ARG A NH1 
2359 N  NH2 . ARG A 298 ? 0.31317 0.33820 0.28191 -0.01419 0.04677  -0.01753 293 ARG A NH2 
2360 N  N   . ILE A 299 ? 0.34978 0.37278 0.28125 0.01662  0.06365  -0.04049 294 ILE A N   
2361 C  CA  . ILE A 299 ? 0.31520 0.32110 0.24110 0.01744  0.05483  -0.04435 294 ILE A CA  
2362 C  C   . ILE A 299 ? 0.35761 0.36076 0.29658 0.01282  0.04865  -0.04027 294 ILE A C   
2363 O  O   . ILE A 299 ? 0.39293 0.40614 0.34511 0.01194  0.05045  -0.03664 294 ILE A O   
2364 C  CB  . ILE A 299 ? 0.33602 0.33455 0.26029 0.02588  0.05450  -0.05281 294 ILE A CB  
2365 C  CG1 . ILE A 299 ? 0.43454 0.44085 0.37470 0.03093  0.05757  -0.05233 294 ILE A CG1 
2366 C  CG2 . ILE A 299 ? 0.40890 0.40747 0.31645 0.03125  0.05981  -0.05826 294 ILE A CG2 
2367 C  CD1 . ILE A 299 ? 0.53894 0.53142 0.48078 0.03752  0.05487  -0.05850 294 ILE A CD1 
2368 N  N   . SER A 300 ? 0.34706 0.33757 0.28223 0.01026  0.04118  -0.04129 295 SER A N   
2369 C  CA  . SER A 300 ? 0.30831 0.29462 0.25518 0.00728  0.03598  -0.03851 295 SER A CA  
2370 C  C   . SER A 300 ? 0.33748 0.31042 0.28251 0.00760  0.02946  -0.04366 295 SER A C   
2371 O  O   . SER A 300 ? 0.36031 0.32788 0.29374 0.00880  0.02704  -0.04894 295 SER A O   
2372 C  CB  . SER A 300 ? 0.33714 0.32651 0.28545 0.00053  0.03438  -0.03165 295 SER A CB  
2373 O  OG  . SER A 300 ? 0.37101 0.35314 0.30717 -0.00187 0.03053  -0.03153 295 SER A OG  
2374 N  N   . LEU A 301 ? 0.32594 0.29409 0.28268 0.00652  0.02676  -0.04241 296 LEU A N   
2375 C  CA  . LEU A 301 ? 0.30018 0.25733 0.26022 0.00497  0.02113  -0.04672 296 LEU A CA  
2376 C  C   . LEU A 301 ? 0.33745 0.29479 0.30609 0.00026  0.01795  -0.04120 296 LEU A C   
2377 O  O   . LEU A 301 ? 0.31759 0.27665 0.29483 0.00057  0.02059  -0.03646 296 LEU A O   
2378 C  CB  . LEU A 301 ? 0.34155 0.29011 0.30825 0.00883  0.02317  -0.05108 296 LEU A CB  
2379 C  CG  . LEU A 301 ? 0.34633 0.28384 0.32160 0.00539  0.01880  -0.05467 296 LEU A CG  
2380 C  CD1 . LEU A 301 ? 0.36079 0.29611 0.32976 0.00246  0.01162  -0.06169 296 LEU A CD1 
2381 C  CD2 . LEU A 301 ? 0.37729 0.30319 0.35804 0.00903  0.02236  -0.05837 296 LEU A CD2 
2382 N  N   . ALA A 302 ? 0.34568 0.30147 0.31105 -0.00299 0.01216  -0.04201 297 ALA A N   
2383 C  CA  . ALA A 302 ? 0.32347 0.27934 0.29702 -0.00651 0.00899  -0.03777 297 ALA A CA  
2384 C  C   . ALA A 302 ? 0.31103 0.26112 0.29470 -0.00814 0.00475  -0.04284 297 ALA A C   
2385 O  O   . ALA A 302 ? 0.34133 0.28925 0.32110 -0.00832 -0.00066 -0.04961 297 ALA A O   
2386 C  CB  . ALA A 302 ? 0.29401 0.25255 0.25825 -0.00819 0.00554  -0.03457 297 ALA A CB  
2387 N  N   . MET A 303 ? 0.32500 0.27290 0.32164 -0.00937 0.00740  -0.03987 298 MET A N   
2388 C  CA  . MET A 303 ? 0.30482 0.24893 0.31464 -0.01254 0.00470  -0.04325 298 MET A CA  
2389 C  C   . MET A 303 ? 0.33579 0.28563 0.35005 -0.01465 0.00086  -0.03978 298 MET A C   
2390 O  O   . MET A 303 ? 0.32576 0.27771 0.34188 -0.01428 0.00430  -0.03296 298 MET A O   
2391 C  CB  . MET A 303 ? 0.27377 0.21122 0.29442 -0.01248 0.01124  -0.04086 298 MET A CB  
2392 C  CG  . MET A 303 ? 0.30650 0.23595 0.32355 -0.00913 0.01524  -0.04416 298 MET A CG  
2393 S  SD  . MET A 303 ? 0.38950 0.31310 0.40314 -0.01020 0.00978  -0.05656 298 MET A SD  
2394 C  CE  . MET A 303 ? 0.37344 0.29300 0.40644 -0.01749 0.00654  -0.06104 298 MET A CE  
2395 N  N   . LEU A 304 ? 0.33663 0.28902 0.35200 -0.01598 -0.00672 -0.04503 299 LEU A N   
2396 C  CA  . LEU A 304 ? 0.29778 0.25597 0.31471 -0.01604 -0.01172 -0.04244 299 LEU A CA  
2397 C  C   . LEU A 304 ? 0.29716 0.25845 0.33430 -0.01916 -0.01354 -0.04526 299 LEU A C   
2398 O  O   . LEU A 304 ? 0.33072 0.29304 0.37549 -0.02133 -0.01887 -0.05344 299 LEU A O   
2399 C  CB  . LEU A 304 ? 0.32035 0.28034 0.32289 -0.01369 -0.01949 -0.04589 299 LEU A CB  
2400 C  CG  . LEU A 304 ? 0.34222 0.29963 0.32514 -0.01122 -0.01622 -0.04297 299 LEU A CG  
2401 C  CD1 . LEU A 304 ? 0.33823 0.29521 0.30552 -0.00840 -0.02281 -0.04814 299 LEU A CD1 
2402 C  CD2 . LEU A 304 ? 0.36635 0.32446 0.34376 -0.01094 -0.01282 -0.03400 299 LEU A CD2 
2403 N  N   . TYR A 305 ? 0.29645 0.25984 0.34269 -0.01951 -0.00903 -0.03912 300 TYR A N   
2404 C  CA  . TYR A 305 ? 0.31392 0.28129 0.38114 -0.02265 -0.00795 -0.04051 300 TYR A CA  
2405 C  C   . TYR A 305 ? 0.32259 0.29911 0.39504 -0.02082 -0.01353 -0.03966 300 TYR A C   
2406 O  O   . TYR A 305 ? 0.33502 0.31164 0.40123 -0.01772 -0.01108 -0.03310 300 TYR A O   
2407 C  CB  . TYR A 305 ? 0.34249 0.30516 0.41597 -0.02329 0.00271  -0.03408 300 TYR A CB  
2408 C  CG  . TYR A 305 ? 0.31789 0.27100 0.39052 -0.02458 0.00792  -0.03555 300 TYR A CG  
2409 C  CD1 . TYR A 305 ? 0.33128 0.28095 0.41849 -0.02938 0.00836  -0.04159 300 TYR A CD1 
2410 C  CD2 . TYR A 305 ? 0.33561 0.28311 0.39370 -0.02085 0.01212  -0.03145 300 TYR A CD2 
2411 C  CE1 . TYR A 305 ? 0.38563 0.32364 0.47111 -0.02991 0.01330  -0.04306 300 TYR A CE1 
2412 C  CE2 . TYR A 305 ? 0.36161 0.29989 0.41854 -0.02036 0.01668  -0.03277 300 TYR A CE2 
2413 C  CZ  . TYR A 305 ? 0.35289 0.28503 0.42257 -0.02463 0.01747  -0.03833 300 TYR A CZ  
2414 O  OH  . TYR A 305 ? 0.38063 0.30077 0.44854 -0.02363 0.02230  -0.03967 300 TYR A OH  
2415 N  N   . SER A 306 ? 0.30664 0.29087 0.39120 -0.02237 -0.02134 -0.04691 301 SER A N   
2416 C  CA  . SER A 306 ? 0.34529 0.34004 0.43706 -0.01940 -0.02792 -0.04721 301 SER A CA  
2417 C  C   . SER A 306 ? 0.39060 0.39438 0.50955 -0.02292 -0.02413 -0.04826 301 SER A C   
2418 O  O   . SER A 306 ? 0.39236 0.39318 0.52433 -0.02859 -0.01709 -0.04942 301 SER A O   
2419 C  CB  . SER A 306 ? 0.37924 0.37923 0.46563 -0.01724 -0.04075 -0.05496 301 SER A CB  
2420 O  OG  . SER A 306 ? 0.54896 0.54070 0.60897 -0.01344 -0.04281 -0.05273 301 SER A OG  
