data_9DEN
# 
_entry.id   9DEN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DEN         pdb_00009den 10.2210/pdb9den/pdb 
WWPDB D_1000287910 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DEN 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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              sethh@gene.com 
_pdbx_contact_author.name_first         Seth 
_pdbx_contact_author.name_last          Harris 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1728-9771 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ultsch, M.'    1 ?                   
'Tenorio, C.A.' 2 ?                   
'Dueber, E.C.'  3 ?                   
'Harris, S.F.'  4 0000-0003-1728-9771 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                705 
_citation.page_last                 717.e4 
_citation.title                     
'Discovery and characterization of potent macrocycle inhibitors of ubiquitin-specific protease-7.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.01.021 
_citation.pdbx_database_id_PubMed   39983720 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Miranda, R.'   1  ? 
primary 'Anson, F.'     2  ? 
primary 'Smith, S.T.'   3  ? 
primary 'Ultsch, M.'    4  ? 
primary 'Tenorio, C.A.' 5  ? 
primary 'Rouge, L.'     6  ? 
primary 'Farrell, B.'   7  ? 
primary 'Adaligil, E.'  8  ? 
primary 'Holden, J.K.'  9  ? 
primary 'Harris, S.F.'  10 ? 
primary 'Dueber, E.C.'  11 ? 
# 
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 'Ubiquitin carboxyl-terminal hydrolase 7' 42476.953 2 3.4.19.12 ? ? ? 
2 polymer     syn 'Macrocycle peptide  MC07'                1894.249  2 ?         ? ? ? 
3 non-polymer syn ETHANOL                                   46.068    1 ?         ? ? ? 
4 water       nat water                                     18.015    9 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Deubiquitinating enzyme 7,Herpesvirus-associated ubiquitin-specific protease,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MGSSHHHHHHSSGLVPRGSHMKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYE
LQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRRED
YYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFE
FPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLS
VRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQK
;
;MGSSHHHHHHSSGLVPRGSHMKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYE
LQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRRED
YYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFE
FPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLS
VRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQK
;
B,A ? 
2 'polypeptide(L)' no yes '(ACE)F(MEA)N(MEA)PN(DI8)YRRCGKK' XFFNFPNXYRRCGKK D,C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 ETHANOL EOH 
4 water   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  LYS n 
1 23  LYS n 
1 24  HIS n 
1 25  THR n 
1 26  GLY n 
1 27  TYR n 
1 28  VAL n 
1 29  GLY n 
1 30  LEU n 
1 31  LYS n 
1 32  ASN n 
1 33  GLN n 
1 34  GLY n 
1 35  ALA n 
1 36  THR n 
1 37  CYS n 
1 38  TYR n 
1 39  MET n 
1 40  ASN n 
1 41  SER n 
1 42  LEU n 
1 43  LEU n 
1 44  GLN n 
1 45  THR n 
1 46  LEU n 
1 47  PHE n 
1 48  PHE n 
1 49  THR n 
1 50  ASN n 
1 51  GLN n 
1 52  LEU n 
1 53  ARG n 
1 54  LYS n 
1 55  ALA n 
1 56  VAL n 
1 57  TYR n 
1 58  MET n 
1 59  MET n 
1 60  PRO n 
1 61  THR n 
1 62  GLU n 
1 63  GLY n 
1 64  ASP n 
1 65  ASP n 
1 66  SER n 
1 67  SER n 
1 68  LYS n 
1 69  SER n 
1 70  VAL n 
1 71  PRO n 
1 72  LEU n 
1 73  ALA n 
1 74  LEU n 
1 75  GLN n 
1 76  ARG n 
1 77  VAL n 
1 78  PHE n 
1 79  TYR n 
1 80  GLU n 
1 81  LEU n 
1 82  GLN n 
1 83  HIS n 
1 84  SER n 
1 85  ASP n 
1 86  LYS n 
1 87  PRO n 
1 88  VAL n 
1 89  GLY n 
1 90  THR n 
1 91  LYS n 
1 92  LYS n 
1 93  LEU n 
1 94  THR n 
1 95  LYS n 
1 96  SER n 
1 97  PHE n 
1 98  GLY n 
1 99  TRP n 
1 100 GLU n 
1 101 THR n 
1 102 LEU n 
1 103 ASP n 
1 104 SER n 
1 105 PHE n 
1 106 MET n 
1 107 GLN n 
1 108 HIS n 
1 109 ASP n 
1 110 VAL n 
1 111 GLN n 
1 112 GLU n 
1 113 LEU n 
1 114 CYS n 
1 115 ARG n 
1 116 VAL n 
1 117 LEU n 
1 118 LEU n 
1 119 ASP n 
1 120 ASN n 
1 121 VAL n 
1 122 GLU n 
1 123 ASN n 
1 124 LYS n 
1 125 MET n 
1 126 LYS n 
1 127 GLY n 
1 128 THR n 
1 129 CYS n 
1 130 VAL n 
1 131 GLU n 
1 132 GLY n 
1 133 THR n 
1 134 ILE n 
1 135 PRO n 
1 136 LYS n 
1 137 LEU n 
1 138 PHE n 
1 139 ARG n 
1 140 GLY n 
1 141 LYS n 
1 142 MET n 
1 143 VAL n 
1 144 SER n 
1 145 TYR n 
1 146 ILE n 
1 147 GLN n 
1 148 CYS n 
1 149 LYS n 
1 150 GLU n 
1 151 VAL n 
1 152 ASP n 
1 153 TYR n 
1 154 ARG n 
1 155 SER n 
1 156 ASP n 
1 157 ARG n 
1 158 ARG n 
1 159 GLU n 
1 160 ASP n 
1 161 TYR n 
1 162 TYR n 
1 163 ASP n 
1 164 ILE n 
1 165 GLN n 
1 166 LEU n 
1 167 SER n 
1 168 ILE n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 LYS n 
1 173 ASN n 
1 174 ILE n 
1 175 PHE n 
1 176 GLU n 
1 177 SER n 
1 178 PHE n 
1 179 VAL n 
1 180 ASP n 
1 181 TYR n 
1 182 VAL n 
1 183 ALA n 
1 184 VAL n 
1 185 GLU n 
1 186 GLN n 
1 187 LEU n 
1 188 ASP n 
1 189 GLY n 
1 190 ASP n 
1 191 ASN n 
1 192 LYS n 
1 193 TYR n 
1 194 ASP n 
1 195 ALA n 
1 196 GLY n 
1 197 GLU n 
1 198 HIS n 
1 199 GLY n 
1 200 LEU n 
1 201 GLN n 
1 202 GLU n 
1 203 ALA n 
1 204 GLU n 
1 205 LYS n 
1 206 GLY n 
1 207 VAL n 
1 208 LYS n 
1 209 PHE n 
1 210 LEU n 
1 211 THR n 
1 212 LEU n 
1 213 PRO n 
1 214 PRO n 
1 215 VAL n 
1 216 LEU n 
1 217 HIS n 
1 218 LEU n 
1 219 GLN n 
1 220 LEU n 
1 221 MET n 
1 222 ARG n 
1 223 PHE n 
1 224 MET n 
1 225 TYR n 
1 226 ASP n 
1 227 PRO n 
1 228 GLN n 
1 229 THR n 
1 230 ASP n 
1 231 GLN n 
1 232 ASN n 
1 233 ILE n 
1 234 LYS n 
1 235 ILE n 
1 236 ASN n 
1 237 ASP n 
1 238 ARG n 
1 239 PHE n 
1 240 GLU n 
1 241 PHE n 
1 242 PRO n 
1 243 GLU n 
1 244 GLN n 
1 245 LEU n 
1 246 PRO n 
1 247 LEU n 
1 248 ASP n 
1 249 GLU n 
1 250 PHE n 
1 251 LEU n 
1 252 GLN n 
1 253 LYS n 
1 254 THR n 
1 255 ASP n 
1 256 PRO n 
1 257 LYS n 
1 258 ASP n 
1 259 PRO n 
1 260 ALA n 
1 261 ASN n 
1 262 TYR n 
1 263 ILE n 
1 264 LEU n 
1 265 HIS n 
1 266 ALA n 
1 267 VAL n 
1 268 LEU n 
1 269 VAL n 
1 270 HIS n 
1 271 SER n 
1 272 GLY n 
1 273 ASP n 
1 274 ASN n 
1 275 HIS n 
1 276 GLY n 
1 277 GLY n 
1 278 HIS n 
1 279 TYR n 
1 280 VAL n 
1 281 VAL n 
1 282 TYR n 
1 283 LEU n 
1 284 ASN n 
1 285 PRO n 
1 286 LYS n 
1 287 GLY n 
1 288 ASP n 
1 289 GLY n 
1 290 LYS n 
1 291 TRP n 
1 292 CYS n 
1 293 LYS n 
1 294 PHE n 
1 295 ASP n 
1 296 ASP n 
1 297 ASP n 
1 298 VAL n 
1 299 VAL n 
1 300 SER n 
1 301 ARG n 
1 302 CYS n 
1 303 THR n 
1 304 LYS n 
1 305 GLU n 
1 306 GLU n 
1 307 ALA n 
1 308 ILE n 
1 309 GLU n 
1 310 HIS n 
1 311 ASN n 
1 312 TYR n 
1 313 GLY n 
1 314 GLY n 
1 315 HIS n 
1 316 ASP n 
1 317 ASP n 
1 318 ASP n 
1 319 LEU n 
1 320 SER n 
1 321 VAL n 
1 322 ARG n 
1 323 HIS n 
1 324 CYS n 
1 325 THR n 
1 326 ASN n 
1 327 ALA n 
1 328 TYR n 
1 329 MET n 
1 330 LEU n 
1 331 VAL n 
1 332 TYR n 
1 333 ILE n 
1 334 ARG n 
1 335 GLU n 
1 336 SER n 
1 337 LYS n 
1 338 LEU n 
1 339 SER n 
1 340 GLU n 
1 341 VAL n 
1 342 LEU n 
1 343 GLN n 
1 344 ALA n 
1 345 VAL n 
1 346 THR n 
1 347 ASP n 
1 348 HIS n 
1 349 ASP n 
1 350 ILE n 
1 351 PRO n 
1 352 GLN n 
1 353 GLN n 
1 354 LEU n 
1 355 VAL n 
1 356 GLU n 
1 357 ARG n 
1 358 LEU n 
1 359 GLN n 
1 360 GLU n 
1 361 GLU n 
1 362 LYS n 
1 363 ARG n 
1 364 ILE n 
1 365 GLU n 
1 366 ALA n 
1 367 GLN n 
1 368 LYS n 
2 1   ACE n 
2 2   PHE n 
2 3   MEA n 
2 4   ASN n 
2 5   MEA n 
2 6   PRO n 
2 7   ASN n 
2 8   DI8 n 
2 9   TYR n 
2 10  ARG n 
2 11  ARG n 
2 12  CYS n 
2 13  GLY n 
2 14  LYS n 
2 15  LYS 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                   368 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'USP7, HAUSP' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       15 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
ACE non-polymer         . 'ACETYL GROUP'                                          ? 'C2 H4 O'        44.053  
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 
DI8 'L-peptide linking' . '(3S)-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid' ? 'C10 H11 N O2'   177.200 
EOH non-polymer         . ETHANOL                                                 ? 'C2 H6 O'        46.068  
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 
MEA 'L-peptide linking' n N-METHYLPHENYLALANINE                                   ? 'C10 H13 N O2'   179.216 
MET 'L-peptide linking' y METHIONINE                                              ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                  ? 'C3 H7 N O3'     105.093 
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   MET 1   187 ?   ?   ?   B . n 
A 1 2   GLY 2   188 ?   ?   ?   B . n 
A 1 3   SER 3   189 ?   ?   ?   B . n 
A 1 4   SER 4   190 ?   ?   ?   B . n 
A 1 5   HIS 5   191 ?   ?   ?   B . n 
A 1 6   HIS 6   192 ?   ?   ?   B . n 
A 1 7   HIS 7   193 ?   ?   ?   B . n 
A 1 8   HIS 8   194 ?   ?   ?   B . n 
A 1 9   HIS 9   195 ?   ?   ?   B . n 
A 1 10  HIS 10  196 ?   ?   ?   B . n 
A 1 11  SER 11  197 ?   ?   ?   B . n 
A 1 12  SER 12  198 ?   ?   ?   B . n 
A 1 13  GLY 13  199 ?   ?   ?   B . n 
A 1 14  LEU 14  200 ?   ?   ?   B . n 
A 1 15  VAL 15  201 ?   ?   ?   B . n 
A 1 16  PRO 16  202 ?   ?   ?   B . n 
A 1 17  ARG 17  203 ?   ?   ?   B . n 
A 1 18  GLY 18  204 ?   ?   ?   B . n 
A 1 19  SER 19  205 ?   ?   ?   B . n 
A 1 20  HIS 20  206 ?   ?   ?   B . n 
A 1 21  MET 21  207 ?   ?   ?   B . n 
A 1 22  LYS 22  208 ?   ?   ?   B . n 
A 1 23  LYS 23  209 ?   ?   ?   B . n 
A 1 24  HIS 24  210 210 HIS HIS B . n 
A 1 25  THR 25  211 211 THR THR B . n 
A 1 26  GLY 26  212 212 GLY GLY B . n 
A 1 27  TYR 27  213 213 TYR TYR B . n 
A 1 28  VAL 28  214 214 VAL VAL B . n 
A 1 29  GLY 29  215 215 GLY GLY B . n 
A 1 30  LEU 30  216 216 LEU LEU B . n 
A 1 31  LYS 31  217 217 LYS LYS B . n 
A 1 32  ASN 32  218 218 ASN ASN B . n 
A 1 33  GLN 33  219 219 GLN GLN B . n 
A 1 34  GLY 34  220 220 GLY GLY B . n 
A 1 35  ALA 35  221 221 ALA ALA B . n 
A 1 36  THR 36  222 222 THR THR B . n 
A 1 37  CYS 37  223 223 CYS CYS B . n 
A 1 38  TYR 38  224 224 TYR TYR B . n 
A 1 39  MET 39  225 225 MET MET B . n 
A 1 40  ASN 40  226 226 ASN ASN B . n 
A 1 41  SER 41  227 227 SER SER B . n 
A 1 42  LEU 42  228 228 LEU LEU B . n 
A 1 43  LEU 43  229 229 LEU LEU B . n 
A 1 44  GLN 44  230 230 GLN GLN B . n 
A 1 45  THR 45  231 231 THR THR B . n 
A 1 46  LEU 46  232 232 LEU LEU B . n 
A 1 47  PHE 47  233 233 PHE PHE B . n 
A 1 48  PHE 48  234 234 PHE PHE B . n 
A 1 49  THR 49  235 235 THR THR B . n 
A 1 50  ASN 50  236 236 ASN ASN B . n 
A 1 51  GLN 51  237 237 GLN GLN B . n 
A 1 52  LEU 52  238 238 LEU LEU B . n 
A 1 53  ARG 53  239 239 ARG ARG B . n 
A 1 54  LYS 54  240 240 LYS LYS B . n 
A 1 55  ALA 55  241 241 ALA ALA B . n 
A 1 56  VAL 56  242 242 VAL VAL B . n 
A 1 57  TYR 57  243 243 TYR TYR B . n 
A 1 58  MET 58  244 244 MET MET B . n 
A 1 59  MET 59  245 245 MET MET B . n 
A 1 60  PRO 60  246 246 PRO PRO B . n 
A 1 61  THR 61  247 247 THR THR B . n 
A 1 62  GLU 62  248 248 GLU GLU B . n 
A 1 63  GLY 63  249 249 GLY GLY B . n 
A 1 64  ASP 64  250 250 ASP ASP B . n 
A 1 65  ASP 65  251 251 ASP ASP B . n 
A 1 66  SER 66  252 252 SER SER B . n 
A 1 67  SER 67  253 253 SER SER B . n 
A 1 68  LYS 68  254 254 LYS LYS B . n 
A 1 69  SER 69  255 255 SER SER B . n 
A 1 70  VAL 70  256 256 VAL VAL B . n 
A 1 71  PRO 71  257 257 PRO PRO B . n 
A 1 72  LEU 72  258 258 LEU LEU B . n 
A 1 73  ALA 73  259 259 ALA ALA B . n 
A 1 74  LEU 74  260 260 LEU LEU B . n 
A 1 75  GLN 75  261 261 GLN GLN B . n 
A 1 76  ARG 76  262 262 ARG ARG B . n 
A 1 77  VAL 77  263 263 VAL VAL B . n 
A 1 78  PHE 78  264 264 PHE PHE B . n 
A 1 79  TYR 79  265 265 TYR TYR B . n 
A 1 80  GLU 80  266 266 GLU GLU B . n 
A 1 81  LEU 81  267 267 LEU LEU B . n 
A 1 82  GLN 82  268 268 GLN GLN B . n 
A 1 83  HIS 83  269 269 HIS HIS B . n 
A 1 84  SER 84  270 270 SER SER B . n 
A 1 85  ASP 85  271 271 ASP ASP B . n 
A 1 86  LYS 86  272 272 LYS LYS B . n 
A 1 87  PRO 87  273 273 PRO PRO B . n 
A 1 88  VAL 88  274 274 VAL VAL B . n 
A 1 89  GLY 89  275 275 GLY GLY B . n 
A 1 90  THR 90  276 276 THR THR B . n 
A 1 91  LYS 91  277 277 LYS LYS B . n 
A 1 92  LYS 92  278 278 LYS LYS B . n 
A 1 93  LEU 93  279 279 LEU LEU B . n 
A 1 94  THR 94  280 280 THR THR B . n 
A 1 95  LYS 95  281 281 LYS LYS B . n 
A 1 96  SER 96  282 282 SER SER B . n 
A 1 97  PHE 97  283 283 PHE PHE B . n 
A 1 98  GLY 98  284 284 GLY GLY B . n 
A 1 99  TRP 99  285 285 TRP TRP B . n 
A 1 100 GLU 100 286 286 GLU GLU B . n 
A 1 101 THR 101 287 287 THR THR B . n 
A 1 102 LEU 102 288 288 LEU LEU B . n 
A 1 103 ASP 103 289 289 ASP ASP B . n 
A 1 104 SER 104 290 290 SER SER B . n 
A 1 105 PHE 105 291 291 PHE PHE B . n 
A 1 106 MET 106 292 292 MET MET B . n 
A 1 107 GLN 107 293 293 GLN GLN B . n 
A 1 108 HIS 108 294 294 HIS HIS B . n 
A 1 109 ASP 109 295 295 ASP ASP B . n 
A 1 110 VAL 110 296 296 VAL VAL B . n 
A 1 111 GLN 111 297 297 GLN GLN B . n 
A 1 112 GLU 112 298 298 GLU GLU B . n 
A 1 113 LEU 113 299 299 LEU LEU B . n 
A 1 114 CYS 114 300 300 CYS CYS B . n 
A 1 115 ARG 115 301 301 ARG ARG B . n 
A 1 116 VAL 116 302 302 VAL VAL B . n 
A 1 117 LEU 117 303 303 LEU LEU B . n 
A 1 118 LEU 118 304 304 LEU LEU B . n 
A 1 119 ASP 119 305 305 ASP ASP B . n 
A 1 120 ASN 120 306 306 ASN ASN B . n 
A 1 121 VAL 121 307 307 VAL VAL B . n 
A 1 122 GLU 122 308 308 GLU GLU B . n 
A 1 123 ASN 123 309 309 ASN ASN B . n 
A 1 124 LYS 124 310 310 LYS LYS B . n 
A 1 125 MET 125 311 311 MET MET B . n 
A 1 126 LYS 126 312 312 LYS LYS B . n 
A 1 127 GLY 127 313 313 GLY GLY B . n 
A 1 128 THR 128 314 314 THR THR B . n 
A 1 129 CYS 129 315 315 CYS CYS B . n 
A 1 130 VAL 130 316 316 VAL VAL B . n 
A 1 131 GLU 131 317 317 GLU GLU B . n 
A 1 132 GLY 132 318 318 GLY GLY B . n 
A 1 133 THR 133 319 319 THR THR B . n 
A 1 134 ILE 134 320 320 ILE ILE B . n 
A 1 135 PRO 135 321 321 PRO PRO B . n 
A 1 136 LYS 136 322 322 LYS LYS B . n 
A 1 137 LEU 137 323 323 LEU LEU B . n 
A 1 138 PHE 138 324 324 PHE PHE B . n 
A 1 139 ARG 139 325 325 ARG ARG B . n 
A 1 140 GLY 140 326 326 GLY GLY B . n 
A 1 141 LYS 141 327 327 LYS LYS B . n 
A 1 142 MET 142 328 328 MET MET B . n 
A 1 143 VAL 143 329 329 VAL VAL B . n 
A 1 144 SER 144 330 330 SER SER B . n 
A 1 145 TYR 145 331 331 TYR TYR B . n 
A 1 146 ILE 146 332 332 ILE ILE B . n 
A 1 147 GLN 147 333 333 GLN GLN B . n 
A 1 148 CYS 148 334 334 CYS CYS B . n 
A 1 149 LYS 149 335 335 LYS LYS B . n 
A 1 150 GLU 150 336 336 GLU GLU B . n 
A 1 151 VAL 151 337 337 VAL VAL B . n 
A 1 152 ASP 152 338 338 ASP ASP B . n 
A 1 153 TYR 153 339 339 TYR TYR B . n 
A 1 154 ARG 154 340 340 ARG ARG B . n 
A 1 155 SER 155 341 341 SER SER B . n 
A 1 156 ASP 156 342 342 ASP ASP B . n 
A 1 157 ARG 157 343 343 ARG ARG B . n 
A 1 158 ARG 158 344 344 ARG ARG B . n 
A 1 159 GLU 159 345 345 GLU GLU B . n 
A 1 160 ASP 160 346 346 ASP ASP B . n 
A 1 161 TYR 161 347 347 TYR TYR B . n 
A 1 162 TYR 162 348 348 TYR TYR B . n 
A 1 163 ASP 163 349 349 ASP ASP B . n 
A 1 164 ILE 164 350 350 ILE ILE B . n 
A 1 165 GLN 165 351 351 GLN GLN B . n 
A 1 166 LEU 166 352 352 LEU LEU B . n 
A 1 167 SER 167 353 353 SER SER B . n 
A 1 168 ILE 168 354 354 ILE ILE B . n 
A 1 169 LYS 169 355 355 LYS LYS B . n 
A 1 170 GLY 170 356 356 GLY GLY B . n 
A 1 171 LYS 171 357 357 LYS LYS B . n 
A 1 172 LYS 172 358 358 LYS LYS B . n 
A 1 173 ASN 173 359 359 ASN ASN B . n 
A 1 174 ILE 174 360 360 ILE ILE B . n 
A 1 175 PHE 175 361 361 PHE PHE B . n 
A 1 176 GLU 176 362 362 GLU GLU B . n 
A 1 177 SER 177 363 363 SER SER B . n 
A 1 178 PHE 178 364 364 PHE PHE B . n 
A 1 179 VAL 179 365 365 VAL VAL B . n 
A 1 180 ASP 180 366 366 ASP ASP B . n 
A 1 181 TYR 181 367 367 TYR TYR B . n 
A 1 182 VAL 182 368 368 VAL VAL B . n 
A 1 183 ALA 183 369 369 ALA ALA B . n 
A 1 184 VAL 184 370 370 VAL VAL B . n 
A 1 185 GLU 185 371 371 GLU GLU B . n 
A 1 186 GLN 186 372 372 GLN GLN B . n 
A 1 187 LEU 187 373 373 LEU LEU B . n 
A 1 188 ASP 188 374 374 ASP ASP B . n 
A 1 189 GLY 189 375 375 GLY GLY B . n 
A 1 190 ASP 190 376 376 ASP ASP B . n 
A 1 191 ASN 191 377 377 ASN ASN B . n 
A 1 192 LYS 192 378 378 LYS LYS B . n 
A 1 193 TYR 193 379 379 TYR TYR B . n 
A 1 194 ASP 194 380 380 ASP ASP B . n 
A 1 195 ALA 195 381 381 ALA ALA B . n 
A 1 196 GLY 196 382 382 GLY GLY B . n 
A 1 197 GLU 197 383 383 GLU GLU B . n 
A 1 198 HIS 198 384 384 HIS HIS B . n 
A 1 199 GLY 199 385 385 GLY GLY B . n 
A 1 200 LEU 200 386 386 LEU LEU B . n 
A 1 201 GLN 201 387 387 GLN GLN B . n 
A 1 202 GLU 202 388 388 GLU GLU B . n 
A 1 203 ALA 203 389 389 ALA ALA B . n 
A 1 204 GLU 204 390 390 GLU GLU B . n 
A 1 205 LYS 205 391 391 LYS LYS B . n 
A 1 206 GLY 206 392 392 GLY GLY B . n 
A 1 207 VAL 207 393 393 VAL VAL B . n 
A 1 208 LYS 208 394 394 LYS LYS B . n 
A 1 209 PHE 209 395 395 PHE PHE B . n 
A 1 210 LEU 210 396 396 LEU LEU B . n 
A 1 211 THR 211 397 397 THR THR B . n 
A 1 212 LEU 212 398 398 LEU LEU B . n 
A 1 213 PRO 213 399 399 PRO PRO B . n 
A 1 214 PRO 214 400 400 PRO PRO B . n 
A 1 215 VAL 215 401 401 VAL VAL B . n 
A 1 216 LEU 216 402 402 LEU LEU B . n 
A 1 217 HIS 217 403 403 HIS HIS B . n 
A 1 218 LEU 218 404 404 LEU LEU B . n 
A 1 219 GLN 219 405 405 GLN GLN B . n 
A 1 220 LEU 220 406 406 LEU LEU B . n 
A 1 221 MET 221 407 407 MET MET B . n 
A 1 222 ARG 222 408 408 ARG ARG B . n 
A 1 223 PHE 223 409 409 PHE PHE B . n 
A 1 224 MET 224 410 410 MET MET B . n 
A 1 225 TYR 225 411 411 TYR TYR B . n 
A 1 226 ASP 226 412 ?   ?   ?   B . n 
A 1 227 PRO 227 413 ?   ?   ?   B . n 
A 1 228 GLN 228 414 414 GLN GLN B . n 
A 1 229 THR 229 415 415 THR THR B . n 
A 1 230 ASP 230 416 416 ASP ASP B . n 
A 1 231 GLN 231 417 417 GLN GLN B . n 
A 1 232 ASN 232 418 418 ASN ASN B . n 
A 1 233 ILE 233 419 419 ILE ILE B . n 
A 1 234 LYS 234 420 420 LYS LYS B . n 
A 1 235 ILE 235 421 421 ILE ILE B . n 
A 1 236 ASN 236 422 422 ASN ASN B . n 
A 1 237 ASP 237 423 423 ASP ASP B . n 
A 1 238 ARG 238 424 424 ARG ARG B . n 
A 1 239 PHE 239 425 425 PHE PHE B . n 
A 1 240 GLU 240 426 426 GLU GLU B . n 
A 1 241 PHE 241 427 427 PHE PHE B . n 
A 1 242 PRO 242 428 428 PRO PRO B . n 
A 1 243 GLU 243 429 429 GLU GLU B . n 
A 1 244 GLN 244 430 430 GLN GLN B . n 
A 1 245 LEU 245 431 431 LEU LEU B . n 
A 1 246 PRO 246 432 432 PRO PRO B . n 
A 1 247 LEU 247 433 433 LEU LEU B . n 
A 1 248 ASP 248 434 434 ASP ASP B . n 
A 1 249 GLU 249 435 435 GLU GLU B . n 
A 1 250 PHE 250 436 436 PHE PHE B . n 
A 1 251 LEU 251 437 437 LEU LEU B . n 
A 1 252 GLN 252 438 438 GLN GLN B . n 
A 1 253 LYS 253 439 439 LYS LYS B . n 
A 1 254 THR 254 440 440 THR THR B . n 
A 1 255 ASP 255 441 441 ASP ASP B . n 
A 1 256 PRO 256 442 442 PRO PRO B . n 
A 1 257 LYS 257 443 443 LYS LYS B . n 
A 1 258 ASP 258 444 444 ASP ASP B . n 
A 1 259 PRO 259 445 445 PRO PRO B . n 
A 1 260 ALA 260 446 446 ALA ALA B . n 
A 1 261 ASN 261 447 447 ASN ASN B . n 
A 1 262 TYR 262 448 448 TYR TYR B . n 
A 1 263 ILE 263 449 449 ILE ILE B . n 
A 1 264 LEU 264 450 450 LEU LEU B . n 
A 1 265 HIS 265 451 451 HIS HIS B . n 
A 1 266 ALA 266 452 452 ALA ALA B . n 
A 1 267 VAL 267 453 453 VAL VAL B . n 
A 1 268 LEU 268 454 454 LEU LEU B . n 
A 1 269 VAL 269 455 455 VAL VAL B . n 
A 1 270 HIS 270 456 456 HIS HIS B . n 
A 1 271 SER 271 457 457 SER SER B . n 
A 1 272 GLY 272 458 458 GLY GLY B . n 
A 1 273 ASP 273 459 459 ASP ASP B . n 
A 1 274 ASN 274 460 460 ASN ASN B . n 
A 1 275 HIS 275 461 461 HIS HIS B . n 
A 1 276 GLY 276 462 462 GLY GLY B . n 
A 1 277 GLY 277 463 463 GLY GLY B . n 
A 1 278 HIS 278 464 464 HIS HIS B . n 
A 1 279 TYR 279 465 465 TYR TYR B . n 
A 1 280 VAL 280 466 466 VAL VAL B . n 
A 1 281 VAL 281 467 467 VAL VAL B . n 
A 1 282 TYR 282 468 468 TYR TYR B . n 
A 1 283 LEU 283 469 469 LEU LEU B . n 
A 1 284 ASN 284 470 470 ASN ASN B . n 
A 1 285 PRO 285 471 471 PRO PRO B . n 
A 1 286 LYS 286 472 472 LYS LYS B . n 
A 1 287 GLY 287 473 473 GLY GLY B . n 
A 1 288 ASP 288 474 474 ASP ASP B . n 
A 1 289 GLY 289 475 475 GLY GLY B . n 
A 1 290 LYS 290 476 476 LYS LYS B . n 
A 1 291 TRP 291 477 477 TRP TRP B . n 
A 1 292 CYS 292 478 478 CYS CYS B . n 
A 1 293 LYS 293 479 479 LYS LYS B . n 
A 1 294 PHE 294 480 480 PHE PHE B . n 
A 1 295 ASP 295 481 481 ASP ASP B . n 
A 1 296 ASP 296 482 482 ASP ASP B . n 
A 1 297 ASP 297 483 483 ASP ASP B . n 
A 1 298 VAL 298 484 484 VAL VAL B . n 
A 1 299 VAL 299 485 485 VAL VAL B . n 
A 1 300 SER 300 486 486 SER SER B . n 
A 1 301 ARG 301 487 487 ARG ARG B . n 
A 1 302 CYS 302 488 488 CYS CYS B . n 
A 1 303 THR 303 489 489 THR THR B . n 
A 1 304 LYS 304 490 490 LYS LYS B . n 
A 1 305 GLU 305 491 491 GLU GLU B . n 
A 1 306 GLU 306 492 492 GLU GLU B . n 
A 1 307 ALA 307 493 493 ALA ALA B . n 
A 1 308 ILE 308 494 494 ILE ILE B . n 
A 1 309 GLU 309 495 495 GLU GLU B . n 
A 1 310 HIS 310 496 496 HIS HIS B . n 
A 1 311 ASN 311 497 497 ASN ASN B . n 
A 1 312 TYR 312 498 498 TYR TYR B . n 
A 1 313 GLY 313 499 499 GLY GLY B . n 
A 1 314 GLY 314 500 ?   ?   ?   B . n 
A 1 315 HIS 315 501 ?   ?   ?   B . n 
A 1 316 ASP 316 502 ?   ?   ?   B . n 
A 1 317 ASP 317 503 ?   ?   ?   B . n 
A 1 318 ASP 318 504 ?   ?   ?   B . n 
A 1 319 LEU 319 505 ?   ?   ?   B . n 
A 1 320 SER 320 506 ?   ?   ?   B . n 
A 1 321 VAL 321 507 ?   ?   ?   B . n 
A 1 322 ARG 322 508 ?   ?   ?   B . n 
A 1 323 HIS 323 509 509 HIS HIS B . n 
A 1 324 CYS 324 510 510 CYS CYS B . n 
A 1 325 THR 325 511 511 THR THR B . n 
A 1 326 ASN 326 512 512 ASN ASN B . n 
A 1 327 ALA 327 513 513 ALA ALA B . n 
A 1 328 TYR 328 514 514 TYR TYR B . n 
A 1 329 MET 329 515 515 MET MET B . n 
A 1 330 LEU 330 516 516 LEU LEU B . n 
A 1 331 VAL 331 517 517 VAL VAL B . n 
A 1 332 TYR 332 518 518 TYR TYR B . n 
A 1 333 ILE 333 519 519 ILE ILE B . n 
A 1 334 ARG 334 520 520 ARG ARG B . n 
A 1 335 GLU 335 521 521 GLU GLU B . n 
A 1 336 SER 336 522 522 SER SER B . n 
A 1 337 LYS 337 523 523 LYS LYS B . n 
A 1 338 LEU 338 524 524 LEU LEU B . n 
A 1 339 SER 339 525 525 SER SER B . n 
A 1 340 GLU 340 526 526 GLU GLU B . n 
A 1 341 VAL 341 527 527 VAL VAL B . n 
A 1 342 LEU 342 528 528 LEU LEU B . n 
A 1 343 GLN 343 529 529 GLN GLN B . n 
A 1 344 ALA 344 530 530 ALA ALA B . n 
A 1 345 VAL 345 531 531 VAL VAL B . n 
A 1 346 THR 346 532 532 THR THR B . n 
A 1 347 ASP 347 533 533 ASP ASP B . n 
A 1 348 HIS 348 534 534 HIS HIS B . n 
A 1 349 ASP 349 535 535 ASP ASP B . n 
A 1 350 ILE 350 536 536 ILE ILE B . n 
A 1 351 PRO 351 537 537 PRO PRO B . n 
A 1 352 GLN 352 538 538 GLN GLN B . n 
A 1 353 GLN 353 539 539 GLN GLN B . n 
A 1 354 LEU 354 540 540 LEU LEU B . n 
A 1 355 VAL 355 541 541 VAL VAL B . n 
A 1 356 GLU 356 542 542 GLU GLU B . n 
A 1 357 ARG 357 543 543 ARG ARG B . n 
A 1 358 LEU 358 544 544 LEU LEU B . n 
A 1 359 GLN 359 545 545 GLN GLN B . n 
A 1 360 GLU 360 546 546 GLU GLU B . n 
A 1 361 GLU 361 547 547 GLU GLU B . n 
A 1 362 LYS 362 548 548 LYS LYS B . n 
A 1 363 ARG 363 549 549 ARG ARG B . n 
A 1 364 ILE 364 550 550 ILE ILE B . n 
A 1 365 GLU 365 551 551 GLU GLU B . n 
A 1 366 ALA 366 552 552 ALA ALA B . n 
A 1 367 GLN 367 553 553 GLN GLN B . n 
A 1 368 LYS 368 554 ?   ?   ?   B . n 
B 1 1   MET 1   187 ?   ?   ?   A . n 
B 1 2   GLY 2   188 ?   ?   ?   A . n 
B 1 3   SER 3   189 ?   ?   ?   A . n 
B 1 4   SER 4   190 ?   ?   ?   A . n 
B 1 5   HIS 5   191 ?   ?   ?   A . n 
B 1 6   HIS 6   192 ?   ?   ?   A . n 
B 1 7   HIS 7   193 ?   ?   ?   A . n 
B 1 8   HIS 8   194 ?   ?   ?   A . n 
B 1 9   HIS 9   195 ?   ?   ?   A . n 
B 1 10  HIS 10  196 ?   ?   ?   A . n 
B 1 11  SER 11  197 ?   ?   ?   A . n 
B 1 12  SER 12  198 ?   ?   ?   A . n 
B 1 13  GLY 13  199 ?   ?   ?   A . n 
B 1 14  LEU 14  200 ?   ?   ?   A . n 
B 1 15  VAL 15  201 ?   ?   ?   A . n 
B 1 16  PRO 16  202 ?   ?   ?   A . n 
B 1 17  ARG 17  203 ?   ?   ?   A . n 
B 1 18  GLY 18  204 ?   ?   ?   A . n 
B 1 19  SER 19  205 ?   ?   ?   A . n 
B 1 20  HIS 20  206 ?   ?   ?   A . n 
B 1 21  MET 21  207 ?   ?   ?   A . n 
B 1 22  LYS 22  208 ?   ?   ?   A . n 
B 1 23  LYS 23  209 209 LYS LYS A . n 
B 1 24  HIS 24  210 210 HIS HIS A . n 
B 1 25  THR 25  211 211 THR THR A . n 
B 1 26  GLY 26  212 212 GLY GLY A . n 
B 1 27  TYR 27  213 213 TYR TYR A . n 
B 1 28  VAL 28  214 214 VAL VAL A . n 
B 1 29  GLY 29  215 215 GLY GLY A . n 
B 1 30  LEU 30  216 216 LEU LEU A . n 
B 1 31  LYS 31  217 217 LYS LYS A . n 
B 1 32  ASN 32  218 218 ASN ASN A . n 
B 1 33  GLN 33  219 219 GLN GLN A . n 
B 1 34  GLY 34  220 220 GLY GLY A . n 
B 1 35  ALA 35  221 221 ALA ALA A . n 
B 1 36  THR 36  222 222 THR THR A . n 
B 1 37  CYS 37  223 223 CYS CYS A . n 
B 1 38  TYR 38  224 224 TYR TYR A . n 
B 1 39  MET 39  225 225 MET MET A . n 
B 1 40  ASN 40  226 226 ASN ASN A . n 
B 1 41  SER 41  227 227 SER SER A . n 
B 1 42  LEU 42  228 228 LEU LEU A . n 
B 1 43  LEU 43  229 229 LEU LEU A . n 
B 1 44  GLN 44  230 230 GLN GLN A . n 
B 1 45  THR 45  231 231 THR THR A . n 
B 1 46  LEU 46  232 232 LEU LEU A . n 
B 1 47  PHE 47  233 233 PHE PHE A . n 
B 1 48  PHE 48  234 234 PHE PHE A . n 
B 1 49  THR 49  235 235 THR THR A . n 
B 1 50  ASN 50  236 236 ASN ASN A . n 
B 1 51  GLN 51  237 237 GLN GLN A . n 
B 1 52  LEU 52  238 238 LEU LEU A . n 
B 1 53  ARG 53  239 239 ARG ARG A . n 
B 1 54  LYS 54  240 240 LYS LYS A . n 
B 1 55  ALA 55  241 241 ALA ALA A . n 
B 1 56  VAL 56  242 242 VAL VAL A . n 
B 1 57  TYR 57  243 243 TYR TYR A . n 
B 1 58  MET 58  244 244 MET MET A . n 
B 1 59  MET 59  245 245 MET MET A . n 
B 1 60  PRO 60  246 246 PRO PRO A . n 
B 1 61  THR 61  247 247 THR THR A . n 
B 1 62  GLU 62  248 248 GLU GLU A . n 
B 1 63  GLY 63  249 249 GLY GLY A . n 
B 1 64  ASP 64  250 250 ASP ASP A . n 
B 1 65  ASP 65  251 251 ASP ASP A . n 
B 1 66  SER 66  252 252 SER SER A . n 
B 1 67  SER 67  253 253 SER SER A . n 
B 1 68  LYS 68  254 254 LYS LYS A . n 
B 1 69  SER 69  255 255 SER SER A . n 
B 1 70  VAL 70  256 256 VAL VAL A . n 
B 1 71  PRO 71  257 257 PRO PRO A . n 
B 1 72  LEU 72  258 258 LEU LEU A . n 
B 1 73  ALA 73  259 259 ALA ALA A . n 
B 1 74  LEU 74  260 260 LEU LEU A . n 
B 1 75  GLN 75  261 261 GLN GLN A . n 
B 1 76  ARG 76  262 262 ARG ARG A . n 
B 1 77  VAL 77  263 263 VAL VAL A . n 
B 1 78  PHE 78  264 264 PHE PHE A . n 
B 1 79  TYR 79  265 265 TYR TYR A . n 
B 1 80  GLU 80  266 266 GLU GLU A . n 
B 1 81  LEU 81  267 267 LEU LEU A . n 
B 1 82  GLN 82  268 268 GLN GLN A . n 
B 1 83  HIS 83  269 269 HIS HIS A . n 
B 1 84  SER 84  270 270 SER SER A . n 
B 1 85  ASP 85  271 271 ASP ASP A . n 
B 1 86  LYS 86  272 272 LYS LYS A . n 
B 1 87  PRO 87  273 273 PRO PRO A . n 
B 1 88  VAL 88  274 274 VAL VAL A . n 
B 1 89  GLY 89  275 275 GLY GLY A . n 
B 1 90  THR 90  276 276 THR THR A . n 
B 1 91  LYS 91  277 277 LYS LYS A . n 
B 1 92  LYS 92  278 278 LYS LYS A . n 
B 1 93  LEU 93  279 279 LEU LEU A . n 
B 1 94  THR 94  280 280 THR THR A . n 
B 1 95  LYS 95  281 281 LYS LYS A . n 
B 1 96  SER 96  282 282 SER SER A . n 
B 1 97  PHE 97  283 283 PHE PHE A . n 
B 1 98  GLY 98  284 284 GLY GLY A . n 
B 1 99  TRP 99  285 285 TRP TRP A . n 
B 1 100 GLU 100 286 286 GLU GLU A . n 
B 1 101 THR 101 287 287 THR THR A . n 
B 1 102 LEU 102 288 288 LEU LEU A . n 
B 1 103 ASP 103 289 289 ASP ASP A . n 
B 1 104 SER 104 290 290 SER SER A . n 
B 1 105 PHE 105 291 291 PHE PHE A . n 
B 1 106 MET 106 292 292 MET MET A . n 
B 1 107 GLN 107 293 293 GLN GLN A . n 
B 1 108 HIS 108 294 294 HIS HIS A . n 
B 1 109 ASP 109 295 295 ASP ASP A . n 
B 1 110 VAL 110 296 296 VAL VAL A . n 
B 1 111 GLN 111 297 297 GLN GLN A . n 
B 1 112 GLU 112 298 298 GLU GLU A . n 
B 1 113 LEU 113 299 299 LEU LEU A . n 
B 1 114 CYS 114 300 300 CYS CYS A . n 
B 1 115 ARG 115 301 301 ARG ARG A . n 
B 1 116 VAL 116 302 302 VAL VAL A . n 
B 1 117 LEU 117 303 303 LEU LEU A . n 
B 1 118 LEU 118 304 304 LEU LEU A . n 
B 1 119 ASP 119 305 305 ASP ASP A . n 
B 1 120 ASN 120 306 306 ASN ASN A . n 
B 1 121 VAL 121 307 307 VAL VAL A . n 
B 1 122 GLU 122 308 308 GLU GLU A . n 
B 1 123 ASN 123 309 309 ASN ASN A . n 
B 1 124 LYS 124 310 310 LYS LYS A . n 
B 1 125 MET 125 311 311 MET MET A . n 
B 1 126 LYS 126 312 312 LYS LYS A . n 
B 1 127 GLY 127 313 313 GLY GLY A . n 
B 1 128 THR 128 314 314 THR THR A . n 
B 1 129 CYS 129 315 315 CYS CYS A . n 
B 1 130 VAL 130 316 316 VAL VAL A . n 
B 1 131 GLU 131 317 317 GLU GLU A . n 
B 1 132 GLY 132 318 318 GLY GLY A . n 
B 1 133 THR 133 319 319 THR THR A . n 
B 1 134 ILE 134 320 320 ILE ILE A . n 
B 1 135 PRO 135 321 321 PRO PRO A . n 
B 1 136 LYS 136 322 322 LYS LYS A . n 
B 1 137 LEU 137 323 323 LEU LEU A . n 
B 1 138 PHE 138 324 324 PHE PHE A . n 
B 1 139 ARG 139 325 325 ARG ARG A . n 
B 1 140 GLY 140 326 326 GLY GLY A . n 
B 1 141 LYS 141 327 327 LYS LYS A . n 
B 1 142 MET 142 328 328 MET MET A . n 
B 1 143 VAL 143 329 329 VAL VAL A . n 
B 1 144 SER 144 330 330 SER SER A . n 
B 1 145 TYR 145 331 331 TYR TYR A . n 
B 1 146 ILE 146 332 332 ILE ILE A . n 
B 1 147 GLN 147 333 333 GLN GLN A . n 
B 1 148 CYS 148 334 334 CYS CYS A . n 
B 1 149 LYS 149 335 335 LYS LYS A . n 
B 1 150 GLU 150 336 336 GLU GLU A . n 
B 1 151 VAL 151 337 337 VAL VAL A . n 
B 1 152 ASP 152 338 338 ASP ASP A . n 
B 1 153 TYR 153 339 339 TYR TYR A . n 
B 1 154 ARG 154 340 340 ARG ARG A . n 
B 1 155 SER 155 341 341 SER SER A . n 
B 1 156 ASP 156 342 342 ASP ASP A . n 
B 1 157 ARG 157 343 343 ARG ARG A . n 
B 1 158 ARG 158 344 344 ARG ARG A . n 
B 1 159 GLU 159 345 345 GLU GLU A . n 
B 1 160 ASP 160 346 346 ASP ASP A . n 
B 1 161 TYR 161 347 347 TYR TYR A . n 
B 1 162 TYR 162 348 348 TYR TYR A . n 
B 1 163 ASP 163 349 349 ASP ASP A . n 
B 1 164 ILE 164 350 350 ILE ILE A . n 
B 1 165 GLN 165 351 351 GLN GLN A . n 
B 1 166 LEU 166 352 352 LEU LEU A . n 
B 1 167 SER 167 353 353 SER SER A . n 
B 1 168 ILE 168 354 354 ILE ILE A . n 
B 1 169 LYS 169 355 355 LYS LYS A . n 
B 1 170 GLY 170 356 356 GLY GLY A . n 
B 1 171 LYS 171 357 357 LYS LYS A . n 
B 1 172 LYS 172 358 358 LYS LYS A . n 
B 1 173 ASN 173 359 359 ASN ASN A . n 
B 1 174 ILE 174 360 360 ILE ILE A . n 
B 1 175 PHE 175 361 361 PHE PHE A . n 
B 1 176 GLU 176 362 362 GLU GLU A . n 
B 1 177 SER 177 363 363 SER SER A . n 
B 1 178 PHE 178 364 364 PHE PHE A . n 
B 1 179 VAL 179 365 365 VAL VAL A . n 
B 1 180 ASP 180 366 366 ASP ASP A . n 
B 1 181 TYR 181 367 367 TYR TYR A . n 
B 1 182 VAL 182 368 368 VAL VAL A . n 
B 1 183 ALA 183 369 369 ALA ALA A . n 
B 1 184 VAL 184 370 370 VAL VAL A . n 
B 1 185 GLU 185 371 371 GLU GLU A . n 
B 1 186 GLN 186 372 372 GLN GLN A . n 
B 1 187 LEU 187 373 373 LEU LEU A . n 
B 1 188 ASP 188 374 374 ASP ASP A . n 
B 1 189 GLY 189 375 375 GLY GLY A . n 
B 1 190 ASP 190 376 376 ASP ASP A . n 
B 1 191 ASN 191 377 377 ASN ASN A . n 
B 1 192 LYS 192 378 378 LYS LYS A . n 
B 1 193 TYR 193 379 379 TYR TYR A . n 
B 1 194 ASP 194 380 380 ASP ASP A . n 
B 1 195 ALA 195 381 381 ALA ALA A . n 
B 1 196 GLY 196 382 382 GLY GLY A . n 
B 1 197 GLU 197 383 383 GLU GLU A . n 
B 1 198 HIS 198 384 384 HIS HIS A . n 
B 1 199 GLY 199 385 385 GLY GLY A . n 
B 1 200 LEU 200 386 386 LEU LEU A . n 
B 1 201 GLN 201 387 387 GLN GLN A . n 
B 1 202 GLU 202 388 388 GLU GLU A . n 
B 1 203 ALA 203 389 389 ALA ALA A . n 
B 1 204 GLU 204 390 390 GLU GLU A . n 
B 1 205 LYS 205 391 391 LYS LYS A . n 
B 1 206 GLY 206 392 392 GLY GLY A . n 
B 1 207 VAL 207 393 393 VAL VAL A . n 
B 1 208 LYS 208 394 394 LYS LYS A . n 
B 1 209 PHE 209 395 395 PHE PHE A . n 
B 1 210 LEU 210 396 396 LEU LEU A . n 
B 1 211 THR 211 397 397 THR THR A . n 
B 1 212 LEU 212 398 398 LEU LEU A . n 
B 1 213 PRO 213 399 399 PRO PRO A . n 
B 1 214 PRO 214 400 400 PRO PRO A . n 
B 1 215 VAL 215 401 401 VAL VAL A . n 
B 1 216 LEU 216 402 402 LEU LEU A . n 
B 1 217 HIS 217 403 403 HIS HIS A . n 
B 1 218 LEU 218 404 404 LEU LEU A . n 
B 1 219 GLN 219 405 405 GLN GLN A . n 
B 1 220 LEU 220 406 406 LEU LEU A . n 
B 1 221 MET 221 407 407 MET MET A . n 
B 1 222 ARG 222 408 408 ARG ARG A . n 
B 1 223 PHE 223 409 409 PHE PHE A . n 
B 1 224 MET 224 410 410 MET MET A . n 
B 1 225 TYR 225 411 ?   ?   ?   A . n 
B 1 226 ASP 226 412 ?   ?   ?   A . n 
B 1 227 PRO 227 413 ?   ?   ?   A . n 
B 1 228 GLN 228 414 414 GLN GLN A . n 
B 1 229 THR 229 415 415 THR THR A . n 
B 1 230 ASP 230 416 416 ASP ASP A . n 
B 1 231 GLN 231 417 417 GLN GLN A . n 
B 1 232 ASN 232 418 418 ASN ASN A . n 
B 1 233 ILE 233 419 419 ILE ILE A . n 
B 1 234 LYS 234 420 420 LYS LYS A . n 
B 1 235 ILE 235 421 421 ILE ILE A . n 
B 1 236 ASN 236 422 422 ASN ASN A . n 
B 1 237 ASP 237 423 423 ASP ASP A . n 
B 1 238 ARG 238 424 424 ARG ARG A . n 
B 1 239 PHE 239 425 425 PHE PHE A . n 
B 1 240 GLU 240 426 426 GLU GLU A . n 
B 1 241 PHE 241 427 427 PHE PHE A . n 
B 1 242 PRO 242 428 428 PRO PRO A . n 
B 1 243 GLU 243 429 429 GLU GLU A . n 
B 1 244 GLN 244 430 430 GLN GLN A . n 
B 1 245 LEU 245 431 431 LEU LEU A . n 
B 1 246 PRO 246 432 432 PRO PRO A . n 
B 1 247 LEU 247 433 433 LEU LEU A . n 
B 1 248 ASP 248 434 434 ASP ASP A . n 
B 1 249 GLU 249 435 435 GLU GLU A . n 
B 1 250 PHE 250 436 436 PHE PHE A . n 
B 1 251 LEU 251 437 437 LEU LEU A . n 
B 1 252 GLN 252 438 438 GLN GLN A . n 
B 1 253 LYS 253 439 439 LYS LYS A . n 
B 1 254 THR 254 440 440 THR THR A . n 
B 1 255 ASP 255 441 441 ASP ASP A . n 
B 1 256 PRO 256 442 442 PRO PRO A . n 
B 1 257 LYS 257 443 443 LYS LYS A . n 
B 1 258 ASP 258 444 444 ASP ASP A . n 
B 1 259 PRO 259 445 445 PRO PRO A . n 
B 1 260 ALA 260 446 446 ALA ALA A . n 
B 1 261 ASN 261 447 447 ASN ASN A . n 
B 1 262 TYR 262 448 448 TYR TYR A . n 
B 1 263 ILE 263 449 449 ILE ILE A . n 
B 1 264 LEU 264 450 450 LEU LEU A . n 
B 1 265 HIS 265 451 451 HIS HIS A . n 
B 1 266 ALA 266 452 452 ALA ALA A . n 
B 1 267 VAL 267 453 453 VAL VAL A . n 
B 1 268 LEU 268 454 454 LEU LEU A . n 
B 1 269 VAL 269 455 455 VAL VAL A . n 
B 1 270 HIS 270 456 456 HIS HIS A . n 
B 1 271 SER 271 457 457 SER SER A . n 
B 1 272 GLY 272 458 458 GLY GLY A . n 
B 1 273 ASP 273 459 459 ASP ASP A . n 
B 1 274 ASN 274 460 460 ASN ASN A . n 
B 1 275 HIS 275 461 461 HIS HIS A . n 
B 1 276 GLY 276 462 462 GLY GLY A . n 
B 1 277 GLY 277 463 463 GLY GLY A . n 
B 1 278 HIS 278 464 464 HIS HIS A . n 
B 1 279 TYR 279 465 465 TYR TYR A . n 
B 1 280 VAL 280 466 466 VAL VAL A . n 
B 1 281 VAL 281 467 467 VAL VAL A . n 
B 1 282 TYR 282 468 468 TYR TYR A . n 
B 1 283 LEU 283 469 469 LEU LEU A . n 
B 1 284 ASN 284 470 470 ASN ASN A . n 
B 1 285 PRO 285 471 471 PRO PRO A . n 
B 1 286 LYS 286 472 472 LYS LYS A . n 
B 1 287 GLY 287 473 473 GLY GLY A . n 
B 1 288 ASP 288 474 474 ASP ASP A . n 
B 1 289 GLY 289 475 475 GLY GLY A . n 
B 1 290 LYS 290 476 476 LYS LYS A . n 
B 1 291 TRP 291 477 477 TRP TRP A . n 
B 1 292 CYS 292 478 478 CYS CYS A . n 
B 1 293 LYS 293 479 479 LYS LYS A . n 
B 1 294 PHE 294 480 480 PHE PHE A . n 
B 1 295 ASP 295 481 481 ASP ASP A . n 
B 1 296 ASP 296 482 482 ASP ASP A . n 
B 1 297 ASP 297 483 483 ASP ASP A . n 
B 1 298 VAL 298 484 484 VAL VAL A . n 
B 1 299 VAL 299 485 485 VAL VAL A . n 
B 1 300 SER 300 486 486 SER SER A . n 
B 1 301 ARG 301 487 487 ARG ARG A . n 
B 1 302 CYS 302 488 488 CYS CYS A . n 
B 1 303 THR 303 489 489 THR THR A . n 
B 1 304 LYS 304 490 490 LYS LYS A . n 
B 1 305 GLU 305 491 491 GLU GLU A . n 
B 1 306 GLU 306 492 492 GLU GLU A . n 
B 1 307 ALA 307 493 493 ALA ALA A . n 
B 1 308 ILE 308 494 494 ILE ILE A . n 
B 1 309 GLU 309 495 495 GLU GLU A . n 
B 1 310 HIS 310 496 496 HIS HIS A . n 
B 1 311 ASN 311 497 497 ASN ASN A . n 
B 1 312 TYR 312 498 498 TYR TYR A . n 
B 1 313 GLY 313 499 499 GLY GLY A . n 
B 1 314 GLY 314 500 ?   ?   ?   A . n 
B 1 315 HIS 315 501 ?   ?   ?   A . n 
B 1 316 ASP 316 502 ?   ?   ?   A . n 
B 1 317 ASP 317 503 ?   ?   ?   A . n 
B 1 318 ASP 318 504 ?   ?   ?   A . n 
B 1 319 LEU 319 505 ?   ?   ?   A . n 
B 1 320 SER 320 506 ?   ?   ?   A . n 
B 1 321 VAL 321 507 ?   ?   ?   A . n 
B 1 322 ARG 322 508 508 ARG ARG A . n 
B 1 323 HIS 323 509 509 HIS HIS A . n 
B 1 324 CYS 324 510 510 CYS CYS A . n 
B 1 325 THR 325 511 511 THR THR A . n 
B 1 326 ASN 326 512 512 ASN ASN A . n 
B 1 327 ALA 327 513 513 ALA ALA A . n 
B 1 328 TYR 328 514 514 TYR TYR A . n 
B 1 329 MET 329 515 515 MET MET A . n 
B 1 330 LEU 330 516 516 LEU LEU A . n 
B 1 331 VAL 331 517 517 VAL VAL A . n 
B 1 332 TYR 332 518 518 TYR TYR A . n 
B 1 333 ILE 333 519 519 ILE ILE A . n 
B 1 334 ARG 334 520 520 ARG ARG A . n 
B 1 335 GLU 335 521 521 GLU GLU A . n 
B 1 336 SER 336 522 522 SER SER A . n 
B 1 337 LYS 337 523 523 LYS LYS A . n 
B 1 338 LEU 338 524 524 LEU LEU A . n 
B 1 339 SER 339 525 525 SER SER A . n 
B 1 340 GLU 340 526 526 GLU GLU A . n 
B 1 341 VAL 341 527 527 VAL VAL A . n 
B 1 342 LEU 342 528 528 LEU LEU A . n 
B 1 343 GLN 343 529 529 GLN GLN A . n 
B 1 344 ALA 344 530 530 ALA ALA A . n 
B 1 345 VAL 345 531 531 VAL VAL A . n 
B 1 346 THR 346 532 532 THR THR A . n 
B 1 347 ASP 347 533 533 ASP ASP A . n 
B 1 348 HIS 348 534 534 HIS HIS A . n 
B 1 349 ASP 349 535 535 ASP ASP A . n 
B 1 350 ILE 350 536 536 ILE ILE A . n 
B 1 351 PRO 351 537 537 PRO PRO A . n 
B 1 352 GLN 352 538 538 GLN GLN A . n 
B 1 353 GLN 353 539 539 GLN GLN A . n 
B 1 354 LEU 354 540 540 LEU LEU A . n 
B 1 355 VAL 355 541 541 VAL VAL A . n 
B 1 356 GLU 356 542 542 GLU GLU A . n 
B 1 357 ARG 357 543 543 ARG ARG A . n 
B 1 358 LEU 358 544 544 LEU LEU A . n 
B 1 359 GLN 359 545 545 GLN GLN A . n 
B 1 360 GLU 360 546 546 GLU GLU A . n 
B 1 361 GLU 361 547 547 GLU GLU A . n 
B 1 362 LYS 362 548 548 LYS LYS A . n 
B 1 363 ARG 363 549 549 ARG ARG A . n 
B 1 364 ILE 364 550 550 ILE ILE A . n 
B 1 365 GLU 365 551 551 GLU GLU A . n 
B 1 366 ALA 366 552 552 ALA ALA A . n 
B 1 367 GLN 367 553 553 GLN GLN A . n 
B 1 368 LYS 368 554 ?   ?   ?   A . n 
C 2 1   ACE 1   0   0   ACE ACE D . n 
C 2 2   PHE 2   1   1   PHE PHE D . n 
C 2 3   MEA 3   2   2   MEA DRG D . n 
C 2 4   ASN 4   3   3   ASN ASN D . n 
C 2 5   MEA 5   4   4   MEA DRG D . n 
C 2 6   PRO 6   5   5   PRO PRO D . n 
C 2 7   ASN 7   6   6   ASN ASN D . n 
C 2 8   DI8 8   7   7   DI8 TIC D . n 
C 2 9   TYR 9   8   8   TYR TYR D . n 
C 2 10  ARG 10  9   9   ARG ARG D . n 
C 2 11  ARG 11  10  10  ARG ARG D . n 
C 2 12  CYS 12  11  11  CYS CYS D . n 
C 2 13  GLY 13  12  12  GLY GLY D . n 
C 2 14  LYS 14  13  13  LYS LYS D . n 
C 2 15  LYS 15  14  ?   ?   ?   D . n 
D 2 1   ACE 1   0   0   ACE ACE C . n 
D 2 2   PHE 2   1   1   PHE PHE C . n 
D 2 3   MEA 3   2   2   MEA DRG C . n 
D 2 4   ASN 4   3   3   ASN ASN C . n 
D 2 5   MEA 5   4   4   MEA DRG C . n 
D 2 6   PRO 6   5   5   PRO PRO C . n 
D 2 7   ASN 7   6   6   ASN ASN C . n 
D 2 8   DI8 8   7   7   DI8 TIC C . n 
D 2 9   TYR 9   8   8   TYR TYR C . n 
D 2 10  ARG 10  9   9   ARG ARG C . n 
D 2 11  ARG 11  10  10  ARG ARG C . n 
D 2 12  CYS 12  11  11  CYS CYS C . n 
D 2 13  GLY 13  12  12  GLY GLY C . n 
D 2 14  LYS 14  13  13  LYS LYS C . n 
D 2 15  LYS 15  14  14  LYS LYS C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 MEA ? ? MEA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DI8 ? ? DI8 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 EOH 1 601 601 EOH EOH A . 
F 4 HOH 1 601 2   HOH HOH B . 
F 4 HOH 2 602 3   HOH HOH B . 
F 4 HOH 3 603 8   HOH HOH B . 
F 4 HOH 4 604 5   HOH HOH B . 
G 4 HOH 1 701 1   HOH HOH A . 
G 4 HOH 2 702 4   HOH HOH A . 
G 4 HOH 3 703 7   HOH HOH A . 
G 4 HOH 4 704 6   HOH HOH A . 
G 4 HOH 5 705 9   HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B LYS 278 ? CG ? A LYS 92  CG 
2 1 Y 1 B LYS 278 ? CD ? A LYS 92  CD 
3 1 Y 1 B LYS 278 ? CE ? A LYS 92  CE 
4 1 Y 1 B LYS 278 ? NZ ? A LYS 92  NZ 
5 1 Y 1 B LYS 476 ? CG ? A LYS 290 CG 
6 1 Y 1 B LYS 476 ? CD ? A LYS 290 CD 
7 1 Y 1 B LYS 476 ? CE ? A LYS 290 CE 
8 1 Y 1 B LYS 476 ? NZ ? A LYS 290 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.36 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DEN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.362 
_cell.length_a_esd                 ? 
_cell.length_b                     69.675 
_cell.length_b_esd                 ? 
_cell.length_c                     77.617 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9DEN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DEN 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_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    '25% w/v PEG 1500 and 0.1 M MMT (malic acid, MES, Tris) buffer pH 7' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-15 
_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   1.00004 
_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                        'ALS BEAMLINE 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00004 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          72.86 
_reflns.entry_id                                       9DEN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.93 
_reflns.d_resolution_low                               41.66 
_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                                     17031 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.05 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.71 
_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                                0.074 
_reflns.pdbx_Rpim_I_all                                0.040 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.063 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.93 
_reflns_shell.d_res_low                                     3.035 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.46 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1707 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.51 
_reflns_shell.pdbx_Rpim_I_all                               0.26 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.954 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.92 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.43 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DEN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.93 
_refine.ls_d_res_low                             41.66 
_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                     16923 
_refine.ls_number_reflns_R_free                  878 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.08 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2258 
_refine.ls_R_factor_R_free                       0.2497 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2244 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.56 
_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                            0.30 
_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.pdbx_number_atoms_protein        5677 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               5689 
_refine_hist.d_res_high                       2.93 
_refine_hist.d_res_low                        41.66 
# 
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' ? 0.004  ? 5798 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.704  ? 7803 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.536 ? 2182 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 826  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 1016 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.93 3.11  . . 135 2679 98.00 . . . . 0.3412 . . . . . . . . . . . 0.3557 
'X-RAY DIFFRACTION' 3.11 3.35  . . 151 2671 98.00 . . . . 0.3280 . . . . . . . . . . . 0.3533 
'X-RAY DIFFRACTION' 3.35 3.69  . . 176 2665 98.00 . . . . 0.2697 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 3.69 4.23  . . 127 2628 96.00 . . . . 0.2380 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 4.23 5.32  . . 162 2699 98.00 . . . . 0.1835 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 5.32 41.66 . . 127 2703 95.00 . . . . 0.1773 . . . . . . . . . . . 0.2189 
# 
_struct.entry_id                     9DEN 
_struct.title                        'USP7 in complex with macrocycle MC07' 
_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        9DEN 
_struct_keywords.text            'USP7, HAUSP, macrocycle, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'HYDROLASE/HYDROLASE INHIBITOR' 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP UBP7_HUMAN Q93009 Q93009-3 1 
;KKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWET
LDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDY
VAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPAN
YILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEV
LQAVTDHDIPQQLVERLQEEKRIEAQK
;
192 
2 PDB 9DEN       9DEN   ?        2 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DEN B 22 ? 368 ? Q93009 192 ? 538 ? 208 554 
2 1 9DEN A 22 ? 368 ? Q93009 192 ? 538 ? 208 554 
3 2 9DEN D 1  ? 15  ? 9DEN   0   ? 14  ? 0   14  
4 2 9DEN C 1  ? 15  ? 9DEN   0   ? 14  ? 0   14  
# 
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 9DEN MET B 1  ? UNP Q93009 ? ? 'initiating methionine' 187 1  
1 9DEN GLY B 2  ? UNP Q93009 ? ? 'expression tag'        188 2  
1 9DEN SER B 3  ? UNP Q93009 ? ? 'expression tag'        189 3  
1 9DEN SER B 4  ? UNP Q93009 ? ? 'expression tag'        190 4  
1 9DEN HIS B 5  ? UNP Q93009 ? ? 'expression tag'        191 5  
1 9DEN HIS B 6  ? UNP Q93009 ? ? 'expression tag'        192 6  
1 9DEN HIS B 7  ? UNP Q93009 ? ? 'expression tag'        193 7  
1 9DEN HIS B 8  ? UNP Q93009 ? ? 'expression tag'        194 8  
1 9DEN HIS B 9  ? UNP Q93009 ? ? 'expression tag'        195 9  
1 9DEN HIS B 10 ? UNP Q93009 ? ? 'expression tag'        196 10 
1 9DEN SER B 11 ? UNP Q93009 ? ? 'expression tag'        197 11 
1 9DEN SER B 12 ? UNP Q93009 ? ? 'expression tag'        198 12 
1 9DEN GLY B 13 ? UNP Q93009 ? ? 'expression tag'        199 13 
1 9DEN LEU B 14 ? UNP Q93009 ? ? 'expression tag'        200 14 
1 9DEN VAL B 15 ? UNP Q93009 ? ? 'expression tag'        201 15 
1 9DEN PRO B 16 ? UNP Q93009 ? ? 'expression tag'        202 16 
1 9DEN ARG B 17 ? UNP Q93009 ? ? 'expression tag'        203 17 
1 9DEN GLY B 18 ? UNP Q93009 ? ? 'expression tag'        204 18 
1 9DEN SER B 19 ? UNP Q93009 ? ? 'expression tag'        205 19 
1 9DEN HIS B 20 ? UNP Q93009 ? ? 'expression tag'        206 20 
1 9DEN MET B 21 ? UNP Q93009 ? ? 'expression tag'        207 21 
2 9DEN MET A 1  ? UNP Q93009 ? ? 'initiating methionine' 187 22 
2 9DEN GLY A 2  ? UNP Q93009 ? ? 'expression tag'        188 23 
2 9DEN SER A 3  ? UNP Q93009 ? ? 'expression tag'        189 24 
2 9DEN SER A 4  ? UNP Q93009 ? ? 'expression tag'        190 25 
2 9DEN HIS A 5  ? UNP Q93009 ? ? 'expression tag'        191 26 
2 9DEN HIS A 6  ? UNP Q93009 ? ? 'expression tag'        192 27 
2 9DEN HIS A 7  ? UNP Q93009 ? ? 'expression tag'        193 28 
2 9DEN HIS A 8  ? UNP Q93009 ? ? 'expression tag'        194 29 
2 9DEN HIS A 9  ? UNP Q93009 ? ? 'expression tag'        195 30 
2 9DEN HIS A 10 ? UNP Q93009 ? ? 'expression tag'        196 31 
2 9DEN SER A 11 ? UNP Q93009 ? ? 'expression tag'        197 32 
2 9DEN SER A 12 ? UNP Q93009 ? ? 'expression tag'        198 33 
2 9DEN GLY A 13 ? UNP Q93009 ? ? 'expression tag'        199 34 
2 9DEN LEU A 14 ? UNP Q93009 ? ? 'expression tag'        200 35 
2 9DEN VAL A 15 ? UNP Q93009 ? ? 'expression tag'        201 36 
2 9DEN PRO A 16 ? UNP Q93009 ? ? 'expression tag'        202 37 
2 9DEN ARG A 17 ? UNP Q93009 ? ? 'expression tag'        203 38 
2 9DEN GLY A 18 ? UNP Q93009 ? ? 'expression tag'        204 39 
2 9DEN SER A 19 ? UNP Q93009 ? ? 'expression tag'        205 40 
2 9DEN HIS A 20 ? UNP Q93009 ? ? 'expression tag'        206 41 
2 9DEN MET A 21 ? UNP Q93009 ? ? 'expression tag'        207 42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2050  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  16820 ? 
2 'ABSA (A^2)' 2020  ? 
2 MORE         -5    ? 
2 'SSA (A^2)'  16830 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,F   
2 1 B,D,E,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TYR A 38  ? PHE A 48  ? TYR B 224 PHE B 234 1 ? 11 
HELX_P HELX_P2  AA2 THR A 49  ? MET A 58  ? THR B 235 MET B 244 1 ? 10 
HELX_P HELX_P3  AA3 SER A 69  ? SER A 84  ? SER B 255 SER B 270 1 ? 16 
HELX_P HELX_P4  AA4 THR A 90  ? PHE A 97  ? THR B 276 PHE B 283 1 ? 8  
HELX_P HELX_P5  AA5 ASP A 103 ? HIS A 108 ? ASP B 289 HIS B 294 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 109 ? MET A 125 ? ASP B 295 MET B 311 1 ? 17 
HELX_P HELX_P7  AA7 GLY A 132 ? ARG A 139 ? GLY B 318 ARG B 325 1 ? 8  
HELX_P HELX_P8  AA8 ASN A 173 ? ALA A 183 ? ASN B 359 ALA B 369 1 ? 11 
HELX_P HELX_P9  AA9 GLY A 196 ? HIS A 198 ? GLY B 382 HIS B 384 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 248 ? LEU A 251 ? ASP B 434 LEU B 437 5 ? 4  
HELX_P HELX_P11 AB2 THR A 303 ? ILE A 308 ? THR B 489 ILE B 494 1 ? 6  
HELX_P HELX_P12 AB3 GLU A 309 ? TYR A 312 ? GLU B 495 TYR B 498 5 ? 4  
HELX_P HELX_P13 AB4 LYS A 337 ? LEU A 342 ? LYS B 523 LEU B 528 1 ? 6  
HELX_P HELX_P14 AB5 THR A 346 ? ILE A 350 ? THR B 532 ILE B 536 5 ? 5  
HELX_P HELX_P15 AB6 PRO A 351 ? GLN A 367 ? PRO B 537 GLN B 553 1 ? 17 
HELX_P HELX_P16 AB7 TYR B 38  ? PHE B 48  ? TYR A 224 PHE A 234 1 ? 11 
HELX_P HELX_P17 AB8 THR B 49  ? MET B 58  ? THR A 235 MET A 244 1 ? 10 
HELX_P HELX_P18 AB9 SER B 69  ? SER B 84  ? SER A 255 SER A 270 1 ? 16 
HELX_P HELX_P19 AC1 THR B 90  ? PHE B 97  ? THR A 276 PHE A 283 1 ? 8  
HELX_P HELX_P20 AC2 ASP B 103 ? HIS B 108 ? ASP A 289 HIS A 294 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 109 ? LYS B 126 ? ASP A 295 LYS A 312 1 ? 18 
HELX_P HELX_P22 AC4 GLY B 132 ? ARG B 139 ? GLY A 318 ARG A 325 1 ? 8  
HELX_P HELX_P23 AC5 ASN B 173 ? ALA B 183 ? ASN A 359 ALA A 369 1 ? 11 
HELX_P HELX_P24 AC6 ALA B 195 ? GLY B 199 ? ALA A 381 GLY A 385 5 ? 5  
HELX_P HELX_P25 AC7 ASP B 248 ? LEU B 251 ? ASP A 434 LEU A 437 5 ? 4  
HELX_P HELX_P26 AC8 THR B 303 ? ILE B 308 ? THR A 489 ILE A 494 1 ? 6  
HELX_P HELX_P27 AC9 GLU B 309 ? TYR B 312 ? GLU A 495 TYR A 498 5 ? 4  
HELX_P HELX_P28 AD1 LYS B 337 ? LEU B 342 ? LYS A 523 LEU A 528 1 ? 6  
HELX_P HELX_P29 AD2 THR B 346 ? ILE B 350 ? THR A 532 ILE A 536 5 ? 5  
HELX_P HELX_P30 AD3 PRO B 351 ? ALA B 366 ? PRO A 537 ALA A 552 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? C ACE 1 C   ? ? ? 1_555 C PHE 2  N  ? ? D ACE 0 D PHE 1  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale2  covale none ? C ACE 1 CH3 ? ? ? 1_555 C CYS 12 SG ? ? D ACE 0 D CYS 11 1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale3  covale both ? C PHE 2 C   ? ? ? 1_555 C MEA 3  N  ? ? D PHE 1 D MEA 2  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale4  covale both ? C MEA 3 C   ? ? ? 1_555 C ASN 4  N  ? ? D MEA 2 D ASN 3  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale5  covale both ? C ASN 4 C   ? ? ? 1_555 C MEA 5  N  ? ? D ASN 3 D MEA 4  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale6  covale both ? C MEA 5 C   ? ? ? 1_555 C PRO 6  N  ? ? D MEA 4 D PRO 5  1_555 ? ? ? ? ? ? ? 1.347 ? ? 
covale7  covale both ? C ASN 7 C   ? ? ? 1_555 C DI8 8  N  ? ? D ASN 6 D DI8 7  1_555 ? ? ? ? ? ? ? 1.364 ? ? 
covale8  covale both ? C DI8 8 C   ? ? ? 1_555 C TYR 9  N  ? ? D DI8 7 D TYR 8  1_555 ? ? ? ? ? ? ? 1.381 ? ? 
covale9  covale both ? D ACE 1 C   ? ? ? 1_555 D PHE 2  N  ? ? C ACE 0 C PHE 1  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale10 covale none ? D ACE 1 CH3 ? ? ? 1_555 D CYS 12 SG ? ? C ACE 0 C CYS 11 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale11 covale both ? D PHE 2 C   ? ? ? 1_555 D MEA 3  N  ? ? C PHE 1 C MEA 2  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale12 covale both ? D MEA 3 C   ? ? ? 1_555 D ASN 4  N  ? ? C MEA 2 C ASN 3  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale13 covale both ? D ASN 4 C   ? ? ? 1_555 D MEA 5  N  ? ? C ASN 3 C MEA 4  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale14 covale both ? D MEA 5 C   ? ? ? 1_555 D PRO 6  N  ? ? C MEA 4 C PRO 5  1_555 ? ? ? ? ? ? ? 1.344 ? ? 
covale15 covale both ? D ASN 7 C   ? ? ? 1_555 D DI8 8  N  ? ? C ASN 6 C DI8 7  1_555 ? ? ? ? ? ? ? 1.363 ? ? 
covale16 covale both ? D DI8 8 C   ? ? ? 1_555 D TYR 9  N  ? ? C DI8 7 C TYR 8  1_555 ? ? ? ? ? ? ? 1.371 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  MEA C 3 ? .   . .  . MEA D 2 ? 1_555 .   . .  . .     .   .  PHE 1  MEA Methylation 'Named protein modification' 
2  MEA C 5 ? .   . .  . MEA D 4 ? 1_555 .   . .  . .     .   .  PHE 1  MEA Methylation 'Named protein modification' 
3  MEA D 3 ? .   . .  . MEA C 2 ? 1_555 .   . .  . .     .   .  PHE 1  MEA Methylation 'Named protein modification' 
4  MEA D 5 ? .   . .  . MEA C 4 ? 1_555 .   . .  . .     .   .  PHE 1  MEA Methylation 'Named protein modification' 
5  DI8 C 8 ? .   . .  . DI8 D 7 ? 1_555 .   . .  . .     .   .  ?   1  DI8 None        'Non-standard residue'       
6  DI8 D 8 ? .   . .  . DI8 C 7 ? 1_555 .   . .  . .     .   .  ?   1  DI8 None        'Non-standard residue'       
7  ACE C 1 ? PHE C 2  ? ACE D 0 ? 1_555 PHE D 1  ? 1_555 .   .  PHE 15 ACE None        'Terminal acetylation'       
8  ACE D 1 ? PHE D 2  ? ACE C 0 ? 1_555 PHE C 1  ? 1_555 .   .  PHE 15 ACE None        'Terminal acetylation'       
9  ACE C 1 ? CYS C 12 ? ACE D 0 ? 1_555 CYS D 11 ? 1_555 CH3 SG .   .  .   None        'Non-standard linkage'       
10 ACE D 1 ? CYS D 12 ? ACE C 0 ? 1_555 CYS C 11 ? 1_555 CH3 SG .   .  .   None        'Non-standard linkage'       
# 
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 PHE 2 C . ? PHE 1 D MEA 3 C ? MEA 2 D 1 -0.52 
2 MEA 5 C . ? MEA 4 D PRO 6 C ? PRO 5 D 1 -0.85 
3 PHE 2 D . ? PHE 1 C MEA 3 D ? MEA 2 C 1 -0.69 
4 MEA 5 D . ? MEA 4 C PRO 6 D ? PRO 5 C 1 -1.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? 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 ARG A 154 ? TYR A 161 ? ARG B 340 TYR B 347 
AA1 2 GLY A 140 ? CYS A 148 ? GLY B 326 CYS B 334 
AA1 3 ALA A 203 ? PHE A 209 ? ALA B 389 PHE B 395 
AA1 4 GLU A 185 ? LEU A 187 ? GLU B 371 LEU B 373 
AA2 1 ILE A 164 ? SER A 167 ? ILE B 350 SER B 353 
AA2 2 VAL A 215 ? MET A 221 ? VAL B 401 MET B 407 
AA2 3 CYS A 324 ? ARG A 334 ? CYS B 510 ARG B 520 
AA2 4 ASN A 261 ? GLY A 272 ? ASN B 447 GLY B 458 
AA2 5 GLN A 244 ? PRO A 246 ? GLN B 430 PRO B 432 
AA3 1 ILE A 164 ? SER A 167 ? ILE B 350 SER B 353 
AA3 2 VAL A 215 ? MET A 221 ? VAL B 401 MET B 407 
AA3 3 CYS A 324 ? ARG A 334 ? CYS B 510 ARG B 520 
AA3 4 ASN A 261 ? GLY A 272 ? ASN B 447 GLY B 458 
AA3 5 HIS A 278 ? LEU A 283 ? HIS B 464 LEU B 469 
AA3 6 CYS A 292 ? ASP A 295 ? CYS B 478 ASP B 481 
AA3 7 VAL A 298 ? ARG A 301 ? VAL B 484 ARG B 487 
AA4 1 TYR A 193 ? ASP A 194 ? TYR B 379 ASP B 380 
AA4 2 LEU A 200 ? GLN A 201 ? LEU B 386 GLN B 387 
AA5 1 PHE A 223 ? MET A 224 ? PHE B 409 MET B 410 
AA5 2 ILE A 233 ? LYS A 234 ? ILE B 419 LYS B 420 
AA6 1 ARG B 154 ? TYR B 161 ? ARG A 340 TYR A 347 
AA6 2 GLY B 140 ? CYS B 148 ? GLY A 326 CYS A 334 
AA6 3 ALA B 203 ? PHE B 209 ? ALA A 389 PHE A 395 
AA6 4 GLU B 185 ? GLN B 186 ? GLU A 371 GLN A 372 
AA7 1 ILE B 164 ? SER B 167 ? ILE A 350 SER A 353 
AA7 2 VAL B 215 ? MET B 221 ? VAL A 401 MET A 407 
AA7 3 ASN B 326 ? ARG B 334 ? ASN A 512 ARG A 520 
AA7 4 ASN B 261 ? SER B 271 ? ASN A 447 SER A 457 
AA7 5 GLN B 244 ? PRO B 246 ? GLN A 430 PRO A 432 
AA8 1 ILE B 164 ? SER B 167 ? ILE A 350 SER A 353 
AA8 2 VAL B 215 ? MET B 221 ? VAL A 401 MET A 407 
AA8 3 ASN B 326 ? ARG B 334 ? ASN A 512 ARG A 520 
AA8 4 ASN B 261 ? SER B 271 ? ASN A 447 SER A 457 
AA8 5 HIS B 278 ? LEU B 283 ? HIS A 464 LEU A 469 
AA8 6 CYS B 292 ? ASP B 295 ? CYS A 478 ASP A 481 
AA8 7 VAL B 298 ? ARG B 301 ? VAL A 484 ARG A 487 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 159 ? O GLU B 345 N MET A 142 ? N MET B 328 
AA1 2 3 N GLN A 147 ? N GLN B 333 O GLU A 204 ? O GLU B 390 
AA1 3 4 O LYS A 205 ? O LYS B 391 N GLU A 185 ? N GLU B 371 
AA2 1 2 N LEU A 166 ? N LEU B 352 O GLN A 219 ? O GLN B 405 
AA2 2 3 N LEU A 220 ? N LEU B 406 O TYR A 328 ? O TYR B 514 
AA2 3 4 O VAL A 331 ? O VAL B 517 N HIS A 265 ? N HIS B 451 
AA2 4 5 O TYR A 262 ? O TYR B 448 N LEU A 245 ? N LEU B 431 
AA3 1 2 N LEU A 166 ? N LEU B 352 O GLN A 219 ? O GLN B 405 
AA3 2 3 N LEU A 220 ? N LEU B 406 O TYR A 328 ? O TYR B 514 
AA3 3 4 O VAL A 331 ? O VAL B 517 N HIS A 265 ? N HIS B 451 
AA3 4 5 N VAL A 269 ? N VAL B 455 O VAL A 280 ? O VAL B 466 
AA3 5 6 N LEU A 283 ? N LEU B 469 O CYS A 292 ? O CYS B 478 
AA3 6 7 N ASP A 295 ? N ASP B 481 O VAL A 298 ? O VAL B 484 
AA4 1 2 N TYR A 193 ? N TYR B 379 O GLN A 201 ? O GLN B 387 
AA5 1 2 N MET A 224 ? N MET B 410 O ILE A 233 ? O ILE B 419 
AA6 1 2 O GLU B 159 ? O GLU A 345 N MET B 142 ? N MET A 328 
AA6 2 3 N GLN B 147 ? N GLN A 333 O GLU B 204 ? O GLU A 390 
AA6 3 4 O LYS B 205 ? O LYS A 391 N GLU B 185 ? N GLU A 371 
AA7 1 2 N LEU B 166 ? N LEU A 352 O GLN B 219 ? O GLN A 405 
AA7 2 3 N LEU B 220 ? N LEU A 406 O TYR B 328 ? O TYR A 514 
AA7 3 4 O VAL B 331 ? O VAL A 517 N HIS B 265 ? N HIS A 451 
AA7 4 5 O TYR B 262 ? O TYR A 448 N LEU B 245 ? N LEU A 431 
AA8 1 2 N LEU B 166 ? N LEU A 352 O GLN B 219 ? O GLN A 405 
AA8 2 3 N LEU B 220 ? N LEU A 406 O TYR B 328 ? O TYR A 514 
AA8 3 4 O VAL B 331 ? O VAL A 517 N HIS B 265 ? N HIS A 451 
AA8 4 5 N SER B 271 ? N SER A 457 O HIS B 278 ? O HIS A 464 
AA8 5 6 N LEU B 283 ? N LEU A 469 O CYS B 292 ? O CYS A 478 
AA8 6 7 N LYS B 293 ? N LYS A 479 O SER B 300 ? O SER A 486 
# 
_pdbx_entry_details.entry_id                   9DEN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     217 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     416 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_554 
_pdbx_validate_symm_contact.dist              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 CYS B 223 ? ? 54.54   -120.61 
2  1 ASP B 376 ? ? 75.57   -9.21   
3  1 THR B 415 ? ? 13.26   -127.53 
4  1 ASP B 416 ? ? -150.72 26.93   
5  1 LYS B 443 ? ? 68.46   -2.09   
6  1 ASP B 444 ? ? -150.63 73.13   
7  1 ASP B 459 ? ? -64.55  -174.59 
8  1 HIS B 461 ? ? -103.71 -69.29  
9  1 ASP B 482 ? ? 55.78   -114.48 
10 1 LEU B 528 ? ? -103.06 40.06   
11 1 HIS A 210 ? ? 72.16   -14.40  
12 1 CYS A 223 ? ? 55.71   -124.79 
13 1 ASP A 376 ? ? 76.17   -8.23   
14 1 GLU A 388 ? ? 57.17   72.75   
15 1 ASP A 416 ? ? -146.92 -5.99   
16 1 LYS A 443 ? ? 68.67   -2.56   
17 1 ASP A 444 ? ? -152.77 75.03   
18 1 ASP A 482 ? ? 55.66   -113.64 
19 1 HIS A 509 ? ? 69.75   -0.09   
20 1 LEU A 528 ? ? -102.32 40.15   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASN 
_pdbx_validate_main_chain_plane.auth_asym_id             C 
_pdbx_validate_main_chain_plane.auth_seq_id              6 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.40 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 23.1358 2.9000  -1.7147  0.7977 ? 0.0128  ? 0.0799  ? 0.9903 ? 0.2208  ? 0.9410 ? 2.6553 ? 
-0.7037 ? 0.1730  ? 1.8739 ? -0.3609 ? 1.7190  ? -0.2600 ? -0.5593 ? -0.7961 ? -0.0077 ? 0.2856  ? -0.1275 ? 0.1418  ? 0.1257  ? 
0.0004  ? 
2  'X-RAY DIFFRACTION' ? refined -4.2234 7.0135  0.2683   0.8271 ? 0.0353  ? -0.0153 ? 1.1650 ? 0.2950  ? 0.9442 ? 2.0458 ? 1.2213 
? -0.2019 ? 0.1881 ? 0.5549  ? 0.1134  ? 0.0052  ? -0.0751 ? -0.3923 ? -0.2490 ? -0.0712 ? 0.2981  ? 0.1245  ? -0.0843 ? 0.0010  ? 
3  'X-RAY DIFFRACTION' ? refined 16.0898 15.5412 1.9294   0.7658 ? -0.0007 ? -0.0078 ? 1.1426 ? 0.1010  ? 0.6973 ? 3.7326 ? 0.2160 
? -0.3125 ? 2.3227 ? -0.3311 ? 1.0209  ? -0.0124 ? -0.3410 ? 0.0498  ? 0.1568  ? -0.0449 ? -0.0302 ? -0.0121 ? 0.1439  ? -0.0016 ? 
4  'X-RAY DIFFRACTION' ? refined 11.6795 6.2735  38.3884  0.7654 ? -0.0018 ? 0.0285  ? 0.7428 ? 0.1874  ? 0.7215 ? 1.7362 ? 
-0.4434 ? 0.2888  ? 1.1751 ? -0.9587 ? 0.6064  ? -0.2753 ? 0.3221  ? 0.1311  ? 0.1848  ? 0.0426  ? 0.2960  ? 0.0131  ? -0.5287 ? 
-0.0033 ? 
5  'X-RAY DIFFRACTION' ? refined 8.6480  -5.8599 36.3508  0.8354 ? -0.0707 ? -0.0293 ? 0.7750 ? 0.2791  ? 0.9540 ? 0.0506 ? 0.0683 
? 0.1034  ? 0.1011 ? 0.0335  ? -0.0359 ? -0.2338 ? 0.3768  ? -0.4229 ? 0.4280  ? -0.1586 ? 0.4700  ? 0.1537  ? -0.1838 ? -0.0000 ? 
6  'X-RAY DIFFRACTION' ? refined 29.5883 2.0871  39.4278  0.7692 ? 0.0161  ? -0.0504 ? 0.5694 ? 0.1368  ? 0.7142 ? 1.9518 ? 
-0.6336 ? -0.0115 ? 1.3267 ? 0.2670  ? 1.3773  ? -0.0589 ? -0.1953 ? -0.6119 ? 0.0763  ? 0.2120  ? -0.0383 ? 0.1546  ? 0.1350  ? 
-0.0017 ? 
7  'X-RAY DIFFRACTION' ? refined 51.9769 4.0581  39.6482  0.8798 ? 0.0109  ? -0.0467 ? 0.8322 ? -0.0829 ? 0.7923 ? 0.5653 ? 0.3177 
? -0.2893 ? 2.5471 ? 0.1425  ? 0.2604  ? -0.6433 ? -0.4155 ? 0.9038  ? 0.5527  ? 0.2631  ? -0.7966 ? -0.1313 ? -0.1305 ? 0.0084  ? 
8  'X-RAY DIFFRACTION' ? refined 24.8550 15.4824 41.0067  0.7668 ? 0.0670  ? -0.0091 ? 0.6466 ? 0.1560  ? 0.6644 ? 2.0889 ? 0.0943 
? -0.0244 ? 2.3811 ? 0.3780  ? 1.9362  ? -0.1097 ? 0.0095  ? 0.2732  ? 0.1459  ? 0.3778  ? -0.0503 ? -0.1401 ? -0.3628 ? -0.0020 ? 
9  'X-RAY DIFFRACTION' ? refined 19.1249 14.9888 35.8044  0.7557 ? 0.0113  ? -0.0469 ? 0.6936 ? 0.1755  ? 0.7768 ? 3.4731 ? 
-0.8344 ? -0.8440 ? 2.8459 ? 1.6220  ? 0.3578  ? -0.1013 ? -0.0077 ? 0.3226  ? -0.1204 ? 0.1366  ? 0.2806  ? -0.0716 ? -0.6820 ? 
0.0023  ? 
10 'X-RAY DIFFRACTION' ? refined -1.8963 -7.6698 35.5521  0.8971 ? -0.0834 ? -0.0806 ? 1.0165 ? -0.1471 ? 1.4904 ? 0.2374 ? 0.5336 
? 0.1180  ? 1.1156 ? 0.3858  ? 0.1331  ? -1.0917 ? 0.7142  ? -1.6477 ? -0.2066 ? -0.3559 ? 0.5186  ? -0.1646 ? -1.2529 ? 0.0601  ? 
11 'X-RAY DIFFRACTION' ? refined 5.7756  6.9885  -16.0587 1.0542 ? -0.1671 ? 0.0079  ? 1.0059 ? -0.0172 ? 0.9885 ? 0.0138 ? 0.0577 
? 0.1347  ? 0.3031 ? 0.3022  ? 0.3435  ? -0.4141 ? -0.4818 ? -0.8490 ? -0.8341 ? -0.1256 ? -0.1097 ? 1.3242  ? -0.6734 ? 0.0000  ? 
12 'X-RAY DIFFRACTION' ? refined 28.3805 4.7058  55.4024  1.0797 ? 0.2359  ? 0.0251  ? 0.8524 ? 0.3104  ? 0.8601 ? 0.3179 ? 0.3556 
? 0.1825  ? 0.5173 ? -0.0286 ? 0.2115  ? -0.7608 ? 0.0345  ? -0.1886 ? 1.3464  ? 0.0775  ? -0.8286 ? 0.1486  ? -0.8157 ? 0.0005  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 210 through 295 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 296 through 419 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 420 through 553 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 209 through 244 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 245 through 269 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 270 through 367 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 368 through 400 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 401 through 487 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 488 through 537 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 538 through 553 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 13 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 14 )
;
# 
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 B MET 187 ? A MET 1   
2  1 Y 1 B GLY 188 ? A GLY 2   
3  1 Y 1 B SER 189 ? A SER 3   
4  1 Y 1 B SER 190 ? A SER 4   
5  1 Y 1 B HIS 191 ? A HIS 5   
6  1 Y 1 B HIS 192 ? A HIS 6   
7  1 Y 1 B HIS 193 ? A HIS 7   
8  1 Y 1 B HIS 194 ? A HIS 8   
9  1 Y 1 B HIS 195 ? A HIS 9   
10 1 Y 1 B HIS 196 ? A HIS 10  
11 1 Y 1 B SER 197 ? A SER 11  
12 1 Y 1 B SER 198 ? A SER 12  
13 1 Y 1 B GLY 199 ? A GLY 13  
14 1 Y 1 B LEU 200 ? A LEU 14  
15 1 Y 1 B VAL 201 ? A VAL 15  
16 1 Y 1 B PRO 202 ? A PRO 16  
17 1 Y 1 B ARG 203 ? A ARG 17  
18 1 Y 1 B GLY 204 ? A GLY 18  
19 1 Y 1 B SER 205 ? A SER 19  
20 1 Y 1 B HIS 206 ? A HIS 20  
21 1 Y 1 B MET 207 ? A MET 21  
22 1 Y 1 B LYS 208 ? A LYS 22  
23 1 Y 1 B LYS 209 ? A LYS 23  
24 1 Y 1 B ASP 412 ? A ASP 226 
25 1 Y 1 B PRO 413 ? A PRO 227 
26 1 Y 1 B GLY 500 ? A GLY 314 
27 1 Y 1 B HIS 501 ? A HIS 315 
28 1 Y 1 B ASP 502 ? A ASP 316 
29 1 Y 1 B ASP 503 ? A ASP 317 
30 1 Y 1 B ASP 504 ? A ASP 318 
31 1 Y 1 B LEU 505 ? A LEU 319 
32 1 Y 1 B SER 506 ? A SER 320 
33 1 Y 1 B VAL 507 ? A VAL 321 
34 1 Y 1 B ARG 508 ? A ARG 322 
35 1 Y 1 B LYS 554 ? A LYS 368 
36 1 Y 1 A MET 187 ? B MET 1   
37 1 Y 1 A GLY 188 ? B GLY 2   
38 1 Y 1 A SER 189 ? B SER 3   
39 1 Y 1 A SER 190 ? B SER 4   
40 1 Y 1 A HIS 191 ? B HIS 5   
41 1 Y 1 A HIS 192 ? B HIS 6   
42 1 Y 1 A HIS 193 ? B HIS 7   
43 1 Y 1 A HIS 194 ? B HIS 8   
44 1 Y 1 A HIS 195 ? B HIS 9   
45 1 Y 1 A HIS 196 ? B HIS 10  
46 1 Y 1 A SER 197 ? B SER 11  
47 1 Y 1 A SER 198 ? B SER 12  
48 1 Y 1 A GLY 199 ? B GLY 13  
49 1 Y 1 A LEU 200 ? B LEU 14  
50 1 Y 1 A VAL 201 ? B VAL 15  
51 1 Y 1 A PRO 202 ? B PRO 16  
52 1 Y 1 A ARG 203 ? B ARG 17  
53 1 Y 1 A GLY 204 ? B GLY 18  
54 1 Y 1 A SER 205 ? B SER 19  
55 1 Y 1 A HIS 206 ? B HIS 20  
56 1 Y 1 A MET 207 ? B MET 21  
57 1 Y 1 A LYS 208 ? B LYS 22  
58 1 Y 1 A TYR 411 ? B TYR 225 
59 1 Y 1 A ASP 412 ? B ASP 226 
60 1 Y 1 A PRO 413 ? B PRO 227 
61 1 Y 1 A GLY 500 ? B GLY 314 
62 1 Y 1 A HIS 501 ? B HIS 315 
63 1 Y 1 A ASP 502 ? B ASP 316 
64 1 Y 1 A ASP 503 ? B ASP 317 
65 1 Y 1 A ASP 504 ? B ASP 318 
66 1 Y 1 A LEU 505 ? B LEU 319 
67 1 Y 1 A SER 506 ? B SER 320 
68 1 Y 1 A VAL 507 ? B VAL 321 
69 1 Y 1 A LYS 554 ? B LYS 368 
70 1 Y 1 D LYS 14  ? C LYS 15  
# 
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 
ACE C    C N N 1   
ACE O    O N N 2   
ACE CH3  C N N 3   
ACE H    H N N 4   
ACE H1   H N N 5   
ACE H2   H N N 6   
ACE H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
DI8 C    C N N 95  
DI8 N    N N N 96  
DI8 O    O N N 97  
DI8 C1   C N N 98  
DI8 C2   C Y N 99  
DI8 C3   C Y N 100 
DI8 C4   C Y N 101 
DI8 C5   C Y N 102 
DI8 C6   C Y N 103 
DI8 C7   C Y N 104 
DI8 C8   C N N 105 
DI8 CA   C N S 106 
DI8 OXT  O N N 107 
DI8 H    H N N 108 
DI8 HXT  H N N 109 
DI8 H1   H N N 110 
DI8 H1A  H N N 111 
DI8 H3   H N N 112 
DI8 H4   H N N 113 
DI8 H5   H N N 114 
DI8 H6   H N N 115 
DI8 H8   H N N 116 
DI8 H8A  H N N 117 
DI8 HA   H N N 118 
EOH C1   C N N 119 
EOH C2   C N N 120 
EOH O    O N N 121 
EOH H11  H N N 122 
EOH H12  H N N 123 
EOH H21  H N N 124 
EOH H22  H N N 125 
EOH H23  H N N 126 
EOH HO   H N N 127 
GLN N    N N N 128 
GLN CA   C N S 129 
GLN C    C N N 130 
GLN O    O N N 131 
GLN CB   C N N 132 
GLN CG   C N N 133 
GLN CD   C N N 134 
GLN OE1  O N N 135 
GLN NE2  N N N 136 
GLN OXT  O N N 137 
GLN H    H N N 138 
GLN H2   H N N 139 
GLN HA   H N N 140 
GLN HB2  H N N 141 
GLN HB3  H N N 142 
GLN HG2  H N N 143 
GLN HG3  H N N 144 
GLN HE21 H N N 145 
GLN HE22 H N N 146 
GLN HXT  H N N 147 
GLU N    N N N 148 
GLU CA   C N S 149 
GLU C    C N N 150 
GLU O    O N N 151 
GLU CB   C N N 152 
GLU CG   C N N 153 
GLU CD   C N N 154 
GLU OE1  O N N 155 
GLU OE2  O N N 156 
GLU OXT  O N N 157 
GLU H    H N N 158 
GLU H2   H N N 159 
GLU HA   H N N 160 
GLU HB2  H N N 161 
GLU HB3  H N N 162 
GLU HG2  H N N 163 
GLU HG3  H N N 164 
GLU HE2  H N N 165 
GLU HXT  H N N 166 
GLY N    N N N 167 
GLY CA   C N N 168 
GLY C    C N N 169 
GLY O    O N N 170 
GLY OXT  O N N 171 
GLY H    H N N 172 
GLY H2   H N N 173 
GLY HA2  H N N 174 
GLY HA3  H N N 175 
GLY HXT  H N N 176 
HIS N    N N N 177 
HIS CA   C N S 178 
HIS C    C N N 179 
HIS O    O N N 180 
HIS CB   C N N 181 
HIS CG   C Y N 182 
HIS ND1  N Y N 183 
HIS CD2  C Y N 184 
HIS CE1  C Y N 185 
HIS NE2  N Y N 186 
HIS OXT  O N N 187 
HIS H    H N N 188 
HIS H2   H N N 189 
HIS HA   H N N 190 
HIS HB2  H N N 191 
HIS HB3  H N N 192 
HIS HD1  H N N 193 
HIS HD2  H N N 194 
HIS HE1  H N N 195 
HIS HE2  H N N 196 
HIS HXT  H N N 197 
HOH O    O N N 198 
HOH H1   H N N 199 
HOH H2   H N N 200 
ILE N    N N N 201 
ILE CA   C N S 202 
ILE C    C N N 203 
ILE O    O N N 204 
ILE CB   C N S 205 
ILE CG1  C N N 206 
ILE CG2  C N N 207 
ILE CD1  C N N 208 
ILE OXT  O N N 209 
ILE H    H N N 210 
ILE H2   H N N 211 
ILE HA   H N N 212 
ILE HB   H N N 213 
ILE HG12 H N N 214 
ILE HG13 H N N 215 
ILE HG21 H N N 216 
ILE HG22 H N N 217 
ILE HG23 H N N 218 
ILE HD11 H N N 219 
ILE HD12 H N N 220 
ILE HD13 H N N 221 
ILE HXT  H N N 222 
LEU N    N N N 223 
LEU CA   C N S 224 
LEU C    C N N 225 
LEU O    O N N 226 
LEU CB   C N N 227 
LEU CG   C N N 228 
LEU CD1  C N N 229 
LEU CD2  C N N 230 
LEU OXT  O N N 231 
LEU H    H N N 232 
LEU H2   H N N 233 
LEU HA   H N N 234 
LEU HB2  H N N 235 
LEU HB3  H N N 236 
LEU HG   H N N 237 
LEU HD11 H N N 238 
LEU HD12 H N N 239 
LEU HD13 H N N 240 
LEU HD21 H N N 241 
LEU HD22 H N N 242 
LEU HD23 H N N 243 
LEU HXT  H N N 244 
LYS N    N N N 245 
LYS CA   C N S 246 
LYS C    C N N 247 
LYS O    O N N 248 
LYS CB   C N N 249 
LYS CG   C N N 250 
LYS CD   C N N 251 
LYS CE   C N N 252 
LYS NZ   N N N 253 
LYS OXT  O N N 254 
LYS H    H N N 255 
LYS H2   H N N 256 
LYS HA   H N N 257 
LYS HB2  H N N 258 
LYS HB3  H N N 259 
LYS HG2  H N N 260 
LYS HG3  H N N 261 
LYS HD2  H N N 262 
LYS HD3  H N N 263 
LYS HE2  H N N 264 
LYS HE3  H N N 265 
LYS HZ1  H N N 266 
LYS HZ2  H N N 267 
LYS HZ3  H N N 268 
LYS HXT  H N N 269 
MEA C1   C N N 270 
MEA N    N N N 271 
MEA CA   C N S 272 
MEA C    C N N 273 
MEA O    O N N 274 
MEA CB   C N N 275 
MEA CG   C Y N 276 
MEA CD1  C Y N 277 
MEA CE1  C Y N 278 
MEA CZ   C Y N 279 
MEA CE2  C Y N 280 
MEA CD2  C Y N 281 
MEA OXT  O N N 282 
MEA HC1  H N N 283 
MEA HC2  H N N 284 
MEA HC3  H N N 285 
MEA H    H N N 286 
MEA HA   H N N 287 
MEA HB1  H N N 288 
MEA HB2  H N N 289 
MEA HD1  H N N 290 
MEA HE1  H N N 291 
MEA HZ   H N N 292 
MEA HE2  H N N 293 
MEA HD2  H N N 294 
MEA HXT  H N N 295 
MET N    N N N 296 
MET CA   C N S 297 
MET C    C N N 298 
MET O    O N N 299 
MET CB   C N N 300 
MET CG   C N N 301 
MET SD   S N N 302 
MET CE   C N N 303 
MET OXT  O N N 304 
MET H    H N N 305 
MET H2   H N N 306 
MET HA   H N N 307 
MET HB2  H N N 308 
MET HB3  H N N 309 
MET HG2  H N N 310 
MET HG3  H N N 311 
MET HE1  H N N 312 
MET HE2  H N N 313 
MET HE3  H N N 314 
MET HXT  H N N 315 
PHE N    N N N 316 
PHE CA   C N S 317 
PHE C    C N N 318 
PHE O    O N N 319 
PHE CB   C N N 320 
PHE CG   C Y N 321 
PHE CD1  C Y N 322 
PHE CD2  C Y N 323 
PHE CE1  C Y N 324 
PHE CE2  C Y N 325 
PHE CZ   C Y N 326 
PHE OXT  O N N 327 
PHE H    H N N 328 
PHE H2   H N N 329 
PHE HA   H N N 330 
PHE HB2  H N N 331 
PHE HB3  H N N 332 
PHE HD1  H N N 333 
PHE HD2  H N N 334 
PHE HE1  H N N 335 
PHE HE2  H N N 336 
PHE HZ   H N N 337 
PHE HXT  H N N 338 
PRO N    N N N 339 
PRO CA   C N S 340 
PRO C    C N N 341 
PRO O    O N N 342 
PRO CB   C N N 343 
PRO CG   C N N 344 
PRO CD   C N N 345 
PRO OXT  O N N 346 
PRO H    H N N 347 
PRO HA   H N N 348 
PRO HB2  H N N 349 
PRO HB3  H N N 350 
PRO HG2  H N N 351 
PRO HG3  H N N 352 
PRO HD2  H N N 353 
PRO HD3  H N N 354 
PRO HXT  H N N 355 
SER N    N N N 356 
SER CA   C N S 357 
SER C    C N N 358 
SER O    O N N 359 
SER CB   C N N 360 
SER OG   O N N 361 
SER OXT  O N N 362 
SER H    H N N 363 
SER H2   H N N 364 
SER HA   H N N 365 
SER HB2  H N N 366 
SER HB3  H N N 367 
SER HG   H N N 368 
SER HXT  H N N 369 
THR N    N N N 370 
THR CA   C N S 371 
THR C    C N N 372 
THR O    O N N 373 
THR CB   C N R 374 
THR OG1  O N N 375 
THR CG2  C N N 376 
THR OXT  O N N 377 
THR H    H N N 378 
THR H2   H N N 379 
THR HA   H N N 380 
THR HB   H N N 381 
THR HG1  H N N 382 
THR HG21 H N N 383 
THR HG22 H N N 384 
THR HG23 H N N 385 
THR HXT  H N N 386 
TRP N    N N N 387 
TRP CA   C N S 388 
TRP C    C N N 389 
TRP O    O N N 390 
TRP CB   C N N 391 
TRP CG   C Y N 392 
TRP CD1  C Y N 393 
TRP CD2  C Y N 394 
TRP NE1  N Y N 395 
TRP CE2  C Y N 396 
TRP CE3  C Y N 397 
TRP CZ2  C Y N 398 
TRP CZ3  C Y N 399 
TRP CH2  C Y N 400 
TRP OXT  O N N 401 
TRP H    H N N 402 
TRP H2   H N N 403 
TRP HA   H N N 404 
TRP HB2  H N N 405 
TRP HB3  H N N 406 
TRP HD1  H N N 407 
TRP HE1  H N N 408 
TRP HE3  H N N 409 
TRP HZ2  H N N 410 
TRP HZ3  H N N 411 
TRP HH2  H N N 412 
TRP HXT  H N N 413 
TYR N    N N N 414 
TYR CA   C N S 415 
TYR C    C N N 416 
TYR O    O N N 417 
TYR CB   C N N 418 
TYR CG   C Y N 419 
TYR CD1  C Y N 420 
TYR CD2  C Y N 421 
TYR CE1  C Y N 422 
TYR CE2  C Y N 423 
TYR CZ   C Y N 424 
TYR OH   O N N 425 
TYR OXT  O N N 426 
TYR H    H N N 427 
TYR H2   H N N 428 
TYR HA   H N N 429 
TYR HB2  H N N 430 
TYR HB3  H N N 431 
TYR HD1  H N N 432 
TYR HD2  H N N 433 
TYR HE1  H N N 434 
TYR HE2  H N N 435 
TYR HH   H N N 436 
TYR HXT  H N N 437 
VAL N    N N N 438 
VAL CA   C N S 439 
VAL C    C N N 440 
VAL O    O N N 441 
VAL CB   C N N 442 
VAL CG1  C N N 443 
VAL CG2  C N N 444 
VAL OXT  O N N 445 
VAL H    H N N 446 
VAL H2   H N N 447 
VAL HA   H N N 448 
VAL HB   H N N 449 
VAL HG11 H N N 450 
VAL HG12 H N N 451 
VAL HG13 H N N 452 
VAL HG21 H N N 453 
VAL HG22 H N N 454 
VAL HG23 H N N 455 
VAL HXT  H N N 456 
# 
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 
ACE C   O    doub N N 1   
ACE C   CH3  sing N N 2   
ACE C   H    sing N N 3   
ACE CH3 H1   sing N N 4   
ACE CH3 H2   sing N N 5   
ACE CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
DI8 O   C    doub N N 89  
DI8 OXT C    sing N N 90  
DI8 C   CA   sing N N 91  
DI8 CA  N    sing N N 92  
DI8 N   C8   sing N N 93  
DI8 N   H    sing N N 94  
DI8 OXT HXT  sing N N 95  
DI8 CA  C1   sing N N 96  
DI8 C1  C2   sing N N 97  
DI8 C1  H1   sing N N 98  
DI8 C1  H1A  sing N N 99  
DI8 C2  C7   doub Y N 100 
DI8 C2  C3   sing Y N 101 
DI8 C3  C4   doub Y N 102 
DI8 C3  H3   sing N N 103 
DI8 C4  C5   sing Y N 104 
DI8 C4  H4   sing N N 105 
DI8 C6  C5   doub Y N 106 
DI8 C5  H5   sing N N 107 
DI8 C7  C6   sing Y N 108 
DI8 C6  H6   sing N N 109 
DI8 C8  C7   sing N N 110 
DI8 C8  H8   sing N N 111 
DI8 C8  H8A  sing N N 112 
DI8 CA  HA   sing N N 113 
EOH C1  C2   sing N N 114 
EOH C1  O    sing N N 115 
EOH C1  H11  sing N N 116 
EOH C1  H12  sing N N 117 
EOH C2  H21  sing N N 118 
EOH C2  H22  sing N N 119 
EOH C2  H23  sing N N 120 
EOH O   HO   sing N N 121 
GLN N   CA   sing N N 122 
GLN N   H    sing N N 123 
GLN N   H2   sing N N 124 
GLN CA  C    sing N N 125 
GLN CA  CB   sing N N 126 
GLN CA  HA   sing N N 127 
GLN C   O    doub N N 128 
GLN C   OXT  sing N N 129 
GLN CB  CG   sing N N 130 
GLN CB  HB2  sing N N 131 
GLN CB  HB3  sing N N 132 
GLN CG  CD   sing N N 133 
GLN CG  HG2  sing N N 134 
GLN CG  HG3  sing N N 135 
GLN CD  OE1  doub N N 136 
GLN CD  NE2  sing N N 137 
GLN NE2 HE21 sing N N 138 
GLN NE2 HE22 sing N N 139 
GLN OXT HXT  sing N N 140 
GLU N   CA   sing N N 141 
GLU N   H    sing N N 142 
GLU N   H2   sing N N 143 
GLU CA  C    sing N N 144 
GLU CA  CB   sing N N 145 
GLU CA  HA   sing N N 146 
GLU C   O    doub N N 147 
GLU C   OXT  sing N N 148 
GLU CB  CG   sing N N 149 
GLU CB  HB2  sing N N 150 
GLU CB  HB3  sing N N 151 
GLU CG  CD   sing N N 152 
GLU CG  HG2  sing N N 153 
GLU CG  HG3  sing N N 154 
GLU CD  OE1  doub N N 155 
GLU CD  OE2  sing N N 156 
GLU OE2 HE2  sing N N 157 
GLU OXT HXT  sing N N 158 
GLY N   CA   sing N N 159 
GLY N   H    sing N N 160 
GLY N   H2   sing N N 161 
GLY CA  C    sing N N 162 
GLY CA  HA2  sing N N 163 
GLY CA  HA3  sing N N 164 
GLY C   O    doub N N 165 
GLY C   OXT  sing N N 166 
GLY OXT HXT  sing N N 167 
HIS N   CA   sing N N 168 
HIS N   H    sing N N 169 
HIS N   H2   sing N N 170 
HIS CA  C    sing N N 171 
HIS CA  CB   sing N N 172 
HIS CA  HA   sing N N 173 
HIS C   O    doub N N 174 
HIS C   OXT  sing N N 175 
HIS CB  CG   sing N N 176 
HIS CB  HB2  sing N N 177 
HIS CB  HB3  sing N N 178 
HIS CG  ND1  sing Y N 179 
HIS CG  CD2  doub Y N 180 
HIS ND1 CE1  doub Y N 181 
HIS ND1 HD1  sing N N 182 
HIS CD2 NE2  sing Y N 183 
HIS CD2 HD2  sing N N 184 
HIS CE1 NE2  sing Y N 185 
HIS CE1 HE1  sing N N 186 
HIS NE2 HE2  sing N N 187 
HIS OXT HXT  sing N N 188 
HOH O   H1   sing N N 189 
HOH O   H2   sing N N 190 
ILE N   CA   sing N N 191 
ILE N   H    sing N N 192 
ILE N   H2   sing N N 193 
ILE CA  C    sing N N 194 
ILE CA  CB   sing N N 195 
ILE CA  HA   sing N N 196 
ILE C   O    doub N N 197 
ILE C   OXT  sing N N 198 
ILE CB  CG1  sing N N 199 
ILE CB  CG2  sing N N 200 
ILE CB  HB   sing N N 201 
ILE CG1 CD1  sing N N 202 
ILE CG1 HG12 sing N N 203 
ILE CG1 HG13 sing N N 204 
ILE CG2 HG21 sing N N 205 
ILE CG2 HG22 sing N N 206 
ILE CG2 HG23 sing N N 207 
ILE CD1 HD11 sing N N 208 
ILE CD1 HD12 sing N N 209 
ILE CD1 HD13 sing N N 210 
ILE OXT HXT  sing N N 211 
LEU N   CA   sing N N 212 
LEU N   H    sing N N 213 
LEU N   H2   sing N N 214 
LEU CA  C    sing N N 215 
LEU CA  CB   sing N N 216 
LEU CA  HA   sing N N 217 
LEU C   O    doub N N 218 
LEU C   OXT  sing N N 219 
LEU CB  CG   sing N N 220 
LEU CB  HB2  sing N N 221 
LEU CB  HB3  sing N N 222 
LEU CG  CD1  sing N N 223 
LEU CG  CD2  sing N N 224 
LEU CG  HG   sing N N 225 
LEU CD1 HD11 sing N N 226 
LEU CD1 HD12 sing N N 227 
LEU CD1 HD13 sing N N 228 
LEU CD2 HD21 sing N N 229 
LEU CD2 HD22 sing N N 230 
LEU CD2 HD23 sing N N 231 
LEU OXT HXT  sing N N 232 
LYS N   CA   sing N N 233 
LYS N   H    sing N N 234 
LYS N   H2   sing N N 235 
LYS CA  C    sing N N 236 
LYS CA  CB   sing N N 237 
LYS CA  HA   sing N N 238 
LYS C   O    doub N N 239 
LYS C   OXT  sing N N 240 
LYS CB  CG   sing N N 241 
LYS CB  HB2  sing N N 242 
LYS CB  HB3  sing N N 243 
LYS CG  CD   sing N N 244 
LYS CG  HG2  sing N N 245 
LYS CG  HG3  sing N N 246 
LYS CD  CE   sing N N 247 
LYS CD  HD2  sing N N 248 
LYS CD  HD3  sing N N 249 
LYS CE  NZ   sing N N 250 
LYS CE  HE2  sing N N 251 
LYS CE  HE3  sing N N 252 
LYS NZ  HZ1  sing N N 253 
LYS NZ  HZ2  sing N N 254 
LYS NZ  HZ3  sing N N 255 
LYS OXT HXT  sing N N 256 
MEA C1  N    sing N N 257 
MEA C1  HC1  sing N N 258 
MEA C1  HC2  sing N N 259 
MEA C1  HC3  sing N N 260 
MEA N   CA   sing N N 261 
MEA N   H    sing N N 262 
MEA CA  C    sing N N 263 
MEA CA  CB   sing N N 264 
MEA CA  HA   sing N N 265 
MEA C   O    doub N N 266 
MEA C   OXT  sing N N 267 
MEA CB  CG   sing N N 268 
MEA CB  HB1  sing N N 269 
MEA CB  HB2  sing N N 270 
MEA CG  CD1  doub Y N 271 
MEA CG  CD2  sing Y N 272 
MEA CD1 CE1  sing Y N 273 
MEA CD1 HD1  sing N N 274 
MEA CE1 CZ   doub Y N 275 
MEA CE1 HE1  sing N N 276 
MEA CZ  CE2  sing Y N 277 
MEA CZ  HZ   sing N N 278 
MEA CE2 CD2  doub Y N 279 
MEA CE2 HE2  sing N N 280 
MEA CD2 HD2  sing N N 281 
MEA OXT HXT  sing N N 282 
MET N   CA   sing N N 283 
MET N   H    sing N N 284 
MET N   H2   sing N N 285 
MET CA  C    sing N N 286 
MET CA  CB   sing N N 287 
MET CA  HA   sing N N 288 
MET C   O    doub N N 289 
MET C   OXT  sing N N 290 
MET CB  CG   sing N N 291 
MET CB  HB2  sing N N 292 
MET CB  HB3  sing N N 293 
MET CG  SD   sing N N 294 
MET CG  HG2  sing N N 295 
MET CG  HG3  sing N N 296 
MET SD  CE   sing N N 297 
MET CE  HE1  sing N N 298 
MET CE  HE2  sing N N 299 
MET CE  HE3  sing N N 300 
MET OXT HXT  sing N N 301 
PHE N   CA   sing N N 302 
PHE N   H    sing N N 303 
PHE N   H2   sing N N 304 
PHE CA  C    sing N N 305 
PHE CA  CB   sing N N 306 
PHE CA  HA   sing N N 307 
PHE C   O    doub N N 308 
PHE C   OXT  sing N N 309 
PHE CB  CG   sing N N 310 
PHE CB  HB2  sing N N 311 
PHE CB  HB3  sing N N 312 
PHE CG  CD1  doub Y N 313 
PHE CG  CD2  sing Y N 314 
PHE CD1 CE1  sing Y N 315 
PHE CD1 HD1  sing N N 316 
PHE CD2 CE2  doub Y N 317 
PHE CD2 HD2  sing N N 318 
PHE CE1 CZ   doub Y N 319 
PHE CE1 HE1  sing N N 320 
PHE CE2 CZ   sing Y N 321 
PHE CE2 HE2  sing N N 322 
PHE CZ  HZ   sing N N 323 
PHE OXT HXT  sing N N 324 
PRO N   CA   sing N N 325 
PRO N   CD   sing N N 326 
PRO N   H    sing N N 327 
PRO CA  C    sing N N 328 
PRO CA  CB   sing N N 329 
PRO CA  HA   sing N N 330 
PRO C   O    doub N N 331 
PRO C   OXT  sing N N 332 
PRO CB  CG   sing N N 333 
PRO CB  HB2  sing N N 334 
PRO CB  HB3  sing N N 335 
PRO CG  CD   sing N N 336 
PRO CG  HG2  sing N N 337 
PRO CG  HG3  sing N N 338 
PRO CD  HD2  sing N N 339 
PRO CD  HD3  sing N N 340 
PRO OXT HXT  sing N N 341 
SER N   CA   sing N N 342 
SER N   H    sing N N 343 
SER N   H2   sing N N 344 
SER CA  C    sing N N 345 
SER CA  CB   sing N N 346 
SER CA  HA   sing N N 347 
SER C   O    doub N N 348 
SER C   OXT  sing N N 349 
SER CB  OG   sing N N 350 
SER CB  HB2  sing N N 351 
SER CB  HB3  sing N N 352 
SER OG  HG   sing N N 353 
SER OXT HXT  sing N N 354 
THR N   CA   sing N N 355 
THR N   H    sing N N 356 
THR N   H2   sing N N 357 
THR CA  C    sing N N 358 
THR CA  CB   sing N N 359 
THR CA  HA   sing N N 360 
THR C   O    doub N N 361 
THR C   OXT  sing N N 362 
THR CB  OG1  sing N N 363 
THR CB  CG2  sing N N 364 
THR CB  HB   sing N N 365 
THR OG1 HG1  sing N N 366 
THR CG2 HG21 sing N N 367 
THR CG2 HG22 sing N N 368 
THR CG2 HG23 sing N N 369 
THR OXT HXT  sing N N 370 
TRP N   CA   sing N N 371 
TRP N   H    sing N N 372 
TRP N   H2   sing N N 373 
TRP CA  C    sing N N 374 
TRP CA  CB   sing N N 375 
TRP CA  HA   sing N N 376 
TRP C   O    doub N N 377 
TRP C   OXT  sing N N 378 
TRP CB  CG   sing N N 379 
TRP CB  HB2  sing N N 380 
TRP CB  HB3  sing N N 381 
TRP CG  CD1  doub Y N 382 
TRP CG  CD2  sing Y N 383 
TRP CD1 NE1  sing Y N 384 
TRP CD1 HD1  sing N N 385 
TRP CD2 CE2  doub Y N 386 
TRP CD2 CE3  sing Y N 387 
TRP NE1 CE2  sing Y N 388 
TRP NE1 HE1  sing N N 389 
TRP CE2 CZ2  sing Y N 390 
TRP CE3 CZ3  doub Y N 391 
TRP CE3 HE3  sing N N 392 
TRP CZ2 CH2  doub Y N 393 
TRP CZ2 HZ2  sing N N 394 
TRP CZ3 CH2  sing Y N 395 
TRP CZ3 HZ3  sing N N 396 
TRP CH2 HH2  sing N N 397 
TRP OXT HXT  sing N N 398 
TYR N   CA   sing N N 399 
TYR N   H    sing N N 400 
TYR N   H2   sing N N 401 
TYR CA  C    sing N N 402 
TYR CA  CB   sing N N 403 
TYR CA  HA   sing N N 404 
TYR C   O    doub N N 405 
TYR C   OXT  sing N N 406 
TYR CB  CG   sing N N 407 
TYR CB  HB2  sing N N 408 
TYR CB  HB3  sing N N 409 
TYR CG  CD1  doub Y N 410 
TYR CG  CD2  sing Y N 411 
TYR CD1 CE1  sing Y N 412 
TYR CD1 HD1  sing N N 413 
TYR CD2 CE2  doub Y N 414 
TYR CD2 HD2  sing N N 415 
TYR CE1 CZ   doub Y N 416 
TYR CE1 HE1  sing N N 417 
TYR CE2 CZ   sing Y N 418 
TYR CE2 HE2  sing N N 419 
TYR CZ  OH   sing N N 420 
TYR OH  HH   sing N N 421 
TYR OXT HXT  sing N N 422 
VAL N   CA   sing N N 423 
VAL N   H    sing N N 424 
VAL N   H2   sing N N 425 
VAL CA  C    sing N N 426 
VAL CA  CB   sing N N 427 
VAL CA  HA   sing N N 428 
VAL C   O    doub N N 429 
VAL C   OXT  sing N N 430 
VAL CB  CG1  sing N N 431 
VAL CB  CG2  sing N N 432 
VAL CB  HB   sing N N 433 
VAL CG1 HG11 sing N N 434 
VAL CG1 HG12 sing N N 435 
VAL CG1 HG13 sing N N 436 
VAL CG2 HG21 sing N N 437 
VAL CG2 HG22 sing N N 438 
VAL CG2 HG23 sing N N 439 
VAL OXT HXT  sing N N 440 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9DEN 
_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]   0.013269 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001012 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014352 
_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]   0.012921 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . HIS A 1 24  ? 36.318  20.463  1.255   1.00 94.99  ? 210 HIS B N   1 
ATOM   2    C CA  . HIS A 1 24  ? 35.083  19.696  1.153   1.00 99.80  ? 210 HIS B CA  1 
ATOM   3    C C   . HIS A 1 24  ? 33.894  20.462  1.744   1.00 102.07 ? 210 HIS B C   1 
ATOM   4    O O   . HIS A 1 24  ? 33.968  21.671  1.959   1.00 103.21 ? 210 HIS B O   1 
ATOM   5    C CB  . HIS A 1 24  ? 35.240  18.340  1.845   1.00 98.45  ? 210 HIS B CB  1 
ATOM   6    C CG  . HIS A 1 24  ? 34.717  17.192  1.039   1.00 107.45 ? 210 HIS B CG  1 
ATOM   7    N ND1 . HIS A 1 24  ? 34.439  15.958  1.586   1.00 98.86  ? 210 HIS B ND1 1 
ATOM   8    C CD2 . HIS A 1 24  ? 34.420  17.096  -0.279  1.00 105.34 ? 210 HIS B CD2 1 
ATOM   9    C CE1 . HIS A 1 24  ? 33.992  15.151  0.640   1.00 98.62  ? 210 HIS B CE1 1 
ATOM   10   N NE2 . HIS A 1 24  ? 33.970  15.817  -0.501  1.00 103.49 ? 210 HIS B NE2 1 
ATOM   11   N N   . THR A 1 25  ? 32.797  19.746  2.004   1.00 96.67  ? 211 THR B N   1 
ATOM   12   C CA  . THR A 1 25  ? 31.597  20.325  2.599   1.00 88.70  ? 211 THR B CA  1 
ATOM   13   C C   . THR A 1 25  ? 31.062  19.476  3.747   1.00 88.03  ? 211 THR B C   1 
ATOM   14   O O   . THR A 1 25  ? 29.982  19.773  4.272   1.00 81.17  ? 211 THR B O   1 
ATOM   15   C CB  . THR A 1 25  ? 30.499  20.522  1.549   1.00 90.56  ? 211 THR B CB  1 
ATOM   16   O OG1 . THR A 1 25  ? 29.312  21.007  2.186   1.00 88.21  ? 211 THR B OG1 1 
ATOM   17   C CG2 . THR A 1 25  ? 30.189  19.209  0.855   1.00 83.98  ? 211 THR B CG2 1 
ATOM   18   N N   . GLY A 1 26  ? 31.778  18.418  4.129   1.00 90.53  ? 212 GLY B N   1 
ATOM   19   C CA  . GLY A 1 26  ? 31.319  17.467  5.118   1.00 81.64  ? 212 GLY B CA  1 
ATOM   20   C C   . GLY A 1 26  ? 30.399  16.398  4.582   1.00 77.52  ? 212 GLY B C   1 
ATOM   21   O O   . GLY A 1 26  ? 30.074  15.454  5.316   1.00 76.25  ? 212 GLY B O   1 
ATOM   22   N N   . TYR A 1 27  ? 29.979  16.505  3.326   1.00 77.68  ? 213 TYR B N   1 
ATOM   23   C CA  . TYR A 1 27  ? 29.085  15.541  2.709   1.00 77.32  ? 213 TYR B CA  1 
ATOM   24   C C   . TYR A 1 27  ? 29.682  15.133  1.373   1.00 72.27  ? 213 TYR B C   1 
ATOM   25   O O   . TYR A 1 27  ? 30.081  15.992  0.581   1.00 73.56  ? 213 TYR B O   1 
ATOM   26   C CB  . TYR A 1 27  ? 27.676  16.120  2.527   1.00 78.56  ? 213 TYR B CB  1 
ATOM   27   C CG  . TYR A 1 27  ? 27.093  16.751  3.777   1.00 73.04  ? 213 TYR B CG  1 
ATOM   28   C CD1 . TYR A 1 27  ? 27.027  16.044  4.971   1.00 73.92  ? 213 TYR B CD1 1 
ATOM   29   C CD2 . TYR A 1 27  ? 26.592  18.050  3.758   1.00 75.18  ? 213 TYR B CD2 1 
ATOM   30   C CE1 . TYR A 1 27  ? 26.485  16.612  6.113   1.00 74.96  ? 213 TYR B CE1 1 
ATOM   31   C CE2 . TYR A 1 27  ? 26.050  18.628  4.897   1.00 73.88  ? 213 TYR B CE2 1 
ATOM   32   C CZ  . TYR A 1 27  ? 25.999  17.903  6.072   1.00 74.94  ? 213 TYR B CZ  1 
ATOM   33   O OH  . TYR A 1 27  ? 25.467  18.467  7.211   1.00 76.18  ? 213 TYR B OH  1 
ATOM   34   N N   . VAL A 1 28  ? 29.751  13.832  1.129   1.00 72.08  ? 214 VAL B N   1 
ATOM   35   C CA  . VAL A 1 28  ? 30.323  13.313  -0.098  1.00 72.62  ? 214 VAL B CA  1 
ATOM   36   C C   . VAL A 1 28  ? 29.190  12.936  -1.040  1.00 70.25  ? 214 VAL B C   1 
ATOM   37   O O   . VAL A 1 28  ? 28.052  12.698  -0.628  1.00 75.89  ? 214 VAL B O   1 
ATOM   38   C CB  . VAL A 1 28  ? 31.247  12.105  0.166   1.00 75.56  ? 214 VAL B CB  1 
ATOM   39   C CG1 . VAL A 1 28  ? 30.428  10.842  0.325   1.00 72.31  ? 214 VAL B CG1 1 
ATOM   40   C CG2 . VAL A 1 28  ? 32.274  11.960  -0.946  1.00 81.93  ? 214 VAL B CG2 1 
ATOM   41   N N   . GLY A 1 29  ? 29.506  12.880  -2.334  1.00 71.39  ? 215 GLY B N   1 
ATOM   42   C CA  . GLY A 1 29  ? 28.520  12.620  -3.355  1.00 70.04  ? 215 GLY B CA  1 
ATOM   43   C C   . GLY A 1 29  ? 28.499  11.170  -3.822  1.00 71.21  ? 215 GLY B C   1 
ATOM   44   O O   . GLY A 1 29  ? 29.253  10.313  -3.365  1.00 72.85  ? 215 GLY B O   1 
ATOM   45   N N   . LEU A 1 30  ? 27.586  10.912  -4.756  1.00 67.87  ? 216 LEU B N   1 
ATOM   46   C CA  . LEU A 1 30  ? 27.448  9.620   -5.410  1.00 68.01  ? 216 LEU B CA  1 
ATOM   47   C C   . LEU A 1 30  ? 27.776  9.777   -6.885  1.00 69.30  ? 216 LEU B C   1 
ATOM   48   O O   . LEU A 1 30  ? 27.307  10.714  -7.535  1.00 70.21  ? 216 LEU B O   1 
ATOM   49   C CB  . LEU A 1 30  ? 26.029  9.069   -5.249  1.00 67.58  ? 216 LEU B CB  1 
ATOM   50   C CG  . LEU A 1 30  ? 25.613  8.624   -3.849  1.00 67.98  ? 216 LEU B CG  1 
ATOM   51   C CD1 . LEU A 1 30  ? 24.114  8.411   -3.781  1.00 67.51  ? 216 LEU B CD1 1 
ATOM   52   C CD2 . LEU A 1 30  ? 26.350  7.353   -3.464  1.00 69.09  ? 216 LEU B CD2 1 
ATOM   53   N N   . LYS A 1 31  ? 28.563  8.853   -7.419  1.00 73.75  ? 217 LYS B N   1 
ATOM   54   C CA  . LYS A 1 31  ? 28.968  8.955   -8.810  1.00 76.41  ? 217 LYS B CA  1 
ATOM   55   C C   . LYS A 1 31  ? 27.830  8.560   -9.742  1.00 77.58  ? 217 LYS B C   1 
ATOM   56   O O   . LYS A 1 31  ? 27.003  7.698   -9.427  1.00 77.74  ? 217 LYS B O   1 
ATOM   57   C CB  . LYS A 1 31  ? 30.212  8.104   -9.067  1.00 73.08  ? 217 LYS B CB  1 
ATOM   58   C CG  . LYS A 1 31  ? 31.431  8.759   -8.460  1.00 78.99  ? 217 LYS B CG  1 
ATOM   59   C CD  . LYS A 1 31  ? 32.705  7.938   -8.475  1.00 83.22  ? 217 LYS B CD  1 
ATOM   60   C CE  . LYS A 1 31  ? 33.825  8.814   -7.922  1.00 96.76  ? 217 LYS B CE  1 
ATOM   61   N NZ  . LYS A 1 31  ? 35.155  8.180   -7.795  1.00 113.63 ? 217 LYS B NZ  1 
ATOM   62   N N   . ASN A 1 32  ? 27.798  9.210   -10.902 1.00 79.52  ? 218 ASN B N   1 
ATOM   63   C CA  . ASN A 1 32  ? 26.864  8.851   -11.959 1.00 69.24  ? 218 ASN B CA  1 
ATOM   64   C C   . ASN A 1 32  ? 27.341  7.554   -12.596 1.00 72.15  ? 218 ASN B C   1 
ATOM   65   O O   . ASN A 1 32  ? 28.302  7.549   -13.370 1.00 80.30  ? 218 ASN B O   1 
ATOM   66   C CB  . ASN A 1 32  ? 26.797  9.981   -12.980 1.00 75.53  ? 218 ASN B CB  1 
ATOM   67   C CG  . ASN A 1 32  ? 25.702  9.785   -14.004 1.00 82.33  ? 218 ASN B CG  1 
ATOM   68   O OD1 . ASN A 1 32  ? 25.268  8.662   -14.267 1.00 87.50  ? 218 ASN B OD1 1 
ATOM   69   N ND2 . ASN A 1 32  ? 25.251  10.882  -14.597 1.00 76.71  ? 218 ASN B ND2 1 
ATOM   70   N N   . GLN A 1 33  ? 26.657  6.450   -12.280 1.00 73.85  ? 219 GLN B N   1 
ATOM   71   C CA  . GLN A 1 33  ? 27.039  5.110   -12.731 1.00 79.22  ? 219 GLN B CA  1 
ATOM   72   C C   . GLN A 1 33  ? 25.826  4.434   -13.364 1.00 84.61  ? 219 GLN B C   1 
ATOM   73   O O   . GLN A 1 33  ? 25.166  3.600   -12.740 1.00 81.01  ? 219 GLN B O   1 
ATOM   74   C CB  . GLN A 1 33  ? 27.594  4.287   -11.578 1.00 79.47  ? 219 GLN B CB  1 
ATOM   75   C CG  . GLN A 1 33  ? 28.890  4.806   -11.005 1.00 82.48  ? 219 GLN B CG  1 
ATOM   76   C CD  . GLN A 1 33  ? 29.446  3.893   -9.936  1.00 86.26  ? 219 GLN B CD  1 
ATOM   77   O OE1 . GLN A 1 33  ? 28.713  3.109   -9.333  1.00 81.65  ? 219 GLN B OE1 1 
ATOM   78   N NE2 . GLN A 1 33  ? 30.750  3.989   -9.692  1.00 79.78  ? 219 GLN B NE2 1 
ATOM   79   N N   . GLY A 1 34  ? 25.523  4.808   -14.596 1.00 102.78 ? 220 GLY B N   1 
ATOM   80   C CA  . GLY A 1 34  ? 24.425  4.197   -15.309 1.00 99.32  ? 220 GLY B CA  1 
ATOM   81   C C   . GLY A 1 34  ? 23.138  4.962   -15.133 1.00 98.20  ? 220 GLY B C   1 
ATOM   82   O O   . GLY A 1 34  ? 23.070  6.019   -14.500 1.00 106.44 ? 220 GLY B O   1 
ATOM   83   N N   . ALA A 1 35  ? 22.080  4.409   -15.717 1.00 72.86  ? 221 ALA B N   1 
ATOM   84   C CA  . ALA A 1 35  ? 20.773  5.057   -15.680 1.00 81.44  ? 221 ALA B CA  1 
ATOM   85   C C   . ALA A 1 35  ? 20.098  4.776   -14.337 1.00 76.33  ? 221 ALA B C   1 
ATOM   86   O O   . ALA A 1 35  ? 19.068  4.106   -14.247 1.00 81.91  ? 221 ALA B O   1 
ATOM   87   C CB  . ALA A 1 35  ? 19.918  4.587   -16.849 1.00 87.95  ? 221 ALA B CB  1 
ATOM   88   N N   . THR A 1 36  ? 20.703  5.300   -13.271 1.00 71.14  ? 222 THR B N   1 
ATOM   89   C CA  . THR A 1 36  ? 20.097  5.145   -11.955 1.00 67.95  ? 222 THR B CA  1 
ATOM   90   C C   . THR A 1 36  ? 19.043  6.203   -11.669 1.00 72.73  ? 222 THR B C   1 
ATOM   91   O O   . THR A 1 36  ? 18.268  6.036   -10.720 1.00 71.79  ? 222 THR B O   1 
ATOM   92   C CB  . THR A 1 36  ? 21.159  5.164   -10.847 1.00 71.55  ? 222 THR B CB  1 
ATOM   93   O OG1 . THR A 1 36  ? 21.834  6.429   -10.830 1.00 83.89  ? 222 THR B OG1 1 
ATOM   94   C CG2 . THR A 1 36  ? 22.163  4.042   -11.049 1.00 72.32  ? 222 THR B CG2 1 
ATOM   95   N N   . CYS A 1 37  ? 18.987  7.271   -12.469 1.00 72.59  ? 223 CYS B N   1 
ATOM   96   C CA  . CYS A 1 37  ? 17.942  8.280   -12.336 1.00 69.06  ? 223 CYS B CA  1 
ATOM   97   C C   . CYS A 1 37  ? 17.873  8.838   -10.923 1.00 67.34  ? 223 CYS B C   1 
ATOM   98   O O   . CYS A 1 37  ? 18.842  9.405   -10.405 1.00 78.55  ? 223 CYS B O   1 
ATOM   99   C CB  . CYS A 1 37  ? 16.580  7.697   -12.722 1.00 72.96  ? 223 CYS B CB  1 
ATOM   100  S SG  . CYS A 1 37  ? 16.313  7.512   -14.493 1.00 70.70  ? 223 CYS B SG  1 
ATOM   101  N N   . TYR A 1 38  ? 16.708  8.677   -10.302 1.00 67.99  ? 224 TYR B N   1 
ATOM   102  C CA  . TYR A 1 38  ? 16.418  9.192   -8.972  1.00 70.02  ? 224 TYR B CA  1 
ATOM   103  C C   . TYR A 1 38  ? 17.170  8.461   -7.868  1.00 71.29  ? 224 TYR B C   1 
ATOM   104  O O   . TYR A 1 38  ? 17.107  8.894   -6.712  1.00 71.69  ? 224 TYR B O   1 
ATOM   105  C CB  . TYR A 1 38  ? 14.923  9.080   -8.722  1.00 65.12  ? 224 TYR B CB  1 
ATOM   106  C CG  . TYR A 1 38  ? 14.367  7.784   -9.259  1.00 67.30  ? 224 TYR B CG  1 
ATOM   107  C CD1 . TYR A 1 38  ? 14.524  6.598   -8.552  1.00 66.82  ? 224 TYR B CD1 1 
ATOM   108  C CD2 . TYR A 1 38  ? 13.698  7.740   -10.477 1.00 66.20  ? 224 TYR B CD2 1 
ATOM   109  C CE1 . TYR A 1 38  ? 14.026  5.406   -9.038  1.00 67.85  ? 224 TYR B CE1 1 
ATOM   110  C CE2 . TYR A 1 38  ? 13.195  6.553   -10.972 1.00 67.24  ? 224 TYR B CE2 1 
ATOM   111  C CZ  . TYR A 1 38  ? 13.361  5.387   -10.247 1.00 68.25  ? 224 TYR B CZ  1 
ATOM   112  O OH  . TYR A 1 38  ? 12.864  4.196   -10.730 1.00 69.33  ? 224 TYR B OH  1 
ATOM   113  N N   . MET A 1 39  ? 17.851  7.358   -8.187  1.00 67.22  ? 225 MET B N   1 
ATOM   114  C CA  . MET A 1 39  ? 18.433  6.514   -7.149  1.00 66.65  ? 225 MET B CA  1 
ATOM   115  C C   . MET A 1 39  ? 19.415  7.289   -6.279  1.00 66.35  ? 225 MET B C   1 
ATOM   116  O O   . MET A 1 39  ? 19.401  7.158   -5.049  1.00 66.74  ? 225 MET B O   1 
ATOM   117  C CB  . MET A 1 39  ? 19.110  5.306   -7.786  1.00 67.49  ? 225 MET B CB  1 
ATOM   118  C CG  . MET A 1 39  ? 19.829  4.424   -6.805  1.00 68.35  ? 225 MET B CG  1 
ATOM   119  S SD  . MET A 1 39  ? 20.529  2.997   -7.629  1.00 69.56  ? 225 MET B SD  1 
ATOM   120  C CE  . MET A 1 39  ? 21.351  2.223   -6.250  1.00 81.94  ? 225 MET B CE  1 
ATOM   121  N N   . ASN A 1 40  ? 20.274  8.101   -6.894  1.00 65.85  ? 226 ASN B N   1 
ATOM   122  C CA  . ASN A 1 40  ? 21.212  8.897   -6.109  1.00 65.75  ? 226 ASN B CA  1 
ATOM   123  C C   . ASN A 1 40  ? 20.477  9.870   -5.193  1.00 65.41  ? 226 ASN B C   1 
ATOM   124  O O   . ASN A 1 40  ? 20.858  10.045  -4.029  1.00 65.81  ? 226 ASN B O   1 
ATOM   125  C CB  . ASN A 1 40  ? 22.175  9.634   -7.036  1.00 68.15  ? 226 ASN B CB  1 
ATOM   126  C CG  . ASN A 1 40  ? 23.104  8.691   -7.762  1.00 66.06  ? 226 ASN B CG  1 
ATOM   127  O OD1 . ASN A 1 40  ? 23.360  7.581   -7.297  1.00 66.78  ? 226 ASN B OD1 1 
ATOM   128  N ND2 . ASN A 1 40  ? 23.605  9.118   -8.914  1.00 68.34  ? 226 ASN B ND2 1 
ATOM   129  N N   . SER A 1 41  ? 19.424  10.517  -5.699  1.00 67.47  ? 227 SER B N   1 
ATOM   130  C CA  . SER A 1 41  ? 18.665  11.444  -4.863  1.00 65.94  ? 227 SER B CA  1 
ATOM   131  C C   . SER A 1 41  ? 18.039  10.724  -3.675  1.00 65.37  ? 227 SER B C   1 
ATOM   132  O O   . SER A 1 41  ? 18.082  11.222  -2.544  1.00 65.72  ? 227 SER B O   1 
ATOM   133  C CB  . SER A 1 41  ? 17.573  12.135  -5.685  1.00 64.16  ? 227 SER B CB  1 
ATOM   134  O OG  . SER A 1 41  ? 18.109  12.953  -6.709  1.00 64.50  ? 227 SER B OG  1 
ATOM   135  N N   . LEU A 1 42  ? 17.457  9.545   -3.913  1.00 65.77  ? 228 LEU B N   1 
ATOM   136  C CA  . LEU A 1 42  ? 16.833  8.792   -2.831  1.00 66.65  ? 228 LEU B CA  1 
ATOM   137  C C   . LEU A 1 42  ? 17.860  8.333   -1.808  1.00 67.38  ? 228 LEU B C   1 
ATOM   138  O O   . LEU A 1 42  ? 17.588  8.342   -0.601  1.00 68.09  ? 228 LEU B O   1 
ATOM   139  C CB  . LEU A 1 42  ? 16.077  7.588   -3.393  1.00 67.15  ? 228 LEU B CB  1 
ATOM   140  C CG  . LEU A 1 42  ? 15.333  6.735   -2.364  1.00 68.30  ? 228 LEU B CG  1 
ATOM   141  C CD1 . LEU A 1 42  ? 14.249  7.547   -1.693  1.00 68.33  ? 228 LEU B CD1 1 
ATOM   142  C CD2 . LEU A 1 42  ? 14.755  5.488   -3.008  1.00 69.02  ? 228 LEU B CD2 1 
ATOM   143  N N   . LEU A 1 43  ? 19.039  7.915   -2.270  1.00 67.39  ? 229 LEU B N   1 
ATOM   144  C CA  . LEU A 1 43  ? 20.040  7.379   -1.355  1.00 68.27  ? 229 LEU B CA  1 
ATOM   145  C C   . LEU A 1 43  ? 20.504  8.431   -0.353  1.00 68.37  ? 229 LEU B C   1 
ATOM   146  O O   . LEU A 1 43  ? 20.638  8.141   0.842   1.00 69.35  ? 229 LEU B O   1 
ATOM   147  C CB  . LEU A 1 43  ? 21.220  6.813   -2.146  1.00 68.34  ? 229 LEU B CB  1 
ATOM   148  C CG  . LEU A 1 43  ? 20.952  5.456   -2.797  1.00 68.89  ? 229 LEU B CG  1 
ATOM   149  C CD1 . LEU A 1 43  ? 22.096  5.040   -3.703  1.00 69.01  ? 229 LEU B CD1 1 
ATOM   150  C CD2 . LEU A 1 43  ? 20.707  4.414   -1.725  1.00 70.16  ? 229 LEU B CD2 1 
ATOM   151  N N   . GLN A 1 44  ? 20.735  9.664   -0.812  1.00 67.55  ? 230 GLN B N   1 
ATOM   152  C CA  . GLN A 1 44  ? 21.123  10.722  0.115   1.00 67.84  ? 230 GLN B CA  1 
ATOM   153  C C   . GLN A 1 44  ? 19.990  11.044  1.080   1.00 69.61  ? 230 GLN B C   1 
ATOM   154  O O   . GLN A 1 44  ? 20.235  11.309  2.263   1.00 74.18  ? 230 GLN B O   1 
ATOM   155  C CB  . GLN A 1 44  ? 21.544  11.975  -0.652  1.00 67.07  ? 230 GLN B CB  1 
ATOM   156  C CG  . GLN A 1 44  ? 22.702  11.769  -1.624  1.00 71.73  ? 230 GLN B CG  1 
ATOM   157  C CD  . GLN A 1 44  ? 24.054  11.688  -0.936  1.00 67.75  ? 230 GLN B CD  1 
ATOM   158  O OE1 . GLN A 1 44  ? 24.834  10.770  -1.185  1.00 68.15  ? 230 GLN B OE1 1 
ATOM   159  N NE2 . GLN A 1 44  ? 24.341  12.656  -0.077  1.00 68.23  ? 230 GLN B NE2 1 
ATOM   160  N N   . THR A 1 45  ? 18.742  11.004  0.598   1.00 70.92  ? 231 THR B N   1 
ATOM   161  C CA  . THR A 1 45  ? 17.590  11.272  1.457   1.00 68.32  ? 231 THR B CA  1 
ATOM   162  C C   . THR A 1 45  ? 17.510  10.264  2.593   1.00 69.63  ? 231 THR B C   1 
ATOM   163  O O   . THR A 1 45  ? 17.271  10.628  3.750   1.00 70.99  ? 231 THR B O   1 
ATOM   164  C CB  . THR A 1 45  ? 16.296  11.239  0.642   1.00 67.75  ? 231 THR B CB  1 
ATOM   165  O OG1 . THR A 1 45  ? 16.318  12.265  -0.360  1.00 66.72  ? 231 THR B OG1 1 
ATOM   166  C CG2 . THR A 1 45  ? 15.093  11.441  1.553   1.00 68.52  ? 231 THR B CG2 1 
ATOM   167  N N   . LEU A 1 46  ? 17.687  8.981   2.276   1.00 70.88  ? 232 LEU B N   1 
ATOM   168  C CA  . LEU A 1 46  ? 17.691  7.964   3.320   1.00 71.33  ? 232 LEU B CA  1 
ATOM   169  C C   . LEU A 1 46  ? 18.944  8.053   4.181   1.00 74.58  ? 232 LEU B C   1 
ATOM   170  O O   . LEU A 1 46  ? 18.889  7.755   5.379   1.00 78.41  ? 232 LEU B O   1 
ATOM   171  C CB  . LEU A 1 46  ? 17.568  6.575   2.696   1.00 71.60  ? 232 LEU B CB  1 
ATOM   172  C CG  . LEU A 1 46  ? 16.299  6.324   1.881   1.00 71.21  ? 232 LEU B CG  1 
ATOM   173  C CD1 . LEU A 1 46  ? 16.405  5.000   1.148   1.00 73.42  ? 232 LEU B CD1 1 
ATOM   174  C CD2 . LEU A 1 46  ? 15.059  6.353   2.768   1.00 72.15  ? 232 LEU B CD2 1 
ATOM   175  N N   . PHE A 1 47  ? 20.075  8.454   3.589   1.00 74.97  ? 233 PHE B N   1 
ATOM   176  C CA  . PHE A 1 47  ? 21.320  8.570   4.347   1.00 74.34  ? 233 PHE B CA  1 
ATOM   177  C C   . PHE A 1 47  ? 21.202  9.605   5.455   1.00 74.79  ? 233 PHE B C   1 
ATOM   178  O O   . PHE A 1 47  ? 21.665  9.376   6.579   1.00 74.37  ? 233 PHE B O   1 
ATOM   179  C CB  . PHE A 1 47  ? 22.475  8.924   3.410   1.00 73.77  ? 233 PHE B CB  1 
ATOM   180  C CG  . PHE A 1 47  ? 23.757  9.268   4.122   1.00 73.25  ? 233 PHE B CG  1 
ATOM   181  C CD1 . PHE A 1 47  ? 24.617  8.271   4.551   1.00 76.24  ? 233 PHE B CD1 1 
ATOM   182  C CD2 . PHE A 1 47  ? 24.110  10.591  4.345   1.00 72.27  ? 233 PHE B CD2 1 
ATOM   183  C CE1 . PHE A 1 47  ? 25.799  8.585   5.200   1.00 76.07  ? 233 PHE B CE1 1 
ATOM   184  C CE2 . PHE A 1 47  ? 25.287  10.910  4.993   1.00 74.24  ? 233 PHE B CE2 1 
ATOM   185  C CZ  . PHE A 1 47  ? 26.134  9.906   5.421   1.00 77.60  ? 233 PHE B CZ  1 
ATOM   186  N N   . PHE A 1 48  ? 20.593  10.751  5.160   1.00 72.15  ? 234 PHE B N   1 
ATOM   187  C CA  . PHE A 1 48  ? 20.411  11.793  6.159   1.00 74.51  ? 234 PHE B CA  1 
ATOM   188  C C   . PHE A 1 48  ? 19.128  11.624  6.956   1.00 74.34  ? 234 PHE B C   1 
ATOM   189  O O   . PHE A 1 48  ? 18.797  12.497  7.763   1.00 78.73  ? 234 PHE B O   1 
ATOM   190  C CB  . PHE A 1 48  ? 20.458  13.174  5.507   1.00 71.98  ? 234 PHE B CB  1 
ATOM   191  C CG  . PHE A 1 48  ? 21.821  13.547  5.011   1.00 71.70  ? 234 PHE B CG  1 
ATOM   192  C CD1 . PHE A 1 48  ? 22.871  13.705  5.900   1.00 76.16  ? 234 PHE B CD1 1 
ATOM   193  C CD2 . PHE A 1 48  ? 22.060  13.727  3.662   1.00 71.58  ? 234 PHE B CD2 1 
ATOM   194  C CE1 . PHE A 1 48  ? 24.136  14.047  5.455   1.00 72.91  ? 234 PHE B CE1 1 
ATOM   195  C CE2 . PHE A 1 48  ? 23.324  14.066  3.208   1.00 77.64  ? 234 PHE B CE2 1 
ATOM   196  C CZ  . PHE A 1 48  ? 24.363  14.224  4.107   1.00 71.59  ? 234 PHE B CZ  1 
ATOM   197  N N   . THR A 1 49  ? 18.390  10.536  6.732   1.00 75.68  ? 235 THR B N   1 
ATOM   198  C CA  . THR A 1 49  ? 17.432  10.044  7.717   1.00 77.01  ? 235 THR B CA  1 
ATOM   199  C C   . THR A 1 49  ? 18.265  9.306   8.761   1.00 76.77  ? 235 THR B C   1 
ATOM   200  O O   . THR A 1 49  ? 18.336  8.075   8.794   1.00 77.36  ? 235 THR B O   1 
ATOM   201  C CB  . THR A 1 49  ? 16.383  9.146   7.071   1.00 80.53  ? 235 THR B CB  1 
ATOM   202  O OG1 . THR A 1 49  ? 15.806  9.816   5.943   1.00 84.86  ? 235 THR B OG1 1 
ATOM   203  C CG2 . THR A 1 49  ? 15.276  8.818   8.065   1.00 76.36  ? 235 THR B CG2 1 
ATOM   204  N N   . ASN A 1 50  ? 18.909  10.099  9.629   1.00 78.67  ? 236 ASN B N   1 
ATOM   205  C CA  . ASN A 1 50  ? 20.016  9.603   10.447  1.00 79.06  ? 236 ASN B CA  1 
ATOM   206  C C   . ASN A 1 50  ? 19.601  8.414   11.299  1.00 80.75  ? 236 ASN B C   1 
ATOM   207  O O   . ASN A 1 50  ? 20.370  7.458   11.456  1.00 81.48  ? 236 ASN B O   1 
ATOM   208  C CB  . ASN A 1 50  ? 20.553  10.720  11.344  1.00 80.09  ? 236 ASN B CB  1 
ATOM   209  C CG  . ASN A 1 50  ? 21.293  11.791  10.570  1.00 80.87  ? 236 ASN B CG  1 
ATOM   210  O OD1 . ASN A 1 50  ? 21.034  12.018  9.387   1.00 79.91  ? 236 ASN B OD1 1 
ATOM   211  N ND2 . ASN A 1 50  ? 22.221  12.462  11.240  1.00 83.63  ? 236 ASN B ND2 1 
ATOM   212  N N   . GLN A 1 51  ? 18.391  8.460   11.864  1.00 81.56  ? 237 GLN B N   1 
ATOM   213  C CA  . GLN A 1 51  ? 17.900  7.346   12.668  1.00 83.38  ? 237 GLN B CA  1 
ATOM   214  C C   . GLN A 1 51  ? 17.763  6.079   11.831  1.00 82.81  ? 237 GLN B C   1 
ATOM   215  O O   . GLN A 1 51  ? 18.043  4.975   12.312  1.00 84.25  ? 237 GLN B O   1 
ATOM   216  C CB  . GLN A 1 51  ? 16.569  7.718   13.314  1.00 84.36  ? 237 GLN B CB  1 
ATOM   217  C CG  . GLN A 1 51  ? 16.077  6.705   14.321  1.00 86.67  ? 237 GLN B CG  1 
ATOM   218  C CD  . GLN A 1 51  ? 14.945  7.239   15.165  1.00 88.08  ? 237 GLN B CD  1 
ATOM   219  O OE1 . GLN A 1 51  ? 14.432  8.330   14.915  1.00 87.25  ? 237 GLN B OE1 1 
ATOM   220  N NE2 . GLN A 1 51  ? 14.555  6.479   16.180  1.00 90.46  ? 237 GLN B NE2 1 
ATOM   221  N N   . LEU A 1 52  ? 17.310  6.213   10.582  1.00 80.92  ? 238 LEU B N   1 
ATOM   222  C CA  . LEU A 1 52  ? 17.299  5.065   9.681   1.00 80.42  ? 238 LEU B CA  1 
ATOM   223  C C   . LEU A 1 52  ? 18.710  4.561   9.426   1.00 80.34  ? 238 LEU B C   1 
ATOM   224  O O   . LEU A 1 52  ? 18.946  3.349   9.361   1.00 81.18  ? 238 LEU B O   1 
ATOM   225  C CB  . LEU A 1 52  ? 16.625  5.434   8.361   1.00 78.51  ? 238 LEU B CB  1 
ATOM   226  C CG  . LEU A 1 52  ? 16.834  4.463   7.200   1.00 77.77  ? 238 LEU B CG  1 
ATOM   227  C CD1 . LEU A 1 52  ? 16.240  3.101   7.528   1.00 79.38  ? 238 LEU B CD1 1 
ATOM   228  C CD2 . LEU A 1 52  ? 16.214  5.027   5.936   1.00 76.00  ? 238 LEU B CD2 1 
ATOM   229  N N   . ARG A 1 53  ? 19.662  5.484   9.285   1.00 79.51  ? 239 ARG B N   1 
ATOM   230  C CA  . ARG A 1 53  ? 21.033  5.099   8.968   1.00 79.80  ? 239 ARG B CA  1 
ATOM   231  C C   . ARG A 1 53  ? 21.644  4.251   10.078  1.00 84.47  ? 239 ARG B C   1 
ATOM   232  O O   . ARG A 1 53  ? 22.228  3.194   9.813   1.00 87.10  ? 239 ARG B O   1 
ATOM   233  C CB  . ARG A 1 53  ? 21.877  6.348   8.707   1.00 78.44  ? 239 ARG B CB  1 
ATOM   234  C CG  . ARG A 1 53  ? 23.379  6.090   8.733   1.00 78.95  ? 239 ARG B CG  1 
ATOM   235  C CD  . ARG A 1 53  ? 24.120  6.954   7.733   1.00 77.44  ? 239 ARG B CD  1 
ATOM   236  N NE  . ARG A 1 53  ? 23.901  8.379   7.952   1.00 76.98  ? 239 ARG B NE  1 
ATOM   237  C CZ  . ARG A 1 53  ? 24.809  9.215   8.436   1.00 77.58  ? 239 ARG B CZ  1 
ATOM   238  N NH1 . ARG A 1 53  ? 26.016  8.800   8.785   1.00 79.28  ? 239 ARG B NH1 1 
ATOM   239  N NH2 . ARG A 1 53  ? 24.498  10.502  8.573   1.00 77.26  ? 239 ARG B NH2 1 
ATOM   240  N N   . LYS A 1 54  ? 21.519  4.697   11.332  1.00 83.04  ? 240 LYS B N   1 
ATOM   241  C CA  . LYS A 1 54  ? 22.094  3.938   12.440  1.00 85.32  ? 240 LYS B CA  1 
ATOM   242  C C   . LYS A 1 54  ? 21.437  2.569   12.569  1.00 87.74  ? 240 LYS B C   1 
ATOM   243  O O   . LYS A 1 54  ? 22.102  1.586   12.922  1.00 89.02  ? 240 LYS B O   1 
ATOM   244  C CB  . LYS A 1 54  ? 21.977  4.730   13.743  1.00 86.84  ? 240 LYS B CB  1 
ATOM   245  C CG  . LYS A 1 54  ? 22.875  5.961   13.791  1.00 86.32  ? 240 LYS B CG  1 
ATOM   246  C CD  . LYS A 1 54  ? 22.603  6.839   15.012  1.00 87.88  ? 240 LYS B CD  1 
ATOM   247  C CE  . LYS A 1 54  ? 23.109  6.210   16.304  1.00 90.62  ? 240 LYS B CE  1 
ATOM   248  N NZ  . LYS A 1 54  ? 22.874  7.097   17.484  1.00 92.35  ? 240 LYS B NZ  1 
ATOM   249  N N   . ALA A 1 55  ? 20.134  2.482   12.284  1.00 86.06  ? 241 ALA B N   1 
ATOM   250  C CA  . ALA A 1 55  ? 19.468  1.183   12.275  1.00 87.21  ? 241 ALA B CA  1 
ATOM   251  C C   . ALA A 1 55  ? 20.048  0.276   11.197  1.00 93.96  ? 241 ALA B C   1 
ATOM   252  O O   . ALA A 1 55  ? 20.234  -0.926  11.418  1.00 101.29 ? 241 ALA B O   1 
ATOM   253  C CB  . ALA A 1 55  ? 17.965  1.360   12.070  1.00 86.85  ? 241 ALA B CB  1 
ATOM   254  N N   . VAL A 1 56  ? 20.341  0.838   10.022  1.00 89.57  ? 242 VAL B N   1 
ATOM   255  C CA  . VAL A 1 56  ? 20.928  0.058   8.934   1.00 92.38  ? 242 VAL B CA  1 
ATOM   256  C C   . VAL A 1 56  ? 22.309  -0.470  9.315   1.00 91.12  ? 242 VAL B C   1 
ATOM   257  O O   . VAL A 1 56  ? 22.645  -1.624  9.027   1.00 91.28  ? 242 VAL B O   1 
ATOM   258  C CB  . VAL A 1 56  ? 20.970  0.905   7.649   1.00 88.39  ? 242 VAL B CB  1 
ATOM   259  C CG1 . VAL A 1 56  ? 21.795  0.216   6.580   1.00 85.72  ? 242 VAL B CG1 1 
ATOM   260  C CG2 . VAL A 1 56  ? 19.557  1.159   7.155   1.00 81.36  ? 242 VAL B CG2 1 
ATOM   261  N N   . TYR A 1 57  ? 23.121  0.355   9.984   1.00 95.16  ? 243 TYR B N   1 
ATOM   262  C CA  . TYR A 1 57  ? 24.457  -0.076  10.391  1.00 91.48  ? 243 TYR B CA  1 
ATOM   263  C C   . TYR A 1 57  ? 24.408  -1.253  11.356  1.00 104.50 ? 243 TYR B C   1 
ATOM   264  O O   . TYR A 1 57  ? 25.299  -2.116  11.331  1.00 100.53 ? 243 TYR B O   1 
ATOM   265  C CB  . TYR A 1 57  ? 25.213  1.079   11.043  1.00 86.24  ? 243 TYR B CB  1 
ATOM   266  C CG  . TYR A 1 57  ? 25.750  2.095   10.076  1.00 84.21  ? 243 TYR B CG  1 
ATOM   267  C CD1 . TYR A 1 57  ? 26.050  1.742   8.768   1.00 82.90  ? 243 TYR B CD1 1 
ATOM   268  C CD2 . TYR A 1 57  ? 25.962  3.409   10.467  1.00 83.80  ? 243 TYR B CD2 1 
ATOM   269  C CE1 . TYR A 1 57  ? 26.549  2.673   7.874   1.00 81.24  ? 243 TYR B CE1 1 
ATOM   270  C CE2 . TYR A 1 57  ? 26.458  4.348   9.584   1.00 82.15  ? 243 TYR B CE2 1 
ATOM   271  C CZ  . TYR A 1 57  ? 26.750  3.973   8.287   1.00 80.87  ? 243 TYR B CZ  1 
ATOM   272  O OH  . TYR A 1 57  ? 27.244  4.908   7.409   1.00 79.42  ? 243 TYR B OH  1 
ATOM   273  N N   . MET A 1 58  ? 23.385  -1.315  12.212  1.00 100.41 ? 244 MET B N   1 
ATOM   274  C CA  . MET A 1 58  ? 23.323  -2.330  13.258  1.00 105.43 ? 244 MET B CA  1 
ATOM   275  C C   . MET A 1 58  ? 22.493  -3.538  12.857  1.00 102.33 ? 244 MET B C   1 
ATOM   276  O O   . MET A 1 58  ? 22.069  -4.309  13.725  1.00 98.94  ? 244 MET B O   1 
ATOM   277  C CB  . MET A 1 58  ? 22.807  -1.713  14.559  1.00 104.03 ? 244 MET B CB  1 
ATOM   278  C CG  . MET A 1 58  ? 23.735  -0.650  15.127  1.00 104.76 ? 244 MET B CG  1 
ATOM   279  S SD  . MET A 1 58  ? 23.242  -0.129  16.772  1.00 134.82 ? 244 MET B SD  1 
ATOM   280  C CE  . MET A 1 58  ? 21.607  0.507   16.392  1.00 113.92 ? 244 MET B CE  1 
ATOM   281  N N   . MET A 1 59  ? 22.248  -3.710  11.551  1.00 102.00 ? 245 MET B N   1 
ATOM   282  C CA  . MET A 1 59  ? 21.493  -4.863  11.103  1.00 106.21 ? 245 MET B CA  1 
ATOM   283  C C   . MET A 1 59  ? 22.385  -6.100  11.130  1.00 103.57 ? 245 MET B C   1 
ATOM   284  O O   . MET A 1 59  ? 23.585  -6.009  10.863  1.00 104.16 ? 245 MET B O   1 
ATOM   285  C CB  . MET A 1 59  ? 20.968  -4.650  9.687   1.00 102.59 ? 245 MET B CB  1 
ATOM   286  C CG  . MET A 1 59  ? 19.978  -3.523  9.529   1.00 96.73  ? 245 MET B CG  1 
ATOM   287  S SD  . MET A 1 59  ? 19.397  -3.471  7.826   1.00 102.56 ? 245 MET B SD  1 
ATOM   288  C CE  . MET A 1 59  ? 20.936  -3.268  6.935   1.00 90.82  ? 245 MET B CE  1 
ATOM   289  N N   . PRO A 1 60  ? 21.821  -7.266  11.421  1.00 105.88 ? 246 PRO B N   1 
ATOM   290  C CA  . PRO A 1 60  ? 22.620  -8.508  11.445  1.00 110.92 ? 246 PRO B CA  1 
ATOM   291  C C   . PRO A 1 60  ? 22.883  -9.052  10.045  1.00 115.58 ? 246 PRO B C   1 
ATOM   292  O O   . PRO A 1 60  ? 22.308  -10.056 9.602   1.00 118.01 ? 246 PRO B O   1 
ATOM   293  C CB  . PRO A 1 60  ? 21.739  -9.442  12.280  1.00 109.32 ? 246 PRO B CB  1 
ATOM   294  C CG  . PRO A 1 60  ? 20.352  -9.020  11.907  1.00 111.62 ? 246 PRO B CG  1 
ATOM   295  C CD  . PRO A 1 60  ? 20.407  -7.517  11.749  1.00 108.28 ? 246 PRO B CD  1 
ATOM   296  N N   . THR A 1 61  ? 23.778  -8.390  9.313   1.00 116.34 ? 247 THR B N   1 
ATOM   297  C CA  . THR A 1 61  ? 24.095  -8.803  7.952   1.00 120.79 ? 247 THR B CA  1 
ATOM   298  C C   . THR A 1 61  ? 25.398  -9.598  7.855   1.00 130.37 ? 247 THR B C   1 
ATOM   299  O O   . THR A 1 61  ? 25.877  -9.843  6.743   1.00 131.20 ? 247 THR B O   1 
ATOM   300  C CB  . THR A 1 61  ? 24.162  -7.586  7.019   1.00 109.34 ? 247 THR B CB  1 
ATOM   301  O OG1 . THR A 1 61  ? 25.078  -6.618  7.548   1.00 105.94 ? 247 THR B OG1 1 
ATOM   302  C CG2 . THR A 1 61  ? 22.788  -6.945  6.871   1.00 105.35 ? 247 THR B CG2 1 
ATOM   303  N N   . GLU A 1 62  ? 25.992  -9.992  8.983   1.00 147.82 ? 248 GLU B N   1 
ATOM   304  C CA  . GLU A 1 62  ? 27.184  -10.833 8.921   1.00 154.05 ? 248 GLU B CA  1 
ATOM   305  C C   . GLU A 1 62  ? 26.831  -12.194 8.333   1.00 141.13 ? 248 GLU B C   1 
ATOM   306  O O   . GLU A 1 62  ? 25.830  -12.808 8.712   1.00 145.84 ? 248 GLU B O   1 
ATOM   307  C CB  . GLU A 1 62  ? 27.832  -10.999 10.301  1.00 161.58 ? 248 GLU B CB  1 
ATOM   308  C CG  . GLU A 1 62  ? 28.277  -9.709  10.994  1.00 171.73 ? 248 GLU B CG  1 
ATOM   309  C CD  . GLU A 1 62  ? 27.170  -8.996  11.745  1.00 165.90 ? 248 GLU B CD  1 
ATOM   310  O OE1 . GLU A 1 62  ? 25.991  -9.375  11.582  1.00 154.00 ? 248 GLU B OE1 1 
ATOM   311  O OE2 . GLU A 1 62  ? 27.489  -8.065  12.519  1.00 168.68 ? 248 GLU B OE2 1 
ATOM   312  N N   . GLY A 1 63  ? 27.657  -12.659 7.402   1.00 123.84 ? 249 GLY B N   1 
ATOM   313  C CA  . GLY A 1 63  ? 27.391  -13.913 6.728   1.00 118.38 ? 249 GLY B CA  1 
ATOM   314  C C   . GLY A 1 63  ? 26.392  -13.845 5.595   1.00 101.41 ? 249 GLY B C   1 
ATOM   315  O O   . GLY A 1 63  ? 25.717  -14.843 5.317   1.00 103.02 ? 249 GLY B O   1 
ATOM   316  N N   . ASP A 1 64  ? 26.270  -12.699 4.934   1.00 98.77  ? 250 ASP B N   1 
ATOM   317  C CA  . ASP A 1 64  ? 25.396  -12.547 3.778   1.00 102.48 ? 250 ASP B CA  1 
ATOM   318  C C   . ASP A 1 64  ? 26.223  -12.550 2.497   1.00 102.42 ? 250 ASP B C   1 
ATOM   319  O O   . ASP A 1 64  ? 27.425  -12.281 2.509   1.00 113.70 ? 250 ASP B O   1 
ATOM   320  C CB  . ASP A 1 64  ? 24.573  -11.255 3.868   1.00 109.95 ? 250 ASP B CB  1 
ATOM   321  C CG  . ASP A 1 64  ? 23.601  -11.252 5.038   1.00 112.47 ? 250 ASP B CG  1 
ATOM   322  O OD1 . ASP A 1 64  ? 23.776  -12.053 5.983   1.00 117.40 ? 250 ASP B OD1 1 
ATOM   323  O OD2 . ASP A 1 64  ? 22.654  -10.438 5.008   1.00 102.45 ? 250 ASP B OD2 1 
ATOM   324  N N   . ASP A 1 65  ? 25.562  -12.846 1.381   1.00 100.75 ? 251 ASP B N   1 
ATOM   325  C CA  . ASP A 1 65  ? 26.252  -12.897 0.097   1.00 104.61 ? 251 ASP B CA  1 
ATOM   326  C C   . ASP A 1 65  ? 26.314  -11.500 -0.510  1.00 107.60 ? 251 ASP B C   1 
ATOM   327  O O   . ASP A 1 65  ? 25.277  -10.866 -0.737  1.00 108.89 ? 251 ASP B O   1 
ATOM   328  C CB  . ASP A 1 65  ? 25.558  -13.872 -0.852  1.00 102.49 ? 251 ASP B CB  1 
ATOM   329  C CG  . ASP A 1 65  ? 26.035  -13.725 -2.286  1.00 108.74 ? 251 ASP B CG  1 
ATOM   330  O OD1 . ASP A 1 65  ? 27.227  -13.999 -2.557  1.00 110.03 ? 251 ASP B OD1 1 
ATOM   331  O OD2 . ASP A 1 65  ? 25.214  -13.330 -3.140  1.00 113.71 ? 251 ASP B OD2 1 
ATOM   332  N N   . SER A 1 66  ? 27.535  -11.024 -0.770  1.00 109.50 ? 252 SER B N   1 
ATOM   333  C CA  . SER A 1 66  ? 27.715  -9.659  -1.255  1.00 102.90 ? 252 SER B CA  1 
ATOM   334  C C   . SER A 1 66  ? 27.023  -9.446  -2.593  1.00 111.25 ? 252 SER B C   1 
ATOM   335  O O   . SER A 1 66  ? 26.472  -8.370  -2.849  1.00 118.91 ? 252 SER B O   1 
ATOM   336  C CB  . SER A 1 66  ? 29.202  -9.328  -1.370  1.00 109.33 ? 252 SER B CB  1 
ATOM   337  O OG  . SER A 1 66  ? 29.389  -8.144  -2.126  1.00 105.29 ? 252 SER B OG  1 
ATOM   338  N N   . SER A 1 67  ? 27.025  -10.466 -3.453  1.00 108.90 ? 253 SER B N   1 
ATOM   339  C CA  . SER A 1 67  ? 26.504  -10.306 -4.805  1.00 111.07 ? 253 SER B CA  1 
ATOM   340  C C   . SER A 1 67  ? 24.987  -10.149 -4.850  1.00 111.96 ? 253 SER B C   1 
ATOM   341  O O   . SER A 1 67  ? 24.459  -9.699  -5.875  1.00 114.91 ? 253 SER B O   1 
ATOM   342  C CB  . SER A 1 67  ? 26.934  -11.499 -5.664  1.00 108.48 ? 253 SER B CB  1 
ATOM   343  O OG  . SER A 1 67  ? 26.205  -12.664 -5.320  1.00 106.86 ? 253 SER B OG  1 
ATOM   344  N N   . LYS A 1 68  ? 24.270  -10.519 -3.785  1.00 106.83 ? 254 LYS B N   1 
ATOM   345  C CA  . LYS A 1 68  ? 22.816  -10.508 -3.827  1.00 107.09 ? 254 LYS B CA  1 
ATOM   346  C C   . LYS A 1 68  ? 22.141  -9.864  -2.620  1.00 109.38 ? 254 LYS B C   1 
ATOM   347  O O   . LYS A 1 68  ? 20.908  -9.898  -2.544  1.00 107.03 ? 254 LYS B O   1 
ATOM   348  C CB  . LYS A 1 68  ? 22.293  -11.947 -3.987  1.00 110.13 ? 254 LYS B CB  1 
ATOM   349  C CG  . LYS A 1 68  ? 22.740  -12.624 -5.275  1.00 105.17 ? 254 LYS B CG  1 
ATOM   350  C CD  . LYS A 1 68  ? 22.205  -14.042 -5.376  1.00 107.34 ? 254 LYS B CD  1 
ATOM   351  C CE  . LYS A 1 68  ? 22.660  -14.705 -6.665  1.00 98.86  ? 254 LYS B CE  1 
ATOM   352  N NZ  . LYS A 1 68  ? 22.126  -16.088 -6.795  1.00 100.31 ? 254 LYS B NZ  1 
ATOM   353  N N   . SER A 1 69  ? 22.892  -9.278  -1.684  1.00 109.37 ? 255 SER B N   1 
ATOM   354  C CA  . SER A 1 69  ? 22.329  -8.750  -0.440  1.00 104.88 ? 255 SER B CA  1 
ATOM   355  C C   . SER A 1 69  ? 22.078  -7.248  -0.551  1.00 98.70  ? 255 SER B C   1 
ATOM   356  O O   . SER A 1 69  ? 23.025  -6.456  -0.627  1.00 101.34 ? 255 SER B O   1 
ATOM   357  C CB  . SER A 1 69  ? 23.251  -9.050  0.741   1.00 104.82 ? 255 SER B CB  1 
ATOM   358  O OG  . SER A 1 69  ? 22.711  -8.552  1.953   1.00 97.20  ? 255 SER B OG  1 
ATOM   359  N N   . VAL A 1 70  ? 20.805  -6.863  -0.568  1.00 95.53  ? 256 VAL B N   1 
ATOM   360  C CA  . VAL A 1 70  ? 20.403  -5.457  -0.524  1.00 95.23  ? 256 VAL B CA  1 
ATOM   361  C C   . VAL A 1 70  ? 20.758  -4.808  0.814   1.00 96.93  ? 256 VAL B C   1 
ATOM   362  O O   . VAL A 1 70  ? 21.290  -3.689  0.811   1.00 100.10 ? 256 VAL B O   1 
ATOM   363  C CB  . VAL A 1 70  ? 18.905  -5.297  -0.837  1.00 89.50  ? 256 VAL B CB  1 
ATOM   364  C CG1 . VAL A 1 70  ? 18.512  -3.830  -0.793  1.00 92.00  ? 256 VAL B CG1 1 
ATOM   365  C CG2 . VAL A 1 70  ? 18.587  -5.887  -2.200  1.00 87.75  ? 256 VAL B CG2 1 
ATOM   366  N N   . PRO A 1 71  ? 20.481  -5.429  1.976   1.00 91.90  ? 257 PRO B N   1 
ATOM   367  C CA  . PRO A 1 71  ? 20.920  -4.798  3.236   1.00 88.28  ? 257 PRO B CA  1 
ATOM   368  C C   . PRO A 1 71  ? 22.421  -4.572  3.313   1.00 94.15  ? 257 PRO B C   1 
ATOM   369  O O   . PRO A 1 71  ? 22.859  -3.536  3.828   1.00 92.90  ? 257 PRO B O   1 
ATOM   370  C CB  . PRO A 1 71  ? 20.427  -5.780  4.307   1.00 95.38  ? 257 PRO B CB  1 
ATOM   371  C CG  . PRO A 1 71  ? 19.269  -6.454  3.683   1.00 96.05  ? 257 PRO B CG  1 
ATOM   372  C CD  . PRO A 1 71  ? 19.653  -6.619  2.241   1.00 95.35  ? 257 PRO B CD  1 
ATOM   373  N N   . LEU A 1 72  ? 23.228  -5.509  2.810   1.00 96.24  ? 258 LEU B N   1 
ATOM   374  C CA  . LEU A 1 72  ? 24.670  -5.294  2.800   1.00 87.33  ? 258 LEU B CA  1 
ATOM   375  C C   . LEU A 1 72  ? 25.046  -4.164  1.854   1.00 84.20  ? 258 LEU B C   1 
ATOM   376  O O   . LEU A 1 72  ? 25.911  -3.339  2.173   1.00 82.62  ? 258 LEU B O   1 
ATOM   377  C CB  . LEU A 1 72  ? 25.399  -6.574  2.401   1.00 91.39  ? 258 LEU B CB  1 
ATOM   378  C CG  . LEU A 1 72  ? 26.923  -6.433  2.390   1.00 96.31  ? 258 LEU B CG  1 
ATOM   379  C CD1 . LEU A 1 72  ? 27.434  -6.135  3.788   1.00 96.26  ? 258 LEU B CD1 1 
ATOM   380  C CD2 . LEU A 1 72  ? 27.595  -7.671  1.814   1.00 102.00 ? 258 LEU B CD2 1 
ATOM   381  N N   . ALA A 1 73  ? 24.401  -4.113  0.685   1.00 82.83  ? 259 ALA B N   1 
ATOM   382  C CA  . ALA A 1 73  ? 24.698  -3.062  -0.280  1.00 83.21  ? 259 ALA B CA  1 
ATOM   383  C C   . ALA A 1 73  ? 24.363  -1.688  0.284   1.00 85.01  ? 259 ALA B C   1 
ATOM   384  O O   . ALA A 1 73  ? 25.143  -0.739  0.127   1.00 86.71  ? 259 ALA B O   1 
ATOM   385  C CB  . ALA A 1 73  ? 23.938  -3.317  -1.581  1.00 78.86  ? 259 ALA B CB  1 
ATOM   386  N N   . LEU A 1 74  ? 23.213  -1.563  0.957   1.00 81.45  ? 260 LEU B N   1 
ATOM   387  C CA  . LEU A 1 74  ? 22.847  -0.287  1.568   1.00 80.94  ? 260 LEU B CA  1 
ATOM   388  C C   . LEU A 1 74  ? 23.803  0.083   2.697   1.00 83.32  ? 260 LEU B C   1 
ATOM   389  O O   . LEU A 1 74  ? 24.117  1.264   2.889   1.00 82.17  ? 260 LEU B O   1 
ATOM   390  C CB  . LEU A 1 74  ? 21.409  -0.331  2.088   1.00 83.48  ? 260 LEU B CB  1 
ATOM   391  C CG  . LEU A 1 74  ? 20.877  1.032   2.548   1.00 76.03  ? 260 LEU B CG  1 
ATOM   392  C CD1 . LEU A 1 74  ? 20.749  1.988   1.369   1.00 78.44  ? 260 LEU B CD1 1 
ATOM   393  C CD2 . LEU A 1 74  ? 19.560  0.906   3.280   1.00 76.73  ? 260 LEU B CD2 1 
ATOM   394  N N   . GLN A 1 75  ? 24.258  -0.908  3.467   1.00 86.74  ? 261 GLN B N   1 
ATOM   395  C CA  . GLN A 1 75  ? 25.285  -0.648  4.472   1.00 81.24  ? 261 GLN B CA  1 
ATOM   396  C C   . GLN A 1 75  ? 26.567  -0.148  3.825   1.00 79.57  ? 261 GLN B C   1 
ATOM   397  O O   . GLN A 1 75  ? 27.200  0.794   4.318   1.00 79.36  ? 261 GLN B O   1 
ATOM   398  C CB  . GLN A 1 75  ? 25.562  -1.918  5.271   1.00 82.46  ? 261 GLN B CB  1 
ATOM   399  C CG  . GLN A 1 75  ? 24.458  -2.302  6.223   1.00 85.06  ? 261 GLN B CG  1 
ATOM   400  C CD  . GLN A 1 75  ? 24.624  -3.710  6.745   1.00 93.41  ? 261 GLN B CD  1 
ATOM   401  O OE1 . GLN A 1 75  ? 25.054  -4.607  6.014   1.00 89.21  ? 261 GLN B OE1 1 
ATOM   402  N NE2 . GLN A 1 75  ? 24.272  -3.918  8.010   1.00 98.10  ? 261 GLN B NE2 1 
ATOM   403  N N   . ARG A 1 76  ? 26.964  -0.770  2.715   1.00 79.43  ? 262 ARG B N   1 
ATOM   404  C CA  . ARG A 1 76  ? 28.197  -0.378  2.050   1.00 79.05  ? 262 ARG B CA  1 
ATOM   405  C C   . ARG A 1 76  ? 28.124  1.061   1.565   1.00 78.33  ? 262 ARG B C   1 
ATOM   406  O O   . ARG A 1 76  ? 29.055  1.847   1.774   1.00 84.80  ? 262 ARG B O   1 
ATOM   407  C CB  . ARG A 1 76  ? 28.483  -1.318  0.886   1.00 79.36  ? 262 ARG B CB  1 
ATOM   408  C CG  . ARG A 1 76  ? 29.837  -1.104  0.268   1.00 79.45  ? 262 ARG B CG  1 
ATOM   409  C CD  . ARG A 1 76  ? 30.040  -2.026  -0.913  1.00 79.91  ? 262 ARG B CD  1 
ATOM   410  N NE  . ARG A 1 76  ? 29.847  -3.426  -0.557  1.00 81.63  ? 262 ARG B NE  1 
ATOM   411  C CZ  . ARG A 1 76  ? 28.776  -4.140  -0.877  1.00 81.81  ? 262 ARG B CZ  1 
ATOM   412  N NH1 . ARG A 1 76  ? 27.775  -3.612  -1.564  1.00 83.34  ? 262 ARG B NH1 1 
ATOM   413  N NH2 . ARG A 1 76  ? 28.712  -5.415  -0.506  1.00 89.27  ? 262 ARG B NH2 1 
ATOM   414  N N   . VAL A 1 77  ? 27.016  1.428   0.918   1.00 75.98  ? 263 VAL B N   1 
ATOM   415  C CA  . VAL A 1 77  ? 26.916  2.771   0.358   1.00 75.43  ? 263 VAL B CA  1 
ATOM   416  C C   . VAL A 1 77  ? 26.819  3.811   1.469   1.00 75.36  ? 263 VAL B C   1 
ATOM   417  O O   . VAL A 1 77  ? 27.403  4.897   1.369   1.00 76.41  ? 263 VAL B O   1 
ATOM   418  C CB  . VAL A 1 77  ? 25.737  2.856   -0.632  1.00 73.25  ? 263 VAL B CB  1 
ATOM   419  C CG1 . VAL A 1 77  ? 24.445  2.483   0.034   1.00 76.90  ? 263 VAL B CG1 1 
ATOM   420  C CG2 . VAL A 1 77  ? 25.642  4.245   -1.237  1.00 71.78  ? 263 VAL B CG2 1 
ATOM   421  N N   . PHE A 1 78  ? 26.093  3.502   2.549   1.00 77.96  ? 264 PHE B N   1 
ATOM   422  C CA  . PHE A 1 78  ? 26.047  4.421   3.683   1.00 78.70  ? 264 PHE B CA  1 
ATOM   423  C C   . PHE A 1 78  ? 27.427  4.600   4.308   1.00 79.08  ? 264 PHE B C   1 
ATOM   424  O O   . PHE A 1 78  ? 27.831  5.726   4.626   1.00 81.31  ? 264 PHE B O   1 
ATOM   425  C CB  . PHE A 1 78  ? 25.052  3.933   4.739   1.00 81.77  ? 264 PHE B CB  1 
ATOM   426  C CG  . PHE A 1 78  ? 23.616  4.265   4.434   1.00 79.05  ? 264 PHE B CG  1 
ATOM   427  C CD1 . PHE A 1 78  ? 23.290  5.107   3.388   1.00 79.00  ? 264 PHE B CD1 1 
ATOM   428  C CD2 . PHE A 1 78  ? 22.592  3.761   5.226   1.00 77.60  ? 264 PHE B CD2 1 
ATOM   429  C CE1 . PHE A 1 78  ? 21.967  5.416   3.116   1.00 76.48  ? 264 PHE B CE1 1 
ATOM   430  C CE2 . PHE A 1 78  ? 21.270  4.071   4.961   1.00 76.89  ? 264 PHE B CE2 1 
ATOM   431  C CZ  . PHE A 1 78  ? 20.958  4.902   3.906   1.00 75.22  ? 264 PHE B CZ  1 
ATOM   432  N N   . TYR A 1 79  ? 28.167  3.504   4.489   1.00 77.73  ? 265 TYR B N   1 
ATOM   433  C CA  . TYR A 1 79  ? 29.504  3.615   5.063   1.00 78.94  ? 265 TYR B CA  1 
ATOM   434  C C   . TYR A 1 79  ? 30.406  4.459   4.178   1.00 78.09  ? 265 TYR B C   1 
ATOM   435  O O   . TYR A 1 79  ? 31.131  5.336   4.662   1.00 79.68  ? 265 TYR B O   1 
ATOM   436  C CB  . TYR A 1 79  ? 30.111  2.229   5.273   1.00 80.54  ? 265 TYR B CB  1 
ATOM   437  C CG  . TYR A 1 79  ? 31.493  2.266   5.892   1.00 83.01  ? 265 TYR B CG  1 
ATOM   438  C CD1 . TYR A 1 79  ? 32.630  2.337   5.099   1.00 82.00  ? 265 TYR B CD1 1 
ATOM   439  C CD2 . TYR A 1 79  ? 31.659  2.239   7.270   1.00 83.66  ? 265 TYR B CD2 1 
ATOM   440  C CE1 . TYR A 1 79  ? 33.888  2.378   5.657   1.00 83.52  ? 265 TYR B CE1 1 
ATOM   441  C CE2 . TYR A 1 79  ? 32.917  2.279   7.838   1.00 85.20  ? 265 TYR B CE2 1 
ATOM   442  C CZ  . TYR A 1 79  ? 34.028  2.348   7.025   1.00 85.11  ? 265 TYR B CZ  1 
ATOM   443  O OH  . TYR A 1 79  ? 35.288  2.385   7.578   1.00 92.73  ? 265 TYR B OH  1 
ATOM   444  N N   . GLU A 1 80  ? 30.373  4.206   2.870   1.00 77.09  ? 266 GLU B N   1 
ATOM   445  C CA  . GLU A 1 80  ? 31.176  5.002   1.955   1.00 76.40  ? 266 GLU B CA  1 
ATOM   446  C C   . GLU A 1 80  ? 30.737  6.461   1.990   1.00 75.31  ? 266 GLU B C   1 
ATOM   447  O O   . GLU A 1 80  ? 31.568  7.371   1.900   1.00 80.19  ? 266 GLU B O   1 
ATOM   448  C CB  . GLU A 1 80  ? 31.077  4.429   0.544   1.00 75.69  ? 266 GLU B CB  1 
ATOM   449  C CG  . GLU A 1 80  ? 31.592  3.006   0.397   1.00 76.96  ? 266 GLU B CG  1 
ATOM   450  C CD  . GLU A 1 80  ? 33.096  2.906   0.547   1.00 85.85  ? 266 GLU B CD  1 
ATOM   451  O OE1 . GLU A 1 80  ? 33.783  3.936   0.373   1.00 79.55  ? 266 GLU B OE1 1 
ATOM   452  O OE2 . GLU A 1 80  ? 33.591  1.794   0.834   1.00 85.06  ? 266 GLU B OE2 1 
ATOM   453  N N   . LEU A 1 81  ? 29.433  6.704   2.140   1.00 74.44  ? 267 LEU B N   1 
ATOM   454  C CA  . LEU A 1 81  ? 28.944  8.074   2.216   1.00 73.76  ? 267 LEU B CA  1 
ATOM   455  C C   . LEU A 1 81  ? 29.334  8.759   3.518   1.00 74.67  ? 267 LEU B C   1 
ATOM   456  O O   . LEU A 1 81  ? 29.243  9.989   3.606   1.00 74.32  ? 267 LEU B O   1 
ATOM   457  C CB  . LEU A 1 81  ? 27.424  8.110   2.058   1.00 75.56  ? 267 LEU B CB  1 
ATOM   458  C CG  . LEU A 1 81  ? 26.863  7.968   0.645   1.00 71.28  ? 267 LEU B CG  1 
ATOM   459  C CD1 . LEU A 1 81  ? 25.345  7.953   0.690   1.00 71.19  ? 267 LEU B CD1 1 
ATOM   460  C CD2 . LEU A 1 81  ? 27.365  9.088   -0.245  1.00 70.49  ? 267 LEU B CD2 1 
ATOM   461  N N   . GLN A 1 82  ? 29.760  8.004   4.529   1.00 76.18  ? 268 GLN B N   1 
ATOM   462  C CA  . GLN A 1 82  ? 30.125  8.594   5.810   1.00 77.65  ? 268 GLN B CA  1 
ATOM   463  C C   . GLN A 1 82  ? 31.624  8.797   5.984   1.00 78.71  ? 268 GLN B C   1 
ATOM   464  O O   . GLN A 1 82  ? 32.030  9.739   6.673   1.00 80.12  ? 268 GLN B O   1 
ATOM   465  C CB  . GLN A 1 82  ? 29.594  7.729   6.960   1.00 78.75  ? 268 GLN B CB  1 
ATOM   466  C CG  . GLN A 1 82  ? 29.860  8.300   8.346   1.00 80.37  ? 268 GLN B CG  1 
ATOM   467  C CD  . GLN A 1 82  ? 28.992  7.668   9.416   1.00 86.74  ? 268 GLN B CD  1 
ATOM   468  O OE1 . GLN A 1 82  ? 27.903  7.165   9.133   1.00 80.68  ? 268 GLN B OE1 1 
ATOM   469  N NE2 . GLN A 1 82  ? 29.475  7.681   10.654  1.00 86.80  ? 268 GLN B NE2 1 
ATOM   470  N N   . HIS A 1 83  ? 32.457  7.957   5.368   1.00 79.00  ? 269 HIS B N   1 
ATOM   471  C CA  . HIS A 1 83  ? 33.904  7.983   5.575   1.00 80.44  ? 269 HIS B CA  1 
ATOM   472  C C   . HIS A 1 83  ? 34.714  8.411   4.359   1.00 79.83  ? 269 HIS B C   1 
ATOM   473  O O   . HIS A 1 83  ? 35.738  9.080   4.519   1.00 80.80  ? 269 HIS B O   1 
ATOM   474  C CB  . HIS A 1 83  ? 34.389  6.603   6.033   1.00 81.88  ? 269 HIS B CB  1 
ATOM   475  C CG  . HIS A 1 83  ? 33.827  6.173   7.352   1.00 83.04  ? 269 HIS B CG  1 
ATOM   476  N ND1 . HIS A 1 83  ? 32.491  5.889   7.536   1.00 84.82  ? 269 HIS B ND1 1 
ATOM   477  C CD2 . HIS A 1 83  ? 34.420  5.986   8.555   1.00 85.08  ? 269 HIS B CD2 1 
ATOM   478  C CE1 . HIS A 1 83  ? 32.287  5.543   8.794   1.00 87.30  ? 269 HIS B CE1 1 
ATOM   479  N NE2 . HIS A 1 83  ? 33.441  5.591   9.433   1.00 85.55  ? 269 HIS B NE2 1 
ATOM   480  N N   . SER A 1 84  ? 34.298  8.039   3.150   1.00 78.48  ? 270 SER B N   1 
ATOM   481  C CA  . SER A 1 84  ? 35.104  8.307   1.966   1.00 81.57  ? 270 SER B CA  1 
ATOM   482  C C   . SER A 1 84  ? 35.161  9.799   1.663   1.00 83.56  ? 270 SER B C   1 
ATOM   483  O O   . SER A 1 84  ? 34.168  10.518  1.804   1.00 80.64  ? 270 SER B O   1 
ATOM   484  C CB  . SER A 1 84  ? 34.545  7.554   0.759   1.00 82.80  ? 270 SER B CB  1 
ATOM   485  O OG  . SER A 1 84  ? 35.229  7.921   -0.429  1.00 84.67  ? 270 SER B OG  1 
ATOM   486  N N   . ASP A 1 85  ? 36.333  10.263  1.233   1.00 95.25  ? 271 ASP B N   1 
ATOM   487  C CA  . ASP A 1 85  ? 36.490  11.633  0.768   1.00 99.29  ? 271 ASP B CA  1 
ATOM   488  C C   . ASP A 1 85  ? 36.307  11.772  -0.736  1.00 101.30 ? 271 ASP B C   1 
ATOM   489  O O   . ASP A 1 85  ? 36.339  12.895  -1.248  1.00 106.71 ? 271 ASP B O   1 
ATOM   490  C CB  . ASP A 1 85  ? 37.865  12.179  1.174   1.00 104.35 ? 271 ASP B CB  1 
ATOM   491  C CG  . ASP A 1 85  ? 38.171  11.951  2.643   1.00 119.86 ? 271 ASP B CG  1 
ATOM   492  O OD1 . ASP A 1 85  ? 38.647  10.846  2.984   1.00 130.61 ? 271 ASP B OD1 1 
ATOM   493  O OD2 . ASP A 1 85  ? 37.919  12.868  3.456   1.00 120.99 ? 271 ASP B OD2 1 
ATOM   494  N N   . LYS A 1 86  ? 36.120  10.668  -1.451  1.00 83.36  ? 272 LYS B N   1 
ATOM   495  C CA  . LYS A 1 86  ? 35.834  10.679  -2.875  1.00 84.67  ? 272 LYS B CA  1 
ATOM   496  C C   . LYS A 1 86  ? 34.425  10.149  -3.119  1.00 80.06  ? 272 LYS B C   1 
ATOM   497  O O   . LYS A 1 86  ? 33.903  9.375   -2.310  1.00 82.75  ? 272 LYS B O   1 
ATOM   498  C CB  . LYS A 1 86  ? 36.858  9.877   -3.692  1.00 80.67  ? 272 LYS B CB  1 
ATOM   499  C CG  . LYS A 1 86  ? 38.172  10.625  -3.891  1.00 77.65  ? 272 LYS B CG  1 
ATOM   500  C CD  . LYS A 1 86  ? 39.177  9.837   -4.720  1.00 78.75  ? 272 LYS B CD  1 
ATOM   501  C CE  . LYS A 1 86  ? 39.658  8.583   -4.010  1.00 83.44  ? 272 LYS B CE  1 
ATOM   502  N NZ  . LYS A 1 86  ? 40.457  8.931   -2.797  1.00 84.04  ? 272 LYS B NZ  1 
ATOM   503  N N   . PRO A 1 87  ? 33.783  10.553  -4.217  1.00 78.73  ? 273 PRO B N   1 
ATOM   504  C CA  . PRO A 1 87  ? 32.379  10.184  -4.434  1.00 74.00  ? 273 PRO B CA  1 
ATOM   505  C C   . PRO A 1 87  ? 32.177  8.677   -4.509  1.00 72.19  ? 273 PRO B C   1 
ATOM   506  O O   . PRO A 1 87  ? 33.037  7.928   -4.978  1.00 77.38  ? 273 PRO B O   1 
ATOM   507  C CB  . PRO A 1 87  ? 32.036  10.862  -5.763  1.00 76.00  ? 273 PRO B CB  1 
ATOM   508  C CG  . PRO A 1 87  ? 32.982  12.010  -5.851  1.00 81.55  ? 273 PRO B CG  1 
ATOM   509  C CD  . PRO A 1 87  ? 34.254  11.534  -5.214  1.00 78.31  ? 273 PRO B CD  1 
ATOM   510  N N   . VAL A 1 88  ? 31.014  8.248   -4.038  1.00 71.31  ? 274 VAL B N   1 
ATOM   511  C CA  . VAL A 1 88  ? 30.703  6.849   -3.772  1.00 71.82  ? 274 VAL B CA  1 
ATOM   512  C C   . VAL A 1 88  ? 30.073  6.212   -5.003  1.00 71.58  ? 274 VAL B C   1 
ATOM   513  O O   . VAL A 1 88  ? 29.295  6.848   -5.726  1.00 71.18  ? 274 VAL B O   1 
ATOM   514  C CB  . VAL A 1 88  ? 29.768  6.750   -2.554  1.00 71.72  ? 274 VAL B CB  1 
ATOM   515  C CG1 . VAL A 1 88  ? 29.336  5.314   -2.305  1.00 72.38  ? 274 VAL B CG1 1 
ATOM   516  C CG2 . VAL A 1 88  ? 30.427  7.365   -1.336  1.00 72.47  ? 274 VAL B CG2 1 
ATOM   517  N N   . GLY A 1 89  ? 30.411  4.949   -5.246  1.00 72.28  ? 275 GLY B N   1 
ATOM   518  C CA  . GLY A 1 89  ? 29.829  4.189   -6.332  1.00 72.20  ? 275 GLY B CA  1 
ATOM   519  C C   . GLY A 1 89  ? 28.685  3.326   -5.833  1.00 75.42  ? 275 GLY B C   1 
ATOM   520  O O   . GLY A 1 89  ? 28.646  2.933   -4.668  1.00 72.82  ? 275 GLY B O   1 
ATOM   521  N N   . THR A 1 90  ? 27.751  3.026   -6.747  1.00 81.57  ? 276 THR B N   1 
ATOM   522  C CA  . THR A 1 90  ? 26.521  2.310   -6.424  1.00 71.92  ? 276 THR B CA  1 
ATOM   523  C C   . THR A 1 90  ? 26.308  1.101   -7.329  1.00 74.66  ? 276 THR B C   1 
ATOM   524  O O   . THR A 1 90  ? 25.169  0.647   -7.490  1.00 72.88  ? 276 THR B O   1 
ATOM   525  C CB  . THR A 1 90  ? 25.314  3.247   -6.527  1.00 70.60  ? 276 THR B CB  1 
ATOM   526  O OG1 . THR A 1 90  ? 25.207  3.743   -7.867  1.00 77.66  ? 276 THR B OG1 1 
ATOM   527  C CG2 . THR A 1 90  ? 25.469  4.427   -5.580  1.00 69.91  ? 276 THR B CG2 1 
ATOM   528  N N   . LYS A 1 91  ? 27.383  0.575   -7.925  1.00 74.52  ? 277 LYS B N   1 
ATOM   529  C CA  . LYS A 1 91  ? 27.245  -0.513  -8.889  1.00 74.92  ? 277 LYS B CA  1 
ATOM   530  C C   . LYS A 1 91  ? 26.724  -1.780  -8.226  1.00 76.12  ? 277 LYS B C   1 
ATOM   531  O O   . LYS A 1 91  ? 25.803  -2.428  -8.739  1.00 84.99  ? 277 LYS B O   1 
ATOM   532  C CB  . LYS A 1 91  ? 28.578  -0.781  -9.581  1.00 75.91  ? 277 LYS B CB  1 
ATOM   533  C CG  . LYS A 1 91  ? 28.492  -1.830  -10.677 1.00 77.23  ? 277 LYS B CG  1 
ATOM   534  C CD  . LYS A 1 91  ? 29.864  -2.139  -11.242 1.00 78.47  ? 277 LYS B CD  1 
ATOM   535  C CE  . LYS A 1 91  ? 29.781  -2.937  -12.530 1.00 87.42  ? 277 LYS B CE  1 
ATOM   536  N NZ  . LYS A 1 91  ? 31.142  -3.137  -13.117 1.00 85.31  ? 277 LYS B NZ  1 
ATOM   537  N N   . LYS A 1 92  ? 27.306  -2.151  -7.083  1.00 76.85  ? 278 LYS B N   1 
ATOM   538  C CA  . LYS A 1 92  ? 26.886  -3.372  -6.404  1.00 82.43  ? 278 LYS B CA  1 
ATOM   539  C C   . LYS A 1 92  ? 25.422  -3.295  -5.989  1.00 82.51  ? 278 LYS B C   1 
ATOM   540  O O   . LYS A 1 92  ? 24.675  -4.271  -6.132  1.00 85.39  ? 278 LYS B O   1 
ATOM   541  C CB  . LYS A 1 92  ? 27.784  -3.629  -5.193  1.00 79.16  ? 278 LYS B CB  1 
ATOM   542  N N   . LEU A 1 93  ? 24.994  -2.140  -5.476  1.00 76.22  ? 279 LEU B N   1 
ATOM   543  C CA  . LEU A 1 93  ? 23.603  -1.978  -5.066  1.00 80.34  ? 279 LEU B CA  1 
ATOM   544  C C   . LEU A 1 93  ? 22.652  -2.094  -6.255  1.00 89.40  ? 279 LEU B C   1 
ATOM   545  O O   . LEU A 1 93  ? 21.580  -2.697  -6.139  1.00 90.03  ? 279 LEU B O   1 
ATOM   546  C CB  . LEU A 1 93  ? 23.426  -0.640  -4.343  1.00 75.00  ? 279 LEU B CB  1 
ATOM   547  C CG  . LEU A 1 93  ? 22.034  -0.262  -3.829  1.00 81.43  ? 279 LEU B CG  1 
ATOM   548  C CD1 . LEU A 1 93  ? 21.385  -1.411  -3.078  1.00 85.72  ? 279 LEU B CD1 1 
ATOM   549  C CD2 . LEU A 1 93  ? 22.112  0.977   -2.943  1.00 72.87  ? 279 LEU B CD2 1 
ATOM   550  N N   . THR A 1 94  ? 23.021  -1.519  -7.407  1.00 87.94  ? 280 THR B N   1 
ATOM   551  C CA  . THR A 1 94  ? 22.187  -1.655  -8.602  1.00 84.49  ? 280 THR B CA  1 
ATOM   552  C C   . THR A 1 94  ? 22.051  -3.117  -9.008  1.00 89.01  ? 280 THR B C   1 
ATOM   553  O O   . THR A 1 94  ? 20.959  -3.575  -9.371  1.00 89.10  ? 280 THR B O   1 
ATOM   554  C CB  . THR A 1 94  ? 22.766  -0.834  -9.756  1.00 89.18  ? 280 THR B CB  1 
ATOM   555  O OG1 . THR A 1 94  ? 22.633  0.565   -9.469  1.00 87.79  ? 280 THR B OG1 1 
ATOM   556  C CG2 . THR A 1 94  ? 22.020  -1.142  -11.054 1.00 87.66  ? 280 THR B CG2 1 
ATOM   557  N N   . LYS A 1 95  ? 23.156  -3.861  -8.969  1.00 97.98  ? 281 LYS B N   1 
ATOM   558  C CA  . LYS A 1 95  ? 23.087  -5.302  -9.177  1.00 105.40 ? 281 LYS B CA  1 
ATOM   559  C C   . LYS A 1 95  ? 22.252  -5.981  -8.099  1.00 98.85  ? 281 LYS B C   1 
ATOM   560  O O   . LYS A 1 95  ? 21.626  -7.015  -8.358  1.00 105.15 ? 281 LYS B O   1 
ATOM   561  C CB  . LYS A 1 95  ? 24.501  -5.889  -9.194  1.00 102.68 ? 281 LYS B CB  1 
ATOM   562  C CG  . LYS A 1 95  ? 24.568  -7.413  -9.221  1.00 101.86 ? 281 LYS B CG  1 
ATOM   563  C CD  . LYS A 1 95  ? 25.921  -7.913  -8.736  1.00 110.24 ? 281 LYS B CD  1 
ATOM   564  C CE  . LYS A 1 95  ? 27.062  -7.176  -9.422  1.00 111.01 ? 281 LYS B CE  1 
ATOM   565  N NZ  . LYS A 1 95  ? 26.966  -7.272  -10.906 1.00 112.51 ? 281 LYS B NZ  1 
ATOM   566  N N   . SER A 1 96  ? 22.215  -5.403  -6.895  1.00 92.20  ? 282 SER B N   1 
ATOM   567  C CA  . SER A 1 96  ? 21.631  -6.092  -5.748  1.00 91.34  ? 282 SER B CA  1 
ATOM   568  C C   . SER A 1 96  ? 20.134  -6.335  -5.928  1.00 94.91  ? 282 SER B C   1 
ATOM   569  O O   . SER A 1 96  ? 19.655  -7.460  -5.751  1.00 91.97  ? 282 SER B O   1 
ATOM   570  C CB  . SER A 1 96  ? 21.899  -5.295  -4.473  1.00 86.07  ? 282 SER B CB  1 
ATOM   571  O OG  . SER A 1 96  ? 21.693  -6.104  -3.334  1.00 100.23 ? 282 SER B OG  1 
ATOM   572  N N   . PHE A 1 97  ? 19.376  -5.293  -6.277  1.00 97.29  ? 283 PHE B N   1 
ATOM   573  C CA  . PHE A 1 97  ? 17.940  -5.427  -6.492  1.00 88.50  ? 283 PHE B CA  1 
ATOM   574  C C   . PHE A 1 97  ? 17.569  -5.634  -7.957  1.00 91.25  ? 283 PHE B C   1 
ATOM   575  O O   . PHE A 1 97  ? 16.380  -5.606  -8.292  1.00 85.93  ? 283 PHE B O   1 
ATOM   576  C CB  . PHE A 1 97  ? 17.196  -4.217  -5.919  1.00 79.26  ? 283 PHE B CB  1 
ATOM   577  C CG  . PHE A 1 97  ? 17.680  -2.894  -6.436  1.00 76.44  ? 283 PHE B CG  1 
ATOM   578  C CD1 . PHE A 1 97  ? 17.247  -2.406  -7.657  1.00 80.75  ? 283 PHE B CD1 1 
ATOM   579  C CD2 . PHE A 1 97  ? 18.547  -2.124  -5.682  1.00 75.68  ? 283 PHE B CD2 1 
ATOM   580  C CE1 . PHE A 1 97  ? 17.686  -1.182  -8.123  1.00 82.72  ? 283 PHE B CE1 1 
ATOM   581  C CE2 . PHE A 1 97  ? 18.990  -0.902  -6.142  1.00 82.62  ? 283 PHE B CE2 1 
ATOM   582  C CZ  . PHE A 1 97  ? 18.558  -0.429  -7.365  1.00 83.70  ? 283 PHE B CZ  1 
ATOM   583  N N   . GLY A 1 98  ? 18.552  -5.835  -8.830  1.00 92.89  ? 284 GLY B N   1 
ATOM   584  C CA  . GLY A 1 98  ? 18.281  -6.334  -10.171 1.00 95.10  ? 284 GLY B CA  1 
ATOM   585  C C   . GLY A 1 98  ? 17.449  -5.440  -11.065 1.00 92.25  ? 284 GLY B C   1 
ATOM   586  O O   . GLY A 1 98  ? 16.568  -5.935  -11.780 1.00 93.23  ? 284 GLY B O   1 
ATOM   587  N N   . TRP A 1 99  ? 17.709  -4.135  -11.055 1.00 92.15  ? 285 TRP B N   1 
ATOM   588  C CA  . TRP A 1 99  ? 17.101  -3.222  -12.025 1.00 89.53  ? 285 TRP B CA  1 
ATOM   589  C C   . TRP A 1 99  ? 18.152  -2.983  -13.102 1.00 92.09  ? 285 TRP B C   1 
ATOM   590  O O   . TRP A 1 99  ? 18.910  -2.011  -13.067 1.00 81.44  ? 285 TRP B O   1 
ATOM   591  C CB  . TRP A 1 99  ? 16.631  -1.929  -11.374 1.00 87.42  ? 285 TRP B CB  1 
ATOM   592  C CG  . TRP A 1 99  ? 15.419  -2.105  -10.518 1.00 82.40  ? 285 TRP B CG  1 
ATOM   593  C CD1 . TRP A 1 99  ? 14.893  -3.281  -10.071 1.00 84.09  ? 285 TRP B CD1 1 
ATOM   594  C CD2 . TRP A 1 99  ? 14.559  -1.070  -10.031 1.00 82.64  ? 285 TRP B CD2 1 
ATOM   595  N NE1 . TRP A 1 99  ? 13.769  -3.042  -9.321  1.00 82.89  ? 285 TRP B NE1 1 
ATOM   596  C CE2 . TRP A 1 99  ? 13.541  -1.691  -9.283  1.00 84.18  ? 285 TRP B CE2 1 
ATOM   597  C CE3 . TRP A 1 99  ? 14.556  0.323   -10.150 1.00 84.18  ? 285 TRP B CE3 1 
ATOM   598  C CZ2 . TRP A 1 99  ? 12.527  -0.968  -8.655  1.00 87.00  ? 285 TRP B CZ2 1 
ATOM   599  C CZ3 . TRP A 1 99  ? 13.550  1.041   -9.525  1.00 83.76  ? 285 TRP B CZ3 1 
ATOM   600  C CH2 . TRP A 1 99  ? 12.549  0.394   -8.787  1.00 84.50  ? 285 TRP B CH2 1 
ATOM   601  N N   . GLU A 1 100 ? 18.201  -3.905  -14.057 1.00 92.87  ? 286 GLU B N   1 
ATOM   602  C CA  . GLU A 1 100 ? 19.224  -3.912  -15.081 1.00 88.86  ? 286 GLU B CA  1 
ATOM   603  C C   . GLU A 1 100 ? 18.673  -3.899  -16.501 1.00 87.72  ? 286 GLU B C   1 
ATOM   604  O O   . GLU A 1 100 ? 19.463  -3.849  -17.450 1.00 88.68  ? 286 GLU B O   1 
ATOM   605  C CB  . GLU A 1 100 ? 20.143  -5.116  -14.850 1.00 96.60  ? 286 GLU B CB  1 
ATOM   606  C CG  . GLU A 1 100 ? 21.001  -4.924  -13.602 1.00 96.25  ? 286 GLU B CG  1 
ATOM   607  C CD  . GLU A 1 100 ? 21.523  -6.225  -13.037 1.00 105.28 ? 286 GLU B CD  1 
ATOM   608  O OE1 . GLU A 1 100 ? 20.717  -7.167  -12.886 1.00 111.58 ? 286 GLU B OE1 1 
ATOM   609  O OE2 . GLU A 1 100 ? 22.735  -6.309  -12.748 1.00 111.11 ? 286 GLU B OE2 1 
ATOM   610  N N   . THR A 1 101 ? 17.354  -3.941  -16.681 1.00 95.64  ? 287 THR B N   1 
ATOM   611  C CA  . THR A 1 101 ? 16.795  -3.755  -18.014 1.00 96.31  ? 287 THR B CA  1 
ATOM   612  C C   . THR A 1 101 ? 16.913  -2.287  -18.419 1.00 94.53  ? 287 THR B C   1 
ATOM   613  O O   . THR A 1 101 ? 16.941  -1.389  -17.574 1.00 96.06  ? 287 THR B O   1 
ATOM   614  C CB  . THR A 1 101 ? 15.333  -4.221  -18.067 1.00 97.36  ? 287 THR B CB  1 
ATOM   615  O OG1 . THR A 1 101 ? 14.612  -3.466  -19.051 1.00 107.57 ? 287 THR B OG1 1 
ATOM   616  C CG2 . THR A 1 101 ? 14.648  -4.077  -16.714 1.00 96.44  ? 287 THR B CG2 1 
ATOM   617  N N   . LEU A 1 102 ? 16.942  -2.050  -19.737 1.00 93.58  ? 288 LEU B N   1 
ATOM   618  C CA  . LEU A 1 102 ? 17.247  -0.718  -20.262 1.00 92.15  ? 288 LEU B CA  1 
ATOM   619  C C   . LEU A 1 102 ? 16.272  0.347   -19.771 1.00 93.82  ? 288 LEU B C   1 
ATOM   620  O O   . LEU A 1 102 ? 16.656  1.511   -19.610 1.00 90.68  ? 288 LEU B O   1 
ATOM   621  C CB  . LEU A 1 102 ? 17.261  -0.757  -21.793 1.00 87.17  ? 288 LEU B CB  1 
ATOM   622  C CG  . LEU A 1 102 ? 18.628  -1.015  -22.436 1.00 84.01  ? 288 LEU B CG  1 
ATOM   623  C CD1 . LEU A 1 102 ? 18.528  -1.095  -23.951 1.00 82.49  ? 288 LEU B CD1 1 
ATOM   624  C CD2 . LEU A 1 102 ? 19.616  0.063   -22.021 1.00 84.55  ? 288 LEU B CD2 1 
ATOM   625  N N   . ASP A 1 103 ? 15.019  -0.025  -19.526 1.00 92.00  ? 289 ASP B N   1 
ATOM   626  C CA  . ASP A 1 103 ? 13.984  0.912   -19.106 1.00 88.28  ? 289 ASP B CA  1 
ATOM   627  C C   . ASP A 1 103 ? 13.609  0.767   -17.633 1.00 93.83  ? 289 ASP B C   1 
ATOM   628  O O   . ASP A 1 103 ? 12.586  1.318   -17.210 1.00 94.78  ? 289 ASP B O   1 
ATOM   629  C CB  . ASP A 1 103 ? 12.756  0.761   -20.005 1.00 85.33  ? 289 ASP B CB  1 
ATOM   630  C CG  . ASP A 1 103 ? 12.357  -0.687  -20.211 1.00 100.17 ? 289 ASP B CG  1 