2421 N  N   . VAL A 307 ? 0.37415 0.38868 0.50177 -0.01912 -0.02812 -0.04745 302 VAL A N   
2422 C  CA  . VAL A 307 ? 0.35746 0.38468 0.51367 -0.02212 -0.02545 -0.04964 302 VAL A CA  
2423 C  C   . VAL A 307 ? 0.38677 0.42663 0.55950 -0.02490 -0.03690 -0.06070 302 VAL A C   
2424 O  O   . VAL A 307 ? 0.40109 0.44040 0.55980 -0.02195 -0.04804 -0.06573 302 VAL A O   
2425 C  CB  . VAL A 307 ? 0.34908 0.38322 0.50875 -0.01573 -0.02336 -0.04391 302 VAL A CB  
2426 C  CG1 . VAL A 307 ? 0.32727 0.34893 0.47067 -0.01332 -0.01285 -0.03456 302 VAL A CG1 
2427 C  CG2 . VAL A 307 ? 0.33493 0.37406 0.48428 -0.00802 -0.03584 -0.04563 302 VAL A CG2 
2428 N  N   . ASN A 308 ? 0.37280 0.42470 0.57577 -0.03070 -0.03409 -0.06485 303 ASN A N   
2429 C  CA  . ASN A 308 ? 0.36473 0.43187 0.58768 -0.03388 -0.04594 -0.07667 303 ASN A CA  
2430 C  C   . ASN A 308 ? 0.45970 0.54316 0.68592 -0.02501 -0.05681 -0.07781 303 ASN A C   
2431 O  O   . ASN A 308 ? 0.43808 0.51905 0.65178 -0.01704 -0.05393 -0.06931 303 ASN A O   
2432 C  CB  . ASN A 308 ? 0.37687 0.45161 0.63373 -0.04459 -0.03857 -0.08115 303 ASN A CB  
2433 C  CG  . ASN A 308 ? 0.41457 0.50006 0.69181 -0.04408 -0.02773 -0.07438 303 ASN A CG  
2434 O  OD1 . ASN A 308 ? 0.36727 0.46403 0.64470 -0.03580 -0.03156 -0.07174 303 ASN A OD1 
2435 N  ND2 . ASN A 308 ? 0.33569 0.41670 0.62940 -0.05240 -0.01345 -0.07136 303 ASN A ND2 
2436 N  N   . ASP A 309 ? 0.38624 0.48637 0.62961 -0.02590 -0.06997 -0.08895 304 ASP A N   
2437 C  CA  . ASP A 309 ? 0.50975 0.62624 0.75561 -0.01597 -0.08268 -0.09112 304 ASP A CA  
2438 C  C   . ASP A 309 ? 0.46555 0.60532 0.74851 -0.01690 -0.08044 -0.09311 304 ASP A C   
2439 O  O   . ASP A 309 ? 0.58009 0.73962 0.87588 -0.01067 -0.09335 -0.09925 304 ASP A O   
2440 C  CB  . ASP A 309 ? 0.59158 0.71387 0.83033 -0.01383 -0.10069 -0.10246 304 ASP A CB  
2441 C  CG  . ASP A 309 ? 0.73150 0.86498 0.99906 -0.02533 -0.10487 -0.11604 304 ASP A CG  
2442 O  OD1 . ASP A 309 ? 0.73542 0.86917 1.02702 -0.03583 -0.09225 -0.11547 304 ASP A OD1 
2443 O  OD2 . ASP A 309 ? 0.83876 0.97829 1.10157 -0.02344 -0.11952 -0.12627 304 ASP A OD2 
2444 N  N   . GLU A 310 ? 0.42818 0.56664 0.72828 -0.02374 -0.06400 -0.08777 305 GLU A N   
2445 C  CA  . GLU A 310 ? 0.43770 0.59922 0.77524 -0.02568 -0.05950 -0.08966 305 GLU A CA  
2446 C  C   . GLU A 310 ? 0.41822 0.58663 0.75188 -0.01302 -0.05789 -0.08213 305 GLU A C   
2447 O  O   . GLU A 310 ? 0.34113 0.53395 0.70194 -0.00926 -0.06244 -0.08645 305 GLU A O   
2448 C  CB  . GLU A 310 ? 0.41467 0.57102 0.77070 -0.03747 -0.04101 -0.08606 305 GLU A CB  
2449 C  CG  . GLU A 310 ? 0.59470 0.74499 0.95955 -0.05011 -0.04122 -0.09393 305 GLU A CG  
2450 C  CD  . GLU A 310 ? 0.79524 0.93392 1.16895 -0.05942 -0.02141 -0.08724 305 GLU A CD  
2451 O  OE1 . GLU A 310 ? 0.75247 0.89230 1.13089 -0.05690 -0.00806 -0.07785 305 GLU A OE1 
2452 O  OE2 . GLU A 310 ? 0.85437 0.98174 1.22830 -0.06819 -0.01907 -0.09105 305 GLU A OE2 
2453 N  N   . LYS A 311 ? 0.38407 0.53191 0.68589 -0.00634 -0.05153 -0.07161 306 LYS A N   
2454 C  CA  . LYS A 311 ? 0.38890 0.53850 0.68418 0.00546  -0.04872 -0.06447 306 LYS A CA  
2455 C  C   . LYS A 311 ? 0.46889 0.60189 0.72719 0.01559  -0.05785 -0.06029 306 LYS A C   
2456 O  O   . LYS A 311 ? 0.39225 0.50749 0.62573 0.01239  -0.05976 -0.05922 306 LYS A O   
2457 C  CB  . LYS A 311 ? 0.43795 0.57724 0.73115 0.00362  -0.02967 -0.05520 306 LYS A CB  
2458 C  CG  . LYS A 311 ? 0.46488 0.61671 0.79122 -0.00640 -0.01699 -0.05670 306 LYS A CG  
2459 C  CD  . LYS A 311 ? 0.54622 0.72465 0.90454 -0.00160 -0.01587 -0.05924 306 LYS A CD  
2460 C  CE  . LYS A 311 ? 0.63937 0.82631 1.02593 -0.01073 0.00203  -0.05714 306 LYS A CE  
2461 N  NZ  . LYS A 311 ? 0.60319 0.76920 0.96734 -0.00925 0.01879  -0.04601 306 LYS A NZ  
2462 N  N   . ASP A 312 ? 0.36557 0.50400 0.62070 0.02806  -0.06266 -0.05768 307 ASP A N   
2463 C  CA  . ASP A 312 ? 0.30166 0.42075 0.52123 0.03763  -0.06797 -0.05157 307 ASP A CA  
2464 C  C   . ASP A 312 ? 0.31865 0.41388 0.51519 0.03438  -0.05463 -0.04288 307 ASP A C   
2465 O  O   . ASP A 312 ? 0.38136 0.47676 0.58882 0.02978  -0.04133 -0.04011 307 ASP A O   
2466 C  CB  . ASP A 312 ? 0.34901 0.47631 0.57096 0.05216  -0.07367 -0.04976 307 ASP A CB  
2467 C  CG  . ASP A 312 ? 0.41433 0.56313 0.65102 0.05858  -0.09071 -0.05791 307 ASP A CG  
2468 O  OD1 . ASP A 312 ? 0.43049 0.58723 0.67432 0.05123  -0.09871 -0.06572 307 ASP A OD1 
2469 O  OD2 . ASP A 312 ? 0.41941 0.57708 0.66007 0.07177  -0.09665 -0.05699 307 ASP A OD2 
2470 N  N   . ILE A 313 ? 0.33702 0.41220 0.50145 0.03683  -0.05814 -0.03865 308 ILE A N   
2471 C  CA  . ILE A 313 ? 0.25258 0.30650 0.39506 0.03428  -0.04751 -0.03127 308 ILE A CA  
2472 C  C   . ILE A 313 ? 0.29430 0.34043 0.42699 0.04435  -0.04491 -0.02565 308 ILE A C   
2473 O  O   . ILE A 313 ? 0.31562 0.35899 0.43785 0.05383  -0.05389 -0.02463 308 ILE A O   
2474 C  CB  . ILE A 313 ? 0.35595 0.39342 0.47136 0.03095  -0.05133 -0.02983 308 ILE A CB  
2475 C  CG1 . ILE A 313 ? 0.31503 0.35870 0.44005 0.02143  -0.05280 -0.03617 308 ILE A CG1 
2476 C  CG2 . ILE A 313 ? 0.32865 0.34656 0.42328 0.02873  -0.04159 -0.02283 308 ILE A CG2 
2477 C  CD1 . ILE A 313 ? 0.44260 0.47275 0.54251 0.01910  -0.05658 -0.03585 308 ILE A CD1 
2478 N  N   . GLU A 314 ? 0.33152 0.37327 0.46673 0.04310  -0.03271 -0.02220 309 GLU A N   
2479 C  CA  . GLU A 314 ? 0.31274 0.34736 0.44090 0.05253  -0.02904 -0.01833 309 GLU A CA  
2480 C  C   . GLU A 314 ? 0.27596 0.30136 0.39921 0.04849  -0.01551 -0.01499 309 GLU A C   
2481 O  O   . GLU A 314 ? 0.26833 0.29790 0.40020 0.03986  -0.00873 -0.01558 309 GLU A O   