ATOM   631  O OD1 . ASP A 1 103 ? 12.881  -1.567  -19.495 1.00 104.88 ? 289 ASP B OD1 1 
ATOM   632  O OD2 . ASP A 1 103 ? 11.533  -0.948  -21.113 1.00 103.16 ? 289 ASP B OD2 1 
ATOM   633  N N   . SER A 1 104 ? 14.411  0.038   -16.848 1.00 88.32  ? 290 SER B N   1 
ATOM   634  C CA  . SER A 1 104 ? 14.020  -0.322  -15.485 1.00 87.71  ? 290 SER B CA  1 
ATOM   635  C C   . SER A 1 104 ? 13.786  0.901   -14.605 1.00 87.35  ? 290 SER B C   1 
ATOM   636  O O   . SER A 1 104 ? 12.773  0.983   -13.901 1.00 94.51  ? 290 SER B O   1 
ATOM   637  C CB  . SER A 1 104 ? 15.088  -1.208  -14.853 1.00 81.90  ? 290 SER B CB  1 
ATOM   638  O OG  . SER A 1 104 ? 16.362  -0.612  -14.990 1.00 93.33  ? 290 SER B OG  1 
ATOM   639  N N   . PHE A 1 105 ? 14.713  1.861   -14.615 1.00 81.03  ? 291 PHE B N   1 
ATOM   640  C CA  . PHE A 1 105 ? 14.548  2.998   -13.719 1.00 80.38  ? 291 PHE B CA  1 
ATOM   641  C C   . PHE A 1 105 ? 13.527  4.002   -14.232 1.00 83.81  ? 291 PHE B C   1 
ATOM   642  O O   . PHE A 1 105 ? 12.855  4.655   -13.424 1.00 83.32  ? 291 PHE B O   1 
ATOM   643  C CB  . PHE A 1 105 ? 15.893  3.674   -13.455 1.00 69.85  ? 291 PHE B CB  1 
ATOM   644  C CG  . PHE A 1 105 ? 16.727  2.953   -12.439 1.00 75.51  ? 291 PHE B CG  1 
ATOM   645  C CD1 . PHE A 1 105 ? 17.518  1.874   -12.803 1.00 84.14  ? 291 PHE B CD1 1 
ATOM   646  C CD2 . PHE A 1 105 ? 16.704  3.343   -11.109 1.00 71.04  ? 291 PHE B CD2 1 
ATOM   647  C CE1 . PHE A 1 105 ? 18.280  1.205   -11.858 1.00 82.30  ? 291 PHE B CE1 1 
ATOM   648  C CE2 . PHE A 1 105 ? 17.464  2.680   -10.159 1.00 71.46  ? 291 PHE B CE2 1 
ATOM   649  C CZ  . PHE A 1 105 ? 18.251  1.609   -10.534 1.00 80.12  ? 291 PHE B CZ  1 
ATOM   650  N N   . MET A 1 106 ? 13.378  4.150   -15.546 1.00 76.96  ? 292 MET B N   1 
ATOM   651  C CA  . MET A 1 106 ? 12.363  5.088   -16.001 1.00 79.23  ? 292 MET B CA  1 
ATOM   652  C C   . MET A 1 106 ? 10.957  4.498   -16.005 1.00 89.87  ? 292 MET B C   1 
ATOM   653  O O   . MET A 1 106 ? 9.988   5.262   -16.053 1.00 91.08  ? 292 MET B O   1 
ATOM   654  C CB  . MET A 1 106 ? 12.721  5.663   -17.373 1.00 75.54  ? 292 MET B CB  1 
ATOM   655  C CG  . MET A 1 106 ? 13.810  6.731   -17.284 1.00 70.68  ? 292 MET B CG  1 
ATOM   656  S SD  . MET A 1 106 ? 14.021  7.705   -18.786 1.00 84.86  ? 292 MET B SD  1 
ATOM   657  C CE  . MET A 1 106 ? 12.356  8.333   -19.021 1.00 91.12  ? 292 MET B CE  1 
ATOM   658  N N   . GLN A 1 107 ? 10.805  3.173   -15.964 1.00 102.46 ? 293 GLN B N   1 
ATOM   659  C CA  . GLN A 1 107 ? 9.448   2.644   -15.872 1.00 100.94 ? 293 GLN B CA  1 
ATOM   660  C C   . GLN A 1 107 ? 8.938   2.627   -14.436 1.00 99.52  ? 293 GLN B C   1 
ATOM   661  O O   . GLN A 1 107 ? 7.723   2.685   -14.210 1.00 101.88 ? 293 GLN B O   1 
ATOM   662  C CB  . GLN A 1 107 ? 9.349   1.230   -16.445 1.00 100.73 ? 293 GLN B CB  1 
ATOM   663  C CG  . GLN A 1 107 ? 9.334   1.147   -17.952 1.00 103.60 ? 293 GLN B CG  1 
ATOM   664  C CD  . GLN A 1 107 ? 8.926   -0.233  -18.423 1.00 116.18 ? 293 GLN B CD  1 
ATOM   665  O OE1 . GLN A 1 107 ? 8.336   -1.007  -17.658 1.00 120.16 ? 293 GLN B OE1 1 
ATOM   666  N NE2 . GLN A 1 107 ? 9.233   -0.557  -19.681 1.00 131.18 ? 293 GLN B NE2 1 
ATOM   667  N N   . HIS A 1 108 ? 9.837   2.519   -13.461 1.00 86.01  ? 294 HIS B N   1 
ATOM   668  C CA  . HIS A 1 108 ? 9.416   2.396   -12.077 1.00 84.27  ? 294 HIS B CA  1 
ATOM   669  C C   . HIS A 1 108 ? 9.306   3.784   -11.451 1.00 78.52  ? 294 HIS B C   1 
ATOM   670  O O   . HIS A 1 108 ? 9.564   4.809   -12.087 1.00 77.36  ? 294 HIS B O   1 
ATOM   671  C CB  . HIS A 1 108 ? 10.389  1.521   -11.286 1.00 86.23  ? 294 HIS B CB  1 
ATOM   672  C CG  . HIS A 1 108 ? 10.457  0.098   -11.753 1.00 88.77  ? 294 HIS B CG  1 
ATOM   673  N ND1 . HIS A 1 108 ? 10.981  -0.264  -12.976 1.00 86.84  ? 294 HIS B ND1 1 
ATOM   674  C CD2 . HIS A 1 108 ? 10.096  -1.056  -11.143 1.00 89.89  ? 294 HIS B CD2 1 
ATOM   675  C CE1 . HIS A 1 108 ? 10.928  -1.578  -13.105 1.00 91.47  ? 294 HIS B CE1 1 
ATOM   676  N NE2 . HIS A 1 108 ? 10.396  -2.082  -12.007 1.00 97.23  ? 294 HIS B NE2 1 
ATOM   677  N N   . ASP A 1 109 ? 8.932   3.819   -10.179 1.00 78.53  ? 295 ASP B N   1 
ATOM   678  C CA  . ASP A 1 109 ? 8.722   5.069   -9.468  1.00 76.70  ? 295 ASP B CA  1 
ATOM   679  C C   . ASP A 1 109 ? 9.761   5.243   -8.368  1.00 73.01  ? 295 ASP B C   1 
ATOM   680  O O   . ASP A 1 109 ? 10.410  4.286   -7.935  1.00 72.54  ? 295 ASP B O   1 
ATOM   681  C CB  . ASP A 1 109 ? 7.315   5.131   -8.857  1.00 80.18  ? 295 ASP B CB  1 
ATOM   682  C CG  . ASP A 1 109 ? 6.210   5.086   -9.902  1.00 77.61  ? 295 ASP B CG  1 
ATOM   683  O OD1 . ASP A 1 109 ? 6.392   5.652   -11.000 1.00 75.99  ? 295 ASP B OD1 1 
ATOM   684  O OD2 . ASP A 1 109 ? 5.157   4.473   -9.620  1.00 73.16  ? 295 ASP B OD2 1 
ATOM   685  N N   . VAL A 1 110 ? 9.902   6.488   -7.907  1.00 75.29  ? 296 VAL B N   1 
ATOM   686  C CA  . VAL A 1 110 ? 10.709  6.737   -6.717  1.00 74.42  ? 296 VAL B CA  1 
ATOM   687  C C   . VAL A 1 110 ? 10.136  5.974   -5.531  1.00 76.18  ? 296 VAL B C   1 
ATOM   688  O O   . VAL A 1 110 ? 10.881  5.434   -4.704  1.00 79.23  ? 296 VAL B O   1 
ATOM   689  C CB  . VAL A 1 110 ? 10.808  8.247   -6.425  1.00 73.24  ? 296 VAL B CB  1 
ATOM   690  C CG1 . VAL A 1 110 ? 11.698  8.917   -7.427  1.00 72.89  ? 296 VAL B CG1 1 
ATOM   691  C CG2 . VAL A 1 110 ? 9.439   8.901   -6.435  1.00 73.28  ? 296 VAL B CG2 1 
ATOM   692  N N   . GLN A 1 111 ? 8.803   5.909   -5.435  1.00 75.14  ? 297 GLN B N   1 
ATOM   693  C CA  . GLN A 1 111 ? 8.171   5.156   -4.356  1.00 75.55  ? 297 GLN B CA  1 
ATOM   694  C C   . GLN A 1 111 ? 8.557   3.684   -4.412  1.00 77.03  ? 297 GLN B C   1 
ATOM   695  O O   . GLN A 1 111 ? 8.846   3.074   -3.376  1.00 76.79  ? 297 GLN B O   1 
ATOM   696  C CB  . GLN A 1 111 ? 6.650   5.306   -4.412  1.00 77.07  ? 297 GLN B CB  1 
ATOM   697  C CG  . GLN A 1 111 ? 6.137   6.739   -4.454  1.00 75.07  ? 297 GLN B CG  1 
ATOM   698  C CD  . GLN A 1 111 ? 5.872   7.247   -5.853  1.00 75.29  ? 297 GLN B CD  1 
ATOM   699  O OE1 . GLN A 1 111 ? 6.784   7.374   -6.666  1.00 75.20  ? 297 GLN B OE1 1 
ATOM   700  N NE2 . GLN A 1 111 ? 4.610   7.538   -6.144  1.00 75.70  ? 297 GLN B NE2 1 
ATOM   701  N N   . GLU A 1 112 ? 8.539   3.089   -5.610  1.00 77.41  ? 298 GLU B N   1 
ATOM   702  C CA  . GLU A 1 112 ? 8.856   1.669   -5.731  1.00 79.11  ? 298 GLU B CA  1 
ATOM   703  C C   . GLU A 1 112 ? 10.287  1.383   -5.291  1.00 79.63  ? 298 GLU B C   1 
ATOM   704  O O   . GLU A 1 112 ? 10.540  0.417   -4.560  1.00 79.09  ? 298 GLU B O   1 
ATOM   705  C CB  . GLU A 1 112 ? 8.648   1.202   -7.172  1.00 79.45  ? 298 GLU B CB  1 
ATOM   706  C CG  . GLU A 1 112 ? 7.236   1.349   -7.694  1.00 79.80  ? 298 GLU B CG  1 
ATOM   707  C CD  . GLU A 1 112 ? 7.035   0.633   -9.016  1.00 85.08  ? 298 GLU B CD  1 
ATOM   708  O OE1 . GLU A 1 112 ? 6.929   -0.612  -9.009  1.00 92.01  ? 298 GLU B OE1 1 
ATOM   709  O OE2 . GLU A 1 112 ? 6.999   1.312   -10.064 1.00 89.32  ? 298 GLU B OE2 1 
ATOM   710  N N   . LEU A 1 113 ? 11.236  2.221   -5.712  1.00 77.59  ? 299 LEU B N   1 
ATOM   711  C CA  . LEU A 1 113 ? 12.620  2.009   -5.311  1.00 79.55  ? 299 LEU B CA  1 
ATOM   712  C C   . LEU A 1 113 ? 12.776  2.149   -3.804  1.00 78.55  ? 299 LEU B C   1 
ATOM   713  O O   . LEU A 1 113 ? 13.506  1.376   -3.173  1.00 84.53  ? 299 LEU B O   1 
ATOM   714  C CB  . LEU A 1 113 ? 13.542  2.984   -6.040  1.00 79.30  ? 299 LEU B CB  1 
ATOM   715  C CG  . LEU A 1 113 ? 15.030  2.716   -5.816  1.00 76.42  ? 299 LEU B CG  1 
ATOM   716  C CD1 . LEU A 1 113 ? 15.391  1.299   -6.245  1.00 77.85  ? 299 LEU B CD1 1 
ATOM   717  C CD2 . LEU A 1 113 ? 15.861  3.743   -6.554  1.00 75.51  ? 299 LEU B CD2 1 
ATOM   718  N N   . CYS A 1 114 ? 12.107  3.141   -3.213  1.00 75.99  ? 300 CYS B N   1 
ATOM   719  C CA  . CYS A 1 114 ? 12.130  3.289   -1.762  1.00 75.61  ? 300 CYS B CA  1 
ATOM   720  C C   . CYS A 1 114 ? 11.469  2.098   -1.077  1.00 79.28  ? 300 CYS B C   1 
ATOM   721  O O   . CYS A 1 114 ? 11.921  1.656   -0.015  1.00 78.12  ? 300 CYS B O   1 
ATOM   722  C CB  . CYS A 1 114 ? 11.443  4.593   -1.361  1.00 74.55  ? 300 CYS B CB  1 
ATOM   723  S SG  . CYS A 1 114 ? 11.562  4.982   0.388   1.00 79.02  ? 300 CYS B SG  1 
ATOM   724  N N   . ARG A 1 115 ? 10.393  1.569   -1.667  1.00 85.87  ? 301 ARG B N   1 
ATOM   725  C CA  . ARG A 1 115 ? 9.772   0.367   -1.118  1.00 86.91  ? 301 ARG B CA  1 
ATOM   726  C C   . ARG A 1 115 ? 10.698  -0.835  -1.232  1.00 87.98  ? 301 ARG B C   1 
ATOM   727  O O   . ARG A 1 115 ? 10.781  -1.647  -0.305  1.00 88.75  ? 301 ARG B O   1 
ATOM   728  C CB  . ARG A 1 115 ? 8.442   0.079   -1.816  1.00 93.11  ? 301 ARG B CB  1 
ATOM   729  C CG  . ARG A 1 115 ? 7.278   0.940   -1.356  1.00 91.02  ? 301 ARG B CG  1 
ATOM   730  C CD  . ARG A 1 115 ? 6.976   0.694   0.113   1.00 90.77  ? 301 ARG B CD  1 
ATOM   731  N NE  . ARG A 1 115 ? 7.694   1.624   0.976   1.00 94.46  ? 301 ARG B NE  1 
ATOM   732  C CZ  . ARG A 1 115 ? 7.861   1.460   2.280   1.00 98.66  ? 301 ARG B CZ  1 
ATOM   733  N NH1 . ARG A 1 115 ? 7.372   0.405   2.913   1.00 101.50 ? 301 ARG B NH1 1 
ATOM   734  N NH2 . ARG A 1 115 ? 8.531   2.380   2.968   1.00 99.03  ? 301 ARG B NH2 1 
ATOM   735  N N   . VAL A 1 116 ? 11.387  -0.975  -2.367  1.00 79.95  ? 302 VAL B N   1 
ATOM   736  C CA  . VAL A 1 116 ? 12.287  -2.110  -2.552  1.00 83.11  ? 302 VAL B CA  1 
ATOM   737  C C   . VAL A 1 116 ? 13.382  -2.099  -1.493  1.00 80.84  ? 302 VAL B C   1 
ATOM   738  O O   . VAL A 1 116 ? 13.695  -3.129  -0.883  1.00 81.95  ? 302 VAL B O   1 
ATOM   739  C CB  . VAL A 1 116 ? 12.882  -2.097  -3.972  1.00 81.81  ? 302 VAL B CB  1 
ATOM   740  C CG1 . VAL A 1 116 ? 14.084  -3.028  -4.051  1.00 82.15  ? 302 VAL B CG1 1 
ATOM   741  C CG2 . VAL A 1 116 ? 11.829  -2.490  -4.993  1.00 81.94  ? 302 VAL B CG2 1 
ATOM   742  N N   . LEU A 1 117 ? 13.982  -0.931  -1.261  1.00 79.47  ? 303 LEU B N   1 
ATOM   743  C CA  . LEU A 1 117 ? 15.042  -0.826  -0.265  1.00 84.22  ? 303 LEU B CA  1 
ATOM   744  C C   . LEU A 1 117 ? 14.494  -0.971  1.151   1.00 82.45  ? 303 LEU B C   1 
ATOM   745  O O   . LEU A 1 117 ? 14.999  -1.775  1.944   1.00 87.62  ? 303 LEU B O   1 
ATOM   746  C CB  . LEU A 1 117 ? 15.775  0.508   -0.423  1.00 81.39  ? 303 LEU B CB  1 
ATOM   747  C CG  . LEU A 1 117 ? 16.452  0.765   -1.771  1.00 77.37  ? 303 LEU B CG  1 
ATOM   748  C CD1 . LEU A 1 117 ? 17.032  2.173   -1.829  1.00 75.80  ? 303 LEU B CD1 1 
ATOM   749  C CD2 . LEU A 1 117 ? 17.520  -0.279  -2.043  1.00 78.43  ? 303 LEU B CD2 1 
ATOM   750  N N   . LEU A 1 118 ? 13.450  -0.208  1.482   1.00 78.64  ? 304 LEU B N   1 
ATOM   751  C CA  . LEU A 1 118 ? 12.989  -0.157  2.866   1.00 78.68  ? 304 LEU B CA  1 
ATOM   752  C C   . LEU A 1 118 ? 12.392  -1.487  3.307   1.00 80.24  ? 304 LEU B C   1 
ATOM   753  O O   . LEU A 1 118 ? 12.567  -1.894  4.461   1.00 82.53  ? 304 LEU B O   1 
ATOM   754  C CB  . LEU A 1 118 ? 11.982  0.974   3.040   1.00 82.20  ? 304 LEU B CB  1 
ATOM   755  C CG  . LEU A 1 118 ? 12.602  2.360   3.223   1.00 79.93  ? 304 LEU B CG  1 
ATOM   756  C CD1 . LEU A 1 118 ? 11.576  3.334   3.776   1.00 85.66  ? 304 LEU B CD1 1 
ATOM   757  C CD2 . LEU A 1 118 ? 13.842  2.307   4.109   1.00 80.66  ? 304 LEU B CD2 1 
ATOM   758  N N   . ASP A 1 119 ? 11.673  -2.171  2.413   1.00 91.60  ? 305 ASP B N   1 
ATOM   759  C CA  . ASP A 1 119 ? 11.150  -3.492  2.749   1.00 93.17  ? 305 ASP B CA  1 
ATOM   760  C C   . ASP A 1 119 ? 12.283  -4.471  3.028   1.00 94.30  ? 305 ASP B C   1 
ATOM   761  O O   . ASP A 1 119 ? 12.200  -5.283  3.957   1.00 97.52  ? 305 ASP B O   1 
ATOM   762  C CB  . ASP A 1 119 ? 10.263  -4.023  1.619   1.00 93.78  ? 305 ASP B CB  1 
ATOM   763  C CG  . ASP A 1 119 ? 8.928   -3.296  1.519   1.00 103.86 ? 305 ASP B CG  1 
ATOM   764  O OD1 . ASP A 1 119 ? 8.389   -2.880  2.568   1.00 98.05  ? 305 ASP B OD1 1 
ATOM   765  O OD2 . ASP A 1 119 ? 8.414   -3.150  0.387   1.00 100.03 ? 305 ASP B OD2 1 
ATOM   766  N N   . ASN A 1 120 ? 13.352  -4.405  2.235   1.00 85.34  ? 306 ASN B N   1 
ATOM   767  C CA  . ASN A 1 120 ? 14.489  -5.292  2.447   1.00 85.33  ? 306 ASN B CA  1 
ATOM   768  C C   . ASN A 1 120 ? 15.136  -5.047  3.804   1.00 88.15  ? 306 ASN B C   1 
ATOM   769  O O   . ASN A 1 120 ? 15.440  -5.993  4.539   1.00 93.20  ? 306 ASN B O   1 
ATOM   770  C CB  . ASN A 1 120 ? 15.508  -5.104  1.329   1.00 91.62  ? 306 ASN B CB  1 
ATOM   771  C CG  . ASN A 1 120 ? 15.223  -5.983  0.139   1.00 89.78  ? 306 ASN B CG  1 
ATOM   772  O OD1 . ASN A 1 120 ? 15.665  -7.129  0.077   1.00 87.56  ? 306 ASN B OD1 1 
ATOM   773  N ND2 . ASN A 1 120 ? 14.487  -5.447  -0.825  1.00 93.79  ? 306 ASN B ND2 1 
ATOM   774  N N   . VAL A 1 121 ? 15.362  -3.778  4.150   1.00 84.69  ? 307 VAL B N   1 
ATOM   775  C CA  . VAL A 1 121 ? 16.006  -3.447  5.419   1.00 89.51  ? 307 VAL B CA  1 
ATOM   776  C C   . VAL A 1 121 ? 15.107  -3.817  6.592   1.00 97.35  ? 307 VAL B C   1 
ATOM   777  O O   . VAL A 1 121 ? 15.562  -4.403  7.582   1.00 101.57 ? 307 VAL B O   1 
ATOM   778  C CB  . VAL A 1 121 ? 16.388  -1.958  5.452   1.00 86.70  ? 307 VAL B CB  1 
ATOM   779  C CG1 . VAL A 1 121 ? 16.657  -1.517  6.877   1.00 95.89  ? 307 VAL B CG1 1 
ATOM   780  C CG2 . VAL A 1 121 ? 17.606  -1.717  4.593   1.00 90.18  ? 307 VAL B CG2 1 
ATOM   781  N N   . GLU A 1 122 ? 13.821  -3.465  6.505   1.00 97.31  ? 308 GLU B N   1 
ATOM   782  C CA  . GLU A 1 122 ? 12.881  -3.800  7.572   1.00 99.77  ? 308 GLU B CA  1 
ATOM   783  C C   . GLU A 1 122 ? 12.769  -5.308  7.748   1.00 98.49  ? 308 GLU B C   1 
ATOM   784  O O   . GLU A 1 122 ? 12.688  -5.809  8.877   1.00 96.46  ? 308 GLU B O   1 
ATOM   785  C CB  . GLU A 1 122 ? 11.513  -3.188  7.272   1.00 92.60  ? 308 GLU B CB  1 
ATOM   786  C CG  . GLU A 1 122 ? 10.435  -3.512  8.290   1.00 92.42  ? 308 GLU B CG  1 
ATOM   787  C CD  . GLU A 1 122 ? 9.073   -3.008  7.854   1.00 101.80 ? 308 GLU B CD  1 
ATOM   788  O OE1 . GLU A 1 122 ? 9.026   -2.198  6.903   1.00 98.38  ? 308 GLU B OE1 1 
ATOM   789  O OE2 . GLU A 1 122 ? 8.052   -3.420  8.450   1.00 96.83  ? 308 GLU B OE2 1 
ATOM   790  N N   . ASN A 1 123 ? 12.762  -6.047  6.637   1.00 96.81  ? 309 ASN B N   1 
ATOM   791  C CA  . ASN A 1 123 ? 12.722  -7.502  6.708   1.00 101.87 ? 309 ASN B CA  1 
ATOM   792  C C   . ASN A 1 123 ? 14.001  -8.047  7.332   1.00 100.56 ? 309 ASN B C   1 
ATOM   793  O O   . ASN A 1 123 ? 13.969  -9.039  8.071   1.00 98.66  ? 309 ASN B O   1 
ATOM   794  C CB  . ASN A 1 123 ? 12.510  -8.074  5.307   1.00 94.47  ? 309 ASN B CB  1 
ATOM   795  C CG  . ASN A 1 123 ? 11.988  -9.488  5.328   1.00 104.59 ? 309 ASN B CG  1 
ATOM   796  O OD1 . ASN A 1 123 ? 11.506  -9.968  6.352   1.00 107.38 ? 309 ASN B OD1 1 
ATOM   797  N ND2 . ASN A 1 123 ? 12.075  -10.167 4.189   1.00 101.19 ? 309 ASN B ND2 1 
ATOM   798  N N   . LYS A 1 124 ? 15.136  -7.404  7.047   1.00 98.26  ? 310 LYS B N   1 
ATOM   799  C CA  . LYS A 1 124 ? 16.402  -7.805  7.651   1.00 97.47  ? 310 LYS B CA  1 
ATOM   800  C C   . LYS A 1 124 ? 16.402  -7.560  9.155   1.00 101.38 ? 310 LYS B C   1 
ATOM   801  O O   . LYS A 1 124 ? 16.983  -8.343  9.916   1.00 107.85 ? 310 LYS B O   1 
ATOM   802  C CB  . LYS A 1 124 ? 17.560  -7.055  6.990   1.00 99.52  ? 310 LYS B CB  1 
ATOM   803  C CG  . LYS A 1 124 ? 18.930  -7.611  7.336   1.00 98.65  ? 310 LYS B CG  1 
ATOM   804  C CD  . LYS A 1 124 ? 19.101  -8.992  6.730   1.00 98.70  ? 310 LYS B CD  1 
ATOM   805  C CE  . LYS A 1 124 ? 20.413  -9.629  7.133   1.00 100.11 ? 310 LYS B CE  1 
ATOM   806  N NZ  . LYS A 1 124 ? 20.620  -10.929 6.436   1.00 110.53 ? 310 LYS B NZ  1 
ATOM   807  N N   . MET A 1 125 ? 15.766  -6.475  9.603   1.00 102.43 ? 311 MET B N   1 
ATOM   808  C CA  . MET A 1 125 ? 15.727  -6.128  11.020  1.00 104.62 ? 311 MET B CA  1 
ATOM   809  C C   . MET A 1 125 ? 14.750  -6.971  11.833  1.00 111.88 ? 311 MET B C   1 
ATOM   810  O O   . MET A 1 125 ? 14.714  -6.821  13.059  1.00 110.63 ? 311 MET B O   1 
ATOM   811  C CB  . MET A 1 125 ? 15.370  -4.651  11.206  1.00 101.15 ? 311 MET B CB  1 
ATOM   812  C CG  . MET A 1 125 ? 16.330  -3.677  10.552  1.00 103.34 ? 311 MET B CG  1 
ATOM   813  S SD  . MET A 1 125 ? 15.901  -1.965  10.929  1.00 109.84 ? 311 MET B SD  1 
ATOM   814  C CE  . MET A 1 125 ? 14.106  -2.031  10.825  1.00 98.30  ? 311 MET B CE  1 
ATOM   815  N N   . LYS A 1 126 ? 13.943  -7.821  11.198  1.00 108.47 ? 312 LYS B N   1 
ATOM   816  C CA  . LYS A 1 126 ? 13.043  -8.683  11.953  1.00 104.41 ? 312 LYS B CA  1 
ATOM   817  C C   . LYS A 1 126 ? 13.833  -9.606  12.870  1.00 113.57 ? 312 LYS B C   1 
ATOM   818  O O   . LYS A 1 126 ? 14.829  -10.211 12.460  1.00 118.90 ? 312 LYS B O   1 
ATOM   819  C CB  . LYS A 1 126 ? 12.169  -9.504  11.006  1.00 110.35 ? 312 LYS B CB  1 
ATOM   820  C CG  . LYS A 1 126 ? 11.150  -8.688  10.224  1.00 118.64 ? 312 LYS B CG  1 
ATOM   821  C CD  . LYS A 1 126 ? 10.344  -9.568  9.282   1.00 108.75 ? 312 LYS B CD  1 
ATOM   822  C CE  . LYS A 1 126 ? 9.326   -8.755  8.510   1.00 102.43 ? 312 LYS B CE  1 
ATOM   823  N NZ  . LYS A 1 126 ? 8.562   -9.609  7.563   1.00 104.49 ? 312 LYS B NZ  1 
ATOM   824  N N   . GLY A 1 127 ? 13.386  -9.708  14.118  1.00 115.74 ? 313 GLY B N   1 
ATOM   825  C CA  . GLY A 1 127 ? 14.087  -10.504 15.100  1.00 109.29 ? 313 GLY B CA  1 
ATOM   826  C C   . GLY A 1 127 ? 15.264  -9.817  15.748  1.00 110.81 ? 313 GLY B C   1 
ATOM   827  O O   . GLY A 1 127 ? 16.024  -10.477 16.466  1.00 123.87 ? 313 GLY B O   1 
ATOM   828  N N   . THR A 1 128 ? 15.438  -8.516  15.530  1.00 109.18 ? 314 THR B N   1 
ATOM   829  C CA  . THR A 1 128 ? 16.576  -7.779  16.062  1.00 115.28 ? 314 THR B CA  1 
ATOM   830  C C   . THR A 1 128 ? 16.132  -6.762  17.107  1.00 108.67 ? 314 THR B C   1 
ATOM   831  O O   . THR A 1 128 ? 14.940  -6.520  17.318  1.00 107.69 ? 314 THR B O   1 
ATOM   832  C CB  . THR A 1 128 ? 17.330  -7.072  14.929  1.00 113.89 ? 314 THR B CB  1 
ATOM   833  O OG1 . THR A 1 128 ? 16.574  -5.938  14.482  1.00 110.45 ? 314 THR B OG1 1 
ATOM   834  C CG2 . THR A 1 128 ? 17.527  -8.027  13.762  1.00 108.64 ? 314 THR B CG2 1 
ATOM   835  N N   . CYS A 1 129 ? 17.131  -6.159  17.764  1.00 109.28 ? 315 CYS B N   1 
ATOM   836  C CA  . CYS A 1 129 ? 16.874  -5.119  18.756  1.00 105.11 ? 315 CYS B CA  1 
ATOM   837  C C   . CYS A 1 129 ? 16.366  -3.831  18.130  1.00 104.99 ? 315 CYS B C   1 
ATOM   838  O O   . CYS A 1 129 ? 15.719  -3.036  18.818  1.00 111.25 ? 315 CYS B O   1 
ATOM   839  C CB  . CYS A 1 129 ? 18.142  -4.818  19.559  1.00 105.81 ? 315 CYS B CB  1 
ATOM   840  S SG  . CYS A 1 129 ? 19.431  -3.919  18.651  1.00 93.16  ? 315 CYS B SG  1 
ATOM   841  N N   . VAL A 1 130 ? 16.657  -3.601  16.857  1.00 106.00 ? 316 VAL B N   1 
ATOM   842  C CA  . VAL A 1 130 ? 16.264  -2.379  16.183  1.00 100.05 ? 316 VAL B CA  1 
ATOM   843  C C   . VAL A 1 130 ? 15.045  -2.613  15.281  1.00 100.47 ? 316 VAL B C   1 
ATOM   844  O O   . VAL A 1 130 ? 14.706  -1.764  14.455  1.00 85.17  ? 316 VAL B O   1 
ATOM   845  C CB  . VAL A 1 130 ? 17.450  -1.775  15.410  1.00 92.61  ? 316 VAL B CB  1 
ATOM   846  C CG1 . VAL A 1 130 ? 17.680  -2.504  14.085  1.00 96.56  ? 316 VAL B CG1 1 
ATOM   847  C CG2 . VAL A 1 130 ? 17.286  -0.272  15.232  1.00 100.38 ? 316 VAL B CG2 1 
ATOM   848  N N   . GLU A 1 131 ? 14.347  -3.734  15.478  1.00 104.55 ? 317 GLU B N   1 
ATOM   849  C CA  . GLU A 1 131 ? 13.236  -4.123  14.615  1.00 103.09 ? 317 GLU B CA  1 
ATOM   850  C C   . GLU A 1 131 ? 12.109  -3.098  14.648  1.00 95.88  ? 317 GLU B C   1 
ATOM   851  O O   . GLU A 1 131 ? 11.807  -2.510  15.690  1.00 86.51  ? 317 GLU B O   1 
ATOM   852  C CB  . GLU A 1 131 ? 12.699  -5.494  15.034  1.00 108.03 ? 317 GLU B CB  1 
ATOM   853  C CG  . GLU A 1 131 ? 11.534  -6.006  14.199  1.00 106.01 ? 317 GLU B CG  1 
ATOM   854  C CD  . GLU A 1 131 ? 11.001  -7.325  14.711  1.00 112.39 ? 317 GLU B CD  1 
ATOM   855  O OE1 . GLU A 1 131 ? 11.071  -7.553  15.938  1.00 111.87 ? 317 GLU B OE1 1 
ATOM   856  O OE2 . GLU A 1 131 ? 10.530  -8.139  13.887  1.00 117.95 ? 317 GLU B OE2 1 
ATOM   857  N N   . GLY A 1 132 ? 11.491  -2.882  13.488  1.00 102.17 ? 318 GLY B N   1 
ATOM   858  C CA  . GLY A 1 132 ? 10.384  -1.961  13.380  1.00 85.46  ? 318 GLY B CA  1 
ATOM   859  C C   . GLY A 1 132 ? 10.780  -0.512  13.243  1.00 89.61  ? 318 GLY B C   1 
ATOM   860  O O   . GLY A 1 132 ? 9.928   0.364   13.425  1.00 90.55  ? 318 GLY B O   1 
ATOM   861  N N   . THR A 1 133 ? 12.049  -0.231  12.943  1.00 91.28  ? 319 THR B N   1 
ATOM   862  C CA  . THR A 1 133 ? 12.482  1.152   12.775  1.00 84.28  ? 319 THR B CA  1 
ATOM   863  C C   . THR A 1 133 ? 11.821  1.792   11.562  1.00 85.69  ? 319 THR B C   1 
ATOM   864  O O   . THR A 1 133 ? 11.376  2.945   11.626  1.00 88.02  ? 319 THR B O   1 
ATOM   865  C CB  . THR A 1 133 ? 14.006  1.212   12.656  1.00 91.31  ? 319 THR B CB  1 
ATOM   866  O OG1 . THR A 1 133 ? 14.601  0.883   13.921  1.00 82.15  ? 319 THR B OG1 1 
ATOM   867  C CG2 . THR A 1 133 ? 14.457  2.603   12.230  1.00 86.07  ? 319 THR B CG2 1 
ATOM   868  N N   . ILE A 1 134 ? 11.752  1.062   10.445  1.00 89.78  ? 320 ILE B N   1 
ATOM   869  C CA  . ILE A 1 134 ? 11.107  1.603   9.247   1.00 86.87  ? 320 ILE B CA  1 
ATOM   870  C C   . ILE A 1 134 ? 9.639   1.930   9.500   1.00 83.87  ? 320 ILE B C   1 
ATOM   871  O O   . ILE A 1 134 ? 9.216   3.051   9.175   1.00 83.37  ? 320 ILE B O   1 
ATOM   872  C CB  . ILE A 1 134 ? 11.317  0.653   8.054   1.00 89.63  ? 320 ILE B CB  1 
ATOM   873  C CG1 . ILE A 1 134 ? 12.663  0.917   7.364   1.00 94.80  ? 320 ILE B CG1 1 
ATOM   874  C CG2 . ILE A 1 134 ? 10.198  0.805   7.036   1.00 84.19  ? 320 ILE B CG2 1 
ATOM   875  C CD1 . ILE A 1 134 ? 13.886  0.468   8.154   1.00 89.45  ? 320 ILE B CD1 1 
ATOM   876  N N   . PRO A 1 135 ? 8.816   1.032   10.064  1.00 88.98  ? 321 PRO B N   1 
ATOM   877  C CA  . PRO A 1 135 ? 7.424   1.422   10.344  1.00 80.63  ? 321 PRO B CA  1 
ATOM   878  C C   . PRO A 1 135 ? 7.295   2.608   11.283  1.00 79.22  ? 321 PRO B C   1 
ATOM   879  O O   . PRO A 1 135 ? 6.415   3.452   11.076  1.00 88.54  ? 321 PRO B O   1 
ATOM   880  C CB  . PRO A 1 135 ? 6.822   0.148   10.951  1.00 80.92  ? 321 PRO B CB  1 
ATOM   881  C CG  . PRO A 1 135 ? 7.645   -0.946  10.416  1.00 81.51  ? 321 PRO B CG  1 
ATOM   882  C CD  . PRO A 1 135 ? 9.035   -0.398  10.352  1.00 98.25  ? 321 PRO B CD  1 
ATOM   883  N N   . LYS A 1 136 ? 8.148   2.712   12.304  1.00 79.81  ? 322 LYS B N   1 
ATOM   884  C CA  . LYS A 1 136 ? 8.004   3.811   13.253  1.00 85.05  ? 322 LYS B CA  1 
ATOM   885  C C   . LYS A 1 136 ? 8.483   5.145   12.693  1.00 85.28  ? 322 LYS B C   1 
ATOM   886  O O   . LYS A 1 136 ? 8.192   6.188   13.290  1.00 89.68  ? 322 LYS B O   1 
ATOM   887  C CB  . LYS A 1 136 ? 8.739   3.509   14.564  1.00 78.32  ? 322 LYS B CB  1 
ATOM   888  C CG  . LYS A 1 136 ? 10.185  3.962   14.601  1.00 85.12  ? 322 LYS B CG  1 
ATOM   889  C CD  . LYS A 1 136 ? 10.821  3.598   15.929  1.00 84.87  ? 322 LYS B CD  1 
ATOM   890  C CE  . LYS A 1 136 ? 10.077  4.266   17.076  1.00 85.04  ? 322 LYS B CE  1 
ATOM   891  N NZ  . LYS A 1 136 ? 10.675  3.929   18.396  1.00 102.80 ? 322 LYS B NZ  1 
ATOM   892  N N   . LEU A 1 137 ? 9.206   5.143   11.575  1.00 78.41  ? 323 LEU B N   1 
ATOM   893  C CA  . LEU A 1 137 ? 9.648   6.384   10.956  1.00 80.15  ? 323 LEU B CA  1 
ATOM   894  C C   . LEU A 1 137 ? 8.769   6.823   9.793   1.00 82.45  ? 323 LEU B C   1 
ATOM   895  O O   . LEU A 1 137 ? 8.540   8.025   9.630   1.00 76.99  ? 323 LEU B O   1 
ATOM   896  C CB  . LEU A 1 137 ? 11.098  6.253   10.471  1.00 76.20  ? 323 LEU B CB  1 
ATOM   897  C CG  . LEU A 1 137 ? 12.185  6.290   11.549  1.00 81.90  ? 323 LEU B CG  1 
ATOM   898  C CD1 . LEU A 1 137 ? 13.555  6.009   10.952  1.00 73.69  ? 323 LEU B CD1 1 
ATOM   899  C CD2 . LEU A 1 137 ? 12.178  7.637   12.252  1.00 80.04  ? 323 LEU B CD2 1 
ATOM   900  N N   . PHE A 1 138 ? 8.235   5.887   9.000   1.00 78.17  ? 324 PHE B N   1 
ATOM   901  C CA  . PHE A 1 138 ? 7.581   6.247   7.751   1.00 76.12  ? 324 PHE B CA  1 
ATOM   902  C C   . PHE A 1 138 ? 6.113   5.858   7.652   1.00 85.37  ? 324 PHE B C   1 
ATOM   903  O O   . PHE A 1 138 ? 5.421   6.405   6.789   1.00 95.18  ? 324 PHE B O   1 
ATOM   904  C CB  . PHE A 1 138 ? 8.306   5.614   6.550   1.00 82.32  ? 324 PHE B CB  1 
ATOM   905  C CG  . PHE A 1 138 ? 9.758   5.980   6.446   1.00 78.90  ? 324 PHE B CG  1 
ATOM   906  C CD1 . PHE A 1 138 ? 10.146  7.120   5.770   1.00 72.56  ? 324 PHE B CD1 1 
ATOM   907  C CD2 . PHE A 1 138 ? 10.731  5.174   7.007   1.00 77.96  ? 324 PHE B CD2 1 
ATOM   908  C CE1 . PHE A 1 138 ? 11.469  7.461   5.665   1.00 76.99  ? 324 PHE B CE1 1 
ATOM   909  C CE2 . PHE A 1 138 ? 12.062  5.508   6.907   1.00 81.18  ? 324 PHE B CE2 1 
ATOM   910  C CZ  . PHE A 1 138 ? 12.433  6.655   6.234   1.00 90.41  ? 324 PHE B CZ  1 
ATOM   911  N N   . ARG A 1 139 ? 5.614   4.940   8.477   1.00 86.21  ? 325 ARG B N   1 
ATOM   912  C CA  . ARG A 1 139 ? 4.246   4.466   8.302   1.00 89.70  ? 325 ARG B CA  1 
ATOM   913  C C   . ARG A 1 139 ? 3.273   5.257   9.172   1.00 96.12  ? 325 ARG B C   1 
ATOM   914  O O   . ARG A 1 139 ? 3.597   5.640   10.300  1.00 87.52  ? 325 ARG B O   1 
ATOM   915  C CB  . ARG A 1 139 ? 4.146   2.966   8.592   1.00 89.51  ? 325 ARG B CB  1 
ATOM   916  C CG  . ARG A 1 139 ? 2.835   2.345   8.123   1.00 98.48  ? 325 ARG B CG  1 
ATOM   917  C CD  . ARG A 1 139 ? 2.730   0.852   8.429   1.00 102.74 ? 325 ARG B CD  1 
ATOM   918  N NE  . ARG A 1 139 ? 2.583   0.546   9.845   1.00 106.79 ? 325 ARG B NE  1 
ATOM   919  C CZ  . ARG A 1 139 ? 2.476   -0.682  10.333  1.00 108.48 ? 325 ARG B CZ  1 
ATOM   920  N NH1 . ARG A 1 139 ? 2.487   -1.743  9.541   1.00 109.05 ? 325 ARG B NH1 1 
ATOM   921  N NH2 . ARG A 1 139 ? 2.364   -0.852  11.647  1.00 109.68 ? 325 ARG B NH2 1 
ATOM   922  N N   . GLY A 1 140 ? 2.074   5.495   8.627   1.00 90.95  ? 326 GLY B N   1 
ATOM   923  C CA  . GLY A 1 140 ? 1.035   6.212   9.338   1.00 86.61  ? 326 GLY B CA  1 
ATOM   924  C C   . GLY A 1 140 ? -0.311  5.532   9.182   1.00 88.42  ? 326 GLY B C   1 
ATOM   925  O O   . GLY A 1 140 ? -0.520  4.710   8.286   1.00 93.68  ? 326 GLY B O   1 
ATOM   926  N N   . LYS A 1 141 ? -1.230  5.895   10.072  1.00 78.20  ? 327 LYS B N   1 
ATOM   927  C CA  . LYS A 1 141 ? -2.564  5.313   10.092  1.00 83.77  ? 327 LYS B CA  1 
ATOM   928  C C   . LYS A 1 141 ? -3.547  6.206   9.346   1.00 87.16  ? 327 LYS B C   1 
ATOM   929  O O   . LYS A 1 141 ? -3.511  7.434   9.468   1.00 91.08  ? 327 LYS B O   1 
ATOM   930  C CB  . LYS A 1 141 ? -3.047  5.093   11.527  1.00 90.94  ? 327 LYS B CB  1 
ATOM   931  C CG  . LYS A 1 141 ? -2.264  4.040   12.306  1.00 83.55  ? 327 LYS B CG  1 
ATOM   932  C CD  . LYS A 1 141 ? -2.793  3.919   13.736  1.00 90.38  ? 327 LYS B CD  1 
ATOM   933  C CE  . LYS A 1 141 ? -2.029  2.874   14.542  1.00 97.56  ? 327 LYS B CE  1 
ATOM   934  N NZ  . LYS A 1 141 ? -2.503  2.771   15.958  1.00 96.47  ? 327 LYS B NZ  1 
ATOM   935  N N   . MET A 1 142 ? -4.412  5.576   8.558   1.00 91.16  ? 328 MET B N   1 
ATOM   936  C CA  . MET A 1 142 ? -5.366  6.280   7.719   1.00 83.43  ? 328 MET B CA  1 
ATOM   937  C C   . MET A 1 142 ? -6.642  5.455   7.630   1.00 88.21  ? 328 MET B C   1 
ATOM   938  O O   . MET A 1 142 ? -6.595  4.222   7.622   1.00 93.78  ? 328 MET B O   1 
ATOM   939  C CB  . MET A 1 142 ? -4.770  6.529   6.332   1.00 77.41  ? 328 MET B CB  1 
ATOM   940  C CG  . MET A 1 142 ? -5.694  7.183   5.343   1.00 77.35  ? 328 MET B CG  1 
ATOM   941  S SD  . MET A 1 142 ? -4.934  7.203   3.710   1.00 82.12  ? 328 MET B SD  1 
ATOM   942  C CE  . MET A 1 142 ? -3.541  8.300   3.977   1.00 76.06  ? 328 MET B CE  1 
ATOM   943  N N   . VAL A 1 143 ? -7.782  6.138   7.569   1.00 89.13  ? 329 VAL B N   1 
ATOM   944  C CA  . VAL A 1 143 ? -9.082  5.486   7.445   1.00 86.57  ? 329 VAL B CA  1 
ATOM   945  C C   . VAL A 1 143 ? -9.730  5.902   6.131   1.00 82.31  ? 329 VAL B C   1 
ATOM   946  O O   . VAL A 1 143 ? -9.751  7.091   5.787   1.00 78.83  ? 329 VAL B O   1 
ATOM   947  C CB  . VAL A 1 143 ? -10.002 5.807   8.638   1.00 79.70  ? 329 VAL B CB  1 
ATOM   948  C CG1 . VAL A 1 143 ? -10.103 7.303   8.861   1.00 79.09  ? 329 VAL B CG1 1 
ATOM   949  C CG2 . VAL A 1 143 ? -11.373 5.204   8.413   1.00 80.41  ? 329 VAL B CG2 1 
ATOM   950  N N   . SER A 1 144 ? -10.227 4.917   5.387   1.00 82.24  ? 330 SER B N   1 
ATOM   951  C CA  . SER A 1 144 ? -11.005 5.139   4.176   1.00 80.95  ? 330 SER B CA  1 
ATOM   952  C C   . SER A 1 144 ? -12.453 4.759   4.458   1.00 87.59  ? 330 SER B C   1 
ATOM   953  O O   . SER A 1 144 ? -12.728 3.637   4.896   1.00 91.27  ? 330 SER B O   1 
ATOM   954  C CB  . SER A 1 144 ? -10.450 4.318   3.012   1.00 86.58  ? 330 SER B CB  1 
ATOM   955  O OG  . SER A 1 144 ? -11.189 4.560   1.829   1.00 88.37  ? 330 SER B OG  1 
ATOM   956  N N   . TYR A 1 145 ? -13.374 5.687   4.208   1.00 85.35  ? 331 TYR B N   1 
ATOM   957  C CA  . TYR A 1 145 ? -14.768 5.506   4.582   1.00 83.56  ? 331 TYR B CA  1 
ATOM   958  C C   . TYR A 1 145 ? -15.693 5.641   3.379   1.00 84.07  ? 331 TYR B C   1 
ATOM   959  O O   . TYR A 1 145 ? -15.414 6.386   2.435   1.00 81.88  ? 331 TYR B O   1 
ATOM   960  C CB  . TYR A 1 145 ? -15.181 6.513   5.668   1.00 84.11  ? 331 TYR B CB  1 
ATOM   961  C CG  . TYR A 1 145 ? -15.155 7.963   5.233   1.00 84.11  ? 331 TYR B CG  1 
ATOM   962  C CD1 . TYR A 1 145 ? -16.262 8.546   4.630   1.00 90.89  ? 331 TYR B CD1 1 
ATOM   963  C CD2 . TYR A 1 145 ? -14.033 8.754   5.446   1.00 81.02  ? 331 TYR B CD2 1 
ATOM   964  C CE1 . TYR A 1 145 ? -16.249 9.868   4.235   1.00 89.60  ? 331 TYR B CE1 1 
ATOM   965  C CE2 . TYR A 1 145 ? -14.013 10.083  5.058   1.00 85.68  ? 331 TYR B CE2 1 
ATOM   966  C CZ  . TYR A 1 145 ? -15.126 10.634  4.451   1.00 88.08  ? 331 TYR B CZ  1 
ATOM   967  O OH  . TYR A 1 145 ? -15.126 11.952  4.056   1.00 88.21  ? 331 TYR B OH  1 
ATOM   968  N N   . ILE A 1 146 ? -16.798 4.896   3.428   1.00 84.19  ? 332 ILE B N   1 
ATOM   969  C CA  . ILE A 1 146 ? -17.896 5.005   2.470   1.00 85.77  ? 332 ILE B CA  1 
ATOM   970  C C   . ILE A 1 146 ? -19.197 5.075   3.264   1.00 88.32  ? 332 ILE B C   1 
ATOM   971  O O   . ILE A 1 146 ? -19.560 4.109   3.946   1.00 91.75  ? 332 ILE B O   1 
ATOM   972  C CB  . ILE A 1 146 ? -17.931 3.827   1.480   1.00 83.20  ? 332 ILE B CB  1 
ATOM   973  C CG1 . ILE A 1 146 ? -16.610 3.717   0.722   1.00 85.43  ? 332 ILE B CG1 1 
ATOM   974  C CG2 . ILE A 1 146 ? -19.076 3.988   0.499   1.00 83.88  ? 332 ILE B CG2 1 
ATOM   975  C CD1 . ILE A 1 146 ? -16.532 2.507   -0.171  1.00 83.45  ? 332 ILE B CD1 1 
ATOM   976  N N   . GLN A 1 147 ? -19.894 6.210   3.178   1.00 89.82  ? 333 GLN B N   1 
ATOM   977  C CA  . GLN A 1 147 ? -21.097 6.472   3.967   1.00 88.55  ? 333 GLN B CA  1 
ATOM   978  C C   . GLN A 1 147 ? -22.305 6.645   3.056   1.00 88.27  ? 333 GLN B C   1 
ATOM   979  O O   . GLN A 1 147 ? -22.325 7.548   2.212   1.00 88.57  ? 333 GLN B O   1 
ATOM   980  C CB  . GLN A 1 147 ? -20.913 7.720   4.834   1.00 88.30  ? 333 GLN B CB  1 
ATOM   981  C CG  . GLN A 1 147 ? -22.170 8.170   5.568   1.00 83.54  ? 333 GLN B CG  1 
ATOM   982  C CD  . GLN A 1 147 ? -22.581 7.215   6.667   1.00 84.45  ? 333 GLN B CD  1 
ATOM   983  O OE1 . GLN A 1 147 ? -21.863 7.044   7.650   1.00 87.00  ? 333 GLN B OE1 1 
ATOM   984  N NE2 . GLN A 1 147 ? -23.752 6.603   6.519   1.00 84.43  ? 333 GLN B NE2 1 
ATOM   985  N N   . CYS A 1 148 ? -23.316 5.798   3.243   1.00 88.87  ? 334 CYS B N   1 
ATOM   986  C CA  . CYS A 1 148 ? -24.579 5.938   2.535   1.00 90.19  ? 334 CYS B CA  1 
ATOM   987  C C   . CYS A 1 148 ? -25.377 7.088   3.140   1.00 94.31  ? 334 CYS B C   1 
ATOM   988  O O   . CYS A 1 148 ? -25.330 7.324   4.350   1.00 98.04  ? 334 CYS B O   1 
ATOM   989  C CB  . CYS A 1 148 ? -25.381 4.635   2.614   1.00 90.26  ? 334 CYS B CB  1 
ATOM   990  S SG  . CYS A 1 148 ? -24.618 3.200   1.804   1.00 85.74  ? 334 CYS B SG  1 
ATOM   991  N N   . LYS A 1 149 ? -26.127 7.801   2.296   1.00 93.57  ? 335 LYS B N   1 
ATOM   992  C CA  . LYS A 1 149 ? -26.846 8.986   2.762   1.00 96.26  ? 335 LYS B CA  1 
ATOM   993  C C   . LYS A 1 149 ? -28.296 8.710   3.158   1.00 98.34  ? 335 LYS B C   1 
ATOM   994  O O   . LYS A 1 149 ? -28.791 9.316   4.111   1.00 102.52 ? 335 LYS B O   1 
ATOM   995  C CB  . LYS A 1 149 ? -26.818 10.092  1.695   1.00 100.58 ? 335 LYS B CB  1 
ATOM   996  C CG  . LYS A 1 149 ? -27.638 9.806   0.439   1.00 110.24 ? 335 LYS B CG  1 
ATOM   997  C CD  . LYS A 1 149 ? -27.573 10.960  -0.553  1.00 117.54 ? 335 LYS B CD  1 
ATOM   998  C CE  . LYS A 1 149 ? -28.394 10.662  -1.797  1.00 111.64 ? 335 LYS B CE  1 
ATOM   999  N NZ  . LYS A 1 149 ? -28.450 11.825  -2.722  1.00 105.18 ? 335 LYS B NZ  1 
ATOM   1000 N N   . GLU A 1 150 ? -28.996 7.820   2.454   1.00 96.49  ? 336 GLU B N   1 
ATOM   1001 C CA  . GLU A 1 150 ? -30.394 7.532   2.746   1.00 94.73  ? 336 GLU B CA  1 
ATOM   1002 C C   . GLU A 1 150 ? -30.586 6.282   3.592   1.00 91.96  ? 336 GLU B C   1 
ATOM   1003 O O   . GLU A 1 150 ? -31.537 6.222   4.383   1.00 96.96  ? 336 GLU B O   1 
ATOM   1004 C CB  . GLU A 1 150 ? -31.207 7.401   1.451   1.00 94.03  ? 336 GLU B CB  1 
ATOM   1005 C CG  . GLU A 1 150 ? -31.159 8.634   0.548   1.00 94.22  ? 336 GLU B CG  1 
ATOM   1006 C CD  . GLU A 1 150 ? -31.842 8.413   -0.795  1.00 109.76 ? 336 GLU B CD  1 
ATOM   1007 O OE1 . GLU A 1 150 ? -32.313 7.283   -1.041  1.00 114.53 ? 336 GLU B OE1 1 
ATOM   1008 O OE2 . GLU A 1 150 ? -31.914 9.365   -1.606  1.00 114.35 ? 336 GLU B OE2 1 
ATOM   1009 N N   . VAL A 1 151 ? -29.730 5.280   3.431   1.00 96.52  ? 337 VAL B N   1 
ATOM   1010 C CA  . VAL A 1 151 ? -29.768 4.064   4.236   1.00 99.67  ? 337 VAL B CA  1 
ATOM   1011 C C   . VAL A 1 151 ? -28.670 4.125   5.294   1.00 94.56  ? 337 VAL B C   1 
ATOM   1012 O O   . VAL A 1 151 ? -27.661 4.822   5.140   1.00 89.18  ? 337 VAL B O   1 
ATOM   1013 C CB  . VAL A 1 151 ? -29.635 2.820   3.329   1.00 96.00  ? 337 VAL B CB  1 
ATOM   1014 C CG1 . VAL A 1 151 ? -29.758 1.530   4.126   1.00 96.26  ? 337 VAL B CG1 1 
ATOM   1015 C CG2 . VAL A 1 151 ? -30.687 2.870   2.245   1.00 88.05  ? 337 VAL B CG2 1 
ATOM   1016 N N   . ASP A 1 152 ? -28.888 3.404   6.396   1.00 99.13  ? 338 ASP B N   1 
ATOM   1017 C CA  . ASP A 1 152 ? -28.016 3.433   7.575   1.00 107.81 ? 338 ASP B CA  1 
ATOM   1018 C C   . ASP A 1 152 ? -26.905 2.385   7.444   1.00 103.19 ? 338 ASP B C   1 
ATOM   1019 O O   . ASP A 1 152 ? -26.899 1.342   8.101   1.00 101.17 ? 338 ASP B O   1 
ATOM   1020 C CB  . ASP A 1 152 ? -28.854 3.198   8.828   1.00 117.35 ? 338 ASP B CB  1 
ATOM   1021 C CG  . ASP A 1 152 ? -28.098 3.459   10.114  1.00 131.60 ? 338 ASP B CG  1 
ATOM   1022 O OD1 . ASP A 1 152 ? -26.863 3.648   10.072  1.00 137.89 ? 338 ASP B OD1 1 
ATOM   1023 O OD2 . ASP A 1 152 ? -28.752 3.443   11.179  1.00 132.12 ? 338 ASP B OD2 1 
ATOM   1024 N N   . TYR A 1 153 ? -25.942 2.678   6.573   1.00 92.90  ? 339 TYR B N   1 
ATOM   1025 C CA  . TYR A 1 153 ? -24.773 1.817   6.456   1.00 92.52  ? 339 TYR B CA  1 
ATOM   1026 C C   . TYR A 1 153 ? -23.519 2.647   6.220   1.00 89.46  ? 339 TYR B C   1 
ATOM   1027 O O   . TYR A 1 153 ? -23.555 3.651   5.504   1.00 86.41  ? 339 TYR B O   1 
ATOM   1028 C CB  . TYR A 1 153 ? -24.946 0.783   5.335   1.00 91.80  ? 339 TYR B CB  1 
ATOM   1029 C CG  . TYR A 1 153 ? -23.759 -0.144  5.182   1.00 88.09  ? 339 TYR B CG  1 
ATOM   1030 C CD1 . TYR A 1 153 ? -23.587 -1.232  6.031   1.00 86.69  ? 339 TYR B CD1 1 
ATOM   1031 C CD2 . TYR A 1 153 ? -22.816 0.064   4.188   1.00 85.91  ? 339 TYR B CD2 1 
ATOM   1032 C CE1 . TYR A 1 153 ? -22.504 -2.079  5.897   1.00 88.99  ? 339 TYR B CE1 1 
ATOM   1033 C CE2 . TYR A 1 153 ? -21.730 -0.779  4.047   1.00 85.95  ? 339 TYR B CE2 1 
ATOM   1034 C CZ  . TYR A 1 153 ? -21.578 -1.849  4.903   1.00 89.71  ? 339 TYR B CZ  1 
ATOM   1035 O OH  . TYR A 1 153 ? -20.495 -2.689  4.764   1.00 88.77  ? 339 TYR B OH  1 
ATOM   1036 N N   . ARG A 1 154 ? -22.413 2.212   6.829   1.00 85.55  ? 340 ARG B N   1 
ATOM   1037 C CA  . ARG A 1 154 ? -21.106 2.835   6.674   1.00 84.40  ? 340 ARG B CA  1 
ATOM   1038 C C   . ARG A 1 154 ? -20.050 1.739   6.714   1.00 84.48  ? 340 ARG B C   1 
ATOM   1039 O O   . ARG A 1 154 ? -20.214 0.731   7.405   1.00 85.54  ? 340 ARG B O   1 
ATOM   1040 C CB  . ARG A 1 154 ? -20.832 3.877   7.770   1.00 84.04  ? 340 ARG B CB  1 
ATOM   1041 C CG  . ARG A 1 154 ? -19.547 4.684   7.588   1.00 83.31  ? 340 ARG B CG  1 
ATOM   1042 C CD  . ARG A 1 154 ? -19.276 5.554   8.805   1.00 83.05  ? 340 ARG B CD  1 
ATOM   1043 N NE  . ARG A 1 154 ? -18.125 6.429   8.628   1.00 82.34  ? 340 ARG B NE  1 
ATOM   1044 C CZ  . ARG A 1 154 ? -18.204 7.695   8.241   1.00 81.99  ? 340 ARG B CZ  1 
ATOM   1045 N NH1 . ARG A 1 154 ? -19.369 8.268   7.989   1.00 82.33  ? 340 ARG B NH1 1 
ATOM   1046 N NH2 . ARG A 1 154 ? -17.088 8.404   8.102   1.00 81.35  ? 340 ARG B NH2 1 
ATOM   1047 N N   . SER A 1 155 ? -18.969 1.932   5.960   1.00 84.04  ? 341 SER B N   1 
ATOM   1048 C CA  . SER A 1 155 ? -17.874 0.966   5.912   1.00 87.47  ? 341 SER B CA  1 
ATOM   1049 C C   . SER A 1 155 ? -16.572 1.689   6.232   1.00 83.45  ? 341 SER B C   1 
ATOM   1050 O O   . SER A 1 155 ? -16.092 2.499   5.431   1.00 82.90  ? 341 SER B O   1 
ATOM   1051 C CB  . SER A 1 155 ? -17.800 0.275   4.551   1.00 84.40  ? 341 SER B CB  1 
ATOM   1052 O OG  . SER A 1 155 ? -16.735 -0.660  4.521   1.00 84.60  ? 341 SER B OG  1 
ATOM   1053 N N   . ASP A 1 156 ? -16.004 1.392   7.398   1.00 83.53  ? 342 ASP B N   1 
ATOM   1054 C CA  . ASP A 1 156 ? -14.738 1.957   7.843   1.00 85.99  ? 342 ASP B CA  1 
ATOM   1055 C C   . ASP A 1 156 ? -13.680 0.867   7.828   1.00 91.61  ? 342 ASP B C   1 
ATOM   1056 O O   . ASP A 1 156 ? -13.840 -0.167  8.485   1.00 95.78  ? 342 ASP B O   1 
ATOM   1057 C CB  . ASP A 1 156 ? -14.866 2.560   9.241   1.00 82.88  ? 342 ASP B CB  1 
ATOM   1058 C CG  . ASP A 1 156 ? -15.596 3.880   9.237   1.00 83.73  ? 342 ASP B CG  1 
ATOM   1059 O OD1 . ASP A 1 156 ? -15.536 4.577   8.202   1.00 82.80  ? 342 ASP B OD1 1 
ATOM   1060 O OD2 . ASP A 1 156 ? -16.246 4.211   10.251  1.00 88.85  ? 342 ASP B OD2 1 
ATOM   1061 N N   . ARG A 1 157 ? -12.609 1.097   7.075   1.00 88.37  ? 343 ARG B N   1 
ATOM   1062 C CA  . ARG A 1 157 ? -11.470 0.193   7.035   1.00 95.74  ? 343 ARG B CA  1 
ATOM   1063 C C   . ARG A 1 157 ? -10.183 0.981   7.229   1.00 101.19 ? 343 ARG B C   1 
ATOM   1064 O O   . ARG A 1 157 ? -10.021 2.076   6.680   1.00 91.26  ? 343 ARG B O   1 
ATOM   1065 C CB  . ARG A 1 157 ? -11.449 -0.599  5.729   1.00 95.30  ? 343 ARG B CB  1 
ATOM   1066 C CG  . ARG A 1 157 ? -11.534 0.265   4.497   1.00 103.21 ? 343 ARG B CG  1 
ATOM   1067 C CD  . ARG A 1 157 ? -11.710 -0.584  3.260   1.00 101.59 ? 343 ARG B CD  1 
ATOM   1068 N NE  . ARG A 1 157 ? -11.641 0.218   2.048   1.00 103.46 ? 343 ARG B NE  1 
ATOM   1069 C CZ  . ARG A 1 157 ? -10.510 0.536   1.436   1.00 98.16  ? 343 ARG B CZ  1 
ATOM   1070 N NH1 . ARG A 1 157 ? -9.339  0.153   1.913   1.00 105.26 ? 343 ARG B NH1 1 
ATOM   1071 N NH2 . ARG A 1 157 ? -10.557 1.258   0.320   1.00 105.11 ? 343 ARG B NH2 1 
ATOM   1072 N N   . ARG A 1 158 ? -9.272  0.408   8.011   1.00 113.84 ? 344 ARG B N   1 
ATOM   1073 C CA  . ARG A 1 158 ? -7.999  1.038   8.331   1.00 114.53 ? 344 ARG B CA  1 
ATOM   1074 C C   . ARG A 1 158 ? -6.966  0.722   7.259   1.00 117.45 ? 344 ARG B C   1 
ATOM   1075 O O   . ARG A 1 158 ? -6.850  -0.421  6.806   1.00 122.85 ? 344 ARG B O   1 
ATOM   1076 C CB  . ARG A 1 158 ? -7.492  0.542   9.689   1.00 129.39 ? 344 ARG B CB  1 
ATOM   1077 C CG  . ARG A 1 158 ? -6.128  1.085   10.104  1.00 140.28 ? 344 ARG B CG  1 
ATOM   1078 C CD  . ARG A 1 158 ? -5.727  0.573   11.491  1.00 148.49 ? 344 ARG B CD  1 
ATOM   1079 N NE  . ARG A 1 158 ? -5.531  -0.874  11.491  1.00 138.15 ? 344 ARG B NE  1 
ATOM   1080 C CZ  . ARG A 1 158 ? -4.460  -1.486  11.001  1.00 140.16 ? 344 ARG B CZ  1 
ATOM   1081 N NH1 . ARG A 1 158 ? -3.465  -0.808  10.451  1.00 127.57 ? 344 ARG B NH1 1 
ATOM   1082 N NH2 . ARG A 1 158 ? -4.397  -2.815  11.041  1.00 140.28 ? 344 ARG B NH2 1 
ATOM   1083 N N   . GLU A 1 159 ? -6.215  1.741   6.855   1.00 101.30 ? 345 GLU B N   1 
ATOM   1084 C CA  . GLU A 1 159 ? -5.113  1.568   5.923   1.00 96.93  ? 345 GLU B CA  1 
ATOM   1085 C C   . GLU A 1 159 ? -3.809  2.073   6.526   1.00 101.01 ? 345 GLU B C   1 
ATOM   1086 O O   . GLU A 1 159 ? -3.798  2.949   7.396   1.00 99.34  ? 345 GLU B O   1 
ATOM   1087 C CB  . GLU A 1 159 ? -5.374  2.292   4.597   1.00 84.49  ? 345 GLU B CB  1 
ATOM   1088 C CG  . GLU A 1 159 ? -6.561  1.768   3.820   1.00 85.95  ? 345 GLU B CG  1 
ATOM   1089 C CD  . GLU A 1 159 ? -6.596  2.294   2.401   1.00 82.53  ? 345 GLU B CD  1 
ATOM   1090 O OE1 . GLU A 1 159 ? -5.519  2.407   1.780   1.00 89.69  ? 345 GLU B OE1 1 
ATOM   1091 O OE2 . GLU A 1 159 ? -7.699  2.599   1.904   1.00 97.47  ? 345 GLU B OE2 1 
ATOM   1092 N N   . ASP A 1 160 ? -2.710  1.490   6.061   1.00 96.65  ? 346 ASP B N   1 
ATOM   1093 C CA  . ASP A 1 160 ? -1.370  1.950   6.378   1.00 90.65  ? 346 ASP B CA  1 
ATOM   1094 C C   . ASP A 1 160 ? -0.743  2.538   5.121   1.00 89.22  ? 346 ASP B C   1 
ATOM   1095 O O   . ASP A 1 160 ? -1.024  2.095   4.003   1.00 85.78  ? 346 ASP B O   1 
ATOM   1096 C CB  . ASP A 1 160 ? -0.498  0.811   6.914   1.00 95.98  ? 346 ASP B CB  1 
ATOM   1097 C CG  . ASP A 1 160 ? -0.817  0.449   8.356   1.00 102.16 ? 346 ASP B CG  1 
ATOM   1098 O OD1 . ASP A 1 160 ? -1.436  1.279   9.059   1.00 102.70 ? 346 ASP B OD1 1 
ATOM   1099 O OD2 . ASP A 1 160 ? -0.433  -0.659  8.789   1.00 101.59 ? 346 ASP B OD2 1 
ATOM   1100 N N   . TYR A 1 161 ? 0.101   3.550   5.309   1.00 90.53  ? 347 TYR B N   1 
ATOM   1101 C CA  . TYR A 1 161 ? 0.783   4.189   4.195   1.00 89.31  ? 347 TYR B CA  1 
ATOM   1102 C C   . TYR A 1 161 ? 2.219   4.507   4.585   1.00 91.75  ? 347 TYR B C   1 
ATOM   1103 O O   . TYR A 1 161 ? 2.511   4.823   5.741   1.00 88.87  ? 347 TYR B O   1 
ATOM   1104 C CB  . TYR A 1 161 ? 0.054   5.468   3.746   1.00 82.47  ? 347 TYR B CB  1 
ATOM   1105 C CG  . TYR A 1 161 ? 0.020   6.571   4.783   1.00 79.25  ? 347 TYR B CG  1 
ATOM   1106 C CD1 . TYR A 1 161 ? -0.973  6.610   5.751   1.00 81.41  ? 347 TYR B CD1 1 
ATOM   1107 C CD2 . TYR A 1 161 ? 0.976   7.575   4.789   1.00 81.40  ? 347 TYR B CD2 1 
ATOM   1108 C CE1 . TYR A 1 161 ? -1.010  7.619   6.699   1.00 83.39  ? 347 TYR B CE1 1 
ATOM   1109 C CE2 . TYR A 1 161 ? 0.947   8.588   5.733   1.00 80.55  ? 347 TYR B CE2 1 
ATOM   1110 C CZ  . TYR A 1 161 ? -0.046  8.605   6.686   1.00 79.54  ? 347 TYR B CZ  1 
ATOM   1111 O OH  . TYR A 1 161 ? -0.074  9.610   7.627   1.00 76.66  ? 347 TYR B OH  1 
ATOM   1112 N N   . TYR A 1 162 ? 3.114   4.415   3.601   1.00 91.34  ? 348 TYR B N   1 
ATOM   1113 C CA  . TYR A 1 162 ? 4.493   4.860   3.740   1.00 80.92  ? 348 TYR B CA  1 
ATOM   1114 C C   . TYR A 1 162 ? 4.804   6.091   2.903   1.00 82.64  ? 348 TYR B C   1 
ATOM   1115 O O   . TYR A 1 162 ? 5.889   6.666   3.050   1.00 85.76  ? 348 TYR B O   1 
ATOM   1116 C CB  . TYR A 1 162 ? 5.456   3.731   3.350   1.00 85.45  ? 348 TYR B CB  1 
ATOM   1117 C CG  . TYR A 1 162 ? 5.552   2.631   4.378   1.00 91.28  ? 348 TYR B CG  1 
ATOM   1118 C CD1 . TYR A 1 162 ? 4.694   1.539   4.340   1.00 95.18  ? 348 TYR B CD1 1 
ATOM   1119 C CD2 . TYR A 1 162 ? 6.501   2.684   5.387   1.00 91.15  ? 348 TYR B CD2 1 
ATOM   1120 C CE1 . TYR A 1 162 ? 4.781   0.528   5.281   1.00 96.15  ? 348 TYR B CE1 1 
ATOM   1121 C CE2 . TYR A 1 162 ? 6.597   1.680   6.330   1.00 93.74  ? 348 TYR B CE2 1 
ATOM   1122 C CZ  . TYR A 1 162 ? 5.735   0.604   6.274   1.00 99.38  ? 348 TYR B CZ  1 
ATOM   1123 O OH  . TYR A 1 162 ? 5.831   -0.398  7.216   1.00 109.70 ? 348 TYR B OH  1 
ATOM   1124 N N   . ASP A 1 163 ? 3.882   6.506   2.040   1.00 79.66  ? 349 ASP B N   1 
ATOM   1125 C CA  . ASP A 1 163 ? 4.081   7.652   1.170   1.00 74.02  ? 349 ASP B CA  1 
ATOM   1126 C C   . ASP A 1 163 ? 2.716   8.162   0.736   1.00 74.22  ? 349 ASP B C   1 
ATOM   1127 O O   . ASP A 1 163 ? 1.728   7.422   0.738   1.00 74.97  ? 349 ASP B O   1 
ATOM   1128 C CB  . ASP A 1 163 ? 4.944   7.272   -0.034  1.00 74.14  ? 349 ASP B CB  1 
ATOM   1129 C CG  . ASP A 1 163 ? 4.526   5.947   -0.642  1.00 85.66  ? 349 ASP B CG  1 
ATOM   1130 O OD1 . ASP A 1 163 ? 3.852   5.160   0.056   1.00 90.75  ? 349 ASP B OD1 1 
ATOM   1131 O OD2 . ASP A 1 163 ? 4.882   5.677   -1.804  1.00 89.29  ? 349 ASP B OD2 1 
ATOM   1132 N N   . ILE A 1 164 ? 2.678   9.436   0.356   1.00 76.45  ? 350 ILE B N   1 
ATOM   1133 C CA  . ILE A 1 164 ? 1.449   10.126  -0.015  1.00 73.76  ? 350 ILE B CA  1 
ATOM   1134 C C   . ILE A 1 164 ? 1.639   10.723  -1.402  1.00 73.70  ? 350 ILE B C   1 
ATOM   1135 O O   . ILE A 1 164 ? 2.564   11.515  -1.618  1.00 73.02  ? 350 ILE B O   1 
ATOM   1136 C CB  . ILE A 1 164 ? 1.083   11.224  0.994   1.00 73.23  ? 350 ILE B CB  1 
ATOM   1137 C CG1 . ILE A 1 164 ? 0.836   10.616  2.370   1.00 73.43  ? 350 ILE B CG1 1 
ATOM   1138 C CG2 . ILE A 1 164 ? -0.153  11.979  0.529   1.00 73.52  ? 350 ILE B CG2 1 
ATOM   1139 C CD1 . ILE A 1 164 ? -0.378  9.731   2.413   1.00 81.92  ? 350 ILE B CD1 1 
ATOM   1140 N N   . GLN A 1 165 ? 0.770   10.352  -2.335  1.00 74.44  ? 351 GLN B N   1 
ATOM   1141 C CA  . GLN A 1 165 ? 0.796   10.894  -3.687  1.00 74.60  ? 351 GLN B CA  1 
ATOM   1142 C C   . GLN A 1 165 ? -0.184  12.058  -3.762  1.00 74.61  ? 351 GLN B C   1 
ATOM   1143 O O   . GLN A 1 165 ? -1.392  11.868  -3.589  1.00 81.60  ? 351 GLN B O   1 
ATOM   1144 C CB  . GLN A 1 165 ? 0.448   9.818   -4.714  1.00 75.53  ? 351 GLN B CB  1 
ATOM   1145 C CG  . GLN A 1 165 ? 1.430   8.656   -4.743  1.00 75.69  ? 351 GLN B CG  1 
ATOM   1146 C CD  . GLN A 1 165 ? 1.192   7.667   -3.620  1.00 76.17  ? 351 GLN B CD  1 
ATOM   1147 O OE1 . GLN A 1 165 ? 0.110   7.092   -3.507  1.00 85.52  ? 351 GLN B OE1 1 
ATOM   1148 N NE2 . GLN A 1 165 ? 2.196   7.478   -2.768  1.00 76.62  ? 351 GLN B NE2 1 
ATOM   1149 N N   . LEU A 1 166 ? 0.331   13.252  -4.034  1.00 74.16  ? 352 LEU B N   1 
ATOM   1150 C CA  . LEU A 1 166 ? -0.456  14.477  -3.976  1.00 74.09  ? 352 LEU B CA  1 
ATOM   1151 C C   . LEU A 1 166 ? -0.831  14.957  -5.371  1.00 74.72  ? 352 LEU B C   1 
ATOM   1152 O O   . LEU A 1 166 ? -0.005  14.953  -6.287  1.00 77.03  ? 352 LEU B O   1 
ATOM   1153 C CB  . LEU A 1 166 ? 0.307   15.582  -3.247  1.00 73.18  ? 352 LEU B CB  1 
ATOM   1154 C CG  . LEU A 1 166 ? 0.476   15.430  -1.739  1.00 72.65  ? 352 LEU B CG  1 
ATOM   1155 C CD1 . LEU A 1 166 ? 1.203   16.640  -1.182  1.00 79.54  ? 352 LEU B CD1 1 
ATOM   1156 C CD2 . LEU A 1 166 ? -0.874  15.259  -1.075  1.00 73.18  ? 352 LEU B CD2 1 
ATOM   1157 N N   . SER A 1 167 ? -2.087  15.368  -5.520  1.00 75.35  ? 353 SER B N   1 
ATOM   1158 C CA  . SER A 1 167 ? -2.546  15.978  -6.759  1.00 76.07  ? 353 SER B CA  1 
ATOM   1159 C C   . SER A 1 167 ? -1.981  17.389  -6.895  1.00 75.66  ? 353 SER B C   1 
ATOM   1160 O O   . SER A 1 167 ? -1.801  18.109  -5.909  1.00 75.01  ? 353 SER B O   1 
ATOM   1161 C CB  . SER A 1 167 ? -4.074  16.008  -6.795  1.00 76.92  ? 353 SER B CB  1 
ATOM   1162 O OG  . SER A 1 167 ? -4.546  16.529  -8.023  1.00 89.34  ? 353 SER B OG  1 
ATOM   1163 N N   . ILE A 1 168 ? -1.702  17.788  -8.137  1.00 76.12  ? 354 ILE B N   1 
ATOM   1164 C CA  . ILE A 1 168 ? -1.009  19.037  -8.432  1.00 75.80  ? 354 ILE B CA  1 
ATOM   1165 C C   . ILE A 1 168 ? -1.831  19.936  -9.347  1.00 76.83  ? 354 ILE B C   1 
ATOM   1166 O O   . ILE A 1 168 ? -1.976  21.135  -9.088  1.00 77.25  ? 354 ILE B O   1 
ATOM   1167 C CB  . ILE A 1 168 ? 0.387   18.774  -9.043  1.00 78.11  ? 354 ILE B CB  1 
ATOM   1168 C CG1 . ILE A 1 168 ? 1.315   18.068  -8.046  1.00 76.50  ? 354 ILE B CG1 1 
ATOM   1169 C CG2 . ILE A 1 168 ? 0.995   20.074  -9.560  1.00 75.21  ? 354 ILE B CG2 1 
ATOM   1170 C CD1 . ILE A 1 168 ? 2.397   18.963  -7.484  1.00 80.09  ? 354 ILE B CD1 1 
ATOM   1171 N N   . LYS A 1 169 ? -2.352  19.381  -10.441 1.00 77.98  ? 355 LYS B N   1 
ATOM   1172 C CA  . LYS A 1 169 ? -3.082  20.180  -11.416 1.00 78.98  ? 355 LYS B CA  1 
ATOM   1173 C C   . LYS A 1 169 ? -4.286  20.839  -10.754 1.00 79.36  ? 355 LYS B C   1 
ATOM   1174 O O   . LYS A 1 169 ? -5.140  20.159  -10.176 1.00 79.47  ? 355 LYS B O   1 
ATOM   1175 C CB  . LYS A 1 169 ? -3.517  19.303  -12.593 1.00 80.04  ? 355 LYS B CB  1 
ATOM   1176 C CG  . LYS A 1 169 ? -4.242  20.041  -13.704 1.00 81.39  ? 355 LYS B CG  1 
ATOM   1177 C CD  . LYS A 1 169 ? -3.355  21.090  -14.342 1.00 81.43  ? 355 LYS B CD  1 
ATOM   1178 C CE  . LYS A 1 169 ? -4.072  21.764  -15.495 1.00 82.98  ? 355 LYS B CE  1 
ATOM   1179 N NZ  . LYS A 1 169 ? -3.252  22.847  -16.103 1.00 84.05  ? 355 LYS B NZ  1 
ATOM   1180 N N   . GLY A 1 170 ? -4.327  22.167  -10.799 1.00 79.59  ? 356 GLY B N   1 
ATOM   1181 C CA  . GLY A 1 170 ? -5.388  22.927  -10.180 1.00 80.03  ? 356 GLY B CA  1 
ATOM   1182 C C   . GLY A 1 170 ? -5.162  23.284  -8.728  1.00 78.99  ? 356 GLY B C   1 
ATOM   1183 O O   . GLY A 1 170 ? -5.926  24.088  -8.180  1.00 91.21  ? 356 GLY B O   1 
ATOM   1184 N N   . LYS A 1 171 ? -4.144  22.723  -8.086  1.00 80.95  ? 357 LYS B N   1 
ATOM   1185 C CA  . LYS A 1 171 ? -3.815  23.028  -6.699  1.00 79.97  ? 357 LYS B CA  1 
ATOM   1186 C C   . LYS A 1 171 ? -2.534  23.848  -6.664  1.00 83.41  ? 357 LYS B C   1 
ATOM   1187 O O   . LYS A 1 171 ? -1.534  23.474  -7.290  1.00 89.17  ? 357 LYS B O   1 
ATOM   1188 C CB  . LYS A 1 171 ? -3.673  21.747  -5.871  1.00 79.30  ? 357 LYS B CB  1 
ATOM   1189 C CG  . LYS A 1 171 ? -5.008  21.061  -5.578  1.00 79.97  ? 357 LYS B CG  1 
ATOM   1190 C CD  . LYS A 1 171 ? -5.503  20.211  -6.745  1.00 80.83  ? 357 LYS B CD  1 
ATOM   1191 C CE  . LYS A 1 171 ? -6.934  19.736  -6.513  1.00 88.68  ? 357 LYS B CE  1 
ATOM   1192 N NZ  . LYS A 1 171 ? -7.430  18.805  -7.574  1.00 97.03  ? 357 LYS B NZ  1 
ATOM   1193 N N   . LYS A 1 172 ? -2.559  24.960  -5.931  1.00 75.81  ? 358 LYS B N   1 
ATOM   1194 C CA  . LYS A 1 172 ? -1.428  25.877  -5.961  1.00 84.76  ? 358 LYS B CA  1 
ATOM   1195 C C   . LYS A 1 172 ? -0.387  25.602  -4.883  1.00 80.40  ? 358 LYS B C   1 
ATOM   1196 O O   . LYS A 1 172 ? 0.793   25.909  -5.089  1.00 81.73  ? 358 LYS B O   1 
ATOM   1197 C CB  . LYS A 1 172 ? -1.923  27.319  -5.841  1.00 79.35  ? 358 LYS B CB  1 
ATOM   1198 C CG  . LYS A 1 172 ? -2.812  27.564  -4.649  1.00 82.46  ? 358 LYS B CG  1 
ATOM   1199 C CD  . LYS A 1 172 ? -3.525  28.903  -4.749  1.00 97.16  ? 358 LYS B CD  1 
ATOM   1200 C CE  . LYS A 1 172 ? -4.501  28.953  -5.925  1.00 98.69  ? 358 LYS B CE  1 
ATOM   1201 N NZ  . LYS A 1 172 ? -3.867  29.355  -7.222  1.00 88.71  ? 358 LYS B NZ  1 
ATOM   1202 N N   . ASN A 1 173 ? -0.779  25.031  -3.744  1.00 73.48  ? 359 ASN B N   1 
ATOM   1203 C CA  . ASN A 1 173 ? 0.174   24.734  -2.684  1.00 72.33  ? 359 ASN B CA  1 
ATOM   1204 C C   . ASN A 1 173 ? -0.221  23.435  -1.990  1.00 74.99  ? 359 ASN B C   1 
ATOM   1205 O O   . ASN A 1 173 ? -1.246  22.820  -2.303  1.00 73.86  ? 359 ASN B O   1 
ATOM   1206 C CB  . ASN A 1 173 ? 0.292   25.900  -1.695  1.00 75.87  ? 359 ASN B CB  1 
ATOM   1207 C CG  . ASN A 1 173 ? -1.035  26.303  -1.097  1.00 76.33  ? 359 ASN B CG  1 
ATOM   1208 O OD1 . ASN A 1 173 ? -1.874  25.461  -0.775  1.00 79.74  ? 359 ASN B OD1 1 
ATOM   1209 N ND2 . ASN A 1 173 ? -1.235  27.604  -0.944  1.00 81.03  ? 359 ASN B ND2 1 
ATOM   1210 N N   . ILE A 1 174 ? 0.613   23.020  -1.033  1.00 76.90  ? 360 ILE B N   1 
ATOM   1211 C CA  . ILE A 1 174 ? 0.393   21.754  -0.338  1.00 75.90  ? 360 ILE B CA  1 
ATOM   1212 C C   . ILE A 1 174 ? -0.909  21.784  0.454   1.00 71.90  ? 360 ILE B C   1 
ATOM   1213 O O   . ILE A 1 174 ? -1.612  20.770  0.551   1.00 72.35  ? 360 ILE B O   1 
ATOM   1214 C CB  . ILE A 1 174 ? 1.604   21.428  0.555   1.00 70.35  ? 360 ILE B CB  1 
ATOM   1215 C CG1 . ILE A 1 174 ? 2.758   20.929  -0.303  1.00 69.94  ? 360 ILE B CG1 1 
ATOM   1216 C CG2 . ILE A 1 174 ? 1.258   20.378  1.583   1.00 74.57  ? 360 ILE B CG2 1 
ATOM   1217 C CD1 . ILE A 1 174 ? 3.801   20.179  0.474   1.00 83.03  ? 360 ILE B CD1 1 
ATOM   1218 N N   . PHE A 1 175 ? -1.256  22.941  1.026   1.00 73.00  ? 361 PHE B N   1 
ATOM   1219 C CA  . PHE A 1 175 ? -2.503  23.052  1.782   1.00 74.79  ? 361 PHE B CA  1 
ATOM   1220 C C   . PHE A 1 175 ? -3.705  22.692  0.917   1.00 78.19  ? 361 PHE B C   1 
ATOM   1221 O O   . PHE A 1 175 ? -4.534  21.855  1.298   1.00 73.97  ? 361 PHE B O   1 
ATOM   1222 C CB  . PHE A 1 175 ? -2.654  24.463  2.353   1.00 72.62  ? 361 PHE B CB  1 
ATOM   1223 C CG  . PHE A 1 175 ? -4.033  24.760  2.870   1.00 80.41  ? 361 PHE B CG  1 
ATOM   1224 C CD1 . PHE A 1 175 ? -4.447  24.276  4.101   1.00 81.22  ? 361 PHE B CD1 1 
ATOM   1225 C CD2 . PHE A 1 175 ? -4.918  25.525  2.127   1.00 79.29  ? 361 PHE B CD2 1 
ATOM   1226 C CE1 . PHE A 1 175 ? -5.716  24.545  4.578   1.00 74.27  ? 361 PHE B CE1 1 
ATOM   1227 C CE2 . PHE A 1 175 ? -6.188  25.797  2.601   1.00 75.21  ? 361 PHE B CE2 1 
ATOM   1228 C CZ  . PHE A 1 175 ? -6.585  25.306  3.827   1.00 76.78  ? 361 PHE B CZ  1 
ATOM   1229 N N   . GLU A 1 176 ? -3.813  23.313  -0.261  1.00 76.04  ? 362 GLU B N   1 
ATOM   1230 C CA  . GLU A 1 176 ? -4.886  22.960  -1.184  1.00 75.03  ? 362 GLU B CA  1 
ATOM   1231 C C   . GLU A 1 176 ? -4.757  21.515  -1.640  1.00 75.00  ? 362 GLU B C   1 
ATOM   1232 O O   . GLU A 1 176 ? -5.764  20.824  -1.836  1.00 75.67  ? 362 GLU B O   1 
ATOM   1233 C CB  . GLU A 1 176 ? -4.877  23.892  -2.395  1.00 75.60  ? 362 GLU B CB  1 
ATOM   1234 C CG  . GLU A 1 176 ? -5.402  25.289  -2.130  1.00 77.01  ? 362 GLU B CG  1 
ATOM   1235 C CD  . GLU A 1 176 ? -5.666  26.058  -3.410  1.00 83.17  ? 362 GLU B CD  1 
ATOM   1236 O OE1 . GLU A 1 176 ? -5.207  25.604  -4.478  1.00 86.03  ? 362 GLU B OE1 1 
ATOM   1237 O OE2 . GLU A 1 176 ? -6.345  27.106  -3.352  1.00 96.22  ? 362 GLU B OE2 1 
ATOM   1238 N N   . SER A 1 177 ? -3.522  21.043  -1.817  1.00 74.84  ? 363 SER B N   1 
ATOM   1239 C CA  . SER A 1 177 ? -3.317  19.663  -2.237  1.00 74.29  ? 363 SER B CA  1 
ATOM   1240 C C   . SER A 1 177 ? -3.868  18.684  -1.208  1.00 76.64  ? 363 SER B C   1 
ATOM   1241 O O   . SER A 1 177 ? -4.498  17.682  -1.567  1.00 74.87  ? 363 SER B O   1 
ATOM   1242 C CB  . SER A 1 177 ? -1.834  19.406  -2.479  1.00 73.51  ? 363 SER B CB  1 
ATOM   1243 O OG  . SER A 1 177 ? -1.649  18.105  -3.001  1.00 73.71  ? 363 SER B OG  1 
ATOM   1244 N N   . PHE A 1 178 ? -3.627  18.950  0.078   1.00 76.72  ? 364 PHE B N   1 
ATOM   1245 C CA  . PHE A 1 178 ? -4.142  18.073  1.122   1.00 73.89  ? 364 PHE B CA  1 
ATOM   1246 C C   . PHE A 1 178 ? -5.655  18.183  1.251   1.00 74.72  ? 364 PHE B C   1 
ATOM   1247 O O   . PHE A 1 178 ? -6.333  17.182  1.515   1.00 75.12  ? 364 PHE B O   1 
ATOM   1248 C CB  . PHE A 1 178 ? -3.466  18.385  2.453   1.00 73.21  ? 364 PHE B CB  1 
ATOM   1249 C CG  . PHE A 1 178 ? -2.289  17.508  2.748   1.00 72.64  ? 364 PHE B CG  1 
ATOM   1250 C CD1 . PHE A 1 178 ? -2.469  16.231  3.250   1.00 72.91  ? 364 PHE B CD1 1 
ATOM   1251 C CD2 . PHE A 1 178 ? -1.003  17.962  2.538   1.00 72.25  ? 364 PHE B CD2 1 
ATOM   1252 C CE1 . PHE A 1 178 ? -1.388  15.419  3.523   1.00 72.53  ? 364 PHE B CE1 1 
ATOM   1253 C CE2 . PHE A 1 178 ? 0.087   17.154  2.816   1.00 76.12  ? 364 PHE B CE2 1 
ATOM   1254 C CZ  . PHE A 1 178 ? -0.109  15.880  3.309   1.00 71.79  ? 364 PHE B CZ  1 
ATOM   1255 N N   . VAL A 1 179 ? -6.203  19.388  1.078   1.00 75.91  ? 365 VAL B N   1 
ATOM   1256 C CA  . VAL A 1 179 ? -7.655  19.554  1.125   1.00 75.90  ? 365 VAL B CA  1 
ATOM   1257 C C   . VAL A 1 179 ? -8.317  18.680  0.070   1.00 76.57  ? 365 VAL B C   1 
ATOM   1258 O O   . VAL A 1 179 ? -9.347  18.044  0.323   1.00 80.24  ? 365 VAL B O   1 
ATOM   1259 C CB  . VAL A 1 179 ? -8.031  21.039  0.956   1.00 76.25  ? 365 VAL B CB  1 
ATOM   1260 C CG1 . VAL A 1 179 ? -9.523  21.193  0.755   1.00 77.29  ? 365 VAL B CG1 1 
ATOM   1261 C CG2 . VAL A 1 179 ? -7.583  21.840  2.168   1.00 75.72  ? 365 VAL B CG2 1 
ATOM   1262 N N   . ASP A 1 180 ? -7.723  18.621  -1.124  1.00 76.57  ? 366 ASP B N   1 
ATOM   1263 C CA  . ASP A 1 180 ? -8.247  17.760  -2.178  1.00 77.24  ? 366 ASP B CA  1 
ATOM   1264 C C   . ASP A 1 180 ? -8.160  16.289  -1.798  1.00 77.11  ? 366 ASP B C   1 
ATOM   1265 O O   . ASP A 1 180 ? -9.028  15.498  -2.181  1.00 77.76  ? 366 ASP B O   1 
ATOM   1266 C CB  . ASP A 1 180 ? -7.495  18.016  -3.482  1.00 77.29  ? 366 ASP B CB  1 
ATOM   1267 C CG  . ASP A 1 180 ? -7.935  17.093  -4.599  1.00 78.02  ? 366 ASP B CG  1 
ATOM   1268 O OD1 . ASP A 1 180 ? -9.086  17.235  -5.060  1.00 83.24  ? 366 ASP B OD1 1 
ATOM   1269 O OD2 . ASP A 1 180 ? -7.131  16.239  -5.025  1.00 85.09  ? 366 ASP B OD2 1 
ATOM   1270 N N   . TYR A 1 181 ? -7.111  15.899  -1.073  1.00 76.33  ? 367 TYR B N   1 
ATOM   1271 C CA  . TYR A 1 181 ? -6.967  14.504  -0.665  1.00 76.32  ? 367 TYR B CA  1 
ATOM   1272 C C   . TYR A 1 181 ? -8.077  14.097  0.296   1.00 76.70  ? 367 TYR B C   1 
ATOM   1273 O O   . TYR A 1 181 ? -8.591  12.975  0.219   1.00 77.94  ? 367 TYR B O   1 
ATOM   1274 C CB  . TYR A 1 181 ? -5.588  14.293  -0.037  1.00 75.49  ? 367 TYR B CB  1 
ATOM   1275 C CG  . TYR A 1 181 ? -5.059  12.868  -0.058  1.00 75.56  ? 367 TYR B CG  1 
ATOM   1276 C CD1 . TYR A 1 181 ? -4.554  12.315  -1.229  1.00 75.75  ? 367 TYR B CD1 1 
ATOM   1277 C CD2 . TYR A 1 181 ? -5.004  12.102  1.102   1.00 75.51  ? 367 TYR B CD2 1 
ATOM   1278 C CE1 . TYR A 1 181 ? -4.045  11.025  -1.257  1.00 75.92  ? 367 TYR B CE1 1 
ATOM   1279 C CE2 . TYR A 1 181 ? -4.493  10.807  1.085   1.00 75.70  ? 367 TYR B CE2 1 
ATOM   1280 C CZ  . TYR A 1 181 ? -4.014  10.276  -0.099  1.00 81.90  ? 367 TYR B CZ  1 
ATOM   1281 O OH  . TYR A 1 181 ? -3.504  8.996   -0.133  1.00 76.78  ? 367 TYR B OH  1 
ATOM   1282 N N   . VAL A 1 182 ? -8.452  14.995  1.217   1.00 81.65  ? 368 VAL B N   1 
ATOM   1283 C CA  . VAL A 1 182 ? -9.520  14.723  2.177   1.00 76.97  ? 368 VAL B CA  1 
ATOM   1284 C C   . VAL A 1 182 ? -10.885 15.154  1.660   1.00 77.75  ? 368 VAL B C   1 
ATOM   1285 O O   . VAL A 1 182 ? -11.888 15.003  2.371   1.00 78.17  ? 368 VAL B O   1 
ATOM   1286 C CB  . VAL A 1 182 ? -9.213  15.414  3.523   1.00 76.52  ? 368 VAL B CB  1 
ATOM   1287 C CG1 . VAL A 1 182 ? -9.988  14.772  4.662   1.00 82.83  ? 368 VAL B CG1 1 
ATOM   1288 C CG2 . VAL A 1 182 ? -7.731  15.354  3.814   1.00 79.52  ? 368 VAL B CG2 1 
ATOM   1289 N N   . ALA A 1 183 ? -10.957 15.690  0.444   1.00 78.04  ? 369 ALA B N   1 
ATOM   1290 C CA  . ALA A 1 183 ? -12.237 16.090  -0.125  1.00 79.10  ? 369 ALA B CA  1 
ATOM   1291 C C   . ALA A 1 183 ? -13.145 14.876  -0.309  1.00 83.63  ? 369 ALA B C   1 
ATOM   1292 O O   . ALA A 1 183 ? -12.686 13.783  -0.652  1.00 88.71  ? 369 ALA B O   1 
ATOM   1293 C CB  . ALA A 1 183 ? -12.022 16.802  -1.460  1.00 79.20  ? 369 ALA B CB  1 
ATOM   1294 N N   . VAL A 1 184 ? -14.441 15.078  -0.085  1.00 80.13  ? 370 VAL B N   1 
ATOM   1295 C CA  . VAL A 1 184 ? -15.417 13.994  -0.145  1.00 87.03  ? 370 VAL B CA  1 
ATOM   1296 C C   . VAL A 1 184 ? -15.738 13.668  -1.598  1.00 88.45  ? 370 VAL B C   1 
ATOM   1297 O O   . VAL A 1 184 ? -16.130 14.549  -2.372  1.00 87.83  ? 370 VAL B O   1 
ATOM   1298 C CB  . VAL A 1 184 ? -16.694 14.374  0.621   1.00 83.60  ? 370 VAL B CB  1 
ATOM   1299 C CG1 . VAL A 1 184 ? -17.764 13.311  0.431   1.00 81.81  ? 370 VAL B CG1 1 
ATOM   1300 C CG2 . VAL A 1 184 ? -16.390 14.588  2.093   1.00 85.71  ? 370 VAL B CG2 1 
ATOM   1301 N N   . GLU A 1 185 ? -15.582 12.399  -1.969  1.00 95.82  ? 371 GLU B N   1 
ATOM   1302 C CA  . GLU A 1 185 ? -15.988 11.923  -3.285  1.00 99.39  ? 371 GLU B CA  1 
ATOM   1303 C C   . GLU A 1 185 ? -17.443 11.466  -3.252  1.00 103.67 ? 371 GLU B C   1 
ATOM   1304 O O   . GLU A 1 185 ? -17.925 10.921  -2.254  1.00 105.75 ? 371 GLU B O   1 
ATOM   1305 C CB  . GLU A 1 185 ? -15.096 10.771  -3.761  1.00 104.89 ? 371 GLU B CB  1 
ATOM   1306 C CG  . GLU A 1 185 ? -15.522 10.174  -5.105  1.00 102.56 ? 371 GLU B CG  1 
ATOM   1307 C CD  . GLU A 1 185 ? -14.617 9.054   -5.578  1.00 112.68 ? 371 GLU B CD  1 
ATOM   1308 O OE1 . GLU A 1 185 ? -13.425 9.039   -5.195  1.00 110.73 ? 371 GLU B OE1 1 
ATOM   1309 O OE2 . GLU A 1 185 ? -15.110 8.179   -6.325  1.00 102.64 ? 371 GLU B OE2 1 
ATOM   1310 N N   . GLN A 1 186 ? -18.141 11.697  -4.358  1.00 102.15 ? 372 GLN B N   1 
ATOM   1311 C CA  . GLN A 1 186 ? -19.555 11.383  -4.479  1.00 94.05  ? 372 GLN B CA  1 
ATOM   1312 C C   . GLN A 1 186 ? -19.726 10.136  -5.335  1.00 97.00  ? 372 GLN B C   1 
ATOM   1313 O O   . GLN A 1 186 ? -19.085 10.004  -6.383  1.00 95.74  ? 372 GLN B O   1 
ATOM   1314 C CB  . GLN A 1 186 ? -20.314 12.563  -5.085  1.00 92.98  ? 372 GLN B CB  1 
ATOM   1315 C CG  . GLN A 1 186 ? -21.582 12.918  -4.345  1.00 101.87 ? 372 GLN B CG  1 
ATOM   1316 C CD  . GLN A 1 186 ? -21.308 13.399  -2.931  1.00 96.67  ? 372 GLN B CD  1 
ATOM   1317 O OE1 . GLN A 1 186 ? -20.167 13.691  -2.570  1.00 84.28  ? 372 GLN B OE1 1 
ATOM   1318 N NE2 . GLN A 1 186 ? -22.359 13.496  -2.126  1.00 100.76 ? 372 GLN B NE2 1 
ATOM   1319 N N   . LEU A 1 187 ? -20.574 9.221   -4.878  1.00 97.30  ? 373 LEU B N   1 
ATOM   1320 C CA  . LEU A 1 187 ? -20.900 7.999   -5.608  1.00 99.86  ? 373 LEU B CA  1 
ATOM   1321 C C   . LEU A 1 187 ? -22.381 8.072   -5.974  1.00 112.08 ? 373 LEU B C   1 
ATOM   1322 O O   . LEU A 1 187 ? -23.244 7.601   -5.230  1.00 105.86 ? 373 LEU B O   1 
ATOM   1323 C CB  . LEU A 1 187 ? -20.587 6.763   -4.780  1.00 96.80  ? 373 LEU B CB  1 
ATOM   1324 C CG  . LEU A 1 187 ? -19.130 6.578   -4.369  1.00 93.65  ? 373 LEU B CG  1 
ATOM   1325 C CD1 . LEU A 1 187 ? -19.014 5.381   -3.446  1.00 92.50  ? 373 LEU B CD1 1 
ATOM   1326 C CD2 . LEU A 1 187 ? -18.246 6.415   -5.597  1.00 99.38  ? 373 LEU B CD2 1 
ATOM   1327 N N   . ASP A 1 188 ? -22.667 8.670   -7.125  1.00 119.07 ? 374 ASP B N   1 
ATOM   1328 C CA  . ASP A 1 188 ? -24.024 8.826   -7.623  1.00 124.43 ? 374 ASP B CA  1 
ATOM   1329 C C   . ASP A 1 188 ? -24.354 7.695   -8.599  1.00 127.91 ? 374 ASP B C   1 
ATOM   1330 O O   . ASP A 1 188 ? -23.586 6.741   -8.758  1.00 127.92 ? 374 ASP B O   1 
ATOM   1331 C CB  . ASP A 1 188 ? -24.173 10.207  -8.269  1.00 117.95 ? 374 ASP B CB  1 
ATOM   1332 C CG  . ASP A 1 188 ? -24.224 11.332  -7.245  1.00 121.59 ? 374 ASP B CG  1 
ATOM   1333 O OD1 . ASP A 1 188 ? -24.809 11.127  -6.158  1.00 130.36 ? 374 ASP B OD1 1 
ATOM   1334 O OD2 . ASP A 1 188 ? -23.669 12.419  -7.529  1.00 118.45 ? 374 ASP B OD2 1 
ATOM   1335 N N   . GLY A 1 189 ? -25.511 7.797   -9.260  1.00 127.29 ? 375 GLY B N   1 
ATOM   1336 C CA  . GLY A 1 189 ? -25.929 6.817   -10.247 1.00 124.91 ? 375 GLY B CA  1 
ATOM   1337 C C   . GLY A 1 189 ? -24.860 6.601   -11.295 1.00 133.18 ? 375 GLY B C   1 
ATOM   1338 O O   . GLY A 1 189 ? -24.150 7.546   -11.650 1.00 134.83 ? 375 GLY B O   1 
ATOM   1339 N N   . ASP A 1 190 ? -24.721 5.364   -11.774 1.00 143.78 ? 376 ASP B N   1 
ATOM   1340 C CA  . ASP A 1 190 ? -23.671 4.866   -12.656 1.00 143.29 ? 376 ASP B CA  1 
ATOM   1341 C C   . ASP A 1 190 ? -22.374 4.671   -11.859 1.00 137.59 ? 376 ASP B C   1 
ATOM   1342 O O   . ASP A 1 190 ? -21.434 4.063   -12.371 1.00 145.27 ? 376 ASP B O   1 
ATOM   1343 C CB  . ASP A 1 190 ? -23.417 5.785   -13.874 1.00 148.57 ? 376 ASP B CB  1 
ATOM   1344 C CG  . ASP A 1 190 ? -22.608 5.118   -14.985 1.00 153.93 ? 376 ASP B CG  1 
ATOM   1345 O OD1 . ASP A 1 190 ? -22.279 3.914   -14.878 1.00 158.62 ? 376 ASP B OD1 1 
ATOM   1346 O OD2 . ASP A 1 190 ? -22.297 5.812   -15.981 1.00 151.06 ? 376 ASP B OD2 1 
ATOM   1347 N N   . ASN A 1 191 ? -22.310 5.132   -10.603 1.00 129.63 ? 377 ASN B N   1 
ATOM   1348 C CA  . ASN A 1 191 ? -21.193 4.839   -9.714  1.00 123.44 ? 377 ASN B CA  1 
ATOM   1349 C C   . ASN A 1 191 ? -21.681 4.453   -8.323  1.00 115.67 ? 377 ASN B C   1 
ATOM   1350 O O   . ASN A 1 191 ? -20.867 4.409   -7.390  1.00 107.79 ? 377 ASN B O   1 
ATOM   1351 C CB  . ASN A 1 191 ? -20.231 6.031   -9.600  1.00 122.59 ? 377 ASN B CB  1 
ATOM   1352 C CG  . ASN A 1 191 ? -19.422 6.256   -10.859 1.00 127.61 ? 377 ASN B CG  1 
ATOM   1353 O OD1 . ASN A 1 191 ? -19.135 5.321   -11.610 1.00 129.85 ? 377 ASN B OD1 1 
ATOM   1354 N ND2 . ASN A 1 191 ? -19.061 7.508   -11.104 1.00 127.87 ? 377 ASN B ND2 1 
ATOM   1355 N N   . LYS A 1 192 ? -22.979 4.184   -8.158  1.00 114.77 ? 378 LYS B N   1 
ATOM   1356 C CA  . LYS A 1 192 ? -23.551 3.935   -6.841  1.00 105.86 ? 378 LYS B CA  1 
ATOM   1357 C C   . LYS A 1 192 ? -22.849 2.783   -6.136  1.00 95.62  ? 378 LYS B C   1 
ATOM   1358 O O   . LYS A 1 192 ? -22.538 1.752   -6.739  1.00 96.48  ? 378 LYS B O   1 
ATOM   1359 C CB  . LYS A 1 192 ? -25.053 3.651   -6.943  1.00 105.91 ? 378 LYS B CB  1 
ATOM   1360 C CG  . LYS A 1 192 ? -25.925 4.903   -6.983  1.00 110.16 ? 378 LYS B CG  1 
ATOM   1361 C CD  . LYS A 1 192 ? -27.393 4.576   -6.703  1.00 101.18 ? 378 LYS B CD  1 
ATOM   1362 C CE  . LYS A 1 192 ? -28.140 4.125   -7.947  1.00 98.98  ? 378 LYS B CE  1 
ATOM   1363 N NZ  . LYS A 1 192 ? -28.369 5.257   -8.880  1.00 108.97 ? 378 LYS B NZ  1 
ATOM   1364 N N   . TYR A 1 193 ? -22.577 2.986   -4.852  1.00 90.34  ? 379 TYR B N   1 
ATOM   1365 C CA  . TYR A 1 193 ? -21.910 1.974   -4.050  1.00 91.00  ? 379 TYR B CA  1 
ATOM   1366 C C   . TYR A 1 193 ? -22.798 0.748   -3.893  1.00 87.01  ? 379 TYR B C   1 
ATOM   1367 O O   . TYR A 1 193 ? -24.014 0.854   -3.715  1.00 87.33  ? 379 TYR B O   1 
ATOM   1368 C CB  . TYR A 1 193 ? -21.548 2.546   -2.681  1.00 89.69  ? 379 TYR B CB  1 
ATOM   1369 C CG  . TYR A 1 193 ? -20.960 1.541   -1.725  1.00 85.56  ? 379 TYR B CG  1 
ATOM   1370 C CD1 . TYR A 1 193 ? -19.642 1.130   -1.851  1.00 89.83  ? 379 TYR B CD1 1 
ATOM   1371 C CD2 . TYR A 1 193 ? -21.718 1.006   -0.696  1.00 85.76  ? 379 TYR B CD2 1 
ATOM   1372 C CE1 . TYR A 1 193 ? -19.095 0.213   -0.975  1.00 93.15  ? 379 TYR B CE1 1 
ATOM   1373 C CE2 . TYR A 1 193 ? -21.180 0.089   0.182   1.00 85.76  ? 379 TYR B CE2 1 
ATOM   1374 C CZ  . TYR A 1 193 ? -19.871 -0.304  0.038   1.00 86.22  ? 379 TYR B CZ  1 
ATOM   1375 O OH  . TYR A 1 193 ? -19.334 -1.214  0.915   1.00 89.60  ? 379 TYR B OH  1 
ATOM   1376 N N   . ASP A 1 194 ? -22.180 -0.424  -3.978  1.00 87.21  ? 380 ASP B N   1 
ATOM   1377 C CA  . ASP A 1 194 ? -22.875 -1.690  -3.775  1.00 87.81  ? 380 ASP B CA  1 
ATOM   1378 C C   . ASP A 1 194 ? -22.963 -1.933  -2.275  1.00 87.54  ? 380 ASP B C   1 
ATOM   1379 O O   . ASP A 1 194 ? -22.032 -2.464  -1.666  1.00 92.83  ? 380 ASP B O   1 
ATOM   1380 C CB  . ASP A 1 194 ? -22.132 -2.816  -4.481  1.00 88.59  ? 380 ASP B CB  1 
ATOM   1381 C CG  . ASP A 1 194 ? -22.830 -4.147  -4.352  1.00 88.98  ? 380 ASP B CG  1 
ATOM   1382 O OD1 . ASP A 1 194 ? -23.980 -4.179  -3.864  1.00 89.84  ? 380 ASP B OD1 1 
ATOM   1383 O OD2 . ASP A 1 194 ? -22.217 -5.167  -4.730  1.00 93.55  ? 380 ASP B OD2 1 
ATOM   1384 N N   . ALA A 1 195 ? -24.080 -1.543  -1.666  1.00 87.56  ? 381 ALA B N   1 
ATOM   1385 C CA  . ALA A 1 195 ? -24.236 -1.713  -0.228  1.00 87.40  ? 381 ALA B CA  1 
ATOM   1386 C C   . ALA A 1 195 ? -24.692 -3.115  0.156   1.00 88.02  ? 381 ALA B C   1 
ATOM   1387 O O   . ALA A 1 195 ? -25.025 -3.345  1.324   1.00 88.07  ? 381 ALA B O   1 
ATOM   1388 C CB  . ALA A 1 195 ? -25.204 -0.670  0.331   1.00 87.22  ? 381 ALA B CB  1 
ATOM   1389 N N   . GLY A 1 196 ? -24.719 -4.047  -0.793  1.00 88.58  ? 382 GLY B N   1 
ATOM   1390 C CA  . GLY A 1 196 ? -25.074 -5.419  -0.489  1.00 89.26  ? 382 GLY B CA  1 
ATOM   1391 C C   . GLY A 1 196 ? -26.514 -5.583  -0.047  1.00 89.58  ? 382 GLY B C   1 
ATOM   1392 O O   . GLY A 1 196 ? -27.438 -5.528  -0.864  1.00 89.88  ? 382 GLY B O   1 
ATOM   1393 N N   . GLU A 1 197 ? -26.700 -5.812  1.256   1.00 89.70  ? 383 GLU B N   1 
ATOM   1394 C CA  . GLU A 1 197 ? -28.035 -5.972  1.828   1.00 89.90  ? 383 GLU B CA  1 
ATOM   1395 C C   . GLU A 1 197 ? -28.936 -4.781  1.526   1.00 90.30  ? 383 GLU B C   1 
ATOM   1396 O O   . GLU A 1 197 ? -30.146 -4.949  1.338   1.00 97.26  ? 383 GLU B O   1 
ATOM   1397 C CB  . GLU A 1 197 ? -27.913 -6.177  3.338   1.00 89.92  ? 383 GLU B CB  1 
ATOM   1398 C CG  . GLU A 1 197 ? -29.218 -6.372  4.076   1.00 90.27  ? 383 GLU B CG  1 
ATOM   1399 C CD  . GLU A 1 197 ? -29.021 -6.411  5.581   1.00 99.65  ? 383 GLU B CD  1 
ATOM   1400 O OE1 . GLU A 1 197 ? -27.856 -6.332  6.033   1.00 92.11  ? 383 GLU B OE1 1 
ATOM   1401 O OE2 . GLU A 1 197 ? -30.031 -6.499  6.313   1.00 107.34 ? 383 GLU B OE2 1 
ATOM   1402 N N   . HIS A 1 198 ? -28.367 -3.582  1.450   1.00 92.22  ? 384 HIS B N   1 
ATOM   1403 C CA  . HIS A 1 198 ? -29.123 -2.367  1.182   1.00 90.29  ? 384 HIS B CA  1 
ATOM   1404 C C   . HIS A 1 198 ? -29.175 -2.023  -0.303  1.00 88.94  ? 384 HIS B C   1 
ATOM   1405 O O   . HIS A 1 198 ? -29.684 -0.956  -0.663  1.00 88.88  ? 384 HIS B O   1 
ATOM   1406 C CB  . HIS A 1 198 ? -28.535 -1.194  1.976   1.00 93.58  ? 384 HIS B CB  1 
ATOM   1407 C CG  . HIS A 1 198 ? -28.469 -1.436  3.454   1.00 94.78  ? 384 HIS B CG  1 
ATOM   1408 N ND1 . HIS A 1 198 ? -27.424 -0.990  4.235   1.00 99.22  ? 384 HIS B ND1 1 
ATOM   1409 C CD2 . HIS A 1 198 ? -29.319 -2.072  4.294   1.00 96.00  ? 384 HIS B CD2 1 
ATOM   1410 C CE1 . HIS A 1 198 ? -27.630 -1.345  5.490   1.00 98.52  ? 384 HIS B CE1 1 
ATOM   1411 N NE2 . HIS A 1 198 ? -28.773 -2.004  5.553   1.00 99.48  ? 384 HIS B NE2 1 
ATOM   1412 N N   . GLY A 1 199 ? -28.634 -2.880  -1.165  1.00 89.21  ? 385 GLY B N   1 
ATOM   1413 C CA  . GLY A 1 199 ? -28.672 -2.636  -2.589  1.00 89.47  ? 385 GLY B CA  1 
ATOM   1414 C C   . GLY A 1 199 ? -27.772 -1.483  -2.998  1.00 88.97  ? 385 GLY B C   1 
ATOM   1415 O O   . GLY A 1 199 ? -26.924 -1.006  -2.247  1.00 91.15  ? 385 GLY B O   1 
ATOM   1416 N N   . LEU A 1 200 ? -27.976 -1.040  -4.232  1.00 89.29  ? 386 LEU B N   1 
ATOM   1417 C CA  . LEU A 1 200 ? -27.228 0.097   -4.747  1.00 88.95  ? 386 LEU B CA  1 
ATOM   1418 C C   . LEU A 1 200 ? -27.643 1.382   -4.041  1.00 88.61  ? 386 LEU B C   1 
ATOM   1419 O O   . LEU A 1 200 ? -28.832 1.647   -3.849  1.00 88.94  ? 386 LEU B O   1 
ATOM   1420 C CB  . LEU A 1 200 ? -27.432 0.210   -6.256  1.00 89.57  ? 386 LEU B CB  1 
ATOM   1421 C CG  . LEU A 1 200 ? -26.160 0.022   -7.084  1.00 89.52  ? 386 LEU B CG  1 
ATOM   1422 C CD1 . LEU A 1 200 ? -25.587 -1.364  -6.860  1.00 89.59  ? 386 LEU B CD1 1 
ATOM   1423 C CD2 . LEU A 1 200 ? -26.457 0.235   -8.557  1.00 90.26  ? 386 LEU B CD2 1 
ATOM   1424 N N   . GLN A 1 201 ? -26.655 2.180   -3.650  1.00 87.97  ? 387 GLN B N   1 
ATOM   1425 C CA  . GLN A 1 201 ? -26.895 3.327   -2.792  1.00 87.62  ? 387 GLN B CA  1 
ATOM   1426 C C   . GLN A 1 201 ? -26.084 4.517   -3.276  1.00 99.75  ? 387 GLN B C   1 
ATOM   1427 O O   . GLN A 1 201 ? -25.014 4.365   -3.873  1.00 103.02 ? 387 GLN B O   1 
ATOM   1428 C CB  . GLN A 1 201 ? -26.543 3.026   -1.333  1.00 87.11  ? 387 GLN B CB  1 
ATOM   1429 C CG  . GLN A 1 201 ? -27.551 2.129   -0.642  1.00 90.23  ? 387 GLN B CG  1 
ATOM   1430 C CD  . GLN A 1 201 ? -28.959 2.696   -0.648  1.00 87.93  ? 387 GLN B CD  1 
ATOM   1431 O OE1 . GLN A 1 201 ? -29.161 3.903   -0.509  1.00 87.85  ? 387 GLN B OE1 1 
ATOM   1432 N NE2 . GLN A 1 201 ? -29.944 1.819   -0.795  1.00 88.46  ? 387 GLN B NE2 1 
ATOM   1433 N N   . GLU A 1 202 ? -26.603 5.707   -2.990  1.00 97.03  ? 388 GLU B N   1 
ATOM   1434 C CA  . GLU A 1 202 ? -25.961 6.967   -3.356  1.00 104.64 ? 388 GLU B CA  1 
ATOM   1435 C C   . GLU A 1 202 ? -25.158 7.439   -2.149  1.00 96.69  ? 388 GLU B C   1 
ATOM   1436 O O   . GLU A 1 202 ? -25.632 8.219   -1.322  1.00 95.98  ? 388 GLU B O   1 
ATOM   1437 C CB  . GLU A 1 202 ? -27.001 7.984   -3.809  1.00 112.76 ? 388 GLU B CB  1 
ATOM   1438 C CG  . GLU A 1 202 ? -27.425 7.802   -5.265  1.00 114.78 ? 388 GLU B CG  1 
ATOM   1439 C CD  . GLU A 1 202 ? -28.538 8.743   -5.688  1.00 132.06 ? 388 GLU B CD  1 
ATOM   1440 O OE1 . GLU A 1 202 ? -29.147 9.387   -4.805  1.00 130.55 ? 388 GLU B OE1 1 
ATOM   1441 O OE2 . GLU A 1 202 ? -28.787 8.856   -6.909  1.00 134.12 ? 388 GLU B OE2 1 
ATOM   1442 N N   . ALA A 1 203 ? -23.931 6.942   -2.037  1.00 93.86  ? 389 ALA B N   1 
ATOM   1443 C CA  . ALA A 1 203 ? -23.099 7.175   -0.871  1.00 85.03  ? 389 ALA B CA  1 
ATOM   1444 C C   . ALA A 1 203 ? -22.061 8.267   -1.132  1.00 87.09  ? 389 ALA B C   1 
ATOM   1445 O O   . ALA A 1 203 ? -22.029 8.906   -2.187  1.00 92.69  ? 389 ALA B O   1 
ATOM   1446 C CB  . ALA A 1 203 ? -22.421 5.865   -0.460  1.00 85.05  ? 389 ALA B CB  1 
ATOM   1447 N N   . GLU A 1 204 ? -21.215 8.494   -0.127  1.00 92.28  ? 390 GLU B N   1 
ATOM   1448 C CA  . GLU A 1 204 ? -20.063 9.380   -0.212  1.00 92.14  ? 390 GLU B CA  1 
ATOM   1449 C C   . GLU A 1 204 ? -18.821 8.613   0.212   1.00 84.32  ? 390 GLU B C   1 
ATOM   1450 O O   . GLU A 1 204 ? -18.856 7.869   1.195   1.00 89.23  ? 390 GLU B O   1 
ATOM   1451 C CB  . GLU A 1 204 ? -20.233 10.613  0.685   1.00 96.12  ? 390 GLU B CB  1 
ATOM   1452 C CG  . GLU A 1 204 ? -21.333 11.560  0.250   1.00 98.29  ? 390 GLU B CG  1 
ATOM   1453 C CD  . GLU A 1 204 ? -21.386 12.821  1.096   1.00 98.89  ? 390 GLU B CD  1 
ATOM   1454 O OE1 . GLU A 1 204 ? -20.639 12.904  2.096   1.00 92.74  ? 390 GLU B OE1 1 
ATOM   1455 O OE2 . GLU A 1 204 ? -22.182 13.725  0.761   1.00 102.67 ? 390 GLU B OE2 1 
ATOM   1456 N N   . LYS A 1 205 ? -17.722 8.802   -0.514  1.00 94.76  ? 391 LYS B N   1 
ATOM   1457 C CA  . LYS A 1 205 ? -16.469 8.121   -0.215  1.00 90.68  ? 391 LYS B CA  1 
ATOM   1458 C C   . LYS A 1 205 ? -15.389 9.139   0.119   1.00 83.96  ? 391 LYS B C   1 
ATOM   1459 O O   . LYS A 1 205 ? -15.269 10.172  -0.546  1.00 81.01  ? 391 LYS B O   1 
ATOM   1460 C CB  . LYS A 1 205 ? -16.002 7.253   -1.387  1.00 89.14  ? 391 LYS B CB  1 
ATOM   1461 C CG  . LYS A 1 205 ? -14.750 6.447   -1.064  1.00 97.35  ? 391 LYS B CG  1 
ATOM   1462 C CD  . LYS A 1 205 ? -14.396 5.463   -2.163  1.00 102.55 ? 391 LYS B CD  1 
ATOM   1463 C CE  . LYS A 1 205 ? -14.003 6.182   -3.443  1.00 106.92 ? 391 LYS B CE  1 
ATOM   1464 N NZ  . LYS A 1 205 ? -12.744 6.965   -3.275  1.00 104.20 ? 391 LYS B NZ  1 
ATOM   1465 N N   . GLY A 1 206 ? -14.608 8.852   1.157   1.00 89.28  ? 392 GLY B N   1 
ATOM   1466 C CA  . GLY A 1 206 ? -13.545 9.762   1.533   1.00 87.25  ? 392 GLY B CA  1 
ATOM   1467 C C   . GLY A 1 206 ? -12.467 9.073   2.341   1.00 79.42  ? 392 GLY B C   1 
ATOM   1468 O O   . GLY A 1 206 ? -12.548 7.883   2.652   1.00 79.75  ? 392 GLY B O   1 
ATOM   1469 N N   . VAL A 1 207 ? -11.438 9.853   2.662   1.00 78.74  ? 393 VAL B N   1 
ATOM   1470 C CA  . VAL A 1 207 ? -10.305 9.403   3.464   1.00 78.47  ? 393 VAL B CA  1 
ATOM   1471 C C   . VAL A 1 207 ? -9.860  10.567  4.339   1.00 77.70  ? 393 VAL B C   1 
ATOM   1472 O O   . VAL A 1 207 ? -9.771  11.707  3.871   1.00 79.54  ? 393 VAL B O   1 
ATOM   1473 C CB  . VAL A 1 207 ? -9.146  8.883   2.579   1.00 78.07  ? 393 VAL B CB  1 
ATOM   1474 C CG1 . VAL A 1 207 ? -9.296  9.373   1.145   1.00 79.95  ? 393 VAL B CG1 1 
ATOM   1475 C CG2 . VAL A 1 207 ? -7.794  9.310   3.137   1.00 78.83  ? 393 VAL B CG2 1 
ATOM   1476 N N   . LYS A 1 208 ? -9.598  10.288  5.616   1.00 77.62  ? 394 LYS B N   1 
ATOM   1477 C CA  . LYS A 1 208 ? -9.082  11.290  6.537   1.00 77.18  ? 394 LYS B CA  1 
ATOM   1478 C C   . LYS A 1 208 ? -7.892  10.713  7.296   1.00 77.94  ? 394 LYS B C   1 
ATOM   1479 O O   . LYS A 1 208 ? -7.779  9.497   7.472   1.00 85.21  ? 394 LYS B O   1 
ATOM   1480 C CB  . LYS A 1 208 ? -10.163 11.780  7.503   1.00 77.47  ? 394 LYS B CB  1 
ATOM   1481 C CG  . LYS A 1 208 ? -10.826 10.679  8.282   1.00 80.13  ? 394 LYS B CG  1 
ATOM   1482 C CD  . LYS A 1 208 ? -11.881 11.216  9.230   1.00 93.54  ? 394 LYS B CD  1 
ATOM   1483 C CE  . LYS A 1 208 ? -13.121 11.705  8.503   1.00 92.75  ? 394 LYS B CE  1 
ATOM   1484 N NZ  . LYS A 1 208 ? -14.128 12.222  9.472   1.00 84.80  ? 394 LYS B NZ  1 
ATOM   1485 N N   . PHE A 1 209 ? -7.002  11.596  7.741   1.00 76.15  ? 395 PHE B N   1 
ATOM   1486 C CA  . PHE A 1 209 ? -5.754  11.167  8.363   1.00 81.89  ? 395 PHE B CA  1 
ATOM   1487 C C   . PHE A 1 209 ? -5.945  10.863  9.841   1.00 82.25  ? 395 PHE B C   1 
ATOM   1488 O O   . PHE A 1 209 ? -6.455  11.695  10.599  1.00 84.69  ? 395 PHE B O   1 
ATOM   1489 C CB  . PHE A 1 209 ? -4.676  12.237  8.198   1.00 77.30  ? 395 PHE B CB  1 
ATOM   1490 C CG  . PHE A 1 209 ? -4.124  12.322  6.812   1.00 74.97  ? 395 PHE B CG  1 
ATOM   1491 C CD1 . PHE A 1 209 ? -3.147  11.437  6.388   1.00 74.52  ? 395 PHE B CD1 1 
ATOM   1492 C CD2 . PHE A 1 209 ? -4.582  13.288  5.929   1.00 75.65  ? 395 PHE B CD2 1 
ATOM   1493 C CE1 . PHE A 1 209 ? -2.640  11.511  5.109   1.00 74.28  ? 395 PHE B CE1 1 
ATOM   1494 C CE2 . PHE A 1 209 ? -4.074  13.368  4.646   1.00 74.29  ? 395 PHE B CE2 1 