2482 C  CB  . GLU A 314 ? 0.35367 0.40861 0.50650 0.06127  -0.03152 -0.02147 309 GLU A CB  
2483 C  CG  . GLU A 314 ? 0.34017 0.41452 0.52300 0.05561  -0.02220 -0.02436 309 GLU A CG  
2484 C  CD  . GLU A 314 ? 0.38676 0.48395 0.59663 0.06419  -0.02401 -0.02776 309 GLU A CD  
2485 O  OE1 . GLU A 314 ? 0.44238 0.53507 0.64486 0.07614  -0.02454 -0.02553 309 GLU A OE1 
2486 O  OE2 . GLU A 314 ? 0.39299 0.51276 0.63237 0.05900  -0.02505 -0.03310 309 GLU A OE2 
2487 N  N   . PRO A 315 ? 0.33542 0.34726 0.44381 0.05512  -0.01172 -0.01171 310 PRO A N   
2488 C  CA  . PRO A 315 ? 0.27685 0.28101 0.37949 0.05282  0.00017  -0.00951 310 PRO A CA  
2489 C  C   . PRO A 315 ? 0.31928 0.34097 0.44624 0.05210  0.00968  -0.01070 310 PRO A C   
2490 O  O   . PRO A 315 ? 0.32564 0.36440 0.47397 0.05732  0.00854  -0.01313 310 PRO A O   
2491 C  CB  . PRO A 315 ? 0.28884 0.27764 0.37466 0.06207  0.00035  -0.00780 310 PRO A CB  
2492 C  CG  . PRO A 315 ? 0.36090 0.34053 0.43402 0.06516  -0.01093 -0.00694 310 PRO A CG  
2493 C  CD  . PRO A 315 ? 0.31272 0.31214 0.40511 0.06480  -0.01852 -0.00986 310 PRO A CD  
2494 N  N   . ALA A 316 ? 0.33293 0.35062 0.45667 0.04588  0.01947  -0.00867 311 ALA A N   
2495 C  CA  . ALA A 316 ? 0.36066 0.39180 0.50450 0.04454  0.03099  -0.00821 311 ALA A CA  
2496 C  C   . ALA A 316 ? 0.30030 0.33594 0.44872 0.05506  0.03730  -0.00801 311 ALA A C   
2497 O  O   . ALA A 316 ? 0.27889 0.29966 0.40661 0.06159  0.03797  -0.00701 311 ALA A O   
2498 C  CB  . ALA A 316 ? 0.34528 0.36678 0.47809 0.03818  0.04028  -0.00474 311 ALA A CB  
2499 N  N   . ALA A 317 ? 0.33799 0.39458 0.51471 0.05644  0.04235  -0.00954 312 ALA A N   
2500 C  CA  . ALA A 317 ? 0.41579 0.48017 0.60042 0.06744  0.04883  -0.00988 312 ALA A CA  
2501 C  C   . ALA A 317 ? 0.27822 0.32944 0.44414 0.07094  0.06156  -0.00648 312 ALA A C   
2502 O  O   . ALA A 317 ? 0.30295 0.34872 0.45940 0.08171  0.06396  -0.00717 312 ALA A O   
2503 C  CB  . ALA A 317 ? 0.37906 0.47120 0.60096 0.06628  0.05388  -0.01208 312 ALA A CB  
2504 N  N   . GLY A 318 ? 0.32689 0.37212 0.48601 0.06293  0.06953  -0.00310 313 GLY A N   
2505 C  CA  . GLY A 318 ? 0.30525 0.33827 0.44426 0.06690  0.08070  0.00000  313 GLY A CA  
2506 C  C   . GLY A 318 ? 0.43492 0.44618 0.54244 0.07156  0.07410  -0.00124 313 GLY A C   
2507 O  O   . GLY A 318 ? 0.36746 0.36913 0.45756 0.07755  0.08145  -0.00069 313 GLY A O   
2508 N  N   . LEU A 319 ? 0.30309 0.30613 0.40268 0.06873  0.06069  -0.00318 314 LEU A N   
2509 C  CA  . LEU A 319 ? 0.29818 0.28045 0.37072 0.07149  0.05437  -0.00461 314 LEU A CA  
2510 C  C   . LEU A 319 ? 0.34235 0.31965 0.41211 0.08193  0.04978  -0.00741 314 LEU A C   
2511 O  O   . LEU A 319 ? 0.37782 0.33595 0.42581 0.08456  0.04565  -0.00901 314 LEU A O   
2512 C  CB  . LEU A 319 ? 0.27200 0.24616 0.33582 0.06247  0.04404  -0.00431 314 LEU A CB  
2513 C  CG  . LEU A 319 ? 0.31803 0.29468 0.38255 0.05302  0.04752  -0.00184 314 LEU A CG  
2514 C  CD1 . LEU A 319 ? 0.29144 0.26198 0.34902 0.04540  0.03752  -0.00215 314 LEU A CD1 
2515 C  CD2 . LEU A 319 ? 0.44088 0.40820 0.48770 0.05460  0.05530  -0.00052 314 LEU A CD2 
2516 N  N   . LEU A 320 ? 0.28161 0.27550 0.37354 0.08801  0.05033  -0.00829 315 LEU A N   
2517 C  CA  . LEU A 320 ? 0.27872 0.26930 0.37020 0.09942  0.04510  -0.01058 315 LEU A CA  
2518 C  C   . LEU A 320 ? 0.38002 0.37861 0.47925 0.11056  0.05613  -0.01198 315 LEU A C   
2519 O  O   . LEU A 320 ? 0.39077 0.40929 0.51099 0.10953  0.06575  -0.01097 315 LEU A O   
2520 C  CB  . LEU A 320 ? 0.29053 0.29587 0.40175 0.09995  0.03506  -0.01113 315 LEU A CB  
2521 C  CG  . LEU A 320 ? 0.26598 0.26611 0.37099 0.08987  0.02452  -0.01002 315 LEU A CG  
2522 C  CD1 . LEU A 320 ? 0.29811 0.31411 0.42155 0.09254  0.01427  -0.01148 315 LEU A CD1 
2523 C  CD2 . LEU A 320 ? 0.32749 0.30043 0.40259 0.08921  0.01904  -0.00898 315 LEU A CD2 
2524 N  N   . ASP A 321 ? 0.33788 0.32030 0.42041 0.12116  0.05539  -0.01438 316 ASP A N   
2525 C  CA  . ASP A 321 ? 0.34982 0.33845 0.43798 0.13416  0.06514  -0.01653 316 ASP A CA  
2526 C  C   . ASP A 321 ? 0.36430 0.33342 0.43671 0.14598  0.05857  -0.01959 316 ASP A C   
2527 O  O   . ASP A 321 ? 0.35143 0.30457 0.41178 0.14329  0.04708  -0.01907 316 ASP A O   
2528 C  CB  . ASP A 321 ? 0.50662 0.49210 0.58314 0.13340  0.07874  -0.01620 316 ASP A CB  
2529 C  CG  . ASP A 321 ? 0.67161 0.62877 0.71425 0.13601  0.07729  -0.01936 316 ASP A CG  
2530 O  OD1 . ASP A 321 ? 0.63996 0.57861 0.66768 0.13241  0.06610  -0.02057 316 ASP A OD1 
2531 O  OD2 . ASP A 321 ? 0.56265 0.51612 0.59336 0.14147  0.08774  -0.02091 316 ASP A OD2 
2532 N  N   . GLU A 322 ? 0.30875 0.27744 0.37998 0.15935  0.06675  -0.02257 317 GLU A N   
2533 C  CA  . GLU A 322 ? 0.32861 0.28171 0.38960 0.16933  0.05970  -0.02564 317 GLU A CA  
2534 C  C   . GLU A 322 ? 0.39985 0.31885 0.42920 0.16556  0.05283  -0.02706 317 GLU A C   
2535 O  O   . GLU A 322 ? 0.44569 0.34893 0.46691 0.17011  0.04469  -0.02765 317 GLU A O   
2536 C  CB  . GLU A 322 ? 0.47998 0.44005 0.54470 0.17832  0.06819  -0.02941 317 GLU A CB  
2537 C  CG  . GLU A 322 ? 0.46098 0.41423 0.50848 0.17571  0.07878  -0.03140 317 GLU A CG  
2538 C  CD  . GLU A 322 ? 0.42529 0.38986 0.47952 0.18497  0.08828  -0.03454 317 GLU A CD  
2539 O  OE1 . GLU A 322 ? 0.41005 0.36301 0.45726 0.19391  0.08505  -0.03832 317 GLU A OE1 
2540 O  OE2 . GLU A 322 ? 0.52075 0.50563 0.58770 0.18302  0.09947  -0.03279 317 GLU A OE2 
2541 N  N   . ASN A 323 ? 0.39292 0.30057 0.40512 0.15702  0.05611  -0.02759 318 ASN A N   
2542 C  CA  . ASN A 323 ? 0.55815 0.43591 0.54313 0.15158  0.04978  -0.03001 318 ASN A CA  
2543 C  C   . ASN A 323 ? 0.48459 0.35932 0.46695 0.13705  0.04214  -0.02631 318 ASN A C   
2544 O  O   . ASN A 323 ? 0.40387 0.25692 0.36650 0.13007  0.03753  -0.02810 318 ASN A O   
2545 C  CB  . ASN A 323 ? 0.56700 0.43544 0.53328 0.15010  0.05638  -0.03484 318 ASN A CB  
2546 C  CG  . ASN A 323 ? 0.60923 0.48301 0.57698 0.16048  0.06338  -0.03849 318 ASN A CG  
2547 O  OD1 . ASN A 323 ? 0.57974 0.46206 0.54417 0.16160  0.07264  -0.03982 318 ASN A OD1 
2548 N  ND2 . ASN A 323 ? 0.49049 0.35834 0.46170 0.16847  0.05928  -0.03980 318 ASN A ND2 
2549 N  N   . ARG A 324 ? 0.34947 0.24677 0.35242 0.13110  0.04066  -0.02177 319 ARG A N   
2550 C  CA  . ARG A 324 ? 0.33603 0.23422 0.33781 0.11661  0.03478  -0.01853 319 ARG A CA  
2551 C  C   . ARG A 324 ? 0.36756 0.27803 0.38574 0.11607  0.02693  -0.01502 319 ARG A C   
2552 O  O   . ARG A 324 ? 0.36049 0.29487 0.40032 0.11348  0.02856  -0.01346 319 ARG A O   
2553 C  CB  . ARG A 324 ? 0.45420 0.36680 0.46131 0.10827  0.04201  -0.01738 319 ARG A CB  
2554 C  CG  . ARG A 324 ? 0.39940 0.30057 0.38748 0.10940  0.04875  -0.02084 319 ARG A CG  
2555 C  CD  . ARG A 324 ? 0.53790 0.44760 0.52524 0.09977  0.05285  -0.01850 319 ARG A CD  
2556 N  NE  . ARG A 324 ? 0.62787 0.55938 0.63447 0.10135  0.06252  -0.01515 319 ARG A NE  
2557 C  CZ  . ARG A 324 ? 0.62752 0.56898 0.63966 0.09333  0.06662  -0.01142 319 ARG A CZ  
2558 N  NH1 . ARG A 324 ? 0.78296 0.71670 0.78347 0.08417  0.06138  -0.01073 319 ARG A NH1 
2559 N  NH2 . ARG A 324 ? 0.66432 0.62379 0.69502 0.09462  0.07667  -0.00823 319 ARG A NH2 
2560 N  N   . PRO A 325 ? 0.36537 0.25914 0.37298 0.11837  0.01821  -0.01382 320 PRO A N   
2561 C  CA  . PRO A 325 ? 0.35312 0.25747 0.37285 0.12019  0.00968  -0.01066 320 PRO A CA  
2562 C  C   . PRO A 325 ? 0.34414 0.25586 0.36630 0.10660  0.00522  -0.00805 320 PRO A C   
2563 O  O   . PRO A 325 ? 0.31375 0.21637 0.32396 0.09578  0.00690  -0.00778 320 PRO A O   
2564 C  CB  . PRO A 325 ? 0.40088 0.27913 0.40223 0.12753  0.00321  -0.00931 320 PRO A CB  
2565 C  CG  . PRO A 325 ? 0.42814 0.28104 0.40705 0.12097  0.00656  -0.01126 320 PRO A CG  
2566 C  CD  . PRO A 325 ? 0.43780 0.30101 0.42134 0.12060  0.01614  -0.01551 320 PRO A CD  
2567 N  N   . ALA A 326 ? 0.32202 0.25140 0.36040 0.10807  -0.00107 -0.00681 321 ALA A N   
2568 C  CA  . ALA A 326 ? 0.35783 0.29235 0.39671 0.09725  -0.00680 -0.00494 321 ALA A CA  
2569 C  C   . ALA A 326 ? 0.29036 0.20004 0.30476 0.09436  -0.01264 -0.00166 321 ALA A C   
2570 O  O   . ALA A 326 ? 0.34262 0.23655 0.34579 0.10345  -0.01663 0.00015  321 ALA A O   
2571 C  CB  . ALA A 326 ? 0.34126 0.29913 0.40158 0.10088  -0.01373 -0.00572 321 ALA A CB  
2572 N  N   A ARG A 327 ? 0.36549 0.27126 0.37187 0.08186  -0.01235 -0.00056 322 ARG A N   
2573 N  N   B ARG A 327 ? 0.36571 0.27137 0.37199 0.08190  -0.01238 -0.00054 322 ARG A N   
2574 C  CA  A ARG A 327 ? 0.42183 0.30662 0.40719 0.07699  -0.01625 0.00289  322 ARG A CA  
2575 C  CA  B ARG A 327 ? 0.42181 0.30631 0.40703 0.07735  -0.01639 0.00295  322 ARG A CA  
2576 C  C   A ARG A 327 ? 0.41725 0.30828 0.40243 0.07557  -0.02416 0.00561  322 ARG A C   
2577 C  C   B ARG A 327 ? 0.41737 0.30830 0.40250 0.07580  -0.02426 0.00564  322 ARG A C   
2578 O  O   A ARG A 327 ? 0.40415 0.27775 0.37122 0.07367  -0.02720 0.00963  322 ARG A O   
2579 O  O   B ARG A 327 ? 0.40393 0.27742 0.37096 0.07407  -0.02739 0.00969  322 ARG A O   
2580 C  CB  A ARG A 327 ? 0.41071 0.28780 0.38687 0.06478  -0.01099 0.00209  322 ARG A CB  
2581 C  CB  B ARG A 327 ? 0.41265 0.28843 0.38795 0.06528  -0.01116 0.00220  322 ARG A CB  
2582 C  CG  A ARG A 327 ? 0.48939 0.35425 0.45846 0.06649  -0.00496 -0.00099 322 ARG A CG  
2583 C  CG  B ARG A 327 ? 0.48898 0.35342 0.45806 0.06731  -0.00501 -0.00101 322 ARG A CG  
2584 C  CD  A ARG A 327 ? 0.55356 0.41488 0.51556 0.05520  -0.00119 -0.00274 322 ARG A CD  
2585 C  CD  B ARG A 327 ? 0.55315 0.41538 0.51622 0.05626  -0.00091 -0.00296 322 ARG A CD  
2586 N  NE  A ARG A 327 ? 0.59335 0.44253 0.54343 0.04639  -0.00421 -0.00012 322 ARG A NE  
2587 N  NE  B ARG A 327 ? 0.62367 0.48821 0.58814 0.05942  0.00530  -0.00709 322 ARG A NE  
2588 C  CZ  A ARG A 327 ? 0.69423 0.53739 0.63694 0.03684  -0.00215 -0.00177 322 ARG A CZ  
2589 C  CZ  B ARG A 327 ? 0.53241 0.40109 0.49483 0.05296  0.00914  -0.00923 322 ARG A CZ  
2590 N  NH1 A ARG A 327 ? 0.68385 0.53068 0.62739 0.03549  0.00175  -0.00616 322 ARG A NH1 
2591 N  NH1 B ARG A 327 ? 0.55884 0.43041 0.51947 0.04278  0.00755  -0.00801 322 ARG A NH1 
2592 N  NH2 A ARG A 327 ? 0.69170 0.52577 0.62596 0.02892  -0.00397 0.00103  322 ARG A NH2 
2593 N  NH2 B ARG A 327 ? 0.72611 0.59634 0.68742 0.05790  0.01479  -0.01262 322 ARG A NH2 
2594 N  N   . TYR A 328 ? 0.34480 0.25967 0.34923 0.07637  -0.02725 0.00326  323 TYR A N   
2595 C  CA  . TYR A 328 ? 0.37103 0.29403 0.37583 0.07543  -0.03567 0.00404  323 TYR A CA  
2596 C  C   . TYR A 328 ? 0.48204 0.42703 0.50801 0.08456  -0.04169 0.00082  323 TYR A C   
2597 O  O   . TYR A 328 ? 0.38277 0.34411 0.42977 0.08561  -0.03690 -0.00275 323 TYR A O   
2598 C  CB  . TYR A 328 ? 0.37683 0.30854 0.38513 0.06276  -0.03373 0.00237  323 TYR A CB  
2599 C  CG  . TYR A 328 ? 0.36769 0.28425 0.36148 0.05337  -0.02697 0.00419  323 TYR A CG  
2600 C  CD1 . TYR A 328 ? 0.37120 0.28895 0.37042 0.04974  -0.01889 0.00227  323 TYR A CD1 
2601 C  CD2 . TYR A 328 ? 0.43403 0.33620 0.40888 0.04846  -0.02859 0.00774  323 TYR A CD2 
2602 C  CE1 . TYR A 328 ? 0.48633 0.39259 0.47355 0.04184  -0.01415 0.00298  323 TYR A CE1 
2603 C  CE2 . TYR A 328 ? 0.46713 0.35848 0.43210 0.03945  -0.02262 0.00863  323 TYR A CE2 
2604 C  CZ  . TYR A 328 ? 0.42760 0.32175 0.39938 0.03634  -0.01623 0.00581  323 TYR A CZ  