ATOM   1495 C CZ  . PHE A 1 209 ? -3.103  12.477  4.236   1.00 74.16  ? 395 PHE B CZ  1 
ATOM   1496 N N   . LEU A 1 210 ? -5.548  9.655   10.244  1.00 79.11  ? 396 LEU B N   1 
ATOM   1497 C CA  . LEU A 1 210 ? -5.510  9.315   11.661  1.00 81.57  ? 396 LEU B CA  1 
ATOM   1498 C C   . LEU A 1 210 ? -4.216  9.802   12.309  1.00 81.95  ? 396 LEU B C   1 
ATOM   1499 O O   . LEU A 1 210 ? -4.243  10.537  13.301  1.00 86.45  ? 396 LEU B O   1 
ATOM   1500 C CB  . LEU A 1 210 ? -5.662  7.802   11.841  1.00 77.86  ? 396 LEU B CB  1 
ATOM   1501 C CG  . LEU A 1 210 ? -7.017  7.212   11.453  1.00 82.79  ? 396 LEU B CG  1 
ATOM   1502 C CD1 . LEU A 1 210 ? -6.977  5.694   11.527  1.00 82.08  ? 396 LEU B CD1 1 
ATOM   1503 C CD2 . LEU A 1 210 ? -8.114  7.768   12.346  1.00 78.84  ? 396 LEU B CD2 1 
ATOM   1504 N N   . THR A 1 211 ? -3.072  9.393   11.761  1.00 82.59  ? 397 THR B N   1 
ATOM   1505 C CA  . THR A 1 211 ? -1.769  9.755   12.301  1.00 77.49  ? 397 THR B CA  1 
ATOM   1506 C C   . THR A 1 211 ? -0.811  10.078  11.162  1.00 76.09  ? 397 THR B C   1 
ATOM   1507 O O   . THR A 1 211 ? -0.988  9.630   10.027  1.00 77.85  ? 397 THR B O   1 
ATOM   1508 C CB  . THR A 1 211 ? -1.176  8.634   13.164  1.00 80.13  ? 397 THR B CB  1 
ATOM   1509 O OG1 . THR A 1 211 ? -1.004  7.458   12.364  1.00 76.71  ? 397 THR B OG1 1 
ATOM   1510 C CG2 . THR A 1 211 ? -2.081  8.321   14.356  1.00 79.18  ? 397 THR B CG2 1 
ATOM   1511 N N   . LEU A 1 212 ? 0.219   10.861  11.487  1.00 78.34  ? 398 LEU B N   1 
ATOM   1512 C CA  . LEU A 1 212 ? 1.251   11.259  10.541  1.00 78.33  ? 398 LEU B CA  1 
ATOM   1513 C C   . LEU A 1 212 ? 2.627   10.812  11.025  1.00 80.57  ? 398 LEU B C   1 
ATOM   1514 O O   . LEU A 1 212 ? 2.963   11.010  12.202  1.00 80.32  ? 398 LEU B O   1 
ATOM   1515 C CB  . LEU A 1 212 ? 1.235   12.782  10.335  1.00 79.61  ? 398 LEU B CB  1 
ATOM   1516 C CG  . LEU A 1 212 ? 0.073   13.373  9.534   1.00 76.71  ? 398 LEU B CG  1 
ATOM   1517 C CD1 . LEU A 1 212 ? 0.047   14.875  9.696   1.00 79.82  ? 398 LEU B CD1 1 
ATOM   1518 C CD2 . LEU A 1 212 ? 0.164   13.001  8.063   1.00 72.59  ? 398 LEU B CD2 1 
ATOM   1519 N N   . PRO A 1 213 ? 3.442   10.214  10.159  1.00 82.93  ? 399 PRO B N   1 
ATOM   1520 C CA  . PRO A 1 213 ? 4.714   9.615   10.594  1.00 78.11  ? 399 PRO B CA  1 
ATOM   1521 C C   . PRO A 1 213 ? 5.745   10.678  10.927  1.00 81.04  ? 399 PRO B C   1 
ATOM   1522 O O   . PRO A 1 213 ? 5.600   11.842  10.524  1.00 77.59  ? 399 PRO B O   1 
ATOM   1523 C CB  . PRO A 1 213 ? 5.149   8.786   9.374   1.00 80.23  ? 399 PRO B CB  1 
ATOM   1524 C CG  . PRO A 1 213 ? 3.949   8.741   8.463   1.00 83.20  ? 399 PRO B CG  1 
ATOM   1525 C CD  . PRO A 1 213 ? 3.200   10.001  8.725   1.00 82.31  ? 399 PRO B CD  1 
ATOM   1526 N N   . PRO A 1 214 ? 6.804   10.317  11.663  1.00 78.04  ? 400 PRO B N   1 
ATOM   1527 C CA  . PRO A 1 214 ? 7.891   11.280  11.907  1.00 76.00  ? 400 PRO B CA  1 
ATOM   1528 C C   . PRO A 1 214 ? 8.586   11.750  10.642  1.00 82.25  ? 400 PRO B C   1 
ATOM   1529 O O   . PRO A 1 214 ? 9.067   12.890  10.598  1.00 82.55  ? 400 PRO B O   1 
ATOM   1530 C CB  . PRO A 1 214 ? 8.851   10.501  12.821  1.00 85.30  ? 400 PRO B CB  1 
ATOM   1531 C CG  . PRO A 1 214 ? 8.019   9.419   13.428  1.00 80.22  ? 400 PRO B CG  1 
ATOM   1532 C CD  . PRO A 1 214 ? 7.032   9.042   12.365  1.00 81.56  ? 400 PRO B CD  1 
ATOM   1533 N N   . VAL A 1 215 ? 8.684   10.901  9.623   1.00 81.41  ? 401 VAL B N   1 
ATOM   1534 C CA  . VAL A 1 215 ? 9.285   11.266  8.343   1.00 78.48  ? 401 VAL B CA  1 
ATOM   1535 C C   . VAL A 1 215 ? 8.219   11.107  7.266   1.00 74.62  ? 401 VAL B C   1 
ATOM   1536 O O   . VAL A 1 215 ? 7.679   10.010  7.071   1.00 74.40  ? 401 VAL B O   1 
ATOM   1537 C CB  . VAL A 1 215 ? 10.530  10.422  8.031   1.00 72.77  ? 401 VAL B CB  1 
ATOM   1538 C CG1 . VAL A 1 215 ? 11.181  10.893  6.738   1.00 74.97  ? 401 VAL B CG1 1 
ATOM   1539 C CG2 . VAL A 1 215 ? 11.522  10.498  9.188   1.00 71.58  ? 401 VAL B CG2 1 
ATOM   1540 N N   . LEU A 1 216 ? 7.922   12.197  6.569   1.00 69.80  ? 402 LEU B N   1 
ATOM   1541 C CA  . LEU A 1 216 ? 6.799   12.272  5.646   1.00 70.22  ? 402 LEU B CA  1 
ATOM   1542 C C   . LEU A 1 216 ? 7.333   12.300  4.223   1.00 73.52  ? 402 LEU B C   1 
ATOM   1543 O O   . LEU A 1 216 ? 8.040   13.239  3.847   1.00 76.32  ? 402 LEU B O   1 
ATOM   1544 C CB  . LEU A 1 216 ? 5.966   13.523  5.927   1.00 71.14  ? 402 LEU B CB  1 
ATOM   1545 C CG  . LEU A 1 216 ? 4.543   13.609  5.383   1.00 70.37  ? 402 LEU B CG  1 
ATOM   1546 C CD1 . LEU A 1 216 ? 3.655   12.573  6.056   1.00 71.24  ? 402 LEU B CD1 1 
ATOM   1547 C CD2 . LEU A 1 216 ? 3.998   15.013  5.593   1.00 70.78  ? 402 LEU B CD2 1 
ATOM   1548 N N   . HIS A 1 217 ? 7.006   11.273  3.440   1.00 71.67  ? 403 HIS B N   1 
ATOM   1549 C CA  . HIS A 1 217 ? 7.401   11.210  2.035   1.00 70.65  ? 403 HIS B CA  1 
ATOM   1550 C C   . HIS A 1 217 ? 6.211   11.641  1.185   1.00 73.75  ? 403 HIS B C   1 
ATOM   1551 O O   . HIS A 1 217 ? 5.219   10.912  1.080   1.00 74.60  ? 403 HIS B O   1 
ATOM   1552 C CB  . HIS A 1 217 ? 7.868   9.808   1.654   1.00 74.63  ? 403 HIS B CB  1 
ATOM   1553 C CG  . HIS A 1 217 ? 9.262   9.501   2.097   1.00 76.29  ? 403 HIS B CG  1 
ATOM   1554 N ND1 . HIS A 1 217 ? 10.069  10.434  2.713   1.00 70.80  ? 403 HIS B ND1 1 
ATOM   1555 C CD2 . HIS A 1 217 ? 9.992   8.364   2.021   1.00 71.62  ? 403 HIS B CD2 1 
ATOM   1556 C CE1 . HIS A 1 217 ? 11.236  9.887   2.995   1.00 70.60  ? 403 HIS B CE1 1 
ATOM   1557 N NE2 . HIS A 1 217 ? 11.216  8.631   2.586   1.00 75.32  ? 403 HIS B NE2 1 
ATOM   1558 N N   . LEU A 1 218 ? 6.313   12.818  0.575   1.00 73.27  ? 404 LEU B N   1 
ATOM   1559 C CA  . LEU A 1 218 ? 5.249   13.373  -0.252  1.00 70.77  ? 404 LEU B CA  1 
ATOM   1560 C C   . LEU A 1 218 ? 5.706   13.382  -1.703  1.00 70.90  ? 404 LEU B C   1 
ATOM   1561 O O   . LEU A 1 218 ? 6.685   14.052  -2.043  1.00 70.28  ? 404 LEU B O   1 
ATOM   1562 C CB  . LEU A 1 218 ? 4.882   14.786  0.198   1.00 70.27  ? 404 LEU B CB  1 
ATOM   1563 C CG  . LEU A 1 218 ? 4.446   14.941  1.652   1.00 70.15  ? 404 LEU B CG  1 
ATOM   1564 C CD1 . LEU A 1 218 ? 4.096   16.391  1.943   1.00 75.38  ? 404 LEU B CD1 1 
ATOM   1565 C CD2 . LEU A 1 218 ? 3.275   14.028  1.948   1.00 70.99  ? 404 LEU B CD2 1 
ATOM   1566 N N   . GLN A 1 219 ? 4.989   12.655  -2.553  1.00 75.18  ? 405 GLN B N   1 
ATOM   1567 C CA  . GLN A 1 219 ? 5.244   12.643  -3.987  1.00 72.09  ? 405 GLN B CA  1 
ATOM   1568 C C   . GLN A 1 219 ? 4.272   13.583  -4.684  1.00 72.39  ? 405 GLN B C   1 
ATOM   1569 O O   . GLN A 1 219 ? 3.060   13.522  -4.446  1.00 75.97  ? 405 GLN B O   1 
ATOM   1570 C CB  . GLN A 1 219 ? 5.109   11.232  -4.557  1.00 72.97  ? 405 GLN B CB  1 
ATOM   1571 C CG  . GLN A 1 219 ? 6.322   10.355  -4.354  1.00 72.86  ? 405 GLN B CG  1 
ATOM   1572 C CD  . GLN A 1 219 ? 6.315   9.678   -3.004  1.00 72.84  ? 405 GLN B CD  1 
ATOM   1573 O OE1 . GLN A 1 219 ? 5.267   9.543   -2.371  1.00 73.13  ? 405 GLN B OE1 1 
ATOM   1574 N NE2 . GLN A 1 219 ? 7.484   9.230   -2.562  1.00 72.57  ? 405 GLN B NE2 1 
ATOM   1575 N N   . LEU A 1 220 ? 4.803   14.451  -5.533  1.00 72.16  ? 406 LEU B N   1 
ATOM   1576 C CA  . LEU A 1 220 ? 4.012   15.479  -6.194  1.00 72.50  ? 406 LEU B CA  1 
ATOM   1577 C C   . LEU A 1 220 ? 3.665   15.001  -7.601  1.00 77.18  ? 406 LEU B C   1 
ATOM   1578 O O   . LEU A 1 220 ? 4.516   15.006  -8.496  1.00 81.74  ? 406 LEU B O   1 
ATOM   1579 C CB  . LEU A 1 220 ? 4.782   16.796  -6.222  1.00 71.77  ? 406 LEU B CB  1 
ATOM   1580 C CG  . LEU A 1 220 ? 5.205   17.372  -4.870  1.00 70.82  ? 406 LEU B CG  1 
ATOM   1581 C CD1 . LEU A 1 220 ? 5.679   18.801  -5.047  1.00 70.30  ? 406 LEU B CD1 1 
ATOM   1582 C CD2 . LEU A 1 220 ? 4.081   17.298  -3.846  1.00 71.03  ? 406 LEU B CD2 1 
ATOM   1583 N N   . MET A 1 221 ? 2.400   14.630  -7.806  1.00 74.65  ? 407 MET B N   1 
ATOM   1584 C CA  . MET A 1 221 ? 1.959   14.006  -9.056  1.00 76.61  ? 407 MET B CA  1 
ATOM   1585 C C   . MET A 1 221 ? 1.738   15.070  -10.133 1.00 82.57  ? 407 MET B C   1 
ATOM   1586 O O   . MET A 1 221 ? 0.613   15.425  -10.492 1.00 84.38  ? 407 MET B O   1 
ATOM   1587 C CB  . MET A 1 221 ? 0.698   13.185  -8.822  1.00 76.39  ? 407 MET B CB  1 
ATOM   1588 C CG  . MET A 1 221 ? 0.862   12.030  -7.846  1.00 76.18  ? 407 MET B CG  1 
ATOM   1589 S SD  . MET A 1 221 ? 1.852   10.687  -8.542  1.00 85.95  ? 407 MET B SD  1 
ATOM   1590 C CE  . MET A 1 221 ? 3.199   10.600  -7.376  1.00 75.49  ? 407 MET B CE  1 
ATOM   1591 N N   . ARG A 1 222 ? 2.853   15.571  -10.673 1.00 75.41  ? 408 ARG B N   1 
ATOM   1592 C CA  . ARG A 1 222 ? 2.811   16.592  -11.721 1.00 75.89  ? 408 ARG B CA  1 
ATOM   1593 C C   . ARG A 1 222 ? 3.015   15.944  -13.090 1.00 76.82  ? 408 ARG B C   1 
ATOM   1594 O O   . ARG A 1 222 ? 4.062   16.074  -13.724 1.00 78.80  ? 408 ARG B O   1 
ATOM   1595 C CB  . ARG A 1 222 ? 3.844   17.686  -11.441 1.00 76.20  ? 408 ARG B CB  1 
ATOM   1596 C CG  . ARG A 1 222 ? 5.178   17.192  -10.899 1.00 73.97  ? 408 ARG B CG  1 
ATOM   1597 C CD  . ARG A 1 222 ? 6.239   18.297  -10.907 1.00 73.17  ? 408 ARG B CD  1 
ATOM   1598 N NE  . ARG A 1 222 ? 5.961   19.364  -9.948  1.00 72.56  ? 408 ARG B NE  1 
ATOM   1599 C CZ  . ARG A 1 222 ? 5.542   20.582  -10.271 1.00 72.84  ? 408 ARG B CZ  1 
ATOM   1600 N NH1 . ARG A 1 222 ? 5.320   20.929  -11.529 1.00 73.77  ? 408 ARG B NH1 1 
ATOM   1601 N NH2 . ARG A 1 222 ? 5.345   21.477  -9.306  1.00 72.29  ? 408 ARG B NH2 1 
ATOM   1602 N N   . PHE A 1 223 ? 1.972   15.261  -13.563 1.00 77.83  ? 409 PHE B N   1 
ATOM   1603 C CA  . PHE A 1 223 ? 1.963   14.670  -14.898 1.00 81.03  ? 409 PHE B CA  1 
ATOM   1604 C C   . PHE A 1 223 ? 0.531   14.309  -15.278 1.00 85.75  ? 409 PHE B C   1 
ATOM   1605 O O   . PHE A 1 223 ? -0.358  14.261  -14.424 1.00 88.43  ? 409 PHE B O   1 
ATOM   1606 C CB  . PHE A 1 223 ? 2.889   13.455  -14.981 1.00 78.79  ? 409 PHE B CB  1 
ATOM   1607 C CG  . PHE A 1 223 ? 2.383   12.248  -14.253 1.00 78.84  ? 409 PHE B CG  1 
ATOM   1608 C CD1 . PHE A 1 223 ? 2.482   12.158  -12.873 1.00 78.89  ? 409 PHE B CD1 1 
ATOM   1609 C CD2 . PHE A 1 223 ? 1.828   11.191  -14.954 1.00 79.92  ? 409 PHE B CD2 1 
ATOM   1610 C CE1 . PHE A 1 223 ? 2.025   11.035  -12.206 1.00 85.07  ? 409 PHE B CE1 1 
ATOM   1611 C CE2 . PHE A 1 223 ? 1.369   10.066  -14.293 1.00 80.66  ? 409 PHE B CE2 1 
ATOM   1612 C CZ  . PHE A 1 223 ? 1.467   9.988   -12.916 1.00 84.40  ? 409 PHE B CZ  1 
ATOM   1613 N N   . MET A 1 224 ? 0.312   14.066  -16.573 1.00 93.13  ? 410 MET B N   1 
ATOM   1614 C CA  . MET A 1 224 ? -1.024  13.718  -17.044 1.00 85.18  ? 410 MET B CA  1 
ATOM   1615 C C   . MET A 1 224 ? -0.953  12.937  -18.351 1.00 93.59  ? 410 MET B C   1 
ATOM   1616 O O   . MET A 1 224 ? -0.062  13.147  -19.178 1.00 93.59  ? 410 MET B O   1 
ATOM   1617 C CB  . MET A 1 224 ? -1.893  14.967  -17.252 1.00 85.50  ? 410 MET B CB  1 
ATOM   1618 C CG  . MET A 1 224 ? -1.348  15.947  -18.287 1.00 87.62  ? 410 MET B CG  1 
ATOM   1619 S SD  . MET A 1 224 ? -2.568  17.158  -18.846 1.00 113.59 ? 410 MET B SD  1 
ATOM   1620 C CE  . MET A 1 224 ? -3.054  17.899  -17.288 1.00 100.12 ? 410 MET B CE  1 
ATOM   1621 N N   . TYR A 1 225 ? -1.920  12.040  -18.523 1.00 100.46 ? 411 TYR B N   1 
ATOM   1622 C CA  . TYR A 1 225 ? -2.175  11.380  -19.801 1.00 107.05 ? 411 TYR B CA  1 
ATOM   1623 C C   . TYR A 1 225 ? -3.624  10.906  -19.798 1.00 109.69 ? 411 TYR B C   1 
ATOM   1624 O O   . TYR A 1 225 ? -3.968  9.857   -20.341 1.00 116.55 ? 411 TYR B O   1 
ATOM   1625 C CB  . TYR A 1 225 ? -1.200  10.218  -20.034 1.00 113.16 ? 411 TYR B CB  1 
ATOM   1626 C CG  . TYR A 1 225 ? -1.385  9.490   -21.357 1.00 117.16 ? 411 TYR B CG  1 
ATOM   1627 C CD1 . TYR A 1 225 ? -1.263  10.159  -22.572 1.00 123.38 ? 411 TYR B CD1 1 
ATOM   1628 C CD2 . TYR A 1 225 ? -1.687  8.135   -21.387 1.00 120.31 ? 411 TYR B CD2 1 
ATOM   1629 C CE1 . TYR A 1 225 ? -1.434  9.494   -23.777 1.00 129.97 ? 411 TYR B CE1 1 
ATOM   1630 C CE2 . TYR A 1 225 ? -1.862  7.462   -22.583 1.00 125.45 ? 411 TYR B CE2 1 
ATOM   1631 C CZ  . TYR A 1 225 ? -1.734  8.144   -23.776 1.00 128.29 ? 411 TYR B CZ  1 
ATOM   1632 O OH  . TYR A 1 225 ? -1.905  7.468   -24.965 1.00 121.54 ? 411 TYR B OH  1 
ATOM   1633 N N   . GLN A 1 228 ? -5.317  11.636  -26.540 1.00 118.32 ? 414 GLN B N   1 
ATOM   1634 C CA  . GLN A 1 228 ? -4.238  12.598  -26.709 1.00 126.96 ? 414 GLN B CA  1 
ATOM   1635 C C   . GLN A 1 228 ? -2.926  11.870  -26.996 1.00 141.71 ? 414 GLN B C   1 
ATOM   1636 O O   . GLN A 1 228 ? -2.716  10.760  -26.490 1.00 144.67 ? 414 GLN B O   1 
ATOM   1637 C CB  . GLN A 1 228 ? -4.080  13.458  -25.461 1.00 130.22 ? 414 GLN B CB  1 
ATOM   1638 C CG  . GLN A 1 228 ? -3.330  12.742  -24.345 1.00 126.67 ? 414 GLN B CG  1 
ATOM   1639 C CD  . GLN A 1 228 ? -3.032  13.648  -23.186 1.00 124.90 ? 414 GLN B CD  1 
ATOM   1640 O OE1 . GLN A 1 228 ? -3.571  14.743  -23.100 1.00 132.25 ? 414 GLN B OE1 1 
ATOM   1641 N NE2 . GLN A 1 228 ? -2.123  13.223  -22.316 1.00 116.70 ? 414 GLN B NE2 1 
ATOM   1642 N N   . THR A 1 229 ? -2.074  12.522  -27.806 1.00 157.94 ? 415 THR B N   1 
ATOM   1643 C CA  . THR A 1 229 ? -0.745  12.091  -28.256 1.00 158.82 ? 415 THR B CA  1 
ATOM   1644 C C   . THR A 1 229 ? -0.513  10.608  -27.956 1.00 161.72 ? 415 THR B C   1 
ATOM   1645 O O   . THR A 1 229 ? -1.317  9.777   -28.392 1.00 160.61 ? 415 THR B O   1 
ATOM   1646 C CB  . THR A 1 229 ? 0.318   13.000  -27.614 1.00 149.19 ? 415 THR B CB  1 
ATOM   1647 O OG1 . THR A 1 229 ? 0.014   14.360  -27.939 1.00 160.38 ? 415 THR B OG1 1 
ATOM   1648 C CG2 . THR A 1 229 ? 1.709   12.739  -28.210 1.00 145.33 ? 415 THR B CG2 1 
ATOM   1649 N N   . ASP A 1 230 ? 0.590   10.229  -27.286 1.00 141.31 ? 416 ASP B N   1 
ATOM   1650 C CA  . ASP A 1 230 ? 0.657   8.915   -26.651 1.00 139.33 ? 416 ASP B CA  1 
ATOM   1651 C C   . ASP A 1 230 ? 1.566   8.905   -25.413 1.00 134.86 ? 416 ASP B C   1 
ATOM   1652 O O   . ASP A 1 230 ? 2.110   7.852   -25.068 1.00 127.38 ? 416 ASP B O   1 
ATOM   1653 C CB  . ASP A 1 230 ? 1.091   7.834   -27.663 1.00 140.37 ? 416 ASP B CB  1 
ATOM   1654 C CG  . ASP A 1 230 ? 0.936   6.418   -27.114 1.00 139.73 ? 416 ASP B CG  1 
ATOM   1655 O OD1 . ASP A 1 230 ? -0.224  5.985   -26.926 1.00 129.36 ? 416 ASP B OD1 1 
ATOM   1656 O OD2 . ASP A 1 230 ? 1.968   5.748   -26.867 1.00 130.39 ? 416 ASP B OD2 1 
ATOM   1657 N N   . GLN A 1 231 ? 1.747   10.033  -24.720 1.00 131.01 ? 417 GLN B N   1 
ATOM   1658 C CA  . GLN A 1 231 ? 2.791   10.057  -23.701 1.00 124.48 ? 417 GLN B CA  1 
ATOM   1659 C C   . GLN A 1 231 ? 2.326   10.709  -22.404 1.00 118.61 ? 417 GLN B C   1 
ATOM   1660 O O   . GLN A 1 231 ? 1.351   11.464  -22.368 1.00 113.72 ? 417 GLN B O   1 
ATOM   1661 C CB  . GLN A 1 231 ? 4.023   10.827  -24.196 1.00 115.72 ? 417 GLN B CB  1 
ATOM   1662 C CG  . GLN A 1 231 ? 4.710   10.236  -25.402 1.00 118.89 ? 417 GLN B CG  1 
ATOM   1663 C CD  . GLN A 1 231 ? 5.867   11.096  -25.865 1.00 124.23 ? 417 GLN B CD  1 
ATOM   1664 O OE1 . GLN A 1 231 ? 6.003   12.249  -25.450 1.00 124.35 ? 417 GLN B OE1 1 
ATOM   1665 N NE2 . GLN A 1 231 ? 6.703   10.546  -26.736 1.00 124.74 ? 417 GLN B NE2 1 
ATOM   1666 N N   . ASN A 1 232 ? 3.077   10.426  -21.334 1.00 110.34 ? 418 ASN B N   1 
ATOM   1667 C CA  . ASN A 1 232 ? 2.906   11.103  -20.055 1.00 102.27 ? 418 ASN B CA  1 
ATOM   1668 C C   . ASN A 1 232 ? 3.827   12.315  -20.055 1.00 94.69  ? 418 ASN B C   1 
ATOM   1669 O O   . ASN A 1 232 ? 5.051   12.172  -20.139 1.00 91.25  ? 418 ASN B O   1 
ATOM   1670 C CB  . ASN A 1 232 ? 3.244   10.180  -18.883 1.00 99.42  ? 418 ASN B CB  1 
ATOM   1671 C CG  . ASN A 1 232 ? 2.396   8.926   -18.852 1.00 104.29 ? 418 ASN B CG  1 
ATOM   1672 O OD1 . ASN A 1 232 ? 1.419   8.800   -19.589 1.00 114.13 ? 418 ASN B OD1 1 
ATOM   1673 N ND2 . ASN A 1 232 ? 2.767   7.987   -17.987 1.00 93.66  ? 418 ASN B ND2 1 
ATOM   1674 N N   . ILE A 1 233 ? 3.239   13.502  -19.978 1.00 94.23  ? 419 ILE B N   1 
ATOM   1675 C CA  . ILE A 1 233 ? 3.979   14.750  -20.079 1.00 93.97  ? 419 ILE B CA  1 
ATOM   1676 C C   . ILE A 1 233 ? 4.009   15.380  -18.685 1.00 88.08  ? 419 ILE B C   1 
ATOM   1677 O O   . ILE A 1 233 ? 3.299   14.953  -17.776 1.00 88.32  ? 419 ILE B O   1 
ATOM   1678 C CB  . ILE A 1 233 ? 3.364   15.688  -21.146 1.00 97.32  ? 419 ILE B CB  1 
ATOM   1679 C CG1 . ILE A 1 233 ? 4.256   16.910  -21.420 1.00 105.80 ? 419 ILE B CG1 1 
ATOM   1680 C CG2 . ILE A 1 233 ? 1.952   16.099  -20.740 1.00 83.92  ? 419 ILE B CG2 1 
ATOM   1681 C CD1 . ILE A 1 233 ? 3.853   17.709  -22.653 1.00 86.91  ? 419 ILE B CD1 1 
ATOM   1682 N N   . LYS A 1 234 ? 4.838   16.408  -18.519 1.00 82.29  ? 420 LYS B N   1 
ATOM   1683 C CA  . LYS A 1 234 ? 5.019   17.041  -17.223 1.00 81.02  ? 420 LYS B CA  1 
ATOM   1684 C C   . LYS A 1 234 ? 4.057   18.205  -17.058 1.00 86.79  ? 420 LYS B C   1 
ATOM   1685 O O   . LYS A 1 234 ? 3.761   18.929  -18.014 1.00 91.32  ? 420 LYS B O   1 
ATOM   1686 C CB  . LYS A 1 234 ? 6.449   17.570  -17.063 1.00 79.94  ? 420 LYS B CB  1 
ATOM   1687 C CG  . LYS A 1 234 ? 7.539   16.525  -17.080 1.00 80.70  ? 420 LYS B CG  1 
ATOM   1688 C CD  . LYS A 1 234 ? 8.733   17.006  -17.888 1.00 89.55  ? 420 LYS B CD  1 
ATOM   1689 C CE  . LYS A 1 234 ? 9.194   18.387  -17.454 1.00 89.60  ? 420 LYS B CE  1 
ATOM   1690 N NZ  . LYS A 1 234 ? 10.136  18.965  -18.451 1.00 89.68  ? 420 LYS B NZ  1 
ATOM   1691 N N   . ILE A 1 235 ? 3.556   18.371  -15.840 1.00 82.77  ? 421 ILE B N   1 
ATOM   1692 C CA  . ILE A 1 235 ? 2.771   19.539  -15.469 1.00 79.94  ? 421 ILE B CA  1 
ATOM   1693 C C   . ILE A 1 235 ? 3.761   20.501  -14.825 1.00 84.18  ? 421 ILE B C   1 
ATOM   1694 O O   . ILE A 1 235 ? 4.126   20.354  -13.654 1.00 78.27  ? 421 ILE B O   1 
ATOM   1695 C CB  . ILE A 1 235 ? 1.617   19.182  -14.528 1.00 79.27  ? 421 ILE B CB  1 
ATOM   1696 C CG1 . ILE A 1 235 ? 0.664   18.204  -15.208 1.00 80.56  ? 421 ILE B CG1 1 
ATOM   1697 C CG2 . ILE A 1 235 ? 0.864   20.427  -14.103 1.00 79.76  ? 421 ILE B CG2 1 
ATOM   1698 C CD1 . ILE A 1 235 ? -0.520  17.847  -14.361 1.00 80.37  ? 421 ILE B CD1 1 
ATOM   1699 N N   . ASN A 1 236 ? 4.203   21.492  -15.594 1.00 83.81  ? 422 ASN B N   1 
ATOM   1700 C CA  . ASN A 1 236 ? 5.212   22.428  -15.125 1.00 79.10  ? 422 ASN B CA  1 
ATOM   1701 C C   . ASN A 1 236 ? 4.623   23.551  -14.297 1.00 79.09  ? 422 ASN B C   1 
ATOM   1702 O O   . ASN A 1 236 ? 5.299   24.564  -14.077 1.00 79.14  ? 422 ASN B O   1 
ATOM   1703 C CB  . ASN A 1 236 ? 5.971   23.010  -16.319 1.00 80.54  ? 422 ASN B CB  1 
ATOM   1704 C CG  . ASN A 1 236 ? 6.606   21.940  -17.181 1.00 80.94  ? 422 ASN B CG  1 
ATOM   1705 O OD1 . ASN A 1 236 ? 7.022   20.891  -16.686 1.00 81.73  ? 422 ASN B OD1 1 
ATOM   1706 N ND2 . ASN A 1 236 ? 6.684   22.199  -18.483 1.00 82.86  ? 422 ASN B ND2 1 
ATOM   1707 N N   . ASP A 1 237 ? 3.401   23.373  -13.801 1.00 81.01  ? 423 ASP B N   1 
ATOM   1708 C CA  . ASP A 1 237 ? 2.711   24.442  -13.103 1.00 80.20  ? 423 ASP B CA  1 
ATOM   1709 C C   . ASP A 1 237 ? 3.409   24.770  -11.789 1.00 78.10  ? 423 ASP B C   1 
ATOM   1710 O O   . ASP A 1 237 ? 4.132   23.953  -11.207 1.00 76.59  ? 423 ASP B O   1 
ATOM   1711 C CB  . ASP A 1 237 ? 1.248   24.070  -12.841 1.00 80.07  ? 423 ASP B CB  1 
ATOM   1712 C CG  . ASP A 1 237 ? 0.465   23.806  -14.119 1.00 81.86  ? 423 ASP B CG  1 
ATOM   1713 O OD1 . ASP A 1 237 ? 1.085   23.753  -15.203 1.00 84.20  ? 423 ASP B OD1 1 
ATOM   1714 O OD2 . ASP A 1 237 ? -0.777  23.664  -14.039 1.00 82.69  ? 423 ASP B OD2 1 
ATOM   1715 N N   . ARG A 1 238 ? 3.182   25.996  -11.331 1.00 78.80  ? 424 ARG B N   1 
ATOM   1716 C CA  . ARG A 1 238 ? 3.742   26.439  -10.067 1.00 80.59  ? 424 ARG B CA  1 
ATOM   1717 C C   . ARG A 1 238 ? 3.039   25.738  -8.914  1.00 82.13  ? 424 ARG B C   1 
ATOM   1718 O O   . ARG A 1 238 ? 1.811   25.614  -8.893  1.00 84.78  ? 424 ARG B O   1 
ATOM   1719 C CB  . ARG A 1 238 ? 3.596   27.954  -9.932  1.00 79.25  ? 424 ARG B CB  1 
ATOM   1720 C CG  . ARG A 1 238 ? 4.140   28.529  -8.640  1.00 81.97  ? 424 ARG B CG  1 
ATOM   1721 C CD  . ARG A 1 238 ? 3.617   29.936  -8.430  1.00 85.39  ? 424 ARG B CD  1 
ATOM   1722 N NE  . ARG A 1 238 ? 4.219   30.577  -7.270  1.00 83.79  ? 424 ARG B NE  1 
ATOM   1723 C CZ  . ARG A 1 238 ? 5.355   31.258  -7.306  1.00 83.06  ? 424 ARG B CZ  1 
ATOM   1724 N NH1 . ARG A 1 238 ? 6.040   31.396  -8.429  1.00 91.70  ? 424 ARG B NH1 1 
ATOM   1725 N NH2 . ARG A 1 238 ? 5.813   31.815  -6.189  1.00 81.24  ? 424 ARG B NH2 1 
ATOM   1726 N N   . PHE A 1 239 ? 3.829   25.276  -7.951  1.00 78.35  ? 425 PHE B N   1 
ATOM   1727 C CA  . PHE A 1 239 ? 3.290   24.602  -6.780  1.00 77.98  ? 425 PHE B CA  1 
ATOM   1728 C C   . PHE A 1 239 ? 4.166   24.965  -5.596  1.00 74.17  ? 425 PHE B C   1 
ATOM   1729 O O   . PHE A 1 239 ? 5.385   24.774  -5.638  1.00 76.04  ? 425 PHE B O   1 
ATOM   1730 C CB  . PHE A 1 239 ? 3.250   23.082  -6.971  1.00 77.64  ? 425 PHE B CB  1 
ATOM   1731 C CG  . PHE A 1 239 ? 2.670   22.340  -5.801  1.00 73.33  ? 425 PHE B CG  1 
ATOM   1732 C CD1 . PHE A 1 239 ? 1.305   22.161  -5.693  1.00 74.09  ? 425 PHE B CD1 1 
ATOM   1733 C CD2 . PHE A 1 239 ? 3.489   21.825  -4.810  1.00 73.72  ? 425 PHE B CD2 1 
ATOM   1734 C CE1 . PHE A 1 239 ? 0.765   21.480  -4.622  1.00 75.78  ? 425 PHE B CE1 1 
ATOM   1735 C CE2 . PHE A 1 239 ? 2.955   21.145  -3.737  1.00 72.04  ? 425 PHE B CE2 1 
ATOM   1736 C CZ  . PHE A 1 239 ? 1.592   20.972  -3.643  1.00 72.80  ? 425 PHE B CZ  1 
ATOM   1737 N N   . GLU A 1 240 ? 3.540   25.470  -4.543  1.00 74.68  ? 426 GLU B N   1 
ATOM   1738 C CA  . GLU A 1 240 ? 4.256   25.992  -3.395  1.00 74.59  ? 426 GLU B CA  1 
ATOM   1739 C C   . GLU A 1 240 ? 4.225   24.980  -2.261  1.00 74.86  ? 426 GLU B C   1 
ATOM   1740 O O   . GLU A 1 240 ? 3.201   24.337  -2.010  1.00 73.83  ? 426 GLU B O   1 
ATOM   1741 C CB  . GLU A 1 240 ? 3.648   27.318  -2.939  1.00 76.12  ? 426 GLU B CB  1 
ATOM   1742 C CG  . GLU A 1 240 ? 3.668   28.393  -4.012  1.00 77.84  ? 426 GLU B CG  1 
ATOM   1743 C CD  . GLU A 1 240 ? 2.965   29.662  -3.581  1.00 86.54  ? 426 GLU B CD  1 
ATOM   1744 O OE1 . GLU A 1 240 ? 2.386   29.676  -2.471  1.00 92.11  ? 426 GLU B OE1 1 
ATOM   1745 O OE2 . GLU A 1 240 ? 3.001   30.647  -4.349  1.00 80.27  ? 426 GLU B OE2 1 
ATOM   1746 N N   . PHE A 1 241 ? 5.358   24.843  -1.583  1.00 73.13  ? 427 PHE B N   1 
ATOM   1747 C CA  . PHE A 1 241 ? 5.469   24.012  -0.402  1.00 72.65  ? 427 PHE B CA  1 
ATOM   1748 C C   . PHE A 1 241 ? 6.207   24.822  0.655   1.00 73.24  ? 427 PHE B C   1 
ATOM   1749 O O   . PHE A 1 241 ? 7.232   25.454  0.348   1.00 73.26  ? 427 PHE B O   1 
ATOM   1750 C CB  . PHE A 1 241 ? 6.201   22.699  -0.707  1.00 71.38  ? 427 PHE B CB  1 
ATOM   1751 C CG  . PHE A 1 241 ? 7.510   22.885  -1.422  1.00 70.90  ? 427 PHE B CG  1 
ATOM   1752 C CD1 . PHE A 1 241 ? 7.554   22.936  -2.804  1.00 70.83  ? 427 PHE B CD1 1 
ATOM   1753 C CD2 . PHE A 1 241 ? 8.696   23.000  -0.715  1.00 74.50  ? 427 PHE B CD2 1 
ATOM   1754 C CE1 . PHE A 1 241 ? 8.754   23.107  -3.469  1.00 70.58  ? 427 PHE B CE1 1 
ATOM   1755 C CE2 . PHE A 1 241 ? 9.900   23.173  -1.376  1.00 70.42  ? 427 PHE B CE2 1 
ATOM   1756 C CZ  . PHE A 1 241 ? 9.927   23.224  -2.755  1.00 72.19  ? 427 PHE B CZ  1 
ATOM   1757 N N   . PRO A 1 242 ? 5.712   24.863  1.886   1.00 73.96  ? 428 PRO B N   1 
ATOM   1758 C CA  . PRO A 1 242 ? 6.345   25.693  2.911   1.00 74.91  ? 428 PRO B CA  1 
ATOM   1759 C C   . PRO A 1 242 ? 7.488   24.975  3.615   1.00 74.59  ? 428 PRO B C   1 
ATOM   1760 O O   . PRO A 1 242 ? 7.559   23.745  3.669   1.00 73.79  ? 428 PRO B O   1 
ATOM   1761 C CB  . PRO A 1 242 ? 5.191   25.966  3.882   1.00 76.23  ? 428 PRO B CB  1 
ATOM   1762 C CG  . PRO A 1 242 ? 4.365   24.726  3.799   1.00 75.50  ? 428 PRO B CG  1 
ATOM   1763 C CD  . PRO A 1 242 ? 4.478   24.225  2.375   1.00 74.26  ? 428 PRO B CD  1 
ATOM   1764 N N   . GLU A 1 243 ? 8.392   25.785  4.165   1.00 75.09  ? 429 GLU B N   1 
ATOM   1765 C CA  . GLU A 1 243 ? 9.469   25.234  4.977   1.00 77.17  ? 429 GLU B CA  1 
ATOM   1766 C C   . GLU A 1 243 ? 8.921   24.532  6.209   1.00 77.63  ? 429 GLU B C   1 
ATOM   1767 O O   . GLU A 1 243 ? 9.483   23.525  6.657   1.00 75.05  ? 429 GLU B O   1 
ATOM   1768 C CB  . GLU A 1 243 ? 10.440  26.346  5.376   1.00 81.60  ? 429 GLU B CB  1 
ATOM   1769 C CG  . GLU A 1 243 ? 11.628  25.875  6.192   1.00 86.52  ? 429 GLU B CG  1 
ATOM   1770 C CD  . GLU A 1 243 ? 12.594  26.998  6.507   1.00 91.84  ? 429 GLU B CD  1 
ATOM   1771 O OE1 . GLU A 1 243 ? 12.129  28.149  6.654   1.00 84.38  ? 429 GLU B OE1 1 
ATOM   1772 O OE2 . GLU A 1 243 ? 13.812  26.721  6.614   1.00 89.82  ? 429 GLU B OE2 1 
ATOM   1773 N N   . GLN A 1 244 ? 7.826   25.043  6.760   1.00 78.94  ? 430 GLN B N   1 
ATOM   1774 C CA  . GLN A 1 244 ? 7.162   24.446  7.906   1.00 77.57  ? 430 GLN B CA  1 
ATOM   1775 C C   . GLN A 1 244 ? 5.721   24.153  7.515   1.00 77.46  ? 430 GLN B C   1 
ATOM   1776 O O   . GLN A 1 244 ? 5.001   25.053  7.070   1.00 78.06  ? 430 GLN B O   1 
ATOM   1777 C CB  . GLN A 1 244 ? 7.243   25.383  9.116   1.00 79.66  ? 430 GLN B CB  1 
ATOM   1778 C CG  . GLN A 1 244 ? 8.688   25.725  9.479   1.00 87.59  ? 430 GLN B CG  1 
ATOM   1779 C CD  . GLN A 1 244 ? 8.811   26.659  10.662  1.00 99.18  ? 430 GLN B CD  1 
ATOM   1780 O OE1 . GLN A 1 244 ? 7.957   27.517  10.886  1.00 106.03 ? 430 GLN B OE1 1 
ATOM   1781 N NE2 . GLN A 1 244 ? 9.896   26.514  11.415  1.00 104.21 ? 430 GLN B NE2 1 
ATOM   1782 N N   . LEU A 1 245 ? 5.304   22.900  7.689   1.00 76.89  ? 431 LEU B N   1 
ATOM   1783 C CA  . LEU A 1 245 ? 4.013   22.424  7.191   1.00 76.66  ? 431 LEU B CA  1 
ATOM   1784 C C   . LEU A 1 245 ? 3.122   21.990  8.346   1.00 79.51  ? 431 LEU B C   1 
ATOM   1785 O O   . LEU A 1 245 ? 3.292   20.880  8.884   1.00 80.62  ? 431 LEU B O   1 
ATOM   1786 C CB  . LEU A 1 245 ? 4.214   21.268  6.211   1.00 74.99  ? 431 LEU B CB  1 
ATOM   1787 C CG  . LEU A 1 245 ? 2.947   20.773  5.514   1.00 74.81  ? 431 LEU B CG  1 
ATOM   1788 C CD1 . LEU A 1 245 ? 2.351   21.886  4.674   1.00 75.16  ? 431 LEU B CD1 1 
ATOM   1789 C CD2 . LEU A 1 245 ? 3.221   19.539  4.668   1.00 73.47  ? 431 LEU B CD2 1 
ATOM   1790 N N   . PRO A 1 246 ? 2.159   22.817  8.759   1.00 84.56  ? 432 PRO B N   1 
ATOM   1791 C CA  . PRO A 1 246 ? 1.202   22.390  9.791   1.00 81.44  ? 432 PRO B CA  1 
ATOM   1792 C C   . PRO A 1 246 ? 0.130   21.496  9.182   1.00 80.39  ? 432 PRO B C   1 
ATOM   1793 O O   . PRO A 1 246 ? -0.471  21.834  8.161   1.00 79.93  ? 432 PRO B O   1 
ATOM   1794 C CB  . PRO A 1 246 ? 0.611   23.711  10.293  1.00 82.90  ? 432 PRO B CB  1 
ATOM   1795 C CG  . PRO A 1 246 ? 0.694   24.619  9.097   1.00 86.26  ? 432 PRO B CG  1 
ATOM   1796 C CD  . PRO A 1 246 ? 1.939   24.213  8.340   1.00 83.29  ? 432 PRO B CD  1 
ATOM   1797 N N   . LEU A 1 247 ? -0.106  20.346  9.814   1.00 81.61  ? 433 LEU B N   1 
ATOM   1798 C CA  . LEU A 1 247 ? -1.065  19.376  9.300   1.00 80.25  ? 433 LEU B CA  1 
ATOM   1799 C C   . LEU A 1 247 ? -2.050  18.911  10.367  1.00 85.04  ? 433 LEU B C   1 
ATOM   1800 O O   . LEU A 1 247 ? -2.674  17.857  10.203  1.00 86.47  ? 433 LEU B O   1 
ATOM   1801 C CB  . LEU A 1 247 ? -0.342  18.173  8.695   1.00 78.60  ? 433 LEU B CB  1 
ATOM   1802 C CG  . LEU A 1 247 ? 0.577   18.452  7.510   1.00 76.91  ? 433 LEU B CG  1 
ATOM   1803 C CD1 . LEU A 1 247 ? 1.204   17.160  7.025   1.00 77.14  ? 433 LEU B CD1 1 
ATOM   1804 C CD2 . LEU A 1 247 ? -0.195  19.129  6.398   1.00 76.71  ? 433 LEU B CD2 1 
ATOM   1805 N N   . ASP A 1 248 ? -2.197  19.665  11.461  1.00 88.95  ? 434 ASP B N   1 
ATOM   1806 C CA  . ASP A 1 248 ? -3.132  19.269  12.512  1.00 91.09  ? 434 ASP B CA  1 
ATOM   1807 C C   . ASP A 1 248 ? -4.569  19.227  11.998  1.00 93.58  ? 434 ASP B C   1 
ATOM   1808 O O   . ASP A 1 248 ? -5.334  18.320  12.348  1.00 91.95  ? 434 ASP B O   1 
ATOM   1809 C CB  . ASP A 1 248 ? -3.021  20.227  13.704  1.00 90.25  ? 434 ASP B CB  1 
ATOM   1810 C CG  . ASP A 1 248 ? -2.335  19.600  14.918  1.00 92.44  ? 434 ASP B CG  1 
ATOM   1811 O OD1 . ASP A 1 248 ? -2.135  18.367  14.940  1.00 97.94  ? 434 ASP B OD1 1 
ATOM   1812 O OD2 . ASP A 1 248 ? -2.008  20.347  15.866  1.00 93.05  ? 434 ASP B OD2 1 
ATOM   1813 N N   . GLU A 1 249 ? -4.951  20.183  11.146  1.00 90.95  ? 435 GLU B N   1 
ATOM   1814 C CA  . GLU A 1 249 ? -6.345  20.281  10.723  1.00 93.73  ? 435 GLU B CA  1 
ATOM   1815 C C   . GLU A 1 249 ? -6.776  19.133  9.818   1.00 91.05  ? 435 GLU B C   1 
ATOM   1816 O O   . GLU A 1 249 ? -7.982  18.903  9.670   1.00 93.30  ? 435 GLU B O   1 
ATOM   1817 C CB  . GLU A 1 249 ? -6.589  21.609  10.012  1.00 87.17  ? 435 GLU B CB  1 
ATOM   1818 C CG  . GLU A 1 249 ? -5.695  21.830  8.820   1.00 89.75  ? 435 GLU B CG  1 
ATOM   1819 C CD  . GLU A 1 249 ? -5.916  23.181  8.189   1.00 96.64  ? 435 GLU B CD  1 
ATOM   1820 O OE1 . GLU A 1 249 ? -6.949  23.814  8.493   1.00 87.48  ? 435 GLU B OE1 1 
ATOM   1821 O OE2 . GLU A 1 249 ? -5.058  23.607  7.387   1.00 102.58 ? 435 GLU B OE2 1 
ATOM   1822 N N   . PHE A 1 250 ? -5.834  18.398  9.230   1.00 84.94  ? 436 PHE B N   1 
ATOM   1823 C CA  . PHE A 1 250 ? -6.172  17.238  8.416   1.00 82.98  ? 436 PHE B CA  1 
ATOM   1824 C C   . PHE A 1 250 ? -6.201  15.946  9.221   1.00 83.51  ? 436 PHE B C   1 
ATOM   1825 O O   . PHE A 1 250 ? -6.551  14.897  8.672   1.00 83.13  ? 436 PHE B O   1 
ATOM   1826 C CB  . PHE A 1 250 ? -5.196  17.103  7.244   1.00 80.89  ? 436 PHE B CB  1 
ATOM   1827 C CG  . PHE A 1 250 ? -5.155  18.310  6.348   1.00 83.45  ? 436 PHE B CG  1 
ATOM   1828 C CD1 . PHE A 1 250 ? -6.121  18.494  5.377   1.00 80.80  ? 436 PHE B CD1 1 
ATOM   1829 C CD2 . PHE A 1 250 ? -4.161  19.266  6.486   1.00 82.67  ? 436 PHE B CD2 1 
ATOM   1830 C CE1 . PHE A 1 250 ? -6.091  19.601  4.551   1.00 80.69  ? 436 PHE B CE1 1 
ATOM   1831 C CE2 . PHE A 1 250 ? -4.129  20.378  5.663   1.00 79.91  ? 436 PHE B CE2 1 
ATOM   1832 C CZ  . PHE A 1 250 ? -5.095  20.546  4.696   1.00 80.24  ? 436 PHE B CZ  1 
ATOM   1833 N N   . LEU A 1 251 ? -5.853  16.001  10.503  1.00 84.61  ? 437 LEU B N   1 
ATOM   1834 C CA  . LEU A 1 251 ? -6.022  14.865  11.391  1.00 85.67  ? 437 LEU B CA  1 
ATOM   1835 C C   . LEU A 1 251 ? -7.461  14.808  11.882  1.00 88.26  ? 437 LEU B C   1 
ATOM   1836 O O   . LEU A 1 251 ? -8.075  15.844  12.153  1.00 88.94  ? 437 LEU B O   1 
ATOM   1837 C CB  . LEU A 1 251 ? -5.081  14.973  12.586  1.00 87.08  ? 437 LEU B CB  1 
ATOM   1838 C CG  . LEU A 1 251 ? -3.587  14.898  12.302  1.00 84.65  ? 437 LEU B CG  1 
ATOM   1839 C CD1 . LEU A 1 251 ? -2.818  15.059  13.599  1.00 85.90  ? 437 LEU B CD1 1 
ATOM   1840 C CD2 . LEU A 1 251 ? -3.255  13.585  11.623  1.00 83.37  ? 437 LEU B CD2 1 
ATOM   1841 N N   . GLN A 1 252 ? -7.999  13.589  12.002  1.00 88.36  ? 438 GLN B N   1 
ATOM   1842 C CA  . GLN A 1 252 ? -9.369  13.447  12.487  1.00 91.04  ? 438 GLN B CA  1 
ATOM   1843 C C   . GLN A 1 252 ? -9.515  14.021  13.889  1.00 94.58  ? 438 GLN B C   1 
ATOM   1844 O O   . GLN A 1 252 ? -10.497 14.712  14.185  1.00 94.46  ? 438 GLN B O   1 
ATOM   1845 C CB  . GLN A 1 252 ? -9.800  11.982  12.455  1.00 90.99  ? 438 GLN B CB  1 
ATOM   1846 C CG  . GLN A 1 252 ? -11.299 11.802  12.636  1.00 96.87  ? 438 GLN B CG  1 
ATOM   1847 C CD  . GLN A 1 252 ? -11.744 10.367  12.445  1.00 100.99 ? 438 GLN B CD  1 
ATOM   1848 O OE1 . GLN A 1 252 ? -10.922 9.451   12.412  1.00 93.60  ? 438 GLN B OE1 1 
ATOM   1849 N NE2 . GLN A 1 252 ? -13.048 10.167  12.284  1.00 100.86 ? 438 GLN B NE2 1 
ATOM   1850 N N   . LYS A 1 253 ? -8.560  13.735  14.768  1.00 99.77  ? 439 LYS B N   1 
ATOM   1851 C CA  . LYS A 1 253 ? -8.503  14.367  16.080  1.00 96.35  ? 439 LYS B CA  1 
ATOM   1852 C C   . LYS A 1 253 ? -7.052  14.712  16.372  1.00 94.14  ? 439 LYS B C   1 
ATOM   1853 O O   . LYS A 1 253 ? -6.205  13.817  16.454  1.00 93.35  ? 439 LYS B O   1 
ATOM   1854 C CB  . LYS A 1 253 ? -9.087  13.474  17.176  1.00 97.57  ? 439 LYS B CB  1 
ATOM   1855 C CG  . LYS A 1 253 ? -9.193  14.189  18.516  1.00 101.85 ? 439 LYS B CG  1 
ATOM   1856 C CD  . LYS A 1 253 ? -9.807  13.317  19.598  1.00 106.62 ? 439 LYS B CD  1 
ATOM   1857 C CE  . LYS A 1 253 ? -9.947  14.092  20.904  1.00 105.99 ? 439 LYS B CE  1 
ATOM   1858 N NZ  . LYS A 1 253 ? -10.500 13.255  22.009  1.00 114.88 ? 439 LYS B NZ  1 
ATOM   1859 N N   . THR A 1 254 ? -6.767  16.005  16.503  1.00 94.34  ? 440 THR B N   1 
ATOM   1860 C CA  . THR A 1 254 ? -5.417  16.454  16.783  1.00 93.66  ? 440 THR B CA  1 
ATOM   1861 C C   . THR A 1 254 ? -5.006  16.075  18.203  1.00 100.47 ? 440 THR B C   1 
ATOM   1862 O O   . THR A 1 254 ? -5.837  15.773  19.065  1.00 98.22  ? 440 THR B O   1 
ATOM   1863 C CB  . THR A 1 254 ? -5.314  17.971  16.608  1.00 93.77  ? 440 THR B CB  1 
ATOM   1864 O OG1 . THR A 1 254 ? -5.861  18.623  17.761  1.00 96.68  ? 440 THR B OG1 1 
ATOM   1865 C CG2 . THR A 1 254 ? -6.089  18.413  15.381  1.00 92.56  ? 440 THR B CG2 1 
ATOM   1866 N N   . ASP A 1 255 ? -3.701  16.104  18.440  1.00 105.44 ? 441 ASP B N   1 
ATOM   1867 C CA  . ASP A 1 255 ? -3.143  15.797  19.755  1.00 101.47 ? 441 ASP B CA  1 
ATOM   1868 C C   . ASP A 1 255 ? -2.376  17.001  20.282  1.00 104.64 ? 441 ASP B C   1 
ATOM   1869 O O   . ASP A 1 255 ? -1.343  17.377  19.695  1.00 105.49 ? 441 ASP B O   1 
ATOM   1870 C CB  . ASP A 1 255 ? -2.232  14.571  19.686  1.00 97.74  ? 441 ASP B CB  1 
ATOM   1871 C CG  . ASP A 1 255 ? -1.588  14.255  21.019  1.00 101.43 ? 441 ASP B CG  1 
ATOM   1872 O OD1 . ASP A 1 255 ? -2.314  13.818  21.934  1.00 108.36 ? 441 ASP B OD1 1 
ATOM   1873 O OD2 . ASP A 1 255 ? -0.364  14.451  21.160  1.00 103.62 ? 441 ASP B OD2 1 
ATOM   1874 N N   . PRO A 1 256 ? -2.843  17.651  21.351  1.00 118.28 ? 442 PRO B N   1 
ATOM   1875 C CA  . PRO A 1 256 ? -2.020  18.667  22.017  1.00 118.95 ? 442 PRO B CA  1 
ATOM   1876 C C   . PRO A 1 256 ? -0.732  18.064  22.557  1.00 112.27 ? 442 PRO B C   1 
ATOM   1877 O O   . PRO A 1 256 ? -0.634  16.861  22.806  1.00 117.36 ? 442 PRO B O   1 
ATOM   1878 C CB  . PRO A 1 256 ? -2.921  19.171  23.153  1.00 114.16 ? 442 PRO B CB  1 
ATOM   1879 C CG  . PRO A 1 256 ? -4.315  18.860  22.693  1.00 105.98 ? 442 PRO B CG  1 
ATOM   1880 C CD  . PRO A 1 256 ? -4.197  17.569  21.930  1.00 103.53 ? 442 PRO B CD  1 
ATOM   1881 N N   . LYS A 1 257 ? 0.277   18.924  22.702  1.00 124.01 ? 443 LYS B N   1 
ATOM   1882 C CA  . LYS A 1 257 ? 1.649   18.586  23.085  1.00 128.33 ? 443 LYS B CA  1 
ATOM   1883 C C   . LYS A 1 257 ? 2.367   17.795  21.992  1.00 132.64 ? 443 LYS B C   1 
ATOM   1884 O O   . LYS A 1 257 ? 3.562   17.496  22.140  1.00 130.22 ? 443 LYS B O   1 
ATOM   1885 C CB  . LYS A 1 257 ? 1.723   17.817  24.416  1.00 128.26 ? 443 LYS B CB  1 
ATOM   1886 C CG  . LYS A 1 257 ? 3.104   17.817  25.072  1.00 137.58 ? 443 LYS B CG  1 
ATOM   1887 C CD  . LYS A 1 257 ? 3.139   16.984  26.345  1.00 152.83 ? 443 LYS B CD  1 
ATOM   1888 C CE  . LYS A 1 257 ? 4.571   16.804  26.842  1.00 141.33 ? 443 LYS B CE  1 
ATOM   1889 N NZ  . LYS A 1 257 ? 4.624   16.127  28.170  1.00 140.43 ? 443 LYS B NZ  1 
ATOM   1890 N N   . ASP A 1 258 ? 1.694   17.474  20.884  1.00 117.96 ? 444 ASP B N   1 
ATOM   1891 C CA  . ASP A 1 258 ? 2.350   16.929  19.693  1.00 102.60 ? 444 ASP B CA  1 
ATOM   1892 C C   . ASP A 1 258 ? 1.544   17.350  18.473  1.00 92.05  ? 444 ASP B C   1 
ATOM   1893 O O   . ASP A 1 258 ? 0.837   16.543  17.858  1.00 93.19  ? 444 ASP B O   1 
ATOM   1894 C CB  . ASP A 1 258 ? 2.467   15.407  19.778  1.00 99.03  ? 444 ASP B CB  1 
ATOM   1895 C CG  . ASP A 1 258 ? 3.515   14.842  18.824  1.00 101.06 ? 444 ASP B CG  1 
ATOM   1896 O OD1 . ASP A 1 258 ? 3.848   15.514  17.825  1.00 101.42 ? 444 ASP B OD1 1 
ATOM   1897 O OD2 . ASP A 1 258 ? 4.010   13.722  19.076  1.00 103.82 ? 444 ASP B OD2 1 
ATOM   1898 N N   . PRO A 1 259 ? 1.622   18.625  18.099  1.00 91.75  ? 445 PRO B N   1 
ATOM   1899 C CA  . PRO A 1 259 ? 0.954   19.073  16.876  1.00 90.83  ? 445 PRO B CA  1 
ATOM   1900 C C   . PRO A 1 259 ? 1.593   18.445  15.654  1.00 87.16  ? 445 PRO B C   1 
ATOM   1901 O O   . PRO A 1 259 ? 2.779   18.108  15.651  1.00 95.09  ? 445 PRO B O   1 
ATOM   1902 C CB  . PRO A 1 259 ? 1.165   20.594  16.886  1.00 90.66  ? 445 PRO B CB  1 
ATOM   1903 C CG  . PRO A 1 259 ? 1.640   20.928  18.264  1.00 93.25  ? 445 PRO B CG  1 
ATOM   1904 C CD  . PRO A 1 259 ? 2.368   19.717  18.741  1.00 94.69  ? 445 PRO B CD  1 
ATOM   1905 N N   . ALA A 1 260 ? 0.795   18.296  14.599  1.00 85.79  ? 446 ALA B N   1 
ATOM   1906 C CA  . ALA A 1 260 ? 1.309   17.778  13.335  1.00 84.60  ? 446 ALA B CA  1 
ATOM   1907 C C   . ALA A 1 260 ? 2.073   18.879  12.594  1.00 82.22  ? 446 ALA B C   1 
ATOM   1908 O O   . ALA A 1 260 ? 1.720   19.307  11.496  1.00 81.08  ? 446 ALA B O   1 
ATOM   1909 C CB  . ALA A 1 260 ? 0.173   17.214  12.492  1.00 82.90  ? 446 ALA B CB  1 
ATOM   1910 N N   . ASN A 1 261 ? 3.162   19.317  13.219  1.00 82.76  ? 447 ASN B N   1 
ATOM   1911 C CA  . ASN A 1 261 ? 4.038   20.332  12.654  1.00 82.00  ? 447 ASN B CA  1 
ATOM   1912 C C   . ASN A 1 261 ? 5.266   19.658  12.059  1.00 80.31  ? 447 ASN B C   1 
ATOM   1913 O O   . ASN A 1 261 ? 5.920   18.846  12.724  1.00 80.68  ? 447 ASN B O   1 
ATOM   1914 C CB  . ASN A 1 261 ? 4.457   21.352  13.714  1.00 84.00  ? 447 ASN B CB  1 
ATOM   1915 C CG  . ASN A 1 261 ? 3.307   22.221  14.167  1.00 85.81  ? 447 ASN B CG  1 
ATOM   1916 O OD1 . ASN A 1 261 ? 2.326   22.396  13.445  1.00 91.59  ? 447 ASN B OD1 1 
ATOM   1917 N ND2 . ASN A 1 261 ? 3.418   22.770  15.370  1.00 96.41  ? 447 ASN B ND2 1 
ATOM   1918 N N   . TYR A 1 262 ? 5.578   20.006  10.814  1.00 78.67  ? 448 TYR B N   1 
ATOM   1919 C CA  . TYR A 1 262 ? 6.639   19.358  10.062  1.00 77.07  ? 448 TYR B CA  1 
ATOM   1920 C C   . TYR A 1 262 ? 7.578   20.401  9.483   1.00 76.57  ? 448 TYR B C   1 
ATOM   1921 O O   . TYR A 1 262 ? 7.186   21.539  9.217   1.00 76.99  ? 448 TYR B O   1 
ATOM   1922 C CB  . TYR A 1 262 ? 6.073   18.480  8.947   1.00 75.62  ? 448 TYR B CB  1 
ATOM   1923 C CG  . TYR A 1 262 ? 5.543   17.171  9.465   1.00 76.00  ? 448 TYR B CG  1 
ATOM   1924 C CD1 . TYR A 1 262 ? 4.316   17.102  10.103  1.00 77.22  ? 448 TYR B CD1 1 
ATOM   1925 C CD2 . TYR A 1 262 ? 6.285   16.009  9.342   1.00 75.35  ? 448 TYR B CD2 1 
ATOM   1926 C CE1 . TYR A 1 262 ? 3.835   15.906  10.593  1.00 77.77  ? 448 TYR B CE1 1 
ATOM   1927 C CE2 . TYR A 1 262 ? 5.815   14.812  9.827   1.00 75.92  ? 448 TYR B CE2 1 
ATOM   1928 C CZ  . TYR A 1 262 ? 4.591   14.764  10.451  1.00 77.13  ? 448 TYR B CZ  1 
ATOM   1929 O OH  . TYR A 1 262 ? 4.128   13.564  10.934  1.00 77.87  ? 448 TYR B OH  1 
ATOM   1930 N N   . ILE A 1 263 ? 8.831   19.996  9.311   1.00 75.88  ? 449 ILE B N   1 
ATOM   1931 C CA  . ILE A 1 263 ? 9.885   20.853  8.787   1.00 75.51  ? 449 ILE B CA  1 
ATOM   1932 C C   . ILE A 1 263 ? 10.403  20.221  7.505   1.00 73.77  ? 449 ILE B C   1 
ATOM   1933 O O   . ILE A 1 263 ? 10.677  19.016  7.468   1.00 73.19  ? 449 ILE B O   1 
ATOM   1934 C CB  . ILE A 1 263 ? 11.015  21.050  9.816   1.00 76.68  ? 449 ILE B CB  1 
ATOM   1935 C CG1 . ILE A 1 263 ? 10.458  21.681  11.095  1.00 78.74  ? 449 ILE B CG1 1 
ATOM   1936 C CG2 . ILE A 1 263 ? 12.140  21.896  9.241   1.00 76.54  ? 449 ILE B CG2 1 
ATOM   1937 C CD1 . ILE A 1 263 ? 11.499  21.952  12.147  1.00 83.70  ? 449 ILE B CD1 1 
ATOM   1938 N N   . LEU A 1 264 ? 10.520  21.029  6.456   1.00 73.15  ? 450 LEU B N   1 
ATOM   1939 C CA  . LEU A 1 264 ? 11.004  20.525  5.179   1.00 71.78  ? 450 LEU B CA  1 
ATOM   1940 C C   . LEU A 1 264 ? 12.438  20.032  5.314   1.00 71.55  ? 450 LEU B C   1 
ATOM   1941 O O   . LEU A 1 264 ? 13.298  20.724  5.868   1.00 72.32  ? 450 LEU B O   1 
ATOM   1942 C CB  . LEU A 1 264 ? 10.924  21.619  4.118   1.00 71.58  ? 450 LEU B CB  1 
ATOM   1943 C CG  . LEU A 1 264 ? 11.397  21.207  2.727   1.00 70.46  ? 450 LEU B CG  1 
ATOM   1944 C CD1 . LEU A 1 264 ? 10.576  20.031  2.214   1.00 69.75  ? 450 LEU B CD1 1 
ATOM   1945 C CD2 . LEU A 1 264 ? 11.320  22.392  1.785   1.00 71.20  ? 450 LEU B CD2 1 
ATOM   1946 N N   . HIS A 1 265 ? 12.692  18.826  4.808   1.00 70.70  ? 451 HIS B N   1 
ATOM   1947 C CA  . HIS A 1 265 ? 14.012  18.216  4.882   1.00 70.59  ? 451 HIS B CA  1 
ATOM   1948 C C   . HIS A 1 265 ? 14.653  18.026  3.517   1.00 70.16  ? 451 HIS B C   1 
ATOM   1949 O O   . HIS A 1 265 ? 15.772  18.493  3.292   1.00 72.92  ? 451 HIS B O   1 
ATOM   1950 C CB  . HIS A 1 265 ? 13.938  16.867  5.608   1.00 70.83  ? 451 HIS B CB  1 
ATOM   1951 C CG  . HIS A 1 265 ? 15.271  16.349  6.042   1.00 71.24  ? 451 HIS B CG  1 
ATOM   1952 N ND1 . HIS A 1 265 ? 15.633  15.025  5.918   1.00 71.07  ? 451 HIS B ND1 1 
ATOM   1953 C CD2 . HIS A 1 265 ? 16.336  16.983  6.586   1.00 72.00  ? 451 HIS B CD2 1 
ATOM   1954 C CE1 . HIS A 1 265 ? 16.862  14.865  6.376   1.00 73.31  ? 451 HIS B CE1 1 
ATOM   1955 N NE2 . HIS A 1 265 ? 17.312  16.038  6.786   1.00 74.96  ? 451 HIS B NE2 1 
ATOM   1956 N N   . ALA A 1 266 ? 13.967  17.365  2.588   1.00 68.92  ? 452 ALA B N   1 
ATOM   1957 C CA  . ALA A 1 266 ? 14.535  17.072  1.282   1.00 68.30  ? 452 ALA B CA  1 
ATOM   1958 C C   . ALA A 1 266 ? 13.585  17.520  0.185   1.00 67.98  ? 452 ALA B C   1 
ATOM   1959 O O   . ALA A 1 266 ? 12.367  17.358  0.296   1.00 68.00  ? 452 ALA B O   1 
ATOM   1960 C CB  . ALA A 1 266 ? 14.829  15.574  1.122   1.00 68.09  ? 452 ALA B CB  1 
ATOM   1961 N N   . VAL A 1 267 ? 14.155  18.053  -0.889  1.00 69.48  ? 453 VAL B N   1 
ATOM   1962 C CA  . VAL A 1 267 ? 13.403  18.471  -2.064  1.00 67.80  ? 453 VAL B CA  1 
ATOM   1963 C C   . VAL A 1 267 ? 14.065  17.795  -3.253  1.00 67.63  ? 453 VAL B C   1 
ATOM   1964 O O   . VAL A 1 267 ? 15.181  18.164  -3.641  1.00 67.78  ? 453 VAL B O   1 
ATOM   1965 C CB  . VAL A 1 267 ? 13.382  19.997  -2.237  1.00 68.29  ? 453 VAL B CB  1 
ATOM   1966 C CG1 . VAL A 1 267 ? 12.532  20.384  -3.439  1.00 68.48  ? 453 VAL B CG1 1 
ATOM   1967 C CG2 . VAL A 1 267 ? 12.860  20.667  -0.977  1.00 68.74  ? 453 VAL B CG2 1 
ATOM   1968 N N   . LEU A 1 268 ? 13.391  16.803  -3.824  1.00 67.50  ? 454 LEU B N   1 
ATOM   1969 C CA  . LEU A 1 268 ? 13.939  16.032  -4.931  1.00 67.60  ? 454 LEU B CA  1 
ATOM   1970 C C   . LEU A 1 268 ? 13.492  16.684  -6.233  1.00 68.03  ? 454 LEU B C   1 
ATOM   1971 O O   . LEU A 1 268 ? 12.292  16.867  -6.464  1.00 69.40  ? 454 LEU B O   1 
ATOM   1972 C CB  . LEU A 1 268 ? 13.488  14.573  -4.858  1.00 67.57  ? 454 LEU B CB  1 
ATOM   1973 C CG  . LEU A 1 268 ? 14.177  13.666  -3.833  1.00 67.47  ? 454 LEU B CG  1 
ATOM   1974 C CD1 . LEU A 1 268 ? 13.813  14.038  -2.407  1.00 67.35  ? 454 LEU B CD1 1 
ATOM   1975 C CD2 . LEU A 1 268 ? 13.812  12.220  -4.105  1.00 67.74  ? 454 LEU B CD2 1 
ATOM   1976 N N   . VAL A 1 269 ? 14.453  17.040  -7.076  1.00 68.39  ? 455 VAL B N   1 
ATOM   1977 C CA  . VAL A 1 269 ? 14.170  17.829  -8.263  1.00 69.07  ? 455 VAL B CA  1 
ATOM   1978 C C   . VAL A 1 269 ? 14.633  17.076  -9.502  1.00 69.69  ? 455 VAL B C   1 
ATOM   1979 O O   . VAL A 1 269 ? 15.556  16.255  -9.461  1.00 69.64  ? 455 VAL B O   1 
ATOM   1980 C CB  . VAL A 1 269 ? 14.840  19.221  -8.173  1.00 69.36  ? 455 VAL B CB  1 
ATOM   1981 C CG1 . VAL A 1 269 ? 14.390  20.129  -9.308  1.00 70.29  ? 455 VAL B CG1 1 
ATOM   1982 C CG2 . VAL A 1 269 ? 14.522  19.870  -6.837  1.00 70.21  ? 455 VAL B CG2 1 
ATOM   1983 N N   . HIS A 1 270 ? 13.971  17.383  -10.615 1.00 72.34  ? 456 HIS B N   1 
ATOM   1984 C CA  . HIS A 1 270 ? 14.235  16.851  -11.941 1.00 71.55  ? 456 HIS B CA  1 
ATOM   1985 C C   . HIS A 1 270 ? 14.347  18.059  -12.860 1.00 72.96  ? 456 HIS B C   1 
ATOM   1986 O O   . HIS A 1 270 ? 13.609  19.032  -12.681 1.00 75.95  ? 456 HIS B O   1 
ATOM   1987 C CB  . HIS A 1 270 ? 13.101  15.903  -12.360 1.00 71.93  ? 456 HIS B CB  1 
ATOM   1988 C CG  . HIS A 1 270 ? 13.068  15.568  -13.818 1.00 75.91  ? 456 HIS B CG  1 
ATOM   1989 N ND1 . HIS A 1 270 ? 13.622  14.412  -14.326 1.00 76.02  ? 456 HIS B ND1 1 
ATOM   1990 C CD2 . HIS A 1 270 ? 12.514  16.215  -14.872 1.00 74.71  ? 456 HIS B CD2 1 
ATOM   1991 C CE1 . HIS A 1 270 ? 13.420  14.367  -15.630 1.00 75.60  ? 456 HIS B CE1 1 
ATOM   1992 N NE2 . HIS A 1 270 ? 12.756  15.451  -15.988 1.00 77.54  ? 456 HIS B NE2 1 
ATOM   1993 N N   . SER A 1 271 ? 15.235  18.010  -13.850 1.00 73.57  ? 457 SER B N   1 
ATOM   1994 C CA  . SER A 1 271 ? 15.351  19.118  -14.790 1.00 75.78  ? 457 SER B CA  1 
ATOM   1995 C C   . SER A 1 271 ? 14.915  18.695  -16.182 1.00 98.93  ? 457 SER B C   1 
ATOM   1996 O O   . SER A 1 271 ? 15.288  17.628  -16.675 1.00 89.64  ? 457 SER B O   1 
ATOM   1997 C CB  . SER A 1 271 ? 16.770  19.677  -14.817 1.00 75.11  ? 457 SER B CB  1 
ATOM   1998 O OG  . SER A 1 271 ? 16.977  20.486  -13.675 1.00 81.50  ? 457 SER B OG  1 
ATOM   1999 N N   . GLY A 1 272 ? 14.133  19.577  -16.802 1.00 128.46 ? 458 GLY B N   1 
ATOM   2000 C CA  . GLY A 1 272 ? 13.196  19.241  -17.853 1.00 125.23 ? 458 GLY B CA  1 
ATOM   2001 C C   . GLY A 1 272 ? 13.303  19.706  -19.289 1.00 134.82 ? 458 GLY B C   1 
ATOM   2002 O O   . GLY A 1 272 ? 12.309  20.218  -19.812 1.00 146.48 ? 458 GLY B O   1 
ATOM   2003 N N   . ASP A 1 273 ? 14.454  19.593  -19.945 1.00 145.54 ? 459 ASP B N   1 
ATOM   2004 C CA  . ASP A 1 273 ? 14.447  19.823  -21.389 1.00 161.49 ? 459 ASP B CA  1 
ATOM   2005 C C   . ASP A 1 273 ? 13.595  18.747  -22.069 1.00 148.17 ? 459 ASP B C   1 
ATOM   2006 O O   . ASP A 1 273 ? 12.972  17.919  -21.396 1.00 144.59 ? 459 ASP B O   1 
ATOM   2007 C CB  . ASP A 1 273 ? 15.863  19.851  -21.977 1.00 159.86 ? 459 ASP B CB  1 
ATOM   2008 C CG  . ASP A 1 273 ? 16.634  18.597  -21.683 1.00 160.92 ? 459 ASP B CG  1 
ATOM   2009 O OD1 . ASP A 1 273 ? 16.037  17.729  -21.028 1.00 155.39 ? 459 ASP B OD1 1 
ATOM   2010 O OD2 . ASP A 1 273 ? 17.800  18.466  -22.144 1.00 146.81 ? 459 ASP B OD2 1 
ATOM   2011 N N   . ASN A 1 274 ? 13.564  18.733  -23.402 1.00 146.98 ? 460 ASN B N   1 
ATOM   2012 C CA  . ASN A 1 274 ? 12.546  17.947  -24.094 1.00 145.70 ? 460 ASN B CA  1 
ATOM   2013 C C   . ASN A 1 274 ? 12.653  16.462  -23.753 1.00 135.37 ? 460 ASN B C   1 
ATOM   2014 O O   . ASN A 1 274 ? 11.663  15.831  -23.365 1.00 122.92 ? 460 ASN B O   1 
ATOM   2015 C CB  . ASN A 1 274 ? 12.695  18.159  -25.598 1.00 139.29 ? 460 ASN B CB  1 
ATOM   2016 C CG  . ASN A 1 274 ? 12.798  19.631  -25.966 1.00 141.16 ? 460 ASN B CG  1 
ATOM   2017 O OD1 . ASN A 1 274 ? 12.348  20.508  -25.225 1.00 146.11 ? 460 ASN B OD1 1 
ATOM   2018 N ND2 . ASN A 1 274 ? 13.431  19.908  -27.103 1.00 133.69 ? 460 ASN B ND2 1 
ATOM   2019 N N   . HIS A 1 275 ? 13.846  15.885  -23.870 1.00 129.64 ? 461 HIS B N   1 
ATOM   2020 C CA  . HIS A 1 275 ? 13.964  14.513  -23.408 1.00 120.37 ? 461 HIS B CA  1 
ATOM   2021 C C   . HIS A 1 275 ? 14.677  14.482  -22.068 1.00 126.27 ? 461 HIS B C   1 
ATOM   2022 O O   . HIS A 1 275 ? 14.069  14.186  -21.041 1.00 123.28 ? 461 HIS B O   1 
ATOM   2023 C CB  . HIS A 1 275 ? 14.706  13.655  -24.422 1.00 114.85 ? 461 HIS B CB  1 
ATOM   2024 C CG  . HIS A 1 275 ? 13.794  12.988  -25.395 1.00 117.19 ? 461 HIS B CG  1 
ATOM   2025 N ND1 . HIS A 1 275 ? 13.045  11.878  -25.068 1.00 116.90 ? 461 HIS B ND1 1 
ATOM   2026 C CD2 . HIS A 1 275 ? 13.472  13.299  -26.673 1.00 120.06 ? 461 HIS B CD2 1 
ATOM   2027 C CE1 . HIS A 1 275 ? 12.319  11.518  -26.112 1.00 119.49 ? 461 HIS B CE1 1 
ATOM   2028 N NE2 . HIS A 1 275 ? 12.558  12.365  -27.098 1.00 121.46 ? 461 HIS B NE2 1 
ATOM   2029 N N   . GLY A 1 276 ? 15.963  14.802  -22.116 1.00 121.14 ? 462 GLY B N   1 
ATOM   2030 C CA  . GLY A 1 276 ? 16.831  15.046  -20.979 1.00 108.75 ? 462 GLY B CA  1 
ATOM   2031 C C   . GLY A 1 276 ? 16.559  14.264  -19.722 1.00 111.00 ? 462 GLY B C   1 
ATOM   2032 O O   . GLY A 1 276 ? 16.391  13.044  -19.754 1.00 131.17 ? 462 GLY B O   1 
ATOM   2033 N N   . GLY A 1 277 ? 16.415  14.997  -18.625 1.00 96.69  ? 463 GLY B N   1 
ATOM   2034 C CA  . GLY A 1 277 ? 16.176  14.411  -17.333 1.00 89.56  ? 463 GLY B CA  1 
ATOM   2035 C C   . GLY A 1 277 ? 17.425  14.277  -16.484 1.00 82.94  ? 463 GLY B C   1 
ATOM   2036 O O   . GLY A 1 277 ? 18.317  13.477  -16.782 1.00 84.27  ? 463 GLY B O   1 
ATOM   2037 N N   . HIS A 1 278 ? 17.474  15.049  -15.396 1.00 81.08  ? 464 HIS B N   1 
ATOM   2038 C CA  . HIS A 1 278 ? 18.593  15.077  -14.459 1.00 75.72  ? 464 HIS B CA  1 
ATOM   2039 C C   . HIS A 1 278 ? 18.043  15.199  -13.049 1.00 74.54  ? 464 HIS B C   1 
ATOM   2040 O O   . HIS A 1 278 ? 17.291  16.135  -12.764 1.00 80.99  ? 464 HIS B O   1 
ATOM   2041 C CB  . HIS A 1 278 ? 19.548  16.243  -14.748 1.00 78.14  ? 464 HIS B CB  1 
ATOM   2042 C CG  . HIS A 1 278 ? 20.841  16.161  -13.998 1.00 78.79  ? 464 HIS B CG  1 
ATOM   2043 N ND1 . HIS A 1 278 ? 21.672  17.245  -13.822 1.00 89.08  ? 464 HIS B ND1 1 
ATOM   2044 C CD2 . HIS A 1 278 ? 21.453  15.118  -13.389 1.00 76.19  ? 464 HIS B CD2 1 
ATOM   2045 C CE1 . HIS A 1 278 ? 22.735  16.879  -13.130 1.00 86.44  ? 464 HIS B CE1 1 
ATOM   2046 N NE2 . HIS A 1 278 ? 22.624  15.593  -12.852 1.00 79.02  ? 464 HIS B NE2 1 
ATOM   2047 N N   . TYR A 1 279 ? 18.429  14.280  -12.167 1.00 72.23  ? 465 TYR B N   1 
ATOM   2048 C CA  . TYR A 1 279 ? 17.830  14.157  -10.842 1.00 71.00  ? 465 TYR B CA  1 
ATOM   2049 C C   . TYR A 1 279 ? 18.834  14.626  -9.797  1.00 70.41  ? 465 TYR B C   1 
ATOM   2050 O O   . TYR A 1 279 ? 19.885  14.003  -9.614  1.00 70.66  ? 465 TYR B O   1 
ATOM   2051 C CB  . TYR A 1 279 ? 17.414  12.709  -10.582 1.00 70.98  ? 465 TYR B CB  1 
ATOM   2052 C CG  . TYR A 1 279 ? 16.542  12.122  -11.673 1.00 73.81  ? 465 TYR B CG  1 
ATOM   2053 C CD1 . TYR A 1 279 ? 17.107  11.611  -12.835 1.00 73.21  ? 465 TYR B CD1 1 
ATOM   2054 C CD2 . TYR A 1 279 ? 15.153  12.109  -11.559 1.00 77.13  ? 465 TYR B CD2 1 
ATOM   2055 C CE1 . TYR A 1 279 ? 16.325  11.083  -13.836 1.00 74.34  ? 465 TYR B CE1 1 
ATOM   2056 C CE2 . TYR A 1 279 ? 14.358  11.584  -12.564 1.00 72.73  ? 465 TYR B CE2 1 
ATOM   2057 C CZ  . TYR A 1 279 ? 14.951  11.071  -13.700 1.00 74.09  ? 465 TYR B CZ  1 
ATOM   2058 O OH  . TYR A 1 279 ? 14.170  10.547  -14.707 1.00 80.30  ? 465 TYR B OH  1 
ATOM   2059 N N   . VAL A 1 280 ? 18.508  15.731  -9.119  1.00 72.22  ? 466 VAL B N   1 
ATOM   2060 C CA  . VAL A 1 280 ? 19.280  16.254  -7.998  1.00 71.15  ? 466 VAL B CA  1 
ATOM   2061 C C   . VAL A 1 280 ? 18.352  16.407  -6.799  1.00 68.71  ? 466 VAL B C   1 
ATOM   2062 O O   . VAL A 1 280 ? 17.128  16.483  -6.936  1.00 68.53  ? 466 VAL B O   1 
ATOM   2063 C CB  . VAL A 1 280 ? 19.967  17.601  -8.320  1.00 69.95  ? 466 VAL B CB  1 
ATOM   2064 C CG1 . VAL A 1 280 ? 20.730  17.514  -9.625  1.00 70.93  ? 466 VAL B CG1 1 
ATOM   2065 C CG2 . VAL A 1 280 ? 18.952  18.739  -8.350  1.00 69.90  ? 466 VAL B CG2 1 
ATOM   2066 N N   . VAL A 1 281 ? 18.951  16.440  -5.607  1.00 70.29  ? 467 VAL B N   1 
ATOM   2067 C CA  . VAL A 1 281 ? 18.213  16.540  -4.352  1.00 68.07  ? 467 VAL B CA  1 
ATOM   2068 C C   . VAL A 1 281 ? 18.767  17.698  -3.531  1.00 68.29  ? 467 VAL B C   1 
ATOM   2069 O O   . VAL A 1 281 ? 19.986  17.855  -3.410  1.00 68.68  ? 467 VAL B O   1 
ATOM   2070 C CB  . VAL A 1 281 ? 18.268  15.226  -3.545  1.00 67.94  ? 467 VAL B CB  1 
ATOM   2071 C CG1 . VAL A 1 281 ? 19.694  14.739  -3.390  1.00 68.36  ? 467 VAL B CG1 1 
ATOM   2072 C CG2 . VAL A 1 281 ? 17.618  15.407  -2.182  1.00 67.79  ? 467 VAL B CG2 1 
ATOM   2073 N N   . TYR A 1 282 ? 17.870  18.520  -2.994  1.00 68.24  ? 468 TYR B N   1 
ATOM   2074 C CA  . TYR A 1 282 ? 18.224  19.603  -2.086  1.00 68.69  ? 468 TYR B CA  1 
ATOM   2075 C C   . TYR A 1 282 ? 17.947  19.158  -0.654  1.00 68.72  ? 468 TYR B C   1 
ATOM   2076 O O   . TYR A 1 282 ? 16.857  18.657  -0.355  1.00 68.42  ? 468 TYR B O   1 
ATOM   2077 C CB  . TYR A 1 282 ? 17.433  20.873  -2.407  1.00 68.98  ? 468 TYR B CB  1 
ATOM   2078 C CG  . TYR A 1 282 ? 17.866  21.600  -3.666  1.00 69.38  ? 468 TYR B CG  1 
ATOM   2079 C CD1 . TYR A 1 282 ? 17.460  21.171  -4.923  1.00 69.24  ? 468 TYR B CD1 1 
ATOM   2080 C CD2 . TYR A 1 282 ? 18.670  22.731  -3.590  1.00 73.33  ? 468 TYR B CD2 1 
ATOM   2081 C CE1 . TYR A 1 282 ? 17.854  21.843  -6.071  1.00 71.71  ? 468 TYR B CE1 1 
ATOM   2082 C CE2 . TYR A 1 282 ? 19.068  23.407  -4.729  1.00 75.43  ? 468 TYR B CE2 1 
ATOM   2083 C CZ  . TYR A 1 282 ? 18.658  22.963  -5.965  1.00 71.48  ? 468 TYR B CZ  1 
ATOM   2084 O OH  . TYR A 1 282 ? 19.059  23.649  -7.089  1.00 71.47  ? 468 TYR B OH  1 
ATOM   2085 N N   . LEU A 1 283 ? 18.930  19.348  0.227   1.00 69.60  ? 469 LEU B N   1 
ATOM   2086 C CA  . LEU A 1 283 ? 18.862  18.831  1.587   1.00 69.63  ? 469 LEU B CA  1 
ATOM   2087 C C   . LEU A 1 283 ? 19.412  19.846  2.578   1.00 70.65  ? 469 LEU B C   1 
ATOM   2088 O O   . LEU A 1 283 ? 20.404  20.526  2.300   1.00 76.08  ? 469 LEU B O   1 
ATOM   2089 C CB  . LEU A 1 283 ? 19.649  17.520  1.708   1.00 69.62  ? 469 LEU B CB  1 
ATOM   2090 C CG  . LEU A 1 283 ? 18.898  16.207  1.503   1.00 69.09  ? 469 LEU B CG  1 
ATOM   2091 C CD1 . LEU A 1 283 ? 19.868  15.099  1.162   1.00 69.22  ? 469 LEU B CD1 1 
ATOM   2092 C CD2 . LEU A 1 283 ? 18.123  15.857  2.758   1.00 69.45  ? 469 LEU B CD2 1 
ATOM   2093 N N   . ASN A 1 284 ? 18.759  19.938  3.739   1.00 71.19  ? 470 ASN B N   1 
ATOM   2094 C CA  . ASN A 1 284 ? 19.364  20.511  4.939   1.00 74.18  ? 470 ASN B CA  1 
ATOM   2095 C C   . ASN A 1 284 ? 19.545  19.358  5.918   1.00 72.92  ? 470 ASN B C   1 
ATOM   2096 O O   . ASN A 1 284 ? 18.651  19.063  6.726   1.00 73.27  ? 470 ASN B O   1 
ATOM   2097 C CB  . ASN A 1 284 ? 18.521  21.641  5.544   1.00 73.39  ? 470 ASN B CB  1 
ATOM   2098 C CG  . ASN A 1 284 ? 17.096  21.227  5.856   1.00 77.37  ? 470 ASN B CG  1 
ATOM   2099 O OD1 . ASN A 1 284 ? 16.492  20.427  5.141   1.00 74.43  ? 470 ASN B OD1 1 
ATOM   2100 N ND2 . ASN A 1 284 ? 16.551  21.771  6.936   1.00 80.39  ? 470 ASN B ND2 1 
ATOM   2101 N N   . PRO A 1 285 ? 20.688  18.674  5.879   1.00 73.10  ? 471 PRO B N   1 
ATOM   2102 C CA  . PRO A 1 285 ? 20.819  17.399  6.601   1.00 73.49  ? 471 PRO B CA  1 
ATOM   2103 C C   . PRO A 1 285 ? 20.589  17.512  8.090   1.00 84.38  ? 471 PRO B C   1 
ATOM   2104 O O   . PRO A 1 285 ? 20.047  16.578  8.695   1.00 89.08  ? 471 PRO B O   1 
ATOM   2105 C CB  . PRO A 1 285 ? 22.261  16.979  6.292   1.00 73.80  ? 471 PRO B CB  1 
ATOM   2106 C CG  . PRO A 1 285 ? 22.594  17.685  5.017   1.00 73.01  ? 471 PRO B CG  1 
ATOM   2107 C CD  . PRO A 1 285 ? 21.898  19.004  5.111   1.00 73.09  ? 471 PRO B CD  1 
ATOM   2108 N N   . LYS A 1 286 ? 20.972  18.630  8.698   1.00 83.53  ? 472 LYS B N   1 
ATOM   2109 C CA  . LYS A 1 286 ? 20.789  18.829  10.126  1.00 81.60  ? 472 LYS B CA  1 
ATOM   2110 C C   . LYS A 1 286 ? 19.439  19.448  10.467  1.00 77.94  ? 472 LYS B C   1 
ATOM   2111 O O   . LYS A 1 286 ? 19.175  19.715  11.643  1.00 80.48  ? 472 LYS B O   1 
ATOM   2112 C CB  . LYS A 1 286 ? 21.918  19.709  10.678  1.00 79.40  ? 472 LYS B CB  1 
ATOM   2113 C CG  . LYS A 1 286 ? 23.306  19.090  10.567  1.00 79.77  ? 472 LYS B CG  1 
ATOM   2114 C CD  . LYS A 1 286 ? 23.373  17.744  11.280  1.00 80.39  ? 472 LYS B CD  1 
ATOM   2115 C CE  . LYS A 1 286 ? 24.781  17.160  11.243  1.00 84.38  ? 472 LYS B CE  1 
ATOM   2116 N NZ  . LYS A 1 286 ? 25.183  16.685  9.886   1.00 80.21  ? 472 LYS B NZ  1 
ATOM   2117 N N   . GLY A 1 287 ? 18.572  19.670  9.481   1.00 78.88  ? 473 GLY B N   1 
ATOM   2118 C CA  . GLY A 1 287 ? 17.298  20.301  9.755   1.00 79.02  ? 473 GLY B CA  1 
ATOM   2119 C C   . GLY A 1 287 ? 17.408  21.732  10.221  1.00 78.07  ? 473 GLY B C   1 
ATOM   2120 O O   . GLY A 1 287 ? 16.424  22.289  10.716  1.00 78.84  ? 473 GLY B O   1 
ATOM   2121 N N   . ASP A 1 288 ? 18.581  22.341  10.076  1.00 78.57  ? 474 ASP B N   1 
ATOM   2122 C CA  . ASP A 1 288 ? 18.856  23.683  10.565  1.00 80.20  ? 474 ASP B CA  1 
ATOM   2123 C C   . ASP A 1 288 ? 18.568  24.769  9.539   1.00 79.59  ? 474 ASP B C   1 
ATOM   2124 O O   . ASP A 1 288 ? 18.833  25.942  9.813   1.00 82.17  ? 474 ASP B O   1 
ATOM   2125 C CB  . ASP A 1 288 ? 20.318  23.785  11.024  1.00 81.44  ? 474 ASP B CB  1 
ATOM   2126 C CG  . ASP A 1 288 ? 21.303  23.294  9.971   1.00 81.30  ? 474 ASP B CG  1 
ATOM   2127 O OD1 . ASP A 1 288 ? 20.861  22.895  8.872   1.00 79.84  ? 474 ASP B OD1 1 
ATOM   2128 O OD2 . ASP A 1 288 ? 22.525  23.299  10.245  1.00 81.19  ? 474 ASP B OD2 1 
ATOM   2129 N N   . GLY A 1 289 ? 18.046  24.416  8.367   1.00 77.76  ? 475 GLY B N   1 
ATOM   2130 C CA  . GLY A 1 289 ? 17.888  25.399  7.316   1.00 77.39  ? 475 GLY B CA  1 
ATOM   2131 C C   . GLY A 1 289 ? 19.158  25.743  6.573   1.00 78.25  ? 475 GLY B C   1 
ATOM   2132 O O   . GLY A 1 289 ? 19.152  26.677  5.763   1.00 77.31  ? 475 GLY B O   1 
ATOM   2133 N N   . LYS A 1 290 ? 20.251  25.031  6.839   1.00 89.42  ? 476 LYS B N   1 
ATOM   2134 C CA  . LYS A 1 290 ? 21.495  25.181  6.088   1.00 84.33  ? 476 LYS B CA  1 
ATOM   2135 C C   . LYS A 1 290 ? 21.460  24.153  4.964   1.00 85.32  ? 476 LYS B C   1 
ATOM   2136 O O   . LYS A 1 290 ? 21.734  22.970  5.179   1.00 85.34  ? 476 LYS B O   1 
ATOM   2137 C CB  . LYS A 1 290 ? 22.703  24.987  6.999   1.00 85.65  ? 476 LYS B CB  1 
ATOM   2138 N N   . TRP A 1 291 ? 21.132  24.607  3.759   1.00 77.12  ? 477 TRP B N   1 
ATOM   2139 C CA  . TRP A 1 291 ? 20.790  23.719  2.659   1.00 79.84  ? 477 TRP B CA  1 
ATOM   2140 C C   . TRP A 1 291 ? 21.983  23.477  1.742   1.00 73.70  ? 477 TRP B C   1 
ATOM   2141 O O   . TRP A 1 291 ? 22.827  24.354  1.539   1.00 73.92  ? 477 TRP B O   1 
ATOM   2142 C CB  . TRP A 1 291 ? 19.630  24.285  1.835   1.00 76.52  ? 477 TRP B CB  1 
ATOM   2143 C CG  . TRP A 1 291 ? 18.316  24.255  2.540   1.00 75.29  ? 477 TRP B CG  1 
ATOM   2144 C CD1 . TRP A 1 291 ? 17.877  25.120  3.498   1.00 78.85  ? 477 TRP B CD1 1 
ATOM   2145 C CD2 . TRP A 1 291 ? 17.269  23.297  2.352   1.00 71.97  ? 477 TRP B CD2 1 
ATOM   2146 N NE1 . TRP A 1 291 ? 16.613  24.768  3.910   1.00 81.04  ? 477 TRP B NE1 1 
ATOM   2147 C CE2 . TRP A 1 291 ? 16.219  23.650  3.223   1.00 74.54  ? 477 TRP B CE2 1 
ATOM   2148 C CE3 . TRP A 1 291 ? 17.115  22.178  1.529   1.00 70.61  ? 477 TRP B CE3 1 
ATOM   2149 C CZ2 . TRP A 1 291 ? 15.035  22.923  3.294   1.00 74.72  ? 477 TRP B CZ2 1 
ATOM   2150 C CZ3 . TRP A 1 291 ? 15.939  21.458  1.600   1.00 70.07  ? 477 TRP B CZ3 1 
ATOM   2151 C CH2 . TRP A 1 291 ? 14.914  21.833  2.475   1.00 72.22  ? 477 TRP B CH2 1 
ATOM   2152 N N   . CYS A 1 292 ? 22.046  22.261  1.199   1.00 72.47  ? 478 CYS B N   1 
ATOM   2153 C CA  . CYS A 1 292 ? 23.034  21.881  0.200   1.00 76.05  ? 478 CYS B CA  1 
ATOM   2154 C C   . CYS A 1 292 ? 22.342  21.269  -1.012  1.00 74.94  ? 478 CYS B C   1 
ATOM   2155 O O   . CYS A 1 292 ? 21.249  20.704  -0.904  1.00 70.28  ? 478 CYS B O   1 
ATOM   2156 C CB  . CYS A 1 292 ? 24.062  20.883  0.754   1.00 72.25  ? 478 CYS B CB  1 
ATOM   2157 S SG  . CYS A 1 292 ? 25.173  21.556  2.005   1.00 77.61  ? 478 CYS B SG  1 
ATOM   2158 N N   . LYS A 1 293 ? 22.987  21.399  -2.174  1.00 73.14  ? 479 LYS B N   1 
ATOM   2159 C CA  . LYS A 1 293 ? 22.543  20.750  -3.402  1.00 70.56  ? 479 LYS B CA  1 
ATOM   2160 C C   . LYS A 1 293 ? 23.449  19.559  -3.684  1.00 70.58  ? 479 LYS B C   1 
ATOM   2161 O O   . LYS A 1 293 ? 24.668  19.713  -3.792  1.00 71.30  ? 479 LYS B O   1 
ATOM   2162 C CB  . LYS A 1 293 ? 22.551  21.709  -4.592  1.00 71.05  ? 479 LYS B CB  1 
ATOM   2163 C CG  . LYS A 1 293 ? 22.344  20.992  -5.929  1.00 70.88  ? 479 LYS B CG  1 
ATOM   2164 C CD  . LYS A 1 293 ? 21.724  21.886  -6.995  1.00 71.33  ? 479 LYS B CD  1 
ATOM   2165 C CE  . LYS A 1 293 ? 22.705  22.865  -7.608  1.00 72.47  ? 479 LYS B CE  1 
ATOM   2166 N NZ  . LYS A 1 293 ? 22.057  23.627  -8.719  1.00 73.13  ? 479 LYS B NZ  1 
ATOM   2167 N N   . PHE A 1 294 ? 22.852  18.382  -3.812  1.00 69.98  ? 480 PHE B N   1 
ATOM   2168 C CA  . PHE A 1 294 ? 23.583  17.146  -4.071  1.00 70.16  ? 480 PHE B CA  1 
ATOM   2169 C C   . PHE A 1 294 ? 23.366  16.778  -5.536  1.00 70.23  ? 480 PHE B C   1 
ATOM   2170 O O   . PHE A 1 294 ? 22.392  16.109  -5.886  1.00 69.80  ? 480 PHE B O   1 
ATOM   2171 C CB  . PHE A 1 294 ? 23.128  16.028  -3.142  1.00 69.79  ? 480 PHE B CB  1 
ATOM   2172 C CG  . PHE A 1 294 ? 23.452  16.267  -1.700  1.00 70.08  ? 480 PHE B CG  1 
ATOM   2173 C CD1 . PHE A 1 294 ? 22.702  17.148  -0.938  1.00 69.93  ? 480 PHE B CD1 1 
ATOM   2174 C CD2 . PHE A 1 294 ? 24.514  15.612  -1.104  1.00 70.76  ? 480 PHE B CD2 1 
ATOM   2175 C CE1 . PHE A 1 294 ? 23.003  17.367  0.396   1.00 70.50  ? 480 PHE B CE1 1 
ATOM   2176 C CE2 . PHE A 1 294 ? 24.820  15.823  0.226   1.00 71.31  ? 480 PHE B CE2 1 
ATOM   2177 C CZ  . PHE A 1 294 ? 24.066  16.703  0.977   1.00 71.21  ? 480 PHE B CZ  1 
ATOM   2178 N N   . ASP A 1 295 ? 24.277  17.241  -6.395  1.00 73.73  ? 481 ASP B N   1 
ATOM   2179 C CA  . ASP A 1 295 ? 24.254  16.925  -7.824  1.00 71.47  ? 481 ASP B CA  1 
ATOM   2180 C C   . ASP A 1 295 ? 25.251  15.799  -8.085  1.00 72.12  ? 481 ASP B C   1 
ATOM   2181 O O   . ASP A 1 295 ? 26.365  16.015  -8.565  1.00 73.05  ? 481 ASP B O   1 
ATOM   2182 C CB  . ASP A 1 295 ? 24.572  18.160  -8.659  1.00 72.44  ? 481 ASP B CB  1 
ATOM   2183 C CG  . ASP A 1 295 ? 24.320  17.937  -10.133 1.00 76.26  ? 481 ASP B CG  1 
ATOM   2184 O OD1 . ASP A 1 295 ? 23.870  16.827  -10.479 1.00 75.38  ? 481 ASP B OD1 1 
ATOM   2185 O OD2 . ASP A 1 295 ? 24.579  18.855  -10.942 1.00 80.08  ? 481 ASP B OD2 1 
ATOM   2186 N N   . ASP A 1 296 ? 24.829  14.575  -7.762  1.00 71.78  ? 482 ASP B N   1 
ATOM   2187 C CA  . ASP A 1 296 ? 25.680  13.395  -7.857  1.00 72.52  ? 482 ASP B CA  1 
ATOM   2188 C C   . ASP A 1 296 ? 26.959  13.569  -7.053  1.00 82.61  ? 482 ASP B C   1 
ATOM   2189 O O   . ASP A 1 296 ? 26.926  13.667  -5.822  1.00 83.03  ? 482 ASP B O   1 
ATOM   2190 C CB  . ASP A 1 296 ? 26.045  13.083  -9.310  1.00 73.58  ? 482 ASP B CB  1 
ATOM   2191 C CG  . ASP A 1 296 ? 24.869  12.615  -10.115 1.00 78.16  ? 482 ASP B CG  1 
ATOM   2192 O OD1 . ASP A 1 296 ? 24.001  11.912  -9.557  1.00 73.83  ? 482 ASP B OD1 1 
ATOM   2193 O OD2 . ASP A 1 296 ? 24.823  12.950  -11.314 1.00 87.37  ? 482 ASP B OD2 1 
ATOM   2194 N N   . ASP A 1 297 ? 28.092  13.608  -7.755  1.00 80.95  ? 483 ASP B N   1 
ATOM   2195 C CA  . ASP A 1 297 ? 29.392  13.770  -7.121  1.00 75.78  ? 483 ASP B CA  1 
ATOM   2196 C C   . ASP A 1 297 ? 29.642  15.191  -6.636  1.00 75.66  ? 483 ASP B C   1 
ATOM   2197 O O   . ASP A 1 297 ? 30.584  15.405  -5.867  1.00 83.41  ? 483 ASP B O   1 
ATOM   2198 C CB  . ASP A 1 297 ? 30.494  13.355  -8.096  1.00 77.21  ? 483 ASP B CB  1 
ATOM   2199 C CG  . ASP A 1 297 ? 30.585  14.280  -9.299  1.00 82.77  ? 483 ASP B CG  1 
ATOM   2200 O OD1 . ASP A 1 297 ? 29.527  14.739  -9.778  1.00 86.87  ? 483 ASP B OD1 1 
ATOM   2201 O OD2 . ASP A 1 297 ? 31.712  14.551  -9.765  1.00 85.01  ? 483 ASP B OD2 1 
ATOM   2202 N N   . VAL A 1 298 ? 28.834  16.157  -7.060  1.00 74.20  ? 484 VAL B N   1 
ATOM   2203 C CA  . VAL A 1 298 ? 29.010  17.554  -6.686  1.00 74.31  ? 484 VAL B CA  1 
ATOM   2204 C C   . VAL A 1 298 ? 28.044  17.866  -5.549  1.00 73.32  ? 484 VAL B C   1 
ATOM   2205 O O   . VAL A 1 298 ? 26.822  17.856  -5.737  1.00 72.47  ? 484 VAL B O   1 
ATOM   2206 C CB  . VAL A 1 298 ? 28.788  18.497  -7.876  1.00 74.71  ? 484 VAL B CB  1 
ATOM   2207 C CG1 . VAL A 1 298 ? 29.054  19.940  -7.466  1.00 75.10  ? 484 VAL B CG1 1 
ATOM   2208 C CG2 . VAL A 1 298 ? 29.669  18.095  -9.049  1.00 75.90  ? 484 VAL B CG2 1 
ATOM   2209 N N   . VAL A 1 299 ? 28.594  18.155  -4.374  1.00 73.63  ? 485 VAL B N   1 
ATOM   2210 C CA  . VAL A 1 299 ? 27.831  18.594  -3.213  1.00 73.10  ? 485 VAL B CA  1 
ATOM   2211 C C   . VAL A 1 299 ? 28.268  20.017  -2.907  1.00 73.84  ? 485 VAL B C   1 
ATOM   2212 O O   . VAL A 1 299 ? 29.451  20.264  -2.637  1.00 77.12  ? 485 VAL B O   1 
ATOM   2213 C CB  . VAL A 1 299 ? 28.053  17.684  -1.996  1.00 73.21  ? 485 VAL B CB  1 
ATOM   2214 C CG1 . VAL A 1 299 ? 27.169  18.131  -0.840  1.00 72.86  ? 485 VAL B CG1 1 
ATOM   2215 C CG2 . VAL A 1 299 ? 27.785  16.227  -2.359  1.00 72.81  ? 485 VAL B CG2 1 
ATOM   2216 N N   . SER A 1 300 ? 27.324  20.951  -2.953  1.00 73.48  ? 486 SER B N   1 
ATOM   2217 C CA  . SER A 1 300 ? 27.645  22.362  -2.819  1.00 74.37  ? 486 SER B CA  1 
ATOM   2218 C C   . SER A 1 300 ? 26.630  23.037  -1.912  1.00 74.14  ? 486 SER B C   1 
ATOM   2219 O O   . SER A 1 300 ? 25.527  22.534  -1.690  1.00 73.18  ? 486 SER B O   1 
ATOM   2220 C CB  . SER A 1 300 ? 27.669  23.063  -4.186  1.00 74.73  ? 486 SER B CB  1 
ATOM   2221 O OG  . SER A 1 300 ? 26.448  22.869  -4.882  1.00 73.83  ? 486 SER B OG  1 
ATOM   2222 N N   . ARG A 1 301 ? 27.029  24.183  -1.375  1.00 76.50  ? 487 ARG B N   1 
ATOM   2223 C CA  . ARG A 1 301 ? 26.121  25.001  -0.590  1.00 75.40  ? 487 ARG B CA  1 
ATOM   2224 C C   . ARG A 1 301 ? 25.196  25.791  -1.508  1.00 75.18  ? 487 ARG B C   1 
ATOM   2225 O O   . ARG A 1 301 ? 25.561  26.160  -2.628  1.00 75.50  ? 487 ARG B O   1 
ATOM   2226 C CB  . ARG A 1 301 ? 26.906  25.948  0.315   1.00 80.64  ? 487 ARG B CB  1 
ATOM   2227 C CG  . ARG A 1 301 ? 27.438  25.285  1.566   1.00 84.47  ? 487 ARG B CG  1 
ATOM   2228 C CD  . ARG A 1 301 ? 26.384  25.286  2.639   1.00 88.43  ? 487 ARG B CD  1 
ATOM   2229 N NE  . ARG A 1 301 ? 25.958  26.641  2.958   1.00 91.60  ? 487 ARG B NE  1 
ATOM   2230 C CZ  . ARG A 1 301 ? 24.973  26.934  3.793   1.00 83.74  ? 487 ARG B CZ  1 
ATOM   2231 N NH1 . ARG A 1 301 ? 24.283  25.985  4.403   1.00 84.54  ? 487 ARG B NH1 1 
ATOM   2232 N NH2 . ARG A 1 301 ? 24.676  28.208  4.024   1.00 84.55  ? 487 ARG B NH2 1 
ATOM   2233 N N   . CYS A 1 302 ? 23.984  26.049  -1.021  1.00 82.94  ? 488 CYS B N   1 
ATOM   2234 C CA  . CYS A 1 302 ? 23.003  26.792  -1.797  1.00 78.68  ? 488 CYS B CA  1 
ATOM   2235 C C   . CYS A 1 302 ? 22.107  27.580  -0.855  1.00 75.31  ? 488 CYS B C   1 
ATOM   2236 O O   . CYS A 1 302 ? 21.984  27.264  0.332   1.00 75.36  ? 488 CYS B O   1 
ATOM   2237 C CB  . CYS A 1 302 ? 22.162  25.862  -2.679  1.00 73.50  ? 488 CYS B CB  1 
ATOM   2238 S SG  . CYS A 1 302 ? 21.257  24.603  -1.758  1.00 76.19  ? 488 CYS B SG  1 
ATOM   2239 N N   . THR A 1 303 ? 21.481  28.616  -1.404  1.00 75.93  ? 489 THR B N   1 
ATOM   2240 C CA  . THR A 1 303 ? 20.580  29.444  -0.619  1.00 76.68  ? 489 THR B CA  1 
ATOM   2241 C C   . THR A 1 303 ? 19.277  28.706  -0.344  1.00 75.58  ? 489 THR B C   1 
ATOM   2242 O O   . THR A 1 303 ? 18.858  27.828  -1.104  1.00 74.38  ? 489 THR B O   1 
ATOM   2243 C CB  . THR A 1 303 ? 20.288  30.752  -1.350  1.00 77.87  ? 489 THR B CB  1 
ATOM   2244 O OG1 . THR A 1 303 ? 19.537  30.484  -2.541  1.00 82.05  ? 489 THR B OG1 1 
ATOM   2245 C CG2 . THR A 1 303 ? 21.584  31.436  -1.737  1.00 81.10  ? 489 THR B CG2 1 
ATOM   2246 N N   . LYS A 1 304 ? 18.625  29.076  0.760   1.00 76.22  ? 490 LYS B N   1 
ATOM   2247 C CA  . LYS A 1 304 ? 17.317  28.498  1.050   1.00 77.04  ? 490 LYS B CA  1 
ATOM   2248 C C   . LYS A 1 304 ? 16.289  28.918  0.010   1.00 75.34  ? 490 LYS B C   1 
ATOM   2249 O O   . LYS A 1 304 ? 15.327  28.184  -0.241  1.00 74.41  ? 490 LYS B O   1 
ATOM   2250 C CB  . LYS A 1 304 ? 16.864  28.890  2.454   1.00 76.52  ? 490 LYS B CB  1 
ATOM   2251 C CG  . LYS A 1 304 ? 15.740  28.030  2.999   1.00 75.91  ? 490 LYS B CG  1 
ATOM   2252 C CD  . LYS A 1 304 ? 15.795  27.968  4.517   1.00 80.96  ? 490 LYS B CD  1 
ATOM   2253 C CE  . LYS A 1 304 ? 15.622  29.342  5.144   1.00 84.94  ? 490 LYS B CE  1 
ATOM   2254 N NZ  . LYS A 1 304 ? 14.289  29.923  4.815   1.00 99.53  ? 490 LYS B NZ  1 
ATOM   2255 N N   . GLU A 1 305 ? 16.478  30.086  -0.606  1.00 76.47  ? 491 GLU B N   1 
ATOM   2256 C CA  . GLU A 1 305 ? 15.641  30.468  -1.736  1.00 76.57  ? 491 GLU B CA  1 
ATOM   2257 C C   . GLU A 1 305 ? 15.842  29.520  -2.911  1.00 75.36  ? 491 GLU B C   1 
ATOM   2258 O O   . GLU A 1 305 ? 14.890  29.200  -3.630  1.00 74.96  ? 491 GLU B O   1 
ATOM   2259 C CB  . GLU A 1 305 ? 15.936  31.910  -2.155  1.00 78.29  ? 491 GLU B CB  1 
ATOM   2260 C CG  . GLU A 1 305 ? 15.418  32.972  -1.196  1.00 83.51  ? 491 GLU B CG  1 
ATOM   2261 C CD  . GLU A 1 305 ? 16.303  33.146  0.022   1.00 82.78  ? 491 GLU B CD  1 
ATOM   2262 O OE1 . GLU A 1 305 ? 17.294  32.399  0.149   1.00 86.30  ? 491 GLU B OE1 1 
ATOM   2263 O OE2 . GLU A 1 305 ? 16.013  34.037  0.849   1.00 88.62  ? 491 GLU B OE2 1 
ATOM   2264 N N   . GLU A 1 306 ? 17.083  29.081  -3.142  1.00 77.03  ? 492 GLU B N   1 
ATOM   2265 C CA  . GLU A 1 306 ? 17.339  28.170  -4.252  1.00 75.04  ? 492 GLU B CA  1 
ATOM   2266 C C   . GLU A 1 306 ? 16.718  26.796  -4.018  1.00 72.75  ? 492 GLU B C   1 
ATOM   2267 O O   . GLU A 1 306 ? 16.330  26.120  -4.978  1.00 72.24  ? 492 GLU B O   1 
ATOM   2268 C CB  . GLU A 1 306 ? 18.845  28.047  -4.484  1.00 74.32  ? 492 GLU B CB  1 
ATOM   2269 C CG  . GLU A 1 306 ? 19.239  27.218  -5.693  1.00 74.08  ? 492 GLU B CG  1 
ATOM   2270 C CD  . GLU A 1 306 ? 20.737  27.216  -5.919  1.00 87.50  ? 492 GLU B CD  1 
ATOM   2271 O OE1 . GLU A 1 306 ? 21.442  27.980  -5.220  1.00 77.41  ? 492 GLU B OE1 1 
ATOM   2272 O OE2 . GLU A 1 306 ? 21.209  26.459  -6.797  1.00 92.90  ? 492 GLU B OE2 1 
ATOM   2273 N N   . ALA A 1 307 ? 16.579  26.382  -2.761  1.00 72.38  ? 493 ALA B N   1 
ATOM   2274 C CA  . ALA A 1 307 ? 16.044  25.061  -2.462  1.00 71.27  ? 493 ALA B CA  1 
ATOM   2275 C C   . ALA A 1 307 ? 14.525  25.031  -2.393  1.00 73.50  ? 493 ALA B C   1 
ATOM   2276 O O   . ALA A 1 307 ? 13.918  24.005  -2.726  1.00 71.53  ? 493 ALA B O   1 
ATOM   2277 C CB  . ALA A 1 307 ? 16.625  24.545  -1.144  1.00 71.15  ? 493 ALA B CB  1 
ATOM   2278 N N   . ILE A 1 308 ? 13.891  26.124  -1.977  1.00 73.81  ? 494 ILE B N   1 
ATOM   2279 C CA  . ILE A 1 308 ? 12.457  26.101  -1.712  1.00 72.17  ? 494 ILE B CA  1 
ATOM   2280 C C   . ILE A 1 308 ? 11.707  26.941  -2.739  1.00 72.91  ? 494 ILE B C   1 
ATOM   2281 O O   . ILE A 1 308 ? 10.953  26.400  -3.554  1.00 75.38  ? 494 ILE B O   1 
ATOM   2282 C CB  . ILE A 1 308 ? 12.166  26.579  -0.276  1.00 72.92  ? 494 ILE B CB  1 
ATOM   2283 C CG1 . ILE A 1 308 ? 12.913  25.690  0.724   1.00 72.43  ? 494 ILE B CG1 1 
ATOM   2284 C CG2 . ILE A 1 308 ? 10.674  26.547  0.006   1.00 73.19  ? 494 ILE B CG2 1 
ATOM   2285 C CD1 . ILE A 1 308 ? 12.662  26.035  2.180   1.00 81.72  ? 494 ILE B CD1 1 
ATOM   2286 N N   . GLU A 1 309 ? 11.939  28.257  -2.747  1.00 74.15  ? 495 GLU B N   1 
ATOM   2287 C CA  . GLU A 1 309 ? 11.145  29.135  -3.604  1.00 75.18  ? 495 GLU B CA  1 
ATOM   2288 C C   . GLU A 1 309 ? 11.453  28.911  -5.079  1.00 75.04  ? 495 GLU B C   1 
ATOM   2289 O O   . GLU A 1 309 ? 10.558  28.997  -5.928  1.00 75.50  ? 495 GLU B O   1 
ATOM   2290 C CB  . GLU A 1 309 ? 11.373  30.602  -3.233  1.00 76.81  ? 495 GLU B CB  1 
ATOM   2291 C CG  . GLU A 1 309 ? 10.425  31.149  -2.168  1.00 82.81  ? 495 GLU B CG  1 
ATOM   2292 C CD  . GLU A 1 309 ? 10.849  30.834  -0.745  1.00 87.72  ? 495 GLU B CD  1 
ATOM   2293 O OE1 . GLU A 1 309 ? 12.051  30.574  -0.509  1.00 77.07  ? 495 GLU B OE1 1 
ATOM   2294 O OE2 . GLU A 1 309 ? 9.965   30.852  0.142   1.00 93.79  ? 495 GLU B OE2 1 
ATOM   2295 N N   . HIS A 1 310 ? 12.709  28.624  -5.406  1.00 74.64  ? 496 HIS B N   1 
ATOM   2296 C CA  . HIS A 1 310 ? 13.117  28.468  -6.795  1.00 74.81  ? 496 HIS B CA  1 
ATOM   2297 C C   . HIS A 1 310 ? 12.656  27.152  -7.415  1.00 73.83  ? 496 HIS B C   1 
ATOM   2298 O O   . HIS A 1 310 ? 12.745  27.001  -8.639  1.00 74.26  ? 496 HIS B O   1 
ATOM   2299 C CB  . HIS A 1 310 ? 14.643  28.603  -6.904  1.00 76.47  ? 496 HIS B CB  1 
ATOM   2300 C CG  . HIS A 1 310 ? 15.143  30.006  -6.714  1.00 77.24  ? 496 HIS B CG  1 
ATOM   2301 N ND1 . HIS A 1 310 ? 16.483  30.330  -6.745  1.00 79.33  ? 496 HIS B ND1 1 
ATOM   2302 C CD2 . HIS A 1 310 ? 14.481  31.170  -6.507  1.00 82.70  ? 496 HIS B CD2 1 
ATOM   2303 C CE1 . HIS A 1 310 ? 16.625  31.631  -6.555  1.00 79.92  ? 496 HIS B CE1 1 
ATOM   2304 N NE2 . HIS A 1 310 ? 15.426  32.164  -6.409  1.00 78.85  ? 496 HIS B NE2 1 
ATOM   2305 N N   . ASN A 1 311 ? 12.147  26.209  -6.623  1.00 72.78  ? 497 ASN B N   1 
ATOM   2306 C CA  . ASN A 1 311 ? 11.653  24.943  -7.148  1.00 72.04  ? 497 ASN B CA  1 
ATOM   2307 C C   . ASN A 1 311 ? 10.136  24.900  -7.255  1.00 72.35  ? 497 ASN B C   1 
ATOM   2308 O O   . ASN A 1 311 ? 9.570   23.827  -7.486  1.00 73.47  ? 497 ASN B O   1 
ATOM   2309 C CB  . ASN A 1 311 ? 12.148  23.781  -6.291  1.00 70.86  ? 497 ASN B CB  1 
ATOM   2310 C CG  . ASN A 1 311 ? 13.612  23.481  -6.524  1.00 70.62  ? 497 ASN B CG  1 
ATOM   2311 O OD1 . ASN A 1 311 ? 13.991  22.989  -7.586  1.00 70.72  ? 497 ASN B OD1 1 
ATOM   2312 N ND2 . ASN A 1 311 ? 14.444  23.773  -5.531  1.00 76.80  ? 497 ASN B ND2 1 
ATOM   2313 N N   . TYR A 1 312 ? 9.470   26.044  -7.101  1.00 73.36  ? 498 TYR B N   1 
ATOM   2314 C CA  . TYR A 1 312 ? 8.016   26.070  -7.181  1.00 73.87  ? 498 TYR B CA  1 
ATOM   2315 C C   . TYR A 1 312 ? 7.512   25.830  -8.601  1.00 74.55  ? 498 TYR B C   1 
ATOM   2316 O O   . TYR A 1 312 ? 6.394   25.337  -8.779  1.00 77.56  ? 498 TYR B O   1 
ATOM   2317 C CB  . TYR A 1 312 ? 7.504   27.402  -6.637  1.00 75.04  ? 498 TYR B CB  1 
ATOM   2318 C CG  . TYR A 1 312 ? 7.587   27.514  -5.127  1.00 74.69  ? 498 TYR B CG  1 
ATOM   2319 C CD1 . TYR A 1 312 ? 7.857   26.401  -4.338  1.00 73.44  ? 498 TYR B CD1 1 
ATOM   2320 C CD2 . TYR A 1 312 ? 7.392   28.732  -4.491  1.00 75.89  ? 498 TYR B CD2 1 
ATOM   2321 C CE1 . TYR A 1 312 ? 7.926   26.499  -2.956  1.00 73.41  ? 498 TYR B CE1 1 
ATOM   2322 C CE2 . TYR A 1 312 ? 7.461   28.840  -3.115  1.00 75.88  ? 498 TYR B CE2 1 
ATOM   2323 C CZ  . TYR A 1 312 ? 7.729   27.723  -2.351  1.00 74.65  ? 498 TYR B CZ  1 
ATOM   2324 O OH  . TYR A 1 312 ? 7.796   27.839  -0.979  1.00 74.92  ? 498 TYR B OH  1 
ATOM   2325 N N   . GLY A 1 313 ? 8.311   26.152  -9.615  1.00 75.13  ? 499 GLY B N   1 
ATOM   2326 C CA  . GLY A 1 313 ? 7.931   25.903  -10.997 1.00 76.05  ? 499 GLY B CA  1 
ATOM   2327 C C   . GLY A 1 313 ? 7.412   27.108  -11.762 1.00 77.91  ? 499 GLY B C   1 
ATOM   2328 O O   . GLY A 1 313 ? 6.892   28.059  -11.179 1.00 78.54  ? 499 GLY B O   1 
ATOM   2329 N N   . HIS A 1 323 ? 15.166  23.474  -20.316 1.00 137.69 ? 509 HIS B N   1 
ATOM   2330 C CA  . HIS A 1 323 ? 15.557  23.064  -18.966 1.00 131.70 ? 509 HIS B CA  1 
ATOM   2331 C C   . HIS A 1 323 ? 14.576  23.473  -17.888 1.00 126.48 ? 509 HIS B C   1 
ATOM   2332 O O   . HIS A 1 323 ? 14.921  24.220  -16.969 1.00 112.03 ? 509 HIS B O   1 
ATOM   2333 C CB  . HIS A 1 323 ? 16.936  23.615  -18.611 1.00 134.58 ? 509 HIS B CB  1 
ATOM   2334 C CG  . HIS A 1 323 ? 18.058  22.910  -19.300 1.00 151.57 ? 509 HIS B CG  1 
ATOM   2335 N ND1 . HIS A 1 323 ? 18.330  21.575  -19.087 1.00 154.10 ? 509 HIS B ND1 1 
ATOM   2336 C CD2 . HIS A 1 323 ? 18.978  23.345  -20.194 1.00 160.31 ? 509 HIS B CD2 1 
ATOM   2337 C CE1 . HIS A 1 323 ? 19.368  21.217  -19.823 1.00 162.34 ? 509 HIS B CE1 1 
ATOM   2338 N NE2 . HIS A 1 323 ? 19.780  22.272  -20.504 1.00 161.24 ? 509 HIS B NE2 1 
ATOM   2339 N N   . CYS A 1 324 ? 13.339  23.005  -18.020 1.00 116.15 ? 510 CYS B N   1 
ATOM   2340 C CA  . CYS A 1 324 ? 12.310  23.322  -17.040 1.00 100.71 ? 510 CYS B CA  1 
ATOM   2341 C C   . CYS A 1 324 ? 12.496  22.431  -15.813 1.00 94.62  ? 510 CYS B C   1 
ATOM   2342 O O   . CYS A 1 324 ? 12.247  21.223  -15.867 1.00 92.98  ? 510 CYS B O   1 
ATOM   2343 C CB  . CYS A 1 324 ? 10.934  23.135  -17.668 1.00 86.40  ? 510 CYS B CB  1 
ATOM   2344 S SG  . CYS A 1 324 ? 9.576   23.287  -16.502 1.00 89.23  ? 510 CYS B SG  1 
ATOM   2345 N N   . THR A 1 325 ? 12.901  23.023  -14.693 1.00 84.60  ? 511 THR B N   1 
ATOM   2346 C CA  . THR A 1 325 ? 13.103  22.261  -13.467 1.00 87.09  ? 511 THR B CA  1 
ATOM   2347 C C   . THR A 1 325 ? 11.777  22.090  -12.727 1.00 76.53  ? 511 THR B C   1 
ATOM   2348 O O   . THR A 1 325 ? 10.997  23.040  -12.610 1.00 74.57  ? 511 THR B O   1 
ATOM   2349 C CB  . THR A 1 325 ? 14.141  22.940  -12.571 1.00 85.29  ? 511 THR B CB  1 
ATOM   2350 O OG1 . THR A 1 325 ? 13.502  23.925  -11.747 1.00 94.85  ? 511 THR B OG1 1 
ATOM   2351 C CG2 . THR A 1 325 ? 15.210  23.612  -13.417 1.00 76.71  ? 511 THR B CG2 1 
ATOM   2352 N N   . ASN A 1 326 ? 11.508  20.876  -12.245 1.00 73.26  ? 512 ASN B N   1 
ATOM   2353 C CA  . ASN A 1 326 ? 10.287  20.594  -11.500 1.00 72.56  ? 512 ASN B CA  1 
ATOM   2354 C C   . ASN A 1 326 ? 10.606  19.820  -10.231 1.00 71.20  ? 512 ASN B C   1 
ATOM   2355 O O   . ASN A 1 326 ? 11.422  18.893  -10.243 1.00 70.78  ? 512 ASN B O   1 
ATOM   2356 C CB  . ASN A 1 326 ? 9.272   19.806  -12.334 1.00 73.29  ? 512 ASN B CB  1 
ATOM   2357 C CG  . ASN A 1 326 ? 8.751   20.595  -13.508 1.00 74.90  ? 512 ASN B CG  1 
ATOM   2358 O OD1 . ASN A 1 326 ? 7.897   21.468  -13.350 1.00 75.40  ? 512 ASN B OD1 1 
ATOM   2359 N ND2 . ASN A 1 326 ? 9.252   20.288  -14.699 1.00 75.95  ? 512 ASN B ND2 1 