2605 O  OH  . TYR A 328 ? 0.45635 0.34211 0.41962 0.02817  -0.01170 0.00571  323 TYR A OH  
2606 N  N   . ARG A 329 ? 0.36205 0.30840 0.38278 0.09129  -0.05204 0.00205  324 ARG A N   
2607 C  CA  . ARG A 329 ? 0.37347 0.34346 0.41643 0.10022  -0.05923 -0.00208 324 ARG A CA  
2608 C  C   . ARG A 329 ? 0.41571 0.40884 0.47781 0.09137  -0.06227 -0.00775 324 ARG A C   
2609 O  O   . ARG A 329 ? 0.40584 0.39414 0.45916 0.08068  -0.06094 -0.00772 324 ARG A O   
2610 C  CB  . ARG A 329 ? 0.55044 0.51376 0.58048 0.11383  -0.07040 0.00103  324 ARG A CB  
2611 C  CG  . ARG A 329 ? 0.51510 0.47625 0.53028 0.11141  -0.07931 0.00220  324 ARG A CG  
2612 C  CD  . ARG A 329 ? 0.58293 0.54337 0.58914 0.12730  -0.09171 0.00448  324 ARG A CD  
2613 N  NE  . ARG A 329 ? 0.57945 0.53369 0.56497 0.12604  -0.09943 0.00660  324 ARG A NE  
2614 C  CZ  . ARG A 329 ? 0.73763 0.71314 0.73339 0.12471  -0.10897 0.00032  324 ARG A CZ  
2615 N  NH1 . ARG A 329 ? 0.62983 0.63489 0.65846 0.12407  -0.11263 -0.00841 324 ARG A NH1 
2616 N  NH2 . ARG A 329 ? 0.68300 0.64979 0.65566 0.12364  -0.11451 0.00244  324 ARG A NH2 
2617 N  N   . LYS A 330 ? 0.33339 0.35206 0.42325 0.09597  -0.06604 -0.01313 325 LYS A N   
2618 C  CA  . LYS A 330 ? 0.36999 0.41161 0.48313 0.08708  -0.06820 -0.01977 325 LYS A CA  
2619 C  C   . LYS A 330 ? 0.30616 0.35311 0.41279 0.08891  -0.08247 -0.02269 325 LYS A C   
2620 O  O   . LYS A 330 ? 0.36290 0.41042 0.46243 0.10144  -0.09299 -0.02175 325 LYS A O   
2621 C  CB  . LYS A 330 ? 0.36263 0.43064 0.51066 0.09045  -0.06582 -0.02473 325 LYS A CB  
2622 C  CG  . LYS A 330 ? 0.38425 0.47778 0.56045 0.08225  -0.06991 -0.03260 325 LYS A CG  
2623 C  CD  . LYS A 330 ? 0.43306 0.55188 0.64579 0.08280  -0.06341 -0.03660 325 LYS A CD  
2624 C  CE  . LYS A 330 ? 0.40200 0.53775 0.62868 0.09804  -0.07242 -0.03884 325 LYS A CE  
2625 N  NZ  . LYS A 330 ? 0.54810 0.71377 0.81553 0.09698  -0.06637 -0.04400 325 LYS A NZ  
2626 N  N   . VAL A 331 ? 0.36352 0.41331 0.47074 0.07734  -0.08293 -0.02630 326 VAL A N   
2627 C  CA  . VAL A 331 ? 0.34454 0.39959 0.44461 0.07820  -0.09604 -0.03053 326 VAL A CA  
2628 C  C   . VAL A 331 ? 0.35675 0.43100 0.48156 0.06701  -0.09693 -0.03963 326 VAL A C   
2629 O  O   . VAL A 331 ? 0.34758 0.42100 0.48283 0.05611  -0.08549 -0.03990 326 VAL A O   
2630 C  CB  . VAL A 331 ? 0.49467 0.52484 0.55854 0.07635  -0.09608 -0.02473 326 VAL A CB  
2631 C  CG1 . VAL A 331 ? 0.48837 0.49958 0.52754 0.08830  -0.09819 -0.01639 326 VAL A CG1 
2632 C  CG2 . VAL A 331 ? 0.43441 0.45188 0.49267 0.06375  -0.08265 -0.02201 326 VAL A CG2 
2633 N  N   . SER A 332 ? 0.37305 0.46345 0.50604 0.07003  -0.11099 -0.04730 327 SER A N   
2634 C  CA  . SER A 332 ? 0.41063 0.51601 0.56434 0.05872  -0.11319 -0.05706 327 SER A CA  
2635 C  C   . SER A 332 ? 0.40756 0.49413 0.53875 0.04925  -0.10836 -0.05579 327 SER A C   
2636 O  O   . SER A 332 ? 0.38022 0.44626 0.47927 0.05273  -0.10745 -0.04882 327 SER A O   
2637 C  CB  . SER A 332 ? 0.49363 0.61995 0.65870 0.06456  -0.13123 -0.06690 327 SER A CB  
2638 O  OG  . SER A 332 ? 0.47280 0.58569 0.60400 0.07168  -0.14160 -0.06527 327 SER A OG  
2639 N  N   . VAL A 333 ? 0.39632 0.48999 0.54574 0.03715  -0.10460 -0.06260 328 VAL A N   
2640 C  CA  . VAL A 333 ? 0.38941 0.46704 0.52037 0.02881  -0.10000 -0.06250 328 VAL A CA  
2641 C  C   . VAL A 333 ? 0.45010 0.52301 0.55656 0.03380  -0.11284 -0.06609 328 VAL A C   
2642 O  O   . VAL A 333 ? 0.44815 0.50296 0.52680 0.03276  -0.10923 -0.06168 328 VAL A O   
2643 C  CB  . VAL A 333 ? 0.48064 0.56596 0.63722 0.01594  -0.09389 -0.06948 328 VAL A CB  
2644 C  CG1 . VAL A 333 ? 0.52288 0.59121 0.66023 0.00892  -0.08914 -0.06951 328 VAL A CG1 
2645 C  CG2 . VAL A 333 ? 0.37353 0.46215 0.55087 0.01203  -0.07990 -0.06452 328 VAL A CG2 
2646 N  N   . GLU A 334 ? 0.41593 0.50603 0.53222 0.03982  -0.12796 -0.07430 329 GLU A N   
2647 C  CA  . GLU A 334 ? 0.51317 0.59954 0.60399 0.04641  -0.14127 -0.07806 329 GLU A CA  
2648 C  C   . GLU A 334 ? 0.52505 0.59258 0.58018 0.05737  -0.14078 -0.06622 329 GLU A C   
2649 O  O   . GLU A 334 ? 0.49872 0.55049 0.52319 0.05839  -0.14082 -0.06345 329 GLU A O   
2650 C  CB  . GLU A 334 ? 0.55062 0.66158 0.66098 0.05194  -0.15878 -0.08958 329 GLU A CB  
2651 C  CG  . GLU A 334 ? 0.76406 0.87246 0.84558 0.06218  -0.17449 -0.09309 329 GLU A CG  
2652 C  CD  . GLU A 334 ? 0.87826 1.01123 0.97813 0.06924  -0.19111 -0.10308 329 GLU A CD  
2653 O  OE1 . GLU A 334 ? 0.80015 0.95290 0.93816 0.06284  -0.18926 -0.10907 329 GLU A OE1 
2654 O  OE2 . GLU A 334 ? 0.97251 1.10129 1.04608 0.07971  -0.20040 -0.10229 329 GLU A OE2 
2655 N  N   . GLU A 335 ? 0.46612 0.53433 0.52481 0.06575  -0.13963 -0.05911 330 GLU A N   
2656 C  CA  . GLU A 335 ? 0.51610 0.56351 0.54208 0.07546  -0.13793 -0.04736 330 GLU A CA  
2657 C  C   . GLU A 335 ? 0.49040 0.51558 0.49974 0.06715  -0.12200 -0.03870 330 GLU A C   
2658 O  O   . GLU A 335 ? 0.45981 0.46583 0.43780 0.06996  -0.11990 -0.03145 330 GLU A O   
2659 C  CB  . GLU A 335 ? 0.54108 0.59375 0.57701 0.08657  -0.14019 -0.04285 330 GLU A CB  
2660 C  CG  . GLU A 335 ? 0.54659 0.57564 0.55030 0.09698  -0.13831 -0.03066 330 GLU A CG  
2661 C  CD  . GLU A 335 ? 0.68636 0.71994 0.70059 0.10915  -0.14082 -0.02713 330 GLU A CD  
2662 O  OE1 . GLU A 335 ? 0.66513 0.72438 0.70911 0.11278  -0.14849 -0.03504 330 GLU A OE1 
2663 O  OE2 . GLU A 335 ? 0.65352 0.66506 0.64728 0.11496  -0.13479 -0.01683 330 GLU A OE2 
2664 N  N   . PHE A 336 ? 0.41247 0.44056 0.44269 0.05707  -0.11054 -0.03929 331 PHE A N   
2665 C  CA  . PHE A 336 ? 0.42603 0.43646 0.44350 0.04901  -0.09663 -0.03268 331 PHE A CA  
2666 C  C   . PHE A 336 ? 0.46732 0.47028 0.46672 0.04354  -0.09640 -0.03492 331 PHE A C   
2667 O  O   . PHE A 336 ? 0.41536 0.40121 0.39032 0.04277  -0.09024 -0.02785 331 PHE A O   
2668 C  CB  . PHE A 336 ? 0.38493 0.40256 0.42868 0.04042  -0.08619 -0.03425 331 PHE A CB  
2669 C  CG  . PHE A 336 ? 0.39889 0.40041 0.43183 0.03465  -0.07281 -0.02705 331 PHE A CG  
2670 C  CD1 . PHE A 336 ? 0.40845 0.40101 0.43726 0.03861  -0.06703 -0.02012 331 PHE A CD1 
2671 C  CD2 . PHE A 336 ? 0.41287 0.40900 0.44091 0.02573  -0.06650 -0.02811 331 PHE A CD2 
2672 C  CE1 . PHE A 336 ? 0.38516 0.36452 0.40512 0.03316  -0.05614 -0.01496 331 PHE A CE1 
2673 C  CE2 . PHE A 336 ? 0.42061 0.40472 0.44048 0.02109  -0.05547 -0.02226 331 PHE A CE2 
2674 C  CZ  . PHE A 336 ? 0.37401 0.35025 0.39002 0.02445  -0.05072 -0.01600 331 PHE A CZ  
2675 N  N   . ARG A 337 ? 0.38550 0.40140 0.39756 0.03962  -0.10287 -0.04532 332 ARG A N   
2676 C  CA  . ARG A 337 ? 0.43202 0.44156 0.42743 0.03553  -0.10324 -0.04914 332 ARG A CA  
2677 C  C   . ARG A 337 ? 0.45738 0.45586 0.41898 0.04440  -0.10916 -0.04476 332 ARG A C   
2678 O  O   . ARG A 337 ? 0.43865 0.42293 0.37763 0.04222  -0.10193 -0.03981 332 ARG A O   
2679 C  CB  . ARG A 337 ? 0.48602 0.51100 0.50101 0.03125  -0.11156 -0.06259 332 ARG A CB  
2680 C  CG  . ARG A 337 ? 0.63518 0.66461 0.67637 0.01987  -0.10244 -0.06656 332 ARG A CG  
2681 C  CD  . ARG A 337 ? 0.74273 0.77969 0.79400 0.01452  -0.10940 -0.07972 332 ARG A CD  
2682 N  NE  . ARG A 337 ? 0.74801 0.80411 0.81902 0.01737  -0.12331 -0.08935 332 ARG A NE  
2683 C  CZ  . ARG A 337 ? 0.74706 0.81808 0.85299 0.01029  -0.12343 -0.09657 332 ARG A CZ  
2684 N  NH1 . ARG A 337 ? 0.73131 0.79827 0.85407 0.00042  -0.11007 -0.09466 332 ARG A NH1 
2685 N  NH2 . ARG A 337 ? 0.69973 0.79059 0.82437 0.01337  -0.13713 -0.10578 332 ARG A NH2 
2686 N  N   . ALA A 338 ? 0.44475 0.45029 0.40260 0.05499  -0.12218 -0.04644 333 ALA A N   
2687 C  CA  . ALA A 338 ? 0.55049 0.54448 0.47377 0.06506  -0.12812 -0.04142 333 ALA A CA  
2688 C  C   . ALA A 338 ? 0.57461 0.54717 0.47608 0.06635  -0.11663 -0.02717 333 ALA A C   
2689 O  O   . ALA A 338 ? 0.55014 0.50796 0.42166 0.06847  -0.11348 -0.02143 333 ALA A O   
2690 C  CB  . ALA A 338 ? 0.52188 0.52780 0.44676 0.07783  -0.14448 -0.04482 333 ALA A CB  
2691 N  N   . GLY A 339 ? 0.50131 0.47163 0.41756 0.06472  -0.10970 -0.02170 334 GLY A N   
2692 C  CA  . GLY A 339 ? 0.51314 0.46261 0.41099 0.06479  -0.09920 -0.00956 334 GLY A CA  
2693 C  C   . GLY A 339 ? 0.48594 0.42615 0.37731 0.05346  -0.08616 -0.00710 334 GLY A C   
2694 O  O   . GLY A 339 ? 0.50299 0.42670 0.36999 0.05333  -0.07982 0.00093  334 GLY A O   
2695 N  N   . ILE A 340 ? 0.40484 0.35567 0.31845 0.04406  -0.08157 -0.01365 335 ILE A N   
2696 C  CA  . ILE A 340 ? 0.39296 0.33743 0.30240 0.03450  -0.07010 -0.01208 335 ILE A CA  
2697 C  C   . ILE A 340 ? 0.43980 0.37978 0.32629 0.03529  -0.07098 -0.01313 335 ILE A C   
2698 O  O   . ILE A 340 ? 0.48327 0.41170 0.35252 0.03230  -0.06202 -0.00671 335 ILE A O   
2699 C  CB  . ILE A 340 ? 0.40772 0.36404 0.34390 0.02633  -0.06630 -0.01904 335 ILE A CB  
2700 C  CG1 . ILE A 340 ? 0.46087 0.41972 0.41619 0.02549  -0.06247 -0.01654 335 ILE A CG1 
2701 C  CG2 . ILE A 340 ? 0.49430 0.44568 0.42512 0.01850  -0.05632 -0.01839 335 ILE A CG2 
2702 C  CD1 . ILE A 340 ? 0.40039 0.34537 0.34585 0.02319  -0.05296 -0.00802 335 ILE A CD1 
2703 N  N   . PHE A 341 ? 0.46565 0.41539 0.35204 0.03930  -0.08165 -0.02180 336 PHE A N   
2704 C  CA  . PHE A 341 ? 0.50543 0.45139 0.36903 0.04084  -0.08267 -0.02434 336 PHE A CA  
2705 C  C   . PHE A 341 ? 0.58885 0.52080 0.42008 0.04927  -0.08322 -0.01491 336 PHE A C   
2706 O  O   . PHE A 341 ? 0.58881 0.51084 0.39844 0.04787  -0.07515 -0.01029 336 PHE A O   
2707 C  CB  . PHE A 341 ? 0.55663 0.51613 0.42822 0.04313  -0.09522 -0.03758 336 PHE A CB  
2708 C  CG  . PHE A 341 ? 0.55919 0.52983 0.46133 0.03409  -0.09349 -0.04671 336 PHE A CG  
2709 C  CD1 . PHE A 341 ? 0.53257 0.49961 0.44627 0.02556  -0.08056 -0.04299 336 PHE A CD1 
2710 C  CD2 . PHE A 341 ? 0.59635 0.58069 0.51549 0.03421  -0.10491 -0.05901 336 PHE A CD2 
2711 C  CE1 . PHE A 341 ? 0.56578 0.54059 0.50503 0.01823  -0.07824 -0.05002 336 PHE A CE1 
2712 C  CE2 . PHE A 341 ? 0.57856 0.57066 0.52552 0.02527  -0.10202 -0.06656 336 PHE A CE2 
2713 C  CZ  . PHE A 341 ? 0.58876 0.57504 0.54459 0.01772  -0.08825 -0.06137 336 PHE A CZ  
2714 N  N   . GLY A 342 ? 0.50259 0.43326 0.33004 0.05852  -0.09194 -0.01144 337 GLY A N   
2715 C  CA  . GLY A 342 ? 0.53764 0.45314 0.33220 0.06813  -0.09325 -0.00197 337 GLY A CA  
2716 C  C   . GLY A 342 ? 0.56143 0.45786 0.34385 0.06395  -0.07895 0.01118  337 GLY A C   
2717 O  O   . GLY A 342 ? 0.61199 0.49413 0.36608 0.06605  -0.07298 0.01902  337 GLY A O   
2718 N  N   . LYS A 343 ? 0.55123 0.44698 0.35473 0.05777  -0.07296 0.01351  338 LYS A N   
2719 C  CA  . LYS A 343 ? 0.55909 0.43703 0.35359 0.05262  -0.06019 0.02437  338 LYS A CA  
2720 C  C   . LYS A 343 ? 0.54771 0.42484 0.34004 0.04173  -0.04784 0.02470  338 LYS A C   
2721 O  O   . LYS A 343 ? 0.57856 0.44089 0.35539 0.03821  -0.03752 0.03376  338 LYS A O   
2722 C  CB  . LYS A 343 ? 0.53840 0.41622 0.35509 0.04977  -0.05820 0.02518  338 LYS A CB  
2723 C  CG  . LYS A 343 ? 0.56341 0.43915 0.38058 0.06152  -0.06806 0.02699  338 LYS A CG  
2724 C  CD  . LYS A 343 ? 0.74383 0.59486 0.53555 0.06743  -0.06440 0.03930  338 LYS A CD  
2725 C  CE  . LYS A 343 ? 0.76258 0.61073 0.55717 0.07989  -0.07335 0.04120  338 LYS A CE  
2726 N  NZ  . LYS A 343 ? 1.11787 0.93850 0.88580 0.08671  -0.06974 0.05377  338 LYS A NZ  
2727 N  N   . PHE A 344 ? 0.53682 0.42954 0.34556 0.03631  -0.04827 0.01502  339 PHE A N   
2728 C  CA  . PHE A 344 ? 0.54857 0.44221 0.35472 0.02811  -0.03745 0.01467  339 PHE A CA  