ATOM   2360 N N   . ALA A 1 327 ? 9.957   20.215  -9.136  1.00 70.75  ? 513 ALA B N   1 
ATOM   2361 C CA  . ALA A 1 327 ? 10.047  19.500  -7.870  1.00 69.77  ? 513 ALA B CA  1 
ATOM   2362 C C   . ALA A 1 327 ? 8.968   18.427  -7.836  1.00 71.23  ? 513 ALA B C   1 
ATOM   2363 O O   . ALA A 1 327 ? 7.790   18.721  -8.068  1.00 70.86  ? 513 ALA B O   1 
ATOM   2364 C CB  . ALA A 1 327 ? 9.883   20.463  -6.693  1.00 69.64  ? 513 ALA B CB  1 
ATOM   2365 N N   . TYR A 1 328 ? 9.368   17.179  -7.574  1.00 69.22  ? 514 TYR B N   1 
ATOM   2366 C CA  . TYR A 1 328 ? 8.427   16.069  -7.625  1.00 69.38  ? 514 TYR B CA  1 
ATOM   2367 C C   . TYR A 1 328 ? 8.270   15.299  -6.323  1.00 68.81  ? 514 TYR B C   1 
ATOM   2368 O O   . TYR A 1 328 ? 7.257   14.611  -6.165  1.00 69.08  ? 514 TYR B O   1 
ATOM   2369 C CB  . TYR A 1 328 ? 8.818   15.078  -8.734  1.00 69.86  ? 514 TYR B CB  1 
ATOM   2370 C CG  . TYR A 1 328 ? 10.145  14.392  -8.530  1.00 69.44  ? 514 TYR B CG  1 
ATOM   2371 C CD1 . TYR A 1 328 ? 11.335  15.019  -8.876  1.00 69.41  ? 514 TYR B CD1 1 
ATOM   2372 C CD2 . TYR A 1 328 ? 10.209  13.106  -8.009  1.00 69.27  ? 514 TYR B CD2 1 
ATOM   2373 C CE1 . TYR A 1 328 ? 12.551  14.392  -8.696  1.00 69.19  ? 514 TYR B CE1 1 
ATOM   2374 C CE2 . TYR A 1 328 ? 11.422  12.468  -7.827  1.00 69.10  ? 514 TYR B CE2 1 
ATOM   2375 C CZ  . TYR A 1 328 ? 12.588  13.117  -8.170  1.00 69.04  ? 514 TYR B CZ  1 
ATOM   2376 O OH  . TYR A 1 328 ? 13.798  12.492  -7.991  1.00 71.24  ? 514 TYR B OH  1 
ATOM   2377 N N   . MET A 1 329 ? 9.223   15.383  -5.396  1.00 68.24  ? 515 MET B N   1 
ATOM   2378 C CA  . MET A 1 329 ? 9.115   14.682  -4.122  1.00 67.97  ? 515 MET B CA  1 
ATOM   2379 C C   . MET A 1 329 ? 9.652   15.552  -2.993  1.00 67.74  ? 515 MET B C   1 
ATOM   2380 O O   . MET A 1 329 ? 10.680  16.218  -3.144  1.00 67.61  ? 515 MET B O   1 
ATOM   2381 C CB  . MET A 1 329 ? 9.860   13.340  -4.165  1.00 67.91  ? 515 MET B CB  1 
ATOM   2382 C CG  . MET A 1 329 ? 9.813   12.550  -2.869  1.00 67.89  ? 515 MET B CG  1 
ATOM   2383 S SD  . MET A 1 329 ? 10.512  10.900  -3.049  1.00 68.17  ? 515 MET B SD  1 
ATOM   2384 C CE  . MET A 1 329 ? 10.475  10.316  -1.355  1.00 68.37  ? 515 MET B CE  1 
ATOM   2385 N N   . LEU A 1 330 ? 8.951   15.532  -1.858  1.00 67.90  ? 516 LEU B N   1 
ATOM   2386 C CA  . LEU A 1 330 ? 9.306   16.315  -0.683  1.00 68.03  ? 516 LEU B CA  1 
ATOM   2387 C C   . LEU A 1 330 ? 9.359   15.414  0.544   1.00 68.21  ? 516 LEU B C   1 
ATOM   2388 O O   . LEU A 1 330 ? 8.568   14.473  0.665   1.00 68.40  ? 516 LEU B O   1 
ATOM   2389 C CB  . LEU A 1 330 ? 8.294   17.438  -0.454  1.00 68.51  ? 516 LEU B CB  1 
ATOM   2390 C CG  . LEU A 1 330 ? 8.018   18.331  -1.664  1.00 68.64  ? 516 LEU B CG  1 
ATOM   2391 C CD1 . LEU A 1 330 ? 6.873   19.290  -1.374  1.00 69.35  ? 516 LEU B CD1 1 
ATOM   2392 C CD2 . LEU A 1 330 ? 9.269   19.084  -2.084  1.00 68.51  ? 516 LEU B CD2 1 
ATOM   2393 N N   . VAL A 1 331 ? 10.294  15.699  1.452   1.00 68.37  ? 517 VAL B N   1 
ATOM   2394 C CA  . VAL A 1 331 ? 10.434  14.962  2.706   1.00 68.86  ? 517 VAL B CA  1 
ATOM   2395 C C   . VAL A 1 331 ? 10.322  15.946  3.861   1.00 70.25  ? 517 VAL B C   1 
ATOM   2396 O O   . VAL A 1 331 ? 11.101  16.904  3.946   1.00 72.03  ? 517 VAL B O   1 
ATOM   2397 C CB  . VAL A 1 331 ? 11.760  14.191  2.785   1.00 68.76  ? 517 VAL B CB  1 
ATOM   2398 C CG1 . VAL A 1 331 ? 11.802  13.374  4.064   1.00 69.53  ? 517 VAL B CG1 1 
ATOM   2399 C CG2 . VAL A 1 331 ? 11.935  13.294  1.571   1.00 68.26  ? 517 VAL B CG2 1 
ATOM   2400 N N   . TYR A 1 332 ? 9.369   15.696  4.757   1.00 70.31  ? 518 TYR B N   1 
ATOM   2401 C CA  . TYR A 1 332 ? 9.158   16.506  5.946   1.00 71.37  ? 518 TYR B CA  1 
ATOM   2402 C C   . TYR A 1 332 ? 9.426   15.663  7.186   1.00 72.28  ? 518 TYR B C   1 
ATOM   2403 O O   . TYR A 1 332 ? 9.179   14.454  7.199   1.00 76.11  ? 518 TYR B O   1 
ATOM   2404 C CB  . TYR A 1 332 ? 7.727   17.064  6.001   1.00 71.86  ? 518 TYR B CB  1 
ATOM   2405 C CG  . TYR A 1 332 ? 7.478   18.224  5.065   1.00 71.52  ? 518 TYR B CG  1 
ATOM   2406 C CD1 . TYR A 1 332 ? 7.074   18.006  3.756   1.00 70.70  ? 518 TYR B CD1 1 
ATOM   2407 C CD2 . TYR A 1 332 ? 7.660   19.537  5.483   1.00 72.25  ? 518 TYR B CD2 1 
ATOM   2408 C CE1 . TYR A 1 332 ? 6.848   19.061  2.891   1.00 70.63  ? 518 TYR B CE1 1 
ATOM   2409 C CE2 . TYR A 1 332 ? 7.438   20.602  4.623   1.00 72.16  ? 518 TYR B CE2 1 
ATOM   2410 C CZ  . TYR A 1 332 ? 7.032   20.356  3.328   1.00 71.34  ? 518 TYR B CZ  1 
ATOM   2411 O OH  . TYR A 1 332 ? 6.807   21.406  2.465   1.00 71.49  ? 518 TYR B OH  1 
ATOM   2412 N N   . ILE A 1 333 ? 9.926   16.309  8.235   1.00 73.34  ? 519 ILE B N   1 
ATOM   2413 C CA  . ILE A 1 333 ? 10.190  15.654  9.511   1.00 74.61  ? 519 ILE B CA  1 
ATOM   2414 C C   . ILE A 1 333 ? 9.408   16.384  10.590  1.00 76.85  ? 519 ILE B C   1 
ATOM   2415 O O   . ILE A 1 333 ? 9.434   17.619  10.649  1.00 76.51  ? 519 ILE B O   1 
ATOM   2416 C CB  . ILE A 1 333 ? 11.690  15.636  9.845   1.00 74.89  ? 519 ILE B CB  1 
ATOM   2417 C CG1 . ILE A 1 333 ? 12.462  14.875  8.769   1.00 75.86  ? 519 ILE B CG1 1 
ATOM   2418 C CG2 . ILE A 1 333 ? 11.922  15.011  11.211  1.00 79.56  ? 519 ILE B CG2 1 
ATOM   2419 C CD1 . ILE A 1 333 ? 13.940  14.780  9.042   1.00 74.30  ? 519 ILE B CD1 1 
ATOM   2420 N N   . ARG A 1 334 ? 8.713   15.620  11.435  1.00 81.89  ? 520 ARG B N   1 
ATOM   2421 C CA  . ARG A 1 334 ? 7.894   16.212  12.486  1.00 78.98  ? 520 ARG B CA  1 
ATOM   2422 C C   . ARG A 1 334 ? 8.766   16.961  13.481  1.00 80.46  ? 520 ARG B C   1 
ATOM   2423 O O   . ARG A 1 334 ? 9.849   16.504  13.858  1.00 84.17  ? 520 ARG B O   1 
ATOM   2424 C CB  . ARG A 1 334 ? 7.075   15.138  13.206  1.00 83.51  ? 520 ARG B CB  1 
ATOM   2425 C CG  . ARG A 1 334 ? 5.886   15.683  13.999  1.00 81.73  ? 520 ARG B CG  1 
ATOM   2426 C CD  . ARG A 1 334 ? 5.172   14.574  14.767  1.00 85.90  ? 520 ARG B CD  1 
ATOM   2427 N NE  . ARG A 1 334 ? 3.922   15.024  15.373  1.00 97.28  ? 520 ARG B NE  1 
ATOM   2428 C CZ  . ARG A 1 334 ? 2.709   14.759  14.902  1.00 84.36  ? 520 ARG B CZ  1 
ATOM   2429 N NH1 . ARG A 1 334 ? 2.531   14.021  13.819  1.00 85.50  ? 520 ARG B NH1 1 
ATOM   2430 N NH2 . ARG A 1 334 ? 1.646   15.250  15.534  1.00 86.03  ? 520 ARG B NH2 1 
ATOM   2431 N N   . GLU A 1 335 ? 8.274   18.120  13.914  1.00 81.58  ? 521 GLU B N   1 
ATOM   2432 C CA  . GLU A 1 335 ? 9.060   18.974  14.791  1.00 83.20  ? 521 GLU B CA  1 
ATOM   2433 C C   . GLU A 1 335 ? 9.364   18.275  16.111  1.00 85.19  ? 521 GLU B C   1 
ATOM   2434 O O   . GLU A 1 335 ? 10.485  18.368  16.626  1.00 89.22  ? 521 GLU B O   1 
ATOM   2435 C CB  . GLU A 1 335 ? 8.320   20.290  15.016  1.00 84.33  ? 521 GLU B CB  1 
ATOM   2436 C CG  . GLU A 1 335 ? 9.229   21.480  15.238  1.00 95.43  ? 521 GLU B CG  1 
ATOM   2437 C CD  . GLU A 1 335 ? 8.472   22.796  15.246  1.00 111.78 ? 521 GLU B CD  1 
ATOM   2438 O OE1 . GLU A 1 335 ? 7.258   22.791  15.554  1.00 106.80 ? 521 GLU B OE1 1 
ATOM   2439 O OE2 . GLU A 1 335 ? 9.091   23.836  14.937  1.00 121.07 ? 521 GLU B OE2 1 
ATOM   2440 N N   . SER A 1 336 ? 8.383   17.553  16.664  1.00 86.13  ? 522 SER B N   1 
ATOM   2441 C CA  . SER A 1 336 ? 8.595   16.848  17.926  1.00 88.31  ? 522 SER B CA  1 
ATOM   2442 C C   . SER A 1 336 ? 9.624   15.730  17.789  1.00 96.02  ? 522 SER B C   1 
ATOM   2443 O O   . SER A 1 336 ? 10.264  15.357  18.778  1.00 103.05 ? 522 SER B O   1 
ATOM   2444 C CB  . SER A 1 336 ? 7.271   16.284  18.455  1.00 89.49  ? 522 SER B CB  1 
ATOM   2445 O OG  . SER A 1 336 ? 6.670   15.377  17.544  1.00 87.66  ? 522 SER B OG  1 
ATOM   2446 N N   . LYS A 1 337 ? 9.793   15.184  16.586  1.00 91.20  ? 523 LYS B N   1 
ATOM   2447 C CA  . LYS A 1 337 ? 10.703  14.072  16.352  1.00 92.18  ? 523 LYS B CA  1 
ATOM   2448 C C   . LYS A 1 337 ? 12.017  14.493  15.702  1.00 90.39  ? 523 LYS B C   1 
ATOM   2449 O O   . LYS A 1 337 ? 12.828  13.625  15.368  1.00 84.12  ? 523 LYS B O   1 
ATOM   2450 C CB  . LYS A 1 337 ? 10.013  13.015  15.480  1.00 83.51  ? 523 LYS B CB  1 
ATOM   2451 C CG  . LYS A 1 337 ? 8.659   12.571  16.014  1.00 84.28  ? 523 LYS B CG  1 
ATOM   2452 C CD  . LYS A 1 337 ? 8.805   11.849  17.342  1.00 94.41  ? 523 LYS B CD  1 
ATOM   2453 C CE  . LYS A 1 337 ? 7.465   11.366  17.864  1.00 93.67  ? 523 LYS B CE  1 
ATOM   2454 N NZ  . LYS A 1 337 ? 7.613   10.655  19.166  1.00 95.96  ? 523 LYS B NZ  1 
ATOM   2455 N N   . LEU A 1 338 ? 12.246  15.796  15.513  1.00 88.87  ? 524 LEU B N   1 
ATOM   2456 C CA  . LEU A 1 338 ? 13.359  16.235  14.674  1.00 84.73  ? 524 LEU B CA  1 
ATOM   2457 C C   . LEU A 1 338 ? 14.709  15.817  15.249  1.00 83.89  ? 524 LEU B C   1 
ATOM   2458 O O   . LEU A 1 338 ? 15.586  15.359  14.510  1.00 86.05  ? 524 LEU B O   1 
ATOM   2459 C CB  . LEU A 1 338 ? 13.303  17.748  14.469  1.00 86.07  ? 524 LEU B CB  1 
ATOM   2460 C CG  . LEU A 1 338 ? 14.365  18.323  13.527  1.00 80.75  ? 524 LEU B CG  1 
ATOM   2461 C CD1 . LEU A 1 338 ? 14.331  17.637  12.169  1.00 78.99  ? 524 LEU B CD1 1 
ATOM   2462 C CD2 . LEU A 1 338 ? 14.169  19.819  13.365  1.00 81.06  ? 524 LEU B CD2 1 
ATOM   2463 N N   . SER A 1 339 ? 14.900  15.973  16.562  1.00 87.11  ? 525 SER B N   1 
ATOM   2464 C CA  . SER A 1 339 ? 16.193  15.640  17.156  1.00 86.83  ? 525 SER B CA  1 
ATOM   2465 C C   . SER A 1 339 ? 16.455  14.139  17.142  1.00 86.74  ? 525 SER B C   1 
ATOM   2466 O O   . SER A 1 339 ? 17.590  13.704  16.909  1.00 89.51  ? 525 SER B O   1 
ATOM   2467 C CB  . SER A 1 339 ? 16.265  16.168  18.589  1.00 89.82  ? 525 SER B CB  1 
ATOM   2468 O OG  . SER A 1 339 ? 16.261  17.582  18.612  1.00 92.10  ? 525 SER B OG  1 
ATOM   2469 N N   . GLU A 1 340 ? 15.423  13.333  17.391  1.00 86.98  ? 526 GLU B N   1 
ATOM   2470 C CA  . GLU A 1 340 ? 15.602  11.885  17.422  1.00 87.20  ? 526 GLU B CA  1 
ATOM   2471 C C   . GLU A 1 340 ? 15.781  11.311  16.020  1.00 87.19  ? 526 GLU B C   1 
ATOM   2472 O O   . GLU A 1 340 ? 16.575  10.385  15.821  1.00 84.76  ? 526 GLU B O   1 
ATOM   2473 C CB  . GLU A 1 340 ? 14.417  11.239  18.141  1.00 88.49  ? 526 GLU B CB  1 
ATOM   2474 C CG  . GLU A 1 340 ? 14.587  9.760   18.427  1.00 90.24  ? 526 GLU B CG  1 
ATOM   2475 C CD  . GLU A 1 340 ? 13.384  9.157   19.127  1.00 91.73  ? 526 GLU B CD  1 
ATOM   2476 O OE1 . GLU A 1 340 ? 12.273  9.716   19.004  1.00 105.69 ? 526 GLU B OE1 1 
ATOM   2477 O OE2 . GLU A 1 340 ? 13.560  8.134   19.824  1.00 92.75  ? 526 GLU B OE2 1 
ATOM   2478 N N   . VAL A 1 341 ? 15.055  11.848  15.034  1.00 93.46  ? 527 VAL B N   1 
ATOM   2479 C CA  . VAL A 1 341 ? 15.207  11.381  13.657  1.00 84.84  ? 527 VAL B CA  1 
ATOM   2480 C C   . VAL A 1 341 ? 16.579  11.754  13.110  1.00 80.48  ? 527 VAL B C   1 
ATOM   2481 O O   . VAL A 1 341 ? 17.193  10.988  12.358  1.00 79.19  ? 527 VAL B O   1 
ATOM   2482 C CB  . VAL A 1 341 ? 14.073  11.940  12.778  1.00 78.99  ? 527 VAL B CB  1 
ATOM   2483 C CG1 . VAL A 1 341 ? 14.337  11.643  11.313  1.00 78.78  ? 527 VAL B CG1 1 
ATOM   2484 C CG2 . VAL A 1 341 ? 12.741  11.343  13.201  1.00 81.94  ? 527 VAL B CG2 1 
ATOM   2485 N N   . LEU A 1 342 ? 17.081  12.930  13.477  1.00 81.89  ? 528 LEU B N   1 
ATOM   2486 C CA  . LEU A 1 342 ? 18.371  13.427  13.005  1.00 83.13  ? 528 LEU B CA  1 
ATOM   2487 C C   . LEU A 1 342 ? 19.456  13.286  14.065  1.00 89.34  ? 528 LEU B C   1 
ATOM   2488 O O   . LEU A 1 342 ? 20.275  14.193  14.235  1.00 95.53  ? 528 LEU B O   1 
ATOM   2489 C CB  . LEU A 1 342 ? 18.255  14.880  12.552  1.00 82.86  ? 528 LEU B CB  1 
ATOM   2490 C CG  . LEU A 1 342 ? 17.365  15.187  11.344  1.00 77.46  ? 528 LEU B CG  1 
ATOM   2491 C CD1 . LEU A 1 342 ? 17.595  16.609  10.845  1.00 77.03  ? 528 LEU B CD1 1 
ATOM   2492 C CD2 . LEU A 1 342 ? 17.601  14.185  10.231  1.00 76.02  ? 528 LEU B CD2 1 
ATOM   2493 N N   . GLN A 1 343 ? 19.468  12.170  14.802  1.00 89.29  ? 529 GLN B N   1 
ATOM   2494 C CA  . GLN A 1 343 ? 20.501  11.928  15.805  1.00 85.88  ? 529 GLN B CA  1 
ATOM   2495 C C   . GLN A 1 343 ? 21.893  12.122  15.224  1.00 88.28  ? 529 GLN B C   1 
ATOM   2496 O O   . GLN A 1 343 ? 22.128  11.932  14.027  1.00 90.79  ? 529 GLN B O   1 
ATOM   2497 C CB  . GLN A 1 343 ? 20.410  10.509  16.366  1.00 87.17  ? 529 GLN B CB  1 
ATOM   2498 C CG  . GLN A 1 343 ? 19.220  10.233  17.235  1.00 91.53  ? 529 GLN B CG  1 
ATOM   2499 C CD  . GLN A 1 343 ? 19.092  8.762   17.558  1.00 95.41  ? 529 GLN B CD  1 
ATOM   2500 O OE1 . GLN A 1 343 ? 20.092  8.039   17.595  1.00 90.24  ? 529 GLN B OE1 1 
ATOM   2501 N NE2 . GLN A 1 343 ? 17.865  8.306   17.799  1.00 89.59  ? 529 GLN B NE2 1 
ATOM   2502 N N   . ALA A 1 344 ? 22.827  12.504  16.088  1.00 87.58  ? 530 ALA B N   1 
ATOM   2503 C CA  . ALA A 1 344 ? 24.222  12.467  15.691  1.00 87.74  ? 530 ALA B CA  1 
ATOM   2504 C C   . ALA A 1 344 ? 24.631  11.022  15.453  1.00 87.87  ? 530 ALA B C   1 
ATOM   2505 O O   . ALA A 1 344 ? 24.225  10.115  16.186  1.00 89.17  ? 530 ALA B O   1 
ATOM   2506 C CB  . ALA A 1 344 ? 25.104  13.105  16.764  1.00 95.62  ? 530 ALA B CB  1 
ATOM   2507 N N   . VAL A 1 345 ? 25.409  10.803  14.401  1.00 86.66  ? 531 VAL B N   1 
ATOM   2508 C CA  . VAL A 1 345 ? 25.893  9.476   14.041  1.00 92.10  ? 531 VAL B CA  1 
ATOM   2509 C C   . VAL A 1 345 ? 27.420  9.511   14.040  1.00 96.27  ? 531 VAL B C   1 
ATOM   2510 O O   . VAL A 1 345 ? 28.031  10.225  13.234  1.00 89.88  ? 531 VAL B O   1 
ATOM   2511 C CB  . VAL A 1 345 ? 25.334  9.022   12.684  1.00 84.46  ? 531 VAL B CB  1 
ATOM   2512 C CG1 . VAL A 1 345 ? 25.277  10.196  11.722  1.00 82.57  ? 531 VAL B CG1 1 
ATOM   2513 C CG2 . VAL A 1 345 ? 26.180  7.891   12.115  1.00 93.84  ? 531 VAL B CG2 1 
ATOM   2514 N N   . THR A 1 346 ? 28.031  8.739   14.937  1.00 94.87  ? 532 THR B N   1 
ATOM   2515 C CA  . THR A 1 346 ? 29.480  8.672   15.074  1.00 95.54  ? 532 THR B CA  1 
ATOM   2516 C C   . THR A 1 346 ? 30.029  7.436   14.364  1.00 98.45  ? 532 THR B C   1 
ATOM   2517 O O   . THR A 1 346 ? 29.292  6.507   14.020  1.00 101.41 ? 532 THR B O   1 
ATOM   2518 C CB  . THR A 1 346 ? 29.900  8.657   16.551  1.00 95.18  ? 532 THR B CB  1 
ATOM   2519 O OG1 . THR A 1 346 ? 29.418  7.462   17.180  1.00 100.03 ? 532 THR B OG1 1 
ATOM   2520 C CG2 . THR A 1 346 ? 29.349  9.874   17.288  1.00 95.60  ? 532 THR B CG2 1 
ATOM   2521 N N   . ASP A 1 347 ? 31.349  7.438   14.145  1.00 95.75  ? 533 ASP B N   1 
ATOM   2522 C CA  . ASP A 1 347 ? 31.999  6.328   13.456  1.00 93.20  ? 533 ASP B CA  1 
ATOM   2523 C C   . ASP A 1 347 ? 31.960  5.034   14.256  1.00 95.36  ? 533 ASP B C   1 
ATOM   2524 O O   . ASP A 1 347 ? 32.061  3.952   13.667  1.00 95.34  ? 533 ASP B O   1 
ATOM   2525 C CB  . ASP A 1 347 ? 33.448  6.695   13.139  1.00 94.11  ? 533 ASP B CB  1 
ATOM   2526 C CG  . ASP A 1 347 ? 33.557  7.711   12.021  1.00 100.66 ? 533 ASP B CG  1 
ATOM   2527 O OD1 . ASP A 1 347 ? 32.503  8.098   11.465  1.00 97.53  ? 533 ASP B OD1 1 
ATOM   2528 O OD2 . ASP A 1 347 ? 34.695  8.119   11.694  1.00 111.66 ? 533 ASP B OD2 1 
ATOM   2529 N N   . HIS A 1 348 ? 31.836  5.124   15.577  1.00 101.45 ? 534 HIS B N   1 
ATOM   2530 C CA  . HIS A 1 348 ? 31.714  3.958   16.440  1.00 103.79 ? 534 HIS B CA  1 
ATOM   2531 C C   . HIS A 1 348 ? 30.310  3.366   16.463  1.00 103.06 ? 534 HIS B C   1 
ATOM   2532 O O   . HIS A 1 348 ? 30.144  2.240   16.944  1.00 105.70 ? 534 HIS B O   1 
ATOM   2533 C CB  . HIS A 1 348 ? 32.188  4.327   17.845  1.00 108.11 ? 534 HIS B CB  1 
ATOM   2534 C CG  . HIS A 1 348 ? 33.638  4.696   17.894  1.00 114.05 ? 534 HIS B CG  1 
ATOM   2535 N ND1 . HIS A 1 348 ? 34.634  3.757   18.048  1.00 117.62 ? 534 HIS B ND1 1 
ATOM   2536 C CD2 . HIS A 1 348 ? 34.264  5.889   17.756  1.00 112.93 ? 534 HIS B CD2 1 
ATOM   2537 C CE1 . HIS A 1 348 ? 35.811  4.358   18.030  1.00 130.42 ? 534 HIS B CE1 1 
ATOM   2538 N NE2 . HIS A 1 348 ? 35.614  5.652   17.854  1.00 128.03 ? 534 HIS B NE2 1 
ATOM   2539 N N   . ASP A 1 349 ? 29.303  4.091   15.966  1.00 98.46  ? 535 ASP B N   1 
ATOM   2540 C CA  . ASP A 1 349 ? 27.970  3.517   15.836  1.00 98.75  ? 535 ASP B CA  1 
ATOM   2541 C C   . ASP A 1 349 ? 27.959  2.329   14.885  1.00 94.89  ? 535 ASP B C   1 
ATOM   2542 O O   . ASP A 1 349 ? 27.038  1.508   14.941  1.00 98.28  ? 535 ASP B O   1 
ATOM   2543 C CB  . ASP A 1 349 ? 26.979  4.583   15.362  1.00 94.53  ? 535 ASP B CB  1 
ATOM   2544 C CG  . ASP A 1 349 ? 26.630  5.584   16.454  1.00 98.97  ? 535 ASP B CG  1 
ATOM   2545 O OD1 . ASP A 1 349 ? 26.401  5.159   17.609  1.00 99.93  ? 535 ASP B OD1 1 
ATOM   2546 O OD2 . ASP A 1 349 ? 26.589  6.797   16.158  1.00 92.99  ? 535 ASP B OD2 1 
ATOM   2547 N N   . ILE A 1 350 ? 28.956  2.228   14.013  1.00 94.20  ? 536 ILE B N   1 
ATOM   2548 C CA  . ILE A 1 350 ? 29.065  1.123   13.066  1.00 96.67  ? 536 ILE B CA  1 
ATOM   2549 C C   . ILE A 1 350 ? 29.796  -0.024  13.758  1.00 105.77 ? 536 ILE B C   1 
ATOM   2550 O O   . ILE A 1 350 ? 30.913  0.185   14.261  1.00 98.67  ? 536 ILE B O   1 
ATOM   2551 C CB  . ILE A 1 350 ? 29.803  1.554   11.796  1.00 92.84  ? 536 ILE B CB  1 
ATOM   2552 C CG1 . ILE A 1 350 ? 29.265  2.904   11.321  1.00 89.85  ? 536 ILE B CG1 1 
ATOM   2553 C CG2 . ILE A 1 350 ? 29.649  0.498   10.717  1.00 91.81  ? 536 ILE B CG2 1 
ATOM   2554 C CD1 . ILE A 1 350 ? 29.891  3.404   10.051  1.00 88.35  ? 536 ILE B CD1 1 
ATOM   2555 N N   . PRO A 1 351 ? 29.222  -1.227  13.800  1.00 106.00 ? 537 PRO B N   1 
ATOM   2556 C CA  . PRO A 1 351 ? 29.893  -2.353  14.465  1.00 110.10 ? 537 PRO B CA  1 
ATOM   2557 C C   . PRO A 1 351 ? 31.225  -2.690  13.807  1.00 106.11 ? 537 PRO B C   1 
ATOM   2558 O O   . PRO A 1 351 ? 31.409  -2.520  12.600  1.00 102.58 ? 537 PRO B O   1 
ATOM   2559 C CB  . PRO A 1 351 ? 28.888  -3.502  14.317  1.00 101.25 ? 537 PRO B CB  1 
ATOM   2560 C CG  . PRO A 1 351 ? 27.569  -2.824  14.128  1.00 98.80  ? 537 PRO B CG  1 
ATOM   2561 C CD  . PRO A 1 351 ? 27.862  -1.575  13.359  1.00 97.47  ? 537 PRO B CD  1 
ATOM   2562 N N   . GLN A 1 352 ? 32.165  -3.165  14.630  1.00 104.79 ? 538 GLN B N   1 
ATOM   2563 C CA  . GLN A 1 352 ? 33.516  -3.426  14.140  1.00 115.30 ? 538 GLN B CA  1 
ATOM   2564 C C   . GLN A 1 352 ? 33.545  -4.527  13.085  1.00 113.54 ? 538 GLN B C   1 
ATOM   2565 O O   . GLN A 1 352 ? 34.305  -4.435  12.111  1.00 111.89 ? 538 GLN B O   1 
ATOM   2566 C CB  . GLN A 1 352 ? 34.439  -3.792  15.301  1.00 122.41 ? 538 GLN B CB  1 
ATOM   2567 C CG  . GLN A 1 352 ? 34.839  -2.620  16.178  1.00 124.68 ? 538 GLN B CG  1 
ATOM   2568 C CD  . GLN A 1 352 ? 35.734  -3.039  17.329  1.00 139.06 ? 538 GLN B CD  1 
ATOM   2569 O OE1 . GLN A 1 352 ? 35.760  -4.208  17.722  1.00 129.88 ? 538 GLN B OE1 1 
ATOM   2570 N NE2 . GLN A 1 352 ? 36.477  -2.084  17.877  1.00 148.90 ? 538 GLN B NE2 1 
ATOM   2571 N N   . GLN A 1 353 ? 32.730  -5.577  13.247  1.00 107.50 ? 539 GLN B N   1 
ATOM   2572 C CA  . GLN A 1 353 ? 32.707  -6.621  12.220  1.00 112.77 ? 539 GLN B CA  1 
ATOM   2573 C C   . GLN A 1 353 ? 32.143  -6.118  10.901  1.00 109.56 ? 539 GLN B C   1 
ATOM   2574 O O   . GLN A 1 353 ? 32.570  -6.582  9.840   1.00 113.90 ? 539 GLN B O   1 
ATOM   2575 C CB  . GLN A 1 353 ? 31.943  -7.856  12.696  1.00 127.31 ? 539 GLN B CB  1 
ATOM   2576 C CG  . GLN A 1 353 ? 32.677  -8.629  13.791  1.00 141.55 ? 539 GLN B CG  1 
ATOM   2577 C CD  . GLN A 1 353 ? 31.936  -9.877  14.225  1.00 152.17 ? 539 GLN B CD  1 
ATOM   2578 O OE1 . GLN A 1 353 ? 30.718  -9.985  14.058  1.00 152.80 ? 539 GLN B OE1 1 
ATOM   2579 N NE2 . GLN A 1 353 ? 32.672  -10.838 14.778  1.00 143.64 ? 539 GLN B NE2 1 
ATOM   2580 N N   . LEU A 1 354 ? 31.186  -5.188  10.938  1.00 105.01 ? 540 LEU B N   1 
ATOM   2581 C CA  . LEU A 1 354 ? 30.747  -4.563  9.696   1.00 98.18  ? 540 LEU B CA  1 
ATOM   2582 C C   . LEU A 1 354 ? 31.889  -3.775  9.067   1.00 97.54  ? 540 LEU B C   1 
ATOM   2583 O O   . LEU A 1 354 ? 32.094  -3.823  7.848   1.00 96.54  ? 540 LEU B O   1 
ATOM   2584 C CB  . LEU A 1 354 ? 29.545  -3.656  9.948   1.00 96.54  ? 540 LEU B CB  1 
ATOM   2585 C CG  . LEU A 1 354 ? 28.940  -3.025  8.690   1.00 93.04  ? 540 LEU B CG  1 
ATOM   2586 C CD1 . LEU A 1 354 ? 28.466  -4.095  7.719   1.00 93.11  ? 540 LEU B CD1 1 
ATOM   2587 C CD2 . LEU A 1 354 ? 27.805  -2.093  9.058   1.00 91.17  ? 540 LEU B CD2 1 
ATOM   2588 N N   . VAL A 1 355 ? 32.639  -3.036  9.889   1.00 103.03 ? 541 VAL B N   1 
ATOM   2589 C CA  . VAL A 1 355 ? 33.772  -2.263  9.387   1.00 102.86 ? 541 VAL B CA  1 
ATOM   2590 C C   . VAL A 1 355 ? 34.823  -3.192  8.788   1.00 100.73 ? 541 VAL B C   1 
ATOM   2591 O O   . VAL A 1 355 ? 35.425  -2.888  7.750   1.00 99.12  ? 541 VAL B O   1 
ATOM   2592 C CB  . VAL A 1 355 ? 34.357  -1.384  10.509  1.00 98.98  ? 541 VAL B CB  1 
ATOM   2593 C CG1 . VAL A 1 355 ? 35.594  -0.655  10.026  1.00 104.40 ? 541 VAL B CG1 1 
ATOM   2594 C CG2 . VAL A 1 355 ? 33.317  -0.388  11.000  1.00 99.90  ? 541 VAL B CG2 1 
ATOM   2595 N N   . GLU A 1 356 ? 35.058  -4.341  9.427   1.00 102.57 ? 542 GLU B N   1 
ATOM   2596 C CA  . GLU A 1 356 ? 36.087  -5.257  8.943   1.00 104.76 ? 542 GLU B CA  1 
ATOM   2597 C C   . GLU A 1 356 ? 35.748  -5.820  7.567   1.00 103.74 ? 542 GLU B C   1 
ATOM   2598 O O   . GLU A 1 356 ? 36.630  -5.942  6.708   1.00 104.31 ? 542 GLU B O   1 
ATOM   2599 C CB  . GLU A 1 356 ? 36.293  -6.398  9.941   1.00 113.06 ? 542 GLU B CB  1 
ATOM   2600 C CG  . GLU A 1 356 ? 36.998  -6.004  11.232  1.00 114.31 ? 542 GLU B CG  1 
ATOM   2601 C CD  . GLU A 1 356 ? 36.990  -7.120  12.263  1.00 130.10 ? 542 GLU B CD  1 
ATOM   2602 O OE1 . GLU A 1 356 ? 36.180  -8.060  12.116  1.00 139.14 ? 542 GLU B OE1 1 
ATOM   2603 O OE2 . GLU A 1 356 ? 37.797  -7.059  13.216  1.00 138.37 ? 542 GLU B OE2 1 
ATOM   2604 N N   . ARG A 1 357 ? 34.483  -6.177  7.335   1.00 102.48 ? 543 ARG B N   1 
ATOM   2605 C CA  . ARG A 1 357 ? 34.131  -6.793  6.058   1.00 101.92 ? 543 ARG B CA  1 
ATOM   2606 C C   . ARG A 1 357 ? 34.232  -5.800  4.904   1.00 99.51  ? 543 ARG B C   1 
ATOM   2607 O O   . ARG A 1 357 ? 34.706  -6.151  3.816   1.00 99.94  ? 543 ARG B O   1 
ATOM   2608 C CB  . ARG A 1 357 ? 32.724  -7.392  6.122   1.00 101.32 ? 543 ARG B CB  1 
ATOM   2609 C CG  . ARG A 1 357 ? 32.346  -8.128  4.839   1.00 106.74 ? 543 ARG B CG  1 
ATOM   2610 C CD  . ARG A 1 357 ? 30.980  -8.791  4.901   1.00 107.58 ? 543 ARG B CD  1 
ATOM   2611 N NE  . ARG A 1 357 ? 30.663  -9.445  3.636   1.00 105.88 ? 543 ARG B NE  1 
ATOM   2612 C CZ  . ARG A 1 357 ? 29.515  -10.054 3.370   1.00 107.63 ? 543 ARG B CZ  1 
ATOM   2613 N NH1 . ARG A 1 357 ? 28.546  -10.124 4.268   1.00 108.64 ? 543 ARG B NH1 1 
ATOM   2614 N NH2 . ARG A 1 357 ? 29.332  -10.599 2.170   1.00 105.44 ? 543 ARG B NH2 1 
ATOM   2615 N N   . LEU A 1 358 ? 33.779  -4.564  5.113   1.00 97.18  ? 544 LEU B N   1 
ATOM   2616 C CA  . LEU A 1 358 ? 33.812  -3.580  4.036   1.00 95.00  ? 544 LEU B CA  1 
ATOM   2617 C C   . LEU A 1 358 ? 35.237  -3.200  3.663   1.00 95.96  ? 544 LEU B C   1 
ATOM   2618 O O   . LEU A 1 358 ? 35.560  -3.082  2.475   1.00 97.59  ? 544 LEU B O   1 
ATOM   2619 C CB  . LEU A 1 358 ? 33.014  -2.342  4.432   1.00 92.60  ? 544 LEU B CB  1 
ATOM   2620 C CG  . LEU A 1 358 ? 31.520  -2.358  4.108   1.00 90.76  ? 544 LEU B CG  1 
ATOM   2621 C CD1 . LEU A 1 358 ? 30.722  -3.246  5.057   1.00 91.81  ? 544 LEU B CD1 1 
ATOM   2622 C CD2 . LEU A 1 358 ? 31.008  -0.944  4.152   1.00 88.43  ? 544 LEU B CD2 1 
ATOM   2623 N N   . GLN A 1 359 ? 36.110  -3.017  4.657   1.00 97.54  ? 545 GLN B N   1 
ATOM   2624 C CA  . GLN A 1 359 ? 37.503  -2.710  4.351   1.00 98.72  ? 545 GLN B CA  1 
ATOM   2625 C C   . GLN A 1 359 ? 38.180  -3.867  3.633   1.00 100.86 ? 545 GLN B C   1 
ATOM   2626 O O   . GLN A 1 359 ? 39.043  -3.645  2.777   1.00 101.27 ? 545 GLN B O   1 
ATOM   2627 C CB  . GLN A 1 359 ? 38.262  -2.343  5.625   1.00 100.26 ? 545 GLN B CB  1 
ATOM   2628 C CG  . GLN A 1 359 ? 37.777  -1.052  6.270   1.00 101.55 ? 545 GLN B CG  1 
ATOM   2629 C CD  . GLN A 1 359 ? 38.529  -0.720  7.541   1.00 113.52 ? 545 GLN B CD  1 
ATOM   2630 O OE1 . GLN A 1 359 ? 39.112  -1.598  8.181   1.00 133.46 ? 545 GLN B OE1 1 
ATOM   2631 N NE2 . GLN A 1 359 ? 38.524  0.556   7.916   1.00 101.25 ? 545 GLN B NE2 1 
ATOM   2632 N N   . GLU A 1 360 ? 37.802  -5.103  3.962   1.00 102.44 ? 546 GLU B N   1 
ATOM   2633 C CA  . GLU A 1 360 ? 38.339  -6.249  3.239   1.00 104.62 ? 546 GLU B CA  1 
ATOM   2634 C C   . GLU A 1 360 ? 37.934  -6.208  1.771   1.00 103.23 ? 546 GLU B C   1 
ATOM   2635 O O   . GLU A 1 360 ? 38.748  -6.501  0.888   1.00 104.53 ? 546 GLU B O   1 
ATOM   2636 C CB  . GLU A 1 360 ? 37.880  -7.551  3.894   1.00 106.60 ? 546 GLU B CB  1 
ATOM   2637 C CG  . GLU A 1 360 ? 38.261  -8.805  3.115   1.00 108.96 ? 546 GLU B CG  1 
ATOM   2638 C CD  . GLU A 1 360 ? 39.765  -9.033  3.042   1.00 114.59 ? 546 GLU B CD  1 
ATOM   2639 O OE1 . GLU A 1 360 ? 40.478  -8.701  4.015   1.00 112.64 ? 546 GLU B OE1 1 
ATOM   2640 O OE2 . GLU A 1 360 ? 40.232  -9.558  2.007   1.00 114.32 ? 546 GLU B OE2 1 
ATOM   2641 N N   . GLU A 1 361 ? 36.679  -5.853  1.489   1.00 100.80 ? 547 GLU B N   1 
ATOM   2642 C CA  . GLU A 1 361 ? 36.249  -5.737  0.099   1.00 99.57  ? 547 GLU B CA  1 
ATOM   2643 C C   . GLU A 1 361 ? 37.048  -4.670  -0.641  1.00 98.74  ? 547 GLU B C   1 
ATOM   2644 O O   . GLU A 1 361 ? 37.488  -4.891  -1.776  1.00 99.51  ? 547 GLU B O   1 
ATOM   2645 C CB  . GLU A 1 361 ? 34.756  -5.426  0.029   1.00 97.16  ? 547 GLU B CB  1 
ATOM   2646 C CG  . GLU A 1 361 ? 33.855  -6.591  0.392   1.00 98.10  ? 547 GLU B CG  1 
ATOM   2647 C CD  . GLU A 1 361 ? 32.410  -6.324  0.023   1.00 95.91  ? 547 GLU B CD  1 
ATOM   2648 O OE1 . GLU A 1 361 ? 32.114  -5.191  -0.410  1.00 93.64  ? 547 GLU B OE1 1 
ATOM   2649 O OE2 . GLU A 1 361 ? 31.578  -7.247  0.146   1.00 98.50  ? 547 GLU B OE2 1 
ATOM   2650 N N   . LYS A 1 362 ? 37.261  -3.512  -0.007  1.00 97.41  ? 548 LYS B N   1 
ATOM   2651 C CA  . LYS A 1 362 ? 38.037  -2.455  -0.650  1.00 96.79  ? 548 LYS B CA  1 
ATOM   2652 C C   . LYS A 1 362 ? 39.484  -2.875  -0.871  1.00 102.30 ? 548 LYS B C   1 
ATOM   2653 O O   . LYS A 1 362 ? 40.108  -2.443  -1.847  1.00 108.29 ? 548 LYS B O   1 
ATOM   2654 C CB  . LYS A 1 362 ? 37.965  -1.167  0.175   1.00 95.17  ? 548 LYS B CB  1 
ATOM   2655 C CG  . LYS A 1 362 ? 36.612  -0.474  0.098   1.00 98.44  ? 548 LYS B CG  1 
ATOM   2656 C CD  . LYS A 1 362 ? 36.661  0.949   0.640   1.00 92.51  ? 548 LYS B CD  1 
ATOM   2657 C CE  . LYS A 1 362 ? 36.916  0.968   2.141   1.00 93.73  ? 548 LYS B CE  1 
ATOM   2658 N NZ  . LYS A 1 362 ? 36.956  2.354   2.695   1.00 91.69  ? 548 LYS B NZ  1 
ATOM   2659 N N   . ARG A 1 363 ? 40.032  -3.718  0.012   1.00 101.68 ? 549 ARG B N   1 
ATOM   2660 C CA  . ARG A 1 363 ? 41.363  -4.269  -0.227  1.00 104.50 ? 549 ARG B CA  1 
ATOM   2661 C C   . ARG A 1 363 ? 41.384  -5.130  -1.484  1.00 105.64 ? 549 ARG B C   1 
ATOM   2662 O O   . ARG A 1 363 ? 42.327  -5.055  -2.280  1.00 113.75 ? 549 ARG B O   1 
ATOM   2663 C CB  . ARG A 1 363 ? 41.837  -5.089  0.975   1.00 106.94 ? 549 ARG B CB  1 
ATOM   2664 C CG  . ARG A 1 363 ? 42.105  -4.300  2.243   1.00 106.70 ? 549 ARG B CG  1 
ATOM   2665 C CD  . ARG A 1 363 ? 42.821  -5.167  3.275   1.00 109.82 ? 549 ARG B CD  1 
ATOM   2666 N NE  . ARG A 1 363 ? 42.754  -4.602  4.616   1.00 109.73 ? 549 ARG B NE  1 
ATOM   2667 C CZ  . ARG A 1 363 ? 41.883  -4.975  5.544   1.00 109.60 ? 549 ARG B CZ  1 
ATOM   2668 N NH1 . ARG A 1 363 ? 41.010  -5.944  5.322   1.00 109.58 ? 549 ARG B NH1 1 
ATOM   2669 N NH2 . ARG A 1 363 ? 41.883  -4.358  6.722   1.00 121.73 ? 549 ARG B NH2 1 
ATOM   2670 N N   . ILE A 1 364 ? 40.358  -5.963  -1.673  1.00 105.41 ? 550 ILE B N   1 
ATOM   2671 C CA  . ILE A 1 364 ? 40.327  -6.857  -2.828  1.00 106.84 ? 550 ILE B CA  1 
ATOM   2672 C C   . ILE A 1 364 ? 40.232  -6.068  -4.129  1.00 109.10 ? 550 ILE B C   1 
ATOM   2673 O O   . ILE A 1 364 ? 40.860  -6.427  -5.133  1.00 115.92 ? 550 ILE B O   1 
ATOM   2674 C CB  . ILE A 1 364 ? 39.169  -7.863  -2.689  1.00 113.02 ? 550 ILE B CB  1 
ATOM   2675 C CG1 . ILE A 1 364 ? 39.307  -8.643  -1.379  1.00 110.70 ? 550 ILE B CG1 1 
ATOM   2676 C CG2 . ILE A 1 364 ? 39.140  -8.814  -3.877  1.00 108.73 ? 550 ILE B CG2 1 
ATOM   2677 C CD1 . ILE A 1 364 ? 38.148  -9.572  -1.090  1.00 108.80 ? 550 ILE B CD1 1 
ATOM   2678 N N   . GLU A 1 365 ? 39.459  -4.977  -4.137  1.00 102.45 ? 551 GLU B N   1 
ATOM   2679 C CA  . GLU A 1 365 ? 39.368  -4.166  -5.350  1.00 102.01 ? 551 GLU B CA  1 
ATOM   2680 C C   . GLU A 1 365 ? 40.670  -3.434  -5.655  1.00 113.59 ? 551 GLU B C   1 
ATOM   2681 O O   . GLU A 1 365 ? 41.028  -3.276  -6.828  1.00 110.58 ? 551 GLU B O   1 
ATOM   2682 C CB  . GLU A 1 365 ? 38.217  -3.167  -5.245  1.00 98.08  ? 551 GLU B CB  1 
ATOM   2683 C CG  . GLU A 1 365 ? 36.847  -3.811  -5.279  1.00 109.72 ? 551 GLU B CG  1 
ATOM   2684 C CD  . GLU A 1 365 ? 35.730  -2.802  -5.137  1.00 121.21 ? 551 GLU B CD  1 
ATOM   2685 O OE1 . GLU A 1 365 ? 36.026  -1.633  -4.811  1.00 122.86 ? 551 GLU B OE1 1 
ATOM   2686 O OE2 . GLU A 1 365 ? 34.558  -3.175  -5.359  1.00 127.01 ? 551 GLU B OE2 1 
ATOM   2687 N N   . ALA A 1 366 ? 41.402  -2.999  -4.627  1.00 113.44 ? 552 ALA B N   1 
ATOM   2688 C CA  . ALA A 1 366 ? 42.623  -2.233  -4.855  1.00 107.09 ? 552 ALA B CA  1 
ATOM   2689 C C   . ALA A 1 366 ? 43.726  -3.061  -5.496  1.00 106.36 ? 552 ALA B C   1 
ATOM   2690 O O   . ALA A 1 366 ? 44.736  -2.490  -5.920  1.00 107.34 ? 552 ALA B O   1 
ATOM   2691 C CB  . ALA A 1 366 ? 43.124  -1.628  -3.543  1.00 103.07 ? 552 ALA B CB  1 
ATOM   2692 N N   . GLN A 1 367 ? 43.566  -4.379  -5.555  1.00 108.15 ? 553 GLN B N   1 
ATOM   2693 C CA  . GLN A 1 367 ? 44.574  -5.269  -6.118  1.00 112.49 ? 553 GLN B CA  1 
ATOM   2694 C C   . GLN A 1 367 ? 44.197  -5.722  -7.528  1.00 112.09 ? 553 GLN B C   1 
ATOM   2695 O O   . GLN A 1 367 ? 43.324  -6.575  -7.702  1.00 112.20 ? 553 GLN B O   1 
ATOM   2696 C CB  . GLN A 1 367 ? 44.759  -6.479  -5.204  1.00 121.94 ? 553 GLN B CB  1 
ATOM   2697 C CG  . GLN A 1 367 ? 45.045  -6.106  -3.751  1.00 114.94 ? 553 GLN B CG  1 
ATOM   2698 C CD  . GLN A 1 367 ? 44.800  -7.257  -2.793  1.00 116.09 ? 553 GLN B CD  1 
ATOM   2699 O OE1 . GLN A 1 367 ? 44.843  -8.426  -3.182  1.00 122.83 ? 553 GLN B OE1 1 
ATOM   2700 N NE2 . GLN A 1 367 ? 44.517  -6.929  -1.535  1.00 113.88 ? 553 GLN B NE2 1 
ATOM   2701 N N   . LYS B 1 23  ? 0.265   13.655  37.525  1.00 73.79  ? 209 LYS A N   1 
ATOM   2702 C CA  . LYS B 1 23  ? -0.105  14.719  36.594  1.00 102.37 ? 209 LYS A CA  1 
ATOM   2703 C C   . LYS B 1 23  ? 0.308   16.083  37.126  1.00 116.00 ? 209 LYS A C   1 
ATOM   2704 O O   . LYS B 1 23  ? 1.055   16.166  38.106  1.00 122.85 ? 209 LYS A O   1 
ATOM   2705 C CB  . LYS B 1 23  ? -1.613  14.712  36.321  1.00 107.49 ? 209 LYS A CB  1 
ATOM   2706 C CG  . LYS B 1 23  ? -2.482  14.989  37.548  1.00 104.53 ? 209 LYS A CG  1 
ATOM   2707 C CD  . LYS B 1 23  ? -3.951  15.129  37.174  1.00 99.20  ? 209 LYS A CD  1 
ATOM   2708 C CE  . LYS B 1 23  ? -4.792  15.471  38.390  1.00 100.27 ? 209 LYS A CE  1 
ATOM   2709 N NZ  . LYS B 1 23  ? -4.365  16.756  39.012  1.00 89.48  ? 209 LYS A NZ  1 
ATOM   2710 N N   . HIS B 1 24  ? -0.173  17.130  36.446  1.00 130.66 ? 210 HIS A N   1 
ATOM   2711 C CA  . HIS B 1 24  ? 0.124   18.542  36.676  1.00 130.11 ? 210 HIS A CA  1 
ATOM   2712 C C   . HIS B 1 24  ? 1.541   18.895  36.235  1.00 145.06 ? 210 HIS A C   1 
ATOM   2713 O O   . HIS B 1 24  ? 1.877   20.072  36.058  1.00 140.17 ? 210 HIS A O   1 
ATOM   2714 C CB  . HIS B 1 24  ? -0.053  18.903  38.161  1.00 131.50 ? 210 HIS A CB  1 
ATOM   2715 C CG  . HIS B 1 24  ? 1.198   19.420  38.806  1.00 143.83 ? 210 HIS A CG  1 
ATOM   2716 N ND1 . HIS B 1 24  ? 1.567   20.748  38.756  1.00 147.32 ? 210 HIS A ND1 1 
ATOM   2717 C CD2 . HIS B 1 24  ? 2.181   18.783  39.487  1.00 141.40 ? 210 HIS A CD2 1 
ATOM   2718 C CE1 . HIS B 1 24  ? 2.714   20.908  39.393  1.00 144.55 ? 210 HIS A CE1 1 
ATOM   2719 N NE2 . HIS B 1 24  ? 3.108   19.732  39.845  1.00 137.66 ? 210 HIS A NE2 1 
ATOM   2720 N N   . THR B 1 25  ? 2.365   17.874  36.007  1.00 120.73 ? 211 THR A N   1 
ATOM   2721 C CA  . THR B 1 25  ? 3.708   18.067  35.490  1.00 105.19 ? 211 THR A CA  1 
ATOM   2722 C C   . THR B 1 25  ? 4.079   17.026  34.448  1.00 89.78  ? 211 THR A C   1 
ATOM   2723 O O   . THR B 1 25  ? 5.182   17.093  33.898  1.00 84.35  ? 211 THR A O   1 
ATOM   2724 C CB  . THR B 1 25  ? 4.726   18.034  36.640  1.00 97.67  ? 211 THR A CB  1 
ATOM   2725 O OG1 . THR B 1 25  ? 6.052   18.125  36.112  1.00 90.67  ? 211 THR A OG1 1 
ATOM   2726 C CG2 . THR B 1 25  ? 4.588   16.748  37.430  1.00 92.46  ? 211 THR A CG2 1 
ATOM   2727 N N   . GLY B 1 26  ? 3.195   16.078  34.149  1.00 87.61  ? 212 GLY A N   1 
ATOM   2728 C CA  . GLY B 1 26  ? 3.534   14.984  33.273  1.00 83.32  ? 212 GLY A CA  1 
ATOM   2729 C C   . GLY B 1 26  ? 4.318   13.875  33.934  1.00 83.90  ? 212 GLY A C   1 
ATOM   2730 O O   . GLY B 1 26  ? 4.561   12.846  33.292  1.00 92.45  ? 212 GLY A O   1 
ATOM   2731 N N   . TYR B 1 27  ? 4.727   14.047  35.192  1.00 79.44  ? 213 TYR A N   1 
ATOM   2732 C CA  . TYR B 1 27  ? 5.538   13.064  35.898  1.00 75.61  ? 213 TYR A CA  1 
ATOM   2733 C C   . TYR B 1 27  ? 4.909   12.760  37.251  1.00 68.53  ? 213 TYR A C   1 
ATOM   2734 O O   . TYR B 1 27  ? 4.554   13.679  37.997  1.00 67.63  ? 213 TYR A O   1 
ATOM   2735 C CB  . TYR B 1 27  ? 6.978   13.567  36.088  1.00 78.77  ? 213 TYR A CB  1 
ATOM   2736 C CG  . TYR B 1 27  ? 7.630   14.095  34.824  1.00 69.22  ? 213 TYR A CG  1 
ATOM   2737 C CD1 . TYR B 1 27  ? 7.697   13.319  33.674  1.00 67.27  ? 213 TYR A CD1 1 
ATOM   2738 C CD2 . TYR B 1 27  ? 8.179   15.372  34.784  1.00 67.80  ? 213 TYR A CD2 1 
ATOM   2739 C CE1 . TYR B 1 27  ? 8.296   13.799  32.519  1.00 64.38  ? 213 TYR A CE1 1 
ATOM   2740 C CE2 . TYR B 1 27  ? 8.773   15.863  33.634  1.00 64.53  ? 213 TYR A CE2 1 
ATOM   2741 C CZ  . TYR B 1 27  ? 8.830   15.072  32.505  1.00 63.87  ? 213 TYR A CZ  1 
ATOM   2742 O OH  . TYR B 1 27  ? 9.418   15.555  31.359  1.00 63.91  ? 213 TYR A OH  1 
ATOM   2743 N N   . VAL B 1 28  ? 4.771   11.476  37.564  1.00 67.33  ? 214 VAL A N   1 
ATOM   2744 C CA  . VAL B 1 28  ? 4.185   11.038  38.819  1.00 67.94  ? 214 VAL A CA  1 
ATOM   2745 C C   . VAL B 1 28  ? 5.309   10.631  39.761  1.00 66.40  ? 214 VAL A C   1 
ATOM   2746 O O   . VAL B 1 28  ? 6.430   10.329  39.342  1.00 69.94  ? 214 VAL A O   1 
ATOM   2747 C CB  . VAL B 1 28  ? 3.186   9.879   38.619  1.00 75.28  ? 214 VAL A CB  1 
ATOM   2748 C CG1 . VAL B 1 28  ? 3.925   8.552   38.511  1.00 71.18  ? 214 VAL A CG1 1 
ATOM   2749 C CG2 . VAL B 1 28  ? 2.154   9.862   39.740  1.00 70.66  ? 214 VAL A CG2 1 
ATOM   2750 N N   . GLY B 1 29  ? 5.005   10.618  41.060  1.00 70.91  ? 215 GLY A N   1 
ATOM   2751 C CA  . GLY B 1 29  ? 5.994   10.360  42.080  1.00 69.22  ? 215 GLY A CA  1 
ATOM   2752 C C   . GLY B 1 29  ? 6.007   8.922   42.585  1.00 69.12  ? 215 GLY A C   1 
ATOM   2753 O O   . GLY B 1 29  ? 5.233   8.063   42.167  1.00 64.41  ? 215 GLY A O   1 
ATOM   2754 N N   . LEU B 1 30  ? 6.926   8.685   43.521  1.00 67.93  ? 216 LEU A N   1 
ATOM   2755 C CA  . LEU B 1 30  ? 7.093   7.407   44.197  1.00 65.55  ? 216 LEU A CA  1 
ATOM   2756 C C   . LEU B 1 30  ? 6.724   7.571   45.662  1.00 72.48  ? 216 LEU A C   1 
ATOM   2757 O O   . LEU B 1 30  ? 7.065   8.579   46.287  1.00 75.19  ? 216 LEU A O   1 
ATOM   2758 C CB  . LEU B 1 30  ? 8.528   6.896   44.088  1.00 61.45  ? 216 LEU A CB  1 
ATOM   2759 C CG  . LEU B 1 30  ? 8.995   6.422   42.720  1.00 62.08  ? 216 LEU A CG  1 
ATOM   2760 C CD1 . LEU B 1 30  ? 10.498  6.261   42.718  1.00 67.39  ? 216 LEU A CD1 1 
ATOM   2761 C CD2 . LEU B 1 30  ? 8.327   5.111   42.385  1.00 62.08  ? 216 LEU A CD2 1 
ATOM   2762 N N   . LYS B 1 31  ? 6.017   6.589   46.203  1.00 73.43  ? 217 LYS A N   1 
ATOM   2763 C CA  . LYS B 1 31  ? 5.548   6.698   47.575  1.00 75.71  ? 217 LYS A CA  1 
ATOM   2764 C C   . LYS B 1 31  ? 6.692   6.483   48.570  1.00 73.17  ? 217 LYS A C   1 
ATOM   2765 O O   . LYS B 1 31  ? 7.602   5.679   48.344  1.00 72.22  ? 217 LYS A O   1 
ATOM   2766 C CB  . LYS B 1 31  ? 4.414   5.691   47.812  1.00 70.67  ? 217 LYS A CB  1 
ATOM   2767 C CG  . LYS B 1 31  ? 3.148   6.277   48.442  1.00 84.62  ? 217 LYS A CG  1 
ATOM   2768 C CD  . LYS B 1 31  ? 3.515   7.026   49.701  1.00 91.68  ? 217 LYS A CD  1 
ATOM   2769 C CE  . LYS B 1 31  ? 2.326   7.706   50.332  1.00 92.22  ? 217 LYS A CE  1 
ATOM   2770 N NZ  . LYS B 1 31  ? 2.773   8.542   51.484  1.00 90.48  ? 217 LYS A NZ  1 
ATOM   2771 N N   . ASN B 1 32  ? 6.641   7.222   49.677  1.00 77.74  ? 218 ASN A N   1 
ATOM   2772 C CA  . ASN B 1 32  ? 7.536   7.015   50.811  1.00 76.17  ? 218 ASN A CA  1 
ATOM   2773 C C   . ASN B 1 32  ? 7.043   5.793   51.579  1.00 78.29  ? 218 ASN A C   1 
ATOM   2774 O O   . ASN B 1 32  ? 5.980   5.830   52.211  1.00 80.98  ? 218 ASN A O   1 
ATOM   2775 C CB  . ASN B 1 32  ? 7.575   8.258   51.698  1.00 82.18  ? 218 ASN A CB  1 
ATOM   2776 C CG  . ASN B 1 32  ? 8.672   8.199   52.753  1.00 88.76  ? 218 ASN A CG  1 
ATOM   2777 O OD1 . ASN B 1 32  ? 9.126   7.123   53.136  1.00 89.04  ? 218 ASN A OD1 1 
ATOM   2778 N ND2 . ASN B 1 32  ? 9.099   9.367   53.232  1.00 90.39  ? 218 ASN A ND2 1 
ATOM   2779 N N   . GLN B 1 33  ? 7.812   4.706   51.525  1.00 81.32  ? 219 GLN A N   1 
ATOM   2780 C CA  . GLN B 1 33  ? 7.430   3.435   52.137  1.00 83.35  ? 219 GLN A CA  1 
ATOM   2781 C C   . GLN B 1 33  ? 8.537   2.966   53.083  1.00 78.41  ? 219 GLN A C   1 
ATOM   2782 O O   . GLN B 1 33  ? 9.079   1.868   52.957  1.00 84.68  ? 219 GLN A O   1 
ATOM   2783 C CB  . GLN B 1 33  ? 7.119   2.385   51.069  1.00 83.37  ? 219 GLN A CB  1 
ATOM   2784 C CG  . GLN B 1 33  ? 5.866   2.675   50.245  1.00 84.79  ? 219 GLN A CG  1 
ATOM   2785 C CD  . GLN B 1 33  ? 5.547   1.565   49.258  1.00 80.82  ? 219 GLN A CD  1 
ATOM   2786 O OE1 . GLN B 1 33  ? 6.429   0.808   48.863  1.00 84.11  ? 219 GLN A OE1 1 
ATOM   2787 N NE2 . GLN B 1 33  ? 4.279   1.449   48.874  1.00 81.13  ? 219 GLN A NE2 1 
ATOM   2788 N N   . GLY B 1 34  ? 8.847   3.804   54.068  1.00 77.35  ? 220 GLY A N   1 
ATOM   2789 C CA  . GLY B 1 34  ? 9.881   3.490   55.032  1.00 78.95  ? 220 GLY A CA  1 
ATOM   2790 C C   . GLY B 1 34  ? 11.208  4.118   54.663  1.00 72.85  ? 220 GLY A C   1 
ATOM   2791 O O   . GLY B 1 34  ? 11.328  4.912   53.725  1.00 67.98  ? 220 GLY A O   1 
ATOM   2792 N N   . ALA B 1 35  ? 12.230  3.727   55.423  1.00 70.79  ? 221 ALA A N   1 
ATOM   2793 C CA  . ALA B 1 35  ? 13.569  4.277   55.260  1.00 71.10  ? 221 ALA A CA  1 
ATOM   2794 C C   . ALA B 1 35  ? 14.215  3.712   54.004  1.00 66.92  ? 221 ALA A C   1 
ATOM   2795 O O   . ALA B 1 35  ? 15.171  2.935   54.071  1.00 68.44  ? 221 ALA A O   1 
ATOM   2796 C CB  . ALA B 1 35  ? 14.428  3.970   56.487  1.00 74.49  ? 221 ALA A CB  1 
ATOM   2797 N N   . THR B 1 36  ? 13.672  4.099   52.854  1.00 68.71  ? 222 THR A N   1 
ATOM   2798 C CA  . THR B 1 36  ? 14.189  3.700   51.558  1.00 59.95  ? 222 THR A CA  1 
ATOM   2799 C C   . THR B 1 36  ? 15.371  4.552   51.120  1.00 65.63  ? 222 THR A C   1 
ATOM   2800 O O   . THR B 1 36  ? 16.061  4.187   50.160  1.00 70.65  ? 222 THR A O   1 
ATOM   2801 C CB  . THR B 1 36  ? 13.071  3.784   50.516  1.00 69.15  ? 222 THR A CB  1 
ATOM   2802 O OG1 . THR B 1 36  ? 13.302  2.819   49.485  1.00 77.62  ? 222 THR A OG1 1 
ATOM   2803 C CG2 . THR B 1 36  ? 13.014  5.185   49.895  1.00 62.74  ? 222 THR A CG2 1 
ATOM   2804 N N   . CYS B 1 37  ? 15.610  5.670   51.800  1.00 63.01  ? 223 CYS A N   1 
ATOM   2805 C CA  . CYS B 1 37  ? 16.763  6.548   51.570  1.00 63.76  ? 223 CYS A CA  1 
ATOM   2806 C C   . CYS B 1 37  ? 16.794  6.979   50.106  1.00 65.74  ? 223 CYS A C   1 
ATOM   2807 O O   . CYS B 1 37  ? 15.800  7.531   49.605  1.00 71.01  ? 223 CYS A O   1 
ATOM   2808 C CB  . CYS B 1 37  ? 18.023  5.839   52.058  1.00 64.83  ? 223 CYS A CB  1 
ATOM   2809 S SG  . CYS B 1 37  ? 18.290  5.833   53.839  1.00 74.98  ? 223 CYS A SG  1 
ATOM   2810 N N   . TYR B 1 38  ? 17.894  6.754   49.393  1.00 69.84  ? 224 TYR A N   1 
ATOM   2811 C CA  . TYR B 1 38  ? 18.113  7.205   48.027  1.00 66.45  ? 224 TYR A CA  1 
ATOM   2812 C C   . TYR B 1 38  ? 17.285  6.458   46.995  1.00 64.42  ? 224 TYR A C   1 
ATOM   2813 O O   . TYR B 1 38  ? 17.274  6.871   45.831  1.00 67.57  ? 224 TYR A O   1 
ATOM   2814 C CB  . TYR B 1 38  ? 19.594  7.047   47.705  1.00 57.62  ? 224 TYR A CB  1 
ATOM   2815 C CG  . TYR B 1 38  ? 20.153  5.763   48.273  1.00 61.79  ? 224 TYR A CG  1 
ATOM   2816 C CD1 . TYR B 1 38  ? 19.959  4.552   47.621  1.00 65.59  ? 224 TYR A CD1 1 
ATOM   2817 C CD2 . TYR B 1 38  ? 20.851  5.754   49.476  1.00 58.54  ? 224 TYR A CD2 1 
ATOM   2818 C CE1 . TYR B 1 38  ? 20.455  3.371   48.143  1.00 64.25  ? 224 TYR A CE1 1 
ATOM   2819 C CE2 . TYR B 1 38  ? 21.349  4.576   50.007  1.00 59.57  ? 224 TYR A CE2 1 
ATOM   2820 C CZ  . TYR B 1 38  ? 21.146  3.388   49.334  1.00 63.14  ? 224 TYR A CZ  1 
ATOM   2821 O OH  . TYR B 1 38  ? 21.635  2.207   49.845  1.00 66.56  ? 224 TYR A OH  1 
ATOM   2822 N N   . MET B 1 39  ? 16.596  5.383   47.384  1.00 63.48  ? 225 MET A N   1 
ATOM   2823 C CA  . MET B 1 39  ? 15.992  4.501   46.391  1.00 64.38  ? 225 MET A CA  1 
ATOM   2824 C C   . MET B 1 39  ? 15.018  5.246   45.485  1.00 66.12  ? 225 MET A C   1 
ATOM   2825 O O   . MET B 1 39  ? 15.052  5.076   44.261  1.00 64.34  ? 225 MET A O   1 
ATOM   2826 C CB  . MET B 1 39  ? 15.294  3.333   47.081  1.00 60.97  ? 225 MET A CB  1 
ATOM   2827 C CG  . MET B 1 39  ? 14.588  2.408   46.117  1.00 63.14  ? 225 MET A CG  1 
ATOM   2828 S SD  . MET B 1 39  ? 13.822  1.016   46.944  1.00 67.34  ? 225 MET A SD  1 
ATOM   2829 C CE  . MET B 1 39  ? 13.090  0.171   45.554  1.00 76.75  ? 225 MET A CE  1 
ATOM   2830 N N   . ASN B 1 40  ? 14.157  6.091   46.054  1.00 63.58  ? 226 ASN A N   1 
ATOM   2831 C CA  . ASN B 1 40  ? 13.233  6.837   45.208  1.00 63.79  ? 226 ASN A CA  1 
ATOM   2832 C C   . ASN B 1 40  ? 13.983  7.741   44.240  1.00 59.64  ? 226 ASN A C   1 
ATOM   2833 O O   . ASN B 1 40  ? 13.657  7.793   43.048  1.00 60.35  ? 226 ASN A O   1 
ATOM   2834 C CB  . ASN B 1 40  ? 12.268  7.658   46.062  1.00 66.98  ? 226 ASN A CB  1 
ATOM   2835 C CG  . ASN B 1 40  ? 11.297  6.797   46.826  1.00 64.48  ? 226 ASN A CG  1 
ATOM   2836 O OD1 . ASN B 1 40  ? 11.006  5.665   46.431  1.00 59.59  ? 226 ASN A OD1 1 
ATOM   2837 N ND2 . ASN B 1 40  ? 10.787  7.325   47.931  1.00 76.07  ? 226 ASN A ND2 1 
ATOM   2838 N N   . SER B 1 41  ? 15.007  8.446   44.727  1.00 63.23  ? 227 SER A N   1 
ATOM   2839 C CA  . SER B 1 41  ? 15.764  9.335   43.852  1.00 64.70  ? 227 SER A CA  1 
ATOM   2840 C C   . SER B 1 41  ? 16.451  8.557   42.738  1.00 60.16  ? 227 SER A C   1 
ATOM   2841 O O   . SER B 1 41  ? 16.429  8.975   41.575  1.00 57.52  ? 227 SER A O   1 
ATOM   2842 C CB  . SER B 1 41  ? 16.788  10.131  44.662  1.00 65.41  ? 227 SER A CB  1 
ATOM   2843 O OG  . SER B 1 41  ? 16.151  10.999  45.584  1.00 66.96  ? 227 SER A OG  1 
ATOM   2844 N N   . LEU B 1 42  ? 17.058  7.418   43.075  1.00 56.33  ? 228 LEU A N   1 
ATOM   2845 C CA  . LEU B 1 42  ? 17.729  6.620   42.056  1.00 56.81  ? 228 LEU A CA  1 
ATOM   2846 C C   . LEU B 1 42  ? 16.730  6.070   41.047  1.00 59.29  ? 228 LEU A C   1 
ATOM   2847 O O   . LEU B 1 42  ? 17.011  6.034   39.843  1.00 60.13  ? 228 LEU A O   1 
ATOM   2848 C CB  . LEU B 1 42  ? 18.518  5.485   42.707  1.00 53.76  ? 228 LEU A CB  1 
ATOM   2849 C CG  . LEU B 1 42  ? 19.349  4.619   41.757  1.00 53.13  ? 228 LEU A CG  1 
ATOM   2850 C CD1 . LEU B 1 42  ? 20.423  5.459   41.096  1.00 52.71  ? 228 LEU A CD1 1 
ATOM   2851 C CD2 . LEU B 1 42  ? 19.963  3.435   42.486  1.00 52.60  ? 228 LEU A CD2 1 
ATOM   2852 N N   . LEU B 1 43  ? 15.556  5.642   41.517  1.00 62.09  ? 229 LEU A N   1 
ATOM   2853 C CA  . LEU B 1 43  ? 14.573  5.049   40.617  1.00 57.46  ? 229 LEU A CA  1 
ATOM   2854 C C   . LEU B 1 43  ? 14.095  6.051   39.574  1.00 59.63  ? 229 LEU A C   1 
ATOM   2855 O O   . LEU B 1 43  ? 13.949  5.709   38.396  1.00 67.18  ? 229 LEU A O   1 
ATOM   2856 C CB  . LEU B 1 43  ? 13.396  4.493   41.416  1.00 57.79  ? 229 LEU A CB  1 
ATOM   2857 C CG  . LEU B 1 43  ? 13.657  3.161   42.120  1.00 56.68  ? 229 LEU A CG  1 
ATOM   2858 C CD1 . LEU B 1 43  ? 12.495  2.800   43.025  1.00 60.02  ? 229 LEU A CD1 1 
ATOM   2859 C CD2 . LEU B 1 43  ? 13.894  2.070   41.094  1.00 56.51  ? 229 LEU A CD2 1 
ATOM   2860 N N   . GLN B 1 44  ? 13.849  7.295   39.983  1.00 58.34  ? 230 GLN A N   1 
ATOM   2861 C CA  . GLN B 1 44  ? 13.454  8.307   39.010  1.00 57.93  ? 230 GLN A CA  1 
ATOM   2862 C C   . GLN B 1 44  ? 14.594  8.623   38.050  1.00 64.11  ? 230 GLN A C   1 
ATOM   2863 O O   . GLN B 1 44  ? 14.362  8.861   36.859  1.00 69.10  ? 230 GLN A O   1 
ATOM   2864 C CB  . GLN B 1 44  ? 12.986  9.570   39.723  1.00 63.22  ? 230 GLN A CB  1 
ATOM   2865 C CG  . GLN B 1 44  ? 11.782  10.210  39.060  1.00 75.69  ? 230 GLN A CG  1 
ATOM   2866 C CD  . GLN B 1 44  ? 10.463  9.630   39.539  1.00 68.11  ? 230 GLN A CD  1 
ATOM   2867 O OE1 . GLN B 1 44  ? 9.590   9.295   38.737  1.00 71.31  ? 230 GLN A OE1 1 
ATOM   2868 N NE2 . GLN B 1 44  ? 10.309  9.519   40.855  1.00 67.28  ? 230 GLN A NE2 1 
ATOM   2869 N N   . THR B 1 45  ? 15.832  8.630   38.553  1.00 70.34  ? 231 THR A N   1 
ATOM   2870 C CA  . THR B 1 45  ? 16.992  8.891   37.704  1.00 63.41  ? 231 THR A CA  1 
ATOM   2871 C C   . THR B 1 45  ? 17.128  7.836   36.614  1.00 62.23  ? 231 THR A C   1 
ATOM   2872 O O   . THR B 1 45  ? 17.349  8.157   35.441  1.00 60.73  ? 231 THR A O   1 
ATOM   2873 C CB  . THR B 1 45  ? 18.264  8.925   38.553  1.00 58.41  ? 231 THR A CB  1 
ATOM   2874 O OG1 . THR B 1 45  ? 18.180  9.983   39.516  1.00 63.63  ? 231 THR A OG1 1 
ATOM   2875 C CG2 . THR B 1 45  ? 19.481  9.134   37.671  1.00 61.33  ? 231 THR A CG2 1 
ATOM   2876 N N   . LEU B 1 46  ? 17.005  6.562   36.991  1.00 64.29  ? 232 LEU A N   1 
ATOM   2877 C CA  . LEU B 1 46  ? 17.085  5.481   36.016  1.00 65.79  ? 232 LEU A CA  1 
ATOM   2878 C C   . LEU B 1 46  ? 15.859  5.440   35.111  1.00 74.04  ? 232 LEU A C   1 
ATOM   2879 O O   . LEU B 1 46  ? 15.975  5.078   33.934  1.00 75.15  ? 232 LEU A O   1 
ATOM   2880 C CB  . LEU B 1 46  ? 17.265  4.148   36.743  1.00 62.04  ? 232 LEU A CB  1 
ATOM   2881 C CG  . LEU B 1 46  ? 18.532  4.032   37.593  1.00 61.10  ? 232 LEU A CG  1 
ATOM   2882 C CD1 . LEU B 1 46  ? 18.502  2.782   38.454  1.00 53.85  ? 232 LEU A CD1 1 
ATOM   2883 C CD2 . LEU B 1 46  ? 19.766  4.036   36.701  1.00 63.10  ? 232 LEU A CD2 1 
ATOM   2884 N N   . PHE B 1 47  ? 14.688  5.817   35.633  1.00 70.08  ? 233 PHE A N   1 
ATOM   2885 C CA  . PHE B 1 47  ? 13.468  5.799   34.831  1.00 68.88  ? 233 PHE A CA  1 
ATOM   2886 C C   . PHE B 1 47  ? 13.587  6.722   33.626  1.00 70.06  ? 233 PHE A C   1 
ATOM   2887 O O   . PHE B 1 47  ? 13.150  6.374   32.522  1.00 72.65  ? 233 PHE A O   1 
ATOM   2888 C CB  . PHE B 1 47  ? 12.269  6.193   35.698  1.00 71.65  ? 233 PHE A CB  1 
ATOM   2889 C CG  . PHE B 1 47  ? 10.993  6.411   34.927  1.00 68.57  ? 233 PHE A CG  1 
ATOM   2890 C CD1 . PHE B 1 47  ? 10.181  5.343   34.584  1.00 66.34  ? 233 PHE A CD1 1 
ATOM   2891 C CD2 . PHE B 1 47  ? 10.596  7.689   34.570  1.00 66.20  ? 233 PHE A CD2 1 
ATOM   2892 C CE1 . PHE B 1 47  ? 9.005   5.548   33.885  1.00 65.39  ? 233 PHE A CE1 1 
ATOM   2893 C CE2 . PHE B 1 47  ? 9.424   7.896   33.871  1.00 66.49  ? 233 PHE A CE2 1 
ATOM   2894 C CZ  . PHE B 1 47  ? 8.627   6.824   33.530  1.00 63.49  ? 233 PHE A CZ  1 
ATOM   2895 N N   . PHE B 1 48  ? 14.173  7.902   33.818  1.00 64.33  ? 234 PHE A N   1 
ATOM   2896 C CA  . PHE B 1 48  ? 14.358  8.867   32.745  1.00 66.51  ? 234 PHE A CA  1 
ATOM   2897 C C   . PHE B 1 48  ? 15.651  8.651   31.967  1.00 67.60  ? 234 PHE A C   1 
ATOM   2898 O O   . PHE B 1 48  ? 15.991  9.476   31.113  1.00 64.21  ? 234 PHE A O   1 
ATOM   2899 C CB  . PHE B 1 48  ? 14.296  10.285  33.305  1.00 66.32  ? 234 PHE A CB  1 
ATOM   2900 C CG  . PHE B 1 48  ? 12.931  10.673  33.778  1.00 68.74  ? 234 PHE A CG  1 
ATOM   2901 C CD1 . PHE B 1 48  ? 11.880  10.768  32.882  1.00 67.20  ? 234 PHE A CD1 1 
ATOM   2902 C CD2 . PHE B 1 48  ? 12.690  10.929  35.113  1.00 70.32  ? 234 PHE A CD2 1 
ATOM   2903 C CE1 . PHE B 1 48  ? 10.618  11.123  33.305  1.00 61.28  ? 234 PHE A CE1 1 
ATOM   2904 C CE2 . PHE B 1 48  ? 11.423  11.282  35.544  1.00 71.33  ? 234 PHE A CE2 1 
ATOM   2905 C CZ  . PHE B 1 48  ? 10.389  11.379  34.637  1.00 61.17  ? 234 PHE A CZ  1 
ATOM   2906 N N   . THR B 1 49  ? 16.392  7.583   32.266  1.00 67.53  ? 235 THR A N   1 
ATOM   2907 C CA  . THR B 1 49  ? 17.371  7.036   31.329  1.00 67.00  ? 235 THR A CA  1 
ATOM   2908 C C   . THR B 1 49  ? 16.585  6.224   30.302  1.00 72.93  ? 235 THR A C   1 
ATOM   2909 O O   . THR B 1 49  ? 16.515  4.993   30.348  1.00 70.74  ? 235 THR A O   1 
ATOM   2910 C CB  . THR B 1 49  ? 18.409  6.186   32.044  1.00 59.44  ? 235 THR A CB  1 
ATOM   2911 O OG1 . THR B 1 49  ? 18.949  6.928   33.141  1.00 72.06  ? 235 THR A OG1 1 
ATOM   2912 C CG2 . THR B 1 49  ? 19.531  5.839   31.088  1.00 61.50  ? 235 THR A CG2 1 
ATOM   2913 N N   . ASN B 1 50  ? 15.980  6.951   29.357  1.00 70.60  ? 236 ASN A N   1 
ATOM   2914 C CA  . ASN B 1 50  ? 14.907  6.400   28.532  1.00 71.15  ? 236 ASN A CA  1 
ATOM   2915 C C   . ASN B 1 50  ? 15.348  5.163   27.754  1.00 68.67  ? 236 ASN A C   1 
ATOM   2916 O O   . ASN B 1 50  ? 14.578  4.204   27.618  1.00 68.62  ? 236 ASN A O   1 
ATOM   2917 C CB  . ASN B 1 50  ? 14.388  7.479   27.587  1.00 70.41  ? 236 ASN A CB  1 
ATOM   2918 C CG  . ASN B 1 50  ? 13.609  8.559   28.312  1.00 67.09  ? 236 ASN A CG  1 
ATOM   2919 O OD1 . ASN B 1 50  ? 14.136  9.255   29.178  1.00 62.68  ? 236 ASN A OD1 1 
ATOM   2920 N ND2 . ASN B 1 50  ? 12.343  8.709   27.950  1.00 75.67  ? 236 ASN A ND2 1 
ATOM   2921 N N   . GLN B 1 51  ? 16.568  5.170   27.213  1.00 62.74  ? 237 GLN A N   1 
ATOM   2922 C CA  . GLN B 1 51  ? 17.054  3.989   26.503  1.00 70.32  ? 237 GLN A CA  1 
ATOM   2923 C C   . GLN B 1 51  ? 17.167  2.791   27.438  1.00 72.14  ? 237 GLN A C   1 
ATOM   2924 O O   . GLN B 1 51  ? 16.857  1.658   27.050  1.00 68.32  ? 237 GLN A O   1 
ATOM   2925 C CB  . GLN B 1 51  ? 18.401  4.282   25.845  1.00 68.21  ? 237 GLN A CB  1 
ATOM   2926 C CG  . GLN B 1 51  ? 18.899  3.148   24.965  1.00 71.81  ? 237 GLN A CG  1 
ATOM   2927 C CD  . GLN B 1 51  ? 20.046  3.561   24.069  1.00 71.74  ? 237 GLN A CD  1 
ATOM   2928 O OE1 . GLN B 1 51  ? 20.561  4.673   24.176  1.00 79.00  ? 237 GLN A OE1 1 
ATOM   2929 N NE2 . GLN B 1 51  ? 20.453  2.665   23.177  1.00 74.31  ? 237 GLN A NE2 1 
ATOM   2930 N N   . LEU B 1 52  ? 17.620  3.025   28.673  1.00 72.23  ? 238 LEU A N   1 
ATOM   2931 C CA  . LEU B 1 52  ? 17.625  1.973   29.683  1.00 66.89  ? 238 LEU A CA  1 
ATOM   2932 C C   . LEU B 1 52  ? 16.210  1.488   29.970  1.00 71.91  ? 238 LEU A C   1 
ATOM   2933 O O   . LEU B 1 52  ? 15.980  0.289   30.172  1.00 71.64  ? 238 LEU A O   1 
ATOM   2934 C CB  . LEU B 1 52  ? 18.280  2.492   30.961  1.00 60.01  ? 238 LEU A CB  1 
ATOM   2935 C CG  . LEU B 1 52  ? 18.077  1.681   32.237  1.00 62.89  ? 238 LEU A CG  1 
ATOM   2936 C CD1 . LEU B 1 52  ? 18.726  0.308   32.103  1.00 58.28  ? 238 LEU A CD1 1 
ATOM   2937 C CD2 . LEU B 1 52  ? 18.597  2.447   33.444  1.00 58.22  ? 238 LEU A CD2 1 
ATOM   2938 N N   . ARG B 1 53  ? 15.249  2.412   29.991  1.00 71.08  ? 239 ARG A N   1 
ATOM   2939 C CA  . ARG B 1 53  ? 13.873  2.051   30.311  1.00 74.89  ? 239 ARG A CA  1 
ATOM   2940 C C   . ARG B 1 53  ? 13.300  1.085   29.279  1.00 73.50  ? 239 ARG A C   1 
ATOM   2941 O O   . ARG B 1 53  ? 12.724  0.051   29.636  1.00 75.12  ? 239 ARG A O   1 
ATOM   2942 C CB  . ARG B 1 53  ? 13.022  3.319   30.418  1.00 71.27  ? 239 ARG A CB  1 
ATOM   2943 C CG  . ARG B 1 53  ? 11.528  3.086   30.401  1.00 68.80  ? 239 ARG A CG  1 
ATOM   2944 C CD  . ARG B 1 53  ? 10.817  4.062   31.327  1.00 76.50  ? 239 ARG A CD  1 
ATOM   2945 N NE  . ARG B 1 53  ? 11.058  5.463   30.996  1.00 75.61  ? 239 ARG A NE  1 
ATOM   2946 C CZ  . ARG B 1 53  ? 10.153  6.274   30.465  1.00 68.40  ? 239 ARG A CZ  1 
ATOM   2947 N NH1 . ARG B 1 53  ? 8.936   5.851   30.166  1.00 69.62  ? 239 ARG A NH1 1 
ATOM   2948 N NH2 . ARG B 1 53  ? 10.475  7.545   30.238  1.00 63.19  ? 239 ARG A NH2 1 
ATOM   2949 N N   . LYS B 1 54  ? 13.464  1.398   27.990  1.00 72.07  ? 240 LYS A N   1 
ATOM   2950 C CA  . LYS B 1 54  ? 12.932  0.529   26.942  1.00 68.78  ? 240 LYS A CA  1 
ATOM   2951 C C   . LYS B 1 54  ? 13.591  -0.845  26.975  1.00 72.47  ? 240 LYS A C   1 
ATOM   2952 O O   . LYS B 1 54  ? 12.945  -1.862  26.690  1.00 75.95  ? 240 LYS A O   1 
ATOM   2953 C CB  . LYS B 1 54  ? 13.119  1.185   25.574  1.00 71.62  ? 240 LYS A CB  1 
ATOM   2954 C CG  . LYS B 1 54  ? 12.539  0.391   24.412  1.00 83.64  ? 240 LYS A CG  1 
ATOM   2955 C CD  . LYS B 1 54  ? 12.817  1.085   23.083  1.00 81.21  ? 240 LYS A CD  1 
ATOM   2956 C CE  . LYS B 1 54  ? 12.229  0.310   21.914  1.00 92.50  ? 240 LYS A CE  1 
ATOM   2957 N NZ  . LYS B 1 54  ? 12.449  1.018   20.621  1.00 105.40 ? 240 LYS A NZ  1 
ATOM   2958 N N   . ALA B 1 55  ? 14.882  -0.892  27.313  1.00 76.58  ? 241 ALA A N   1 
ATOM   2959 C CA  . ALA B 1 55  ? 15.574  -2.169  27.454  1.00 74.61  ? 241 ALA A CA  1 
ATOM   2960 C C   . ALA B 1 55  ? 14.987  -2.997  28.590  1.00 72.51  ? 241 ALA A C   1 
ATOM   2961 O O   . ALA B 1 55  ? 14.841  -4.219  28.470  1.00 76.28  ? 241 ALA A O   1 
ATOM   2962 C CB  . ALA B 1 55  ? 17.065  -1.931  27.683  1.00 67.30  ? 241 ALA A CB  1 
ATOM   2963 N N   . VAL B 1 56  ? 14.649  -2.348  29.704  1.00 68.69  ? 242 VAL A N   1 
ATOM   2964 C CA  . VAL B 1 56  ? 14.049  -3.054  30.832  1.00 77.57  ? 242 VAL A CA  1 
ATOM   2965 C C   . VAL B 1 56  ? 12.712  -3.667  30.427  1.00 77.63  ? 242 VAL A C   1 
ATOM   2966 O O   . VAL B 1 56  ? 12.383  -4.794  30.818  1.00 76.04  ? 242 VAL A O   1 
ATOM   2967 C CB  . VAL B 1 56  ? 13.907  -2.097  32.031  1.00 79.43  ? 242 VAL A CB  1 
ATOM   2968 C CG1 . VAL B 1 56  ? 13.065  -2.719  33.131  1.00 71.65  ? 242 VAL A CG1 1 
ATOM   2969 C CG2 . VAL B 1 56  ? 15.283  -1.708  32.563  1.00 74.94  ? 242 VAL A CG2 1 
ATOM   2970 N N   . TYR B 1 57  ? 11.938  -2.949  29.607  1.00 80.83  ? 243 TYR A N   1 
ATOM   2971 C CA  . TYR B 1 57  ? 10.630  -3.438  29.173  1.00 76.06  ? 243 TYR A CA  1 
ATOM   2972 C C   . TYR B 1 57  ? 10.712  -4.750  28.395  1.00 79.41  ? 243 TYR A C   1 
ATOM   2973 O O   . TYR B 1 57  ? 9.774   -5.553  28.447  1.00 74.81  ? 243 TYR A O   1 
ATOM   2974 C CB  . TYR B 1 57  ? 9.929   -2.373  28.322  1.00 69.93  ? 243 TYR A CB  1 
ATOM   2975 C CG  . TYR B 1 57  ? 9.359   -1.206  29.105  1.00 65.58  ? 243 TYR A CG  1 
ATOM   2976 C CD1 . TYR B 1 57  ? 8.998   -1.347  30.436  1.00 71.15  ? 243 TYR A CD1 1 
ATOM   2977 C CD2 . TYR B 1 57  ? 9.176   0.036   28.508  1.00 65.52  ? 243 TYR A CD2 1 
ATOM   2978 C CE1 . TYR B 1 57  ? 8.473   -0.285  31.154  1.00 71.83  ? 243 TYR A CE1 1 
ATOM   2979 C CE2 . TYR B 1 57  ? 8.653   1.107   29.219  1.00 64.88  ? 243 TYR A CE2 1 
ATOM   2980 C CZ  . TYR B 1 57  ? 8.302   0.940   30.542  1.00 68.89  ? 243 TYR A CZ  1 
ATOM   2981 O OH  . TYR B 1 57  ? 7.777   1.991   31.266  1.00 73.22  ? 243 TYR A OH  1 
ATOM   2982 N N   . MET B 1 58  ? 11.803  -4.986  27.663  1.00 77.22  ? 244 MET A N   1 
ATOM   2983 C CA  . MET B 1 58  ? 11.883  -6.114  26.740  1.00 75.79  ? 244 MET A CA  1 
ATOM   2984 C C   . MET B 1 58  ? 12.587  -7.344  27.318  1.00 80.73  ? 244 MET A C   1 
ATOM   2985 O O   . MET B 1 58  ? 13.011  -8.216  26.553  1.00 76.93  ? 244 MET A O   1 
ATOM   2986 C CB  . MET B 1 58  ? 12.572  -5.679  25.449  1.00 67.30  ? 244 MET A CB  1 
ATOM   2987 C CG  . MET B 1 58  ? 11.822  -4.604  24.691  1.00 77.98  ? 244 MET A CG  1 
ATOM   2988 S SD  . MET B 1 58  ? 12.541  -4.294  23.067  1.00 106.56 ? 244 MET A SD  1 
ATOM   2989 C CE  . MET B 1 58  ? 14.216  -3.803  23.482  1.00 85.68  ? 244 MET A CE  1 
ATOM   2990 N N   . MET B 1 59  ? 12.728  -7.440  28.642  1.00 79.44  ? 245 MET A N   1 
ATOM   2991 C CA  . MET B 1 59  ? 13.402  -8.602  29.207  1.00 83.15  ? 245 MET A CA  1 
ATOM   2992 C C   . MET B 1 59  ? 12.481  -9.821  29.252  1.00 84.41  ? 245 MET A C   1 
ATOM   2993 O O   . MET B 1 59  ? 11.270  -9.681  29.436  1.00 88.09  ? 245 MET A O   1 
ATOM   2994 C CB  . MET B 1 59  ? 13.909  -8.283  30.608  1.00 89.10  ? 245 MET A CB  1 
ATOM   2995 C CG  . MET B 1 59  ? 15.010  -7.238  30.613  1.00 80.17  ? 245 MET A CG  1 
ATOM   2996 S SD  . MET B 1 59  ? 15.629  -6.880  32.259  1.00 80.99  ? 245 MET A SD  1 
ATOM   2997 C CE  . MET B 1 59  ? 14.155  -6.249  33.043  1.00 73.68  ? 245 MET A CE  1 
ATOM   2998 N N   . PRO B 1 60  ? 13.038  -11.044 29.090  1.00 90.31  ? 246 PRO A N   1 
ATOM   2999 C CA  . PRO B 1 60  ? 12.207  -12.274 29.133  1.00 93.18  ? 246 PRO A CA  1 
ATOM   3000 C C   . PRO B 1 60  ? 11.838  -12.680 30.555  1.00 93.42  ? 246 PRO A C   1 
ATOM   3001 O O   . PRO B 1 60  ? 12.316  -13.673 31.118  1.00 90.66  ? 246 PRO A O   1 
ATOM   3002 C CB  . PRO B 1 60  ? 13.108  -13.312 28.445  1.00 87.04  ? 246 PRO A CB  1 
ATOM   3003 C CG  . PRO B 1 60  ? 14.226  -12.539 27.804  1.00 89.41  ? 246 PRO A CG  1 
ATOM   3004 C CD  . PRO B 1 60  ? 14.415  -11.340 28.672  1.00 87.45  ? 246 PRO A CD  1 
ATOM   3005 N N   . THR B 1 61  ? 10.932  -11.907 31.143  1.00 94.43  ? 247 THR A N   1 
ATOM   3006 C CA  . THR B 1 61  ? 10.484  -12.092 32.515  1.00 99.50  ? 247 THR A CA  1 
ATOM   3007 C C   . THR B 1 61  ? 9.123   -12.777 32.611  1.00 97.19  ? 247 THR A C   1 
ATOM   3008 O O   . THR B 1 61  ? 8.502   -12.747 33.678  1.00 97.12  ? 247 THR A O   1 
ATOM   3009 C CB  . THR B 1 61  ? 10.459  -10.739 33.230  1.00 97.53  ? 247 THR A CB  1 
ATOM   3010 O OG1 . THR B 1 61  ? 9.683   -9.808  32.465  1.00 91.77  ? 247 THR A OG1 1 
ATOM   3011 C CG2 . THR B 1 61  ? 11.876  -10.202 33.381  1.00 90.72  ? 247 THR A CG2 1 
ATOM   3012 N N   . GLU B 1 62  ? 8.646   -13.394 31.525  1.00 92.81  ? 248 GLU A N   1 
ATOM   3013 C CA  . GLU B 1 62  ? 7.327   -14.024 31.548  1.00 98.33  ? 248 GLU A CA  1 
ATOM   3014 C C   . GLU B 1 62  ? 7.262   -15.141 32.586  1.00 98.25  ? 248 GLU A C   1 
ATOM   3015 O O   . GLU B 1 62  ? 6.312   -15.219 33.375  1.00 101.23 ? 248 GLU A O   1 
ATOM   3016 C CB  . GLU B 1 62  ? 6.982   -14.589 30.165  1.00 94.82  ? 248 GLU A CB  1 
ATOM   3017 C CG  . GLU B 1 62  ? 7.109   -13.623 28.997  1.00 101.73 ? 248 GLU A CG  1 
ATOM   3018 C CD  . GLU B 1 62  ? 8.543   -13.552 28.493  1.00 100.30 ? 248 GLU A CD  1 
ATOM   3019 O OE1 . GLU B 1 62  ? 9.430   -14.102 29.182  1.00 99.98  ? 248 GLU A OE1 1 
ATOM   3020 O OE2 . GLU B 1 62  ? 8.786   -12.968 27.413  1.00 95.95  ? 248 GLU A OE2 1 
ATOM   3021 N N   . GLY B 1 63  ? 8.273   -16.006 32.609  1.00 90.35  ? 249 GLY A N   1 
ATOM   3022 C CA  . GLY B 1 63  ? 8.276   -17.169 33.481  1.00 99.31  ? 249 GLY A CA  1 
ATOM   3023 C C   . GLY B 1 63  ? 9.025   -16.978 34.782  1.00 102.49 ? 249 GLY A C   1 
ATOM   3024 O O   . GLY B 1 63  ? 9.586   -17.930 35.338  1.00 103.77 ? 249 GLY A O   1 
ATOM   3025 N N   . ASP B 1 64  ? 9.043   -15.750 35.280  1.00 96.64  ? 250 ASP A N   1 
ATOM   3026 C CA  . ASP B 1 64  ? 9.726   -15.444 36.524  1.00 98.54  ? 250 ASP A CA  1 
ATOM   3027 C C   . ASP B 1 64  ? 8.727   -15.315 37.667  1.00 94.15  ? 250 ASP A C   1 
ATOM   3028 O O   . ASP B 1 64  ? 7.532   -15.093 37.460  1.00 98.15  ? 250 ASP A O   1 
ATOM   3029 C CB  . ASP B 1 64  ? 10.538  -14.155 36.386  1.00 97.36  ? 250 ASP A CB  1 
ATOM   3030 C CG  . ASP B 1 64  ? 11.637  -14.265 35.339  1.00 100.81 ? 250 ASP A CG  1 
ATOM   3031 O OD1 . ASP B 1 64  ? 11.566  -15.165 34.471  1.00 101.32 ? 250 ASP A OD1 1 
ATOM   3032 O OD2 . ASP B 1 64  ? 12.575  -13.441 35.385  1.00 106.11 ? 250 ASP A OD2 1 
ATOM   3033 N N   . ASP B 1 65  ? 9.243   -15.454 38.885  1.00 87.12  ? 251 ASP A N   1 
ATOM   3034 C CA  . ASP B 1 65  ? 8.430   -15.372 40.091  1.00 93.36  ? 251 ASP A CA  1 
ATOM   3035 C C   . ASP B 1 65  ? 8.297   -13.907 40.488  1.00 93.24  ? 251 ASP A C   1 
ATOM   3036 O O   . ASP B 1 65  ? 9.303   -13.233 40.724  1.00 92.72  ? 251 ASP A O   1 
ATOM   3037 C CB  . ASP B 1 65  ? 9.059   -16.197 41.215  1.00 86.06  ? 251 ASP A CB  1 
ATOM   3038 C CG  . ASP B 1 65  ? 8.439   -15.912 42.568  1.00 91.83  ? 251 ASP A CG  1 
ATOM   3039 O OD1 . ASP B 1 65  ? 8.793   -14.887 43.191  1.00 92.99  ? 251 ASP A OD1 1 
ATOM   3040 O OD2 . ASP B 1 65  ? 7.586   -16.713 43.001  1.00 100.61 ? 251 ASP A OD2 1 
ATOM   3041 N N   . SER B 1 66  ? 7.054   -13.425 40.575  1.00 92.27  ? 252 SER A N   1 
ATOM   3042 C CA  . SER B 1 66  ? 6.822   -12.001 40.808  1.00 91.67  ? 252 SER A CA  1 
ATOM   3043 C C   . SER B 1 66  ? 7.428   -11.538 42.128  1.00 91.14  ? 252 SER A C   1 
ATOM   3044 O O   . SER B 1 66  ? 7.953   -10.422 42.222  1.00 95.48  ? 252 SER A O   1 
ATOM   3045 C CB  . SER B 1 66  ? 5.321   -11.713 40.778  1.00 101.12 ? 252 SER A CB  1 
ATOM   3046 O OG  . SER B 1 66  ? 5.028   -10.435 41.315  1.00 105.76 ? 252 SER A OG  1 
ATOM   3047 N N   . SER B 1 67  ? 7.353   -12.373 43.163  1.00 89.74  ? 253 SER A N   1 
ATOM   3048 C CA  . SER B 1 67  ? 7.837   -11.965 44.474  1.00 92.06  ? 253 SER A CA  1 
ATOM   3049 C C   . SER B 1 67  ? 9.357   -11.941 44.558  1.00 90.67  ? 253 SER A C   1 
ATOM   3050 O O   . SER B 1 67  ? 9.898   -11.306 45.470  1.00 92.14  ? 253 SER A O   1 
ATOM   3051 C CB  . SER B 1 67  ? 7.271   -12.889 45.554  1.00 96.17  ? 253 SER A CB  1 
ATOM   3052 O OG  . SER B 1 67  ? 7.911   -14.153 45.523  1.00 90.40  ? 253 SER A OG  1 
ATOM   3053 N N   . LYS B 1 68  ? 10.059  -12.599 43.627  1.00 88.44  ? 254 LYS A N   1 
ATOM   3054 C CA  . LYS B 1 68  ? 11.506  -12.756 43.731  1.00 86.94  ? 254 LYS A CA  1 
ATOM   3055 C C   . LYS B 1 68  ? 12.264  -12.358 42.468  1.00 86.65  ? 254 LYS A C   1 
ATOM   3056 O O   . LYS B 1 68  ? 13.486  -12.550 42.411  1.00 88.45  ? 254 LYS A O   1 
ATOM   3057 C CB  . LYS B 1 68  ? 11.860  -14.204 44.103  1.00 84.25  ? 254 LYS A CB  1 
ATOM   3058 C CG  . LYS B 1 68  ? 11.330  -14.646 45.462  1.00 92.41  ? 254 LYS A CG  1 
ATOM   3059 C CD  . LYS B 1 68  ? 11.716  -16.082 45.781  1.00 96.82  ? 254 LYS A CD  1 
ATOM   3060 C CE  . LYS B 1 68  ? 11.189  -16.504 47.145  1.00 98.82  ? 254 LYS A CE  1 
ATOM   3061 N NZ  . LYS B 1 68  ? 11.597  -17.896 47.479  1.00 104.45 ? 254 LYS A NZ  1 
ATOM   3062 N N   . SER B 1 69  ? 11.591  -11.811 41.459  1.00 87.06  ? 255 SER A N   1 
ATOM   3063 C CA  . SER B 1 69  ? 12.239  -11.433 40.206  1.00 81.89  ? 255 SER A CA  1 
ATOM   3064 C C   . SER B 1 69  ? 12.583  -9.950  40.277  1.00 77.84  ? 255 SER A C   1 
ATOM   3065 O O   . SER B 1 69  ? 11.692  -9.094  40.242  1.00 74.02  ? 255 SER A O   1 
ATOM   3066 C CB  . SER B 1 69  ? 11.344  -11.731 39.005  1.00 87.79  ? 255 SER A CB  1 
ATOM   3067 O OG  . SER B 1 69  ? 11.972  -11.366 37.788  1.00 84.05  ? 255 SER A OG  1 
ATOM   3068 N N   . VAL B 1 70  ? 13.881  -9.650  40.382  1.00 86.31  ? 256 VAL A N   1 
ATOM   3069 C CA  . VAL B 1 70  ? 14.323  -8.253  40.342  1.00 80.81  ? 256 VAL A CA  1 
ATOM   3070 C C   . VAL B 1 70  ? 14.035  -7.619  38.991  1.00 73.46  ? 256 VAL A C   1 
ATOM   3071 O O   . VAL B 1 70  ? 13.563  -6.472  38.959  1.00 71.23  ? 256 VAL A O   1 
ATOM   3072 C CB  . VAL B 1 70  ? 15.795  -8.150  40.764  1.00 69.97  ? 256 VAL A CB  1 
ATOM   3073 C CG1 . VAL B 1 70  ? 16.246  -6.698  40.751  1.00 70.80  ? 256 VAL A CG1 1 
ATOM   3074 C CG2 . VAL B 1 70  ? 15.990  -8.769  42.138  1.00 70.07  ? 256 VAL A CG2 1 
ATOM   3075 N N   . PRO B 1 71  ? 14.310  -8.264  37.850  1.00 69.97  ? 257 PRO A N   1 
ATOM   3076 C CA  . PRO B 1 71  ? 13.894  -7.664  36.573  1.00 71.40  ? 257 PRO A CA  1 
ATOM   3077 C C   . PRO B 1 71  ? 12.396  -7.426  36.466  1.00 79.91  ? 257 PRO A C   1 
ATOM   3078 O O   . PRO B 1 71  ? 11.979  -6.391  35.932  1.00 83.65  ? 257 PRO A O   1 
ATOM   3079 C CB  . PRO B 1 71  ? 14.378  -8.691  35.541  1.00 79.59  ? 257 PRO A CB  1 
ATOM   3080 C CG  . PRO B 1 71  ? 15.514  -9.365  36.194  1.00 78.61  ? 257 PRO A CG  1 
ATOM   3081 C CD  . PRO B 1 71  ? 15.124  -9.474  37.632  1.00 73.25  ? 257 PRO A CD  1 
ATOM   3082 N N   . LEU B 1 72  ? 11.568  -8.347  36.967  1.00 80.77  ? 258 LEU A N   1 
ATOM   3083 C CA  . LEU B 1 72  ? 10.126  -8.137  36.886  1.00 77.17  ? 258 LEU A CA  1 
ATOM   3084 C C   . LEU B 1 72  ? 9.684   -6.990  37.784  1.00 73.57  ? 258 LEU A C   1 
ATOM   3085 O O   . LEU B 1 72  ? 8.845   -6.172  37.389  1.00 77.35  ? 258 LEU A O   1 
ATOM   3086 C CB  . LEU B 1 72  ? 9.376   -9.419  37.244  1.00 79.33  ? 258 LEU A CB  1 
ATOM   3087 C CG  . LEU B 1 72  ? 7.854   -9.306  37.124  1.00 85.95  ? 258 LEU A CG  1 
ATOM   3088 C CD1 . LEU B 1 72  ? 7.459   -9.024  35.682  1.00 85.23  ? 258 LEU A CD1 1 
ATOM   3089 C CD2 . LEU B 1 72  ? 7.169   -10.566 37.613  1.00 91.25  ? 258 LEU A CD2 1 
ATOM   3090 N N   . ALA B 1 73  ? 10.240  -6.912  38.993  1.00 72.09  ? 259 ALA A N   1 
ATOM   3091 C CA  . ALA B 1 73  ? 9.875   -5.831  39.899  1.00 75.64  ? 259 ALA A CA  1 
ATOM   3092 C C   . ALA B 1 73  ? 10.272  -4.477  39.326  1.00 73.72  ? 259 ALA A C   1 
ATOM   3093 O O   . ALA B 1 73  ? 9.500   -3.514  39.394  1.00 78.04  ? 259 ALA A O   1 
ATOM   3094 C CB  . ALA B 1 73  ? 10.517  -6.052  41.268  1.00 77.79  ? 259 ALA A CB  1 
ATOM   3095 N N   . LEU B 1 74  ? 11.470  -4.386  38.744  1.00 71.98  ? 260 LEU A N   1 
ATOM   3096 C CA  . LEU B 1 74  ? 11.902  -3.124  38.153  1.00 74.44  ? 260 LEU A CA  1 
ATOM   3097 C C   . LEU B 1 74  ? 11.035  -2.748  36.956  1.00 74.98  ? 260 LEU A C   1 
ATOM   3098 O O   . LEU B 1 74  ? 10.772  -1.563  36.722  1.00 73.72  ? 260 LEU A O   1 
ATOM   3099 C CB  . LEU B 1 74  ? 13.374  -3.200  37.756  1.00 71.32  ? 260 LEU A CB  1 
ATOM   3100 C CG  . LEU B 1 74  ? 13.962  -1.847  37.363  1.00 74.33  ? 260 LEU A CG  1 
ATOM   3101 C CD1 . LEU B 1 74  ? 13.977  -0.931  38.579  1.00 71.35  ? 260 LEU A CD1 1 
ATOM   3102 C CD2 . LEU B 1 74  ? 15.356  -2.007  36.786  1.00 70.63  ? 260 LEU A CD2 1 
ATOM   3103 N N   . GLN B 1 75  ? 10.598  -3.739  36.174  1.00 76.60  ? 261 GLN A N   1 
ATOM   3104 C CA  . GLN B 1 75  ? 9.633   -3.464  35.113  1.00 74.59  ? 261 GLN A CA  1 
ATOM   3105 C C   . GLN B 1 75  ? 8.338   -2.908  35.687  1.00 75.60  ? 261 GLN A C   1 
ATOM   3106 O O   . GLN B 1 75  ? 7.751   -1.972  35.131  1.00 72.73  ? 261 GLN A O   1 
ATOM   3107 C CB  . GLN B 1 75  ? 9.349   -4.730  34.303  1.00 74.04  ? 261 GLN A CB  1 
ATOM   3108 C CG  . GLN B 1 75  ? 10.460  -5.149  33.362  1.00 74.68  ? 261 GLN A CG  1 
ATOM   3109 C CD  . GLN B 1 75  ? 10.267  -6.554  32.822  1.00 78.62  ? 261 GLN A CD  1 
ATOM   3110 O OE1 . GLN B 1 75  ? 9.824   -7.451  33.540  1.00 79.89  ? 261 GLN A OE1 1 
ATOM   3111 N NE2 . GLN B 1 75  ? 10.590  -6.750  31.549  1.00 77.73  ? 261 GLN A NE2 1 
ATOM   3112 N N   . ARG B 1 76  ? 7.883   -3.469  36.809  1.00 75.14  ? 262 ARG A N   1 
ATOM   3113 C CA  . ARG B 1 76  ? 6.621   -3.041  37.399  1.00 78.93  ? 262 ARG A CA  1 
ATOM   3114 C C   . ARG B 1 76  ? 6.660   -1.565  37.777  1.00 77.10  ? 262 ARG A C   1 
ATOM   3115 O O   . ARG B 1 76  ? 5.730   -0.811  37.472  1.00 76.40  ? 262 ARG A O   1 
ATOM   3116 C CB  . ARG B 1 76  ? 6.302   -3.909  38.616  1.00 75.48  ? 262 ARG A CB  1 
ATOM   3117 C CG  . ARG B 1 76  ? 4.926   -3.687  39.192  1.00 72.41  ? 262 ARG A CG  1 
ATOM   3118 C CD  . ARG B 1 76  ? 4.684   -4.554  40.420  1.00 79.96  ? 262 ARG A CD  1 
ATOM   3119 N NE  . ARG B 1 76  ? 4.866   -5.979  40.158  1.00 83.75  ? 262 ARG A NE  1 
ATOM   3120 C CZ  . ARG B 1 76  ? 5.916   -6.692  40.545  1.00 83.56  ? 262 ARG A CZ  1 
ATOM   3121 N NH1 . ARG B 1 76  ? 6.914   -6.143  41.219  1.00 82.30  ? 262 ARG A NH1 1 
ATOM   3122 N NH2 . ARG B 1 76  ? 5.960   -7.991  40.261  1.00 80.03  ? 262 ARG A NH2 1 
ATOM   3123 N N   . VAL B 1 77  ? 7.739   -1.130  38.433  1.00 72.23  ? 263 VAL A N   1 
ATOM   3124 C CA  . VAL B 1 77  ? 7.812   0.256   38.887  1.00 68.44  ? 263 VAL A CA  1 
ATOM   3125 C C   . VAL B 1 77  ? 7.971   1.207   37.703  1.00 68.81  ? 263 VAL A C   1 
ATOM   3126 O O   . VAL B 1 77  ? 7.404   2.307   37.695  1.00 69.81  ? 263 VAL A O   1 
ATOM   3127 C CB  . VAL B 1 77  ? 8.934   0.426   39.929  1.00 64.16  ? 263 VAL A CB  1 
ATOM   3128 C CG1 . VAL B 1 77  ? 10.274  -0.006  39.369  1.00 80.09  ? 263 VAL A CG1 1 
ATOM   3129 C CG2 . VAL B 1 77  ? 8.990   1.867   40.422  1.00 67.63  ? 263 VAL A CG2 1 
ATOM   3130 N N   . PHE B 1 78  ? 8.742   0.807   36.688  1.00 70.15  ? 264 PHE A N   1 
ATOM   3131 C CA  . PHE B 1 78  ? 8.861   1.632   35.489  1.00 74.09  ? 264 PHE A CA  1 
ATOM   3132 C C   . PHE B 1 78  ? 7.508   1.796   34.808  1.00 71.10  ? 264 PHE A C   1 
ATOM   3133 O O   . PHE B 1 78  ? 7.152   2.893   34.360  1.00 69.96  ? 264 PHE A O   1 
ATOM   3134 C CB  . PHE B 1 78  ? 9.872   1.014   34.519  1.00 78.82  ? 264 PHE A CB  1 
ATOM   3135 C CG  . PHE B 1 78  ? 11.313  1.287   34.872  1.00 80.39  ? 264 PHE A CG  1 
ATOM   3136 C CD1 . PHE B 1 78  ? 11.644  2.202   35.856  1.00 76.50  ? 264 PHE A CD1 1 
ATOM   3137 C CD2 . PHE B 1 78  ? 12.337  0.624   34.212  1.00 75.56  ? 264 PHE A CD2 1 
ATOM   3138 C CE1 . PHE B 1 78  ? 12.972  2.450   36.174  1.00 74.86  ? 264 PHE A CE1 1 
ATOM   3139 C CE2 . PHE B 1 78  ? 13.659  0.869   34.529  1.00 69.65  ? 264 PHE A CE2 1 
ATOM   3140 C CZ  . PHE B 1 78  ? 13.976  1.782   35.510  1.00 67.97  ? 264 PHE A CZ  1 
ATOM   3141 N N   . TYR B 1 79  ? 6.746   0.710   34.716  1.00 76.42  ? 265 TYR A N   1 
ATOM   3142 C CA  . TYR B 1 79  ? 5.416   0.775   34.121  1.00 78.17  ? 265 TYR A CA  1 
ATOM   3143 C C   . TYR B 1 79  ? 4.498   1.695   34.921  1.00 77.28  ? 265 TYR A C   1 
ATOM   3144 O O   . TYR B 1 79  ? 3.801   2.544   34.352  1.00 79.83  ? 265 TYR A O   1 
ATOM   3145 C CB  . TYR B 1 79  ? 4.842   -0.639  34.037  1.00 78.25  ? 265 TYR A CB  1 
ATOM   3146 C CG  . TYR B 1 79  ? 3.479   -0.776  33.393  1.00 80.37  ? 265 TYR A CG  1 
ATOM   3147 C CD1 . TYR B 1 79  ? 2.316   -0.683  34.150  1.00 86.40  ? 265 TYR A CD1 1 
ATOM   3148 C CD2 . TYR B 1 79  ? 3.355   -1.042  32.035  1.00 86.25  ? 265 TYR A CD2 1 
ATOM   3149 C CE1 . TYR B 1 79  ? 1.067   -0.824  33.566  1.00 88.24  ? 265 TYR A CE1 1 
ATOM   3150 C CE2 . TYR B 1 79  ? 2.111   -1.184  31.441  1.00 89.24  ? 265 TYR A CE2 1 
ATOM   3151 C CZ  . TYR B 1 79  ? 0.970   -1.074  32.211  1.00 91.10  ? 265 TYR A CZ  1 
ATOM   3152 O OH  . TYR B 1 79  ? -0.269  -1.215  31.622  1.00 90.31  ? 265 TYR A OH  1 
ATOM   3153 N N   . GLU B 1 80  ? 4.501   1.555   36.249  1.00 70.39  ? 266 GLU A N   1 
ATOM   3154 C CA  . GLU B 1 80  ? 3.649   2.397   37.085  1.00 69.10  ? 266 GLU A CA  1 
ATOM   3155 C C   . GLU B 1 80  ? 4.030   3.869   36.973  1.00 66.34  ? 266 GLU A C   1 
ATOM   3156 O O   . GLU B 1 80  ? 3.158   4.744   36.986  1.00 71.54  ? 266 GLU A O   1 
ATOM   3157 C CB  . GLU B 1 80  ? 3.714   1.935   38.540  1.00 72.07  ? 266 GLU A CB  1 
ATOM   3158 C CG  . GLU B 1 80  ? 3.190   0.528   38.795  1.00 81.38  ? 266 GLU A CG  1 
ATOM   3159 C CD  . GLU B 1 80  ? 1.684   0.418   38.633  1.00 80.25  ? 266 GLU A CD  1 
ATOM   3160 O OE1 . GLU B 1 80  ? 1.003   1.461   38.709  1.00 82.82  ? 266 GLU A OE1 1 
ATOM   3161 O OE2 . GLU B 1 80  ? 1.179   -0.710  38.443  1.00 82.74  ? 266 GLU A OE2 1 
ATOM   3162 N N   . LEU B 1 81  ? 5.323   4.165   36.854  1.00 72.26  ? 267 LEU A N   1 
ATOM   3163 C CA  . LEU B 1 81  ? 5.749   5.553   36.725  1.00 70.55  ? 267 LEU A CA  1 
ATOM   3164 C C   . LEU B 1 81  ? 5.364   6.167   35.387  1.00 65.07  ? 267 LEU A C   1 
ATOM   3165 O O   . LEU B 1 81  ? 5.421   7.393   35.251  1.00 63.37  ? 267 LEU A O   1 
ATOM   3166 C CB  . LEU B 1 81  ? 7.261   5.664   36.928  1.00 62.75  ? 267 LEU A CB  1 
ATOM   3167 C CG  . LEU B 1 81  ? 7.754   5.628   38.369  1.00 62.06  ? 267 LEU A CG  1 
ATOM   3168 C CD1 . LEU B 1 81  ? 9.263   5.667   38.397  1.00 68.01  ? 267 LEU A CD1 1 
ATOM   3169 C CD2 . LEU B 1 81  ? 7.179   6.802   39.135  1.00 66.32  ? 267 LEU A CD2 1 
ATOM   3170 N N   . GLN B 1 82  ? 4.981   5.357   34.403  1.00 63.73  ? 268 GLN A N   1 
ATOM   3171 C CA  . GLN B 1 82  ? 4.632   5.873   33.087  1.00 71.65  ? 268 GLN A CA  1 
ATOM   3172 C C   . GLN B 1 82  ? 3.133   6.043   32.880  1.00 74.83  ? 268 GLN A C   1 
ATOM   3173 O O   . GLN B 1 82  ? 2.719   6.936   32.133  1.00 84.49  ? 268 GLN A O   1 
ATOM   3174 C CB  . GLN B 1 82  ? 5.200   4.956   31.995  1.00 73.47  ? 268 GLN A CB  1 
ATOM   3175 C CG  . GLN B 1 82  ? 4.971   5.447   30.565  1.00 71.53  ? 268 GLN A CG  1 
ATOM   3176 C CD  . GLN B 1 82  ? 5.876   4.761   29.559  1.00 71.48  ? 268 GLN A CD  1 
ATOM   3177 O OE1 . GLN B 1 82  ? 6.953   4.273   29.910  1.00 80.90  ? 268 GLN A OE1 1 
ATOM   3178 N NE2 . GLN B 1 82  ? 5.450   4.729   28.299  1.00 74.18  ? 268 GLN A NE2 1 
ATOM   3179 N N   . HIS B 1 83  ? 2.307   5.233   33.532  1.00 70.85  ? 269 HIS A N   1 
ATOM   3180 C CA  . HIS B 1 83  ? 0.866   5.261   33.309  1.00 78.63  ? 269 HIS A CA  1 
ATOM   3181 C C   . HIS B 1 83  ? 0.080   5.789   34.496  1.00 80.79  ? 269 HIS A C   1 
ATOM   3182 O O   . HIS B 1 83  ? -0.936  6.466   34.305  1.00 81.64  ? 269 HIS A O   1 
ATOM   3183 C CB  . HIS B 1 83  ? 0.354   3.856   32.965  1.00 80.95  ? 269 HIS A CB  1 
ATOM   3184 C CG  . HIS B 1 83  ? 0.924   3.293   31.701  1.00 84.18  ? 269 HIS A CG  1 
ATOM   3185 N ND1 . HIS B 1 83  ? 2.254   2.957   31.567  1.00 82.29  ? 269 HIS A ND1 1 
ATOM   3186 C CD2 . HIS B 1 83  ? 0.341   2.998   30.514  1.00 87.29  ? 269 HIS A CD2 1 
ATOM   3187 C CE1 . HIS B 1 83  ? 2.467   2.485   30.352  1.00 84.91  ? 269 HIS A CE1 1 
ATOM   3188 N NE2 . HIS B 1 83  ? 1.322   2.499   29.693  1.00 83.73  ? 269 HIS A NE2 1 
ATOM   3189 N N   . SER B 1 84  ? 0.515   5.487   35.717  1.00 69.25  ? 270 SER A N   1 
ATOM   3190 C CA  . SER B 1 84  ? -0.265  5.839   36.894  1.00 72.22  ? 270 SER A CA  1 
ATOM   3191 C C   . SER B 1 84  ? -0.278  7.344   37.125  1.00 77.30  ? 270 SER A C   1 
ATOM   3192 O O   . SER B 1 84  ? 0.733   8.029   36.946  1.00 78.46  ? 270 SER A O   1 
ATOM   3193 C CB  . SER B 1 84  ? 0.286   5.132   38.131  1.00 79.16  ? 270 SER A CB  1 
ATOM   3194 O OG  . SER B 1 84  ? -0.386  5.581   39.294  1.00 90.42  ? 270 SER A OG  1 
ATOM   3195 N N   . ASP B 1 85  ? -1.438  7.851   37.531  1.00 80.07  ? 271 ASP A N   1 
ATOM   3196 C CA  . ASP B 1 85  ? -1.597  9.223   37.986  1.00 78.67  ? 271 ASP A CA  1 
ATOM   3197 C C   . ASP B 1 85  ? -1.456  9.336   39.493  1.00 80.77  ? 271 ASP A C   1 
ATOM   3198 O O   . ASP B 1 85  ? -1.564  10.442  40.033  1.00 77.43  ? 271 ASP A O   1 
ATOM   3199 C CB  . ASP B 1 85  ? -2.961  9.775   37.565  1.00 91.14  ? 271 ASP A CB  1 
ATOM   3200 C CG  . ASP B 1 85  ? -3.264  9.522   36.107  1.00 100.85 ? 271 ASP A CG  1 
ATOM   3201 O OD1 . ASP B 1 85  ? -3.760  8.419   35.782  1.00 102.94 ? 271 ASP A OD1 1 
ATOM   3202 O OD2 . ASP B 1 85  ? -2.989  10.422  35.286  1.00 99.65  ? 271 ASP A OD2 1 
ATOM   3203 N N   . LYS B 1 86  ? -1.216  8.209   40.173  1.00 89.62  ? 272 LYS A N   1 
ATOM   3204 C CA  . LYS B 1 86  ? -1.080  8.045   41.606  1.00 90.41  ? 272 LYS A CA  1 
ATOM   3205 C C   . LYS B 1 86  ? 0.367   7.727   41.962  1.00 94.36  ? 272 LYS A C   1 
ATOM   3206 O O   . LYS B 1 86  ? 1.099   7.158   41.143  1.00 102.60 ? 272 LYS A O   1 
ATOM   3207 C CB  . LYS B 1 86  ? -1.960  6.883   42.083  1.00 95.25  ? 272 LYS A CB  1 
ATOM   3208 C CG  . LYS B 1 86  ? -3.458  7.103   41.990  1.00 103.08 ? 272 LYS A CG  1 
ATOM   3209 C CD  . LYS B 1 86  ? -4.207  5.857   42.463  1.00 112.37 ? 272 LYS A CD  1 
ATOM   3210 C CE  . LYS B 1 86  ? -3.855  4.640   41.589  1.00 118.26 ? 272 LYS A CE  1 
ATOM   3211 N NZ  . LYS B 1 86  ? -4.267  4.758   40.161  1.00 119.95 ? 272 LYS A NZ  1 
ATOM   3212 N N   . PRO B 1 87  ? 0.812   8.081   43.168  1.00 81.72  ? 273 PRO A N   1 
ATOM   3213 C CA  . PRO B 1 87  ? 2.198   7.788   43.552  1.00 74.67  ? 273 PRO A CA  1 
ATOM   3214 C C   . PRO B 1 87  ? 2.455   6.286   43.551  1.00 75.77  ? 273 PRO A C   1 
ATOM   3215 O O   . PRO B 1 87  ? 1.583   5.489   43.906  1.00 76.91  ? 273 PRO A O   1 
ATOM   3216 C CB  . PRO B 1 87  ? 2.306   8.382   44.961  1.00 71.46  ? 273 PRO A CB  1 
ATOM   3217 C CG  . PRO B 1 87  ? 1.312   9.483   44.971  1.00 77.53  ? 273 PRO A CG  1 
ATOM   3218 C CD  . PRO B 1 87  ? 0.162   8.997   44.118  1.00 89.85  ? 273 PRO A CD  1 
ATOM   3219 N N   . VAL B 1 88  ? 3.660   5.908   43.147  1.00 68.93  ? 274 VAL A N   1 
ATOM   3220 C CA  . VAL B 1 88  ? 3.989   4.516   42.863  1.00 68.28  ? 274 VAL A CA  1 
ATOM   3221 C C   . VAL B 1 88  ? 4.607   3.863   44.095  1.00 70.74  ? 274 VAL A C   1 
ATOM   3222 O O   . VAL B 1 88  ? 5.360   4.499   44.840  1.00 70.15  ? 274 VAL A O   1 
ATOM   3223 C CB  . VAL B 1 88  ? 4.924   4.433   41.642  1.00 65.30  ? 274 VAL A CB  1 
ATOM   3224 C CG1 . VAL B 1 88  ? 5.378   3.005   41.395  1.00 68.09  ? 274 VAL A CG1 1 
ATOM   3225 C CG2 . VAL B 1 88  ? 4.229   5.003   40.414  1.00 61.61  ? 274 VAL A CG2 1 
ATOM   3226 N N   . GLY B 1 89  ? 4.276   2.592   44.319  1.00 69.47  ? 275 GLY A N   1 
ATOM   3227 C CA  . GLY B 1 89  ? 4.845   1.816   45.404  1.00 73.36  ? 275 GLY A CA  1 
ATOM   3228 C C   . GLY B 1 89  ? 5.988   0.927   44.946  1.00 74.49  ? 275 GLY A C   1 
ATOM   3229 O O   . GLY B 1 89  ? 6.067   0.537   43.784  1.00 65.40  ? 275 GLY A O   1 
ATOM   3230 N N   . THR B 1 90  ? 6.887   0.610   45.888  1.00 76.10  ? 276 THR A N   1 
ATOM   3231 C CA  . THR B 1 90  ? 8.094   -0.160  45.598  1.00 72.82  ? 276 THR A CA  1 
ATOM   3232 C C   . THR B 1 90  ? 8.250   -1.349  46.539  1.00 75.10  ? 276 THR A C   1 
ATOM   3233 O O   . THR B 1 90  ? 9.371   -1.829  46.739  1.00 75.44  ? 276 THR A O   1 
ATOM   3234 C CB  . THR B 1 90  ? 9.341   0.725   45.676  1.00 71.43  ? 276 THR A CB  1 
ATOM   3235 O OG1 . THR B 1 90  ? 9.457   1.271   46.997  1.00 84.90  ? 276 THR A OG1 1 
ATOM   3236 C CG2 . THR B 1 90  ? 9.268   1.859   44.668  1.00 61.97  ? 276 THR A CG2 1 
ATOM   3237 N N   . LYS B 1 91  ? 7.149   -1.829  47.122  1.00 79.93  ? 277 LYS A N   1 
ATOM   3238 C CA  . LYS B 1 91  ? 7.232   -2.890  48.121  1.00 77.69  ? 277 LYS A CA  1 
ATOM   3239 C C   . LYS B 1 91  ? 7.769   -4.179  47.517  1.00 79.32  ? 277 LYS A C   1 
ATOM   3240 O O   . LYS B 1 91  ? 8.681   -4.806  48.070  1.00 83.97  ? 277 LYS A O   1 
ATOM   3241 C CB  . LYS B 1 91  ? 5.854   -3.124  48.737  1.00 82.09  ? 277 LYS A CB  1 
ATOM   3242 C CG  . LYS B 1 91  ? 5.373   -2.013  49.647  1.00 84.39  ? 277 LYS A CG  1 
ATOM   3243 C CD  . LYS B 1 91  ? 6.196   -1.967  50.924  1.00 84.14  ? 277 LYS A CD  1 
ATOM   3244 C CE  . LYS B 1 91  ? 5.512   -1.138  52.004  1.00 91.07  ? 277 LYS A CE  1 
ATOM   3245 N NZ  . LYS B 1 91  ? 4.139   -1.630  52.316  1.00 98.61  ? 277 LYS A NZ  1 
ATOM   3246 N N   . LYS B 1 92  ? 7.215   -4.591  46.374  1.00 77.33  ? 278 LYS A N   1 
ATOM   3247 C CA  . LYS B 1 92  ? 7.677   -5.822  45.745  1.00 84.11  ? 278 LYS A CA  1 
ATOM   3248 C C   . LYS B 1 92  ? 9.140   -5.713  45.344  1.00 79.37  ? 278 LYS A C   1 
ATOM   3249 O O   . LYS B 1 92  ? 9.907   -6.669  45.507  1.00 80.81  ? 278 LYS A O   1 
ATOM   3250 C CB  . LYS B 1 92  ? 6.801   -6.167  44.541  1.00 82.98  ? 278 LYS A CB  1 
ATOM   3251 C CG  . LYS B 1 92  ? 5.467   -6.780  44.928  1.00 81.60  ? 278 LYS A CG  1 
ATOM   3252 C CD  . LYS B 1 92  ? 4.735   -7.349  43.724  1.00 91.53  ? 278 LYS A CD  1 
ATOM   3253 C CE  . LYS B 1 92  ? 3.383   -7.924  44.131  1.00 93.41  ? 278 LYS A CE  1 
ATOM   3254 N NZ  . LYS B 1 92  ? 2.644   -8.510  42.978  1.00 94.94  ? 278 LYS A NZ  1 
ATOM   3255 N N   . LEU B 1 93  ? 9.546   -4.554  44.817  1.00 74.66  ? 279 LEU A N   1 
ATOM   3256 C CA  . LEU B 1 93  ? 10.939  -4.368  44.425  1.00 75.60  ? 279 LEU A CA  1 
ATOM   3257 C C   . LEU B 1 93  ? 11.863  -4.467  45.632  1.00 78.80  ? 279 LEU A C   1 
ATOM   3258 O O   . LEU B 1 93  ? 12.946  -5.059  45.549  1.00 73.31  ? 279 LEU A O   1 
ATOM   3259 C CB  . LEU B 1 93  ? 11.107  -3.023  43.717  1.00 73.40  ? 279 LEU A CB  1 
ATOM   3260 C CG  . LEU B 1 93  ? 12.509  -2.641  43.237  1.00 74.22  ? 279 LEU A CG  1 
ATOM   3261 C CD1 . LEU B 1 93  ? 13.178  -3.786  42.490  1.00 77.04  ? 279 LEU A CD1 1 
ATOM   3262 C CD2 . LEU B 1 93  ? 12.427  -1.404  42.360  1.00 67.03  ? 279 LEU A CD2 1 
ATOM   3263 N N   . THR B 1 94  ? 11.453  -3.887  46.760  1.00 83.77  ? 280 THR A N   1 
ATOM   3264 C CA  . THR B 1 94  ? 12.220  -4.020  47.994  1.00 78.25  ? 280 THR A CA  1 
ATOM   3265 C C   . THR B 1 94  ? 12.316  -5.479  48.422  1.00 75.94  ? 280 THR A C   1 
ATOM   3266 O O   . THR B 1 94  ? 13.399  -5.973  48.759  1.00 70.78  ? 280 THR A O   1 
ATOM   3267 C CB  . THR B 1 94  ? 11.568  -3.170  49.085  1.00 81.58  ? 280 THR A CB  1 
ATOM   3268 O OG1 . THR B 1 94  ? 11.785  -1.782  48.804  1.00 82.73  ? 280 THR A OG1 1 
ATOM   3269 C CG2 . THR B 1 94  ? 12.113  -3.518  50.448  1.00 82.07  ? 280 THR A CG2 1 
ATOM   3270 N N   . LYS B 1 95  ? 11.189  -6.194  48.374  1.00 83.50  ? 281 LYS A N   1 
ATOM   3271 C CA  . LYS B 1 95  ? 11.199  -7.633  48.614  1.00 84.58  ? 281 LYS A CA  1 
ATOM   3272 C C   . LYS B 1 95  ? 12.052  -8.357  47.583  1.00 80.05  ? 281 LYS A C   1 
ATOM   3273 O O   . LYS B 1 95  ? 12.644  -9.401  47.882  1.00 79.46  ? 281 LYS A O   1 
ATOM   3274 C CB  . LYS B 1 95  ? 9.758   -8.158  48.590  1.00 83.15  ? 281 LYS A CB  1 
ATOM   3275 C CG  . LYS B 1 95  ? 9.589   -9.677  48.625  1.00 86.04  ? 281 LYS A CG  1 
ATOM   3276 C CD  . LYS B 1 95  ? 9.618   -10.230 50.041  1.00 84.11  ? 281 LYS A CD  1 
ATOM   3277 C CE  . LYS B 1 95  ? 8.774   -11.487 50.147  1.00 86.76  ? 281 LYS A CE  1 
ATOM   3278 N NZ  . LYS B 1 95  ? 7.368   -11.191 49.766  1.00 84.18  ? 281 LYS A NZ  1 
ATOM   3279 N N   . SER B 1 96  ? 12.143  -7.802  46.373  1.00 82.67  ? 282 SER A N   1 
ATOM   3280 C CA  . SER B 1 96  ? 12.770  -8.516  45.269  1.00 78.55  ? 282 SER A CA  1 
ATOM   3281 C C   . SER B 1 96  ? 14.254  -8.744  45.530  1.00 80.98  ? 282 SER A C   1 
ATOM   3282 O O   . SER B 1 96  ? 14.744  -9.875  45.428  1.00 84.73  ? 282 SER A O   1 
ATOM   3283 C CB  . SER B 1 96  ? 12.554  -7.741  43.973  1.00 76.84  ? 282 SER A CB  1 
ATOM   3284 O OG  . SER B 1 96  ? 12.774  -8.581  42.867  1.00 81.99  ? 282 SER A OG  1 
ATOM   3285 N N   . PHE B 1 97  ? 14.987  -7.683  45.870  1.00 81.33  ? 283 PHE A N   1 
ATOM   3286 C CA  . PHE B 1 97  ? 16.398  -7.803  46.213  1.00 79.17  ? 283 PHE A CA  1 
ATOM   3287 C C   . PHE B 1 97  ? 16.621  -7.884  47.720  1.00 82.52  ? 283 PHE A C   1 
ATOM   3288 O O   . PHE B 1 97  ? 17.767  -7.799  48.174  1.00 82.41  ? 283 PHE A O   1 
ATOM   3289 C CB  . PHE B 1 97  ? 17.219  -6.663  45.592  1.00 70.89  ? 283 PHE A CB  1 
ATOM   3290 C CG  . PHE B 1 97  ? 16.738  -5.279  45.936  1.00 66.08  ? 283 PHE A CG  1 
ATOM   3291 C CD1 . PHE B 1 97  ? 17.088  -4.683  47.135  1.00 65.97  ? 283 PHE A CD1 1 
ATOM   3292 C CD2 . PHE B 1 97  ? 15.980  -4.555  45.032  1.00 70.76  ? 283 PHE A CD2 1 
ATOM   3293 C CE1 . PHE B 1 97  ? 16.666  -3.404  47.437  1.00 66.76  ? 283 PHE A CE1 1 
ATOM   3294 C CE2 . PHE B 1 97  ? 15.555  -3.275  45.330  1.00 71.69  ? 283 PHE A CE2 1 
ATOM   3295 C CZ  . PHE B 1 97  ? 15.899  -2.699  46.534  1.00 71.77  ? 283 PHE A CZ  1 
ATOM   3296 N N   . GLY B 1 98  ? 15.548  -8.033  48.494  1.00 78.53  ? 284 GLY A N   1 
ATOM   3297 C CA  . GLY B 1 98  ? 15.628  -8.396  49.904  1.00 77.24  ? 284 GLY A CA  1 
ATOM   3298 C C   . GLY B 1 98  ? 16.288  -7.390  50.822  1.00 79.34  ? 284 GLY A C   1 
ATOM   3299 O O   . GLY B 1 98  ? 17.052  -7.777  51.716  1.00 75.93  ? 284 GLY A O   1 
ATOM   3300 N N   . TRP B 1 99  ? 16.014  -6.102  50.623  1.00 80.87  ? 285 TRP A N   1 
ATOM   3301 C CA  . TRP B 1 99  ? 16.416  -5.067  51.572  1.00 78.64  ? 285 TRP A CA  1 
ATOM   3302 C C   . TRP B 1 99  ? 15.192  -4.645  52.378  1.00 79.60  ? 285 TRP A C   1 
ATOM   3303 O O   . TRP B 1 99  ? 14.577  -3.614  52.117  1.00 86.78  ? 285 TRP A O   1 
ATOM   3304 C CB  . TRP B 1 99  ? 17.022  -3.877  50.838  1.00 75.17  ? 285 TRP A CB  1 
ATOM   3305 C CG  . TRP B 1 99  ? 18.367  -4.112  50.241  1.00 72.71  ? 285 TRP A CG  1 
ATOM   3306 C CD1 . TRP B 1 99  ? 18.992  -5.310  50.059  1.00 68.18  ? 285 TRP A CD1 1 
ATOM   3307 C CD2 . TRP B 1 99  ? 19.261  -3.110  49.747  1.00 72.45  ? 285 TRP A CD2 1 
ATOM   3308 N NE1 . TRP B 1 99  ? 20.224  -5.113  49.480  1.00 74.12  ? 285 TRP A NE1 1 
ATOM   3309 C CE2 . TRP B 1 99  ? 20.411  -3.770  49.279  1.00 70.50  ? 285 TRP A CE2 1 
ATOM   3310 C CE3 . TRP B 1 99  ? 19.198  -1.716  49.658  1.00 68.86  ? 285 TRP A CE3 1 
ATOM   3311 C CZ2 . TRP B 1 99  ? 21.486  -3.086  48.727  1.00 70.01  ? 285 TRP A CZ2 1 
ATOM   3312 C CZ3 . TRP B 1 99  ? 20.267  -1.039  49.114  1.00 68.49  ? 285 TRP A CZ3 1 
ATOM   3313 C CH2 . TRP B 1 99  ? 21.394  -1.723  48.651  1.00 71.40  ? 285 TRP A CH2 1 
ATOM   3314 N N   . GLU B 1 100 ? 14.870  -5.413  53.417  1.00 79.01  ? 286 GLU A N   1 
ATOM   3315 C CA  . GLU B 1 100 ? 13.647  -5.144  54.161  1.00 87.59  ? 286 GLU A CA  1 
ATOM   3316 C C   . GLU B 1 100 ? 13.871  -4.819  55.628  1.00 91.79  ? 286 GLU A C   1 
ATOM   3317 O O   . GLU B 1 100 ? 12.900  -4.492  56.321  1.00 93.14  ? 286 GLU A O   1 
ATOM   3318 C CB  . GLU B 1 100 ? 12.675  -6.332  54.066  1.00 85.69  ? 286 GLU A CB  1 
ATOM   3319 C CG  . GLU B 1 100 ? 12.028  -6.512  52.703  1.00 83.08  ? 286 GLU A CG  1 
ATOM   3320 C CD  . GLU B 1 100 ? 11.459  -7.903  52.517  1.00 90.20  ? 286 GLU A CD  1 
ATOM   3321 O OE1 . GLU B 1 100 ? 12.171  -8.882  52.820  1.00 92.15  ? 286 GLU A OE1 1 
ATOM   3322 O OE2 . GLU B 1 100 ? 10.294  -8.015  52.082  1.00 89.58  ? 286 GLU A OE2 1 
ATOM   3323 N N   . THR B 1 101 ? 15.099  -4.910  56.122  1.00 90.82  ? 287 THR A N   1 
ATOM   3324 C CA  . THR B 1 101 ? 15.408  -4.443  57.460  1.00 86.86  ? 287 THR A CA  1 
ATOM   3325 C C   . THR B 1 101 ? 15.510  -2.921  57.482  1.00 89.04  ? 287 THR A C   1 
ATOM   3326 O O   . THR B 1 101 ? 15.708  -2.272  56.451  1.00 84.33  ? 287 THR A O   1 
ATOM   3327 C CB  . THR B 1 101 ? 16.707  -5.065  57.965  1.00 91.40  ? 287 THR A CB  1 
ATOM   3328 O OG1 . THR B 1 101 ? 17.337  -4.171  58.893  1.00 101.29 ? 287 THR A OG1 1 
ATOM   3329 C CG2 . THR B 1 101 ? 17.647  -5.355  56.807  1.00 86.22  ? 287 THR A CG2 1 
ATOM   3330 N N   . LEU B 1 102 ? 15.347  -2.350  58.679  1.00 88.56  ? 288 LEU A N   1 
ATOM   3331 C CA  . LEU B 1 102 ? 15.375  -0.896  58.812  1.00 88.21  ? 288 LEU A CA  1 
ATOM   3332 C C   . LEU B 1 102 ? 16.690  -0.299  58.336  1.00 88.76  ? 288 LEU A C   1 
ATOM   3333 O O   . LEU B 1 102 ? 16.711  0.839   57.854  1.00 92.45  ? 288 LEU A O   1 
ATOM   3334 C CB  . LEU B 1 102 ? 15.142  -0.483  60.262  1.00 87.78  ? 288 LEU A CB  1 
ATOM   3335 C CG  . LEU B 1 102 ? 13.716  -0.140  60.661  1.00 90.50  ? 288 LEU A CG  1 
ATOM   3336 C CD1 . LEU B 1 102 ? 13.671  0.210   62.132  1.00 87.17  ? 288 LEU A CD1 1 
ATOM   3337 C CD2 . LEU B 1 102 ? 13.209  1.013   59.810  1.00 87.10  ? 288 LEU A CD2 1 
ATOM   3338 N N   . ASP B 1 103 ? 17.791  -1.041  58.448  1.00 86.63  ? 289 ASP A N   1 
ATOM   3339 C CA  . ASP B 1 103 ? 19.106  -0.513  58.121  1.00 81.45  ? 289 ASP A CA  1 
ATOM   3340 C C   . ASP B 1 103 ? 19.620  -0.995  56.775  1.00 76.14  ? 289 ASP A C   1 
ATOM   3341 O O   . ASP B 1 103 ? 20.768  -0.709  56.430  1.00 83.56  ? 289 ASP A O   1 
ATOM   3342 C CB  . ASP B 1 103 ? 20.110  -0.898  59.209  1.00 94.15  ? 289 ASP A CB  1 
ATOM   3343 C CG  . ASP B 1 103 ? 20.069  -2.384  59.544  1.00 98.42  ? 289 ASP A CG  1 
ATOM   3344 O OD1 . ASP B 1 103 ? 19.421  -3.155  58.802  1.00 100.34 ? 289 ASP A OD1 1 
ATOM   3345 O OD2 . ASP B 1 103 ? 20.714  -2.786  60.538  1.00 95.04  ? 289 ASP A OD2 1 
ATOM   3346 N N   . SER B 1 104 ? 18.791  -1.697  55.999  1.00 82.28  ? 290 SER A N   1 
ATOM   3347 C CA  . SER B 1 104 ? 19.268  -2.293  54.755  1.00 80.72  ? 290 SER A CA  1 
ATOM   3348 C C   . SER B 1 104 ? 19.760  -1.224  53.788  1.00 71.45  ? 290 SER A C   1 
ATOM   3349 O O   . SER B 1 104 ? 20.828  -1.361  53.182  1.00 76.49  ? 290 SER A O   1 
ATOM   3350 C CB  . SER B 1 104 ? 18.165  -3.141  54.121  1.00 83.87  ? 290 SER A CB  1 
ATOM   3351 O OG  . SER B 1 104 ? 16.943  -2.428  54.038  1.00 85.04  ? 290 SER A OG  1 
ATOM   3352 N N   . PHE B 1 105 ? 18.983  -0.153  53.626  1.00 74.13  ? 291 PHE A N   1 
ATOM   3353 C CA  . PHE B 1 105 ? 19.344  0.917   52.703  1.00 76.62  ? 291 PHE A CA  1 
ATOM   3354 C C   . PHE B 1 105 ? 20.378  1.873   53.289  1.00 78.66  ? 291 PHE A C   1 
ATOM   3355 O O   . PHE B 1 105 ? 21.169  2.456   52.540  1.00 83.21  ? 291 PHE A O   1 
ATOM   3356 C CB  . PHE B 1 105 ? 18.089  1.683   52.289  1.00 68.04  ? 291 PHE A CB  1 
ATOM   3357 C CG  . PHE B 1 105 ? 17.247  0.947   51.290  1.00 73.88  ? 291 PHE A CG  1 
ATOM   3358 C CD1 . PHE B 1 105 ? 16.324  0.003   51.706  1.00 70.11  ? 291 PHE A CD1 1 
ATOM   3359 C CD2 . PHE B 1 105 ? 17.400  1.174   49.935  1.00 71.01  ? 291 PHE A CD2 1 
ATOM   3360 C CE1 . PHE B 1 105 ? 15.559  -0.685  50.787  1.00 70.78  ? 291 PHE A CE1 1 
ATOM   3361 C CE2 . PHE B 1 105 ? 16.639  0.487   49.013  1.00 68.93  ? 291 PHE A CE2 1 
ATOM   3362 C CZ  . PHE B 1 105 ? 15.718  -0.443  49.440  1.00 69.01  ? 291 PHE A CZ  1 
ATOM   3363 N N   . MET B 1 106 ? 20.397  2.037   54.613  1.00 75.97  ? 292 MET A N   1 
ATOM   3364 C CA  . MET B 1 106 ? 21.322  2.955   55.266  1.00 74.84  ? 292 MET A CA  1 
ATOM   3365 C C   . MET B 1 106 ? 22.727  2.390   55.358  1.00 81.83  ? 292 MET A C   1 
ATOM   3366 O O   . MET B 1 106 ? 23.686  3.153   55.533  1.00 79.78  ? 292 MET A O   1 
ATOM   3367 C CB  . MET B 1 106 ? 20.824  3.247   56.677  1.00 81.26  ? 292 MET A CB  1 
ATOM   3368 C CG  . MET B 1 106 ? 19.624  4.143   56.728  1.00 81.71  ? 292 MET A CG  1 
ATOM   3369 S SD  . MET B 1 106 ? 19.217  4.614   58.417  1.00 87.47  ? 292 MET A SD  1 
ATOM   3370 C CE  . MET B 1 106 ? 20.769  5.318   58.972  1.00 98.19  ? 292 MET A CE  1 
ATOM   3371 N N   . GLN B 1 107 ? 22.854  1.066   55.243  1.00 83.95  ? 293 GLN A N   1 
ATOM   3372 C CA  . GLN B 1 107 ? 24.141  0.383   55.289  1.00 77.84  ? 293 GLN A CA  1 
ATOM   3373 C C   . GLN B 1 107 ? 24.867  0.428   53.961  1.00 74.78  ? 293 GLN A C   1 
ATOM   3374 O O   . GLN B 1 107 ? 26.100  0.412   53.941  1.00 81.36  ? 293 GLN A O   1 
ATOM   3375 C CB  . GLN B 1 107 ? 23.928  -1.078  55.689  1.00 76.35  ? 293 GLN A CB  1 
ATOM   3376 C CG  . GLN B 1 107 ? 23.793  -1.329  57.165  1.00 83.23  ? 293 GLN A CG  1 
ATOM   3377 C CD  . GLN B 1 107 ? 23.279  -2.723  57.464  1.00 88.55  ? 293 GLN A CD  1 
ATOM   3378 O OE1 . GLN B 1 107 ? 23.285  -3.608  56.601  1.00 91.45  ? 293 GLN A OE1 1 
ATOM   3379 N NE2 . GLN B 1 107 ? 22.804  -2.920  58.687  1.00 97.24  ? 293 GLN A NE2 1 
ATOM   3380 N N   . HIS B 1 108 ? 24.134  0.463   52.855  1.00 67.48  ? 294 HIS A N   1 
ATOM   3381 C CA  . HIS B 1 108 ? 24.727  0.402   51.534  1.00 68.44  ? 294 HIS A CA  1 
ATOM   3382 C C   . HIS B 1 108 ? 24.938  1.802   50.965  1.00 68.77  ? 294 HIS A C   1 
ATOM   3383 O O   . HIS B 1 108 ? 24.684  2.820   51.614  1.00 70.58  ? 294 HIS A O   1 
ATOM   3384 C CB  . HIS B 1 108 ? 23.862  -0.448  50.612  1.00 67.53  ? 294 HIS A CB  1 
ATOM   3385 C CG  . HIS B 1 108 ? 23.753  -1.876  51.044  1.00 70.47  ? 294 HIS A CG  1 
ATOM   3386 N ND1 . HIS B 1 108 ? 23.089  -2.256  52.191  1.00 76.78  ? 294 HIS A ND1 1 
ATOM   3387 C CD2 . HIS B 1 108 ? 24.230  -3.015  50.490  1.00 73.18  ? 294 HIS A CD2 1 
ATOM   3388 C CE1 . HIS B 1 108 ? 23.156  -3.569  52.319  1.00 82.02  ? 294 HIS A CE1 1 
ATOM   3389 N NE2 . HIS B 1 108 ? 23.843  -4.054  51.300  1.00 80.68  ? 294 HIS A NE2 1 
ATOM   3390 N N   . ASP B 1 109 ? 25.409  1.839   49.724  1.00 64.80  ? 295 ASP A N   1 
ATOM   3391 C CA  . ASP B 1 109 ? 25.714  3.053   48.990  1.00 60.02  ? 295 ASP A CA  1 
ATOM   3392 C C   . ASP B 1 109 ? 24.726  3.212   47.839  1.00 61.94  ? 295 ASP A C   1 
ATOM   3393 O O   . ASP B 1 109 ? 24.065  2.253   47.433  1.00 67.34  ? 295 ASP A O   1 
ATOM   3394 C CB  . ASP B 1 109 ? 27.152  3.004   48.453  1.00 70.09  ? 295 ASP A CB  1 
ATOM   3395 C CG  . ASP B 1 109 ? 28.194  2.918   49.560  1.00 71.32  ? 295 ASP A CG  1 
ATOM   3396 O OD1 . ASP B 1 109 ? 27.979  3.517   50.635  1.00 71.47  ? 295 ASP A OD1 1 
ATOM   3397 O OD2 . ASP B 1 109 ? 29.237  2.259   49.350  1.00 72.70  ? 295 ASP A OD2 1 
ATOM   3398 N N   . VAL B 1 110 ? 24.625  4.436   47.308  1.00 59.72  ? 296 VAL A N   1 
ATOM   3399 C CA  . VAL B 1 110 ? 23.850  4.625   46.082  1.00 58.56  ? 296 VAL A CA  1 
ATOM   3400 C C   . VAL B 1 110 ? 24.437  3.781   44.962  1.00 66.11  ? 296 VAL A C   1 
ATOM   3401 O O   . VAL B 1 110 ? 23.705  3.212   44.142  1.00 68.98  ? 296 VAL A O   1 
ATOM   3402 C CB  . VAL B 1 110 ? 23.784  6.112   45.683  1.00 58.10  ? 296 VAL A CB  1 
ATOM   3403 C CG1 . VAL B 1 110 ? 22.879  6.855   46.595  1.00 64.95  ? 296 VAL A CG1 1 
ATOM   3404 C CG2 . VAL B 1 110 ? 25.158  6.744   45.700  1.00 64.75  ? 296 VAL A CG2 1 
ATOM   3405 N N   . GLN B 1 111 ? 25.767  3.681   44.918  1.00 64.63  ? 297 GLN A N   1 
ATOM   3406 C CA  . GLN B 1 111 ? 26.430  2.874   43.901  1.00 68.26  ? 297 GLN A CA  1 
ATOM   3407 C C   . GLN B 1 111 ? 26.008  1.413   43.998  1.00 70.16  ? 297 GLN A C   1 
ATOM   3408 O O   . GLN B 1 111 ? 25.666  0.784   42.990  1.00 67.39  ? 297 GLN A O   1 
ATOM   3409 C CB  . GLN B 1 111 ? 27.945  2.981   44.067  1.00 72.12  ? 297 GLN A CB  1 
ATOM   3410 C CG  . GLN B 1 111 ? 28.495  4.388   44.154  1.00 71.05  ? 297 GLN A CG  1 
ATOM   3411 C CD  . GLN B 1 111 ? 28.619  4.878   45.581  1.00 67.61  ? 297 GLN A CD  1 
ATOM   3412 O OE1 . GLN B 1 111 ? 27.624  5.056   46.272  1.00 66.93  ? 297 GLN A OE1 1 
ATOM   3413 N NE2 . GLN B 1 111 ? 29.850  5.054   46.044  1.00 74.25  ? 297 GLN A NE2 1 
ATOM   3414 N N   . GLU B 1 112 ? 26.018  0.861   45.215  1.00 69.71  ? 298 GLU A N   1 
ATOM   3415 C CA  . GLU B 1 112 ? 25.702  -0.551  45.391  1.00 70.30  ? 298 GLU A CA  1 
ATOM   3416 C C   . GLU B 1 112 ? 24.275  -0.855  44.962  1.00 67.29  ? 298 GLU A C   1 
ATOM   3417 O O   . GLU B 1 112 ? 24.019  -1.885  44.326  1.00 69.65  ? 298 GLU A O   1 
ATOM   3418 C CB  . GLU B 1 112 ? 25.932  -0.975  46.842  1.00 75.87  ? 298 GLU A CB  1 
ATOM   3419 C CG  . GLU B 1 112 ? 27.366  -0.849  47.326  1.00 59.85  ? 298 GLU A CG  1 
ATOM   3420 C CD  . GLU B 1 112 ? 27.568  -1.524  48.665  1.00 68.49  ? 298 GLU A CD  1 
ATOM   3421 O OE1 . GLU B 1 112 ? 26.932  -1.090  49.648  1.00 65.89  ? 298 GLU A OE1 1 
ATOM   3422 O OE2 . GLU B 1 112 ? 28.347  -2.499  48.733  1.00 75.90  ? 298 GLU A OE2 1 
ATOM   3423 N N   . LEU B 1 113 ? 23.326  0.016   45.316  1.00 69.67  ? 299 LEU A N   1 
ATOM   3424 C CA  . LEU B 1 113 ? 21.945  -0.207  44.898  1.00 73.90  ? 299 LEU A CA  1 
ATOM   3425 C C   . LEU B 1 113 ? 21.808  -0.130  43.383  1.00 64.49  ? 299 LEU A C   1 
ATOM   3426 O O   . LEU B 1 113 ? 21.114  -0.952  42.774  1.00 67.82  ? 299 LEU A O   1 
ATOM   3427 C CB  . LEU B 1 113 ? 21.008  0.799   45.564  1.00 68.98  ? 299 LEU A CB  1 
ATOM   3428 C CG  . LEU B 1 113 ? 19.541  0.475   45.284  1.00 62.84  ? 299 LEU A CG  1 
ATOM   3429 C CD1 . LEU B 1 113 ? 19.234  -0.933  45.761  1.00 64.68  ? 299 LEU A CD1 1 
ATOM   3430 C CD2 . LEU B 1 113 ? 18.607  1.483   45.927  1.00 62.84  ? 299 LEU A CD2 1 
ATOM   3431 N N   . CYS B 1 114 ? 22.467  0.849   42.757  1.00 63.70  ? 300 CYS A N   1 
ATOM   3432 C CA  . CYS B 1 114 ? 22.436  0.946   41.300  1.00 66.92  ? 300 CYS A CA  1 
ATOM   3433 C C   . CYS B 1 114 ? 23.103  -0.260  40.650  1.00 70.68  ? 300 CYS A C   1 
ATOM   3434 O O   . CYS B 1 114 ? 22.656  -0.732  39.598  1.00 75.42  ? 300 CYS A O   1 
ATOM   3435 C CB  . CYS B 1 114 ? 23.104  2.241   40.841  1.00 62.89  ? 300 CYS A CB  1 
ATOM   3436 S SG  . CYS B 1 114 ? 22.963  2.554   39.076  1.00 84.31  ? 300 CYS A SG  1 
ATOM   3437 N N   . ARG B 1 115 ? 24.181  -0.769  41.255  1.00 66.66  ? 301 ARG A N   1 
ATOM   3438 C CA  . ARG B 1 115 ? 24.824  -1.968  40.724  1.00 70.37  ? 301 ARG A CA  1 
ATOM   3439 C C   . ARG B 1 115 ? 23.908  -3.178  40.837  1.00 73.58  ? 301 ARG A C   1 
ATOM   3440 O O   . ARG B 1 115 ? 23.809  -3.978  39.901  1.00 78.86  ? 301 ARG A O   1 
ATOM   3441 C CB  . ARG B 1 115 ? 26.131  -2.250  41.464  1.00 76.87  ? 301 ARG A CB  1 
ATOM   3442 C CG  . ARG B 1 115 ? 27.308  -1.357  41.113  1.00 81.33  ? 301 ARG A CG  1 
ATOM   3443 C CD  . ARG B 1 115 ? 28.181  -1.191  42.358  1.00 98.99  ? 301 ARG A CD  1 
ATOM   3444 N NE  . ARG B 1 115 ? 29.292  -0.259  42.196  1.00 96.92  ? 301 ARG A NE  1 
ATOM   3445 C CZ  . ARG B 1 115 ? 30.013  0.215   43.205  1.00 92.00  ? 301 ARG A CZ  1 
ATOM   3446 N NH1 . ARG B 1 115 ? 29.753  -0.125  44.459  1.00 82.95  ? 301 ARG A NH1 1 
ATOM   3447 N NH2 . ARG B 1 115 ? 31.022  1.045   42.951  1.00 89.21  ? 301 ARG A NH2 1 
ATOM   3448 N N   . VAL B 1 116 ? 23.234  -3.328  41.979  1.00 71.34  ? 302 VAL A N   1 
ATOM   3449 C CA  . VAL B 1 116 ? 22.344  -4.468  42.188  1.00 68.63  ? 302 VAL A CA  1 
ATOM   3450 C C   . VAL B 1 116 ? 21.225  -4.475  41.156  1.00 71.98  ? 302 VAL A C   1 
ATOM   3451 O O   . VAL B 1 116 ? 20.900  -5.519  40.575  1.00 74.10  ? 302 VAL A O   1 
ATOM   3452 C CB  . VAL B 1 116 ? 21.799  -4.454  43.627  1.00 78.50  ? 302 VAL A CB  1 
ATOM   3453 C CG1 . VAL B 1 116 ? 20.594  -5.369  43.755  1.00 80.04  ? 302 VAL A CG1 1 
ATOM   3454 C CG2 . VAL B 1 116 ? 22.896  -4.873  44.598  1.00 80.84  ? 302 VAL A CG2 1 
ATOM   3455 N N   . LEU B 1 117 ? 20.619  -3.316  40.907  1.00 68.64  ? 303 LEU A N   1 
ATOM   3456 C CA  . LEU B 1 117 ? 19.545  -3.256  39.924  1.00 71.34  ? 303 LEU A CA  1 
ATOM   3457 C C   . LEU B 1 117 ? 20.071  -3.511  38.515  1.00 74.61  ? 303 LEU A C   1 
ATOM   3458 O O   . LEU B 1 117 ? 19.545  -4.366  37.793  1.00 79.81  ? 303 LEU A O   1 
ATOM   3459 C CB  . LEU B 1 117 ? 18.840  -1.903  40.006  1.00 67.40  ? 303 LEU A CB  1 
ATOM   3460 C CG  . LEU B 1 117 ? 18.170  -1.582  41.342  1.00 59.00  ? 303 LEU A CG  1 
ATOM   3461 C CD1 . LEU B 1 117 ? 17.633  -0.164  41.336  1.00 57.80  ? 303 LEU A CD1 1 
ATOM   3462 C CD2 . LEU B 1 117 ? 17.055  -2.579  41.627  1.00 60.61  ? 303 LEU A CD2 1 
ATOM   3463 N N   . LEU B 1 118 ? 21.124  -2.793  38.111  1.00 70.89  ? 304 LEU A N   1 
ATOM   3464 C CA  . LEU B 1 118 ? 21.589  -2.879  36.727  1.00 67.84  ? 304 LEU A CA  1 
ATOM   3465 C C   . LEU B 1 118 ? 22.206  -4.237  36.419  1.00 74.01  ? 304 LEU A C   1 
ATOM   3466 O O   . LEU B 1 118 ? 22.039  -4.757  35.309  1.00 77.30  ? 304 LEU A O   1 
ATOM   3467 C CB  . LEU B 1 118 ? 22.578  -1.754  36.418  1.00 60.05  ? 304 LEU A CB  1 
ATOM   3468 C CG  . LEU B 1 118 ? 22.013  -0.398  35.978  1.00 66.78  ? 304 LEU A CG  1 
ATOM   3469 C CD1 . LEU B 1 118 ? 20.836  0.059   36.828  1.00 65.17  ? 304 LEU A CD1 1 
ATOM   3470 C CD2 . LEU B 1 118 ? 23.114  0.651   35.986  1.00 67.23  ? 304 LEU A CD2 1 
ATOM   3471 N N   . ASP B 1 119 ? 22.932  -4.823  37.375  1.00 76.19  ? 305 ASP A N   1 
ATOM   3472 C CA  . ASP B 1 119 ? 23.498  -6.151  37.150  1.00 75.87  ? 305 ASP A CA  1 
ATOM   3473 C C   . ASP B 1 119 ? 22.397  -7.178  36.919  1.00 80.82  ? 305 ASP A C   1 
ATOM   3474 O O   . ASP B 1 119 ? 22.539  -8.072  36.076  1.00 85.87  ? 305 ASP A O   1 
ATOM   3475 C CB  . ASP B 1 119 ? 24.387  -6.566  38.326  1.00 81.07  ? 305 ASP A CB  1 
ATOM   3476 C CG  . ASP B 1 119 ? 25.693  -5.776  38.391  1.00 83.32  ? 305 ASP A CG  1 
ATOM   3477 O OD1 . ASP B 1 119 ? 26.234  -5.408  37.325  1.00 85.93  ? 305 ASP A OD1 1 
ATOM   3478 O OD2 . ASP B 1 119 ? 26.174  -5.519  39.517  1.00 78.45  ? 305 ASP A OD2 1 
ATOM   3479 N N   . ASN B 1 120 ? 21.291  -7.069  37.661  1.00 80.87  ? 306 ASN A N   1 
ATOM   3480 C CA  . ASN B 1 120 ? 20.170  -7.981  37.456  1.00 73.57  ? 306 ASN A CA  1 
ATOM   3481 C C   . ASN B 1 120 ? 19.607  -7.843  36.051  1.00 80.91  ? 306 ASN A C   1 
ATOM   3482 O O   . ASN B 1 120 ? 19.371  -8.840  35.361  1.00 89.25  ? 306 ASN A O   1 
ATOM   3483 C CB  . ASN B 1 120 ? 19.075  -7.715  38.488  1.00 67.29  ? 306 ASN A CB  1 
ATOM   3484 C CG  . ASN B 1 120 ? 19.246  -8.533  39.742  1.00 73.49  ? 306 ASN A CG  1 
ATOM   3485 O OD1 . ASN B 1 120 ? 18.758  -9.660  39.830  1.00 76.35  ? 306 ASN A OD1 1 
ATOM   3486 N ND2 . ASN B 1 120 ? 19.933  -7.970  40.729  1.00 78.62  ? 306 ASN A ND2 1 
ATOM   3487 N N   . VAL B 1 121 ? 19.390  -6.603  35.611  1.00 80.84  ? 307 VAL A N   1 
ATOM   3488 C CA  . VAL B 1 121 ? 18.831  -6.363  34.285  1.00 71.11  ? 307 VAL A CA  1 
ATOM   3489 C C   . VAL B 1 121 ? 19.818  -6.787  33.207  1.00 80.96  ? 307 VAL A C   1 
ATOM   3490 O O   . VAL B 1 121 ? 19.450  -7.464  32.240  1.00 77.09  ? 307 VAL A O   1 
ATOM   3491 C CB  . VAL B 1 121 ? 18.440  -4.883  34.135  1.00 69.20  ? 307 VAL A CB  1 
ATOM   3492 C CG1 . VAL B 1 121 ? 18.239  -4.541  32.673  1.00 74.27  ? 307 VAL A CG1 1 
ATOM   3493 C CG2 . VAL B 1 121 ? 17.190  -4.582  34.947  1.00 78.96  ? 307 VAL A CG2 1 
ATOM   3494 N N   . GLU B 1 122 ? 21.091  -6.411  33.371  1.00 81.18  ? 308 GLU A N   1 
ATOM   3495 C CA  . GLU B 1 122 ? 22.110  -6.758  32.386  1.00 77.00  ? 308 GLU A CA  1 
ATOM   3496 C C   . GLU B 1 122 ? 22.240  -8.267  32.235  1.00 79.90  ? 308 GLU A C   1 
ATOM   3497 O O   . GLU B 1 122 ? 22.358  -8.779  31.115  1.00 79.00  ? 308 GLU A O   1 
ATOM   3498 C CB  . GLU B 1 122 ? 23.446  -6.145  32.798  1.00 76.98  ? 308 GLU A CB  1 
ATOM   3499 C CG  . GLU B 1 122 ? 24.618  -6.491  31.899  1.00 84.24  ? 308 GLU A CG  1 
ATOM   3500 C CD  . GLU B 1 122 ? 25.936  -5.984  32.462  1.00 90.45  ? 308 GLU A CD  1 
ATOM   3501 O OE1 . GLU B 1 122 ? 25.901  -5.152  33.396  1.00 89.58  ? 308 GLU A OE1 1 
ATOM   3502 O OE2 . GLU B 1 122 ? 27.006  -6.424  31.986  1.00 92.61  ? 308 GLU A OE2 1 
ATOM   3503 N N   . ASN B 1 123 ? 22.212  -8.996  33.353  1.00 81.58  ? 309 ASN A N   1 
ATOM   3504 C CA  . ASN B 1 123 ? 22.250  -10.453 33.285  1.00 88.73  ? 309 ASN A CA  1 
ATOM   3505 C C   . ASN B 1 123 ? 20.969  -11.013 32.682  1.00 86.20  ? 309 ASN A C   1 
ATOM   3506 O O   . ASN B 1 123 ? 21.010  -11.993 31.929  1.00 88.61  ? 309 ASN A O   1 
ATOM   3507 C CB  . ASN B 1 123 ? 22.485  -11.041 34.677  1.00 91.42  ? 309 ASN A CB  1 
ATOM   3508 C CG  . ASN B 1 123 ? 22.954  -12.489 34.632  1.00 103.89 ? 309 ASN A CG  1 
ATOM   3509 O OD1 . ASN B 1 123 ? 23.396  -12.988 33.594  1.00 103.19 ? 309 ASN A OD1 1 
ATOM   3510 N ND2 . ASN B 1 123 ? 22.833  -13.180 35.762  1.00 107.08 ? 309 ASN A ND2 1 
ATOM   3511 N N   . LYS B 1 124 ? 19.822  -10.400 32.990  1.00 86.42  ? 310 LYS A N   1 
ATOM   3512 C CA  . LYS B 1 124 ? 18.563  -10.870 32.420  1.00 82.10  ? 310 LYS A CA  1 
ATOM   3513 C C   . LYS B 1 124 ? 18.540  -10.672 30.911  1.00 81.35  ? 310 LYS A C   1 
ATOM   3514 O O   . LYS B 1 124 ? 18.014  -11.514 30.174  1.00 76.33  ? 310 LYS A O   1 
ATOM   3515 C CB  . LYS B 1 124 ? 17.385  -10.150 33.076  1.00 81.42  ? 310 LYS A CB  1 
ATOM   3516 C CG  . LYS B 1 124 ? 16.037  -10.788 32.781  1.00 80.76  ? 310 LYS A CG  1 
ATOM   3517 C CD  . LYS B 1 124 ? 15.942  -12.150 33.443  1.00 75.86  ? 310 LYS A CD  1 
ATOM   3518 C CE  . LYS B 1 124 ? 14.649  -12.852 33.094  1.00 81.06  ? 310 LYS A CE  1 
ATOM   3519 N NZ  . LYS B 1 124 ? 14.506  -14.134 33.837  1.00 76.54  ? 310 LYS A NZ  1 
ATOM   3520 N N   . MET B 1 125 ? 19.111  -9.567  30.437  1.00 79.33  ? 311 MET A N   1 
ATOM   3521 C CA  . MET B 1 125 ? 19.157  -9.271  29.014  1.00 77.19  ? 311 MET A CA  1 
ATOM   3522 C C   . MET B 1 125 ? 20.222  -10.072 28.274  1.00 78.84  ? 311 MET A C   1 
ATOM   3523 O O   . MET B 1 125 ? 20.254  -10.033 27.039  1.00 74.83  ? 311 MET A O   1 
ATOM   3524 C CB  . MET B 1 125 ? 19.409  -7.778  28.816  1.00 71.01  ? 311 MET A CB  1 
ATOM   3525 C CG  . MET B 1 125 ? 18.354  -6.904  29.464  1.00 76.60  ? 311 MET A CG  1 
ATOM   3526 S SD  . MET B 1 125 ? 18.651  -5.161  29.167  1.00 74.56  ? 311 MET A SD  1 
ATOM   3527 C CE  . MET B 1 125 ? 20.434  -5.129  29.333  1.00 79.66  ? 311 MET A CE  1 
ATOM   3528 N N   . LYS B 1 126 ? 21.096  -10.779 28.987  1.00 80.45  ? 312 LYS A N   1 
ATOM   3529 C CA  . LYS B 1 126 ? 22.073  -11.626 28.319  1.00 82.94  ? 312 LYS A CA  1 
ATOM   3530 C C   . LYS B 1 126 ? 21.359  -12.724 27.544  1.00 80.56  ? 312 LYS A C   1 
ATOM   3531 O O   . LYS B 1 126 ? 20.444  -13.372 28.059  1.00 81.75  ? 312 LYS A O   1 
ATOM   3532 C CB  . LYS B 1 126 ? 23.052  -12.225 29.332  1.00 88.74  ? 312 LYS A CB  1 
ATOM   3533 C CG  . LYS B 1 126 ? 23.989  -11.204 29.970  1.00 88.14  ? 312 LYS A CG  1 
ATOM   3534 C CD  . LYS B 1 126 ? 24.902  -11.845 31.006  1.00 82.10  ? 312 LYS A CD  1 
ATOM   3535 C CE  . LYS B 1 126 ? 25.814  -10.812 31.652  1.00 91.49  ? 312 LYS A CE  1 
ATOM   3536 N NZ  . LYS B 1 126 ? 26.679  -11.405 32.713  1.00 93.23  ? 312 LYS A NZ  1 
ATOM   3537 N N   . GLY B 1 127 ? 21.786  -12.934 26.304  1.00 82.47  ? 313 GLY A N   1 
ATOM   3538 C CA  . GLY B 1 127 ? 21.141  -13.890 25.432  1.00 81.54  ? 313 GLY A CA  1 
ATOM   3539 C C   . GLY B 1 127 ? 19.916  -13.372 24.718  1.00 79.59  ? 313 GLY A C   1 
ATOM   3540 O O   . GLY B 1 127 ? 19.209  -14.163 24.083  1.00 76.24  ? 313 GLY A O   1 
ATOM   3541 N N   . THR B 1 128 ? 19.638  -12.075 24.805  1.00 83.87  ? 314 THR A N   1 
ATOM   3542 C CA  . THR B 1 128 ? 18.495  -11.450 24.155  1.00 77.98  ? 314 THR A CA  1 
ATOM   3543 C C   . THR B 1 128 ? 18.982  -10.478 23.088  1.00 79.52  ? 314 THR A C   1 
ATOM   3544 O O   . THR B 1 128 ? 20.180  -10.213 22.951  1.00 80.86  ? 314 THR A O   1 
ATOM   3545 C CB  . THR B 1 128 ? 17.613  -10.712 25.169  1.00 75.01  ? 314 THR A CB  1 
ATOM   3546 O OG1 . THR B 1 128 ? 18.256  -9.491  25.557  1.00 73.09  ? 314 THR A OG1 1 
ATOM   3547 C CG2 . THR B 1 128 ? 17.383  -11.571 26.405  1.00 72.08  ? 314 THR A CG2 1 
ATOM   3548 N N   . CYS B 1 129 ? 18.029  -9.928  22.333  1.00 78.33  ? 315 CYS A N   1 
ATOM   3549 C CA  . CYS B 1 129 ? 18.382  -8.932  21.329  1.00 82.16  ? 315 CYS A CA  1 
ATOM   3550 C C   . CYS B 1 129 ? 18.880  -7.642  21.965  1.00 77.44  ? 315 CYS A C   1 
ATOM   3551 O O   . CYS B 1 129 ? 19.594  -6.877  21.311  1.00 79.82  ? 315 CYS A O   1 
ATOM   3552 C CB  . CYS B 1 129 ? 17.185  -8.626  20.430  1.00 84.15  ? 315 CYS A CB  1 
ATOM   3553 S SG  . CYS B 1 129 ? 15.903  -7.650  21.242  1.00 75.02  ? 315 CYS A SG  1 
ATOM   3554 N N   . VAL B 1 130 ? 18.532  -7.397  23.223  1.00 74.40  ? 316 VAL A N   1 
ATOM   3555 C CA  . VAL B 1 130 ? 18.877  -6.161  23.906  1.00 74.80  ? 316 VAL A CA  1 
ATOM   3556 C C   . VAL B 1 130 ? 20.087  -6.356  24.830  1.00 77.06  ? 316 VAL A C   1 
ATOM   3557 O O   . VAL B 1 130 ? 20.361  -5.516  25.692  1.00 69.14  ? 316 VAL A O   1 
ATOM   3558 C CB  . VAL B 1 130 ? 17.657  -5.594  24.655  1.00 67.84  ? 316 VAL A CB  1 
ATOM   3559 C CG1 . VAL B 1 130 ? 17.411  -6.340  25.963  1.00 71.39  ? 316 VAL A CG1 1 
ATOM   3560 C CG2 . VAL B 1 130 ? 17.776  -4.090  24.863  1.00 75.38  ? 316 VAL A CG2 1 
ATOM   3561 N N   . GLU B 1 131 ? 20.835  -7.441  24.636  1.00 75.37  ? 317 GLU A N   1 
ATOM   3562 C CA  . GLU B 1 131 ? 21.970  -7.759  25.493  1.00 79.28  ? 317 GLU A CA  1 
ATOM   3563 C C   . GLU B 1 131 ? 23.035  -6.670  25.435  1.00 80.23  ? 317 GLU A C   1 
ATOM   3564 O O   . GLU B 1 131 ? 23.338  -6.126  24.369  1.00 78.06  ? 317 GLU A O   1 
ATOM   3565 C CB  . GLU B 1 131 ? 22.576  -9.098  25.065  1.00 84.32  ? 317 GLU A CB  1 
ATOM   3566 C CG  . GLU B 1 131 ? 23.800  -9.540  25.847  1.00 75.38  ? 317 GLU A CG  1 
ATOM   3567 C CD  . GLU B 1 131 ? 24.394  -10.824 25.296  1.00 80.55  ? 317 GLU A CD  1 
ATOM   3568 O OE1 . GLU B 1 131 ? 23.657  -11.827 25.195  1.00 82.23  ? 317 GLU A OE1 1 
ATOM   3569 O OE2 . GLU B 1 131 ? 25.593  -10.825 24.947  1.00 86.25  ? 317 GLU A OE2 1 
ATOM   3570 N N   . GLY B 1 132 ? 23.611  -6.361  26.594  1.00 81.56  ? 318 GLY A N   1 
ATOM   3571 C CA  . GLY B 1 132 ? 24.668  -5.376  26.680  1.00 68.80  ? 318 GLY A CA  1 
ATOM   3572 C C   . GLY B 1 132 ? 24.223  -3.931  26.734  1.00 71.65  ? 318 GLY A C   1 
ATOM   3573 O O   . GLY B 1 132 ? 25.054  -3.041  26.526  1.00 70.67  ? 318 GLY A O   1 
ATOM   3574 N N   . THR B 1 133 ? 22.943  -3.658  26.991  1.00 79.43  ? 319 THR A N   1 
ATOM   3575 C CA  . THR B 1 133 ? 22.504  -2.268  27.064  1.00 72.67  ? 319 THR A CA  1 
ATOM   3576 C C   . THR B 1 133 ? 23.122  -1.549  28.257  1.00 66.09  ? 319 THR A C   1 
ATOM   3577 O O   . THR B 1 133 ? 23.596  -0.415  28.124  1.00 63.64  ? 319 THR A O   1 
ATOM   3578 C CB  . THR B 1 133 ? 20.979  -2.189  27.128  1.00 64.94  ? 319 THR A CB  1 
ATOM   3579 O OG1 . THR B 1 133 ? 20.426  -2.566  25.860  1.00 60.09  ? 319 THR A OG1 1 
ATOM   3580 C CG2 . THR B 1 133 ? 20.539  -0.775  27.469  1.00 57.51  ? 319 THR A CG2 1 
ATOM   3581 N N   . ILE B 1 134 ? 23.130  -2.191  29.429  1.00 71.12  ? 320 ILE A N   1 
ATOM   3582 C CA  . ILE B 1 134 ? 23.720  -1.559  30.609  1.00 68.36  ? 320 ILE A CA  1 
ATOM   3583 C C   . ILE B 1 134 ? 25.194  -1.241  30.402  1.00 63.37  ? 320 ILE A C   1 
ATOM   3584 O O   . ILE B 1 134 ? 25.597  -0.098  30.674  1.00 65.43  ? 320 ILE A O   1 
ATOM   3585 C CB  . ILE B 1 134 ? 23.461  -2.423  31.864  1.00 72.02  ? 320 ILE A CB  1 
ATOM   3586 C CG1 . ILE B 1 134 ? 22.109  -2.077  32.486  1.00 74.32  ? 320 ILE A CG1 1 
ATOM   3587 C CG2 . ILE B 1 134 ? 24.561  -2.217  32.893  1.00 64.85  ? 320 ILE A CG2 1 
ATOM   3588 C CD1 . ILE B 1 134 ? 20.927  -2.520  31.681  1.00 69.70  ? 320 ILE A CD1 1 
ATOM   3589 N N   . PRO B 1 135 ? 26.041  -2.167  29.933  1.00 70.70  ? 321 PRO A N   1 
ATOM   3590 C CA  . PRO B 1 135 ? 27.443  -1.787  29.686  1.00 67.91  ? 321 PRO A CA  1 
ATOM   3591 C C   . PRO B 1 135 ? 27.603  -0.662  28.679  1.00 66.98  ? 321 PRO A C   1 
ATOM   3592 O O   . PRO B 1 135 ? 28.457  0.210   28.870  1.00 75.05  ? 321 PRO A O   1 
ATOM   3593 C CB  . PRO B 1 135 ? 28.071  -3.092  29.180  1.00 64.94  ? 321 PRO A CB  1 
ATOM   3594 C CG  . PRO B 1 135 ? 27.220  -4.160  29.743  1.00 65.81  ? 321 PRO A CG  1 
ATOM   3595 C CD  . PRO B 1 135 ? 25.831  -3.611  29.721  1.00 74.65  ? 321 PRO A CD  1 
ATOM   3596 N N   . LYS B 1 136 ? 26.789  -0.632  27.622  1.00 59.96  ? 322 LYS A N   1 
ATOM   3597 C CA  . LYS B 1 136 ? 26.968  0.392   26.601  1.00 56.63  ? 322 LYS A CA  1 
ATOM   3598 C C   . LYS B 1 136 ? 26.497  1.760   27.066  1.00 61.62  ? 322 LYS A C   1 
ATOM   3599 O O   . LYS B 1 136 ? 26.861  2.765   26.449  1.00 72.26  ? 322 LYS A O   1 
ATOM   3600 C CB  . LYS B 1 136 ? 26.235  -0.016  25.316  1.00 58.85  ? 322 LYS A CB  1 
ATOM   3601 C CG  . LYS B 1 136 ? 24.786  0.450   25.239  1.00 72.01  ? 322 LYS A CG  1 
ATOM   3602 C CD  . LYS B 1 136 ? 24.074  -0.067  23.985  1.00 77.38  ? 322 LYS A CD  1 
ATOM   3603 C CE  . LYS B 1 136 ? 24.735  0.390   22.695  1.00 83.52  ? 322 LYS A CE  1 
ATOM   3604 N NZ  . LYS B 1 136 ? 24.004  -0.134  21.499  1.00 77.54  ? 322 LYS A NZ  1 
ATOM   3605 N N   . LEU B 1 137 ? 25.733  1.827   28.151  1.00 62.82  ? 323 LEU A N   1 
ATOM   3606 C CA  . LEU B 1 137 ? 25.249  3.095   28.675  1.00 60.82  ? 323 LEU A CA  1 
ATOM   3607 C C   . LEU B 1 137 ? 26.063  3.614   29.849  1.00 65.63  ? 323 LEU A C   1 
ATOM   3608 O O   . LEU B 1 137 ? 26.233  4.832   29.972  1.00 64.80  ? 323 LEU A O   1 
ATOM   3609 C CB  . LEU B 1 137 ? 23.786  2.961   29.116  1.00 62.18  ? 323 LEU A CB  1 
ATOM   3610 C CG  . LEU B 1 137 ? 22.711  2.881   28.036  1.00 62.07  ? 323 LEU A CG  1 
ATOM   3611 C CD1 . LEU B 1 137 ? 21.377  2.623   28.694  1.00 57.52  ? 323 LEU A CD1 1 
ATOM   3612 C CD2 . LEU B 1 137 ? 22.671  4.156   27.214  1.00 64.21  ? 323 LEU A CD2 1 
ATOM   3613 N N   . PHE B 1 138 ? 26.579  2.722   30.704  1.00 68.03  ? 324 PHE A N   1 
ATOM   3614 C CA  . PHE B 1 138 ? 27.147  3.107   31.990  1.00 65.20  ? 324 PHE A CA  1 
ATOM   3615 C C   . PHE B 1 138 ? 28.615  2.753   32.180  1.00 67.62  ? 324 PHE A C   1 
ATOM   3616 O O   . PHE B 1 138 ? 29.238  3.288   33.103  1.00 73.48  ? 324 PHE A O   1 
ATOM   3617 C CB  . PHE B 1 138 ? 26.358  2.463   33.144  1.00 63.71  ? 324 PHE A CB  1 
ATOM   3618 C CG  . PHE B 1 138 ? 24.888  2.791   33.143  1.00 61.06  ? 324 PHE A CG  1 
ATOM   3619 C CD1 . PHE B 1 138 ? 24.417  3.929   33.779  1.00 55.33  ? 324 PHE A CD1 1 
ATOM   3620 C CD2 . PHE B 1 138 ? 23.977  1.948   32.527  1.00 62.40  ? 324 PHE A CD2 1 
ATOM   3621 C CE1 . PHE B 1 138 ? 23.071  4.228   33.792  1.00 61.24  ? 324 PHE A CE1 1 
ATOM   3622 C CE2 . PHE B 1 138 ? 22.629  2.242   32.534  1.00 61.35  ? 324 PHE A CE2 1 
ATOM   3623 C CZ  . PHE B 1 138 ? 22.175  3.385   33.167  1.00 64.58  ? 324 PHE A CZ  1 
ATOM   3624 N N   . ARG B 1 139 ? 29.176  1.867   31.366  1.00 69.57  ? 325 ARG A N   1 
ATOM   3625 C CA  . ARG B 1 139 ? 30.541  1.401   31.559  1.00 65.56  ? 325 ARG A CA  1 
ATOM   3626 C C   . ARG B 1 139 ? 31.524  2.276   30.796  1.00 58.39  ? 325 ARG A C   1 
ATOM   3627 O O   . ARG B 1 139 ? 31.230  2.761   29.701  1.00 58.33  ? 325 ARG A O   1 
ATOM   3628 C CB  . ARG B 1 139 ? 30.698  -0.038  31.076  1.00 76.81  ? 325 ARG A CB  1 
ATOM   3629 C CG  . ARG B 1 139 ? 32.010  -0.688  31.471  1.00 78.40  ? 325 ARG A CG  1 
ATOM   3630 C CD  . ARG B 1 139 ? 32.150  -2.016  30.770  1.00 81.68  ? 325 ARG A CD  1 
ATOM   3631 N NE  . ARG B 1 139 ? 32.364  -1.784  29.347  1.00 82.51  ? 325 ARG A NE  1 
ATOM   3632 C CZ  . ARG B 1 139 ? 32.512  -2.740  28.441  1.00 94.01  ? 325 ARG A CZ  1 
ATOM   3633 N NH1 . ARG B 1 139 ? 32.473  -4.019  28.775  1.00 95.60  ? 325 ARG A NH1 1 
ATOM   3634 N NH2 . ARG B 1 139 ? 32.710  -2.403  27.170  1.00 100.47 ? 325 ARG A NH2 1 
ATOM   3635 N N   . GLY B 1 140 ? 32.705  2.470   31.384  1.00 66.40  ? 326 GLY A N   1 
ATOM   3636 C CA  . GLY B 1 140 ? 33.762  3.202   30.727  1.00 70.06  ? 326 GLY A CA  1 
ATOM   3637 C C   . GLY B 1 140 ? 35.091  2.487   30.873  1.00 68.81  ? 326 GLY A C   1 
ATOM   3638 O O   . GLY B 1 140 ? 35.300  1.681   31.781  1.00 64.43  ? 326 GLY A O   1 
ATOM   3639 N N   . LYS B 1 141 ? 35.998  2.809   29.959  1.00 72.13  ? 327 LYS A N   1 
ATOM   3640 C CA  . LYS B 1 141 ? 37.327  2.217   29.941  1.00 71.48  ? 327 LYS A CA  1 
ATOM   3641 C C   . LYS B 1 141 ? 38.308  3.165   30.613  1.00 66.31  ? 327 LYS A C   1 
ATOM   3642 O O   . LYS B 1 141 ? 38.245  4.384   30.424  1.00 68.23  ? 327 LYS A O   1 
ATOM   3643 C CB  . LYS B 1 141 ? 37.787  1.907   28.516  1.00 72.43  ? 327 LYS A CB  1 
ATOM   3644 C CG  . LYS B 1 141 ? 36.993  0.819   27.798  1.00 77.74  ? 327 LYS A CG  1 
ATOM   3645 C CD  . LYS B 1 141 ? 37.528  0.651   26.376  1.00 94.70  ? 327 LYS A CD  1 
ATOM   3646 C CE  . LYS B 1 141 ? 36.779  -0.413  25.581  1.00 93.51  ? 327 LYS A CE  1 
ATOM   3647 N NZ  . LYS B 1 141 ? 37.285  -0.529  24.174  1.00 78.10  ? 327 LYS A NZ  1 
ATOM   3648 N N   . MET B 1 142 ? 39.202  2.598   31.411  1.00 72.06  ? 328 MET A N   1 
ATOM   3649 C CA  . MET B 1 142 ? 40.167  3.365   32.180  1.00 68.70  ? 328 MET A CA  1 
ATOM   3650 C C   . MET B 1 142 ? 41.462  2.571   32.215  1.00 72.18  ? 328 MET A C   1 
ATOM   3651 O O   . MET B 1 142 ? 41.431  1.340   32.290  1.00 75.11  ? 328 MET A O   1 
ATOM   3652 C CB  . MET B 1 142 ? 39.641  3.622   33.600  1.00 62.14  ? 328 MET A CB  1 
ATOM   3653 C CG  . MET B 1 142 ? 40.581  4.369   34.520  1.00 63.05  ? 328 MET A CG  1 
ATOM   3654 S SD  . MET B 1 142 ? 39.963  4.405   36.218  1.00 77.29  ? 328 MET A SD  1 
ATOM   3655 C CE  . MET B 1 142 ? 38.472  5.379   36.034  1.00 70.17  ? 328 MET A CE  1 
ATOM   3656 N N   . VAL B 1 143 ? 42.597  3.269   32.167  1.00 71.24  ? 329 VAL A N   1 
ATOM   3657 C CA  . VAL B 1 143 ? 43.910  2.637   32.235  1.00 70.11  ? 329 VAL A CA  1 
ATOM   3658 C C   . VAL B 1 143 ? 44.602  3.105   33.507  1.00 68.06  ? 329 VAL A C   1 
ATOM   3659 O O   . VAL B 1 143 ? 44.633  4.305   33.804  1.00 67.05  ? 329 VAL A O   1 
ATOM   3660 C CB  . VAL B 1 143 ? 44.773  2.946   30.995  1.00 70.36  ? 329 VAL A CB  1 
ATOM   3661 C CG1 . VAL B 1 143 ? 44.856  4.446   30.743  1.00 67.87  ? 329 VAL A CG1 1 
ATOM   3662 C CG2 . VAL B 1 143 ? 46.162  2.349   31.160  1.00 66.95  ? 329 VAL A CG2 1 
ATOM   3663 N N   . SER B 1 144 ? 45.131  2.152   34.264  1.00 68.85  ? 330 SER A N   1 
ATOM   3664 C CA  . SER B 1 144 ? 45.921  2.424   35.453  1.00 71.15  ? 330 SER A CA  1 
ATOM   3665 C C   . SER B 1 144 ? 47.370  2.087   35.144  1.00 74.14  ? 330 SER A C   1 
ATOM   3666 O O   . SER B 1 144 ? 47.667  0.972   34.700  1.00 75.90  ? 330 SER A O   1 
ATOM   3667 C CB  . SER B 1 144 ? 45.421  1.603   36.644  1.00 71.01  ? 330 SER A CB  1 
ATOM   3668 O OG  . SER B 1 144 ? 46.166  1.891   37.813  1.00 86.54  ? 330 SER A OG  1 
ATOM   3669 N N   . TYR B 1 145 ? 48.265  3.047   35.364  1.00 71.97  ? 331 TYR A N   1 
ATOM   3670 C CA  . TYR B 1 145 ? 49.660  2.899   34.985  1.00 73.82  ? 331 TYR A CA  1 
ATOM   3671 C C   . TYR B 1 145 ? 50.562  3.057   36.200  1.00 76.87  ? 331 TYR A C   1 
ATOM   3672 O O   . TYR B 1 145 ? 50.259  3.811   37.132  1.00 77.98  ? 331 TYR A O   1 
ATOM   3673 C CB  . TYR B 1 145 ? 50.063  3.919   33.909  1.00 72.04  ? 331 TYR A CB  1 
ATOM   3674 C CG  . TYR B 1 145 ? 50.027  5.360   34.364  1.00 72.85  ? 331 TYR A CG  1 
ATOM   3675 C CD1 . TYR B 1 145 ? 51.144  5.955   34.931  1.00 78.46  ? 331 TYR A CD1 1 
ATOM   3676 C CD2 . TYR B 1 145 ? 48.883  6.129   34.214  1.00 72.19  ? 331 TYR A CD2 1 
ATOM   3677 C CE1 . TYR B 1 145 ? 51.122  7.268   35.348  1.00 74.63  ? 331 TYR A CE1 1 
ATOM   3678 C CE2 . TYR B 1 145 ? 48.853  7.449   34.623  1.00 76.54  ? 331 TYR A CE2 1 
ATOM   3679 C CZ  . TYR B 1 145 ? 49.977  8.011   35.191  1.00 75.93  ? 331 TYR A CZ  1 
ATOM   3680 O OH  . TYR B 1 145 ? 49.960  9.322   35.607  1.00 84.03  ? 331 TYR A OH  1 
ATOM   3681 N N   . ILE B 1 146 ? 51.673  2.329   36.178  1.00 73.59  ? 332 ILE A N   1 
ATOM   3682 C CA  . ILE B 1 146 ? 52.737  2.462   37.164  1.00 74.64  ? 332 ILE A CA  1 
ATOM   3683 C C   . ILE B 1 146 ? 54.036  2.553   36.377  1.00 77.05  ? 332 ILE A C   1 
ATOM   3684 O O   . ILE B 1 146 ? 54.421  1.593   35.698  1.00 77.99  ? 332 ILE A O   1 
ATOM   3685 C CB  . ILE B 1 146 ? 52.770  1.288   38.151  1.00 77.35  ? 332 ILE A CB  1 
ATOM   3686 C CG1 . ILE B 1 146 ? 51.418  1.142   38.854  1.00 73.94  ? 332 ILE A CG1 1 
ATOM   3687 C CG2 . ILE B 1 146 ? 53.893  1.477   39.162  1.00 82.90  ? 332 ILE A CG2 1 
ATOM   3688 C CD1 . ILE B 1 146 ? 51.309  -0.077  39.736  1.00 68.97  ? 332 ILE A CD1 1 
ATOM   3689 N N   . GLN B 1 147 ? 54.702  3.703   36.446  1.00 84.14  ? 333 GLN A N   1 
ATOM   3690 C CA  . GLN B 1 147 ? 55.896  3.961   35.649  1.00 90.53  ? 333 GLN A CA  1 
ATOM   3691 C C   . GLN B 1 147 ? 57.096  4.156   36.568  1.00 91.89  ? 333 GLN A C   1 
ATOM   3692 O O   . GLN B 1 147 ? 57.088  5.047   37.426  1.00 93.46  ? 333 GLN A O   1 
ATOM   3693 C CB  . GLN B 1 147 ? 55.701  5.182   34.748  1.00 90.93  ? 333 GLN A CB  1 
ATOM   3694 C CG  . GLN B 1 147 ? 56.958  5.578   33.983  1.00 87.83  ? 333 GLN A CG  1 
ATOM   3695 C CD  . GLN B 1 147 ? 57.331  4.576   32.901  1.00 93.23  ? 333 GLN A CD  1 
ATOM   3696 O OE1 . GLN B 1 147 ? 56.612  4.414   31.914  1.00 92.63  ? 333 GLN A OE1 1 
ATOM   3697 N NE2 . GLN B 1 147 ? 58.455  3.892   33.089  1.00 96.89  ? 333 GLN A NE2 1 
ATOM   3698 N N   . CYS B 1 148 ? 58.121  3.325   36.383  1.00 88.74  ? 334 CYS A N   1 
ATOM   3699 C CA  . CYS B 1 148 ? 59.362  3.475   37.126  1.00 88.00  ? 334 CYS A CA  1 
ATOM   3700 C C   . CYS B 1 148 ? 60.148  4.663   36.590  1.00 94.37  ? 334 CYS A C   1 
ATOM   3701 O O   . CYS B 1 148 ? 60.123  4.960   35.393  1.00 102.22 ? 334 CYS A O   1 
ATOM   3702 C CB  . CYS B 1 148 ? 60.200  2.198   37.026  1.00 88.57  ? 334 CYS A CB  1 
ATOM   3703 S SG  . CYS B 1 148 ? 59.450  0.738   37.782  1.00 79.23  ? 334 CYS A SG  1 
ATOM   3704 N N   . LYS B 1 149 ? 60.857  5.346   37.486  1.00 99.81  ? 335 LYS A N   1 
ATOM   3705 C CA  . LYS B 1 149 ? 61.563  6.566   37.107  1.00 103.81 ? 335 LYS A CA  1 
ATOM   3706 C C   . LYS B 1 149 ? 63.027  6.337   36.743  1.00 101.07 ? 335 LYS A C   1 
ATOM   3707 O O   . LYS B 1 149 ? 63.541  7.005   35.842  1.00 103.29 ? 335 LYS A O   1 
ATOM   3708 C CB  . LYS B 1 149 ? 61.468  7.603   38.235  1.00 103.17 ? 335 LYS A CB  1 
ATOM   3709 C CG  . LYS B 1 149 ? 62.232  7.242   39.498  1.00 115.37 ? 335 LYS A CG  1 
ATOM   3710 C CD  . LYS B 1 149 ? 62.088  8.302   40.581  1.00 121.75 ? 335 LYS A CD  1 
ATOM   3711 C CE  . LYS B 1 149 ? 62.862  7.902   41.831  1.00 120.17 ? 335 LYS A CE  1 
ATOM   3712 N NZ  . LYS B 1 149 ? 62.874  8.962   42.878  1.00 118.63 ? 335 LYS A NZ  1 
ATOM   3713 N N   . GLU B 1 150 ? 63.718  5.417   37.418  1.00 98.45  ? 336 GLU A N   1 
ATOM   3714 C CA  . GLU B 1 150 ? 65.136  5.186   37.172  1.00 105.97 ? 336 GLU A CA  1 
ATOM   3715 C C   . GLU B 1 150 ? 65.402  3.980   36.277  1.00 98.63  ? 336 GLU A C   1 
ATOM   3716 O O   . GLU B 1 150 ? 66.340  4.008   35.473  1.00 103.99 ? 336 GLU A O   1 
ATOM   3717 C CB  . GLU B 1 150 ? 65.869  5.036   38.509  1.00 108.17 ? 336 GLU A CB  1 
ATOM   3718 C CG  . GLU B 1 150 ? 65.656  6.247   39.432  1.00 108.32 ? 336 GLU A CG  1 
ATOM   3719 C CD  . GLU B 1 150 ? 66.222  6.057   40.827  1.00 114.77 ? 336 GLU A CD  1 
ATOM   3720 O OE1 . GLU B 1 150 ? 66.756  4.964   41.106  1.00 125.05 ? 336 GLU A OE1 1 
ATOM   3721 O OE2 . GLU B 1 150 ? 66.126  6.998   41.647  1.00 114.45 ? 336 GLU A OE2 1 
ATOM   3722 N N   . VAL B 1 151 ? 64.609  2.920   36.398  1.00 96.18  ? 337 VAL A N   1 
ATOM   3723 C CA  . VAL B 1 151 ? 64.692  1.774   35.499  1.00 91.33  ? 337 VAL A CA  1 
ATOM   3724 C C   . VAL B 1 151 ? 63.526  1.855   34.524  1.00 91.82  ? 337 VAL A C   1 
ATOM   3725 O O   . VAL B 1 151 ? 62.464  2.406   34.834  1.00 93.52  ? 337 VAL A O   1 
ATOM   3726 C CB  . VAL B 1 151 ? 64.707  0.446   36.285  1.00 89.25  ? 337 VAL A CB  1 
ATOM   3727 C CG1 . VAL B 1 151 ? 64.848  -0.749  35.351  1.00 87.13  ? 337 VAL A CG1 1 
ATOM   3728 C CG2 . VAL B 1 151 ? 65.858  0.465   37.274  1.00 88.86  ? 337 VAL A CG2 1 
ATOM   3729 N N   . ASP B 1 152 ? 63.728  1.308   33.327  1.00 86.00  ? 338 ASP A N   1 
ATOM   3730 C CA  . ASP B 1 152 ? 62.773  1.449   32.229  1.00 91.54  ? 338 ASP A CA  1 
ATOM   3731 C C   . ASP B 1 152 ? 61.775  0.289   32.248  1.00 91.84  ? 338 ASP A C   1 
ATOM   3732 O O   . ASP B 1 152 ? 61.870  -0.675  31.483  1.00 83.63  ? 338 ASP A O   1 
ATOM   3733 C CB  . ASP B 1 152 ? 63.516  1.551   30.905  1.00 97.25  ? 338 ASP A CB  1 
ATOM   3734 C CG  . ASP B 1 152 ? 62.633  2.030   29.780  1.00 103.61 ? 338 ASP A CG  1 
ATOM   3735 O OD1 . ASP B 1 152 ? 61.397  2.093   29.969  1.00 103.23 ? 338 ASP A OD1 1 
ATOM   3736 O OD2 . ASP B 1 152 ? 63.183  2.362   28.709  1.00 103.35 ? 338 ASP A OD2 1 
ATOM   3737 N N   . TYR B 1 153 ? 60.800  0.391   33.153  1.00 88.58  ? 339 TYR A N   1 
ATOM   3738 C CA  . TYR B 1 153 ? 59.693  -0.555  33.226  1.00 79.27  ? 339 TYR A CA  1 
ATOM   3739 C C   . TYR B 1 153 ? 58.392  0.202   33.438  1.00 77.57  ? 339 TYR A C   1 
ATOM   3740 O O   . TYR B 1 153 ? 58.352  1.188   34.179  1.00 77.63  ? 339 TYR A O   1 
ATOM   3741 C CB  . TYR B 1 153 ? 59.866  -1.574  34.362  1.00 80.69  ? 339 TYR A CB  1 
ATOM   3742 C CG  . TYR B 1 153 ? 58.705  -2.544  34.478  1.00 78.79  ? 339 TYR A CG  1 
ATOM   3743 C CD1 . TYR B 1 153 ? 58.619  -3.662  33.661  1.00 79.42  ? 339 TYR A CD1 1 
ATOM   3744 C CD2 . TYR B 1 153 ? 57.678  -2.321  35.388  1.00 77.29  ? 339 TYR A CD2 1 
ATOM   3745 C CE1 . TYR B 1 153 ? 57.554  -4.543  33.760  1.00 79.01  ? 339 TYR A CE1 1 
ATOM   3746 C CE2 . TYR B 1 153 ? 56.608  -3.194  35.491  1.00 76.49  ? 339 TYR A CE2 1 
ATOM   3747 C CZ  . TYR B 1 153 ? 56.552  -4.305  34.674  1.00 81.61  ? 339 TYR A CZ  1 
ATOM   3748 O OH  . TYR B 1 153 ? 55.494  -5.183  34.763  1.00 86.01  ? 339 TYR A OH  1 
ATOM   3749 N N   . ARG B 1 154 ? 57.328  -0.281  32.797  1.00 84.42  ? 340 ARG A N   1 
ATOM   3750 C CA  . ARG B 1 154 ? 56.002  0.311   32.905  1.00 79.07  ? 340 ARG A CA  1 
ATOM   3751 C C   . ARG B 1 154 ? 54.946  -0.787  32.895  1.00 72.89  ? 340 ARG A C   1 
ATOM   3752 O O   . ARG B 1 154 ? 55.096  -1.813  32.225  1.00 73.75  ? 340 ARG A O   1 
ATOM   3753 C CB  . ARG B 1 154 ? 55.731  1.297   31.762  1.00 78.09  ? 340 ARG A CB  1 
ATOM   3754 C CG  . ARG B 1 154 ? 54.410  2.034   31.880  1.00 82.63  ? 340 ARG A CG  1 
ATOM   3755 C CD  . ARG B 1 154 ? 54.129  2.850   30.633  1.00 84.33  ? 340 ARG A CD  1 
ATOM   3756 N NE  . ARG B 1 154 ? 52.896  3.616   30.752  1.00 87.97  ? 340 ARG A NE  1 
ATOM   3757 C CZ  . ARG B 1 154 ? 52.834  4.884   31.135  1.00 86.90  ? 340 ARG A CZ  1 
ATOM   3758 N NH1 . ARG B 1 154 ? 53.924  5.566   31.443  1.00 75.68  ? 340 ARG A NH1 1 
ATOM   3759 N NH2 . ARG B 1 154 ? 51.647  5.479   31.218  1.00 89.98  ? 340 ARG A NH2 1 
ATOM   3760 N N   . SER B 1 155 ? 53.870  -0.558  33.645  1.00 76.22  ? 341 SER A N   1 
ATOM   3761 C CA  . SER B 1 155 ? 52.764  -1.504  33.750  1.00 78.26  ? 341 SER A CA  1 
ATOM   3762 C C   . SER B 1 155 ? 51.461  -0.779  33.435  1.00 71.99  ? 341 SER A C   1 
ATOM   3763 O O   . SER B 1 155 ? 51.030  0.091   34.199  1.00 68.53  ? 341 SER A O   1 
ATOM   3764 C CB  . SER B 1 155 ? 52.718  -2.140  35.139  1.00 72.12  ? 341 SER A CB  1 
ATOM   3765 O OG  . SER B 1 155 ? 51.649  -3.061  35.234  1.00 82.06  ? 341 SER A OG  1 
ATOM   3766 N N   . ASP B 1 156 ? 50.851  -1.119  32.303  1.00 75.14  ? 342 ASP A N   1 
ATOM   3767 C CA  . ASP B 1 156 ? 49.563  -0.572  31.895  1.00 70.94  ? 342 ASP A CA  1 
ATOM   3768 C C   . ASP B 1 156 ? 48.522  -1.676  31.984  1.00 74.47  ? 342 ASP A C   1 
ATOM   3769 O O   . ASP B 1 156 ? 48.659  -2.715  31.328  1.00 78.66  ? 342 ASP A O   1 
ATOM   3770 C CB  . ASP B 1 156 ? 49.622  -0.009  30.476  1.00 67.35  ? 342 ASP A CB  1 
ATOM   3771 C CG  . ASP B 1 156 ? 50.361  1.308   30.404  1.00 77.41  ? 342 ASP A CG  1 
ATOM   3772 O OD1 . ASP B 1 156 ? 50.371  2.037   31.416  1.00 80.48  ? 342 ASP A OD1 1 
ATOM   3773 O OD2 . ASP B 1 156 ? 50.948  1.610   29.345  1.00 84.65  ? 342 ASP A OD2 1 
ATOM   3774 N N   . ARG B 1 157 ? 47.488  -1.450  32.789  1.00 73.48  ? 343 ARG A N   1 
ATOM   3775 C CA  . ARG B 1 157 ? 46.369  -2.373  32.895  1.00 75.56  ? 343 ARG A CA  1 
ATOM   3776 C C   . ARG B 1 157 ? 45.078  -1.592  32.736  1.00 76.68  ? 343 ARG A C   1 
ATOM   3777 O O   . ARG B 1 157 ? 44.944  -0.483  33.261  1.00 76.71  ? 343 ARG A O   1 
ATOM   3778 C CB  . ARG B 1 157 ? 46.355  -3.114  34.240  1.00 74.54  ? 343 ARG A CB  1 
ATOM   3779 C CG  . ARG B 1 157 ? 46.339  -2.210  35.457  1.00 72.77  ? 343 ARG A CG  1 
ATOM   3780 C CD  . ARG B 1 157 ? 46.521  -3.013  36.726  1.00 78.52  ? 343 ARG A CD  1 
ATOM   3781 N NE  . ARG B 1 157 ? 46.323  -2.199  37.917  1.00 88.01  ? 343 ARG A NE  1 
ATOM   3782 C CZ  . ARG B 1 157 ? 45.143  -1.981  38.478  1.00 89.94  ? 343 ARG A CZ  1 
ATOM   3783 N NH1 . ARG B 1 157 ? 44.034  -2.491  37.970  1.00 86.59  ? 343 ARG A NH1 1 
ATOM   3784 N NH2 . ARG B 1 157 ? 45.073  -1.229  39.573  1.00 95.87  ? 343 ARG A NH2 1 
ATOM   3785 N N   . ARG B 1 158 ? 44.137  -2.157  31.992  1.00 79.80  ? 344 ARG A N   1 
ATOM   3786 C CA  . ARG B 1 158 ? 42.847  -1.514  31.810  1.00 79.95  ? 344 ARG A CA  1 
ATOM   3787 C C   . ARG B 1 158 ? 41.880  -1.947  32.903  1.00 78.60  ? 344 ARG A C   1 
ATOM   3788 O O   . ARG B 1 158 ? 41.801  -3.129  33.250  1.00 85.92  ? 344 ARG A O   1 
ATOM   3789 C CB  . ARG B 1 158 ? 42.260  -1.821  30.430  1.00 87.03  ? 344 ARG A CB  1 
ATOM   3790 C CG  . ARG B 1 158 ? 40.870  -1.222  30.225  1.00 82.12  ? 344 ARG A CG  1 
ATOM   3791 C CD  . ARG B 1 158 ? 40.371  -1.400  28.799  1.00 94.40  ? 344 ARG A CD  1 
ATOM   3792 N NE  . ARG B 1 158 ? 40.151  -2.788  28.411  1.00 102.89 ? 344 ARG A NE  1 
ATOM   3793 C CZ  . ARG B 1 158 ? 39.096  -3.512  28.760  1.00 96.35  ? 344 ARG A CZ  1 
ATOM   3794 N NH1 . ARG B 1 158 ? 38.141  -3.018  29.530  1.00 90.07  ? 344 ARG A NH1 1 
ATOM   3795 N NH2 . ARG B 1 158 ? 38.989  -4.758  28.309  1.00 96.19  ? 344 ARG A NH2 1 
ATOM   3796 N N   . GLU B 1 159 ? 41.144  -0.980  33.440  1.00 73.84  ? 345 GLU A N   1 
ATOM   3797 C CA  . GLU B 1 159 ? 40.075  -1.236  34.390  1.00 77.89  ? 345 GLU A CA  1 
ATOM   3798 C C   . GLU B 1 159 ? 38.767  -0.724  33.806  1.00 76.25  ? 345 GLU A C   1 
ATOM   3799 O O   . GLU B 1 159 ? 38.753  0.199   32.986  1.00 77.50  ? 345 GLU A O   1 
ATOM   3800 C CB  . GLU B 1 159 ? 40.317  -0.560  35.750  1.00 73.70  ? 345 GLU A CB  1 
ATOM   3801 C CG  . GLU B 1 159 ? 41.519  -1.050  36.519  1.00 76.51  ? 345 GLU A CG  1 
ATOM   3802 C CD  . GLU B 1 159 ? 41.510  -0.567  37.959  1.00 88.10  ? 345 GLU A CD  1 
ATOM   3803 O OE1 . GLU B 1 159 ? 40.416  -0.529  38.566  1.00 88.07  ? 345 GLU A OE1 1 
ATOM   3804 O OE2 . GLU B 1 159 ? 42.594  -0.227  38.484  1.00 92.44  ? 345 GLU A OE2 1 
ATOM   3805 N N   . ASP B 1 160 ? 37.668  -1.333  34.229  1.00 65.99  ? 346 ASP A N   1 
ATOM   3806 C CA  . ASP B 1 160 ? 36.343  -0.883  33.845  1.00 71.09  ? 346 ASP A CA  1 
ATOM   3807 C C   . ASP B 1 160 ? 35.636  -0.277  35.052  1.00 69.13  ? 346 ASP A C   1 
ATOM   3808 O O   . ASP B 1 160 ? 35.866  -0.681  36.196  1.00 66.92  ? 346 ASP A O   1 
ATOM   3809 C CB  . ASP B 1 160 ? 35.520  -2.037  33.261  1.00 80.64  ? 346 ASP A CB  1 
ATOM   3810 C CG  . ASP B 1 160 ? 35.940  -2.393  31.842  1.00 79.85  ? 346 ASP A CG  1 
ATOM   3811 O OD1 . ASP B 1 160 ? 36.593  -1.553  31.185  1.00 81.61  ? 346 ASP A OD1 1 
ATOM   3812 O OD2 . ASP B 1 160 ? 35.606  -3.505  31.377  1.00 81.59  ? 346 ASP A OD2 1 
ATOM   3813 N N   . TYR B 1 161 ? 34.791  0.718   34.784  1.00 60.91  ? 347 TYR A N   1 
ATOM   3814 C CA  . TYR B 1 161 ? 34.036  1.399   35.824  1.00 58.85  ? 347 TYR A CA  1 
ATOM   3815 C C   . TYR B 1 161 ? 32.627  1.681   35.324  1.00 65.62  ? 347 TYR A C   1 
ATOM   3816 O O   . TYR B 1 161 ? 32.408  1.898   34.130  1.00 71.87  ? 347 TYR A O   1 
ATOM   3817 C CB  . TYR B 1 161 ? 34.719  2.709   36.251  1.00 63.44  ? 347 TYR A CB  1 
ATOM   3818 C CG  . TYR B 1 161 ? 34.764  3.766   35.169  1.00 63.94  ? 347 TYR A CG  1 
ATOM   3819 C CD1 . TYR B 1 161 ? 35.780  3.779   34.223  1.00 65.04  ? 347 TYR A CD1 1 
ATOM   3820 C CD2 . TYR B 1 161 ? 33.797  4.758   35.103  1.00 62.00  ? 347 TYR A CD2 1 
ATOM   3821 C CE1 . TYR B 1 161 ? 35.823  4.746   33.235  1.00 63.37  ? 347 TYR A CE1 1 
ATOM   3822 C CE2 . TYR B 1 161 ? 33.833  5.730   34.122  1.00 60.23  ? 347 TYR A CE2 1 
ATOM   3823 C CZ  . TYR B 1 161 ? 34.848  5.719   33.190  1.00 62.46  ? 347 TYR A CZ  1 
ATOM   3824 O OH  . TYR B 1 161 ? 34.886  6.683   32.211  1.00 62.85  ? 347 TYR A OH  1 
ATOM   3825 N N   . TYR B 1 162 ? 31.670  1.667   36.255  1.00 70.26  ? 348 TYR A N   1 
ATOM   3826 C CA  . TYR B 1 162 ? 30.307  2.105   35.986  1.00 61.19  ? 348 TYR A CA  1 
ATOM   3827 C C   . TYR B 1 162 ? 29.965  3.419   36.665  1.00 57.08  ? 348 TYR A C   1 
ATOM   3828 O O   . TYR B 1 162 ? 28.911  3.995   36.369  1.00 66.13  ? 348 TYR A O   1 
ATOM   3829 C CB  . TYR B 1 162 ? 29.298  1.035   36.428  1.00 62.02  ? 348 TYR A CB  1 
ATOM   3830 C CG  . TYR B 1 162 ? 29.231  -0.138  35.489  1.00 67.00  ? 348 TYR A CG  1 
ATOM   3831 C CD1 . TYR B 1 162 ? 28.393  -0.110  34.385  1.00 68.31  ? 348 TYR A CD1 1 
ATOM   3832 C CD2 . TYR B 1 162 ? 30.013  -1.265  35.693  1.00 68.19  ? 348 TYR A CD2 1 
ATOM   3833 C CE1 . TYR B 1 162 ? 28.328  -1.174  33.511  1.00 75.51  ? 348 TYR A CE1 1 
ATOM   3834 C CE2 . TYR B 1 162 ? 29.956  -2.338  34.824  1.00 77.81  ? 348 TYR A CE2 1 
ATOM   3835 C CZ  . TYR B 1 162 ? 29.111  -2.288  33.734  1.00 82.57  ? 348 TYR A CZ  1 
ATOM   3836 O OH  . TYR B 1 162 ? 29.046  -3.354  32.862  1.00 91.67  ? 348 TYR A OH  1 
ATOM   3837 N N   . ASP B 1 163 ? 30.837  3.916   37.536  1.00 55.81  ? 349 ASP A N   1 
ATOM   3838 C CA  . ASP B 1 163 ? 30.604  5.152   38.262  1.00 55.77  ? 349 ASP A CA  1 
ATOM   3839 C C   . ASP B 1 163 ? 31.946  5.694   38.732  1.00 56.75  ? 349 ASP A C   1 
ATOM   3840 O O   . ASP B 1 163 ? 32.936  4.963   38.822  1.00 55.93  ? 349 ASP A O   1 
ATOM   3841 C CB  . ASP B 1 163 ? 29.652  4.925   39.435  1.00 59.42  ? 349 ASP A CB  1 
ATOM   3842 C CG  . ASP B 1 163 ? 29.992  3.675   40.214  1.00 70.22  ? 349 ASP A CG  1 
ATOM   3843 O OD1 . ASP B 1 163 ? 30.704  2.806   39.667  1.00 76.39  ? 349 ASP A OD1 1 
ATOM   3844 O OD2 . ASP B 1 163 ? 29.523  3.544   41.360  1.00 75.41  ? 349 ASP A OD2 1 
ATOM   3845 N N   . ILE B 1 164 ? 31.965  6.992   39.016  1.00 53.23  ? 350 ILE A N   1 
ATOM   3846 C CA  . ILE B 1 164 ? 33.174  7.700   39.411  1.00 51.96  ? 350 ILE A CA  1 
ATOM   3847 C C   . ILE B 1 164 ? 32.920  8.382   40.748  1.00 57.06  ? 350 ILE A C   1 
ATOM   3848 O O   . ILE B 1 164 ? 32.027  9.230   40.858  1.00 63.02  ? 350 ILE A O   1 
ATOM   3849 C CB  . ILE B 1 164 ? 33.596  8.726   38.350  1.00 51.58  ? 350 ILE A CB  1 
ATOM   3850 C CG1 . ILE B 1 164 ? 33.947  8.024   37.039  1.00 55.79  ? 350 ILE A CG1 1 
ATOM   3851 C CG2 . ILE B 1 164 ? 34.770  9.548   38.849  1.00 62.48  ? 350 ILE A CG2 1 
ATOM   3852 C CD1 . ILE B 1 164 ? 35.187  7.161   37.127  1.00 67.20  ? 350 ILE A CD1 1 
ATOM   3853 N N   . GLN B 1 165 ? 33.722  8.037   41.752  1.00 60.09  ? 351 GLN A N   1 
ATOM   3854 C CA  . GLN B 1 165 ? 33.644  8.660   43.067  1.00 54.96  ? 351 GLN A CA  1 
ATOM   3855 C C   . GLN B 1 165 ? 34.653  9.804   43.119  1.00 62.48  ? 351 GLN A C   1 
ATOM   3856 O O   . GLN B 1 165 ? 35.862  9.573   42.998  1.00 65.24  ? 351 GLN A O   1 
ATOM   3857 C CB  . GLN B 1 165 ? 33.926  7.638   44.170  1.00 53.95  ? 351 GLN A CB  1 
ATOM   3858 C CG  . GLN B 1 165 ? 32.924  6.480   44.273  1.00 60.60  ? 351 GLN A CG  1 
ATOM   3859 C CD  . GLN B 1 165 ? 33.143  5.382   43.239  1.00 63.55  ? 351 GLN A CD  1 
ATOM   3860 O OE1 . GLN B 1 165 ? 34.215  4.783   43.169  1.00 70.71  ? 351 GLN A OE1 1 
ATOM   3861 N NE2 . GLN B 1 165 ? 32.115  5.102   42.444  1.00 61.26  ? 351 GLN A NE2 1 
ATOM   3862 N N   . LEU B 1 166 ? 34.166  11.029  43.304  1.00 59.45  ? 352 LEU A N   1 
ATOM   3863 C CA  . LEU B 1 166 ? 35.001  12.222  43.215  1.00 59.74  ? 352 LEU A CA  1 
ATOM   3864 C C   . LEU B 1 166 ? 35.325  12.772  44.599  1.00 59.11  ? 352 LEU A C   1 
ATOM   3865 O O   . LEU B 1 166 ? 34.440  12.881  45.452  1.00 64.82  ? 352 LEU A O   1 
ATOM   3866 C CB  . LEU B 1 166 ? 34.307  13.301  42.388  1.00 58.63  ? 352 LEU A CB  1 
ATOM   3867 C CG  . LEU B 1 166 ? 34.193  13.031  40.896  1.00 55.65  ? 352 LEU A CG  1 
ATOM   3868 C CD1 . LEU B 1 166 ? 33.548  14.225  40.228  1.00 60.70  ? 352 LEU A CD1 1 
ATOM   3869 C CD2 . LEU B 1 166 ? 35.555  12.750  40.309  1.00 52.15  ? 352 LEU A CD2 1 
ATOM   3870 N N   . SER B 1 167 ? 36.593  13.124  44.809  1.00 64.60  ? 353 SER A N   1 
ATOM   3871 C CA  . SER B 1 167 ? 37.018  13.799  46.030  1.00 67.00  ? 353 SER A CA  1 
ATOM   3872 C C   . SER B 1 167 ? 36.563  15.259  46.013  1.00 64.80  ? 353 SER A C   1 
ATOM   3873 O O   . SER B 1 167 ? 36.530  15.907  44.964  1.00 59.87  ? 353 SER A O   1 
ATOM   3874 C CB  . SER B 1 167 ? 38.540  13.712  46.175  1.00 63.38  ? 353 SER A CB  1 
ATOM   3875 O OG  . SER B 1 167 ? 38.992  14.289  47.387  1.00 68.71  ? 353 SER A OG  1 
ATOM   3876 N N   . ILE B 1 168 ? 36.224  15.786  47.196  1.00 60.44  ? 354 ILE A N   1 
ATOM   3877 C CA  . ILE B 1 168 ? 35.609  17.103  47.326  1.00 61.33  ? 354 ILE A CA  1 
ATOM   3878 C C   . ILE B 1 168 ? 36.412  18.023  48.236  1.00 67.08  ? 354 ILE A C   1 
ATOM   3879 O O   . ILE B 1 168 ? 36.626  19.197  47.912  1.00 69.19  ? 354 ILE A O   1 
ATOM   3880 C CB  . ILE B 1 168 ? 34.157  16.997  47.821  1.00 68.83  ? 354 ILE A CB  1 
ATOM   3881 C CG1 . ILE B 1 168 ? 33.322  16.234  46.804  1.00 63.52  ? 354 ILE A CG1 1 
ATOM   3882 C CG2 . ILE B 1 168 ? 33.582  18.386  48.093  1.00 65.62  ? 354 ILE A CG2 1 
ATOM   3883 C CD1 . ILE B 1 168 ? 31.931  16.069  47.250  1.00 69.59  ? 354 ILE A CD1 1 
ATOM   3884 N N   . LYS B 1 169 ? 36.830  17.521  49.398  1.00 67.61  ? 355 LYS A N   1 
ATOM   3885 C CA  . LYS B 1 169 ? 37.500  18.360  50.385  1.00 65.21  ? 355 LYS A CA  1 
ATOM   3886 C C   . LYS B 1 169 ? 38.713  19.039  49.769  1.00 60.44  ? 355 LYS A C   1 
ATOM   3887 O O   . LYS B 1 169 ? 39.626  18.373  49.272  1.00 69.42  ? 355 LYS A O   1 
ATOM   3888 C CB  . LYS B 1 169 ? 37.917  17.521  51.594  1.00 65.97  ? 355 LYS A CB  1 
ATOM   3889 C CG  . LYS B 1 169 ? 38.629  18.300  52.701  1.00 70.23  ? 355 LYS A CG  1 
ATOM   3890 C CD  . LYS B 1 169 ? 37.755  19.389  53.307  1.00 69.67  ? 355 LYS A CD  1 
ATOM   3891 C CE  . LYS B 1 169 ? 38.476  20.091  54.451  1.00 76.73  ? 355 LYS A CE  1 
ATOM   3892 N NZ  . LYS B 1 169 ? 37.665  21.205  55.018  1.00 75.42  ? 355 LYS A NZ  1 
ATOM   3893 N N   . GLY B 1 170 ? 38.706  20.370  49.781  1.00 61.21  ? 356 GLY A N   1 
ATOM   3894 C CA  . GLY B 1 170 ? 39.758  21.147  49.174  1.00 60.28  ? 356 GLY A CA  1 
ATOM   3895 C C   . GLY B 1 170 ? 39.551  21.453  47.709  1.00 61.88  ? 356 GLY A C   1 
ATOM   3896 O O   . GLY B 1 170 ? 40.302  22.263  47.151  1.00 68.19  ? 356 GLY A O   1 
ATOM   3897 N N   . LYS B 1 171 ? 38.547  20.855  47.075  1.00 68.45  ? 357 LYS A N   1 
ATOM   3898 C CA  . LYS B 1 171 ? 38.250  21.082  45.667  1.00 63.26  ? 357 LYS A CA  1 
ATOM   3899 C C   . LYS B 1 171 ? 37.007  21.950  45.561  1.00 64.57  ? 357 LYS A C   1 
ATOM   3900 O O   . LYS B 1 171 ? 35.991  21.669  46.206  1.00 68.08  ? 357 LYS A O   1 
ATOM   3901 C CB  . LYS B 1 171 ? 38.028  19.765  44.917  1.00 58.17  ? 357 LYS A CB  1 
ATOM   3902 C CG  . LYS B 1 171 ? 39.274  18.917  44.704  1.00 65.38  ? 357 LYS A CG  1 
ATOM   3903 C CD  . LYS B 1 171 ? 39.595  18.057  45.921  1.00 67.69  ? 357 LYS A CD  1 
ATOM   3904 C CE  . LYS B 1 171 ? 40.944  17.377  45.775  1.00 72.02  ? 357 LYS A CE  1 
ATOM   3905 N NZ  . LYS B 1 171 ? 41.219  16.425  46.886  1.00 85.12  ? 357 LYS A NZ  1 
ATOM   3906 N N   . LYS B 1 172 ? 37.091  23.001  44.752  1.00 64.82  ? 358 LYS A N   1 
ATOM   3907 C CA  . LYS B 1 172 ? 35.997  23.956  44.670  1.00 70.41  ? 358 LYS A CA  1 
ATOM   3908 C C   . LYS B 1 172 ? 34.995  23.612  43.580  1.00 70.52  ? 358 LYS A C   1 
ATOM   3909 O O   . LYS B 1 172 ? 33.815  23.957  43.710  1.00 73.72  ? 358 LYS A O   1 
ATOM   3910 C CB  . LYS B 1 172 ? 36.543  25.369  44.445  1.00 67.27  ? 358 LYS A CB  1 
ATOM   3911 C CG  . LYS B 1 172 ? 37.354  25.540  43.175  1.00 68.88  ? 358 LYS A CG  1 
ATOM   3912 C CD  . LYS B 1 172 ? 37.989  26.926  43.106  1.00 77.90  ? 358 LYS A CD  1 
ATOM   3913 C CE  . LYS B 1 172 ? 39.033  27.142  44.208  1.00 83.32  ? 358 LYS A CE  1 
ATOM   3914 N NZ  . LYS B 1 172 ? 38.501  27.788  45.447  1.00 80.74  ? 358 LYS A NZ  1 
ATOM   3915 N N   . ASN B 1 173 ? 35.424  22.929  42.519  1.00 65.48  ? 359 ASN A N   1 
ATOM   3916 C CA  . ASN B 1 173 ? 34.523  22.562  41.437  1.00 64.79  ? 359 ASN A CA  1 
ATOM   3917 C C   . ASN B 1 173 ? 34.898  21.189  40.896  1.00 65.07  ? 359 ASN A C   1 
ATOM   3918 O O   . ASN B 1 173 ? 35.883  20.575  41.315  1.00 61.05  ? 359 ASN A O   1 
ATOM   3919 C CB  . ASN B 1 173 ? 34.533  23.611  40.315  1.00 60.10  ? 359 ASN A CB  1 
ATOM   3920 C CG  . ASN B 1 173 ? 35.924  23.873  39.765  1.00 68.14  ? 359 ASN A CG  1 
ATOM   3921 O OD1 . ASN B 1 173 ? 36.730  22.958  39.594  1.00 66.75  ? 359 ASN A OD1 1 
ATOM   3922 N ND2 . ASN B 1 173 ? 36.214  25.139  39.493  1.00 80.89  ? 359 ASN A ND2 1 
ATOM   3923 N N   . ILE B 1 174 ? 34.080  20.709  39.956  1.00 70.38  ? 360 ILE A N   1 
ATOM   3924 C CA  . ILE B 1 174 ? 34.306  19.395  39.362  1.00 66.59  ? 360 ILE A CA  1 
ATOM   3925 C C   . ILE B 1 174 ? 35.616  19.371  38.590  1.00 63.14  ? 360 ILE A C   1 
ATOM   3926 O O   . ILE B 1 174 ? 36.309  18.347  38.563  1.00 64.40  ? 360 ILE A O   1 
ATOM   3927 C CB  . ILE B 1 174 ? 33.106  18.994  38.481  1.00 58.23  ? 360 ILE A CB  1 
ATOM   3928 C CG1 . ILE B 1 174 ? 31.943  18.542  39.356  1.00 57.95  ? 360 ILE A CG1 1 
ATOM   3929 C CG2 . ILE B 1 174 ? 33.476  17.888  37.519  1.00 60.41  ? 360 ILE A CG2 1 
ATOM   3930 C CD1 . ILE B 1 174 ? 30.917  17.718  38.613  1.00 69.06  ? 360 ILE A CD1 1 
ATOM   3931 N N   . PHE B 1 175 ? 35.980  20.488  37.953  1.00 62.55  ? 361 PHE A N   1 
ATOM   3932 C CA  . PHE B 1 175 ? 37.241  20.546  37.221  1.00 60.48  ? 361 PHE A CA  1 
ATOM   3933 C C   . PHE B 1 175 ? 38.417  20.216  38.131  1.00 70.19  ? 361 PHE A C   1 
ATOM   3934 O O   . PHE B 1 175 ? 39.226  19.333  37.823  1.00 65.66  ? 361 PHE A O   1 
ATOM   3935 C CB  . PHE B 1 175 ? 37.425  21.928  36.594  1.00 60.35  ? 361 PHE A CB  1 
ATOM   3936 C CG  . PHE B 1 175 ? 38.821  22.186  36.108  1.00 69.51  ? 361 PHE A CG  1 
ATOM   3937 C CD1 . PHE B 1 175 ? 39.263  21.653  34.909  1.00 70.45  ? 361 PHE A CD1 1 
ATOM   3938 C CD2 . PHE B 1 175 ? 39.697  22.955  36.858  1.00 70.29  ? 361 PHE A CD2 1 
ATOM   3939 C CE1 . PHE B 1 175 ? 40.550  21.888  34.466  1.00 63.52  ? 361 PHE A CE1 1 
ATOM   3940 C CE2 . PHE B 1 175 ? 40.982  23.191  36.417  1.00 64.16  ? 361 PHE A CE2 1 
ATOM   3941 C CZ  . PHE B 1 175 ? 41.407  22.658  35.220  1.00 61.16  ? 361 PHE A CZ  1 
ATOM   3942 N N   . GLU B 1 176 ? 38.514  20.901  39.273  1.00 66.89  ? 362 GLU A N   1 
ATOM   3943 C CA  . GLU B 1 176 ? 39.568  20.576  40.227  1.00 59.66  ? 362 GLU A CA  1 
ATOM   3944 C C   . GLU B 1 176 ? 39.409  19.158  40.758  1.00 59.60  ? 362 GLU A C   1 
ATOM   3945 O O   . GLU B 1 176 ? 40.401  18.464  41.003  1.00 69.17  ? 362 GLU A O   1 
ATOM   3946 C CB  . GLU B 1 176 ? 39.573  21.579  41.378  1.00 59.60  ? 362 GLU A CB  1 
ATOM   3947 C CG  . GLU B 1 176 ? 40.153  22.936  41.036  1.00 67.46  ? 362 GLU A CG  1 
ATOM   3948 C CD  . GLU B 1 176 ? 40.415  23.764  42.277  1.00 73.64  ? 362 GLU A CD  1 
ATOM   3949 O OE1 . GLU B 1 176 ? 39.912  23.383  43.354  1.00 69.30  ? 362 GLU A OE1 1 
ATOM   3950 O OE2 . GLU B 1 176 ? 41.133  24.783  42.184  1.00 82.94  ? 362 GLU A OE2 1 
ATOM   3951 N N   . SER B 1 177 ? 38.167  18.708  40.941  1.00 65.53  ? 363 SER A N   1 
ATOM   3952 C CA  . SER B 1 177 ? 37.943  17.349  41.423  1.00 67.18  ? 363 SER A CA  1 
ATOM   3953 C C   . SER B 1 177 ? 38.504  16.321  40.443  1.00 66.55  ? 363 SER A C   1 
ATOM   3954 O O   . SER B 1 177 ? 39.132  15.336  40.854  1.00 60.78  ? 363 SER A O   1 
ATOM   3955 C CB  . SER B 1 177 ? 36.450  17.123  41.661  1.00 56.17  ? 363 SER A CB  1 
ATOM   3956 O OG  . SER B 1 177 ? 36.209  15.860  42.255  1.00 58.40  ? 363 SER A OG  1 
ATOM   3957 N N   . PHE B 1 178 ? 38.295  16.539  39.141  1.00 71.51  ? 364 PHE A N   1 
ATOM   3958 C CA  . PHE B 1 178 ? 38.840  15.624  38.142  1.00 66.54  ? 364 PHE A CA  1 
ATOM   3959 C C   . PHE B 1 178 ? 40.360  15.701  38.092  1.00 62.20  ? 364 PHE A C   1 
ATOM   3960 O O   . PHE B 1 178 ? 41.027  14.681  37.892  1.00 61.04  ? 364 PHE A O   1 
ATOM   3961 C CB  . PHE B 1 178 ? 38.242  15.921  36.765  1.00 64.99  ? 364 PHE A CB  1 
ATOM   3962 C CG  . PHE B 1 178 ? 37.091  15.034  36.400  1.00 58.15  ? 364 PHE A CG  1 
ATOM   3963 C CD1 . PHE B 1 178 ? 37.316  13.771  35.885  1.00 57.48  ? 364 PHE A CD1 1 
ATOM   3964 C CD2 . PHE B 1 178 ? 35.789  15.454  36.582  1.00 61.07  ? 364 PHE A CD2 1 
ATOM   3965 C CE1 . PHE B 1 178 ? 36.265  12.948  35.553  1.00 60.77  ? 364 PHE A CE1 1 
ATOM   3966 C CE2 . PHE B 1 178 ? 34.730  14.634  36.253  1.00 60.36  ? 364 PHE A CE2 1 
ATOM   3967 C CZ  . PHE B 1 178 ? 34.968  13.380  35.737  1.00 59.36  ? 364 PHE A CZ  1 
ATOM   3968 N N   . VAL B 1 179 ? 40.922  16.899  38.280  1.00 65.99  ? 365 VAL A N   1 
ATOM   3969 C CA  . VAL B 1 179 ? 42.376  17.046  38.304  1.00 63.40  ? 365 VAL A CA  1 
ATOM   3970 C C   . VAL B 1 179 ? 42.977  16.184  39.407  1.00 58.66  ? 365 VAL A C   1 
ATOM   3971 O O   . VAL B 1 179 ? 44.004  15.525  39.209  1.00 65.21  ? 365 VAL A O   1 
ATOM   3972 C CB  . VAL B 1 179 ? 42.759  18.530  38.466  1.00 57.81  ? 365 VAL A CB  1 
ATOM   3973 C CG1 . VAL B 1 179 ? 44.246  18.680  38.710  1.00 59.04  ? 365 VAL A CG1 1 
ATOM   3974 C CG2 . VAL B 1 179 ? 42.322  19.331  37.243  1.00 58.59  ? 365 VAL A CG2 1 
ATOM   3975 N N   . ASP B 1 180 ? 42.334  16.159  40.578  1.00 58.35  ? 366 ASP A N   1 
ATOM   3976 C CA  . ASP B 1 180 ? 42.799  15.311  41.671  1.00 62.67  ? 366 ASP A CA  1 
ATOM   3977 C C   . ASP B 1 180 ? 42.699  13.834  41.312  1.00 65.84  ? 366 ASP A C   1 
ATOM   3978 O O   . ASP B 1 180 ? 43.543  13.028  41.725  1.00 68.46  ? 366 ASP A O   1 
ATOM   3979 C CB  . ASP B 1 180 ? 41.996  15.603  42.938  1.00 65.92  ? 366 ASP A CB  1 
ATOM   3980 C CG  . ASP B 1 180 ? 42.351  14.673  44.086  1.00 70.25  ? 366 ASP A CG  1 
ATOM   3981 O OD1 . ASP B 1 180 ? 43.483  14.766  44.607  1.00 68.10  ? 366 ASP A OD1 1 
ATOM   3982 O OD2 . ASP B 1 180 ? 41.490  13.853  44.474  1.00 75.53  ? 366 ASP A OD2 1 
ATOM   3983 N N   . TYR B 1 181 ? 41.665  13.458  40.556  1.00 65.06  ? 367 TYR A N   1 
ATOM   3984 C CA  . TYR B 1 181 ? 41.499  12.060  40.168  1.00 63.23  ? 367 TYR A CA  1 
ATOM   3985 C C   . TYR B 1 181 ? 42.640  11.600  39.269  1.00 62.31  ? 367 TYR A C   1 
ATOM   3986 O O   . TYR B 1 181 ? 43.134  10.474  39.403  1.00 64.92  ? 367 TYR A O   1 
ATOM   3987 C CB  . TYR B 1 181 ? 40.151  11.880  39.467  1.00 57.75  ? 367 TYR A CB  1 
ATOM   3988 C CG  . TYR B 1 181 ? 39.604  10.465  39.463  1.00 54.63  ? 367 TYR A CG  1 
ATOM   3989 C CD1 . TYR B 1 181 ? 38.991  9.929   40.587  1.00 54.60  ? 367 TYR A CD1 1 
ATOM   3990 C CD2 . TYR B 1 181 ? 39.691  9.671   38.328  1.00 54.61  ? 367 TYR A CD2 1 
ATOM   3991 C CE1 . TYR B 1 181 ? 38.480  8.639   40.577  1.00 56.11  ? 367 TYR A CE1 1 
ATOM   3992 C CE2 . TYR B 1 181 ? 39.189  8.382   38.310  1.00 56.43  ? 367 TYR A CE2 1 
ATOM   3993 C CZ  . TYR B 1 181 ? 38.585  7.870   39.434  1.00 56.88  ? 367 TYR A CZ  1 
ATOM   3994 O OH  . TYR B 1 181 ? 38.085  6.586   39.407  1.00 57.05  ? 367 TYR A OH  1 
ATOM   3995 N N   . VAL B 1 182 ? 43.072  12.463  38.341  1.00 70.05  ? 368 VAL A N   1 
ATOM   3996 C CA  . VAL B 1 182 ? 44.163  12.142  37.427  1.00 69.21  ? 368 VAL A CA  1 
ATOM   3997 C C   . VAL B 1 182 ? 45.522  12.548  37.980  1.00 70.40  ? 368 VAL A C   1 
ATOM   3998 O O   . VAL B 1 182 ? 46.542  12.360  37.303  1.00 69.99  ? 368 VAL A O   1 
ATOM   3999 C CB  . VAL B 1 182 ? 43.923  12.819  36.061  1.00 68.98  ? 368 VAL A CB  1 
ATOM   4000 C CG1 . VAL B 1 182 ? 44.715  12.135  34.971  1.00 70.25  ? 368 VAL A CG1 1 
ATOM   4001 C CG2 . VAL B 1 182 ? 42.451  12.803  35.718  1.00 68.51  ? 368 VAL A CG2 1 
ATOM   4002 N N   . ALA B 1 183 ? 45.570  13.091  39.194  1.00 71.96  ? 369 ALA A N   1 
ATOM   4003 C CA  . ALA B 1 183 ? 46.838  13.500  39.783  1.00 73.29  ? 369 ALA A CA  1 
ATOM   4004 C C   . ALA B 1 183 ? 47.756  12.298  39.969  1.00 76.42  ? 369 ALA A C   1 
ATOM   4005 O O   . ALA B 1 183 ? 47.305  11.190  40.271  1.00 77.66  ? 369 ALA A O   1 
ATOM   4006 C CB  . ALA B 1 183 ? 46.597  14.196  41.123  1.00 75.16  ? 369 ALA A CB  1 
ATOM   4007 N N   . VAL B 1 184 ? 49.051  12.521  39.754  1.00 79.20  ? 370 VAL A N   1 
ATOM   4008 C CA  . VAL B 1 184 ? 50.050  11.462  39.857  1.00 82.79  ? 370 VAL A CA  1 
ATOM   4009 C C   . VAL B 1 184 ? 50.376  11.226  41.325  1.00 85.41  ? 370 VAL A C   1 
ATOM   4010 O O   . VAL B 1 184 ? 50.766  12.154  42.042  1.00 81.64  ? 370 VAL A O   1 
ATOM   4011 C CB  . VAL B 1 184 ? 51.314  11.821  39.066  1.00 82.61  ? 370 VAL A CB  1 
ATOM   4012 C CG1 . VAL B 1 184 ? 52.408  10.789  39.312  1.00 76.76  ? 370 VAL A CG1 1 
ATOM   4013 C CG2 . VAL B 1 184 ? 50.985  11.933  37.590  1.00 76.65  ? 370 VAL A CG2 1 
ATOM   4014 N N   . GLU B 1 185 ? 50.228  9.983   41.771  1.00 87.87  ? 371 GLU A N   1 
ATOM   4015 C CA  . GLU B 1 185 ? 50.632  9.594   43.112  1.00 86.38  ? 371 GLU A CA  1 
ATOM   4016 C C   . GLU B 1 185 ? 52.089  9.157   43.088  1.00 84.73  ? 371 GLU A C   1 
ATOM   4017 O O   . GLU B 1 185 ? 52.562  8.558   42.118  1.00 84.69  ? 371 GLU A O   1 
ATOM   4018 C CB  . GLU B 1 185 ? 49.751  8.463   43.651  1.00 94.02  ? 371 GLU A CB  1 
ATOM   4019 C CG  . GLU B 1 185 ? 50.160  7.957   45.034  1.00 101.17 ? 371 GLU A CG  1 
ATOM   4020 C CD  . GLU B 1 185 ? 49.245  6.866   45.561  1.00 108.90 ? 371 GLU A CD  1 
ATOM   4021 O OE1 . GLU B 1 185 ? 48.061  6.824   45.155  1.00 107.82 ? 371 GLU A OE1 1 
ATOM   4022 O OE2 . GLU B 1 185 ? 49.716  6.048   46.382  1.00 108.07 ? 371 GLU A OE2 1 
ATOM   4023 N N   . GLN B 1 186 ? 52.799  9.459   44.167  1.00 89.01  ? 372 GLN A N   1 
ATOM   4024 C CA  . GLN B 1 186 ? 54.219  9.167   44.259  1.00 84.20  ? 372 GLN A CA  1 
ATOM   4025 C C   . GLN B 1 186 ? 54.454  7.947   45.136  1.00 90.25  ? 372 GLN A C   1 
ATOM   4026 O O   . GLN B 1 186 ? 53.856  7.810   46.208  1.00 99.22  ? 372 GLN A O   1 
ATOM   4027 C CB  . GLN B 1 186 ? 54.985  10.371  44.806  1.00 81.76  ? 372 GLN A CB  1 
ATOM   4028 C CG  . GLN B 1 186 ? 56.266  10.669  44.057  1.00 86.46  ? 372 GLN A CG  1 
ATOM   4029 C CD  . GLN B 1 186 ? 56.039  11.070  42.611  1.00 85.93  ? 372 GLN A CD  1 
ATOM   4030 O OE1 . GLN B 1 186 ? 54.921  11.375  42.200  1.00 87.70  ? 372 GLN A OE1 1 
ATOM   4031 N NE2 . GLN B 1 186 ? 57.109  11.064  41.828  1.00 98.48  ? 372 GLN A NE2 1 
ATOM   4032 N N   . LEU B 1 187 ? 55.316  7.055   44.657  1.00 92.66  ? 373 LEU A N   1 
ATOM   4033 C CA  . LEU B 1 187 ? 55.710  5.844   45.367  1.00 95.09  ? 373 LEU A CA  1 
ATOM   4034 C C   . LEU B 1 187 ? 57.195  5.967   45.684  1.00 105.07 ? 373 LEU A C   1 
ATOM   4035 O O   . LEU B 1 187 ? 58.035  5.522   44.902  1.00 105.58 ? 373 LEU A O   1 
ATOM   4036 C CB  . LEU B 1 187 ? 55.432  4.602   44.525  1.00 94.25  ? 373 LEU A CB  1 
ATOM   4037 C CG  . LEU B 1 187 ? 53.995  4.307   44.102  1.00 89.80  ? 373 LEU A CG  1 
ATOM   4038 C CD1 . LEU B 1 187 ? 53.974  3.116   43.159  1.00 83.80  ? 373 LEU A CD1 1 
ATOM   4039 C CD2 . LEU B 1 187 ? 53.121  4.047   45.315  1.00 95.39  ? 373 LEU A CD2 1 
ATOM   4040 N N   . ASP B 1 188 ? 57.521  6.575   46.819  1.00 108.19 ? 374 ASP A N   1 
ATOM   4041 C CA  . ASP B 1 188 ? 58.902  6.720   47.257  1.00 105.81 ? 374 ASP A CA  1 
ATOM   4042 C C   . ASP B 1 188 ? 59.241  5.585   48.222  1.00 112.26 ? 374 ASP A C   1 
ATOM   4043 O O   . ASP B 1 188 ? 58.478  4.625   48.363  1.00 110.60 ? 374 ASP A O   1 
ATOM   4044 C CB  . ASP B 1 188 ? 59.116  8.102   47.879  1.00 112.56 ? 374 ASP A CB  1 
ATOM   4045 C CG  . ASP B 1 188 ? 59.172  9.212   46.840  1.00 115.37 ? 374 ASP A CG  1 
ATOM   4046 O OD1 . ASP B 1 188 ? 59.717  8.974   45.739  1.00 117.01 ? 374 ASP A OD1 1 
ATOM   4047 O OD2 . ASP B 1 188 ? 58.663  10.321  47.124  1.00 112.28 ? 374 ASP A OD2 1 
ATOM   4048 N N   . GLY B 1 189 ? 60.403  5.676   48.879  1.00 115.87 ? 375 GLY A N   1 
ATOM   4049 C CA  . GLY B 1 189 ? 60.802  4.672   49.852  1.00 103.23 ? 375 GLY A CA  1 
ATOM   4050 C C   . GLY B 1 189 ? 59.693  4.456   50.860  1.00 118.94 ? 375 GLY A C   1 
ATOM   4051 O O   . GLY B 1 189 ? 58.997  5.413   51.214  1.00 130.66 ? 375 GLY A O   1 
ATOM   4052 N N   . ASP B 1 190 ? 59.504  3.213   51.311  1.00 115.51 ? 376 ASP A N   1 
ATOM   4053 C CA  . ASP B 1 190 ? 58.392  2.720   52.123  1.00 121.00 ? 376 ASP A CA  1 
ATOM   4054 C C   . ASP B 1 190 ? 57.147  2.546   51.246  1.00 119.44 ? 376 ASP A C   1 
ATOM   4055 O O   . ASP B 1 190 ? 56.165  1.959   51.698  1.00 121.34 ? 376 ASP A O   1 
ATOM   4056 C CB  . ASP B 1 190 ? 58.061  3.640   53.323  1.00 130.86 ? 376 ASP A CB  1 
ATOM   4057 C CG  . ASP B 1 190 ? 57.153  2.982   54.373  1.00 130.75 ? 376 ASP A CG  1 
ATOM   4058 O OD1 . ASP B 1 190 ? 56.814  1.784   54.252  1.00 132.54 ? 376 ASP A OD1 1 
ATOM   4059 O OD2 . ASP B 1 190 ? 56.762  3.691   55.329  1.00 119.10 ? 376 ASP A OD2 1 
ATOM   4060 N N   . ASN B 1 191 ? 57.173  2.998   49.987  1.00 115.49 ? 377 ASN A N   1 
ATOM   4061 C CA  . ASN B 1 191 ? 56.089  2.769   49.041  1.00 111.63 ? 377 ASN A CA  1 
ATOM   4062 C C   . ASN B 1 191 ? 56.608  2.332   47.678  1.00 108.42 ? 377 ASN A C   1 
ATOM   4063 O O   . ASN B 1 191 ? 55.836  2.317   46.712  1.00 101.27 ? 377 ASN A O   1 
ATOM   4064 C CB  . ASN B 1 191 ? 55.233  4.028   48.884  1.00 113.03 ? 377 ASN A CB  1 
ATOM   4065 C CG  . ASN B 1 191 ? 54.409  4.320   50.106  1.00 124.94 ? 377 ASN A CG  1 
ATOM   4066 O OD1 . ASN B 1 191 ? 54.040  3.410   50.849  1.00 132.07 ? 377 ASN A OD1 1 
ATOM   4067 N ND2 . ASN B 1 191 ? 54.128  5.596   50.338  1.00 123.37 ? 377 ASN A ND2 1 
ATOM   4068 N N   . LYS B 1 192 ? 57.888  1.969   47.585  1.00 106.27 ? 378 LYS A N   1 
ATOM   4069 C CA  . LYS B 1 192 ? 58.512  1.666   46.304  1.00 96.79  ? 378 LYS A CA  1 
ATOM   4070 C C   . LYS B 1 192 ? 57.757  0.561   45.580  1.00 87.18  ? 378 LYS A C   1 
ATOM   4071 O O   . LYS B 1 192 ? 57.392  -0.456  46.176  1.00 76.84  ? 378 LYS A O   1 
ATOM   4072 C CB  . LYS B 1 192 ? 59.967  1.255   46.525  1.00 99.36  ? 378 LYS A CB  1 
ATOM   4073 C CG  . LYS B 1 192 ? 60.910  2.424   46.693  1.00 101.20 ? 378 LYS A CG  1 
ATOM   4074 C CD  . LYS B 1 192 ? 62.376  2.005   46.557  1.00 98.11  ? 378 LYS A CD  1 
ATOM   4075 C CE  . LYS B 1 192 ? 62.968  1.485   47.864  1.00 98.54  ? 378 LYS A CE  1 
ATOM   4076 N NZ  . LYS B 1 192 ? 63.188  2.573   48.851  1.00 96.17  ? 378 LYS A NZ  1 
ATOM   4077 N N   . TYR B 1 193 ? 57.504  0.776   44.292  1.00 88.27  ? 379 TYR A N   1 
ATOM   4078 C CA  . TYR B 1 193 ? 56.802  -0.224  43.503  1.00 79.75  ? 379 TYR A CA  1 
ATOM   4079 C C   . TYR B 1 193 ? 57.652  -1.475  43.345  1.00 79.03  ? 379 TYR A C   1 
ATOM   4080 O O   . TYR B 1 193 ? 58.865  -1.401  43.128  1.00 83.65  ? 379 TYR A O   1 
ATOM   4081 C CB  . TYR B 1 193 ? 56.425  0.333   42.135  1.00 72.76  ? 379 TYR A CB  1 
ATOM   4082 C CG  . TYR B 1 193 ? 55.859  -0.716  41.210  1.00 72.05  ? 379 TYR A CG  1 
ATOM   4083 C CD1 . TYR B 1 193 ? 54.572  -1.196  41.382  1.00 69.64  ? 379 TYR A CD1 1 
ATOM   4084 C CD2 . TYR B 1 193 ? 56.607  -1.213  40.154  1.00 78.84  ? 379 TYR A CD2 1 
ATOM   4085 C CE1 . TYR B 1 193 ? 54.051  -2.155  40.534  1.00 75.28  ? 379 TYR A CE1 1 
ATOM   4086 C CE2 . TYR B 1 193 ? 56.091  -2.167  39.299  1.00 78.91  ? 379 TYR A CE2 1 
ATOM   4087 C CZ  . TYR B 1 193 ? 54.814  -2.634  39.493  1.00 75.11  ? 379 TYR A CZ  1 
ATOM   4088 O OH  . TYR B 1 193 ? 54.301  -3.584  38.641  1.00 81.94  ? 379 TYR A OH  1 
ATOM   4089 N N   . ASP B 1 194 ? 57.002  -2.631  43.461  1.00 80.66  ? 380 ASP A N   1 