2729 C  C   . PHE A 344 ? 0.49774 0.38295 0.27352 0.03235  -0.03451 0.01903  339 PHE A C   
2730 O  O   . PHE A 344 ? 0.51983 0.39835 0.28623 0.02675  -0.02230 0.02506  339 PHE A O   
2731 C  CB  . PHE A 344 ? 0.51044 0.42025 0.33685 0.02398  -0.03971 0.00329  339 PHE A CB  
2732 C  CG  . PHE A 344 ? 0.47096 0.38300 0.29598 0.01727  -0.02919 0.00223  339 PHE A CG  
2733 C  CD1 . PHE A 344 ? 0.50790 0.42162 0.34829 0.00893  -0.01989 0.00434  339 PHE A CD1 
2734 C  CD2 . PHE A 344 ? 0.50384 0.41710 0.31192 0.02027  -0.02899 -0.00142 339 PHE A CD2 
2735 C  CE1 . PHE A 344 ? 0.45811 0.37606 0.29894 0.00388  -0.01077 0.00315  339 PHE A CE1 
2736 C  CE2 . PHE A 344 ? 0.48401 0.40044 0.29184 0.01523  -0.01884 -0.00261 339 PHE A CE2 
2737 C  CZ  . PHE A 344 ? 0.45863 0.37811 0.28379 0.00713  -0.00983 -0.00017 339 PHE A CZ  
2738 N  N   . SER A 345 ? 0.49333 0.37968 0.25356 0.04247  -0.04554 0.01581  340 SER A N   
2739 C  CA  . SER A 345 ? 0.57414 0.45209 0.30181 0.04834  -0.04330 0.01977  340 SER A CA  
2740 C  C   . SER A 345 ? 0.67876 0.53663 0.38445 0.04957  -0.03418 0.03466  340 SER A C   
2741 O  O   . SER A 345 ? 0.65529 0.50466 0.33787 0.04935  -0.02448 0.04079  340 SER A O   
2742 C  CB  . SER A 345 ? 0.61953 0.50272 0.33456 0.06026  -0.05923 0.01289  340 SER A CB  
2743 O  OG  . SER A 345 ? 0.69122 0.59195 0.42958 0.05780  -0.06781 -0.00139 340 SER A OG  
2744 N  N   . ARG A 346 ? 0.58654 0.43574 0.29893 0.05085  -0.03626 0.04066  341 ARG A N   
2745 C  CA  . ARG A 346 ? 0.68291 0.50985 0.37607 0.05155  -0.02767 0.05475  341 ARG A CA  
2746 C  C   . ARG A 346 ? 0.65359 0.47551 0.36234 0.03784  -0.01365 0.05906  341 ARG A C   
2747 O  O   . ARG A 346 ? 0.70146 0.50391 0.39739 0.03578  -0.00497 0.07020  341 ARG A O   
2748 C  CB  . ARG A 346 ? 0.66794 0.48554 0.35742 0.06211  -0.03802 0.05886  341 ARG A CB  
2749 C  CG  . ARG A 346 ? 0.78207 0.60844 0.46168 0.07627  -0.05472 0.05301  341 ARG A CG  
2750 C  CD  . ARG A 346 ? 0.87093 0.68732 0.54590 0.08792  -0.06375 0.05863  341 ARG A CD  
2751 N  NE  . ARG A 346 ? 1.18149 1.01537 0.86366 0.09901  -0.08188 0.04889  341 ARG A NE  
2752 C  CZ  . ARG A 346 ? 0.99347 0.84563 0.70835 0.09741  -0.08980 0.03921  341 ARG A CZ  
2753 N  NH1 . ARG A 346 ? 1.05876 0.91316 0.79963 0.08650  -0.08164 0.03818  341 ARG A NH1 
2754 N  NH2 . ARG A 346 ? 0.97818 0.84737 0.69990 0.10706  -0.10619 0.03015  341 ARG A NH2 
2755 N  N   . GLY A 347 ? 0.59817 0.43646 0.33381 0.02864  -0.01150 0.05043  342 GLY A N   
2756 C  CA  . GLY A 347 ? 0.67289 0.50895 0.42511 0.01654  -0.00065 0.05293  342 GLY A CA  
2757 C  C   . GLY A 347 ? 0.70198 0.52831 0.46496 0.01627  -0.00321 0.05575  342 GLY A C   
2758 O  O   . GLY A 347 ? 0.76122 0.57592 0.52628 0.00835  0.00600  0.06146  342 GLY A O   
2759 N  N   . GLU A 348 ? 0.66609 0.49729 0.43672 0.02471  -0.01538 0.05125  343 GLU A N   
2760 C  CA  . GLU A 348 ? 0.57865 0.40149 0.35900 0.02671  -0.01836 0.05309  343 GLU A CA  
2761 C  C   . GLU A 348 ? 0.60541 0.44654 0.41499 0.02408  -0.02309 0.04313  343 GLU A C   
2762 O  O   . GLU A 348 ? 0.60425 0.46320 0.42511 0.02274  -0.02629 0.03513  343 GLU A O   
2763 C  CB  . GLU A 348 ? 0.63035 0.44229 0.39370 0.04085  -0.02781 0.05782  343 GLU A CB  
2764 C  CG  . GLU A 348 ? 0.70838 0.49753 0.43993 0.04452  -0.02207 0.06984  343 GLU A CG  
2765 C  CD  . GLU A 348 ? 0.77850 0.56085 0.48971 0.06098  -0.03337 0.07353  343 GLU A CD  
2766 O  OE1 . GLU A 348 ? 0.89380 0.69061 0.61884 0.06897  -0.04604 0.06609  343 GLU A OE1 
2767 O  OE2 . GLU A 348 ? 0.91649 0.67959 0.59801 0.06620  -0.02944 0.08402  343 GLU A OE2 
2768 N  N   . ARG A 349 ? 0.54454 0.37956 0.36532 0.02360  -0.02285 0.04382  344 ARG A N   
2769 C  CA  . ARG A 349 ? 0.59917 0.44900 0.44580 0.02118  -0.02519 0.03590  344 ARG A CA  
2770 C  C   . ARG A 349 ? 0.50782 0.36294 0.36120 0.03233  -0.03569 0.03326  344 ARG A C   
2771 O  O   . ARG A 349 ? 0.55543 0.39733 0.40338 0.03873  -0.03734 0.03773  344 ARG A O   
2772 C  CB  . ARG A 349 ? 0.60653 0.44783 0.46119 0.01337  -0.01758 0.03715  344 ARG A CB  
2773 C  CG  . ARG A 349 ? 0.69994 0.55581 0.57819 0.01089  -0.01841 0.02964  344 ARG A CG  
2774 C  CD  . ARG A 349 ? 0.60301 0.46641 0.49016 -0.00002 -0.01113 0.02673  344 ARG A CD  
2775 N  NE  . ARG A 349 ? 0.52296 0.40269 0.42957 -0.00072 -0.01256 0.01985  344 ARG A NE  
2776 C  CZ  . ARG A 349 ? 0.60682 0.48712 0.52411 -0.00272 -0.01037 0.01750  344 ARG A CZ  
2777 N  NH1 . ARG A 349 ? 0.77692 0.64276 0.68880 -0.00462 -0.00753 0.02003  344 ARG A NH1 
2778 N  NH2 . ARG A 349 ? 0.57930 0.47375 0.51197 -0.00268 -0.01078 0.01241  344 ARG A NH2 
2779 N  N   . TYR A 350 ? 0.49448 0.36909 0.36099 0.03461  -0.04258 0.02558  345 TYR A N   
2780 C  CA  . TYR A 350 ? 0.50641 0.39008 0.38233 0.04480  -0.05302 0.02215  345 TYR A CA  
2781 C  C   . TYR A 350 ? 0.44009 0.32502 0.33395 0.04568  -0.05132 0.02097  345 TYR A C   
2782 O  O   . TYR A 350 ? 0.52120 0.40341 0.41562 0.05561  -0.05686 0.02250  345 TYR A O   
2783 C  CB  . TYR A 350 ? 0.42684 0.33168 0.31638 0.04458  -0.05992 0.01298  345 TYR A CB  
2784 C  CG  . TYR A 350 ? 0.47933 0.39866 0.38664 0.05264  -0.06988 0.00766  345 TYR A CG  
2785 C  CD1 . TYR A 350 ? 0.49560 0.41189 0.39228 0.06507  -0.07937 0.01028  345 TYR A CD1 
2786 C  CD2 . TYR A 350 ? 0.45511 0.39170 0.39029 0.04819  -0.06944 0.00029  345 TYR A CD2 
2787 C  CE1 . TYR A 350 ? 0.51268 0.44547 0.42853 0.07282  -0.08886 0.00477  345 TYR A CE1 
2788 C  CE2 . TYR A 350 ? 0.44017 0.39232 0.39469 0.05470  -0.07751 -0.00478 345 TYR A CE2 
2789 C  CZ  . TYR A 350 ? 0.47329 0.42483 0.41931 0.06693  -0.08752 -0.00299 345 TYR A CZ  