ATOM   4090 C CA  . ASP B 1 194 ? 57.656  -3.923  43.270  1.00 76.25  ? 380 ASP A CA  1 
ATOM   4091 C C   . ASP B 1 194 ? 57.714  -4.204  41.778  1.00 78.00  ? 380 ASP A C   1 
ATOM   4092 O O   . ASP B 1 194 ? 56.774  -4.735  41.182  1.00 76.20  ? 380 ASP A O   1 
ATOM   4093 C CB  . ASP B 1 194 ? 56.909  -5.023  44.012  1.00 83.64  ? 380 ASP A CB  1 
ATOM   4094 C CG  . ASP B 1 194 ? 57.584  -6.381  43.884  1.00 86.66  ? 380 ASP A CG  1 
ATOM   4095 O OD1 . ASP B 1 194 ? 58.717  -6.452  43.359  1.00 86.21  ? 380 ASP A OD1 1 
ATOM   4096 O OD2 . ASP B 1 194 ? 56.969  -7.384  44.309  1.00 98.02  ? 380 ASP A OD2 1 
ATOM   4097 N N   . ALA B 1 195 ? 58.839  -3.848  41.166  1.00 78.26  ? 381 ALA A N   1 
ATOM   4098 C CA  . ALA B 1 195 ? 59.025  -4.055  39.739  1.00 75.02  ? 381 ALA A CA  1 
ATOM   4099 C C   . ALA B 1 195 ? 59.463  -5.472  39.410  1.00 74.21  ? 381 ALA A C   1 
ATOM   4100 O O   . ALA B 1 195 ? 59.862  -5.730  38.268  1.00 64.84  ? 381 ALA A O   1 
ATOM   4101 C CB  . ALA B 1 195 ? 60.029  -3.050  39.177  1.00 68.89  ? 381 ALA A CB  1 
ATOM   4102 N N   . GLY B 1 196 ? 59.420  -6.382  40.383  1.00 76.44  ? 382 GLY A N   1 
ATOM   4103 C CA  . GLY B 1 196 ? 59.729  -7.770  40.114  1.00 79.25  ? 382 GLY A CA  1 
ATOM   4104 C C   . GLY B 1 196 ? 61.172  -7.967  39.714  1.00 76.23  ? 382 GLY A C   1 
ATOM   4105 O O   . GLY B 1 196 ? 62.076  -7.936  40.554  1.00 74.20  ? 382 GLY A O   1 
ATOM   4106 N N   . GLU B 1 197 ? 61.386  -8.186  38.415  1.00 77.00  ? 383 GLU A N   1 
ATOM   4107 C CA  . GLU B 1 197 ? 62.734  -8.368  37.890  1.00 76.57  ? 383 GLU A CA  1 
ATOM   4108 C C   . GLU B 1 197 ? 63.649  -7.205  38.265  1.00 75.87  ? 383 GLU A C   1 
ATOM   4109 O O   . GLU B 1 197 ? 64.854  -7.401  38.463  1.00 85.02  ? 383 GLU A O   1 
ATOM   4110 C CB  . GLU B 1 197 ? 62.657  -8.537  36.372  1.00 77.53  ? 383 GLU A CB  1 
ATOM   4111 C CG  . GLU B 1 197 ? 63.975  -8.795  35.688  1.00 83.33  ? 383 GLU A CG  1 
ATOM   4112 C CD  . GLU B 1 197 ? 63.846  -8.799  34.180  1.00 91.33  ? 383 GLU A CD  1 
ATOM   4113 O OE1 . GLU B 1 197 ? 62.714  -8.622  33.680  1.00 83.20  ? 383 GLU A OE1 1 
ATOM   4114 O OE2 . GLU B 1 197 ? 64.878  -8.984  33.498  1.00 104.95 ? 383 GLU A OE2 1 
ATOM   4115 N N   . HIS B 1 198 ? 63.103  -5.992  38.372  1.00 72.57  ? 384 HIS A N   1 
ATOM   4116 C CA  . HIS B 1 198 ? 63.878  -4.815  38.743  1.00 69.46  ? 384 HIS A CA  1 
ATOM   4117 C C   . HIS B 1 198 ? 63.833  -4.491  40.234  1.00 74.76  ? 384 HIS A C   1 
ATOM   4118 O O   . HIS B 1 198 ? 64.429  -3.492  40.648  1.00 77.07  ? 384 HIS A O   1 
ATOM   4119 C CB  . HIS B 1 198 ? 63.391  -3.596  37.957  1.00 75.88  ? 384 HIS A CB  1 
ATOM   4120 C CG  . HIS B 1 198 ? 63.421  -3.778  36.473  1.00 84.87  ? 384 HIS A CG  1 
ATOM   4121 N ND1 . HIS B 1 198 ? 62.448  -3.264  35.643  1.00 89.80  ? 384 HIS A ND1 1 
ATOM   4122 C CD2 . HIS B 1 198 ? 64.309  -4.406  35.668  1.00 90.80  ? 384 HIS A CD2 1 
ATOM   4123 C CE1 . HIS B 1 198 ? 62.732  -3.574  34.391  1.00 86.83  ? 384 HIS A CE1 1 
ATOM   4124 N NE2 . HIS B 1 198 ? 63.856  -4.266  34.379  1.00 91.05  ? 384 HIS A NE2 1 
ATOM   4125 N N   . GLY B 1 199 ? 63.144  -5.289  41.049  1.00 76.38  ? 385 GLY A N   1 
ATOM   4126 C CA  . GLY B 1 199 ? 63.105  -4.994  42.472  1.00 74.61  ? 385 GLY A CA  1 
ATOM   4127 C C   . GLY B 1 199 ? 62.304  -3.734  42.785  1.00 77.37  ? 385 GLY A C   1 
ATOM   4128 O O   . GLY B 1 199 ? 61.546  -3.216  41.968  1.00 86.70  ? 385 GLY A O   1 
ATOM   4129 N N   . LEU B 1 200 ? 62.491  -3.244  44.009  1.00 77.61  ? 386 LEU A N   1 
ATOM   4130 C CA  . LEU B 1 200 ? 61.858  -1.994  44.420  1.00 80.42  ? 386 LEU A CA  1 
ATOM   4131 C C   . LEU B 1 200 ? 62.446  -0.833  43.624  1.00 81.81  ? 386 LEU A C   1 
ATOM   4132 O O   . LEU B 1 200 ? 63.660  -0.763  43.414  1.00 81.38  ? 386 LEU A O   1 
ATOM   4133 C CB  . LEU B 1 200 ? 62.042  -1.773  45.921  1.00 86.92  ? 386 LEU A CB  1 
ATOM   4134 C CG  . LEU B 1 200 ? 61.049  -2.467  46.867  1.00 87.02  ? 386 LEU A CG  1 
ATOM   4135 C CD1 . LEU B 1 200 ? 61.108  -3.990  46.768  1.00 80.54  ? 386 LEU A CD1 1 
ATOM   4136 C CD2 . LEU B 1 200 ? 61.272  -2.015  48.308  1.00 90.25  ? 386 LEU A CD2 1 
ATOM   4137 N N   . GLN B 1 201 ? 61.583  0.089   43.176  1.00 81.65  ? 387 GLN A N   1 
ATOM   4138 C CA  . GLN B 1 201 ? 62.023  1.038   42.155  1.00 88.80  ? 387 GLN A CA  1 
ATOM   4139 C C   . GLN B 1 201 ? 61.670  2.511   42.322  1.00 94.78  ? 387 GLN A C   1 
ATOM   4140 O O   . GLN B 1 201 ? 62.205  3.310   41.547  1.00 95.77  ? 387 GLN A O   1 
ATOM   4141 C CB  . GLN B 1 201 ? 61.490  0.593   40.786  1.00 84.42  ? 387 GLN A CB  1 
ATOM   4142 C CG  . GLN B 1 201 ? 62.254  -0.553  40.181  1.00 83.46  ? 387 GLN A CG  1 
ATOM   4143 C CD  . GLN B 1 201 ? 63.712  -0.209  40.008  1.00 81.68  ? 387 GLN A CD  1 
ATOM   4144 O OE1 . GLN B 1 201 ? 64.052  0.931   39.689  1.00 81.35  ? 387 GLN A OE1 1 
ATOM   4145 N NE2 . GLN B 1 201 ? 64.584  -1.188  40.214  1.00 77.85  ? 387 GLN A NE2 1 
ATOM   4146 N N   . GLU B 1 202 ? 60.819  2.918   43.267  1.00 98.12  ? 388 GLU A N   1 
ATOM   4147 C CA  . GLU B 1 202 ? 60.412  4.323   43.388  1.00 101.49 ? 388 GLU A CA  1 
ATOM   4148 C C   . GLU B 1 202 ? 59.787  4.815   42.077  1.00 97.97  ? 388 GLU A C   1 
ATOM   4149 O O   . GLU B 1 202 ? 60.372  5.581   41.311  1.00 105.90 ? 388 GLU A O   1 
ATOM   4150 C CB  . GLU B 1 202 ? 61.571  5.244   43.811  1.00 105.45 ? 388 GLU A CB  1 
ATOM   4151 C CG  . GLU B 1 202 ? 61.801  5.344   45.312  1.00 109.96 ? 388 GLU A CG  1 
ATOM   4152 C CD  . GLU B 1 202 ? 63.023  6.163   45.686  1.00 118.94 ? 388 GLU A CD  1 
ATOM   4153 O OE1 . GLU B 1 202 ? 63.828  6.500   44.791  1.00 133.65 ? 388 GLU A OE1 1 
ATOM   4154 O OE2 . GLU B 1 202 ? 63.184  6.446   46.895  1.00 106.39 ? 388 GLU A OE2 1 
ATOM   4155 N N   . ALA B 1 203 ? 58.577  4.336   41.833  1.00 93.45  ? 389 ALA A N   1 
ATOM   4156 C CA  . ALA B 1 203 ? 57.869  4.621   40.598  1.00 90.46  ? 389 ALA A CA  1 
ATOM   4157 C C   . ALA B 1 203 ? 56.804  5.695   40.825  1.00 88.42  ? 389 ALA A C   1 
ATOM   4158 O O   . ALA B 1 203 ? 56.707  6.308   41.893  1.00 90.15  ? 389 ALA A O   1 
ATOM   4159 C CB  . ALA B 1 203 ? 57.254  3.339   40.035  1.00 90.11  ? 389 ALA A CB  1 
ATOM   4160 N N   . GLU B 1 204 ? 56.013  5.945   39.781  1.00 91.58  ? 390 GLU A N   1 
ATOM   4161 C CA  . GLU B 1 204 ? 54.846  6.814   39.846  1.00 90.53  ? 390 GLU A CA  1 
ATOM   4162 C C   . GLU B 1 204 ? 53.613  6.047   39.390  1.00 76.16  ? 390 GLU A C   1 
ATOM   4163 O O   . GLU B 1 204 ? 53.655  5.331   38.386  1.00 78.28  ? 390 GLU A O   1 
ATOM   4164 C CB  . GLU B 1 204 ? 55.012  8.055   38.971  1.00 88.00  ? 390 GLU A CB  1 
ATOM   4165 C CG  . GLU B 1 204 ? 56.062  9.031   39.446  1.00 88.07  ? 390 GLU A CG  1 
ATOM   4166 C CD  . GLU B 1 204 ? 56.072  10.289  38.608  1.00 89.69  ? 390 GLU A CD  1 
ATOM   4167 O OE1 . GLU B 1 204 ? 55.345  10.318  37.592  1.00 85.33  ? 390 GLU A OE1 1 
ATOM   4168 O OE2 . GLU B 1 204 ? 56.789  11.248  38.971  1.00 82.77  ? 390 GLU A OE2 1 
ATOM   4169 N N   . LYS B 1 205 ? 52.510  6.226   40.114  1.00 77.95  ? 391 LYS A N   1 
ATOM   4170 C CA  . LYS B 1 205 ? 51.251  5.549   39.830  1.00 84.30  ? 391 LYS A CA  1 
ATOM   4171 C C   . LYS B 1 205 ? 50.171  6.576   39.518  1.00 76.88  ? 391 LYS A C   1 
ATOM   4172 O O   . LYS B 1 205 ? 50.055  7.599   40.200  1.00 79.18  ? 391 LYS A O   1 
ATOM   4173 C CB  . LYS B 1 205 ? 50.825  4.659   41.011  1.00 82.00  ? 391 LYS A CB  1 
ATOM   4174 C CG  . LYS B 1 205 ? 49.563  3.836   40.781  1.00 88.44  ? 391 LYS A CG  1 
ATOM   4175 C CD  . LYS B 1 205 ? 49.358  2.815   41.902  1.00 84.39  ? 391 LYS A CD  1 
ATOM   4176 C CE  . LYS B 1 205 ? 49.126  3.485   43.246  1.00 85.94  ? 391 LYS A CE  1 
ATOM   4177 N NZ  . LYS B 1 205 ? 47.861  4.261   43.262  1.00 87.81  ? 391 LYS A NZ  1 
ATOM   4178 N N   . GLY B 1 206 ? 49.380  6.296   38.487  1.00 67.64  ? 392 GLY A N   1 
ATOM   4179 C CA  . GLY B 1 206 ? 48.340  7.219   38.083  1.00 76.76  ? 392 GLY A CA  1 
ATOM   4180 C C   . GLY B 1 206 ? 47.241  6.511   37.324  1.00 73.05  ? 392 GLY A C   1 
ATOM   4181 O O   . GLY B 1 206 ? 47.288  5.302   37.088  1.00 73.45  ? 392 GLY A O   1 
ATOM   4182 N N   . VAL B 1 207 ? 46.236  7.293   36.943  1.00 65.55  ? 393 VAL A N   1 
ATOM   4183 C CA  . VAL B 1 207 ? 45.070  6.790   36.228  1.00 66.60  ? 393 VAL A CA  1 
ATOM   4184 C C   . VAL B 1 207 ? 44.640  7.833   35.207  1.00 63.19  ? 393 VAL A C   1 
ATOM   4185 O O   . VAL B 1 207 ? 44.556  9.023   35.526  1.00 68.08  ? 393 VAL A O   1 
ATOM   4186 C CB  . VAL B 1 207 ? 43.922  6.473   37.207  1.00 66.86  ? 393 VAL A CB  1 
ATOM   4187 C CG1 . VAL B 1 207 ? 42.577  6.641   36.538  1.00 65.26  ? 393 VAL A CG1 1 
ATOM   4188 C CG2 . VAL B 1 207 ? 44.081  5.067   37.767  1.00 74.32  ? 393 VAL A CG2 1 
ATOM   4189 N N   . LYS B 1 208 ? 44.351  7.390   33.988  1.00 61.93  ? 394 LYS A N   1 
ATOM   4190 C CA  . LYS B 1 208 ? 43.873  8.281   32.946  1.00 62.22  ? 394 LYS A CA  1 
ATOM   4191 C C   . LYS B 1 208 ? 42.639  7.671   32.300  1.00 64.22  ? 394 LYS A C   1 
ATOM   4192 O O   . LYS B 1 208 ? 42.491  6.447   32.244  1.00 68.27  ? 394 LYS A O   1 
ATOM   4193 C CB  . LYS B 1 208 ? 44.964  8.529   31.900  1.00 65.65  ? 394 LYS A CB  1 
ATOM   4194 C CG  . LYS B 1 208 ? 44.678  9.674   30.945  1.00 76.27  ? 394 LYS A CG  1 
ATOM   4195 C CD  . LYS B 1 208 ? 44.576  10.993  31.687  1.00 70.89  ? 394 LYS A CD  1 
ATOM   4196 C CE  . LYS B 1 208 ? 45.704  11.942  31.305  1.00 67.05  ? 394 LYS A CE  1 
ATOM   4197 N NZ  . LYS B 1 208 ? 45.594  12.391  29.884  1.00 71.88  ? 394 LYS A NZ  1 
ATOM   4198 N N   . PHE B 1 209 ? 41.753  8.532   31.805  1.00 61.64  ? 395 PHE A N   1 
ATOM   4199 C CA  . PHE B 1 209 ? 40.489  8.083   31.235  1.00 64.24  ? 395 PHE A CA  1 
ATOM   4200 C C   . PHE B 1 209 ? 40.697  7.711   29.773  1.00 69.50  ? 395 PHE A C   1 
ATOM   4201 O O   . PHE B 1 209 ? 41.144  8.538   28.969  1.00 74.41  ? 395 PHE A O   1 
ATOM   4202 C CB  . PHE B 1 209 ? 39.411  9.158   31.367  1.00 63.49  ? 395 PHE A CB  1 
ATOM   4203 C CG  . PHE B 1 209 ? 38.853  9.294   32.757  1.00 68.23  ? 395 PHE A CG  1 
ATOM   4204 C CD1 . PHE B 1 209 ? 37.855  8.442   33.203  1.00 62.16  ? 395 PHE A CD1 1 
ATOM   4205 C CD2 . PHE B 1 209 ? 39.328  10.266  33.621  1.00 67.65  ? 395 PHE A CD2 1 
ATOM   4206 C CE1 . PHE B 1 209 ? 37.341  8.560   34.480  1.00 63.00  ? 395 PHE A CE1 1 
ATOM   4207 C CE2 . PHE B 1 209 ? 38.817  10.387  34.899  1.00 65.16  ? 395 PHE A CE2 1 
ATOM   4208 C CZ  . PHE B 1 209 ? 37.822  9.533   35.328  1.00 64.52  ? 395 PHE A CZ  1 
ATOM   4209 N N   . LEU B 1 210 ? 40.360  6.469   29.430  1.00 66.34  ? 396 LEU A N   1 
ATOM   4210 C CA  . LEU B 1 210 ? 40.370  6.060   28.032  1.00 69.52  ? 396 LEU A CA  1 
ATOM   4211 C C   . LEU B 1 210 ? 39.080  6.487   27.347  1.00 71.96  ? 396 LEU A C   1 
ATOM   4212 O O   . LEU B 1 210 ? 39.101  7.186   26.328  1.00 75.59  ? 396 LEU A O   1 
ATOM   4213 C CB  . LEU B 1 210 ? 40.563  4.546   27.926  1.00 67.51  ? 396 LEU A CB  1 
ATOM   4214 C CG  . LEU B 1 210 ? 41.918  3.996   28.375  1.00 70.34  ? 396 LEU A CG  1 
ATOM   4215 C CD1 . LEU B 1 210 ? 41.914  2.474   28.357  1.00 64.91  ? 396 LEU A CD1 1 
ATOM   4216 C CD2 . LEU B 1 210 ? 43.032  4.543   27.498  1.00 70.91  ? 396 LEU A CD2 1 
ATOM   4217 N N   . THR B 1 211 ? 37.942  6.079   27.904  1.00 70.97  ? 397 THR A N   1 
ATOM   4218 C CA  . THR B 1 211 ? 36.642  6.414   27.351  1.00 67.59  ? 397 THR A CA  1 
ATOM   4219 C C   . THR B 1 211 ? 35.712  6.785   28.494  1.00 61.30  ? 397 THR A C   1 
ATOM   4220 O O   . THR B 1 211 ? 35.907  6.374   29.639  1.00 64.81  ? 397 THR A O   1 
ATOM   4221 C CB  . THR B 1 211 ? 36.029  5.255   26.558  1.00 74.08  ? 397 THR A CB  1 
ATOM   4222 O OG1 . THR B 1 211 ? 35.806  4.143   27.435  1.00 63.76  ? 397 THR A OG1 1 
ATOM   4223 C CG2 . THR B 1 211 ? 36.954  4.827   25.417  1.00 73.23  ? 397 THR A CG2 1 
ATOM   4224 N N   . LEU B 1 212 ? 34.693  7.569   28.163  1.00 65.28  ? 398 LEU A N   1 
ATOM   4225 C CA  . LEU B 1 212 ? 33.677  7.991   29.109  1.00 64.50  ? 398 LEU A CA  1 
ATOM   4226 C C   . LEU B 1 212 ? 32.307  7.536   28.617  1.00 65.76  ? 398 LEU A C   1 
ATOM   4227 O O   . LEU B 1 212 ? 31.992  7.708   27.430  1.00 65.95  ? 398 LEU A O   1 
ATOM   4228 C CB  . LEU B 1 212 ? 33.699  9.516   29.290  1.00 63.98  ? 398 LEU A CB  1 
ATOM   4229 C CG  . LEU B 1 212 ? 34.843  10.133  30.089  1.00 63.26  ? 398 LEU A CG  1 
ATOM   4230 C CD1 . LEU B 1 212 ? 34.876  11.632  29.879  1.00 64.91  ? 398 LEU A CD1 1 
ATOM   4231 C CD2 . LEU B 1 212 ? 34.654  9.815   31.556  1.00 63.46  ? 398 LEU A CD2 1 
ATOM   4232 N N   . PRO B 1 213 ? 31.471  6.964   29.481  1.00 71.19  ? 399 PRO A N   1 
ATOM   4233 C CA  . PRO B 1 213 ? 30.219  6.346   29.017  1.00 61.49  ? 399 PRO A CA  1 
ATOM   4234 C C   . PRO B 1 213 ? 29.229  7.396   28.549  1.00 61.73  ? 399 PRO A C   1 
ATOM   4235 O O   . PRO B 1 213 ? 29.393  8.590   28.845  1.00 63.09  ? 399 PRO A O   1 
ATOM   4236 C CB  . PRO B 1 213 ? 29.700  5.613   30.268  1.00 59.98  ? 399 PRO A CB  1 
ATOM   4237 C CG  . PRO B 1 213 ? 30.848  5.615   31.248  1.00 60.66  ? 399 PRO A CG  1 
ATOM   4238 C CD  . PRO B 1 213 ? 31.637  6.841   30.938  1.00 66.21  ? 399 PRO A CD  1 
ATOM   4239 N N   . PRO B 1 214 ? 28.203  6.998   27.787  1.00 61.64  ? 400 PRO A N   1 
ATOM   4240 C CA  . PRO B 1 214 ? 27.140  7.957   27.444  1.00 63.28  ? 400 PRO A CA  1 
ATOM   4241 C C   . PRO B 1 214 ? 26.419  8.500   28.663  1.00 64.56  ? 400 PRO A C   1 
ATOM   4242 O O   . PRO B 1 214 ? 26.001  9.664   28.658  1.00 66.19  ? 400 PRO A O   1 
ATOM   4243 C CB  . PRO B 1 214 ? 26.200  7.135   26.549  1.00 62.78  ? 400 PRO A CB  1 
ATOM   4244 C CG  . PRO B 1 214 ? 27.040  6.017   26.036  1.00 60.94  ? 400 PRO A CG  1 
ATOM   4245 C CD  . PRO B 1 214 ? 27.990  5.691   27.145  1.00 60.17  ? 400 PRO A CD  1 
ATOM   4246 N N   . VAL B 1 215 ? 26.279  7.701   29.717  1.00 55.98  ? 401 VAL A N   1 
ATOM   4247 C CA  . VAL B 1 215 ? 25.655  8.131   30.962  1.00 60.50  ? 401 VAL A CA  1 
ATOM   4248 C C   . VAL B 1 215 ? 26.706  8.045   32.062  1.00 60.10  ? 401 VAL A C   1 
ATOM   4249 O O   . VAL B 1 215 ? 27.250  6.966   32.330  1.00 61.75  ? 401 VAL A O   1 
ATOM   4250 C CB  . VAL B 1 215 ? 24.419  7.287   31.310  1.00 64.67  ? 401 VAL A CB  1 
ATOM   4251 C CG1 . VAL B 1 215 ? 23.759  7.823   32.567  1.00 55.12  ? 401 VAL A CG1 1 
ATOM   4252 C CG2 . VAL B 1 215 ? 23.429  7.278   30.144  1.00 57.65  ? 401 VAL A CG2 1 
ATOM   4253 N N   . LEU B 1 216 ? 26.990  9.181   32.694  1.00 54.25  ? 402 LEU A N   1 
ATOM   4254 C CA  . LEU B 1 216 ? 28.086  9.316   33.645  1.00 53.77  ? 402 LEU A CA  1 
ATOM   4255 C C   . LEU B 1 216 ? 27.502  9.454   35.044  1.00 53.38  ? 402 LEU A C   1 
ATOM   4256 O O   . LEU B 1 216 ? 26.803  10.432  35.332  1.00 59.56  ? 402 LEU A O   1 
ATOM   4257 C CB  . LEU B 1 216 ? 28.954  10.528  33.291  1.00 58.39  ? 402 LEU A CB  1 
ATOM   4258 C CG  . LEU B 1 216 ? 30.372  10.673  33.859  1.00 55.78  ? 402 LEU A CG  1 
ATOM   4259 C CD1 . LEU B 1 216 ? 31.294  9.595   33.320  1.00 54.07  ? 402 LEU A CD1 1 
ATOM   4260 C CD2 . LEU B 1 216 ? 30.933  12.054  33.547  1.00 54.22  ? 402 LEU A CD2 1 
ATOM   4261 N N   . HIS B 1 217 ? 27.784  8.478   35.910  1.00 53.17  ? 403 HIS A N   1 
ATOM   4262 C CA  . HIS B 1 217 ? 27.337  8.500   37.303  1.00 54.36  ? 403 HIS A CA  1 
ATOM   4263 C C   . HIS B 1 217 ? 28.479  8.998   38.185  1.00 58.51  ? 403 HIS A C   1 
ATOM   4264 O O   . HIS B 1 217 ? 29.474  8.291   38.384  1.00 58.29  ? 403 HIS A O   1 
ATOM   4265 C CB  . HIS B 1 217 ? 26.868  7.120   37.763  1.00 55.15  ? 403 HIS A CB  1 
ATOM   4266 C CG  . HIS B 1 217 ? 25.467  6.783   37.357  1.00 59.83  ? 403 HIS A CG  1 
ATOM   4267 N ND1 . HIS B 1 217 ? 24.639  7.677   36.712  1.00 56.21  ? 403 HIS A ND1 1 
ATOM   4268 C CD2 . HIS B 1 217 ? 24.745  5.649   37.515  1.00 56.92  ? 403 HIS A CD2 1 
ATOM   4269 C CE1 . HIS B 1 217 ? 23.470  7.106   36.485  1.00 56.49  ? 403 HIS A CE1 1 
ATOM   4270 N NE2 . HIS B 1 217 ? 23.509  5.875   36.962  1.00 57.81  ? 403 HIS A NE2 1 
ATOM   4271 N N   . LEU B 1 218 ? 28.322  10.200  38.733  1.00 53.65  ? 404 LEU A N   1 
ATOM   4272 C CA  . LEU B 1 218 ? 29.330  10.827  39.579  1.00 52.91  ? 404 LEU A CA  1 
ATOM   4273 C C   . LEU B 1 218 ? 28.822  10.883  41.013  1.00 53.06  ? 404 LEU A C   1 
ATOM   4274 O O   . LEU B 1 218 ? 27.820  11.548  41.292  1.00 57.11  ? 404 LEU A O   1 
ATOM   4275 C CB  . LEU B 1 218 ? 29.649  12.239  39.087  1.00 53.09  ? 404 LEU A CB  1 
ATOM   4276 C CG  . LEU B 1 218 ? 30.125  12.393  37.647  1.00 53.21  ? 404 LEU A CG  1 
ATOM   4277 C CD1 . LEU B 1 218 ? 30.381  13.860  37.326  1.00 53.62  ? 404 LEU A CD1 1 
ATOM   4278 C CD2 . LEU B 1 218 ? 31.374  11.565  37.432  1.00 55.98  ? 404 LEU A CD2 1 
ATOM   4279 N N   . GLN B 1 219 ? 29.520  10.209  41.919  1.00 53.21  ? 405 GLN A N   1 
ATOM   4280 C CA  . GLN B 1 219 ? 29.239  10.298  43.343  1.00 53.59  ? 405 GLN A CA  1 
ATOM   4281 C C   . GLN B 1 219 ? 30.209  11.286  43.977  1.00 58.17  ? 405 GLN A C   1 
ATOM   4282 O O   . GLN B 1 219 ? 31.425  11.186  43.784  1.00 58.86  ? 405 GLN A O   1 
ATOM   4283 C CB  . GLN B 1 219 ? 29.347  8.933   44.021  1.00 53.86  ? 405 GLN A CB  1 
ATOM   4284 C CG  . GLN B 1 219 ? 28.109  8.068   43.915  1.00 59.21  ? 405 GLN A CG  1 
ATOM   4285 C CD  . GLN B 1 219 ? 28.053  7.270   42.637  1.00 61.61  ? 405 GLN A CD  1 
ATOM   4286 O OE1 . GLN B 1 219 ? 29.074  7.037   41.997  1.00 63.31  ? 405 GLN A OE1 1 
ATOM   4287 N NE2 . GLN B 1 219 ? 26.853  6.837   42.260  1.00 61.57  ? 405 GLN A NE2 1 
ATOM   4288 N N   . LEU B 1 220 ? 29.667  12.235  44.730  1.00 62.28  ? 406 LEU A N   1 
ATOM   4289 C CA  . LEU B 1 220 ? 30.440  13.321  45.317  1.00 55.91  ? 406 LEU A CA  1 
ATOM   4290 C C   . LEU B 1 220 ? 30.762  12.959  46.762  1.00 67.00  ? 406 LEU A C   1 
ATOM   4291 O O   . LEU B 1 220 ? 29.884  12.990  47.630  1.00 66.29  ? 406 LEU A O   1 
ATOM   4292 C CB  . LEU B 1 220 ? 29.669  14.635  45.227  1.00 55.01  ? 406 LEU A CB  1 
ATOM   4293 C CG  . LEU B 1 220 ? 29.293  15.096  43.823  1.00 54.60  ? 406 LEU A CG  1 
ATOM   4294 C CD1 . LEU B 1 220 ? 28.810  16.532  43.861  1.00 55.16  ? 406 LEU A CD1 1 
ATOM   4295 C CD2 . LEU B 1 220 ? 30.482  14.951  42.897  1.00 55.19  ? 406 LEU A CD2 1 
ATOM   4296 N N   . MET B 1 221 ? 32.032  12.638  47.016  1.00 64.52  ? 407 MET A N   1 
ATOM   4297 C CA  . MET B 1 221 ? 32.476  12.114  48.308  1.00 62.65  ? 407 MET A CA  1 
ATOM   4298 C C   . MET B 1 221 ? 32.680  13.254  49.309  1.00 68.13  ? 407 MET A C   1 
ATOM   4299 O O   . MET B 1 221 ? 33.801  13.637  49.651  1.00 75.04  ? 407 MET A O   1 
ATOM   4300 C CB  . MET B 1 221 ? 33.761  11.320  48.128  1.00 61.01  ? 407 MET A CB  1 
ATOM   4301 C CG  . MET B 1 221 ? 33.635  10.131  47.198  1.00 61.56  ? 407 MET A CG  1 
ATOM   4302 S SD  . MET B 1 221 ? 32.682  8.790   47.921  1.00 69.13  ? 407 MET A SD  1 
ATOM   4303 C CE  . MET B 1 221 ? 31.352  8.666   46.754  1.00 55.42  ? 407 MET A CE  1 
ATOM   4304 N N   . ARG B 1 222 ? 31.567  13.797  49.797  1.00 58.85  ? 408 ARG A N   1 
ATOM   4305 C CA  . ARG B 1 222 ? 31.629  14.856  50.804  1.00 67.99  ? 408 ARG A CA  1 
ATOM   4306 C C   . ARG B 1 222 ? 31.379  14.266  52.192  1.00 71.85  ? 408 ARG A C   1 
ATOM   4307 O O   . ARG B 1 222 ? 30.323  14.446  52.798  1.00 77.22  ? 408 ARG A O   1 
ATOM   4308 C CB  . ARG B 1 222 ? 30.632  15.967  50.481  1.00 67.59  ? 408 ARG A CB  1 
ATOM   4309 C CG  . ARG B 1 222 ? 29.298  15.474  49.961  1.00 68.30  ? 408 ARG A CG  1 
ATOM   4310 C CD  . ARG B 1 222 ? 28.244  16.576  49.954  1.00 65.93  ? 408 ARG A CD  1 
ATOM   4311 N NE  . ARG B 1 222 ? 28.509  17.635  48.985  1.00 61.12  ? 408 ARG A NE  1 
ATOM   4312 C CZ  . ARG B 1 222 ? 28.921  18.857  49.300  1.00 65.05  ? 408 ARG A CZ  1 
ATOM   4313 N NH1 . ARG B 1 222 ? 29.144  19.210  50.556  1.00 68.86  ? 408 ARG A NH1 1 
ATOM   4314 N NH2 . ARG B 1 222 ? 29.120  19.746  48.330  1.00 58.93  ? 408 ARG A NH2 1 
ATOM   4315 N N   . PHE B 1 223 ? 32.390  13.563  52.703  1.00 75.61  ? 409 PHE A N   1 
ATOM   4316 C CA  . PHE B 1 223 ? 32.297  13.028  54.057  1.00 80.44  ? 409 PHE A CA  1 
ATOM   4317 C C   . PHE B 1 223 ? 33.677  12.626  54.554  1.00 80.98  ? 409 PHE A C   1 
ATOM   4318 O O   . PHE B 1 223 ? 34.617  12.462  53.773  1.00 79.50  ? 409 PHE A O   1 
ATOM   4319 C CB  . PHE B 1 223 ? 31.357  11.821  54.136  1.00 80.99  ? 409 PHE A CB  1 
ATOM   4320 C CG  . PHE B 1 223 ? 31.936  10.558  53.562  1.00 78.61  ? 409 PHE A CG  1 
ATOM   4321 C CD1 . PHE B 1 223 ? 31.988  10.361  52.193  1.00 75.03  ? 409 PHE A CD1 1 
ATOM   4322 C CD2 . PHE B 1 223 ? 32.422  9.564   54.397  1.00 77.96  ? 409 PHE A CD2 1 
ATOM   4323 C CE1 . PHE B 1 223 ? 32.514  9.196   51.665  1.00 75.28  ? 409 PHE A CE1 1 
ATOM   4324 C CE2 . PHE B 1 223 ? 32.951  8.398   53.876  1.00 79.09  ? 409 PHE A CE2 1 
ATOM   4325 C CZ  . PHE B 1 223 ? 32.995  8.213   52.506  1.00 76.57  ? 409 PHE A CZ  1 
ATOM   4326 N N   . MET B 1 224 ? 33.774  12.464  55.872  1.00 88.46  ? 410 MET A N   1 
ATOM   4327 C CA  . MET B 1 224 ? 35.005  12.024  56.526  1.00 87.01  ? 410 MET A CA  1 
ATOM   4328 C C   . MET B 1 224 ? 34.700  11.434  57.902  1.00 85.22  ? 410 MET A C   1 
ATOM   4329 O O   . MET B 1 224 ? 35.477  10.642  58.439  1.00 97.05  ? 410 MET A O   1 
ATOM   4330 C CB  . MET B 1 224 ? 35.999  13.180  56.648  1.00 87.66  ? 410 MET A CB  1 
ATOM   4331 C CG  . MET B 1 224 ? 35.498  14.356  57.469  1.00 85.18  ? 410 MET A CG  1 
ATOM   4332 S SD  . MET B 1 224 ? 36.821  15.502  57.919  1.00 120.04 ? 410 MET A SD  1 
ATOM   4333 C CE  . MET B 1 224 ? 37.480  15.937  56.308  1.00 93.77  ? 410 MET A CE  1 
ATOM   4334 N N   . GLN B 1 228 ? 40.310  10.888  65.808  1.00 120.04 ? 414 GLN A N   1 
ATOM   4335 C CA  . GLN B 1 228 ? 39.103  10.565  66.574  1.00 117.95 ? 414 GLN A CA  1 
ATOM   4336 C C   . GLN B 1 228 ? 37.991  10.087  65.640  1.00 126.12 ? 414 GLN A C   1 
ATOM   4337 O O   . GLN B 1 228 ? 37.896  10.544  64.494  1.00 124.66 ? 414 GLN A O   1 
ATOM   4338 C CB  . GLN B 1 228 ? 38.646  11.787  67.370  1.00 114.95 ? 414 GLN A CB  1 
ATOM   4339 C CG  . GLN B 1 228 ? 37.947  12.850  66.537  1.00 122.11 ? 414 GLN A CG  1 
ATOM   4340 C CD  . GLN B 1 228 ? 37.369  13.958  67.384  1.00 124.57 ? 414 GLN A CD  1 
ATOM   4341 O OE1 . GLN B 1 228 ? 37.649  14.049  68.580  1.00 128.70 ? 414 GLN A OE1 1 
ATOM   4342 N NE2 . GLN B 1 228 ? 36.527  14.792  66.774  1.00 95.65  ? 414 GLN A NE2 1 
ATOM   4343 N N   . THR B 1 229 ? 37.174  9.143   66.107  1.00 129.13 ? 415 THR A N   1 
ATOM   4344 C CA  . THR B 1 229 ? 36.087  8.626   65.284  1.00 135.81 ? 415 THR A CA  1 
ATOM   4345 C C   . THR B 1 229 ? 35.058  7.933   66.163  1.00 142.16 ? 415 THR A C   1 
ATOM   4346 O O   . THR B 1 229 ? 35.421  7.225   67.104  1.00 141.12 ? 415 THR A O   1 
ATOM   4347 C CB  . THR B 1 229 ? 36.613  7.622   64.235  1.00 135.13 ? 415 THR A CB  1 
ATOM   4348 O OG1 . THR B 1 229 ? 37.524  8.279   63.344  1.00 132.78 ? 415 THR A OG1 1 
ATOM   4349 C CG2 . THR B 1 229 ? 35.469  6.997   63.416  1.00 132.59 ? 415 THR A CG2 1 
ATOM   4350 N N   . ASP B 1 230 ? 33.778  8.159   65.873  1.00 161.42 ? 416 ASP A N   1 
ATOM   4351 C CA  . ASP B 1 230 ? 32.761  7.209   66.308  1.00 156.74 ? 416 ASP A CA  1 
ATOM   4352 C C   . ASP B 1 230 ? 31.638  7.165   65.282  1.00 150.26 ? 416 ASP A C   1 
ATOM   4353 O O   . ASP B 1 230 ? 30.728  6.333   65.369  1.00 142.45 ? 416 ASP A O   1 
ATOM   4354 C CB  . ASP B 1 230 ? 32.208  7.577   67.685  1.00 149.65 ? 416 ASP A CB  1 
ATOM   4355 C CG  . ASP B 1 230 ? 31.310  6.495   68.250  1.00 157.89 ? 416 ASP A CG  1 
ATOM   4356 O OD1 . ASP B 1 230 ? 31.832  5.433   68.643  1.00 167.30 ? 416 ASP A OD1 1 
ATOM   4357 O OD2 . ASP B 1 230 ? 30.074  6.689   68.250  1.00 159.52 ? 416 ASP A OD2 1 
ATOM   4358 N N   . GLN B 1 231 ? 31.715  8.047   64.290  1.00 135.85 ? 417 GLN A N   1 
ATOM   4359 C CA  . GLN B 1 231 ? 30.664  8.173   63.290  1.00 120.27 ? 417 GLN A CA  1 
ATOM   4360 C C   . GLN B 1 231 ? 31.259  8.612   61.958  1.00 110.96 ? 417 GLN A C   1 
ATOM   4361 O O   . GLN B 1 231 ? 32.429  9.000   61.860  1.00 117.38 ? 417 GLN A O   1 
ATOM   4362 C CB  . GLN B 1 231 ? 29.552  9.142   63.713  1.00 120.68 ? 417 GLN A CB  1 
ATOM   4363 C CG  . GLN B 1 231 ? 28.703  8.717   64.899  1.00 121.75 ? 417 GLN A CG  1 
ATOM   4364 C CD  . GLN B 1 231 ? 27.663  9.767   65.253  1.00 112.65 ? 417 GLN A CD  1 
ATOM   4365 O OE1 . GLN B 1 231 ? 27.748  10.914  64.813  1.00 107.46 ? 417 GLN A OE1 1 
ATOM   4366 N NE2 . GLN B 1 231 ? 26.655  9.369   66.016  1.00 112.81 ? 417 GLN A NE2 1 
ATOM   4367 N N   . ASN B 1 232 ? 30.433  8.509   60.920  1.00 103.66 ? 418 ASN A N   1 
ATOM   4368 C CA  . ASN B 1 232 ? 30.722  9.088   59.613  1.00 99.03  ? 418 ASN A CA  1 
ATOM   4369 C C   . ASN B 1 232 ? 30.119  10.492  59.567  1.00 91.36  ? 418 ASN A C   1 
ATOM   4370 O O   . ASN B 1 232 ? 28.902  10.650  59.725  1.00 87.33  ? 418 ASN A O   1 
ATOM   4371 C CB  . ASN B 1 232 ? 30.142  8.221   58.495  1.00 92.90  ? 418 ASN A CB  1 
ATOM   4372 C CG  . ASN B 1 232 ? 30.700  6.808   58.486  1.00 88.64  ? 418 ASN A CG  1 
ATOM   4373 O OD1 . ASN B 1 232 ? 31.822  6.574   58.039  1.00 85.51  ? 418 ASN A OD1 1 
ATOM   4374 N ND2 . ASN B 1 232 ? 29.907  5.854   58.965  1.00 85.41  ? 418 ASN A ND2 1 
ATOM   4375 N N   . ILE B 1 233 ? 30.960  11.506  59.363  1.00 85.97  ? 419 ILE A N   1 
ATOM   4376 C CA  . ILE B 1 233 ? 30.527  12.898  59.403  1.00 84.30  ? 419 ILE A CA  1 
ATOM   4377 C C   . ILE B 1 233 ? 30.475  13.441  57.976  1.00 86.55  ? 419 ILE A C   1 
ATOM   4378 O O   . ILE B 1 233 ? 31.113  12.912  57.063  1.00 89.87  ? 419 ILE A O   1 
ATOM   4379 C CB  . ILE B 1 233 ? 31.483  13.733  60.295  1.00 89.60  ? 419 ILE A CB  1 
ATOM   4380 C CG1 . ILE B 1 233 ? 30.992  15.171  60.501  1.00 95.47  ? 419 ILE A CG1 1 
ATOM   4381 C CG2 . ILE B 1 233 ? 32.894  13.716  59.722  1.00 88.13  ? 419 ILE A CG2 1 
ATOM   4382 C CD1 . ILE B 1 233 ? 31.761  15.940  61.574  1.00 85.65  ? 419 ILE A CD1 1 
ATOM   4383 N N   . LYS B 1 234 ? 29.730  14.534  57.792  1.00 80.89  ? 420 LYS A N   1 
ATOM   4384 C CA  . LYS B 1 234 ? 29.534  15.142  56.480  1.00 79.67  ? 420 LYS A CA  1 
ATOM   4385 C C   . LYS B 1 234 ? 30.440  16.350  56.286  1.00 80.76  ? 420 LYS A C   1 
ATOM   4386 O O   . LYS B 1 234 ? 30.718  17.091  57.233  1.00 81.46  ? 420 LYS A O   1 
ATOM   4387 C CB  . LYS B 1 234 ? 28.080  15.573  56.268  1.00 76.49  ? 420 LYS A CB  1 
ATOM   4388 C CG  . LYS B 1 234 ? 27.118  14.423  56.227  1.00 78.02  ? 420 LYS A CG  1 
ATOM   4389 C CD  . LYS B 1 234 ? 25.800  14.743  56.924  1.00 75.85  ? 420 LYS A CD  1 
ATOM   4390 C CE  . LYS B 1 234 ? 25.158  16.029  56.383  1.00 82.45  ? 420 LYS A CE  1 
ATOM   4391 N NZ  . LYS B 1 234 ? 25.381  17.225  57.262  1.00 74.65  ? 420 LYS A NZ  1 
ATOM   4392 N N   . ILE B 1 235 ? 30.911  16.524  55.056  1.00 76.81  ? 421 ILE A N   1 
ATOM   4393 C CA  . ILE B 1 235 ? 31.656  17.705  54.631  1.00 77.70  ? 421 ILE A CA  1 
ATOM   4394 C C   . ILE B 1 235 ? 30.670  18.641  53.934  1.00 83.54  ? 421 ILE A C   1 
ATOM   4395 O O   . ILE B 1 235 ? 30.296  18.416  52.779  1.00 83.56  ? 421 ILE A O   1 
ATOM   4396 C CB  . ILE B 1 235 ? 32.824  17.330  53.713  1.00 74.44  ? 421 ILE A CB  1 
ATOM   4397 C CG1 . ILE B 1 235 ? 33.819  16.425  54.444  1.00 82.38  ? 421 ILE A CG1 1 
ATOM   4398 C CG2 . ILE B 1 235 ? 33.499  18.566  53.178  1.00 70.71  ? 421 ILE A CG2 1 
ATOM   4399 C CD1 . ILE B 1 235 ? 35.038  16.037  53.614  1.00 75.16  ? 421 ILE A CD1 1 
ATOM   4400 N N   . ASN B 1 236 ? 30.233  19.695  54.632  1.00 79.66  ? 422 ASN A N   1 
ATOM   4401 C CA  . ASN B 1 236 ? 29.270  20.653  54.091  1.00 78.01  ? 422 ASN A CA  1 
ATOM   4402 C C   . ASN B 1 236 ? 29.919  21.738  53.235  1.00 81.27  ? 422 ASN A C   1 
ATOM   4403 O O   . ASN B 1 236 ? 29.312  22.798  53.039  1.00 87.39  ? 422 ASN A O   1 
ATOM   4404 C CB  . ASN B 1 236 ? 28.470  21.300  55.224  1.00 79.21  ? 422 ASN A CB  1 
ATOM   4405 C CG  . ASN B 1 236 ? 27.714  20.288  56.049  1.00 87.96  ? 422 ASN A CG  1 
ATOM   4406 O OD1 . ASN B 1 236 ? 27.254  19.269  55.529  1.00 89.69  ? 422 ASN A OD1 1 
ATOM   4407 N ND2 . ASN B 1 236 ? 27.584  20.555  57.344  1.00 86.41  ? 422 ASN A ND2 1 
ATOM   4408 N N   . ASP B 1 237 ? 31.128  21.503  52.732  1.00 77.93  ? 423 ASP A N   1 
ATOM   4409 C CA  . ASP B 1 237 ? 31.856  22.521  51.989  1.00 78.31  ? 423 ASP A CA  1 
ATOM   4410 C C   . ASP B 1 237 ? 31.176  22.828  50.655  1.00 72.85  ? 423 ASP A C   1 
ATOM   4411 O O   . ASP B 1 237 ? 30.422  22.019  50.103  1.00 70.78  ? 423 ASP A O   1 
ATOM   4412 C CB  . ASP B 1 237 ? 33.298  22.077  51.736  1.00 83.31  ? 423 ASP A CB  1 
ATOM   4413 C CG  . ASP B 1 237 ? 34.065  21.823  53.016  1.00 84.20  ? 423 ASP A CG  1 
ATOM   4414 O OD1 . ASP B 1 237 ? 33.438  21.847  54.099  1.00 82.64  ? 423 ASP A OD1 1 
ATOM   4415 O OD2 . ASP B 1 237 ? 35.294  21.591  52.936  1.00 81.85  ? 423 ASP A OD2 1 
ATOM   4416 N N   . ARG B 1 238 ? 31.454  24.025  50.144  1.00 69.55  ? 424 ARG A N   1 
ATOM   4417 C CA  . ARG B 1 238 ? 30.934  24.432  48.846  1.00 69.75  ? 424 ARG A CA  1 
ATOM   4418 C C   . ARG B 1 238 ? 31.645  23.691  47.718  1.00 76.59  ? 424 ARG A C   1 
ATOM   4419 O O   . ARG B 1 238 ? 32.872  23.547  47.719  1.00 73.79  ? 424 ARG A O   1 
ATOM   4420 C CB  . ARG B 1 238 ? 31.092  25.939  48.657  1.00 67.85  ? 424 ARG A CB  1 
ATOM   4421 C CG  . ARG B 1 238 ? 30.582  26.428  47.315  1.00 68.07  ? 424 ARG A CG  1 
ATOM   4422 C CD  . ARG B 1 238 ? 31.073  27.825  47.015  1.00 69.43  ? 424 ARG A CD  1 
ATOM   4423 N NE  . ARG B 1 238 ? 30.491  28.351  45.788  1.00 66.26  ? 424 ARG A NE  1 
ATOM   4424 C CZ  . ARG B 1 238 ? 29.323  28.975  45.727  1.00 78.70  ? 424 ARG A CZ  1 
ATOM   4425 N NH1 . ARG B 1 238 ? 28.577  29.151  46.807  1.00 83.61  ? 424 ARG A NH1 1 
ATOM   4426 N NH2 . ARG B 1 238 ? 28.889  29.427  44.554  1.00 78.41  ? 424 ARG A NH2 1 
ATOM   4427 N N   . PHE B 1 239 ? 30.861  23.224  46.747  1.00 74.54  ? 425 PHE A N   1 
ATOM   4428 C CA  . PHE B 1 239 ? 31.384  22.491  45.600  1.00 68.05  ? 425 PHE A CA  1 
ATOM   4429 C C   . PHE B 1 239 ? 30.524  22.808  44.384  1.00 64.13  ? 425 PHE A C   1 
ATOM   4430 O O   . PHE B 1 239 ? 29.301  22.656  44.438  1.00 70.78  ? 425 PHE A O   1 
ATOM   4431 C CB  . PHE B 1 239 ? 31.394  20.988  45.893  1.00 67.04  ? 425 PHE A CB  1 
ATOM   4432 C CG  . PHE B 1 239 ? 31.920  20.145  44.773  1.00 65.02  ? 425 PHE A CG  1 
ATOM   4433 C CD1 . PHE B 1 239 ? 33.279  19.935  44.626  1.00 62.63  ? 425 PHE A CD1 1 
ATOM   4434 C CD2 . PHE B 1 239 ? 31.050  19.523  43.892  1.00 63.97  ? 425 PHE A CD2 1 
ATOM   4435 C CE1 . PHE B 1 239 ? 33.758  19.145  43.603  1.00 63.77  ? 425 PHE A CE1 1 
ATOM   4436 C CE2 . PHE B 1 239 ? 31.524  18.731  42.870  1.00 59.33  ? 425 PHE A CE2 1 
ATOM   4437 C CZ  . PHE B 1 239 ? 32.877  18.540  42.725  1.00 61.54  ? 425 PHE A CZ  1 
ATOM   4438 N N   . GLU B 1 240 ? 31.156  23.246  43.300  1.00 59.44  ? 426 GLU A N   1 
ATOM   4439 C CA  . GLU B 1 240 ? 30.443  23.713  42.118  1.00 59.53  ? 426 GLU A CA  1 
ATOM   4440 C C   . GLU B 1 240 ? 30.473  22.667  41.010  1.00 63.68  ? 426 GLU A C   1 
ATOM   4441 O O   . GLU B 1 240 ? 31.488  21.996  40.800  1.00 69.23  ? 426 GLU A O   1 
ATOM   4442 C CB  . GLU B 1 240 ? 31.041  25.025  41.604  1.00 61.92  ? 426 GLU A CB  1 
ATOM   4443 C CG  . GLU B 1 240 ? 31.010  26.170  42.605  1.00 63.46  ? 426 GLU A CG  1 
ATOM   4444 C CD  . GLU B 1 240 ? 31.705  27.413  42.083  1.00 73.98  ? 426 GLU A CD  1 
ATOM   4445 O OE1 . GLU B 1 240 ? 32.276  27.350  40.971  1.00 78.14  ? 426 GLU A OE1 1 
ATOM   4446 O OE2 . GLU B 1 240 ? 31.680  28.451  42.782  1.00 72.86  ? 426 GLU A OE2 1 
ATOM   4447 N N   . PHE B 1 241 ? 29.341  22.519  40.311  1.00 58.28  ? 427 PHE A N   1 
ATOM   4448 C CA  . PHE B 1 241 ? 29.252  21.658  39.136  1.00 60.16  ? 427 PHE A CA  1 
ATOM   4449 C C   . PHE B 1 241 ? 28.495  22.403  38.038  1.00 63.58  ? 427 PHE A C   1 
ATOM   4450 O O   . PHE B 1 241 ? 27.433  22.994  38.311  1.00 63.01  ? 427 PHE A O   1 
ATOM   4451 C CB  . PHE B 1 241 ? 28.574  20.318  39.450  1.00 56.60  ? 427 PHE A CB  1 
ATOM   4452 C CG  . PHE B 1 241 ? 27.245  20.451  40.136  1.00 63.42  ? 427 PHE A CG  1 
ATOM   4453 C CD1 . PHE B 1 241 ? 27.162  20.519  41.514  1.00 60.70  ? 427 PHE A CD1 1 
ATOM   4454 C CD2 . PHE B 1 241 ? 26.072  20.492  39.397  1.00 68.81  ? 427 PHE A CD2 1 
ATOM   4455 C CE1 . PHE B 1 241 ? 25.938  20.639  42.142  1.00 66.09  ? 427 PHE A CE1 1 
ATOM   4456 C CE2 . PHE B 1 241 ? 24.845  20.611  40.019  1.00 64.18  ? 427 PHE A CE2 1 
ATOM   4457 C CZ  . PHE B 1 241 ? 24.777  20.684  41.392  1.00 66.01  ? 427 PHE A CZ  1 
ATOM   4458 N N   . PRO B 1 242 ? 29.001  22.404  36.809  1.00 58.50  ? 428 PRO A N   1 
ATOM   4459 C CA  . PRO B 1 242 ? 28.368  23.165  35.730  1.00 59.46  ? 428 PRO A CA  1 
ATOM   4460 C C   . PRO B 1 242 ? 27.263  22.384  35.029  1.00 61.57  ? 428 PRO A C   1 
ATOM   4461 O O   . PRO B 1 242 ? 27.194  21.155  35.083  1.00 58.09  ? 428 PRO A O   1 
ATOM   4462 C CB  . PRO B 1 242 ? 29.535  23.418  34.768  1.00 63.74  ? 428 PRO A CB  1 
ATOM   4463 C CG  . PRO B 1 242 ? 30.375  22.182  34.921  1.00 58.89  ? 428 PRO A CG  1 
ATOM   4464 C CD  . PRO B 1 242 ? 30.243  21.746  36.364  1.00 58.09  ? 428 PRO A CD  1 
ATOM   4465 N N   . GLU B 1 243 ? 26.375  23.136  34.370  1.00 64.07  ? 429 GLU A N   1 
ATOM   4466 C CA  . GLU B 1 243 ? 25.350  22.502  33.546  1.00 64.06  ? 429 GLU A CA  1 
ATOM   4467 C C   . GLU B 1 243 ? 25.974  21.721  32.397  1.00 66.84  ? 429 GLU A C   1 
ATOM   4468 O O   . GLU B 1 243 ? 25.454  20.672  31.999  1.00 68.63  ? 429 GLU A O   1 
ATOM   4469 C CB  . GLU B 1 243 ? 24.376  23.555  33.009  1.00 68.09  ? 429 GLU A CB  1 
ATOM   4470 C CG  . GLU B 1 243 ? 23.214  22.987  32.192  1.00 78.39  ? 429 GLU A CG  1 
ATOM   4471 C CD  . GLU B 1 243 ? 22.229  24.058  31.738  1.00 85.51  ? 429 GLU A CD  1 
ATOM   4472 O OE1 . GLU B 1 243 ? 22.667  25.197  31.468  1.00 82.29  ? 429 GLU A OE1 1 
ATOM   4473 O OE2 . GLU B 1 243 ? 21.012  23.765  31.683  1.00 76.55  ? 429 GLU A OE2 1 
ATOM   4474 N N   . GLN B 1 244 ? 27.082  22.218  31.856  1.00 71.32  ? 430 GLN A N   1 
ATOM   4475 C CA  . GLN B 1 244 ? 27.814  21.565  30.781  1.00 63.88  ? 430 GLN A CA  1 
ATOM   4476 C C   . GLN B 1 244 ? 29.250  21.337  31.228  1.00 62.91  ? 430 GLN A C   1 
ATOM   4477 O O   . GLN B 1 244 ? 29.925  22.277  31.663  1.00 60.46  ? 430 GLN A O   1 
ATOM   4478 C CB  . GLN B 1 244 ? 27.771  22.405  29.504  1.00 63.62  ? 430 GLN A CB  1 
ATOM   4479 C CG  . GLN B 1 244 ? 26.365  22.678  28.994  1.00 69.25  ? 430 GLN A CG  1 
ATOM   4480 C CD  . GLN B 1 244 ? 26.371  23.515  27.736  1.00 86.74  ? 430 GLN A CD  1 
ATOM   4481 O OE1 . GLN B 1 244 ? 27.237  24.372  27.554  1.00 90.82  ? 430 GLN A OE1 1 
ATOM   4482 N NE2 . GLN B 1 244 ? 25.415  23.262  26.848  1.00 97.01  ? 430 GLN A NE2 1 
ATOM   4483 N N   . LEU B 1 245 ? 29.709  20.093  31.116  1.00 63.37  ? 431 LEU A N   1 
ATOM   4484 C CA  . LEU B 1 245 ? 31.000  19.665  31.654  1.00 58.52  ? 431 LEU A CA  1 
ATOM   4485 C C   . LEU B 1 245 ? 31.925  19.171  30.549  1.00 65.45  ? 431 LEU A C   1 
ATOM   4486 O O   . LEU B 1 245 ? 31.758  18.041  30.056  1.00 65.01  ? 431 LEU A O   1 
ATOM   4487 C CB  . LEU B 1 245 ? 30.791  18.573  32.700  1.00 57.22  ? 431 LEU A CB  1 
ATOM   4488 C CG  . LEU B 1 245 ? 32.034  18.116  33.454  1.00 57.55  ? 431 LEU A CG  1 
ATOM   4489 C CD1 . LEU B 1 245 ? 32.625  19.280  34.232  1.00 61.96  ? 431 LEU A CD1 1 
ATOM   4490 C CD2 . LEU B 1 245 ? 31.682  16.961  34.379  1.00 55.74  ? 431 LEU A CD2 1 
ATOM   4491 N N   . PRO B 1 246 ? 32.908  19.968  30.121  1.00 66.38  ? 432 PRO A N   1 
ATOM   4492 C CA  . PRO B 1 246 ? 33.891  19.476  29.145  1.00 60.70  ? 432 PRO A CA  1 
ATOM   4493 C C   . PRO B 1 246 ? 34.929  18.603  29.835  1.00 60.00  ? 432 PRO A C   1 
ATOM   4494 O O   . PRO B 1 246 ? 35.494  18.986  30.861  1.00 67.24  ? 432 PRO A O   1 
ATOM   4495 C CB  . PRO B 1 246 ? 34.518  20.761  28.599  1.00 62.28  ? 432 PRO A CB  1 
ATOM   4496 C CG  . PRO B 1 246 ? 34.411  21.722  29.736  1.00 62.16  ? 432 PRO A CG  1 
ATOM   4497 C CD  . PRO B 1 246 ? 33.140  21.380  30.475  1.00 64.84  ? 432 PRO A CD  1 
ATOM   4498 N N   . LEU B 1 247 ? 35.170  17.415  29.274  1.00 59.95  ? 433 LEU A N   1 
ATOM   4499 C CA  . LEU B 1 247 ? 36.104  16.466  29.871  1.00 59.29  ? 433 LEU A CA  1 
ATOM   4500 C C   . LEU B 1 247 ? 37.114  15.932  28.862  1.00 66.92  ? 433 LEU A C   1 
ATOM   4501 O O   . LEU B 1 247 ? 37.730  14.890  29.109  1.00 70.32  ? 433 LEU A O   1 
ATOM   4502 C CB  . LEU B 1 247 ? 35.358  15.300  30.527  1.00 59.60  ? 433 LEU A CB  1 
ATOM   4503 C CG  . LEU B 1 247 ? 34.398  15.600  31.683  1.00 57.06  ? 433 LEU A CG  1 
ATOM   4504 C CD1 . LEU B 1 247 ? 33.763  14.317  32.195  1.00 56.08  ? 433 LEU A CD1 1 
ATOM   4505 C CD2 . LEU B 1 247 ? 35.106  16.325  32.812  1.00 57.10  ? 433 LEU A CD2 1 
ATOM   4506 N N   . ASP B 1 248 ? 37.295  16.612  27.726  1.00 70.74  ? 434 ASP A N   1 
ATOM   4507 C CA  . ASP B 1 248 ? 38.264  16.140  26.740  1.00 71.53  ? 434 ASP A CA  1 
ATOM   4508 C C   . ASP B 1 248 ? 39.670  16.121  27.318  1.00 71.97  ? 434 ASP A C   1 
ATOM   4509 O O   . ASP B 1 248 ? 40.469  15.233  27.000  1.00 75.68  ? 434 ASP A O   1 
ATOM   4510 C CB  . ASP B 1 248 ? 38.219  17.005  25.482  1.00 73.71  ? 434 ASP A CB  1 
ATOM   4511 C CG  . ASP B 1 248 ? 37.572  16.292  24.314  1.00 80.50  ? 434 ASP A CG  1 
ATOM   4512 O OD1 . ASP B 1 248 ? 37.355  15.063  24.416  1.00 74.33  ? 434 ASP A OD1 1 
ATOM   4513 O OD2 . ASP B 1 248 ? 37.288  16.957  23.293  1.00 84.29  ? 434 ASP A OD2 1 
ATOM   4514 N N   . GLU B 1 249 ? 39.994  17.100  28.162  1.00 68.99  ? 435 GLU A N   1 
ATOM   4515 C CA  . GLU B 1 249 ? 41.351  17.210  28.678  1.00 75.82  ? 435 GLU A CA  1 
ATOM   4516 C C   . GLU B 1 249 ? 41.713  16.080  29.636  1.00 71.06  ? 435 GLU A C   1 
ATOM   4517 O O   . GLU B 1 249 ? 42.901  15.887  29.918  1.00 76.90  ? 435 GLU A O   1 
ATOM   4518 C CB  . GLU B 1 249 ? 41.548  18.573  29.344  1.00 66.06  ? 435 GLU A CB  1 
ATOM   4519 C CG  . GLU B 1 249 ? 40.559  18.901  30.433  1.00 69.15  ? 435 GLU A CG  1 
ATOM   4520 C CD  . GLU B 1 249 ? 40.760  20.301  30.978  1.00 78.62  ? 435 GLU A CD  1 
ATOM   4521 O OE1 . GLU B 1 249 ? 41.839  20.885  30.734  1.00 66.98  ? 435 GLU A OE1 1 
ATOM   4522 O OE2 . GLU B 1 249 ? 39.832  20.826  31.630  1.00 78.37  ? 435 GLU A OE2 1 
ATOM   4523 N N   . PHE B 1 250 ? 40.736  15.332  30.144  1.00 66.65  ? 436 PHE A N   1 
ATOM   4524 C CA  . PHE B 1 250 ? 41.037  14.190  31.000  1.00 69.41  ? 436 PHE A CA  1 
ATOM   4525 C C   . PHE B 1 250 ? 41.111  12.873  30.237  1.00 65.09  ? 436 PHE A C   1 
ATOM   4526 O O   . PHE B 1 250 ? 41.452  11.846  30.832  1.00 62.24  ? 436 PHE A O   1 
ATOM   4527 C CB  . PHE B 1 250 ? 40.009  14.105  32.130  1.00 63.20  ? 436 PHE A CB  1 
ATOM   4528 C CG  . PHE B 1 250 ? 39.897  15.379  32.910  1.00 67.91  ? 436 PHE A CG  1 
ATOM   4529 C CD1 . PHE B 1 250 ? 40.841  15.708  33.865  1.00 61.97  ? 436 PHE A CD1 1 
ATOM   4530 C CD2 . PHE B 1 250 ? 38.860  16.262  32.672  1.00 66.29  ? 436 PHE A CD2 1 
ATOM   4531 C CE1 . PHE B 1 250 ? 40.752  16.893  34.568  1.00 60.13  ? 436 PHE A CE1 1 
ATOM   4532 C CE2 . PHE B 1 250 ? 38.765  17.446  33.379  1.00 67.32  ? 436 PHE A CE2 1 
ATOM   4533 C CZ  . PHE B 1 250 ? 39.713  17.762  34.324  1.00 60.68  ? 436 PHE A CZ  1 
ATOM   4534 N N   . LEU B 1 251 ? 40.808  12.881  28.941  1.00 65.99  ? 437 LEU A N   1 
ATOM   4535 C CA  . LEU B 1 251 ? 41.019  11.716  28.094  1.00 69.21  ? 437 LEU A CA  1 
ATOM   4536 C C   . LEU B 1 251 ? 42.462  11.653  27.619  1.00 76.35  ? 437 LEU A C   1 
ATOM   4537 O O   . LEU B 1 251 ? 43.075  12.680  27.309  1.00 80.86  ? 437 LEU A O   1 
ATOM   4538 C CB  . LEU B 1 251 ? 40.081  11.748  26.887  1.00 73.08  ? 437 LEU A CB  1 
ATOM   4539 C CG  . LEU B 1 251 ? 38.600  11.581  27.193  1.00 64.34  ? 437 LEU A CG  1 
ATOM   4540 C CD1 . LEU B 1 251 ? 37.788  11.673  25.915  1.00 64.28  ? 437 LEU A CD1 1 
ATOM   4541 C CD2 . LEU B 1 251 ? 38.406  10.238  27.865  1.00 62.72  ? 437 LEU A CD2 1 
ATOM   4542 N N   . GLN B 1 252 ? 43.007  10.434  27.567  1.00 71.96  ? 438 GLN A N   1 
ATOM   4543 C CA  . GLN B 1 252 ? 44.380  10.262  27.102  1.00 79.16  ? 438 GLN A CA  1 
ATOM   4544 C C   . GLN B 1 252 ? 44.534  10.715  25.654  1.00 79.79  ? 438 GLN A C   1 
ATOM   4545 O O   . GLN B 1 252 ? 45.514  11.384  25.305  1.00 86.60  ? 438 GLN A O   1 
ATOM   4546 C CB  . GLN B 1 252 ? 44.814  8.807   27.262  1.00 78.05  ? 438 GLN A CB  1 
ATOM   4547 C CG  . GLN B 1 252 ? 46.316  8.611   27.143  1.00 84.57  ? 438 GLN A CG  1 
ATOM   4548 C CD  . GLN B 1 252 ? 46.745  7.192   27.441  1.00 82.75  ? 438 GLN A CD  1 
ATOM   4549 O OE1 . GLN B 1 252 ? 45.920  6.281   27.506  1.00 79.16  ? 438 GLN A OE1 1 
ATOM   4550 N NE2 . GLN B 1 252 ? 48.044  6.997   27.637  1.00 94.56  ? 438 GLN A NE2 1 
ATOM   4551 N N   . LYS B 1 253 ? 43.571  10.369  24.799  1.00 80.59  ? 439 LYS A N   1 
ATOM   4552 C CA  . LYS B 1 253 ? 43.538  10.835  23.414  1.00 78.47  ? 439 LYS A CA  1 
ATOM   4553 C C   . LYS B 1 253 ? 42.114  11.266  23.103  1.00 79.02  ? 439 LYS A C   1 
ATOM   4554 O O   . LYS B 1 253 ? 41.199  10.437  23.099  1.00 78.11  ? 439 LYS A O   1 
ATOM   4555 C CB  . LYS B 1 253 ? 43.995  9.746   22.444  1.00 84.38  ? 439 LYS A CB  1 
ATOM   4556 C CG  . LYS B 1 253 ? 44.070  10.192  20.990  1.00 86.05  ? 439 LYS A CG  1 
ATOM   4557 C CD  . LYS B 1 253 ? 44.540  9.055   20.097  1.00 92.28  ? 439 LYS A CD  1 
ATOM   4558 C CE  . LYS B 1 253 ? 44.652  9.500   18.648  1.00 97.61  ? 439 LYS A CE  1 
ATOM   4559 N NZ  . LYS B 1 253 ? 45.061  8.386   17.744  1.00 104.45 ? 439 LYS A NZ  1 
ATOM   4560 N N   . THR B 1 254 ? 41.925  12.561  22.869  1.00 81.87  ? 440 THR A N   1 
ATOM   4561 C CA  . THR B 1 254 ? 40.606  13.074  22.546  1.00 76.72  ? 440 THR A CA  1 
ATOM   4562 C C   . THR B 1 254 ? 40.200  12.653  21.137  1.00 83.20  ? 440 THR A C   1 
ATOM   4563 O O   . THR B 1 254 ? 41.025  12.240  20.316  1.00 77.33  ? 440 THR A O   1 
ATOM   4564 C CB  . THR B 1 254 ? 40.566  14.597  22.658  1.00 69.55  ? 440 THR A CB  1 
ATOM   4565 O OG1 . THR B 1 254 ? 41.170  15.175  21.495  1.00 72.70  ? 440 THR A OG1 1 
ATOM   4566 C CG2 . THR B 1 254 ? 41.315  15.061  23.895  1.00 78.47  ? 440 THR A CG2 1 
ATOM   4567 N N   . ASP B 1 255 ? 38.906  12.760  20.868  1.00 88.21  ? 441 ASP A N   1 
ATOM   4568 C CA  . ASP B 1 255 ? 38.355  12.463  19.547  1.00 81.35  ? 441 ASP A CA  1 
ATOM   4569 C C   . ASP B 1 255 ? 37.673  13.698  18.983  1.00 82.14  ? 441 ASP A C   1 
ATOM   4570 O O   . ASP B 1 255 ? 36.633  14.126  19.520  1.00 89.82  ? 441 ASP A O   1 
ATOM   4571 C CB  . ASP B 1 255 ? 37.367  11.300  19.617  1.00 84.08  ? 441 ASP A CB  1 
ATOM   4572 C CG  . ASP B 1 255 ? 36.696  11.029  18.284  1.00 91.10  ? 441 ASP A CG  1 
ATOM   4573 O OD1 . ASP B 1 255 ? 37.384  10.555  17.356  1.00 85.61  ? 441 ASP A OD1 1 
ATOM   4574 O OD2 . ASP B 1 255 ? 35.480  11.296  18.158  1.00 100.98 ? 441 ASP A OD2 1 
ATOM   4575 N N   . PRO B 1 256 ? 38.211  14.317  17.935  1.00 82.66  ? 442 PRO A N   1 
ATOM   4576 C CA  . PRO B 1 256 ? 37.442  15.333  17.213  1.00 83.03  ? 442 PRO A CA  1 
ATOM   4577 C C   . PRO B 1 256 ? 36.195  14.704  16.616  1.00 91.51  ? 442 PRO A C   1 
ATOM   4578 O O   . PRO B 1 256 ? 36.128  13.493  16.397  1.00 95.57  ? 442 PRO A O   1 
ATOM   4579 C CB  . PRO B 1 256 ? 38.412  15.818  16.129  1.00 78.52  ? 442 PRO A CB  1 
ATOM   4580 C CG  . PRO B 1 256 ? 39.775  15.506  16.688  1.00 76.13  ? 442 PRO A CG  1 
ATOM   4581 C CD  . PRO B 1 256 ? 39.599  14.225  17.451  1.00 87.37  ? 442 PRO A CD  1 
ATOM   4582 N N   . LYS B 1 257 ? 35.187  15.543  16.387  1.00 89.50  ? 443 LYS A N   1 
ATOM   4583 C CA  . LYS B 1 257 ? 33.837  15.179  15.958  1.00 89.16  ? 443 LYS A CA  1 
ATOM   4584 C C   . LYS B 1 257 ? 33.072  14.436  17.051  1.00 95.08  ? 443 LYS A C   1 
ATOM   4585 O O   . LYS B 1 257 ? 31.892  14.117  16.852  1.00 101.63 ? 443 LYS A O   1 
ATOM   4586 C CB  . LYS B 1 257 ? 33.807  14.370  14.644  1.00 97.58  ? 443 LYS A CB  1 
ATOM   4587 C CG  . LYS B 1 257 ? 33.749  12.842  14.755  1.00 97.40  ? 443 LYS A CG  1 
ATOM   4588 C CD  . LYS B 1 257 ? 33.980  12.182  13.400  1.00 99.32  ? 443 LYS A CD  1 
ATOM   4589 C CE  . LYS B 1 257 ? 35.144  12.800  12.634  1.00 88.50  ? 443 LYS A CE  1 
ATOM   4590 N NZ  . LYS B 1 257 ? 35.271  12.155  11.301  1.00 93.95  ? 443 LYS A NZ  1 
ATOM   4591 N N   . ASP B 1 258 ? 33.695  14.162  18.200  1.00 91.77  ? 444 ASP A N   1 
ATOM   4592 C CA  . ASP B 1 258 ? 32.976  13.733  19.404  1.00 89.81  ? 444 ASP A CA  1 
ATOM   4593 C C   . ASP B 1 258 ? 33.776  14.144  20.628  1.00 84.28  ? 444 ASP A C   1 
ATOM   4594 O O   . ASP B 1 258 ? 34.435  13.317  21.272  1.00 83.37  ? 444 ASP A O   1 
ATOM   4595 C CB  . ASP B 1 258 ? 32.705  12.227  19.418  1.00 82.12  ? 444 ASP A CB  1 
ATOM   4596 C CG  . ASP B 1 258 ? 31.617  11.842  20.420  1.00 84.75  ? 444 ASP A CG  1 
ATOM   4597 O OD1 . ASP B 1 258 ? 31.387  12.614  21.377  1.00 83.60  ? 444 ASP A OD1 1 
ATOM   4598 O OD2 . ASP B 1 258 ? 30.987  10.774  20.258  1.00 93.49  ? 444 ASP A OD2 1 
ATOM   4599 N N   . PRO B 1 259 ? 33.762  15.429  20.970  1.00 81.51  ? 445 PRO A N   1 
ATOM   4600 C CA  . PRO B 1 259 ? 34.398  15.860  22.216  1.00 73.78  ? 445 PRO A CA  1 
ATOM   4601 C C   . PRO B 1 259 ? 33.658  15.269  23.400  1.00 76.50  ? 445 PRO A C   1 
ATOM   4602 O O   . PRO B 1 259 ? 32.467  14.958  23.322  1.00 78.72  ? 445 PRO A O   1 
ATOM   4603 C CB  . PRO B 1 259 ? 34.264  17.387  22.184  1.00 76.83  ? 445 PRO A CB  1 
ATOM   4604 C CG  . PRO B 1 259 ? 33.851  17.726  20.775  1.00 80.64  ? 445 PRO A CG  1 
ATOM   4605 C CD  . PRO B 1 259 ? 33.092  16.544  20.287  1.00 82.70  ? 445 PRO A CD  1 
ATOM   4606 N N   . ALA B 1 260 ? 34.383  15.097  24.504  1.00 76.35  ? 446 ALA A N   1 
ATOM   4607 C CA  . ALA B 1 260 ? 33.793  14.592  25.744  1.00 65.48  ? 446 ALA A CA  1 
ATOM   4608 C C   . ALA B 1 260 ? 33.036  15.723  26.441  1.00 65.63  ? 446 ALA A C   1 
ATOM   4609 O O   . ALA B 1 260 ? 33.399  16.193  27.521  1.00 68.54  ? 446 ALA A O   1 
ATOM   4610 C CB  . ALA B 1 260 ? 34.868  13.998  26.641  1.00 71.58  ? 446 ALA A CB  1 
ATOM   4611 N N   . ASN B 1 261 ? 31.963  16.169  25.788  1.00 67.48  ? 447 ASN A N   1 
ATOM   4612 C CA  . ASN B 1 261 ? 31.091  17.213  26.313  1.00 62.50  ? 447 ASN A CA  1 
ATOM   4613 C C   . ASN B 1 261 ? 29.840  16.575  26.898  1.00 62.02  ? 447 ASN A C   1 
ATOM   4614 O O   . ASN B 1 261 ? 29.211  15.729  26.254  1.00 65.76  ? 447 ASN A O   1 
ATOM   4615 C CB  . ASN B 1 261 ? 30.715  18.226  25.228  1.00 62.62  ? 447 ASN A CB  1 
ATOM   4616 C CG  . ASN B 1 261 ? 31.895  19.082  24.790  1.00 70.68  ? 447 ASN A CG  1 
ATOM   4617 O OD1 . ASN B 1 261 ? 32.149  19.252  23.595  1.00 80.07  ? 447 ASN A OD1 1 
ATOM   4618 N ND2 . ASN B 1 261 ? 32.620  19.629  25.760  1.00 70.73  ? 447 ASN A ND2 1 
ATOM   4619 N N   . TYR B 1 262 ? 29.484  16.979  28.117  1.00 59.16  ? 448 TYR A N   1 
ATOM   4620 C CA  . TYR B 1 262 ? 28.396  16.362  28.861  1.00 63.03  ? 448 TYR A CA  1 
ATOM   4621 C C   . TYR B 1 262 ? 27.420  17.423  29.356  1.00 61.91  ? 448 TYR A C   1 
ATOM   4622 O O   . TYR B 1 262 ? 27.786  18.582  29.571  1.00 61.31  ? 448 TYR A O   1 
ATOM   4623 C CB  . TYR B 1 262 ? 28.942  15.531  30.031  1.00 57.19  ? 448 TYR A CB  1 
ATOM   4624 C CG  . TYR B 1 262 ? 29.503  14.203  29.575  1.00 59.25  ? 448 TYR A CG  1 
ATOM   4625 C CD1 . TYR B 1 262 ? 30.746  14.127  28.958  1.00 60.98  ? 448 TYR A CD1 1 
ATOM   4626 C CD2 . TYR B 1 262 ? 28.785  13.028  29.745  1.00 57.56  ? 448 TYR A CD2 1 
ATOM   4627 C CE1 . TYR B 1 262 ? 31.259  12.919  28.526  1.00 59.08  ? 448 TYR A CE1 1 
ATOM   4628 C CE2 . TYR B 1 262 ? 29.292  11.814  29.318  1.00 63.27  ? 448 TYR A CE2 1 
ATOM   4629 C CZ  . TYR B 1 262 ? 30.530  11.766  28.709  1.00 60.65  ? 448 TYR A CZ  1 
ATOM   4630 O OH  . TYR B 1 262 ? 31.031  10.559  28.281  1.00 56.99  ? 448 TYR A OH  1 
ATOM   4631 N N   . ILE B 1 263 ? 26.164  17.013  29.510  1.00 58.42  ? 449 ILE A N   1 
ATOM   4632 C CA  . ILE B 1 263 ? 25.084  17.893  29.936  1.00 60.31  ? 449 ILE A CA  1 
ATOM   4633 C C   . ILE B 1 263 ? 24.510  17.350  31.235  1.00 57.92  ? 449 ILE A C   1 
ATOM   4634 O O   . ILE B 1 263 ? 24.294  16.140  31.366  1.00 58.45  ? 449 ILE A O   1 
ATOM   4635 C CB  . ILE B 1 263 ? 23.995  18.016  28.854  1.00 60.09  ? 449 ILE A CB  1 
ATOM   4636 C CG1 . ILE B 1 263 ? 24.619  18.535  27.559  1.00 62.06  ? 449 ILE A CG1 1 
ATOM   4637 C CG2 . ILE B 1 263 ? 22.888  18.952  29.307  1.00 60.80  ? 449 ILE A CG2 1 
ATOM   4638 C CD1 . ILE B 1 263 ? 23.636  18.720  26.444  1.00 81.57  ? 449 ILE A CD1 1 
ATOM   4639 N N   . LEU B 1 264 ? 24.307  18.240  32.204  1.00 57.97  ? 450 LEU A N   1 
ATOM   4640 C CA  . LEU B 1 264 ? 23.772  17.849  33.502  1.00 57.31  ? 450 LEU A CA  1 
ATOM   4641 C C   . LEU B 1 264 ? 22.341  17.338  33.370  1.00 58.98  ? 450 LEU A C   1 
ATOM   4642 O O   . LEU B 1 264 ? 21.492  17.983  32.745  1.00 64.03  ? 450 LEU A O   1 
ATOM   4643 C CB  . LEU B 1 264 ? 23.826  19.034  34.463  1.00 57.64  ? 450 LEU A CB  1 
ATOM   4644 C CG  . LEU B 1 264 ? 23.339  18.771  35.885  1.00 58.97  ? 450 LEU A CG  1 
ATOM   4645 C CD1 . LEU B 1 264 ? 24.153  17.652  36.513  1.00 56.10  ? 450 LEU A CD1 1 
ATOM   4646 C CD2 . LEU B 1 264 ? 23.430  20.041  36.716  1.00 63.68  ? 450 LEU A CD2 1 
ATOM   4647 N N   . HIS B 1 265 ? 22.069  16.181  33.972  1.00 62.33  ? 451 HIS A N   1 
ATOM   4648 C CA  . HIS B 1 265 ? 20.750  15.562  33.900  1.00 62.84  ? 451 HIS A CA  1 
ATOM   4649 C C   . HIS B 1 265 ? 20.061  15.474  35.254  1.00 60.87  ? 451 HIS A C   1 
ATOM   4650 O O   . HIS B 1 265 ? 18.920  15.930  35.392  1.00 63.57  ? 451 HIS A O   1 
ATOM   4651 C CB  . HIS B 1 265 ? 20.862  14.159  33.280  1.00 58.19  ? 451 HIS A CB  1 
ATOM   4652 C CG  . HIS B 1 265 ? 19.558  13.606  32.797  1.00 57.87  ? 451 HIS A CG  1 
ATOM   4653 N ND1 . HIS B 1 265 ? 19.172  12.302  33.023  1.00 57.67  ? 451 HIS A ND1 1 
ATOM   4654 C CD2 . HIS B 1 265 ? 18.557  14.176  32.083  1.00 62.75  ? 451 HIS A CD2 1 
ATOM   4655 C CE1 . HIS B 1 265 ? 17.985  12.096  32.479  1.00 66.15  ? 451 HIS A CE1 1 
ATOM   4656 N NE2 . HIS B 1 265 ? 17.590  13.217  31.901  1.00 63.63  ? 451 HIS A NE2 1 
ATOM   4657 N N   . ALA B 1 266 ? 20.715  14.893  36.259  1.00 57.68  ? 452 ALA A N   1 
ATOM   4658 C CA  . ALA B 1 266 ? 20.117  14.688  37.571  1.00 57.95  ? 452 ALA A CA  1 
ATOM   4659 C C   . ALA B 1 266 ? 21.051  15.190  38.665  1.00 63.05  ? 452 ALA A C   1 
ATOM   4660 O O   . ALA B 1 266 ? 22.274  15.068  38.552  1.00 59.03  ? 452 ALA A O   1 
ATOM   4661 C CB  . ALA B 1 266 ? 19.790  13.208  37.802  1.00 58.85  ? 452 ALA A CB  1 
ATOM   4662 N N   . VAL B 1 267 ? 20.470  15.760  39.721  1.00 70.46  ? 453 VAL A N   1 
ATOM   4663 C CA  . VAL B 1 267 ? 21.213  16.232  40.893  1.00 63.40  ? 453 VAL A CA  1 
ATOM   4664 C C   . VAL B 1 267 ? 20.550  15.646  42.138  1.00 59.42  ? 453 VAL A C   1 
ATOM   4665 O O   . VAL B 1 267 ? 19.457  16.078  42.523  1.00 63.55  ? 453 VAL A O   1 
ATOM   4666 C CB  . VAL B 1 267 ? 21.260  17.766  40.969  1.00 60.98  ? 453 VAL A CB  1 
ATOM   4667 C CG1 . VAL B 1 267 ? 22.083  18.224  42.164  1.00 66.39  ? 453 VAL A CG1 1 
ATOM   4668 C CG2 . VAL B 1 267 ? 21.820  18.351  39.676  1.00 57.16  ? 453 VAL A CG2 1 
ATOM   4669 N N   . LEU B 1 268 ? 21.207  14.671  42.769  1.00 56.83  ? 454 LEU A N   1 
ATOM   4670 C CA  . LEU B 1 268 ? 20.674  13.984  43.944  1.00 58.70  ? 454 LEU A CA  1 
ATOM   4671 C C   . LEU B 1 268 ? 21.217  14.628  45.216  1.00 58.05  ? 454 LEU A C   1 
ATOM   4672 O O   . LEU B 1 268 ? 22.434  14.686  45.415  1.00 57.81  ? 454 LEU A O   1 
ATOM   4673 C CB  . LEU B 1 268 ? 21.030  12.496  43.917  1.00 59.07  ? 454 LEU A CB  1 
ATOM   4674 C CG  . LEU B 1 268 ? 20.256  11.569  42.972  1.00 63.22  ? 454 LEU A CG  1 
ATOM   4675 C CD1 . LEU B 1 268 ? 20.601  11.833  41.515  1.00 64.17  ? 454 LEU A CD1 1 
ATOM   4676 C CD2 . LEU B 1 268 ? 20.496  10.106  43.321  1.00 58.51  ? 454 LEU A CD2 1 
ATOM   4677 N N   . VAL B 1 269 ? 20.317  15.090  46.085  1.00 58.97  ? 455 VAL A N   1 
ATOM   4678 C CA  . VAL B 1 269 ? 20.695  15.832  47.281  1.00 61.47  ? 455 VAL A CA  1 
ATOM   4679 C C   . VAL B 1 269 ? 20.109  15.143  48.509  1.00 66.97  ? 455 VAL A C   1 
ATOM   4680 O O   . VAL B 1 269 ? 19.120  14.408  48.429  1.00 60.47  ? 455 VAL A O   1 
ATOM   4681 C CB  . VAL B 1 269 ? 20.252  17.306  47.224  1.00 59.94  ? 455 VAL A CB  1 
ATOM   4682 C CG1 . VAL B 1 269 ? 20.457  17.869  45.823  1.00 65.13  ? 455 VAL A CG1 1 
ATOM   4683 C CG2 . VAL B 1 269 ? 18.813  17.441  47.664  1.00 60.90  ? 455 VAL A CG2 1 
ATOM   4684 N N   . HIS B 1 270 ? 20.748  15.384  49.661  1.00 66.78  ? 456 HIS A N   1 
ATOM   4685 C CA  . HIS B 1 270 ? 20.328  14.810  50.933  1.00 61.25  ? 456 HIS A CA  1 
ATOM   4686 C C   . HIS B 1 270 ? 20.212  15.855  52.035  1.00 66.07  ? 456 HIS A C   1 
ATOM   4687 O O   . HIS B 1 270 ? 21.013  16.792  52.112  1.00 69.58  ? 456 HIS A O   1 
ATOM   4688 C CB  . HIS B 1 270 ? 21.317  13.728  51.390  1.00 62.53  ? 456 HIS A CB  1 
ATOM   4689 C CG  . HIS B 1 270 ? 21.214  13.389  52.846  1.00 65.40  ? 456 HIS A CG  1 
ATOM   4690 N ND1 . HIS B 1 270 ? 20.486  12.317  53.313  1.00 68.42  ? 456 HIS A ND1 1 
ATOM   4691 C CD2 . HIS B 1 270 ? 21.749  13.985  53.939  1.00 63.12  ? 456 HIS A CD2 1 
ATOM   4692 C CE1 . HIS B 1 270 ? 20.575  12.267  54.630  1.00 65.69  ? 456 HIS A CE1 1 
ATOM   4693 N NE2 . HIS B 1 270 ? 21.335  13.269  55.035  1.00 66.16  ? 456 HIS A NE2 1 
ATOM   4694 N N   . SER B 1 271 ? 19.169  15.702  52.853  1.00 67.61  ? 457 SER A N   1 
ATOM   4695 C CA  . SER B 1 271 ? 18.997  16.371  54.137  1.00 67.37  ? 457 SER A CA  1 
ATOM   4696 C C   . SER B 1 271 ? 18.674  15.309  55.185  1.00 74.91  ? 457 SER A C   1 
ATOM   4697 O O   . SER B 1 271 ? 17.916  14.376  54.902  1.00 82.40  ? 457 SER A O   1 
ATOM   4698 C CB  . SER B 1 271 ? 17.895  17.439  54.086  1.00 66.82  ? 457 SER A CB  1 
ATOM   4699 O OG  . SER B 1 271 ? 18.363  18.604  53.426  1.00 77.81  ? 457 SER A OG  1 
ATOM   4700 N N   . GLY B 1 272 ? 19.227  15.438  56.393  1.00 79.39  ? 458 GLY A N   1 
ATOM   4701 C CA  . GLY B 1 272 ? 19.265  14.340  57.349  1.00 78.37  ? 458 GLY A CA  1 
ATOM   4702 C C   . GLY B 1 272 ? 18.280  14.561  58.484  1.00 78.01  ? 458 GLY A C   1 
ATOM   4703 O O   . GLY B 1 272 ? 18.025  15.701  58.882  1.00 87.19  ? 458 GLY A O   1 
ATOM   4704 N N   . ASP B 1 273 ? 17.734  13.465  59.021  1.00 82.66  ? 459 ASP A N   1 
ATOM   4705 C CA  . ASP B 1 273 ? 16.811  13.561  60.152  1.00 85.16  ? 459 ASP A CA  1 
ATOM   4706 C C   . ASP B 1 273 ? 16.654  12.196  60.833  1.00 84.04  ? 459 ASP A C   1 
ATOM   4707 O O   . ASP B 1 273 ? 17.307  11.214  60.468  1.00 83.50  ? 459 ASP A O   1 
ATOM   4708 C CB  . ASP B 1 273 ? 15.459  14.120  59.681  1.00 89.09  ? 459 ASP A CB  1 
ATOM   4709 C CG  . ASP B 1 273 ? 14.780  13.246  58.617  1.00 79.37  ? 459 ASP A CG  1 
ATOM   4710 O OD1 . ASP B 1 273 ? 15.255  12.129  58.327  1.00 84.19  ? 459 ASP A OD1 1 
ATOM   4711 O OD2 . ASP B 1 273 ? 13.785  13.715  58.026  1.00 74.12  ? 459 ASP A OD2 1 
ATOM   4712 N N   . ASN B 1 274 ? 15.767  12.158  61.839  1.00 81.40  ? 460 ASN A N   1 
ATOM   4713 C CA  . ASN B 1 274 ? 15.595  10.998  62.722  1.00 79.33  ? 460 ASN A CA  1 
ATOM   4714 C C   . ASN B 1 274 ? 15.028  9.757   62.039  1.00 80.21  ? 460 ASN A C   1 
ATOM   4715 O O   . ASN B 1 274 ? 15.350  8.636   62.453  1.00 79.33  ? 460 ASN A O   1 
ATOM   4716 C CB  . ASN B 1 274 ? 14.722  11.356  63.923  1.00 82.24  ? 460 ASN A CB  1 
ATOM   4717 C CG  . ASN B 1 274 ? 15.511  12.008  65.032  1.00 83.52  ? 460 ASN A CG  1 
ATOM   4718 O OD1 . ASN B 1 274 ? 16.718  11.813  65.137  1.00 88.21  ? 460 ASN A OD1 1 
ATOM   4719 N ND2 . ASN B 1 274 ? 14.833  12.759  65.889  1.00 88.04  ? 460 ASN A ND2 1 
ATOM   4720 N N   . HIS B 1 275 ? 14.150  9.915   61.048  1.00 83.17  ? 461 HIS A N   1 
ATOM   4721 C CA  . HIS B 1 275 ? 13.484  8.782   60.412  1.00 82.74  ? 461 HIS A CA  1 
ATOM   4722 C C   . HIS B 1 275 ? 14.169  8.296   59.134  1.00 89.70  ? 461 HIS A C   1 
ATOM   4723 O O   . HIS B 1 275 ? 13.549  7.563   58.352  1.00 89.88  ? 461 HIS A O   1 
ATOM   4724 C CB  . HIS B 1 275 ? 12.047  9.157   60.071  1.00 83.75  ? 461 HIS A CB  1 
ATOM   4725 C CG  . HIS B 1 275 ? 11.947  9.929   58.797  1.00 88.80  ? 461 HIS A CG  1 
ATOM   4726 N ND1 . HIS B 1 275 ? 11.559  9.357   57.603  1.00 100.44 ? 461 HIS A ND1 1 
ATOM   4727 C CD2 . HIS B 1 275 ? 12.258  11.215  58.513  1.00 94.53  ? 461 HIS A CD2 1 
ATOM   4728 C CE1 . HIS B 1 275 ? 11.588  10.271  56.648  1.00 91.46  ? 461 HIS A CE1 1 
ATOM   4729 N NE2 . HIS B 1 275 ? 12.006  11.409  57.174  1.00 96.33  ? 461 HIS A NE2 1 
ATOM   4730 N N   . GLY B 1 276 ? 15.418  8.665   58.900  1.00 89.88  ? 462 GLY A N   1 
ATOM   4731 C CA  . GLY B 1 276 ? 16.152  8.156   57.769  1.00 79.99  ? 462 GLY A CA  1 
ATOM   4732 C C   . GLY B 1 276 ? 16.485  9.143   56.674  1.00 79.59  ? 462 GLY A C   1 
ATOM   4733 O O   . GLY B 1 276 ? 16.778  8.706   55.554  1.00 87.26  ? 462 GLY A O   1 
ATOM   4734 N N   . GLY B 1 277 ? 16.419  10.442  56.937  1.00 76.20  ? 463 GLY A N   1 
ATOM   4735 C CA  . GLY B 1 277 ? 16.837  11.422  55.954  1.00 73.19  ? 463 GLY A CA  1 
ATOM   4736 C C   . GLY B 1 277 ? 15.717  11.906  55.062  1.00 76.75  ? 463 GLY A C   1 
ATOM   4737 O O   . GLY B 1 277 ? 14.552  11.510  55.165  1.00 87.03  ? 463 GLY A O   1 
ATOM   4738 N N   . HIS B 1 278 ? 16.098  12.814  54.167  1.00 73.78  ? 464 HIS A N   1 
ATOM   4739 C CA  . HIS B 1 278 ? 15.190  13.352  53.162  1.00 66.93  ? 464 HIS A CA  1 
ATOM   4740 C C   . HIS B 1 278 ? 15.994  13.459  51.876  1.00 68.59  ? 464 HIS A C   1 
ATOM   4741 O O   . HIS B 1 278 ? 16.931  14.260  51.781  1.00 64.26  ? 464 HIS A O   1 
ATOM   4742 C CB  . HIS B 1 278 ? 14.620  14.706  53.586  1.00 68.22  ? 464 HIS A CB  1 
ATOM   4743 C CG  . HIS B 1 278 ? 13.490  15.186  52.728  1.00 69.68  ? 464 HIS A CG  1 
ATOM   4744 N ND1 . HIS B 1 278 ? 13.070  16.498  52.717  1.00 69.58  ? 464 HIS A ND1 1 
ATOM   4745 C CD2 . HIS B 1 278 ? 12.699  14.531  51.845  1.00 69.58  ? 464 HIS A CD2 1 
ATOM   4746 C CE1 . HIS B 1 278 ? 12.068  16.632  51.867  1.00 81.72  ? 464 HIS A CE1 1 
ATOM   4747 N NE2 . HIS B 1 278 ? 11.824  15.453  51.324  1.00 79.23  ? 464 HIS A NE2 1 
ATOM   4748 N N   . TYR B 1 279 ? 15.618  12.648  50.893  1.00 69.53  ? 465 TYR A N   1 
ATOM   4749 C CA  . TYR B 1 279 ? 16.328  12.503  49.629  1.00 62.64  ? 465 TYR A CA  1 
ATOM   4750 C C   . TYR B 1 279 ? 15.414  13.001  48.524  1.00 62.75  ? 465 TYR A C   1 
ATOM   4751 O O   . TYR B 1 279 ? 14.363  12.404  48.269  1.00 63.50  ? 465 TYR A O   1 
ATOM   4752 C CB  . TYR B 1 279 ? 16.737  11.048  49.388  1.00 61.96  ? 465 TYR A CB  1 
ATOM   4753 C CG  . TYR B 1 279 ? 17.619  10.461  50.470  1.00 64.32  ? 465 TYR A CG  1 
ATOM   4754 C CD1 . TYR B 1 279 ? 17.085  10.022  51.671  1.00 65.50  ? 465 TYR A CD1 1 
ATOM   4755 C CD2 . TYR B 1 279 ? 18.989  10.318  50.273  1.00 70.56  ? 465 TYR A CD2 1 
ATOM   4756 C CE1 . TYR B 1 279 ? 17.892  9.488   52.657  1.00 71.96  ? 465 TYR A CE1 1 
ATOM   4757 C CE2 . TYR B 1 279 ? 19.804  9.775   51.253  1.00 64.38  ? 465 TYR A CE2 1 
ATOM   4758 C CZ  . TYR B 1 279 ? 19.247  9.358   52.442  1.00 66.03  ? 465 TYR A CZ  1 
ATOM   4759 O OH  . TYR B 1 279 ? 20.033  8.817   53.434  1.00 63.30  ? 465 TYR A OH  1 
ATOM   4760 N N   . VAL B 1 280 ? 15.806  14.083  47.870  1.00 62.21  ? 466 VAL A N   1 
ATOM   4761 C CA  . VAL B 1 280 ? 15.091  14.540  46.692  1.00 65.02  ? 466 VAL A CA  1 
ATOM   4762 C C   . VAL B 1 280 ? 16.090  14.591  45.548  1.00 63.39  ? 466 VAL A C   1 
ATOM   4763 O O   . VAL B 1 280 ? 17.301  14.709  45.751  1.00 64.47  ? 466 VAL A O   1 
ATOM   4764 C CB  . VAL B 1 280 ? 14.407  15.909  46.894  1.00 66.76  ? 466 VAL A CB  1 
ATOM   4765 C CG1 . VAL B 1 280 ? 13.584  15.912  48.171  1.00 65.18  ? 466 VAL A CG1 1 
ATOM   4766 C CG2 . VAL B 1 280 ? 15.427  17.029  46.900  1.00 64.95  ? 466 VAL A CG2 1 
ATOM   4767 N N   . VAL B 1 281 ? 15.567  14.483  44.331  1.00 63.85  ? 467 VAL A N   1 
ATOM   4768 C CA  . VAL B 1 281 ? 16.385  14.464  43.127  1.00 64.87  ? 467 VAL A CA  1 
ATOM   4769 C C   . VAL B 1 281 ? 15.836  15.507  42.166  1.00 60.29  ? 467 VAL A C   1 
ATOM   4770 O O   . VAL B 1 281 ? 14.621  15.592  41.962  1.00 65.34  ? 467 VAL A O   1 
ATOM   4771 C CB  . VAL B 1 281 ? 16.421  13.064  42.481  1.00 63.36  ? 467 VAL A CB  1 
ATOM   4772 C CG1 . VAL B 1 281 ? 15.016  12.517  42.287  1.00 66.39  ? 467 VAL A CG1 1 
ATOM   4773 C CG2 . VAL B 1 281 ? 17.188  13.092  41.164  1.00 60.98  ? 467 VAL A CG2 1 
ATOM   4774 N N   . TYR B 1 282 ? 16.730  16.310  41.597  1.00 62.02  ? 468 TYR A N   1 
ATOM   4775 C CA  . TYR B 1 282 ? 16.379  17.313  40.602  1.00 66.86  ? 468 TYR A CA  1 
ATOM   4776 C C   . TYR B 1 282 ? 16.685  16.762  39.215  1.00 71.38  ? 468 TYR A C   1 
ATOM   4777 O O   . TYR B 1 282 ? 17.776  16.227  38.985  1.00 62.07  ? 468 TYR A O   1 
ATOM   4778 C CB  . TYR B 1 282 ? 17.154  18.609  40.840  1.00 66.89  ? 468 TYR A CB  1 
ATOM   4779 C CG  . TYR B 1 282 ? 16.706  19.398  42.053  1.00 63.91  ? 468 TYR A CG  1 
ATOM   4780 C CD1 . TYR B 1 282 ? 17.124  19.047  43.329  1.00 66.22  ? 468 TYR A CD1 1 
ATOM   4781 C CD2 . TYR B 1 282 ? 15.872  20.500  41.918  1.00 70.21  ? 468 TYR A CD2 1 
ATOM   4782 C CE1 . TYR B 1 282 ? 16.720  19.772  44.443  1.00 71.63  ? 468 TYR A CE1 1 
ATOM   4783 C CE2 . TYR B 1 282 ? 15.463  21.231  43.022  1.00 74.41  ? 468 TYR A CE2 1 
ATOM   4784 C CZ  . TYR B 1 282 ? 15.887  20.864  44.282  1.00 77.19  ? 468 TYR A CZ  1 
ATOM   4785 O OH  . TYR B 1 282 ? 15.476  21.592  45.378  1.00 71.24  ? 468 TYR A OH  1 
ATOM   4786 N N   . LEU B 1 283 ? 15.721  16.889  38.299  1.00 69.18  ? 469 LEU A N   1 
ATOM   4787 C CA  . LEU B 1 283 ? 15.805  16.271  36.983  1.00 61.99  ? 469 LEU A CA  1 
ATOM   4788 C C   . LEU B 1 283 ? 15.276  17.211  35.912  1.00 64.66  ? 469 LEU A C   1 
ATOM   4789 O O   . LEU B 1 283 ? 14.290  17.919  36.136  1.00 69.65  ? 469 LEU A O   1 
ATOM   4790 C CB  . LEU B 1 283 ? 14.995  14.972  36.942  1.00 62.24  ? 469 LEU A CB  1 
ATOM   4791 C CG  . LEU B 1 283 ? 15.703  13.666  37.284  1.00 63.46  ? 469 LEU A CG  1 
ATOM   4792 C CD1 . LEU B 1 283 ? 14.678  12.601  37.648  1.00 65.77  ? 469 LEU A CD1 1 
ATOM   4793 C CD2 . LEU B 1 283 ? 16.573  13.214  36.123  1.00 60.93  ? 469 LEU A CD2 1 
ATOM   4794 N N   . ASN B 1 284 ? 15.935  17.217  34.747  1.00 67.55  ? 470 ASN A N   1 
ATOM   4795 C CA  . ASN B 1 284 ? 15.323  17.691  33.507  1.00 69.81  ? 470 ASN A CA  1 
ATOM   4796 C C   . ASN B 1 284 ? 15.177  16.468  32.609  1.00 67.06  ? 470 ASN A C   1 
ATOM   4797 O O   . ASN B 1 284 ? 16.104  16.113  31.866  1.00 62.60  ? 470 ASN A O   1 
ATOM   4798 C CB  . ASN B 1 284 ? 16.121  18.810  32.820  1.00 67.67  ? 470 ASN A CB  1 
ATOM   4799 C CG  . ASN B 1 284 ? 17.558  18.428  32.505  1.00 73.45  ? 470 ASN A CG  1 
ATOM   4800 O OD1 . ASN B 1 284 ? 18.197  17.685  33.247  1.00 74.21  ? 470 ASN A OD1 1 
ATOM   4801 N ND2 . ASN B 1 284 ? 18.078  18.957  31.401  1.00 74.54  ? 470 ASN A ND2 1 
ATOM   4802 N N   . PRO B 1 285 ? 14.041  15.767  32.676  1.00 73.65  ? 471 PRO A N   1 
ATOM   4803 C CA  . PRO B 1 285 ? 13.938  14.448  32.029  1.00 67.47  ? 471 PRO A CA  1 
ATOM   4804 C C   . PRO B 1 285 ? 14.164  14.471  30.533  1.00 69.56  ? 471 PRO A C   1 
ATOM   4805 O O   . PRO B 1 285 ? 14.718  13.508  29.989  1.00 73.32  ? 471 PRO A O   1 
ATOM   4806 C CB  . PRO B 1 285 ? 12.508  14.012  32.368  1.00 64.93  ? 471 PRO A CB  1 
ATOM   4807 C CG  . PRO B 1 285 ? 12.159  14.779  33.595  1.00 65.07  ? 471 PRO A CG  1 
ATOM   4808 C CD  . PRO B 1 285 ? 12.822  16.111  33.425  1.00 68.58  ? 471 PRO A CD  1 
ATOM   4809 N N   . LYS B 1 286 ? 13.747  15.531  29.848  1.00 67.44  ? 472 LYS A N   1 
ATOM   4810 C CA  . LYS B 1 286 ? 13.938  15.630  28.408  1.00 72.60  ? 472 LYS A CA  1 
ATOM   4811 C C   . LYS B 1 286 ? 15.256  16.293  28.028  1.00 74.39  ? 472 LYS A C   1 
ATOM   4812 O O   . LYS B 1 286 ? 15.496  16.520  26.838  1.00 82.45  ? 472 LYS A O   1 
ATOM   4813 C CB  . LYS B 1 286 ? 12.765  16.379  27.768  1.00 70.68  ? 472 LYS A CB  1 
ATOM   4814 C CG  . LYS B 1 286 ? 11.435  15.644  27.888  1.00 77.68  ? 472 LYS A CG  1 
ATOM   4815 C CD  . LYS B 1 286 ? 10.298  16.412  27.223  1.00 92.42  ? 472 LYS A CD  1 
ATOM   4816 C CE  . LYS B 1 286 ? 9.997   17.710  27.956  1.00 86.85  ? 472 LYS A CE  1 
ATOM   4817 N NZ  . LYS B 1 286 ? 8.800   18.392  27.387  1.00 97.75  ? 472 LYS A NZ  1 
ATOM   4818 N N   . GLY B 1 287 ? 16.111  16.609  28.999  1.00 70.11  ? 473 GLY A N   1 
ATOM   4819 C CA  . GLY B 1 287 ? 17.366  17.268  28.702  1.00 65.09  ? 473 GLY A CA  1 
ATOM   4820 C C   . GLY B 1 287 ? 17.235  18.675  28.172  1.00 72.28  ? 473 GLY A C   1 
ATOM   4821 O O   . GLY B 1 287 ? 18.211  19.219  27.649  1.00 76.42  ? 473 GLY A O   1 
ATOM   4822 N N   . ASP B 1 288 ? 16.062  19.284  28.295  1.00 73.34  ? 474 ASP A N   1 
ATOM   4823 C CA  . ASP B 1 288 ? 15.814  20.603  27.736  1.00 72.48  ? 474 ASP A CA  1 
ATOM   4824 C C   . ASP B 1 288 ? 16.152  21.733  28.698  1.00 76.29  ? 474 ASP A C   1 
ATOM   4825 O O   . ASP B 1 288 ? 15.906  22.897  28.368  1.00 77.43  ? 474 ASP A O   1 
ATOM   4826 C CB  . ASP B 1 288 ? 14.349  20.720  27.298  1.00 77.79  ? 474 ASP A CB  1 
ATOM   4827 C CG  . ASP B 1 288 ? 13.369  20.309  28.388  1.00 83.93  ? 474 ASP A CG  1 
ATOM   4828 O OD1 . ASP B 1 288 ? 13.812  19.947  29.502  1.00 79.64  ? 474 ASP A OD1 1 
ATOM   4829 O OD2 . ASP B 1 288 ? 12.147  20.350  28.121  1.00 81.04  ? 474 ASP A OD2 1 
ATOM   4830 N N   . GLY B 1 289 ? 16.692  21.427  29.876  1.00 73.32  ? 475 GLY A N   1 
ATOM   4831 C CA  . GLY B 1 289 ? 16.898  22.456  30.874  1.00 77.66  ? 475 GLY A CA  1 
ATOM   4832 C C   . GLY B 1 289 ? 15.646  22.872  31.612  1.00 82.84  ? 475 GLY A C   1 
ATOM   4833 O O   . GLY B 1 289 ? 15.686  23.851  32.369  1.00 75.74  ? 475 GLY A O   1 
ATOM   4834 N N   . LYS B 1 290 ? 14.527  22.182  31.389  1.00 86.90  ? 476 LYS A N   1 
ATOM   4835 C CA  . LYS B 1 290 ? 13.286  22.397  32.131  1.00 83.48  ? 476 LYS A CA  1 
ATOM   4836 C C   . LYS B 1 290 ? 13.261  21.412  33.296  1.00 82.06  ? 476 LYS A C   1 
ATOM   4837 O O   . LYS B 1 290 ? 12.953  20.230  33.118  1.00 78.81  ? 476 LYS A O   1 
ATOM   4838 C CB  . LYS B 1 290 ? 12.077  22.227  31.219  1.00 82.35  ? 476 LYS A CB  1 
ATOM   4839 C CG  . LYS B 1 290 ? 11.961  23.276  30.124  1.00 84.06  ? 476 LYS A CG  1 
ATOM   4840 C CD  . LYS B 1 290 ? 10.671  23.097  29.337  1.00 94.73  ? 476 LYS A CD  1 
ATOM   4841 C CE  . LYS B 1 290 ? 10.549  24.122  28.220  1.00 101.31 ? 476 LYS A CE  1 
ATOM   4842 N NZ  . LYS B 1 290 ? 9.254   24.002  27.487  1.00 101.10 ? 476 LYS A NZ  1 
ATOM   4843 N N   . TRP B 1 291 ? 13.568  21.903  34.496  1.00 73.44  ? 477 TRP A N   1 
ATOM   4844 C CA  . TRP B 1 291 ? 13.877  21.057  35.643  1.00 74.05  ? 477 TRP A CA  1 
ATOM   4845 C C   . TRP B 1 291 ? 12.668  20.859  36.553  1.00 72.65  ? 477 TRP A C   1 
ATOM   4846 O O   . TRP B 1 291 ? 11.851  21.768  36.733  1.00 74.54  ? 477 TRP A O   1 
ATOM   4847 C CB  . TRP B 1 291 ? 15.038  21.659  36.444  1.00 73.55  ? 477 TRP A CB  1 
ATOM   4848 C CG  . TRP B 1 291 ? 16.361  21.559  35.730  1.00 70.61  ? 477 TRP A CG  1 
ATOM   4849 C CD1 . TRP B 1 291 ? 16.783  22.322  34.681  1.00 71.93  ? 477 TRP A CD1 1 
ATOM   4850 C CD2 . TRP B 1 291 ? 17.438  20.663  36.030  1.00 65.76  ? 477 TRP A CD2 1 
ATOM   4851 N NE1 . TRP B 1 291 ? 18.044  21.946  34.295  1.00 75.13  ? 477 TRP A NE1 1 
ATOM   4852 C CE2 . TRP B 1 291 ? 18.472  20.931  35.110  1.00 71.70  ? 477 TRP A CE2 1 
ATOM   4853 C CE3 . TRP B 1 291 ? 17.627  19.656  36.981  1.00 66.20  ? 477 TRP A CE3 1 
ATOM   4854 C CZ2 . TRP B 1 291 ? 19.676  20.230  35.114  1.00 71.93  ? 477 TRP A CZ2 1 
ATOM   4855 C CZ3 . TRP B 1 291 ? 18.828  18.961  36.984  1.00 68.50  ? 477 TRP A CZ3 1 
ATOM   4856 C CH2 . TRP B 1 291 ? 19.835  19.251  36.057  1.00 69.12  ? 477 TRP A CH2 1 
ATOM   4857 N N   . CYS B 1 292 ? 12.569  19.660  37.132  1.00 74.36  ? 478 CYS A N   1 
ATOM   4858 C CA  . CYS B 1 292 ? 11.546  19.315  38.112  1.00 71.77  ? 478 CYS A CA  1 
ATOM   4859 C C   . CYS B 1 292 ? 12.201  18.765  39.371  1.00 71.33  ? 478 CYS A C   1 
ATOM   4860 O O   . CYS B 1 292 ? 13.290  18.186  39.323  1.00 69.33  ? 478 CYS A O   1 
ATOM   4861 C CB  . CYS B 1 292 ? 10.553  18.272  37.578  1.00 67.31  ? 478 CYS A CB  1 
ATOM   4862 S SG  . CYS B 1 292 ? 9.484   18.843  36.251  1.00 71.38  ? 478 CYS A SG  1 
ATOM   4863 N N   . LYS B 1 293 ? 11.521  18.950  40.499  1.00 66.40  ? 479 LYS A N   1 
ATOM   4864 C CA  . LYS B 1 293 ? 11.947  18.404  41.781  1.00 65.70  ? 479 LYS A CA  1 
ATOM   4865 C C   . LYS B 1 293 ? 11.062  17.216  42.135  1.00 66.19  ? 479 LYS A C   1 
ATOM   4866 O O   . LYS B 1 293 ? 9.836   17.349  42.191  1.00 73.76  ? 479 LYS A O   1 
ATOM   4867 C CB  . LYS B 1 293 ? 11.883  19.463  42.880  1.00 66.64  ? 479 LYS A CB  1 
ATOM   4868 C CG  . LYS B 1 293 ? 12.103  18.894  44.270  1.00 66.42  ? 479 LYS A CG  1 
ATOM   4869 C CD  . LYS B 1 293 ? 12.629  19.941  45.241  1.00 74.43  ? 479 LYS A CD  1 
ATOM   4870 C CE  . LYS B 1 293 ? 11.526  20.882  45.707  1.00 74.87  ? 479 LYS A CE  1 
ATOM   4871 N NZ  . LYS B 1 293 ? 12.013  21.831  46.752  1.00 72.50  ? 479 LYS A NZ  1 
ATOM   4872 N N   . PHE B 1 294 ? 11.682  16.066  42.380  1.00 64.94  ? 480 PHE A N   1 
ATOM   4873 C CA  . PHE B 1 294 ? 10.973  14.835  42.729  1.00 66.18  ? 480 PHE A CA  1 
ATOM   4874 C C   . PHE B 1 294 ? 11.154  14.576  44.226  1.00 65.55  ? 480 PHE A C   1 
ATOM   4875 O O   . PHE B 1 294 ? 12.103  13.913  44.650  1.00 64.38  ? 480 PHE A O   1 
ATOM   4876 C CB  . PHE B 1 294 ? 11.471  13.655  41.895  1.00 66.94  ? 480 PHE A CB  1 
ATOM   4877 C CG  . PHE B 1 294 ? 11.148  13.759  40.431  1.00 66.55  ? 480 PHE A CG  1 
ATOM   4878 C CD1 . PHE B 1 294 ? 11.861  14.609  39.604  1.00 67.53  ? 480 PHE A CD1 1 
ATOM   4879 C CD2 . PHE B 1 294 ? 10.131  12.998  39.881  1.00 68.37  ? 480 PHE A CD2 1 
ATOM   4880 C CE1 . PHE B 1 294 ? 11.561  14.699  38.260  1.00 68.39  ? 480 PHE A CE1 1 
ATOM   4881 C CE2 . PHE B 1 294 ? 9.832   13.079  38.536  1.00 65.92  ? 480 PHE A CE2 1 
ATOM   4882 C CZ  . PHE B 1 294 ? 10.544  13.933  37.726  1.00 67.82  ? 480 PHE A CZ  1 
ATOM   4883 N N   . ASP B 1 295 ? 10.222  15.097  45.024  1.00 70.58  ? 481 ASP A N   1 
ATOM   4884 C CA  . ASP B 1 295 ? 10.226  14.898  46.472  1.00 67.81  ? 481 ASP A CA  1 
ATOM   4885 C C   . ASP B 1 295 ? 9.240   13.774  46.790  1.00 71.04  ? 481 ASP A C   1 
ATOM   4886 O O   . ASP B 1 295 ? 8.123   13.997  47.256  1.00 74.60  ? 481 ASP A O   1 
ATOM   4887 C CB  . ASP B 1 295 ? 9.871   16.199  47.185  1.00 69.14  ? 481 ASP A CB  1 
ATOM   4888 C CG  . ASP B 1 295 ? 10.120  16.137  48.678  1.00 77.87  ? 481 ASP A CG  1 
ATOM   4889 O OD1 . ASP B 1 295 ? 10.587  15.085  49.160  1.00 83.12  ? 481 ASP A OD1 1 
ATOM   4890 O OD2 . ASP B 1 295 ? 9.852   17.145  49.368  1.00 83.69  ? 481 ASP A OD2 1 
ATOM   4891 N N   . ASP B 1 296 ? 9.686   12.542  46.534  1.00 75.30  ? 482 ASP A N   1 
ATOM   4892 C CA  . ASP B 1 296 ? 8.867   11.338  46.663  1.00 74.46  ? 482 ASP A CA  1 
ATOM   4893 C C   . ASP B 1 296 ? 7.597   11.435  45.829  1.00 71.98  ? 482 ASP A C   1 
ATOM   4894 O O   . ASP B 1 296 ? 7.656   11.437  44.595  1.00 72.18  ? 482 ASP A O   1 
ATOM   4895 C CB  . ASP B 1 296 ? 8.522   11.052  48.127  1.00 79.88  ? 482 ASP A CB  1 
ATOM   4896 C CG  . ASP B 1 296 ? 9.723   10.606  48.930  1.00 83.77  ? 482 ASP A CG  1 
ATOM   4897 O OD1 . ASP B 1 296 ? 10.585  9.896   48.366  1.00 73.69  ? 482 ASP A OD1 1 
ATOM   4898 O OD2 . ASP B 1 296 ? 9.800   10.959  50.126  1.00 88.92  ? 482 ASP A OD2 1 
ATOM   4899 N N   . ASP B 1 297 ? 6.440   11.485  46.489  1.00 78.82  ? 483 ASP A N   1 
ATOM   4900 C CA  . ASP B 1 297 ? 5.169   11.580  45.782  1.00 80.23  ? 483 ASP A CA  1 
ATOM   4901 C C   . ASP B 1 297 ? 4.898   12.970  45.216  1.00 74.57  ? 483 ASP A C   1 
ATOM   4902 O O   . ASP B 1 297 ? 3.986   13.116  44.393  1.00 75.81  ? 483 ASP A O   1 
ATOM   4903 C CB  . ASP B 1 297 ? 4.018   11.171  46.705  1.00 76.50  ? 483 ASP A CB  1 
ATOM   4904 C CG  . ASP B 1 297 ? 3.808   12.149  47.839  1.00 83.88  ? 483 ASP A CG  1 
ATOM   4905 O OD1 . ASP B 1 297 ? 4.809   12.682  48.363  1.00 89.91  ? 483 ASP A OD1 1 
ATOM   4906 O OD2 . ASP B 1 297 ? 2.636   12.389  48.203  1.00 81.59  ? 483 ASP A OD2 1 
ATOM   4907 N N   . VAL B 1 298 ? 5.656   13.982  45.625  1.00 75.65  ? 484 VAL A N   1 
ATOM   4908 C CA  . VAL B 1 298 ? 5.453   15.357  45.184  1.00 74.35  ? 484 VAL A CA  1 
ATOM   4909 C C   . VAL B 1 298 ? 6.436   15.628  44.051  1.00 75.80  ? 484 VAL A C   1 
ATOM   4910 O O   . VAL B 1 298 ? 7.653   15.665  44.265  1.00 75.49  ? 484 VAL A O   1 
ATOM   4911 C CB  . VAL B 1 298 ? 5.647   16.350  46.338  1.00 74.97  ? 484 VAL A CB  1 
ATOM   4912 C CG1 . VAL B 1 298 ? 5.346   17.772  45.890  1.00 75.93  ? 484 VAL A CG1 1 
ATOM   4913 C CG2 . VAL B 1 298 ? 4.796   15.955  47.528  1.00 76.84  ? 484 VAL A CG2 1 
ATOM   4914 N N   . VAL B 1 299 ? 5.915   15.818  42.841  1.00 73.01  ? 485 VAL A N   1 
ATOM   4915 C CA  . VAL B 1 299 ? 6.716   16.180  41.677  1.00 71.67  ? 485 VAL A CA  1 
ATOM   4916 C C   . VAL B 1 299 ? 6.256   17.549  41.199  1.00 76.03  ? 485 VAL A C   1 
ATOM   4917 O O   . VAL B 1 299 ? 5.093   17.716  40.811  1.00 91.96  ? 485 VAL A O   1 
ATOM   4918 C CB  . VAL B 1 299 ? 6.592   15.140  40.555  1.00 72.92  ? 485 VAL A CB  1 
ATOM   4919 C CG1 . VAL B 1 299 ? 7.503   15.507  39.395  1.00 72.87  ? 485 VAL A CG1 1 
ATOM   4920 C CG2 . VAL B 1 299 ? 6.918   13.752  41.086  1.00 70.37  ? 485 VAL A CG2 1 
ATOM   4921 N N   . SER B 1 300 ? 7.165   18.522  41.219  1.00 75.25  ? 486 SER A N   1 
ATOM   4922 C CA  . SER B 1 300 ? 6.827   19.900  40.898  1.00 78.74  ? 486 SER A CA  1 
ATOM   4923 C C   . SER B 1 300 ? 7.936   20.522  40.062  1.00 72.26  ? 486 SER A C   1 
ATOM   4924 O O   . SER B 1 300 ? 9.068   20.035  40.029  1.00 73.65  ? 486 SER A O   1 
ATOM   4925 C CB  . SER B 1 300 ? 6.584   20.730  42.164  1.00 75.72  ? 486 SER A CB  1 
ATOM   4926 O OG  . SER B 1 300 ? 7.695   20.654  43.036  1.00 73.09  ? 486 SER A OG  1 
ATOM   4927 N N   . ARG B 1 301 ? 7.587   21.608  39.383  1.00 73.62  ? 487 ARG A N   1 
ATOM   4928 C CA  . ARG B 1 301 ? 8.544   22.389  38.617  1.00 72.93  ? 487 ARG A CA  1 
ATOM   4929 C C   . ARG B 1 301 ? 9.397   23.263  39.530  1.00 72.46  ? 487 ARG A C   1 
ATOM   4930 O O   . ARG B 1 301 ? 8.950   23.718  40.586  1.00 73.50  ? 487 ARG A O   1 
ATOM   4931 C CB  . ARG B 1 301 ? 7.809   23.263  37.602  1.00 74.92  ? 487 ARG A CB  1 
ATOM   4932 C CG  . ARG B 1 301 ? 7.410   22.545  36.326  1.00 77.06  ? 487 ARG A CG  1 
ATOM   4933 C CD  . ARG B 1 301 ? 8.549   22.622  35.330  1.00 82.99  ? 487 ARG A CD  1 
ATOM   4934 N NE  . ARG B 1 301 ? 8.873   24.014  35.032  1.00 90.24  ? 487 ARG A NE  1 
ATOM   4935 C CZ  . ARG B 1 301 ? 9.886   24.409  34.274  1.00 84.89  ? 487 ARG A CZ  1 
ATOM   4936 N NH1 . ARG B 1 301 ? 10.717  23.541  33.725  1.00 86.85  ? 487 ARG A NH1 1 
ATOM   4937 N NH2 . ARG B 1 301 ? 10.067  25.710  34.059  1.00 79.08  ? 487 ARG A NH2 1 
ATOM   4938 N N   . CYS B 1 302 ? 10.635  23.506  39.100  1.00 71.39  ? 488 CYS A N   1 
ATOM   4939 C CA  . CYS B 1 302 ? 11.561  24.325  39.869  1.00 76.38  ? 488 CYS A CA  1 
ATOM   4940 C C   . CYS B 1 302 ? 12.508  25.050  38.923  1.00 70.66  ? 488 CYS A C   1 
ATOM   4941 O O   . CYS B 1 302 ? 12.713  24.639  37.777  1.00 70.48  ? 488 CYS A O   1 
ATOM   4942 C CB  . CYS B 1 302 ? 12.366  23.487  40.867  1.00 69.46  ? 488 CYS A CB  1 
ATOM   4943 S SG  . CYS B 1 302 ? 13.353  22.190  40.096  1.00 71.94  ? 488 CYS A SG  1 
ATOM   4944 N N   . THR B 1 303 ? 13.097  26.130  39.428  1.00 70.75  ? 489 THR A N   1 
ATOM   4945 C CA  . THR B 1 303 ? 14.035  26.908  38.635  1.00 70.66  ? 489 THR A CA  1 
ATOM   4946 C C   . THR B 1 303 ? 15.347  26.151  38.466  1.00 74.64  ? 489 THR A C   1 
ATOM   4947 O O   . THR B 1 303 ? 15.705  25.289  39.274  1.00 76.14  ? 489 THR A O   1 
ATOM   4948 C CB  . THR B 1 303 ? 14.310  28.261  39.288  1.00 71.63  ? 489 THR A CB  1 
ATOM   4949 O OG1 . THR B 1 303 ? 15.027  28.067  40.513  1.00 70.69  ? 489 THR A OG1 1 
ATOM   4950 C CG2 . THR B 1 303 ? 13.008  28.971  39.587  1.00 73.53  ? 489 THR A CG2 1 
ATOM   4951 N N   . LYS B 1 304 ? 16.059  26.475  37.386  1.00 73.41  ? 490 LYS A N   1 
ATOM   4952 C CA  . LYS B 1 304 ? 17.376  25.887  37.165  1.00 72.77  ? 490 LYS A CA  1 
ATOM   4953 C C   . LYS B 1 304 ? 18.372  26.330  38.230  1.00 73.99  ? 490 LYS A C   1 
ATOM   4954 O O   . LYS B 1 304 ? 19.307  25.586  38.549  1.00 72.37  ? 490 LYS A O   1 