2790 O  OH  . TYR A 350 ? 0.52651 0.49661 0.49461 0.07366  -0.09585 -0.00866 345 TYR A OH  
2791 N  N   . ILE A 351 ? 0.46610 0.35540 0.37382 0.03653  -0.04376 0.01815  346 ILE A N   
2792 C  CA  . ILE A 351 ? 0.48079 0.37304 0.40501 0.03776  -0.04169 0.01607  346 ILE A CA  
2793 C  C   . ILE A 351 ? 0.54276 0.41493 0.45497 0.04299  -0.04008 0.02194  346 ILE A C   
2794 O  O   . ILE A 351 ? 0.44453 0.31774 0.36635 0.04948  -0.04138 0.02064  346 ILE A O   
2795 C  CB  . ILE A 351 ? 0.46393 0.36233 0.40022 0.02764  -0.03374 0.01276  346 ILE A CB  
2796 C  CG1 . ILE A 351 ? 0.44308 0.34996 0.39814 0.03004  -0.03227 0.00925  346 ILE A CG1 
2797 C  CG2 . ILE A 351 ? 0.57667 0.45926 0.50028 0.02064  -0.02628 0.01693  346 ILE A CG2 
2798 C  CD1 . ILE A 351 ? 0.40951 0.32222 0.37435 0.02197  -0.02500 0.00651  346 ILE A CD1 
2799 N  N   . ASP A 352 ? 0.47646 0.32936 0.36764 0.04047  -0.03662 0.02848  347 ASP A N   
2800 C  CA  . ASP A 352 ? 0.52521 0.35513 0.40345 0.04504  -0.03475 0.03438  347 ASP A CA  
2801 C  C   . ASP A 352 ? 0.49580 0.32368 0.37034 0.05997  -0.04339 0.03639  347 ASP A C   
2802 O  O   . ASP A 352 ? 0.58220 0.39706 0.45512 0.06667  -0.04307 0.03834  347 ASP A O   
2803 C  CB  . ASP A 352 ? 0.66170 0.47140 0.51834 0.03890  -0.02882 0.04173  347 ASP A CB  
2804 C  CG  . ASP A 352 ? 0.71380 0.52219 0.57556 0.02488  -0.01974 0.03996  347 ASP A CG  
2805 O  OD1 . ASP A 352 ? 0.66218 0.48210 0.54108 0.02133  -0.01848 0.03364  347 ASP A OD1 
2806 O  OD2 . ASP A 352 ? 0.69875 0.49512 0.54737 0.01777  -0.01372 0.04503  347 ASP A OD2 
2807 N  N   . SER A 353 ? 0.47670 0.31749 0.34979 0.06604  -0.05169 0.03529  348 SER A N   
2808 C  CA  . SER A 353 ? 0.48815 0.33028 0.35864 0.08131  -0.06160 0.03655  348 SER A CA  
2809 C  C   . SER A 353 ? 0.52399 0.38527 0.42103 0.08669  -0.06522 0.02957  348 SER A C   
2810 O  O   . SER A 353 ? 0.53007 0.39229 0.42852 0.10012  -0.07222 0.03039  348 SER A O   
2811 C  CB  . SER A 353 ? 0.50411 0.35629 0.36519 0.08624  -0.07066 0.03602  348 SER A CB  
2812 O  OG  . SER A 353 ? 0.52033 0.39885 0.40253 0.08094  -0.07411 0.02660  348 SER A OG  
2813 N  N   . LEU A 354 ? 0.45598 0.33261 0.37375 0.07716  -0.06012 0.02318  349 LEU A N   
2814 C  CA  . LEU A 354 ? 0.42576 0.32083 0.36936 0.08074  -0.06088 0.01709  349 LEU A CA  
2815 C  C   . LEU A 354 ? 0.49161 0.37416 0.43687 0.08184  -0.05330 0.01822  349 LEU A C   
2816 O  O   . LEU A 354 ? 0.41322 0.30835 0.37692 0.08764  -0.05319 0.01433  349 LEU A O   
2817 C  CB  . LEU A 354 ? 0.34521 0.26176 0.30904 0.07041  -0.05840 0.01024  349 LEU A CB  
2818 C  CG  . LEU A 354 ? 0.40770 0.33887 0.37372 0.06908  -0.06634 0.00649  349 LEU A CG  
2819 C  CD1 . LEU A 354 ? 0.46657 0.41577 0.45372 0.05902  -0.06278 -0.00026 349 LEU A CD1 
2820 C  CD2 . LEU A 354 ? 0.41638 0.35891 0.38774 0.08202  -0.07837 0.00459  349 LEU A CD2 
2821 N  N   . ARG A 355 ? 0.43369 0.29240 0.36082 0.07631  -0.04679 0.02283  350 ARG A N   
2822 C  CA  . ARG A 355 ? 0.48316 0.32904 0.41084 0.07630  -0.04000 0.02225  350 ARG A CA  
2823 C  C   . ARG A 355 ? 0.49574 0.33249 0.42115 0.09139  -0.04361 0.02400  350 ARG A C   
2824 O  O   . ARG A 355 ? 0.50049 0.32543 0.41146 0.10020  -0.04937 0.02938  350 ARG A O   
2825 C  CB  . ARG A 355 ? 0.56410 0.38666 0.47390 0.06617  -0.03336 0.02587  350 ARG A CB  
2826 C  CG  . ARG A 355 ? 0.55401 0.38710 0.46865 0.05205  -0.02882 0.02326  350 ARG A CG  
2827 C  CD  . ARG A 355 ? 0.68376 0.49717 0.58395 0.04161  -0.02258 0.02620  350 ARG A CD  
2828 N  NE  . ARG A 355 ? 0.71689 0.54212 0.62078 0.03004  -0.01947 0.02454  350 ARG A NE  
2829 C  CZ  . ARG A 355 ? 0.81030 0.64726 0.72613 0.02326  -0.01573 0.01935  350 ARG A CZ  
2830 N  NH1 . ARG A 355 ? 0.73651 0.57509 0.66072 0.02617  -0.01408 0.01527  350 ARG A NH1 
2831 N  NH2 . ARG A 355 ? 0.77470 0.62178 0.69296 0.01443  -0.01341 0.01839  350 ARG A NH2 
2832 N  N   . ILE A 356 ? 0.44015 0.28207 0.37883 0.09547  -0.03989 0.01964  351 ILE A N   
2833 C  CA  . ILE A 356 ? 0.46081 0.29651 0.40006 0.11095  -0.04258 0.02025  351 ILE A CA  
2834 C  C   . ILE A 356 ? 0.44636 0.24835 0.36518 0.11212  -0.03789 0.02351  351 ILE A C   
2835 O  O   . ILE A 356 ? 0.57787 0.37011 0.49341 0.10224  -0.03070 0.02100  351 ILE A O   
2836 C  CB  . ILE A 356 ? 0.48994 0.34907 0.45426 0.11589  -0.04002 0.01375  351 ILE A CB  
2837 C  CG1 . ILE A 356 ? 0.43133 0.32235 0.41714 0.11572  -0.04592 0.01069  351 ILE A CG1 
2838 C  CG2 . ILE A 356 ? 0.53563 0.38575 0.49961 0.13205  -0.04050 0.01375  351 ILE A CG2 
2839 C  CD1 . ILE A 356 ? 0.51151 0.42768 0.52442 0.11675  -0.04139 0.00479  351 ILE A CD1 
2840 O  OXT . ILE A 356 ? 0.50750 0.29076 0.41250 0.12304  -0.04157 0.02849  351 ILE A OXT 
2841 MN MN  . MN  B .   ? 0.33232 0.28485 0.26681 -0.01501 0.00364  -0.01037 401 MN  A MN  
2842 C  C1  . AKG C .   ? 0.38905 0.34712 0.31738 -0.01066 0.00528  -0.02092 402 AKG A C1  
2843 O  O1  . AKG C .   ? 0.39618 0.35083 0.32651 -0.01060 -0.00026 -0.01946 402 AKG A O1  
2844 O  O2  . AKG C .   ? 0.35526 0.31407 0.28107 -0.00790 0.00484  -0.02734 402 AKG A O2  
2845 C  C2  . AKG C .   ? 0.39716 0.35965 0.32690 -0.01388 0.01313  -0.01594 402 AKG A C2  
2846 O  O5  . AKG C .   ? 0.42514 0.38549 0.35540 -0.01700 0.01372  -0.01069 402 AKG A O5  
2847 C  C3  . AKG C .   ? 0.37872 0.34850 0.31019 -0.01288 0.01957  -0.01842 402 AKG A C3  
2848 C  C4  . AKG C .   ? 0.32786 0.30533 0.26697 -0.01654 0.02556  -0.01438 402 AKG A C4  
2849 C  C5  . AKG C .   ? 0.40925 0.39674 0.35107 -0.01468 0.03208  -0.01667 402 AKG A C5  
2850 O  O3  . AKG C .   ? 0.36957 0.35776 0.30229 -0.01161 0.03495  -0.01943 402 AKG A O3  
2851 O  O4  . AKG C .   ? 0.30757 0.30360 0.26209 -0.01587 0.03416  -0.01576 402 AKG A O4  
# 