ATOM   4955 C CB  . LYS B 1 304 ? 17.879  26.255  35.769  1.00 68.18  ? 490 LYS A CB  1 
ATOM   4956 C CG  . LYS B 1 304 ? 19.027  25.399  35.271  1.00 75.79  ? 490 LYS A CG  1 
ATOM   4957 C CD  . LYS B 1 304 ? 19.041  25.316  33.747  1.00 82.51  ? 490 LYS A CD  1 
ATOM   4958 C CE  . LYS B 1 304 ? 19.236  26.682  33.106  1.00 72.74  ? 490 LYS A CE  1 
ATOM   4959 N NZ  . LYS B 1 304 ? 20.547  27.267  33.491  1.00 95.05  ? 490 LYS A NZ  1 
ATOM   4960 N N   . GLU B 1 305 ? 18.185  27.527  38.795  1.00 77.51  ? 491 GLU A N   1 
ATOM   4961 C CA  . GLU B 1 305 ? 19.013  27.952  39.920  1.00 69.53  ? 491 GLU A CA  1 
ATOM   4962 C C   . GLU B 1 305 ? 18.782  27.068  41.140  1.00 71.97  ? 491 GLU A C   1 
ATOM   4963 O O   . GLU B 1 305 ? 19.729  26.728  41.858  1.00 70.73  ? 491 GLU A O   1 
ATOM   4964 C CB  . GLU B 1 305 ? 18.727  29.413  40.270  1.00 70.74  ? 491 GLU A CB  1 
ATOM   4965 C CG  . GLU B 1 305 ? 19.240  30.440  39.266  1.00 75.96  ? 491 GLU A CG  1 
ATOM   4966 C CD  . GLU B 1 305 ? 18.340  30.596  38.046  1.00 76.40  ? 491 GLU A CD  1 
ATOM   4967 O OE1 . GLU B 1 305 ? 17.336  29.859  37.928  1.00 75.98  ? 491 GLU A OE1 1 
ATOM   4968 O OE2 . GLU B 1 305 ? 18.627  31.481  37.212  1.00 74.44  ? 491 GLU A OE2 1 
ATOM   4969 N N   . GLU B 1 306 ? 17.527  26.689  41.397  1.00 72.52  ? 492 GLU A N   1 
ATOM   4970 C CA  . GLU B 1 306 ? 17.255  25.829  42.543  1.00 72.75  ? 492 GLU A CA  1 
ATOM   4971 C C   . GLU B 1 306 ? 17.846  24.439  42.343  1.00 70.24  ? 492 GLU A C   1 
ATOM   4972 O O   . GLU B 1 306 ? 18.179  23.760  43.320  1.00 69.76  ? 492 GLU A O   1 
ATOM   4973 C CB  . GLU B 1 306 ? 15.749  25.746  42.804  1.00 73.12  ? 492 GLU A CB  1 
ATOM   4974 C CG  . GLU B 1 306 ? 15.383  24.969  44.066  1.00 76.20  ? 492 GLU A CG  1 
ATOM   4975 C CD  . GLU B 1 306 ? 13.893  24.976  44.352  1.00 91.22  ? 492 GLU A CD  1 
ATOM   4976 O OE1 . GLU B 1 306 ? 13.156  25.706  43.652  1.00 86.61  ? 492 GLU A OE1 1 
ATOM   4977 O OE2 . GLU B 1 306 ? 13.460  24.257  45.283  1.00 88.65  ? 492 GLU A OE2 1 
ATOM   4978 N N   . ALA B 1 307 ? 18.004  24.008  41.094  1.00 73.33  ? 493 ALA A N   1 
ATOM   4979 C CA  . ALA B 1 307 ? 18.532  22.681  40.812  1.00 67.86  ? 493 ALA A CA  1 
ATOM   4980 C C   . ALA B 1 307 ? 20.053  22.637  40.781  1.00 68.93  ? 493 ALA A C   1 
ATOM   4981 O O   . ALA B 1 307 ? 20.643  21.603  41.120  1.00 70.18  ? 493 ALA A O   1 
ATOM   4982 C CB  . ALA B 1 307 ? 17.982  22.167  39.479  1.00 67.93  ? 493 ALA A CB  1 
ATOM   4983 N N   . ILE B 1 308 ? 20.707  23.724  40.377  1.00 70.08  ? 494 ILE A N   1 
ATOM   4984 C CA  . ILE B 1 308 ? 22.147  23.685  40.152  1.00 65.50  ? 494 ILE A CA  1 
ATOM   4985 C C   . ILE B 1 308 ? 22.895  24.538  41.171  1.00 65.63  ? 494 ILE A C   1 
ATOM   4986 O O   . ILE B 1 308 ? 23.633  24.009  42.008  1.00 72.89  ? 494 ILE A O   1 
ATOM   4987 C CB  . ILE B 1 308 ? 22.480  24.130  38.715  1.00 66.04  ? 494 ILE A CB  1 
ATOM   4988 C CG1 . ILE B 1 308 ? 21.776  23.221  37.707  1.00 69.53  ? 494 ILE A CG1 1 
ATOM   4989 C CG2 . ILE B 1 308 ? 23.978  24.109  38.471  1.00 67.48  ? 494 ILE A CG2 1 
ATOM   4990 C CD1 . ILE B 1 308 ? 22.097  23.550  36.266  1.00 75.78  ? 494 ILE A CD1 1 
ATOM   4991 N N   . GLU B 1 309 ? 22.691  25.856  41.131  1.00 68.01  ? 495 GLU A N   1 
ATOM   4992 C CA  . GLU B 1 309 ? 23.500  26.749  41.959  1.00 66.48  ? 495 GLU A CA  1 
ATOM   4993 C C   . GLU B 1 309 ? 23.154  26.620  43.438  1.00 66.16  ? 495 GLU A C   1 
ATOM   4994 O O   . GLU B 1 309 ? 24.038  26.717  44.299  1.00 68.67  ? 495 GLU A O   1 
ATOM   4995 C CB  . GLU B 1 309 ? 23.334  28.193  41.495  1.00 71.84  ? 495 GLU A CB  1 
ATOM   4996 C CG  . GLU B 1 309 ? 24.299  28.589  40.393  1.00 77.23  ? 495 GLU A CG  1 
ATOM   4997 C CD  . GLU B 1 309 ? 23.826  28.159  39.011  1.00 81.91  ? 495 GLU A CD  1 
ATOM   4998 O OE1 . GLU B 1 309 ? 22.608  27.936  38.826  1.00 74.73  ? 495 GLU A OE1 1 
ATOM   4999 O OE2 . GLU B 1 309 ? 24.680  28.049  38.106  1.00 94.79  ? 495 GLU A OE2 1 
ATOM   5000 N N   . HIS B 1 310 ? 21.882  26.396  43.758  1.00 66.75  ? 496 HIS A N   1 
ATOM   5001 C CA  . HIS B 1 310 ? 21.483  26.354  45.158  1.00 70.39  ? 496 HIS A CA  1 
ATOM   5002 C C   . HIS B 1 310 ? 21.935  25.081  45.864  1.00 68.82  ? 496 HIS A C   1 
ATOM   5003 O O   . HIS B 1 310 ? 21.828  25.009  47.092  1.00 78.00  ? 496 HIS A O   1 
ATOM   5004 C CB  . HIS B 1 310 ? 19.963  26.507  45.281  1.00 71.66  ? 496 HIS A CB  1 
ATOM   5005 C CG  . HIS B 1 310 ? 19.461  27.887  44.971  1.00 75.77  ? 496 HIS A CG  1 
ATOM   5006 N ND1 . HIS B 1 310 ? 18.123  28.219  45.018  1.00 75.87  ? 496 HIS A ND1 1 
ATOM   5007 C CD2 . HIS B 1 310 ? 20.113  29.013  44.596  1.00 76.37  ? 496 HIS A CD2 1 
ATOM   5008 C CE1 . HIS B 1 310 ? 17.975  29.491  44.696  1.00 70.72  ? 496 HIS A CE1 1 
ATOM   5009 N NE2 . HIS B 1 310 ? 19.166  29.996  44.433  1.00 70.46  ? 496 HIS A NE2 1 
ATOM   5010 N N   . ASN B 1 311 ? 22.433  24.083  45.135  1.00 63.84  ? 497 ASN A N   1 
ATOM   5011 C CA  . ASN B 1 311 ? 22.934  22.856  45.741  1.00 67.60  ? 497 ASN A CA  1 
ATOM   5012 C C   . ASN B 1 311 ? 24.454  22.808  45.814  1.00 67.14  ? 497 ASN A C   1 
ATOM   5013 O O   . ASN B 1 311 ? 25.021  21.744  46.085  1.00 61.95  ? 497 ASN A O   1 
ATOM   5014 C CB  . ASN B 1 311 ? 22.407  21.638  44.988  1.00 67.23  ? 497 ASN A CB  1 
ATOM   5015 C CG  . ASN B 1 311 ? 20.954  21.374  45.284  1.00 69.67  ? 497 ASN A CG  1 
ATOM   5016 O OD1 . ASN B 1 311 ? 20.599  20.964  46.390  1.00 65.93  ? 497 ASN A OD1 1 
ATOM   5017 N ND2 . ASN B 1 311 ? 20.099  21.619  44.302  1.00 75.32  ? 497 ASN A ND2 1 
ATOM   5018 N N   . TYR B 1 312 ? 25.124  23.930  45.563  1.00 62.95  ? 498 TYR A N   1 
ATOM   5019 C CA  . TYR B 1 312 ? 26.577  23.953  45.632  1.00 67.28  ? 498 TYR A CA  1 
ATOM   5020 C C   . TYR B 1 312 ? 27.104  23.834  47.060  1.00 70.85  ? 498 TYR A C   1 
ATOM   5021 O O   . TYR B 1 312 ? 28.246  23.399  47.247  1.00 69.49  ? 498 TYR A O   1 
ATOM   5022 C CB  . TYR B 1 312 ? 27.106  25.224  44.969  1.00 71.64  ? 498 TYR A CB  1 
ATOM   5023 C CG  . TYR B 1 312 ? 27.055  25.202  43.454  1.00 66.24  ? 498 TYR A CG  1 
ATOM   5024 C CD1 . TYR B 1 312 ? 26.768  24.030  42.763  1.00 61.80  ? 498 TYR A CD1 1 
ATOM   5025 C CD2 . TYR B 1 312 ? 27.345  26.341  42.715  1.00 68.31  ? 498 TYR A CD2 1 
ATOM   5026 C CE1 . TYR B 1 312 ? 26.741  24.005  41.376  1.00 60.29  ? 498 TYR A CE1 1 
ATOM   5027 C CE2 . TYR B 1 312 ? 27.325  26.323  41.332  1.00 66.85  ? 498 TYR A CE2 1 
ATOM   5028 C CZ  . TYR B 1 312 ? 27.024  25.155  40.669  1.00 61.06  ? 498 TYR A CZ  1 
ATOM   5029 O OH  . TYR B 1 312 ? 27.007  25.145  39.294  1.00 61.33  ? 498 TYR A OH  1 
ATOM   5030 N N   . GLY B 1 313 ? 26.316  24.215  48.063  1.00 69.19  ? 499 GLY A N   1 
ATOM   5031 C CA  . GLY B 1 313 ? 26.722  24.086  49.453  1.00 66.31  ? 499 GLY A CA  1 
ATOM   5032 C C   . GLY B 1 313 ? 27.213  25.381  50.072  1.00 67.86  ? 499 GLY A C   1 
ATOM   5033 O O   . GLY B 1 313 ? 27.183  26.434  49.433  1.00 67.96  ? 499 GLY A O   1 
ATOM   5034 N N   . ARG B 1 322 ? 22.243  20.346  62.077  1.00 125.96 ? 508 ARG A N   1 
ATOM   5035 C CA  . ARG B 1 322 ? 22.567  19.689  60.817  1.00 131.23 ? 508 ARG A CA  1 
ATOM   5036 C C   . ARG B 1 322 ? 21.617  20.197  59.742  1.00 129.38 ? 508 ARG A C   1 
ATOM   5037 O O   . ARG B 1 322 ? 21.468  21.407  59.567  1.00 137.33 ? 508 ARG A O   1 
ATOM   5038 C CB  . ARG B 1 322 ? 22.484  18.165  60.963  1.00 127.31 ? 508 ARG A CB  1 
ATOM   5039 C CG  . ARG B 1 322 ? 21.340  17.679  61.845  1.00 129.70 ? 508 ARG A CG  1 
ATOM   5040 C CD  . ARG B 1 322 ? 21.322  16.161  61.910  1.00 126.96 ? 508 ARG A CD  1 
ATOM   5041 N NE  . ARG B 1 322 ? 20.185  15.641  62.659  1.00 132.13 ? 508 ARG A NE  1 
ATOM   5042 C CZ  . ARG B 1 322 ? 20.020  14.361  62.964  1.00 128.71 ? 508 ARG A CZ  1 
ATOM   5043 N NH1 . ARG B 1 322 ? 20.911  13.448  62.615  1.00 127.72 ? 508 ARG A NH1 1 
ATOM   5044 N NH2 . ARG B 1 322 ? 18.935  13.988  63.636  1.00 131.23 ? 508 ARG A NH2 1 
ATOM   5045 N N   . HIS B 1 323 ? 20.996  19.267  59.016  1.00 119.07 ? 509 HIS A N   1 
ATOM   5046 C CA  . HIS B 1 323 ? 19.886  19.486  58.090  1.00 113.66 ? 509 HIS A CA  1 
ATOM   5047 C C   . HIS B 1 323 ? 20.297  20.243  56.834  1.00 111.06 ? 509 HIS A C   1 
ATOM   5048 O O   . HIS B 1 323 ? 19.453  20.465  55.958  1.00 110.29 ? 509 HIS A O   1 
ATOM   5049 C CB  . HIS B 1 323 ? 18.733  20.255  58.749  1.00 118.72 ? 509 HIS A CB  1 
ATOM   5050 C CG  . HIS B 1 323 ? 18.054  19.501  59.848  1.00 128.91 ? 509 HIS A CG  1 
ATOM   5051 N ND1 . HIS B 1 323 ? 18.550  18.321  60.361  1.00 128.70 ? 509 HIS A ND1 1 
ATOM   5052 C CD2 . HIS B 1 323 ? 16.933  19.776  60.554  1.00 132.07 ? 509 HIS A CD2 1 
ATOM   5053 C CE1 . HIS B 1 323 ? 17.757  17.896  61.328  1.00 122.02 ? 509 HIS A CE1 1 
ATOM   5054 N NE2 . HIS B 1 323 ? 16.768  18.761  61.464  1.00 126.86 ? 509 HIS A NE2 1 
ATOM   5055 N N   . CYS B 1 324 ? 21.564  20.619  56.701  1.00 105.26 ? 510 CYS A N   1 
ATOM   5056 C CA  . CYS B 1 324 ? 22.010  21.405  55.560  1.00 93.50  ? 510 CYS A CA  1 
ATOM   5057 C C   . CYS B 1 324 ? 22.031  20.536  54.313  1.00 90.28  ? 510 CYS A C   1 
ATOM   5058 O O   . CYS B 1 324 ? 22.625  19.454  54.307  1.00 93.63  ? 510 CYS A O   1 
ATOM   5059 C CB  . CYS B 1 324 ? 23.393  21.990  55.830  1.00 90.19  ? 510 CYS A CB  1 
ATOM   5060 S SG  . CYS B 1 324 ? 24.444  20.885  56.779  1.00 101.87 ? 510 CYS A SG  1 
ATOM   5061 N N   . THR B 1 325 ? 21.372  21.009  53.259  1.00 80.89  ? 511 THR A N   1 
ATOM   5062 C CA  . THR B 1 325 ? 21.230  20.213  52.048  1.00 82.64  ? 511 THR A CA  1 
ATOM   5063 C C   . THR B 1 325 ? 22.559  20.111  51.308  1.00 78.26  ? 511 THR A C   1 
ATOM   5064 O O   . THR B 1 325 ? 23.263  21.108  51.111  1.00 76.13  ? 511 THR A O   1 
ATOM   5065 C CB  . THR B 1 325 ? 20.171  20.838  51.140  1.00 80.09  ? 511 THR A CB  1 
ATOM   5066 O OG1 . THR B 1 325 ? 18.894  20.789  51.788  1.00 78.79  ? 511 THR A OG1 1 
ATOM   5067 C CG2 . THR B 1 325 ? 20.096  20.103  49.813  1.00 74.93  ? 511 THR A CG2 1 
ATOM   5068 N N   . ASN B 1 326 ? 22.899  18.892  50.901  1.00 68.06  ? 512 ASN A N   1 
ATOM   5069 C CA  . ASN B 1 326 ? 24.141  18.597  50.210  1.00 65.74  ? 512 ASN A CA  1 
ATOM   5070 C C   . ASN B 1 326 ? 23.848  17.735  48.993  1.00 66.81  ? 512 ASN A C   1 
ATOM   5071 O O   . ASN B 1 326 ? 23.062  16.787  49.072  1.00 64.69  ? 512 ASN A O   1 
ATOM   5072 C CB  . ASN B 1 326 ? 25.122  17.863  51.135  1.00 67.93  ? 512 ASN A CB  1 
ATOM   5073 C CG  . ASN B 1 326 ? 25.544  18.700  52.324  1.00 81.66  ? 512 ASN A CG  1 
ATOM   5074 O OD1 . ASN B 1 326 ? 25.077  18.487  53.445  1.00 88.50  ? 512 ASN A OD1 1 
ATOM   5075 N ND2 . ASN B 1 326 ? 26.430  19.660  52.087  1.00 84.14  ? 512 ASN A ND2 1 
ATOM   5076 N N   . ALA B 1 327 ? 24.492  18.055  47.874  1.00 67.52  ? 513 ALA A N   1 
ATOM   5077 C CA  . ALA B 1 327 ? 24.407  17.233  46.674  1.00 60.76  ? 513 ALA A CA  1 
ATOM   5078 C C   . ALA B 1 327 ? 25.495  16.167  46.727  1.00 60.09  ? 513 ALA A C   1 
ATOM   5079 O O   . ALA B 1 327 ? 26.669  16.484  46.936  1.00 59.97  ? 513 ALA A O   1 
ATOM   5080 C CB  . ALA B 1 327 ? 24.551  18.089  45.416  1.00 59.80  ? 513 ALA A CB  1 
ATOM   5081 N N   . TYR B 1 328 ? 25.099  14.902  46.554  1.00 59.82  ? 514 TYR A N   1 
ATOM   5082 C CA  . TYR B 1 328 ? 26.020  13.781  46.686  1.00 59.44  ? 514 TYR A CA  1 
ATOM   5083 C C   . TYR B 1 328 ? 26.202  12.952  45.424  1.00 57.94  ? 514 TYR A C   1 
ATOM   5084 O O   . TYR B 1 328 ? 27.200  12.232  45.330  1.00 57.39  ? 514 TYR A O   1 
ATOM   5085 C CB  . TYR B 1 328 ? 25.576  12.843  47.823  1.00 60.92  ? 514 TYR A CB  1 
ATOM   5086 C CG  . TYR B 1 328 ? 24.220  12.206  47.615  1.00 61.30  ? 514 TYR A CG  1 
ATOM   5087 C CD1 . TYR B 1 328 ? 23.059  12.898  47.933  1.00 62.28  ? 514 TYR A CD1 1 
ATOM   5088 C CD2 . TYR B 1 328 ? 24.098  10.919  47.107  1.00 60.85  ? 514 TYR A CD2 1 
ATOM   5089 C CE1 . TYR B 1 328 ? 21.813  12.332  47.750  1.00 64.35  ? 514 TYR A CE1 1 
ATOM   5090 C CE2 . TYR B 1 328 ? 22.849  10.342  46.917  1.00 61.41  ? 514 TYR A CE2 1 
ATOM   5091 C CZ  . TYR B 1 328 ? 21.708  11.056  47.243  1.00 66.77  ? 514 TYR A CZ  1 
ATOM   5092 O OH  . TYR B 1 328 ? 20.454  10.505  47.067  1.00 63.38  ? 514 TYR A OH  1 
ATOM   5093 N N   . MET B 1 329 ? 25.283  13.021  44.463  1.00 57.43  ? 515 MET A N   1 
ATOM   5094 C CA  . MET B 1 329 ? 25.423  12.281  43.216  1.00 56.22  ? 515 MET A CA  1 
ATOM   5095 C C   . MET B 1 329 ? 24.938  13.133  42.052  1.00 55.73  ? 515 MET A C   1 
ATOM   5096 O O   . MET B 1 329 ? 23.939  13.847  42.169  1.00 56.48  ? 515 MET A O   1 
ATOM   5097 C CB  . MET B 1 329 ? 24.652  10.956  43.255  1.00 56.61  ? 515 MET A CB  1 
ATOM   5098 C CG  . MET B 1 329 ? 24.747  10.150  41.972  1.00 55.57  ? 515 MET A CG  1 
ATOM   5099 S SD  . MET B 1 329 ? 24.013  8.510   42.106  1.00 58.48  ? 515 MET A SD  1 
ATOM   5100 C CE  . MET B 1 329 ? 24.155  7.922   40.418  1.00 55.05  ? 515 MET A CE  1 
ATOM   5101 N N   . LEU B 1 330 ? 25.667  13.065  40.937  1.00 54.67  ? 516 LEU A N   1 
ATOM   5102 C CA  . LEU B 1 330 ? 25.339  13.795  39.719  1.00 54.42  ? 516 LEU A CA  1 
ATOM   5103 C C   . LEU B 1 330 ? 25.311  12.831  38.544  1.00 53.76  ? 516 LEU A C   1 
ATOM   5104 O O   . LEU B 1 330 ? 26.109  11.891  38.485  1.00 58.47  ? 516 LEU A O   1 
ATOM   5105 C CB  . LEU B 1 330 ? 26.345  14.910  39.435  1.00 54.16  ? 516 LEU A CB  1 
ATOM   5106 C CG  . LEU B 1 330 ? 26.601  15.925  40.547  1.00 57.64  ? 516 LEU A CG  1 
ATOM   5107 C CD1 . LEU B 1 330 ? 27.758  16.850  40.187  1.00 57.10  ? 516 LEU A CD1 1 
ATOM   5108 C CD2 . LEU B 1 330 ? 25.335  16.728  40.812  1.00 61.47  ? 516 LEU A CD2 1 
ATOM   5109 N N   . VAL B 1 331 ? 24.395  13.066  37.610  1.00 55.43  ? 517 VAL A N   1 
ATOM   5110 C CA  . VAL B 1 331 ? 24.285  12.258  36.403  1.00 53.80  ? 517 VAL A CA  1 
ATOM   5111 C C   . VAL B 1 331 ? 24.446  13.176  35.204  1.00 53.93  ? 517 VAL A C   1 
ATOM   5112 O O   . VAL B 1 331 ? 23.692  14.147  35.048  1.00 54.79  ? 517 VAL A O   1 
ATOM   5113 C CB  . VAL B 1 331 ? 22.954  11.499  36.332  1.00 54.55  ? 517 VAL A CB  1 
ATOM   5114 C CG1 . VAL B 1 331 ? 22.944  10.608  35.109  1.00 54.35  ? 517 VAL A CG1 1 
ATOM   5115 C CG2 . VAL B 1 331 ? 22.746  10.681  37.592  1.00 54.79  ? 517 VAL A CG2 1 
ATOM   5116 N N   . TYR B 1 332 ? 25.424  12.868  34.362  1.00 53.28  ? 518 TYR A N   1 
ATOM   5117 C CA  . TYR B 1 332 ? 25.678  13.609  33.140  1.00 53.64  ? 518 TYR A CA  1 
ATOM   5118 C C   . TYR B 1 332 ? 25.432  12.702  31.944  1.00 55.15  ? 518 TYR A C   1 
ATOM   5119 O O   . TYR B 1 332 ? 25.673  11.492  32.002  1.00 55.97  ? 518 TYR A O   1 
ATOM   5120 C CB  . TYR B 1 332 ? 27.115  14.152  33.109  1.00 56.73  ? 518 TYR A CB  1 
ATOM   5121 C CG  . TYR B 1 332 ? 27.329  15.392  33.952  1.00 53.44  ? 518 TYR A CG  1 
ATOM   5122 C CD1 . TYR B 1 332 ? 27.636  15.296  35.301  1.00 53.08  ? 518 TYR A CD1 1 
ATOM   5123 C CD2 . TYR B 1 332 ? 27.236  16.661  33.390  1.00 54.36  ? 518 TYR A CD2 1 
ATOM   5124 C CE1 . TYR B 1 332 ? 27.831  16.433  36.071  1.00 53.59  ? 518 TYR A CE1 1 
ATOM   5125 C CE2 . TYR B 1 332 ? 27.430  17.800  34.150  1.00 54.83  ? 518 TYR A CE2 1 
ATOM   5126 C CZ  . TYR B 1 332 ? 27.726  17.680  35.489  1.00 54.41  ? 518 TYR A CZ  1 
ATOM   5127 O OH  . TYR B 1 332 ? 27.919  18.813  36.245  1.00 55.82  ? 518 TYR A OH  1 
ATOM   5128 N N   . ILE B 1 333 ? 24.944  13.293  30.858  1.00 55.28  ? 519 ILE A N   1 
ATOM   5129 C CA  . ILE B 1 333 ? 24.707  12.578  29.611  1.00 56.47  ? 519 ILE A CA  1 
ATOM   5130 C C   . ILE B 1 333 ? 25.482  13.286  28.514  1.00 58.72  ? 519 ILE A C   1 
ATOM   5131 O O   . ILE B 1 333 ? 25.445  14.518  28.418  1.00 58.69  ? 519 ILE A O   1 
ATOM   5132 C CB  . ILE B 1 333 ? 23.210  12.497  29.268  1.00 58.24  ? 519 ILE A CB  1 
ATOM   5133 C CG1 . ILE B 1 333 ? 22.467  11.762  30.381  1.00 56.28  ? 519 ILE A CG1 1 
ATOM   5134 C CG2 . ILE B 1 333 ? 23.001  11.780  27.942  1.00 57.94  ? 519 ILE A CG2 1 
ATOM   5135 C CD1 . ILE B 1 333 ? 20.995  11.599  30.121  1.00 60.24  ? 519 ILE A CD1 1 
ATOM   5136 N N   . ARG B 1 334 ? 26.194  12.503  27.705  1.00 59.06  ? 520 ARG A N   1 
ATOM   5137 C CA  . ARG B 1 334 ? 27.012  13.052  26.632  1.00 57.34  ? 520 ARG A CA  1 
ATOM   5138 C C   . ARG B 1 334 ? 26.145  13.756  25.596  1.00 65.74  ? 520 ARG A C   1 
ATOM   5139 O O   . ARG B 1 334 ? 25.061  13.285  25.240  1.00 67.65  ? 520 ARG A O   1 
ATOM   5140 C CB  . ARG B 1 334 ? 27.815  11.932  25.970  1.00 64.72  ? 520 ARG A CB  1 
ATOM   5141 C CG  . ARG B 1 334 ? 29.008  12.401  25.154  1.00 68.93  ? 520 ARG A CG  1 
ATOM   5142 C CD  . ARG B 1 334 ? 29.661  11.228  24.443  1.00 70.71  ? 520 ARG A CD  1 
ATOM   5143 N NE  . ARG B 1 334 ? 30.922  11.596  23.813  1.00 80.34  ? 520 ARG A NE  1 
ATOM   5144 C CZ  . ARG B 1 334 ? 32.120  11.294  24.296  1.00 74.46  ? 520 ARG A CZ  1 
ATOM   5145 N NH1 . ARG B 1 334 ? 32.261  10.592  25.410  1.00 67.12  ? 520 ARG A NH1 1 
ATOM   5146 N NH2 . ARG B 1 334 ? 33.203  11.708  23.646  1.00 78.37  ? 520 ARG A NH2 1 
ATOM   5147 N N   . GLU B 1 335 ? 26.637  14.897  25.108  1.00 63.19  ? 521 GLU A N   1 
ATOM   5148 C CA  . GLU B 1 335 ? 25.870  15.699  24.161  1.00 61.35  ? 521 GLU A CA  1 
ATOM   5149 C C   . GLU B 1 335 ? 25.600  14.926  22.877  1.00 64.87  ? 521 GLU A C   1 
ATOM   5150 O O   . GLU B 1 335 ? 24.490  14.979  22.332  1.00 70.65  ? 521 GLU A O   1 
ATOM   5151 C CB  . GLU B 1 335 ? 26.624  16.993  23.856  1.00 64.96  ? 521 GLU A CB  1 
ATOM   5152 C CG  . GLU B 1 335 ? 25.753  18.173  23.478  1.00 78.61  ? 521 GLU A CG  1 
ATOM   5153 C CD  . GLU B 1 335 ? 26.541  19.468  23.382  1.00 86.33  ? 521 GLU A CD  1 
ATOM   5154 O OE1 . GLU B 1 335 ? 27.768  19.406  23.147  1.00 85.21  ? 521 GLU A OE1 1 
ATOM   5155 O OE2 . GLU B 1 335 ? 25.932  20.548  23.542  1.00 89.62  ? 521 GLU A OE2 1 
ATOM   5156 N N   . SER B 1 336 ? 26.603  14.198  22.381  1.00 69.17  ? 522 SER A N   1 
ATOM   5157 C CA  . SER B 1 336 ? 26.435  13.433  21.149  1.00 73.90  ? 522 SER A CA  1 
ATOM   5158 C C   . SER B 1 336 ? 25.438  12.291  21.312  1.00 70.36  ? 522 SER A C   1 
ATOM   5159 O O   . SER B 1 336 ? 24.844  11.850  20.321  1.00 73.65  ? 522 SER A O   1 
ATOM   5160 C CB  . SER B 1 336 ? 27.790  12.906  20.668  1.00 72.96  ? 522 SER A CB  1 
ATOM   5161 O OG  . SER B 1 336 ? 28.412  12.082  21.637  1.00 66.66  ? 522 SER A OG  1 
ATOM   5162 N N   . LYS B 1 337 ? 25.255  11.787  22.534  1.00 66.36  ? 523 LYS A N   1 
ATOM   5163 C CA  . LYS B 1 337 ? 24.348  10.677  22.804  1.00 71.72  ? 523 LYS A CA  1 
ATOM   5164 C C   . LYS B 1 337 ? 23.028  11.114  23.434  1.00 71.63  ? 523 LYS A C   1 
ATOM   5165 O O   . LYS B 1 337 ? 22.219  10.255  23.795  1.00 68.41  ? 523 LYS A O   1 
ATOM   5166 C CB  . LYS B 1 337 ? 25.021  9.649   23.718  1.00 64.99  ? 523 LYS A CB  1 
ATOM   5167 C CG  . LYS B 1 337 ? 26.364  9.126   23.235  1.00 74.03  ? 523 LYS A CG  1 
ATOM   5168 C CD  . LYS B 1 337 ? 26.225  8.301   21.971  1.00 76.05  ? 523 LYS A CD  1 
ATOM   5169 C CE  . LYS B 1 337 ? 27.571  7.744   21.541  1.00 77.56  ? 523 LYS A CE  1 
ATOM   5170 N NZ  . LYS B 1 337 ? 27.462  6.925   20.305  1.00 91.82  ? 523 LYS A NZ  1 
ATOM   5171 N N   . LEU B 1 338 ? 22.791  12.421  23.577  1.00 73.13  ? 524 LEU A N   1 
ATOM   5172 C CA  . LEU B 1 338 ? 21.680  12.884  24.404  1.00 62.54  ? 524 LEU A CA  1 
ATOM   5173 C C   . LEU B 1 338 ? 20.337  12.420  23.846  1.00 70.59  ? 524 LEU A C   1 
ATOM   5174 O O   . LEU B 1 338 ? 19.475  11.943  24.592  1.00 71.70  ? 524 LEU A O   1 
ATOM   5175 C CB  . LEU B 1 338 ? 21.721  14.409  24.526  1.00 63.29  ? 524 LEU A CB  1 
ATOM   5176 C CG  . LEU B 1 338 ? 20.695  15.056  25.461  1.00 63.58  ? 524 LEU A CG  1 
ATOM   5177 C CD1 . LEU B 1 338 ? 20.817  14.470  26.857  1.00 61.63  ? 524 LEU A CD1 1 
ATOM   5178 C CD2 . LEU B 1 338 ? 20.841  16.572  25.499  1.00 64.47  ? 524 LEU A CD2 1 
ATOM   5179 N N   . SER B 1 339 ? 20.146  12.540  22.531  1.00 74.48  ? 525 SER A N   1 
ATOM   5180 C CA  . SER B 1 339 ? 18.868  12.154  21.938  1.00 68.25  ? 525 SER A CA  1 
ATOM   5181 C C   . SER B 1 339 ? 18.661  10.645  21.989  1.00 71.68  ? 525 SER A C   1 
ATOM   5182 O O   . SER B 1 339 ? 17.531  10.177  22.164  1.00 78.27  ? 525 SER A O   1 
ATOM   5183 C CB  . SER B 1 339 ? 18.776  12.667  20.505  1.00 70.83  ? 525 SER A CB  1 
ATOM   5184 O OG  . SER B 1 339 ? 18.729  14.083  20.495  1.00 77.04  ? 525 SER A OG  1 
ATOM   5185 N N   . GLU B 1 340 ? 19.736  9.867   21.822  1.00 74.48  ? 526 GLU A N   1 
ATOM   5186 C CA  . GLU B 1 340 ? 19.610  8.413   21.887  1.00 68.08  ? 526 GLU A CA  1 
ATOM   5187 C C   . GLU B 1 340 ? 19.360  7.944   23.314  1.00 73.33  ? 526 GLU A C   1 
ATOM   5188 O O   . GLU B 1 340 ? 18.596  6.999   23.536  1.00 78.72  ? 526 GLU A O   1 
ATOM   5189 C CB  . GLU B 1 340 ? 20.862  7.739   21.324  1.00 75.14  ? 526 GLU A CB  1 
ATOM   5190 C CG  . GLU B 1 340 ? 20.740  6.224   21.224  1.00 78.40  ? 526 GLU A CG  1 
ATOM   5191 C CD  . GLU B 1 340 ? 22.005  5.548   20.719  1.00 83.77  ? 526 GLU A CD  1 
ATOM   5192 O OE1 . GLU B 1 340 ? 23.101  6.139   20.839  1.00 83.50  ? 526 GLU A OE1 1 
ATOM   5193 O OE2 . GLU B 1 340 ? 21.899  4.414   20.206  1.00 81.59  ? 526 GLU A OE2 1 
ATOM   5194 N N   . VAL B 1 341 ? 20.008  8.575   24.294  1.00 77.10  ? 527 VAL A N   1 
ATOM   5195 C CA  . VAL B 1 341 ? 19.746  8.228   25.687  1.00 68.33  ? 527 VAL A CA  1 
ATOM   5196 C C   . VAL B 1 341 ? 18.340  8.662   26.083  1.00 69.24  ? 527 VAL A C   1 
ATOM   5197 O O   . VAL B 1 341 ? 17.646  7.965   26.834  1.00 69.33  ? 527 VAL A O   1 
ATOM   5198 C CB  . VAL B 1 341 ? 20.815  8.845   26.606  1.00 62.67  ? 527 VAL A CB  1 
ATOM   5199 C CG1 . VAL B 1 341 ? 20.442  8.638   28.059  1.00 61.36  ? 527 VAL A CG1 1 
ATOM   5200 C CG2 . VAL B 1 341 ? 22.181  8.244   26.313  1.00 66.56  ? 527 VAL A CG2 1 
ATOM   5201 N N   . LEU B 1 342 ? 17.885  9.800   25.563  1.00 63.92  ? 528 LEU A N   1 
ATOM   5202 C CA  . LEU B 1 342 ? 16.586  10.367  25.914  1.00 68.82  ? 528 LEU A CA  1 
ATOM   5203 C C   . LEU B 1 342 ? 15.535  10.117  24.835  1.00 77.19  ? 528 LEU A C   1 
ATOM   5204 O O   . LEU B 1 342 ? 14.735  11.004  24.510  1.00 77.21  ? 528 LEU A O   1 
ATOM   5205 C CB  . LEU B 1 342 ? 16.728  11.856  26.209  1.00 68.32  ? 528 LEU A CB  1 
ATOM   5206 C CG  . LEU B 1 342 ? 17.610  12.173  27.424  1.00 63.25  ? 528 LEU A CG  1 
ATOM   5207 C CD1 . LEU B 1 342 ? 17.452  13.627  27.840  1.00 63.71  ? 528 LEU A CD1 1 
ATOM   5208 C CD2 . LEU B 1 342 ? 17.334  11.240  28.601  1.00 62.27  ? 528 LEU A CD2 1 
ATOM   5209 N N   . GLN B 1 343 ? 15.545  8.914   24.252  1.00 74.20  ? 529 GLN A N   1 
ATOM   5210 C CA  . GLN B 1 343 ? 14.536  8.515   23.279  1.00 73.38  ? 529 GLN A CA  1 
ATOM   5211 C C   . GLN B 1 343 ? 13.135  8.764   23.816  1.00 75.97  ? 529 GLN A C   1 
ATOM   5212 O O   . GLN B 1 343 ? 12.883  8.683   25.022  1.00 72.31  ? 529 GLN A O   1 
ATOM   5213 C CB  . GLN B 1 343 ? 14.663  7.024   22.958  1.00 73.25  ? 529 GLN A CB  1 
ATOM   5214 C CG  . GLN B 1 343 ? 15.882  6.622   22.189  1.00 75.35  ? 529 GLN A CG  1 
ATOM   5215 C CD  . GLN B 1 343 ? 16.074  5.116   22.173  1.00 72.16  ? 529 GLN A CD  1 
ATOM   5216 O OE1 . GLN B 1 343 ? 15.116  4.352   22.271  1.00 79.21  ? 529 GLN A OE1 1 
ATOM   5217 N NE2 . GLN B 1 343 ? 17.321  4.684   22.060  1.00 84.75  ? 529 GLN A NE2 1 
ATOM   5218 N N   . ALA B 1 344 ? 12.213  9.054   22.906  1.00 81.91  ? 530 ALA A N   1 
ATOM   5219 C CA  . ALA B 1 344 ? 10.805  9.059   23.263  1.00 76.06  ? 530 ALA A CA  1 
ATOM   5220 C C   . ALA B 1 344 ? 10.359  7.642   23.594  1.00 76.11  ? 530 ALA A C   1 
ATOM   5221 O O   . ALA B 1 344 ? 10.752  6.681   22.926  1.00 76.25  ? 530 ALA A O   1 
ATOM   5222 C CB  . ALA B 1 344 ? 9.970   9.632   22.123  1.00 80.03  ? 530 ALA A CB  1 
ATOM   5223 N N   . VAL B 1 345 ? 9.536   7.512   24.629  1.00 76.16  ? 531 VAL A N   1 
ATOM   5224 C CA  . VAL B 1 345 ? 9.044   6.215   25.082  1.00 76.44  ? 531 VAL A CA  1 
ATOM   5225 C C   . VAL B 1 345 ? 7.527   6.221   24.966  1.00 83.11  ? 531 VAL A C   1 
ATOM   5226 O O   . VAL B 1 345 ? 6.839   6.973   25.670  1.00 79.54  ? 531 VAL A O   1 
ATOM   5227 C CB  . VAL B 1 345 ? 9.483   5.901   26.518  1.00 78.03  ? 531 VAL A CB  1 
ATOM   5228 C CG1 . VAL B 1 345 ? 8.840   4.602   26.995  1.00 75.07  ? 531 VAL A CG1 1 
ATOM   5229 C CG2 . VAL B 1 345 ? 11.000  5.817   26.602  1.00 81.89  ? 531 VAL A CG2 1 
ATOM   5230 N N   . THR B 1 346 ? 7.005   5.376   24.090  1.00 86.75  ? 532 THR A N   1 
ATOM   5231 C CA  . THR B 1 346 ? 5.575   5.274   23.874  1.00 85.46  ? 532 THR A CA  1 
ATOM   5232 C C   . THR B 1 346 ? 5.020   4.055   24.598  1.00 88.30  ? 532 THR A C   1 
ATOM   5233 O O   . THR B 1 346 ? 5.755   3.145   24.991  1.00 84.74  ? 532 THR A O   1 
ATOM   5234 C CB  . THR B 1 346 ? 5.263   5.182   22.378  1.00 91.26  ? 532 THR A CB  1 
ATOM   5235 O OG1 . THR B 1 346 ? 5.793   3.957   21.853  1.00 92.24  ? 532 THR A OG1 1 
ATOM   5236 C CG2 . THR B 1 346 ? 5.898   6.358   21.642  1.00 86.45  ? 532 THR A CG2 1 
ATOM   5237 N N   . ASP B 1 347 ? 3.697   4.049   24.770  1.00 91.70  ? 533 ASP A N   1 
ATOM   5238 C CA  . ASP B 1 347 ? 3.052   2.918   25.421  1.00 89.25  ? 533 ASP A CA  1 
ATOM   5239 C C   . ASP B 1 347 ? 3.133   1.655   24.577  1.00 91.70  ? 533 ASP A C   1 
ATOM   5240 O O   . ASP B 1 347 ? 3.005   0.553   25.120  1.00 95.91  ? 533 ASP A O   1 
ATOM   5241 C CB  . ASP B 1 347 ? 1.603   3.257   25.757  1.00 90.17  ? 533 ASP A CB  1 
ATOM   5242 C CG  . ASP B 1 347 ? 1.489   4.209   26.937  1.00 96.89  ? 533 ASP A CG  1 
ATOM   5243 O OD1 . ASP B 1 347 ? 2.535   4.572   27.522  1.00 91.76  ? 533 ASP A OD1 1 
ATOM   5244 O OD2 . ASP B 1 347 ? 0.353   4.587   27.288  1.00 108.13 ? 533 ASP A OD2 1 
ATOM   5245 N N   . HIS B 1 348 ? 3.335   1.786   23.267  1.00 91.72  ? 534 HIS A N   1 
ATOM   5246 C CA  . HIS B 1 348 ? 3.504   0.608   22.431  1.00 95.67  ? 534 HIS A CA  1 
ATOM   5247 C C   . HIS B 1 348 ? 4.893   -0.005  22.576  1.00 97.59  ? 534 HIS A C   1 
ATOM   5248 O O   . HIS B 1 348 ? 5.095   -1.152  22.162  1.00 102.08 ? 534 HIS A O   1 
ATOM   5249 C CB  . HIS B 1 348 ? 3.242   0.965   20.968  1.00 101.71 ? 534 HIS A CB  1 
ATOM   5250 C CG  . HIS B 1 348 ? 1.864   1.491   20.715  1.00 111.96 ? 534 HIS A CG  1 
ATOM   5251 N ND1 . HIS B 1 348 ? 0.780   0.670   20.490  1.00 115.55 ? 534 HIS A ND1 1 
ATOM   5252 C CD2 . HIS B 1 348 ? 1.394   2.760   20.649  1.00 114.54 ? 534 HIS A CD2 1 
ATOM   5253 C CE1 . HIS B 1 348 ? -0.299  1.410   20.300  1.00 119.96 ? 534 HIS A CE1 1 
ATOM   5254 N NE2 . HIS B 1 348 ? 0.046   2.682   20.391  1.00 118.68 ? 534 HIS A NE2 1 
ATOM   5255 N N   . ASP B 1 349 ? 5.854   0.733   23.143  1.00 92.53  ? 535 ASP A N   1 
ATOM   5256 C CA  . ASP B 1 349 ? 7.164   0.159   23.430  1.00 93.04  ? 535 ASP A CA  1 
ATOM   5257 C C   . ASP B 1 349 ? 7.089   -0.974  24.448  1.00 94.02  ? 535 ASP A C   1 
ATOM   5258 O O   . ASP B 1 349 ? 7.993   -1.817  24.492  1.00 90.48  ? 535 ASP A O   1 
ATOM   5259 C CB  . ASP B 1 349 ? 8.128   1.242   23.934  1.00 91.43  ? 535 ASP A CB  1 
ATOM   5260 C CG  . ASP B 1 349 ? 8.605   2.175   22.826  1.00 89.59  ? 535 ASP A CG  1 
ATOM   5261 O OD1 . ASP B 1 349 ? 8.939   1.683   21.724  1.00 91.35  ? 535 ASP A OD1 1 
ATOM   5262 O OD2 . ASP B 1 349 ? 8.651   3.404   23.063  1.00 79.73  ? 535 ASP A OD2 1 
ATOM   5263 N N   . ILE B 1 350 ? 6.040   -1.019  25.263  1.00 93.06  ? 536 ILE A N   1 
ATOM   5264 C CA  . ILE B 1 350 ? 5.884   -2.083  26.252  1.00 89.50  ? 536 ILE A CA  1 
ATOM   5265 C C   . ILE B 1 350 ? 5.201   -3.271  25.588  1.00 88.81  ? 536 ILE A C   1 
ATOM   5266 O O   . ILE B 1 350 ? 4.121   -3.114  25.001  1.00 95.35  ? 536 ILE A O   1 
ATOM   5267 C CB  . ILE B 1 350 ? 5.093   -1.603  27.476  1.00 87.36  ? 536 ILE A CB  1 
ATOM   5268 C CG1 . ILE B 1 350 ? 5.624   -0.250  27.944  1.00 82.27  ? 536 ILE A CG1 1 
ATOM   5269 C CG2 . ILE B 1 350 ? 5.184   -2.623  28.602  1.00 86.78  ? 536 ILE A CG2 1 
ATOM   5270 C CD1 . ILE B 1 350 ? 4.940   0.271   29.184  1.00 82.06  ? 536 ILE A CD1 1 
ATOM   5271 N N   . PRO B 1 351 ? 5.794   -4.464  25.644  1.00 87.67  ? 537 PRO A N   1 
ATOM   5272 C CA  . PRO B 1 351 ? 5.174   -5.631  25.005  1.00 90.98  ? 537 PRO A CA  1 
ATOM   5273 C C   . PRO B 1 351 ? 3.819   -5.966  25.616  1.00 102.17 ? 537 PRO A C   1 
ATOM   5274 O O   . PRO B 1 351 ? 3.589   -5.785  26.814  1.00 98.89  ? 537 PRO A O   1 
ATOM   5275 C CB  . PRO B 1 351 ? 6.191   -6.752  25.255  1.00 87.34  ? 537 PRO A CB  1 
ATOM   5276 C CG  . PRO B 1 351 ? 7.488   -6.050  25.499  1.00 94.44  ? 537 PRO A CG  1 
ATOM   5277 C CD  . PRO B 1 351 ? 7.123   -4.773  26.197  1.00 93.45  ? 537 PRO A CD  1 
ATOM   5278 N N   . GLN B 1 352 ? 2.915   -6.465  24.766  1.00 102.46 ? 538 GLN A N   1 
ATOM   5279 C CA  . GLN B 1 352 ? 1.566   -6.784  25.226  1.00 104.46 ? 538 GLN A CA  1 
ATOM   5280 C C   . GLN B 1 352 ? 1.576   -7.906  26.253  1.00 106.10 ? 538 GLN A C   1 
ATOM   5281 O O   . GLN B 1 352 ? 0.753   -7.911  27.175  1.00 109.01 ? 538 GLN A O   1 
ATOM   5282 C CB  . GLN B 1 352 ? 0.671   -7.161  24.047  1.00 117.47 ? 538 GLN A CB  1 
ATOM   5283 C CG  . GLN B 1 352 ? -0.408  -6.136  23.744  1.00 115.13 ? 538 GLN A CG  1 
ATOM   5284 C CD  . GLN B 1 352 ? -1.233  -5.778  24.965  1.00 118.53 ? 538 GLN A CD  1 
ATOM   5285 O OE1 . GLN B 1 352 ? -0.938  -4.808  25.663  1.00 117.28 ? 538 GLN A OE1 1 
ATOM   5286 N NE2 . GLN B 1 352 ? -2.279  -6.555  25.224  1.00 126.90 ? 538 GLN A NE2 1 
ATOM   5287 N N   . GLN B 1 353 ? 2.495   -8.863  26.107  1.00 103.35 ? 539 GLN A N   1 
ATOM   5288 C CA  . GLN B 1 353 ? 2.597   -9.952  27.073  1.00 106.77 ? 539 GLN A CA  1 
ATOM   5289 C C   . GLN B 1 353 ? 2.965   -9.421  28.452  1.00 100.99 ? 539 GLN A C   1 
ATOM   5290 O O   . GLN B 1 353 ? 2.475   -9.916  29.473  1.00 104.97 ? 539 GLN A O   1 
ATOM   5291 C CB  . GLN B 1 353 ? 3.657   -10.950 26.606  1.00 118.98 ? 539 GLN A CB  1 
ATOM   5292 C CG  . GLN B 1 353 ? 3.332   -11.707 25.331  1.00 124.06 ? 539 GLN A CG  1 
ATOM   5293 C CD  . GLN B 1 353 ? 4.460   -12.639 24.920  1.00 133.36 ? 539 GLN A CD  1 
ATOM   5294 O OE1 . GLN B 1 353 ? 5.619   -12.432 25.291  1.00 126.41 ? 539 GLN A OE1 1 
ATOM   5295 N NE2 . GLN B 1 353 ? 4.126   -13.671 24.153  1.00 130.83 ? 539 GLN A NE2 1 
ATOM   5296 N N   . LEU B 1 354 ? 3.833   -8.411  28.499  1.00 100.70 ? 540 LEU A N   1 
ATOM   5297 C CA  . LEU B 1 354 ? 4.153   -7.759  29.761  1.00 93.02  ? 540 LEU A CA  1 
ATOM   5298 C C   . LEU B 1 354 ? 2.971   -6.958  30.294  1.00 89.13  ? 540 LEU A C   1 
ATOM   5299 O O   . LEU B 1 354 ? 2.664   -7.015  31.491  1.00 85.13  ? 540 LEU A O   1 
ATOM   5300 C CB  . LEU B 1 354 ? 5.374   -6.862  29.578  1.00 91.11  ? 540 LEU A CB  1 
ATOM   5301 C CG  . LEU B 1 354 ? 5.947   -6.211  30.832  1.00 79.71  ? 540 LEU A CG  1 
ATOM   5302 C CD1 . LEU B 1 354 ? 6.409   -7.270  31.830  1.00 79.56  ? 540 LEU A CD1 1 
ATOM   5303 C CD2 . LEU B 1 354 ? 7.076   -5.275  30.457  1.00 81.51  ? 540 LEU A CD2 1 
ATOM   5304 N N   . VAL B 1 355 ? 2.286   -6.216  29.418  1.00 97.19  ? 541 VAL A N   1 
ATOM   5305 C CA  . VAL B 1 355 ? 1.194   -5.349  29.859  1.00 100.90 ? 541 VAL A CA  1 
ATOM   5306 C C   . VAL B 1 355 ? 0.089   -6.159  30.519  1.00 98.68  ? 541 VAL A C   1 
ATOM   5307 O O   . VAL B 1 355 ? -0.459  -5.760  31.555  1.00 96.49  ? 541 VAL A O   1 
ATOM   5308 C CB  . VAL B 1 355 ? 0.647   -4.524  28.678  1.00 97.01  ? 541 VAL A CB  1 
ATOM   5309 C CG1 . VAL B 1 355 ? -0.562  -3.705  29.116  1.00 93.78  ? 541 VAL A CG1 1 
ATOM   5310 C CG2 . VAL B 1 355 ? 1.723   -3.609  28.132  1.00 103.24 ? 541 VAL A CG2 1 
ATOM   5311 N N   . GLU B 1 356 ? -0.247  -7.314  29.946  1.00 97.44  ? 542 GLU A N   1 
ATOM   5312 C CA  . GLU B 1 356 ? -1.332  -8.117  30.499  1.00 103.29 ? 542 GLU A CA  1 
ATOM   5313 C C   . GLU B 1 356 ? -0.994  -8.643  31.890  1.00 98.58  ? 542 GLU A C   1 
ATOM   5314 O O   . GLU B 1 356 ? -1.860  -8.666  32.772  1.00 99.19  ? 542 GLU A O   1 
ATOM   5315 C CB  . GLU B 1 356 ? -1.679  -9.253  29.540  1.00 108.72 ? 542 GLU A CB  1 
ATOM   5316 C CG  . GLU B 1 356 ? -2.396  -8.765  28.286  1.00 113.10 ? 542 GLU A CG  1 
ATOM   5317 C CD  . GLU B 1 356 ? -2.545  -9.843  27.238  1.00 129.78 ? 542 GLU A CD  1 
ATOM   5318 O OE1 . GLU B 1 356 ? -1.819  -10.856 27.324  1.00 134.43 ? 542 GLU A OE1 1 
ATOM   5319 O OE2 . GLU B 1 356 ? -3.397  -9.681  26.337  1.00 139.31 ? 542 GLU A OE2 1 
ATOM   5320 N N   . ARG B 1 357 ? 0.253   -9.068  32.111  1.00 96.88  ? 543 ARG A N   1 
ATOM   5321 C CA  . ARG B 1 357 ? 0.600   -9.613  33.420  1.00 95.91  ? 543 ARG A CA  1 
ATOM   5322 C C   . ARG B 1 357 ? 0.552   -8.532  34.495  1.00 93.55  ? 543 ARG A C   1 
ATOM   5323 O O   . ARG B 1 357 ? 0.096   -8.785  35.616  1.00 95.34  ? 543 ARG A O   1 
ATOM   5324 C CB  . ARG B 1 357 ? 1.976   -10.277 33.387  1.00 94.74  ? 543 ARG A CB  1 
ATOM   5325 C CG  . ARG B 1 357 ? 2.321   -10.948 34.708  1.00 94.01  ? 543 ARG A CG  1 
ATOM   5326 C CD  . ARG B 1 357 ? 3.644   -11.686 34.673  1.00 104.62 ? 543 ARG A CD  1 
ATOM   5327 N NE  . ARG B 1 357 ? 3.934   -12.295 35.966  1.00 106.61 ? 543 ARG A NE  1 
ATOM   5328 C CZ  . ARG B 1 357 ? 5.046   -12.958 36.253  1.00 103.12 ? 543 ARG A CZ  1 
ATOM   5329 N NH1 . ARG B 1 357 ? 6.000   -13.129 35.352  1.00 94.77  ? 543 ARG A NH1 1 
ATOM   5330 N NH2 . ARG B 1 357 ? 5.203   -13.464 37.473  1.00 100.61 ? 543 ARG A NH2 1 
ATOM   5331 N N   . LEU B 1 358 ? 1.028   -7.325  34.177  1.00 88.68  ? 544 LEU A N   1 
ATOM   5332 C CA  . LEU B 1 358 ? 0.993   -6.244  35.156  1.00 86.57  ? 544 LEU A CA  1 
ATOM   5333 C C   . LEU B 1 358 ? -0.438  -5.845  35.477  1.00 90.22  ? 544 LEU A C   1 
ATOM   5334 O O   . LEU B 1 358 ? -0.759  -5.550  36.634  1.00 93.26  ? 544 LEU A O   1 
ATOM   5335 C CB  . LEU B 1 358 ? 1.792   -5.042  34.657  1.00 88.42  ? 544 LEU A CB  1 
ATOM   5336 C CG  . LEU B 1 358 ? 3.273   -5.121  35.039  1.00 78.33  ? 544 LEU A CG  1 
ATOM   5337 C CD1 . LEU B 1 358 ? 4.025   -6.109  34.171  1.00 79.32  ? 544 LEU A CD1 1 
ATOM   5338 C CD2 . LEU B 1 358 ? 3.930   -3.769  34.999  1.00 77.50  ? 544 LEU A CD2 1 
ATOM   5339 N N   . GLN B 1 359 ? -1.306  -5.816  34.463  1.00 93.69  ? 545 GLN A N   1 
ATOM   5340 C CA  . GLN B 1 359 ? -2.717  -5.523  34.695  1.00 94.54  ? 545 GLN A CA  1 
ATOM   5341 C C   . GLN B 1 359 ? -3.379  -6.616  35.528  1.00 91.00  ? 545 GLN A C   1 
ATOM   5342 O O   . GLN B 1 359 ? -4.239  -6.330  36.370  1.00 90.98  ? 545 GLN A O   1 
ATOM   5343 C CB  . GLN B 1 359 ? -3.435  -5.369  33.354  1.00 96.43  ? 545 GLN A CB  1 
ATOM   5344 C CG  . GLN B 1 359 ? -2.955  -4.190  32.518  1.00 98.10  ? 545 GLN A CG  1 
ATOM   5345 C CD  . GLN B 1 359 ? -3.639  -4.120  31.167  1.00 107.80 ? 545 GLN A CD  1 
ATOM   5346 O OE1 . GLN B 1 359 ? -4.153  -5.122  30.666  1.00 116.13 ? 545 GLN A OE1 1 
ATOM   5347 N NE2 . GLN B 1 359 ? -3.634  -2.936  30.560  1.00 110.39 ? 545 GLN A NE2 1 
ATOM   5348 N N   . GLU B 1 360 ? -2.980  -7.874  35.311  1.00 91.85  ? 546 GLU A N   1 
ATOM   5349 C CA  . GLU B 1 360 ? -3.518  -8.984  36.092  1.00 93.59  ? 546 GLU A CA  1 
ATOM   5350 C C   . GLU B 1 360 ? -3.150  -8.858  37.565  1.00 92.25  ? 546 GLU A C   1 
ATOM   5351 O O   . GLU B 1 360 ? -3.981  -9.107  38.445  1.00 92.65  ? 546 GLU A O   1 
ATOM   5352 C CB  . GLU B 1 360 ? -3.006  -10.310 35.529  1.00 95.02  ? 546 GLU A CB  1 
ATOM   5353 C CG  . GLU B 1 360 ? -3.404  -11.534 36.338  1.00 96.69  ? 546 GLU A CG  1 
ATOM   5354 C CD  . GLU B 1 360 ? -4.892  -11.796 36.289  1.00 103.96 ? 546 GLU A CD  1 
ATOM   5355 O OE1 . GLU B 1 360 ? -5.502  -11.537 35.230  1.00 101.05 ? 546 GLU A OE1 1 
ATOM   5356 O OE2 . GLU B 1 360 ? -5.449  -12.263 37.305  1.00 113.93 ? 546 GLU A OE2 1 
ATOM   5357 N N   . GLU B 1 361 ? -1.901  -8.483  37.851  1.00 90.97  ? 547 GLU A N   1 
ATOM   5358 C CA  . GLU B 1 361 ? -1.478  -8.314  39.237  1.00 87.77  ? 547 GLU A CA  1 
ATOM   5359 C C   . GLU B 1 361 ? -2.287  -7.228  39.938  1.00 87.96  ? 547 GLU A C   1 
ATOM   5360 O O   . GLU B 1 361 ? -2.706  -7.408  41.088  1.00 89.60  ? 547 GLU A O   1 
ATOM   5361 C CB  . GLU B 1 361 ? 0.018   -8.011  39.293  1.00 88.93  ? 547 GLU A CB  1 
ATOM   5362 C CG  . GLU B 1 361 ? 0.875   -9.221  38.948  1.00 93.51  ? 547 GLU A CG  1 
ATOM   5363 C CD  . GLU B 1 361 ? 2.344   -9.021  39.269  1.00 88.56  ? 547 GLU A CD  1 
ATOM   5364 O OE1 . GLU B 1 361 ? 2.719   -7.900  39.668  1.00 85.77  ? 547 GLU A OE1 1 
ATOM   5365 O OE2 . GLU B 1 361 ? 3.122   -9.988  39.126  1.00 90.24  ? 547 GLU A OE2 1 
ATOM   5366 N N   . LYS B 1 362 ? -2.530  -6.099  39.264  1.00 85.48  ? 548 LYS A N   1 
ATOM   5367 C CA  . LYS B 1 362 ? -3.326  -5.049  39.892  1.00 84.89  ? 548 LYS A CA  1 
ATOM   5368 C C   . LYS B 1 362 ? -4.760  -5.495  40.133  1.00 92.36  ? 548 LYS A C   1 
ATOM   5369 O O   . LYS B 1 362 ? -5.382  -5.054  41.105  1.00 93.34  ? 548 LYS A O   1 
ATOM   5370 C CB  . LYS B 1 362 ? -3.310  -3.767  39.058  1.00 83.78  ? 548 LYS A CB  1 
ATOM   5371 C CG  . LYS B 1 362 ? -1.979  -3.040  39.110  1.00 99.21  ? 548 LYS A CG  1 
ATOM   5372 C CD  . LYS B 1 362 ? -2.081  -1.604  38.615  1.00 88.79  ? 548 LYS A CD  1 
ATOM   5373 C CE  . LYS B 1 362 ? -2.403  -1.528  37.135  1.00 91.59  ? 548 LYS A CE  1 
ATOM   5374 N NZ  . LYS B 1 362 ? -2.480  -0.110  36.668  1.00 91.17  ? 548 LYS A NZ  1 
ATOM   5375 N N   . ARG B 1 363 ? -5.300  -6.363  39.270  1.00 90.51  ? 549 ARG A N   1 
ATOM   5376 C CA  . ARG B 1 363 ? -6.628  -6.915  39.525  1.00 93.35  ? 549 ARG A CA  1 
ATOM   5377 C C   . ARG B 1 363 ? -6.643  -7.750  40.801  1.00 96.06  ? 549 ARG A C   1 
ATOM   5378 O O   . ARG B 1 363 ? -7.567  -7.638  41.615  1.00 102.29 ? 549 ARG A O   1 
ATOM   5379 C CB  . ARG B 1 363 ? -7.089  -7.759  38.337  1.00 96.19  ? 549 ARG A CB  1 
ATOM   5380 C CG  . ARG B 1 363 ? -7.338  -6.983  37.063  1.00 96.60  ? 549 ARG A CG  1 
ATOM   5381 C CD  . ARG B 1 363 ? -8.015  -7.860  36.029  1.00 99.78  ? 549 ARG A CD  1 
ATOM   5382 N NE  . ARG B 1 363 ? -7.921  -7.293  34.689  1.00 99.99  ? 549 ARG A NE  1 
ATOM   5383 C CZ  . ARG B 1 363 ? -7.014  -7.647  33.788  1.00 101.90 ? 549 ARG A CZ  1 
ATOM   5384 N NH1 . ARG B 1 363 ? -6.121  -8.591  34.039  1.00 99.15  ? 549 ARG A NH1 1 
ATOM   5385 N NH2 . ARG B 1 363 ? -6.999  -7.037  32.606  1.00 108.36 ? 549 ARG A NH2 1 
ATOM   5386 N N   . ILE B 1 364 ? -5.634  -8.606  40.983  1.00 95.61  ? 550 ILE A N   1 
ATOM   5387 C CA  . ILE B 1 364 ? -5.561  -9.443  42.178  1.00 93.05  ? 550 ILE A CA  1 
ATOM   5388 C C   . ILE B 1 364 ? -5.324  -8.590  43.420  1.00 90.63  ? 550 ILE A C   1 
ATOM   5389 O O   . ILE B 1 364 ? -5.814  -8.907  44.512  1.00 92.46  ? 550 ILE A O   1 
ATOM   5390 C CB  . ILE B 1 364 ? -4.485  -10.531 42.005  1.00 92.87  ? 550 ILE A CB  1 
ATOM   5391 C CG1 . ILE B 1 364 ? -4.788  -11.359 40.752  1.00 95.52  ? 550 ILE A CG1 1 
ATOM   5392 C CG2 . ILE B 1 364 ? -4.432  -11.427 43.237  1.00 93.22  ? 550 ILE A CG2 1 
ATOM   5393 C CD1 . ILE B 1 364 ? -3.735  -12.394 40.407  1.00 98.29  ? 550 ILE A CD1 1 
ATOM   5394 N N   . GLU B 1 365 ? -4.550  -7.511  43.284  1.00 92.11  ? 551 GLU A N   1 
ATOM   5395 C CA  . GLU B 1 365 ? -4.323  -6.619  44.417  1.00 94.54  ? 551 GLU A CA  1 
ATOM   5396 C C   . GLU B 1 365 ? -5.597  -5.870  44.801  1.00 96.54  ? 551 GLU A C   1 
ATOM   5397 O O   . GLU B 1 365 ? -5.850  -5.634  45.987  1.00 100.82 ? 551 GLU A O   1 
ATOM   5398 C CB  . GLU B 1 365 ? -3.196  -5.636  44.088  1.00 94.03  ? 551 GLU A CB  1 
ATOM   5399 C CG  . GLU B 1 365 ? -1.813  -6.272  43.975  1.00 95.14  ? 551 GLU A CG  1 
ATOM   5400 C CD  . GLU B 1 365 ? -0.735  -5.273  43.592  1.00 102.48 ? 551 GLU A CD  1 
ATOM   5401 O OE1 . GLU B 1 365 ? -1.089  -4.138  43.209  1.00 92.91  ? 551 GLU A OE1 1 
ATOM   5402 O OE2 . GLU B 1 365 ? 0.464   -5.619  43.688  1.00 104.03 ? 551 GLU A OE2 1 
ATOM   5403 N N   . ALA B 1 366 ? -6.421  -5.502  43.815  1.00 104.07 ? 552 ALA A N   1 
ATOM   5404 C CA  . ALA B 1 366 ? -7.633  -4.725  44.074  1.00 105.03 ? 552 ALA A CA  1 
ATOM   5405 C C   . ALA B 1 366 ? -8.710  -5.509  44.812  1.00 102.36 ? 552 ALA A C   1 
ATOM   5406 O O   . ALA B 1 366 ? -9.690  -4.903  45.260  1.00 102.98 ? 552 ALA A O   1 
ATOM   5407 C CB  . ALA B 1 366 ? -8.210  -4.186  42.764  1.00 98.93  ? 552 ALA A CB  1 
ATOM   5408 N N   . GLN B 1 367 ? -8.571  -6.823  44.933  1.00 94.98  ? 553 GLN A N   1 
ATOM   5409 C CA  . GLN B 1 367 ? -9.586  -7.637  45.588  1.00 95.40  ? 553 GLN A CA  1 
ATOM   5410 C C   . GLN B 1 367 ? -9.181  -8.008  47.011  1.00 95.70  ? 553 GLN A C   1 
ATOM   5411 O O   . GLN B 1 367 ? -8.940  -9.176  47.312  1.00 95.42  ? 553 GLN A O   1 
ATOM   5412 C CB  . GLN B 1 367 ? -9.852  -8.894  44.763  1.00 99.30  ? 553 GLN A CB  1 
ATOM   5413 C CG  . GLN B 1 367 ? -10.187 -8.597  43.307  1.00 99.23  ? 553 GLN A CG  1 
ATOM   5414 C CD  . GLN B 1 367 ? -10.061 -9.817  42.422  1.00 101.23 ? 553 GLN A CD  1 
ATOM   5415 O OE1 . GLN B 1 367 ? -10.154 -10.950 42.894  1.00 115.35 ? 553 GLN A OE1 1 
ATOM   5416 N NE2 . GLN B 1 367 ? -9.836  -9.594  41.130  1.00 101.41 ? 553 GLN A NE2 1 
HETATM 5417 C C   . ACE C 2 1   ? 7.460   7.593   -13.869 1.00 74.69  ? 0   ACE D C   1 
HETATM 5418 O O   . ACE C 2 1   ? 7.750   8.560   -14.491 1.00 71.23  ? 0   ACE D O   1 
HETATM 5419 C CH3 . ACE C 2 1   ? 7.336   6.238   -14.565 1.00 79.84  ? 0   ACE D CH3 1 
ATOM   5420 N N   . PHE C 2 2   ? 7.210   7.610   -12.563 1.00 77.14  ? 1   PHE D N   1 
ATOM   5421 C CA  . PHE C 2 2   ? 7.278   8.824   -11.756 1.00 74.42  ? 1   PHE D CA  1 
ATOM   5422 C C   . PHE C 2 2   ? 8.598   8.916   -10.991 1.00 75.40  ? 1   PHE D C   1 
ATOM   5423 O O   . PHE C 2 2   ? 8.930   8.016   -10.224 1.00 74.73  ? 1   PHE D O   1 
ATOM   5424 C CB  . PHE C 2 2   ? 6.103   8.869   -10.779 1.00 74.63  ? 1   PHE D CB  1 
ATOM   5425 C CG  . PHE C 2 2   ? 6.068   10.104  -9.939  1.00 71.91  ? 1   PHE D CG  1 
ATOM   5426 C CD1 . PHE C 2 2   ? 5.435   11.245  -10.400 1.00 73.98  ? 1   PHE D CD1 1 
ATOM   5427 C CD2 . PHE C 2 2   ? 6.670   10.132  -8.694  1.00 71.16  ? 1   PHE D CD2 1 
ATOM   5428 C CE1 . PHE C 2 2   ? 5.404   12.389  -9.638  1.00 70.20  ? 1   PHE D CE1 1 
ATOM   5429 C CE2 . PHE C 2 2   ? 6.643   11.276  -7.925  1.00 70.70  ? 1   PHE D CE2 1 
ATOM   5430 C CZ  . PHE C 2 2   ? 6.009   12.406  -8.397  1.00 69.27  ? 1   PHE D CZ  1 
HETATM 5431 C C1  . MEA C 2 3   ? 10.633  10.218  -10.528 1.00 70.19  ? 2   MEA D C1  1 
HETATM 5432 N N   . MEA C 2 3   ? 9.351   9.998   -11.175 1.00 73.23  ? 2   MEA D N   1 
HETATM 5433 C CA  . MEA C 2 3   ? 9.002   11.096  -12.068 1.00 70.72  ? 2   MEA D CA  1 
HETATM 5434 C C   . MEA C 2 3   ? 10.032  11.156  -13.195 1.00 72.45  ? 2   MEA D C   1 
HETATM 5435 O O   . MEA C 2 3   ? 11.015  11.811  -13.090 1.00 75.10  ? 2   MEA D O   1 
HETATM 5436 C CB  . MEA C 2 3   ? 8.956   12.416  -11.298 1.00 67.73  ? 2   MEA D CB  1 
HETATM 5437 C CG  . MEA C 2 3   ? 8.602   13.646  -12.134 1.00 69.95  ? 2   MEA D CG  1 
HETATM 5438 C CD1 . MEA C 2 3   ? 7.268   13.957  -12.354 1.00 70.74  ? 2   MEA D CD1 1 
HETATM 5439 C CE1 . MEA C 2 3   ? 6.933   15.073  -13.101 1.00 63.54  ? 2   MEA D CE1 1 
HETATM 5440 C CZ  . MEA C 2 3   ? 7.936   15.879  -13.624 1.00 77.79  ? 2   MEA D CZ  1 
HETATM 5441 C CE2 . MEA C 2 3   ? 9.272   15.576  -13.402 1.00 68.10  ? 2   MEA D CE2 1 
HETATM 5442 C CD2 . MEA C 2 3   ? 9.603   14.460  -12.652 1.00 63.17  ? 2   MEA D CD2 1 
ATOM   5443 N N   . ASN C 2 4   ? 9.754   10.446  -14.281 1.00 76.18  ? 3   ASN D N   1 
ATOM   5444 C CA  . ASN C 2 4   ? 10.687  10.363  -15.398 1.00 70.87  ? 3   ASN D CA  1 
ATOM   5445 C C   . ASN C 2 4   ? 10.020  10.708  -16.725 1.00 76.03  ? 3   ASN D C   1 
ATOM   5446 O O   . ASN C 2 4   ? 9.813   9.833   -17.566 1.00 77.25  ? 3   ASN D O   1 
ATOM   5447 C CB  . ASN C 2 4   ? 11.278  8.956   -15.460 1.00 73.41  ? 3   ASN D CB  1 
ATOM   5448 C CG  . ASN C 2 4   ? 11.459  8.343   -14.084 1.00 74.09  ? 3   ASN D CG  1 
ATOM   5449 O OD1 . ASN C 2 4   ? 12.128  8.912   -13.222 1.00 76.86  ? 3   ASN D OD1 1 
ATOM   5450 N ND2 . ASN C 2 4   ? 10.844  7.187   -13.864 1.00 76.62  ? 3   ASN D ND2 1 
HETATM 5451 C C1  . MEA C 2 5   ? 9.952   13.093  -16.007 1.00 71.70  ? 4   MEA D C1  1 
HETATM 5452 N N   . MEA C 2 5   ? 9.704   11.985  -16.924 1.00 78.35  ? 4   MEA D N   1 
HETATM 5453 C CA  . MEA C 2 5   ? 8.910   12.387  -18.088 1.00 83.93  ? 4   MEA D CA  1 
HETATM 5454 C C   . MEA C 2 5   ? 9.663   13.256  -19.119 1.00 89.91  ? 4   MEA D C   1 
HETATM 5455 O O   . MEA C 2 5   ? 10.603  13.911  -18.798 1.00 90.13  ? 4   MEA D O   1 
HETATM 5456 C CB  . MEA C 2 5   ? 7.659   13.106  -17.570 1.00 83.27  ? 4   MEA D CB  1 
HETATM 5457 C CG  . MEA C 2 5   ? 6.833   12.186  -16.673 1.00 75.25  ? 4   MEA D CG  1 
HETATM 5458 C CD1 . MEA C 2 5   ? 6.461   12.608  -15.409 1.00 72.46  ? 4   MEA D CD1 1 
HETATM 5459 C CE1 . MEA C 2 5   ? 5.731   11.773  -14.583 1.00 71.08  ? 4   MEA D CE1 1 
HETATM 5460 C CZ  . MEA C 2 5   ? 5.365   10.513  -15.024 1.00 78.18  ? 4   MEA D CZ  1 
HETATM 5461 C CE2 . MEA C 2 5   ? 5.743   10.087  -16.288 1.00 81.10  ? 4   MEA D CE2 1 
HETATM 5462 C CD2 . MEA C 2 5   ? 6.482   10.920  -17.109 1.00 77.42  ? 4   MEA D CD2 1 
ATOM   5463 N N   . PRO C 2 6   ? 9.209   13.235  -20.387 1.00 93.12  ? 5   PRO D N   1 
ATOM   5464 C CA  . PRO C 2 6   ? 8.077   12.459  -20.915 1.00 97.67  ? 5   PRO D CA  1 
ATOM   5465 C C   . PRO C 2 6   ? 8.422   10.999  -21.225 1.00 102.44 ? 5   PRO D C   1 
ATOM   5466 O O   . PRO C 2 6   ? 9.556   10.693  -21.617 1.00 99.04  ? 5   PRO D O   1 
ATOM   5467 C CB  . PRO C 2 6   ? 7.709   13.217  -22.193 1.00 95.83  ? 5   PRO D CB  1 
ATOM   5468 C CG  . PRO C 2 6   ? 9.011   13.758  -22.671 1.00 101.86 ? 5   PRO D CG  1 
ATOM   5469 C CD  . PRO C 2 6   ? 9.814   14.087  -21.427 1.00 101.39 ? 5   PRO D CD  1 
ATOM   5470 N N   . ASN C 2 7   ? 7.445   10.113  -21.038 1.00 98.30  ? 6   ASN D N   1 
ATOM   5471 C CA  . ASN C 2 7   ? 7.612   8.698   -21.351 1.00 93.31  ? 6   ASN D CA  1 
ATOM   5472 C C   . ASN C 2 7   ? 6.298   8.095   -21.833 1.00 96.64  ? 6   ASN D C   1 
ATOM   5473 O O   . ASN C 2 7   ? 5.231   8.683   -21.650 1.00 101.26 ? 6   ASN D O   1 
ATOM   5474 C CB  . ASN C 2 7   ? 8.151   7.930   -20.135 1.00 88.99  ? 6   ASN D CB  1 
ATOM   5475 C CG  . ASN C 2 7   ? 7.243   8.022   -18.909 1.00 88.61  ? 6   ASN D CG  1 
ATOM   5476 O OD1 . ASN C 2 7   ? 6.017   8.099   -19.014 1.00 91.64  ? 6   ASN D OD1 1 
ATOM   5477 N ND2 . ASN C 2 7   ? 7.856   8.002   -17.731 1.00 87.69  ? 6   ASN D ND2 1 
HETATM 5478 C C   . DI8 C 2 8   ? 4.508   5.211   -21.980 1.00 90.70  ? 7   DI8 D C   1 
HETATM 5479 N N   . DI8 C 2 8   ? 6.181   6.922   -22.519 1.00 98.71  ? 7   DI8 D N   1 
HETATM 5480 O O   . DI8 C 2 8   ? 3.762   4.308   -22.737 1.00 92.28  ? 7   DI8 D O   1 
HETATM 5481 C C1  . DI8 C 2 8   ? 4.746   6.003   -24.367 1.00 101.04 ? 7   DI8 D C1  1 
HETATM 5482 C C2  . DI8 C 2 8   ? 5.932   5.066   -24.759 1.00 100.01 ? 7   DI8 D C2  1 
HETATM 5483 C C3  . DI8 C 2 8   ? 5.735   4.029   -25.699 1.00 100.67 ? 7   DI8 D C3  1 
HETATM 5484 C C4  . DI8 C 2 8   ? 6.809   3.195   -26.037 1.00 99.09  ? 7   DI8 D C4  1 
HETATM 5485 C C5  . DI8 C 2 8   ? 8.059   3.383   -25.444 1.00 96.25  ? 7   DI8 D C5  1 
HETATM 5486 C C6  . DI8 C 2 8   ? 8.239   4.393   -24.524 1.00 97.37  ? 7   DI8 D C6  1 
HETATM 5487 C C7  . DI8 C 2 8   ? 7.135   5.246   -24.177 1.00 98.12  ? 7   DI8 D C7  1 
HETATM 5488 C C8  . DI8 C 2 8   ? 7.356   6.344   -23.174 1.00 95.91  ? 7   DI8 D C8  1 
HETATM 5489 C CA  . DI8 C 2 8   ? 4.851   6.419   -22.883 1.00 96.26  ? 7   DI8 D CA  1 
ATOM   5490 N N   . TYR C 2 9   ? 5.031   5.010   -20.718 1.00 95.66  ? 8   TYR D N   1 
ATOM   5491 C CA  . TYR C 2 9   ? 4.793   3.950   -19.746 1.00 94.00  ? 8   TYR D CA  1 
ATOM   5492 C C   . TYR C 2 9   ? 3.646   4.339   -18.830 1.00 92.24  ? 8   TYR D C   1 
ATOM   5493 O O   . TYR C 2 9   ? 3.657   5.425   -18.249 1.00 88.71  ? 8   TYR D O   1 
ATOM   5494 C CB  . TYR C 2 9   ? 6.041   3.664   -18.904 1.00 90.48  ? 8   TYR D CB  1 
ATOM   5495 C CG  . TYR C 2 9   ? 7.360   3.795   -19.632 1.00 90.69  ? 8   TYR D CG  1 
ATOM   5496 C CD1 . TYR C 2 9   ? 7.650   3.011   -20.738 1.00 96.20  ? 8   TYR D CD1 1 
ATOM   5497 C CD2 . TYR C 2 9   ? 8.328   4.688   -19.191 1.00 85.23  ? 8   TYR D CD2 1 
ATOM   5498 C CE1 . TYR C 2 9   ? 8.865   3.127   -21.398 1.00 97.19  ? 8   TYR D CE1 1 
ATOM   5499 C CE2 . TYR C 2 9   ? 9.543   4.810   -19.843 1.00 90.96  ? 8   TYR D CE2 1 
ATOM   5500 C CZ  . TYR C 2 9   ? 9.805   4.027   -20.946 1.00 89.44  ? 8   TYR D CZ  1 
ATOM   5501 O OH  . TYR C 2 9   ? 11.012  4.143   -21.597 1.00 85.24  ? 8   TYR D OH  1 
ATOM   5502 N N   . ARG C 2 10  ? 2.658   3.453   -18.699 1.00 89.80  ? 9   ARG D N   1 
ATOM   5503 C CA  . ARG C 2 10  ? 1.507   3.702   -17.845 1.00 89.66  ? 9   ARG D CA  1 
ATOM   5504 C C   . ARG C 2 10  ? 1.594   2.931   -16.533 1.00 90.77  ? 9   ARG D C   1 
ATOM   5505 O O   . ARG C 2 10  ? 0.572   2.723   -15.874 1.00 95.04  ? 9   ARG D O   1 
ATOM   5506 C CB  . ARG C 2 10  ? 0.202   3.369   -18.571 1.00 93.59  ? 9   ARG D CB  1 
ATOM   5507 C CG  . ARG C 2 10  ? -0.927  4.360   -18.259 1.00 105.44 ? 9   ARG D CG  1 
ATOM   5508 C CD  . ARG C 2 10  ? -2.270  3.675   -17.977 1.00 109.05 ? 9   ARG D CD  1 
ATOM   5509 N NE  . ARG C 2 10  ? -2.438  3.288   -16.578 1.00 105.92 ? 9   ARG D NE  1 
ATOM   5510 C CZ  . ARG C 2 10  ? -3.139  3.971   -15.679 1.00 105.19 ? 9   ARG D CZ  1 
ATOM   5511 N NH1 . ARG C 2 10  ? -3.744  5.107   -15.988 1.00 106.56 ? 9   ARG D NH1 1 
ATOM   5512 N NH2 . ARG C 2 10  ? -3.237  3.500   -14.438 1.00 102.09 ? 9   ARG D NH2 1 
ATOM   5513 N N   . ARG C 2 11  ? 2.795   2.511   -16.140 1.00 93.20  ? 10  ARG D N   1 
ATOM   5514 C CA  . ARG C 2 11  ? 3.019   1.928   -14.825 1.00 91.51  ? 10  ARG D CA  1 
ATOM   5515 C C   . ARG C 2 11  ? 3.405   2.987   -13.802 1.00 88.86  ? 10  ARG D C   1 
ATOM   5516 O O   . ARG C 2 11  ? 3.541   2.676   -12.612 1.00 89.08  ? 10  ARG D O   1 
ATOM   5517 C CB  . ARG C 2 11  ? 4.118   0.856   -14.910 1.00 93.12  ? 10  ARG D CB  1 
ATOM   5518 C CG  . ARG C 2 11  ? 4.278   0.001   -13.663 1.00 94.43  ? 10  ARG D CG  1 
ATOM   5519 C CD  . ARG C 2 11  ? 5.590   -0.763  -13.653 1.00 98.50  ? 10  ARG D CD  1 
ATOM   5520 N NE  . ARG C 2 11  ? 5.882   -1.301  -12.328 1.00 103.57 ? 10  ARG D NE  1 
ATOM   5521 C CZ  . ARG C 2 11  ? 6.839   -2.181  -12.066 1.00 99.07  ? 10  ARG D CZ  1 
ATOM   5522 N NH1 . ARG C 2 11  ? 7.618   -2.660  -13.022 1.00 98.02  ? 10  ARG D NH1 1 
ATOM   5523 N NH2 . ARG C 2 11  ? 7.013   -2.599  -10.815 1.00 100.54 ? 10  ARG D NH2 1 
ATOM   5524 N N   . CYS C 2 12  ? 3.538   4.237   -14.233 1.00 87.19  ? 11  CYS D N   1 
ATOM   5525 C CA  . CYS C 2 12  ? 3.912   5.315   -13.333 1.00 85.79  ? 11  CYS D CA  1 
ATOM   5526 C C   . CYS C 2 12  ? 2.684   5.773   -12.559 1.00 84.06  ? 11  CYS D C   1 
ATOM   5527 O O   . CYS C 2 12  ? 1.646   6.078   -13.153 1.00 89.74  ? 11  CYS D O   1 
ATOM   5528 C CB  . CYS C 2 12  ? 4.517   6.472   -14.130 1.00 85.90  ? 11  CYS D CB  1 
ATOM   5529 S SG  . CYS C 2 12  ? 6.036   6.062   -15.052 1.00 90.33  ? 11  CYS D SG  1 
ATOM   5530 N N   . GLY C 2 13  ? 2.809   5.855   -11.238 1.00 82.64  ? 12  GLY D N   1 
ATOM   5531 C CA  . GLY C 2 13  ? 1.687   6.270   -10.421 1.00 82.20  ? 12  GLY D CA  1 
ATOM   5532 C C   . GLY C 2 13  ? 0.601   5.216   -10.333 1.00 84.94  ? 12  GLY D C   1 
ATOM   5533 O O   . GLY C 2 13  ? -0.496  5.407   -10.868 1.00 94.90  ? 12  GLY D O   1 
ATOM   5534 N N   . LYS C 2 14  ? 0.896   4.089   -9.691  1.00 86.89  ? 13  LYS D N   1 
ATOM   5535 C CA  . LYS C 2 14  ? -0.077  3.007   -9.554  1.00 93.12  ? 13  LYS D CA  1 
ATOM   5536 C C   . LYS C 2 14  ? 0.314   2.057   -8.423  1.00 91.06  ? 13  LYS D C   1 
ATOM   5537 O O   . LYS C 2 14  ? -0.110  2.226   -7.279  1.00 90.68  ? 13  LYS D O   1 
ATOM   5538 C CB  . LYS C 2 14  ? -0.216  2.224   -10.863 1.00 95.13  ? 13  LYS D CB  1 
ATOM   5539 C CG  . LYS C 2 14  ? 0.953   1.289   -11.145 1.00 94.12  ? 13  LYS D CG  1 
ATOM   5540 C CD  . LYS C 2 14  ? 0.759   0.477   -12.433 1.00 96.31  ? 13  LYS D CD  1 
ATOM   5541 C CE  . LYS C 2 14  ? -0.428  0.964   -13.265 1.00 100.19 ? 13  LYS D CE  1 
ATOM   5542 N NZ  . LYS C 2 14  ? -0.613  0.205   -14.541 1.00 96.98  ? 13  LYS D NZ  1 
HETATM 5543 C C   . ACE D 2 1   ? 26.602  5.489   53.270  1.00 73.34  ? 0   ACE C C   1 
HETATM 5544 O O   . ACE D 2 1   ? 26.201  6.441   53.850  1.00 77.82  ? 0   ACE C O   1 
HETATM 5545 C CH3 . ACE D 2 1   ? 26.686  4.138   53.992  1.00 74.44  ? 0   ACE C CH3 1 
ATOM   5546 N N   . PHE D 2 2   ? 26.994  5.531   51.997  1.00 71.37  ? 1   PHE C N   1 
ATOM   5547 C CA  . PHE D 2 2   ? 26.978  6.757   51.196  1.00 68.35  ? 1   PHE C CA  1 
ATOM   5548 C C   . PHE D 2 2   ? 25.748  6.877   50.293  1.00 66.85  ? 1   PHE C C   1 
ATOM   5549 O O   . PHE D 2 2   ? 25.465  5.982   49.506  1.00 66.21  ? 1   PHE C O   1 
ATOM   5550 C CB  . PHE D 2 2   ? 28.247  6.833   50.342  1.00 66.92  ? 1   PHE C CB  1 
ATOM   5551 C CG  . PHE D 2 2   ? 28.318  8.054   49.471  1.00 65.58  ? 1   PHE C CG  1 
ATOM   5552 C CD1 . PHE D 2 2   ? 28.849  9.237   49.952  1.00 65.79  ? 1   PHE C CD1 1 
ATOM   5553 C CD2 . PHE D 2 2   ? 27.852  8.017   48.167  1.00 64.12  ? 1   PHE C CD2 1 
ATOM   5554 C CE1 . PHE D 2 2   ? 28.912  10.363  49.151  1.00 64.59  ? 1   PHE C CE1 1 
ATOM   5555 C CE2 . PHE D 2 2   ? 27.910  9.137   47.366  1.00 62.93  ? 1   PHE C CE2 1 
ATOM   5556 C CZ  . PHE D 2 2   ? 28.442  10.312  47.859  1.00 63.16  ? 1   PHE C CZ  1 
HETATM 5557 C C1  . MEA D 2 3   ? 23.889  8.333   49.550  1.00 65.67  ? 2   MEA C C1  1 
HETATM 5558 N N   . MEA D 2 3   ? 25.031  7.995   50.375  1.00 66.66  ? 2   MEA C N   1 
HETATM 5559 C CA  . MEA D 2 3   ? 25.340  9.091   51.276  1.00 67.40  ? 2   MEA C CA  1 
HETATM 5560 C C   . MEA D 2 3   ? 24.205  9.218   52.293  1.00 68.61  ? 2   MEA C C   1 
HETATM 5561 O O   . MEA D 2 3   ? 23.314  9.974   52.106  1.00 68.26  ? 2   MEA C O   1 
HETATM 5562 C CB  . MEA D 2 3   ? 25.525  10.392  50.486  1.00 66.15  ? 2   MEA C CB  1 
HETATM 5563 C CG  . MEA D 2 3   ? 25.828  11.631  51.333  1.00 66.82  ? 2   MEA C CG  1 
HETATM 5564 C CD1 . MEA D 2 3   ? 27.134  11.899  51.715  1.00 67.15  ? 2   MEA C CD1 1 
HETATM 5565 C CE1 . MEA D 2 3   ? 27.413  13.020  52.480  1.00 67.76  ? 2   MEA C CE1 1 
HETATM 5566 C CZ  . MEA D 2 3   ? 26.389  13.874  52.861  1.00 70.34  ? 2   MEA C CZ  1 
HETATM 5567 C CE2 . MEA D 2 3   ? 25.086  13.612  52.478  1.00 67.75  ? 2   MEA C CE2 1 
HETATM 5568 C CD2 . MEA D 2 3   ? 24.808  12.494  51.711  1.00 67.12  ? 2   MEA C CD2 1 
ATOM   5569 N N   . ASN D 2 4   ? 24.281  8.446   53.374  1.00 70.08  ? 3   ASN C N   1 
ATOM   5570 C CA  . ASN D 2 4   ? 23.239  8.456   54.399  1.00 71.37  ? 3   ASN C CA  1 
ATOM   5571 C C   . ASN D 2 4   ? 23.791  8.834   55.769  1.00 72.91  ? 3   ASN C C   1 
ATOM   5572 O O   . ASN D 2 4   ? 23.751  8.023   56.695  1.00 76.37  ? 3   ASN C O   1 
ATOM   5573 C CB  . ASN D 2 4   ? 22.556  7.085   54.489  1.00 71.87  ? 3   ASN C CB  1 
ATOM   5574 C CG  . ASN D 2 4   ? 22.425  6.401   53.138  1.00 70.44  ? 3   ASN C CG  1 
ATOM   5575 O OD1 . ASN D 2 4   ? 22.967  5.316   52.923  1.00 71.61  ? 3   ASN C OD1 1 
ATOM   5576 N ND2 . ASN D 2 4   ? 21.691  7.028   52.225  1.00 69.24  ? 3   ASN C ND2 1 
HETATM 5577 C C1  . MEA D 2 5   ? 24.241  11.205  55.012  1.00 71.38  ? 4   MEA C C1  1 
HETATM 5578 N N   . MEA D 2 5   ? 24.287  10.060  55.918  1.00 72.76  ? 4   MEA C N   1 
HETATM 5579 C CA  . MEA D 2 5   ? 24.972  10.408  57.160  1.00 74.16  ? 4   MEA C CA  1 
HETATM 5580 C C   . MEA D 2 5   ? 24.145  11.290  58.112  1.00 78.62  ? 4   MEA C C   1 
HETATM 5581 O O   . MEA D 2 5   ? 23.279  11.998  57.702  1.00 77.04  ? 4   MEA C O   1 
HETATM 5582 C CB  . MEA D 2 5   ? 26.304  11.081  56.816  1.00 77.95  ? 4   MEA C CB  1 
HETATM 5583 C CG  . MEA D 2 5   ? 27.190  10.125  56.021  1.00 74.88  ? 4   MEA C CG  1 
HETATM 5584 C CD1 . MEA D 2 5   ? 27.808  10.551  54.858  1.00 72.17  ? 4   MEA C CD1 1 
HETATM 5585 C CE1 . MEA D 2 5   ? 28.610  9.676   54.146  1.00 75.16  ? 4   MEA C CE1 1 
HETATM 5586 C CZ  . MEA D 2 5   ? 28.797  8.379   54.599  1.00 74.56  ? 4   MEA C CZ  1 
HETATM 5587 C CE2 . MEA D 2 5   ? 28.177  7.955   55.762  1.00 77.22  ? 4   MEA C CE2 1 
HETATM 5588 C CD2 . MEA D 2 5   ? 27.378  8.830   56.478  1.00 75.07  ? 4   MEA C CD2 1 
ATOM   5589 N N   . PRO D 2 6   ? 24.443  11.205  59.420  1.00 77.33  ? 5   PRO C N   1 
ATOM   5590 C CA  . PRO D 2 6   ? 25.461  10.338  60.025  1.00 78.10  ? 5   PRO C CA  1 
ATOM   5591 C C   . PRO D 2 6   ? 24.958  8.922   60.290  1.00 80.50  ? 5   PRO C C   1 
ATOM   5592 O O   . PRO D 2 6   ? 23.749  8.714   60.415  1.00 78.78  ? 5   PRO C O   1 
ATOM   5593 C CB  . PRO D 2 6   ? 25.781  11.052  61.335  1.00 81.96  ? 5   PRO C CB  1 
ATOM   5594 C CG  . PRO D 2 6   ? 24.481  11.680  61.715  1.00 79.70  ? 5   PRO C CG  1 
ATOM   5595 C CD  . PRO D 2 6   ? 23.810  12.079  60.423  1.00 82.72  ? 5   PRO C CD  1 
ATOM   5596 N N   . ASN D 2 7   ? 25.878  7.963   60.367  1.00 83.54  ? 6   ASN C N   1 
ATOM   5597 C CA  . ASN D 2 7   ? 25.527  6.584   60.690  1.00 83.21  ? 6   ASN C CA  1 
ATOM   5598 C C   . ASN D 2 7   ? 26.717  5.842   61.299  1.00 86.49  ? 6   ASN C C   1 
ATOM   5599 O O   . ASN D 2 7   ? 27.785  6.423   61.504  1.00 88.42  ? 6   ASN C O   1 
ATOM   5600 C CB  . ASN D 2 7   ? 25.000  5.845   59.444  1.00 82.18  ? 6   ASN C CB  1 
ATOM   5601 C CG  . ASN D 2 7   ? 26.003  5.801   58.295  1.00 81.40  ? 6   ASN C CG  1 
ATOM   5602 O OD1 . ASN D 2 7   ? 27.217  5.736   58.495  1.00 89.36  ? 6   ASN C OD1 1 
ATOM   5603 N ND2 . ASN D 2 7   ? 25.484  5.830   57.072  1.00 79.93  ? 6   ASN C ND2 1 
HETATM 5604 C C   . DI8 D 2 8   ? 28.113  2.788   61.623  1.00 84.57  ? 7   DI8 C C   1 
HETATM 5605 N N   . DI8 D 2 8   ? 26.592  4.668   61.981  1.00 87.35  ? 7   DI8 C N   1 
HETATM 5606 O O   . DI8 D 2 8   ? 28.673  1.816   62.453  1.00 88.58  ? 7   DI8 C O   1 
HETATM 5607 C C1  . DI8 D 2 8   ? 27.686  3.594   63.973  1.00 84.66  ? 7   DI8 C C1  1 
HETATM 5608 C C2  . DI8 D 2 8   ? 26.378  2.768   64.190  1.00 86.32  ? 7   DI8 C C2  1 
HETATM 5609 C C3  . DI8 D 2 8   ? 26.360  1.705   65.120  1.00 87.76  ? 7   DI8 C C3  1 
HETATM 5610 C C4  . DI8 D 2 8   ? 25.182  0.974   65.300  1.00 88.83  ? 7   DI8 C C4  1 
HETATM 5611 C C5  . DI8 D 2 8   ? 24.038  1.285   64.565  1.00 87.55  ? 7   DI8 C C5  1 
HETATM 5612 C C6  . DI8 D 2 8   ? 24.066  2.320   63.658  1.00 88.20  ? 7   DI8 C C6  1 
HETATM 5613 C C7  . DI8 D 2 8   ? 25.280  3.072   63.474  1.00 89.68  ? 7   DI8 C C7  1 
HETATM 5614 C C8  . DI8 D 2 8   ? 25.296  4.200   62.479  1.00 88.17  ? 7   DI8 C C8  1 
HETATM 5615 C CA  . DI8 D 2 8   ? 27.805  4.024   62.494  1.00 87.32  ? 7   DI8 C CA  1 
ATOM   5616 N N   . TYR D 2 9   ? 27.648  2.569   60.352  1.00 82.63  ? 8   TYR C N   1 
ATOM   5617 C CA  . TYR D 2 9   ? 28.055  1.562   59.379  1.00 83.61  ? 8   TYR C CA  1 
ATOM   5618 C C   . TYR D 2 9   ? 29.371  1.985   58.720  1.00 82.89  ? 8   TYR C C   1 
ATOM   5619 O O   . TYR D 2 9   ? 29.478  3.092   58.188  1.00 81.46  ? 8   TYR C O   1 
ATOM   5620 C CB  . TYR D 2 9   ? 26.945  1.354   58.343  1.00 87.47  ? 8   TYR C CB  1 
ATOM   5621 C CG  . TYR D 2 9   ? 25.551  1.468   58.936  1.00 87.02  ? 8   TYR C CG  1 
ATOM   5622 C CD1 . TYR D 2 9   ? 25.137  0.613   59.953  1.00 85.40  ? 8   TYR C CD1 1 
ATOM   5623 C CD2 . TYR D 2 9   ? 24.650  2.428   58.484  1.00 90.14  ? 8   TYR C CD2 1 
ATOM   5624 C CE1 . TYR D 2 9   ? 23.866  0.712   60.509  1.00 86.72  ? 8   TYR C CE1 1 
ATOM   5625 C CE2 . TYR D 2 9   ? 23.372  2.533   59.035  1.00 90.30  ? 8   TYR C CE2 1 
ATOM   5626 C CZ  . TYR D 2 9   ? 22.990  1.670   60.046  1.00 88.45  ? 8   TYR C CZ  1 
ATOM   5627 O OH  . TYR D 2 9   ? 21.735  1.761   60.602  1.00 81.91  ? 8   TYR C OH  1 
ATOM   5628 N N   . ARG D 2 10  ? 30.371  1.100   58.749  1.00 83.52  ? 9   ARG C N   1 
ATOM   5629 C CA  . ARG D 2 10  ? 31.694  1.413   58.223  1.00 87.97  ? 9   ARG C CA  1 
ATOM   5630 C C   . ARG D 2 10  ? 31.977  0.752   56.877  1.00 86.50  ? 9   ARG C C   1 
ATOM   5631 O O   . ARG D 2 10  ? 33.137  0.682   56.462  1.00 85.17  ? 9   ARG C O   1 
ATOM   5632 C CB  . ARG D 2 10  ? 32.764  1.006   59.236  1.00 89.38  ? 9   ARG C CB  1 
ATOM   5633 C CG  . ARG D 2 10  ? 32.377  1.292   60.676  1.00 92.85  ? 9   ARG C CG  1 
ATOM   5634 C CD  . ARG D 2 10  ? 33.472  0.878   61.639  1.00 110.63 ? 9   ARG C CD  1 
ATOM   5635 N NE  . ARG D 2 10  ? 33.249  1.432   62.969  1.00 125.32 ? 9   ARG C NE  1 
ATOM   5636 C CZ  . ARG D 2 10  ? 34.046  1.226   64.008  1.00 120.91 ? 9   ARG C CZ  1 
ATOM   5637 N NH1 . ARG D 2 10  ? 35.126  0.467   63.911  1.00 114.72 ? 9   ARG C NH1 1 
ATOM   5638 N NH2 . ARG D 2 10  ? 33.755  1.798   65.173  1.00 126.62 ? 9   ARG C NH2 1 
ATOM   5639 N N   . ARG D 2 11  ? 30.950  0.275   56.179  1.00 87.85  ? 10  ARG C N   1 
ATOM   5640 C CA  . ARG D 2 11  ? 31.105  -0.186  54.808  1.00 80.50  ? 10  ARG C CA  1 
ATOM   5641 C C   . ARG D 2 11  ? 30.745  0.890   53.794  1.00 78.47  ? 10  ARG C C   1 
ATOM   5642 O O   . ARG D 2 11  ? 30.798  0.634   52.585  1.00 79.05  ? 10  ARG C O   1 
ATOM   5643 C CB  . ARG D 2 11  ? 30.269  -1.450  54.564  1.00 74.67  ? 10  ARG C CB  1 
ATOM   5644 C CG  . ARG D 2 11  ? 28.773  -1.276  54.714  1.00 88.53  ? 10  ARG C CG  1 
ATOM   5645 C CD  . ARG D 2 11  ? 28.045  -2.536  54.264  1.00 86.85  ? 10  ARG C CD  1 
ATOM   5646 N NE  . ARG D 2 11  ? 28.336  -2.856  52.871  1.00 84.14  ? 10  ARG C NE  1 
ATOM   5647 C CZ  . ARG D 2 11  ? 27.971  -3.977  52.265  1.00 82.62  ? 10  ARG C CZ  1 
ATOM   5648 N NH1 . ARG D 2 11  ? 27.304  -4.924  52.906  1.00 92.44  ? 10  ARG C NH1 1 
ATOM   5649 N NH2 . ARG D 2 11  ? 28.282  -4.153  50.984  1.00 73.58  ? 10  ARG C NH2 1 
ATOM   5650 N N   . CYS D 2 12  ? 30.393  2.086   54.253  1.00 73.26  ? 11  CYS C N   1 
ATOM   5651 C CA  . CYS D 2 12  ? 29.965  3.151   53.360  1.00 75.86  ? 11  CYS C CA  1 
ATOM   5652 C C   . CYS D 2 12  ? 31.155  3.793   52.659  1.00 71.32  ? 11  CYS C C   1 
ATOM   5653 O O   . CYS D 2 12  ? 32.162  4.116   53.296  1.00 78.18  ? 11  CYS C O   1 
ATOM   5654 C CB  . CYS D 2 12  ? 29.192  4.215   54.145  1.00 79.83  ? 11  CYS C CB  1 
ATOM   5655 S SG  . CYS D 2 12  ? 27.655  3.670   54.934  1.00 82.75  ? 11  CYS C SG  1 
ATOM   5656 N N   . GLY D 2 13  ? 31.037  3.973   51.340  1.00 71.62  ? 12  GLY C N   1 
ATOM   5657 C CA  . GLY D 2 13  ? 32.066  4.605   50.539  1.00 70.46  ? 12  GLY C CA  1 
ATOM   5658 C C   . GLY D 2 13  ? 33.284  3.762   50.247  1.00 76.05  ? 12  GLY C C   1 
ATOM   5659 O O   . GLY D 2 13  ? 34.014  4.073   49.301  1.00 84.92  ? 12  GLY C O   1 
ATOM   5660 N N   . LYS D 2 14  ? 33.540  2.716   51.027  1.00 75.98  ? 13  LYS C N   1 
ATOM   5661 C CA  . LYS D 2 14  ? 34.716  1.879   50.826  1.00 79.95  ? 13  LYS C CA  1 
ATOM   5662 C C   . LYS D 2 14  ? 34.807  1.393   49.388  1.00 95.64  ? 13  LYS C C   1 
ATOM   5663 O O   . LYS D 2 14  ? 33.970  0.606   48.934  1.00 94.62  ? 13  LYS C O   1 
ATOM   5664 C CB  . LYS D 2 14  ? 34.678  0.680   51.781  1.00 75.66  ? 13  LYS C CB  1 
ATOM   5665 C CG  . LYS D 2 14  ? 34.706  1.045   53.258  1.00 78.35  ? 13  LYS C CG  1 
ATOM   5666 C CD  . LYS D 2 14  ? 36.012  1.723   53.640  1.00 90.04  ? 13  LYS C CD  1 
ATOM   5667 C CE  . LYS D 2 14  ? 37.190  0.766   53.536  1.00 96.44  ? 13  LYS C CE  1 
ATOM   5668 N NZ  . LYS D 2 14  ? 38.468  1.436   53.904  1.00 97.29  ? 13  LYS C NZ  1 
ATOM   5669 N N   . LYS D 2 15  ? 35.826  1.883   48.680  1.00 104.26 ? 14  LYS C N   1 
ATOM   5670 C CA  . LYS D 2 15  ? 36.221  1.437   47.344  1.00 96.30  ? 14  LYS C CA  1 
ATOM   5671 C C   . LYS D 2 15  ? 37.623  1.976   47.068  1.00 96.16  ? 14  LYS C C   1 
ATOM   5672 O O   . LYS D 2 15  ? 38.116  2.844   47.793  1.00 92.02  ? 14  LYS C O   1 
ATOM   5673 C CB  . LYS D 2 15  ? 35.247  1.912   46.256  1.00 90.09  ? 14  LYS C CB  1 
ATOM   5674 C CG  . LYS D 2 15  ? 34.079  0.963   45.962  1.00 100.39 ? 14  LYS C CG  1 
ATOM   5675 C CD  . LYS D 2 15  ? 34.520  -0.502  45.927  1.00 98.71  ? 14  LYS C CD  1 
ATOM   5676 C CE  . LYS D 2 15  ? 33.320  -1.458  45.830  1.00 99.84  ? 14  LYS C CE  1 
ATOM   5677 N NZ  . LYS D 2 15  ? 32.391  -1.400  47.006  1.00 80.46  ? 14  LYS C NZ  1 
HETATM 5678 C C1  . EOH E 3 .   ? 20.026  8.996   56.709  1.00 59.20  ? 601 EOH A C1  1 
HETATM 5679 C C2  . EOH E 3 .   ? 20.441  10.277  57.426  1.00 60.85  ? 601 EOH A C2  1 
HETATM 5680 O O   . EOH E 3 .   ? 20.816  7.894   57.098  1.00 60.62  ? 601 EOH A O   1 
HETATM 5681 O O   . HOH F 4 .   ? 39.289  8.347   3.422   1.00 70.17  ? 601 HOH B O   1 
HETATM 5682 O O   . HOH F 4 .   ? 14.363  23.220  6.967   1.00 62.18  ? 602 HOH B O   1 
HETATM 5683 O O   . HOH F 4 .   ? 26.393  12.542  8.988   1.00 48.42  ? 603 HOH B O   1 
HETATM 5684 O O   . HOH F 4 .   ? -10.343 20.219  10.780  1.00 57.48  ? 604 HOH B O   1 
HETATM 5685 O O   . HOH G 4 .   ? 9.937   10.144  43.409  1.00 60.56  ? 701 HOH A O   1 
HETATM 5686 O O   . HOH G 4 .   ? 45.756  16.035  37.255  1.00 55.08  ? 702 HOH A O   1 
HETATM 5687 O O   . HOH G 4 .   ? 13.246  9.089   54.373  1.00 64.22  ? 703 HOH A O   1 
HETATM 5688 O O   . HOH G 4 .   ? 38.748  22.676  52.471  1.00 52.63  ? 704 HOH A O   1 
HETATM 5689 O O   . HOH G 4 .   ? 8.415   10.087  29.858  1.00 63.80  ? 705 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 24  ? 1.0751 1.3872 1.1467 -0.0857 -0.0721 -0.0003 210 HIS B N   
2    C CA  . HIS A 24  ? 1.1487 1.4483 1.1950 -0.0717 -0.0604 0.0117  210 HIS B CA  
3    C C   . HIS A 24  ? 1.1975 1.4773 1.2033 -0.0634 -0.0695 0.0045  210 HIS B C   
4    O O   . HIS A 24  ? 1.2198 1.4863 1.2154 -0.0709 -0.0821 -0.0110 210 HIS B O   
5    C CB  . HIS A 24  ? 1.1173 1.4481 1.1751 -0.0542 -0.0591 0.0260  210 HIS B CB  
6    C CG  . HIS A 24  ? 1.2330 1.5547 1.2950 -0.0502 -0.0388 0.0414  210 HIS B CG  
7    N ND1 . HIS A 24  ? 1.1173 1.4563 1.1827 -0.0332 -0.0351 0.0567  210 HIS B ND1 
8    C CD2 . HIS A 24  ? 1.2145 1.5107 1.2773 -0.0609 -0.0217 0.0433  210 HIS B CD2 
9    C CE1 . HIS A 24  ? 1.1181 1.4409 1.1881 -0.0345 -0.0173 0.0661  210 HIS B CE1 
10   N NE2 . HIS A 24  ? 1.1892 1.4868 1.2563 -0.0508 -0.0093 0.0575  210 HIS B NE2 
11   N N   . THR A 25  ? 1.1368 1.4147 1.1216 -0.0478 -0.0628 0.0160  211 THR B N   
12   C CA  . THR A 25  ? 1.0529 1.3168 1.0006 -0.0367 -0.0691 0.0117  211 THR B CA  
13   C C   . THR A 25  ? 1.0402 1.3294 0.9753 -0.0144 -0.0721 0.0231  211 THR B C   
14   O O   . THR A 25  ? 0.9658 1.2479 0.8706 -0.0023 -0.0743 0.0228  211 THR B O   
15   C CB  . THR A 25  ? 1.0934 1.3232 1.0243 -0.0419 -0.0552 0.0152  211 THR B CB  
16   O OG1 . THR A 25  ? 1.0780 1.2984 0.9753 -0.0287 -0.0605 0.0125  211 THR B OG1 
17   C CG2 . THR A 25  ? 1.0050 1.2373 0.9484 -0.0397 -0.0376 0.0327  211 THR B CG2 
18   N N   . GLY A 26  ? 1.0542 1.3731 1.0125 -0.0079 -0.0712 0.0346  212 GLY B N   
19   C CA  . GLY A 26  ? 0.9363 1.2794 0.8864 0.0128  -0.0714 0.0502  212 GLY B CA  
20   C C   . GLY A 26  ? 0.8865 1.2206 0.8383 0.0177  -0.0531 0.0695  212 GLY B C   
21   O O   . GLY A 26  ? 0.8639 1.2181 0.8153 0.0336  -0.0509 0.0863  212 GLY B O   
22   N N   . TYR A 27  ? 0.8976 1.2022 0.8518 0.0044  -0.0405 0.0680  213 TYR B N   
23   C CA  . TYR A 27  ? 0.8959 1.1891 0.8527 0.0068  -0.0246 0.0835  213 TYR B CA  
24   C C   . TYR A 27  ? 0.8285 1.1073 0.8100 -0.0086 -0.0125 0.0827  213 TYR B C   
25   O O   . TYR A 27  ? 0.8505 1.1122 0.8321 -0.0235 -0.0125 0.0695  213 TYR B O   
26   C CB  . TYR A 27  ? 0.9288 1.1999 0.8562 0.0087  -0.0219 0.0819  213 TYR B CB  
27   C CG  . TYR A 27  ? 0.8643 1.1474 0.7636 0.0239  -0.0334 0.0788  213 TYR B CG  
28   C CD1 . TYR A 27  ? 0.8662 1.1792 0.7634 0.0418  -0.0367 0.0919  213 TYR B CD1 
29   C CD2 . TYR A 27  ? 0.9064 1.1704 0.7799 0.0215  -0.0403 0.0631  213 TYR B CD2 
30   C CE1 . TYR A 27  ? 0.8848 1.2105 0.7530 0.0574  -0.0461 0.0887  213 TYR B CE1 
31   C CE2 . TYR A 27  ? 0.8955 1.1700 0.7415 0.0372  -0.0502 0.0584  213 TYR B CE2 
32   C CZ  . TYR A 27  ? 0.8996 1.2059 0.7420 0.0553  -0.0528 0.0708  213 TYR B CZ  
33   O OH  . TYR A 27  ? 0.9212 1.2399 0.7335 0.0725  -0.0618 0.0658  213 TYR B OH  
34   N N   . VAL A 28  ? 0.8169 1.1023 0.8193 -0.0043 -0.0020 0.0971  214 VAL B N   
35   C CA  . VAL A 28  ? 0.8201 1.0937 0.8453 -0.0159 0.0104  0.0961  214 VAL B CA  
36   C C   . VAL A 28  ? 0.8024 1.0492 0.8175 -0.0196 0.0223  0.1002  214 VAL B C   
37   O O   . VAL A 28  ? 0.8797 1.1236 0.8802 -0.0112 0.0223  0.1090  214 VAL B O   
38   C CB  . VAL A 28  ? 0.8390 1.1354 0.8965 -0.0085 0.0140  0.1069  214 VAL B CB  
39   C CG1 . VAL A 28  ? 0.7969 1.0918 0.8590 0.0026  0.0222  0.1246  214 VAL B CG1 
40   C CG2 . VAL A 28  ? 0.9132 1.2045 0.9951 -0.0208 0.0234  0.0998  214 VAL B CG2 
41   N N   . GLY A 29  ? 0.8201 1.0487 0.8436 -0.0323 0.0326  0.0938  215 GLY B N   
42   C CA  . GLY A 29  ? 0.8153 1.0179 0.8280 -0.0375 0.0422  0.0946  215 GLY B CA  
43   C C   . GLY A 29  ? 0.8237 1.0243 0.8576 -0.0341 0.0531  0.1036  215 GLY B C   
44   O O   . GLY A 29  ? 0.8303 1.0490 0.8887 -0.0267 0.0545  0.1108  215 GLY B O   
45   N N   . LEU A 30  ? 0.7924 0.9697 0.8167 -0.0392 0.0601  0.1028  216 LEU B N   
46   C CA  . LEU A 30  ? 0.7915 0.9595 0.8330 -0.0383 0.0700  0.1075  216 LEU B CA  
47   C C   . LEU A 30  ? 0.8159 0.9638 0.8534 -0.0503 0.0792  0.0945  216 LEU B C   
48   O O   . LEU A 30  ? 0.8406 0.9727 0.8544 -0.0590 0.0782  0.0866  216 LEU B O   
49   C CB  . LEU A 30  ? 0.7911 0.9502 0.8263 -0.0339 0.0694  0.1174  216 LEU B CB  
50   C CG  . LEU A 30  ? 0.7871 0.9669 0.8291 -0.0205 0.0639  0.1342  216 LEU B CG  
51   C CD1 . LEU A 30  ? 0.7869 0.9584 0.8196 -0.0188 0.0634  0.1430  216 LEU B CD1 
52   C CD2 . LEU A 30  ? 0.7866 0.9787 0.8596 -0.0123 0.0682  0.1449  216 LEU B CD2 
53   N N   . LYS A 31  ? 0.8648 1.0131 0.9244 -0.0495 0.0885  0.0930  217 LYS B N   
54   C CA  . LYS A 31  ? 0.9055 1.0376 0.9602 -0.0590 0.0987  0.0806  217 LYS B CA  
55   C C   . LYS A 31  ? 0.9341 1.0404 0.9731 -0.0628 0.1018  0.0771  217 LYS B C   
56   O O   . LYS A 31  ? 0.9354 1.0372 0.9814 -0.0572 0.0996  0.0847  217 LYS B O   
57   C CB  . LYS A 31  ? 0.8502 0.9928 0.9337 -0.0551 0.1083  0.0789  217 LYS B CB  
58   C CG  . LYS A 31  ? 0.9121 1.0800 1.0093 -0.0554 0.1053  0.0789  217 LYS B CG  
59   C CD  . LYS A 31  ? 0.9486 1.1341 1.0792 -0.0491 0.1132  0.0797  217 LYS B CD  
60   C CE  . LYS A 31  ? 1.1075 1.3191 1.2500 -0.0523 0.1079  0.0785  217 LYS B CE  
61   N NZ  . LYS A 31  ? 1.3013 1.5369 1.4794 -0.0459 0.1136  0.0803  217 LYS B NZ  
62   N N   . ASN A 32  ? 0.9709 1.0612 0.9892 -0.0726 0.1067  0.0662  218 ASN B N   
63   C CA  . ASN A 32  ? 0.8539 0.9206 0.8561 -0.0767 0.1094  0.0603  218 ASN B CA  
64   C C   . ASN A 32  ? 0.8865 0.9472 0.9075 -0.0731 0.1193  0.0551  218 ASN B C   
65   O O   . ASN A 32  ? 0.9890 1.0498 1.0120 -0.0753 0.1297  0.0463  218 ASN B O   
66   C CB  . ASN A 32  ? 0.9477 1.0013 0.9207 -0.0870 0.1116  0.0514  218 ASN B CB  
67   C CG  . ASN A 32  ? 1.0485 1.0797 0.9999 -0.0908 0.1111  0.0457  218 ASN B CG  
68   O OD1 . ASN A 32  ? 1.1134 1.1366 1.0745 -0.0876 0.1122  0.0439  218 ASN B OD1 
69   N ND2 . ASN A 32  ? 0.9905 1.0109 0.9133 -0.0978 0.1085  0.0428  218 ASN B ND2 
70   N N   . GLN A 33  ? 0.9051 0.9602 0.9407 -0.0674 0.1166  0.0605  219 GLN B N   
71   C CA  . GLN A 33  ? 0.9687 1.0154 1.0257 -0.0623 0.1244  0.0560  219 GLN B CA  
72   C C   . GLN A 33  ? 1.0471 1.0705 1.0972 -0.0654 0.1210  0.0515  219 GLN B C   
73   O O   . GLN A 33  ? 0.9959 1.0175 1.0647 -0.0613 0.1161  0.0613  219 GLN B O   
74   C CB  . GLN A 33  ? 0.9549 1.0189 1.0457 -0.0514 0.1240  0.0690  219 GLN B CB  
75   C CG  . GLN A 33  ? 0.9810 1.0698 1.0831 -0.0479 0.1264  0.0718  219 GLN B CG  
76   C CD  . GLN A 33  ? 1.0120 1.1181 1.1474 -0.0356 0.1256  0.0850  219 GLN B CD  
77   O OE1 . GLN A 33  ? 0.9511 1.0532 1.0978 -0.0300 0.1212  0.0965  219 GLN B OE1 
78   N NE2 . GLN A 33  ? 0.9173 1.0439 1.0700 -0.0312 0.1298  0.0848  219 GLN B NE2 
79   N N   . GLY A 34  ? 1.2915 1.2982 1.3153 -0.0729 0.1232  0.0375  220 GLY B N   
80   C CA  . GLY A 34  ? 1.2574 1.2427 1.2737 -0.0766 0.1185  0.0305  220 GLY B CA  
81   C C   . GLY A 34  ? 1.2500 1.2339 1.2471 -0.0824 0.1070  0.0366  220 GLY B C   
82   O O   . GLY A 34  ? 1.3536 1.3507 1.3400 -0.0830 0.1031  0.0451  220 GLY B O   
83   N N   . ALA A 35  ? 0.9358 0.9032 0.9295 -0.0863 0.1009  0.0312  221 ALA B N   
84   C CA  . ALA A 35  ? 1.0501 1.0166 1.0275 -0.0915 0.0897  0.0361  221 ALA B CA  
85   C C   . ALA A 35  ? 0.9726 0.9533 0.9741 -0.0874 0.0835  0.0552  221 ALA B C   
86   O O   . ALA A 35  ? 1.0402 1.0160 1.0559 -0.0894 0.0769  0.0598  221 ALA B O   
87   C CB  . ALA A 35  ? 1.1434 1.0895 1.1089 -0.0977 0.0843  0.0225  221 ALA B CB  
88   N N   . THR A 36  ? 0.8987 0.8987 0.9056 -0.0814 0.0857  0.0667  222 THR B N   
89   C CA  . THR A 36  ? 0.8468 0.8634 0.8715 -0.0757 0.0807  0.0856  222 THR B CA  
90   C C   . THR A 36  ? 0.9118 0.9353 0.9163 -0.0773 0.0726  0.0914  222 THR B C   
91   O O   . THR A 36  ? 0.8912 0.9279 0.9085 -0.0728 0.0686  0.1067  222 THR B O   
92   C CB  . THR A 36  ? 0.8812 0.9174 0.9202 -0.0669 0.0850  0.0956  222 THR B CB  
93   O OG1 . THR A 36  ? 1.0424 1.0862 1.0590 -0.0677 0.0855  0.0901  222 THR B OG1 
94   C CG2 . THR A 36  ? 0.8844 0.9155 0.9478 -0.0633 0.0930  0.0919  222 THR B CG2 
95   N N   . CYS A 37  ? 0.9229 0.9382 0.8968 -0.0826 0.0709  0.0806  223 CYS B N   
96   C CA  . CYS A 37  ? 0.8837 0.9024 0.8379 -0.0833 0.0631  0.0848  223 CYS B CA  
97   C C   . CYS A 37  ? 0.8537 0.8935 0.8116 -0.0746 0.0610  0.0987  223 CYS B C   
98   O O   . CYS A 37  ? 0.9945 1.0423 0.9476 -0.0711 0.0637  0.0981  223 CYS B O   
99   C CB  . CYS A 37  ? 0.9326 0.9455 0.8942 -0.0870 0.0562  0.0869  223 CYS B CB  
100  S SG  . CYS A 37  ? 0.9183 0.9066 0.8613 -0.0971 0.0537  0.0677  223 CYS B SG  
101  N N   . TYR A 38  ? 0.8558 0.9055 0.8222 -0.0710 0.0559  0.1108  224 TYR B N   
102  C CA  . TYR A 38  ? 0.8743 0.9452 0.8409 -0.0611 0.0539  0.1242  224 TYR B CA  
103  C C   . TYR A 38  ? 0.8775 0.9647 0.8663 -0.0531 0.0584  0.1353  224 TYR B C   
104  O O   . TYR A 38  ? 0.8772 0.9836 0.8632 -0.0435 0.0569  0.1454  224 TYR B O   
105  C CB  . TYR A 38  ? 0.8076 0.8864 0.7803 -0.0593 0.0491  0.1351  224 TYR B CB  
106  C CG  . TYR A 38  ? 0.8290 0.9004 0.8276 -0.0660 0.0491  0.1377  224 TYR B CG  
107  C CD1 . TYR A 38  ? 0.8096 0.8895 0.8397 -0.0628 0.0534  0.1507  224 TYR B CD1 
108  C CD2 . TYR A 38  ? 0.8229 0.8778 0.8147 -0.0756 0.0440  0.1270  224 TYR B CD2 
109  C CE1 . TYR A 38  ? 0.8172 0.8871 0.8735 -0.0698 0.0527  0.1525  224 TYR B CE1 
110  C CE2 . TYR A 38  ? 0.8306 0.8773 0.8469 -0.0825 0.0422  0.1270  224 TYR B CE2 
111  C CZ  . TYR A 38  ? 0.8301 0.8832 0.8798 -0.0801 0.0466  0.1395  224 TYR B CZ  
112  O OH  . TYR A 38  ? 0.8385 0.8804 0.9151 -0.0877 0.0443  0.1391  224 TYR B OH  
113  N N   . MET A 39  ? 0.8213 0.9015 0.8314 -0.0557 0.0635  0.1338  225 MET B N   
114  C CA  . MET A 39  ? 0.8007 0.8963 0.8355 -0.0471 0.0673  0.1474  225 MET B CA  
115  C C   . MET A 39  ? 0.7948 0.9072 0.8190 -0.0394 0.0669  0.1479  225 MET B C   
116  O O   . MET A 39  ? 0.7903 0.9238 0.8219 -0.0289 0.0661  0.1626  225 MET B O   
117  C CB  . MET A 39  ? 0.8083 0.8898 0.8660 -0.0507 0.0729  0.1426  225 MET B CB  
118  C CG  . MET A 39  ? 0.8059 0.9013 0.8899 -0.0413 0.0770  0.1567  225 MET B CG  
119  S SD  . MET A 39  ? 0.8187 0.8936 0.9305 -0.0443 0.0836  0.1497  225 MET B SD  
120  C CE  . MET A 39  ? 0.9592 1.0555 1.0988 -0.0303 0.0870  0.1702  225 MET B CE  
121  N N   . ASN A 40  ? 0.7970 0.9010 0.8039 -0.0445 0.0672  0.1323  226 ASN B N   
122  C CA  . ASN A 40  ? 0.7933 0.9127 0.7920 -0.0391 0.0650  0.1309  226 ASN B CA  
123  C C   . ASN A 40  ? 0.7912 0.9232 0.7709 -0.0322 0.0581  0.1363  226 ASN B C   
124  O O   . ASN A 40  ? 0.7892 0.9416 0.7696 -0.0223 0.0551  0.1432  226 ASN B O   
125  C CB  . ASN A 40  ? 0.8320 0.9392 0.8182 -0.0480 0.0671  0.1139  226 ASN B CB  
126  C CG  . ASN A 40  ? 0.8014 0.9016 0.8070 -0.0515 0.0753  0.1087  226 ASN B CG  
127  O OD1 . ASN A 40  ? 0.7996 0.9077 0.8301 -0.0452 0.0782  0.1178  226 ASN B OD1 
128  N ND2 . ASN A 40  ? 0.8391 0.9244 0.8332 -0.0606 0.0797  0.0946  226 ASN B ND2 
129  N N   . SER A 41  ? 0.8271 0.9479 0.7887 -0.0361 0.0552  0.1326  227 SER B N   
130  C CA  . SER A 41  ? 0.8100 0.9420 0.7535 -0.0278 0.0494  0.1368  227 SER B CA  
131  C C   . SER A 41  ? 0.7904 0.9453 0.7481 -0.0159 0.0503  0.1558  227 SER B C   
132  O O   . SER A 41  ? 0.7919 0.9654 0.7398 -0.0045 0.0470  0.1607  227 SER B O   
133  C CB  . SER A 41  ? 0.7987 0.9150 0.7242 -0.0331 0.0466  0.1313  227 SER B CB  
134  O OG  . SER A 41  ? 0.8155 0.9115 0.7238 -0.0429 0.0458  0.1159  227 SER B OG  
135  N N   . LEU A 42  ? 0.7881 0.9419 0.7690 -0.0181 0.0546  0.1669  228 LEU B N   
136  C CA  . LEU A 42  ? 0.7863 0.9619 0.7841 -0.0078 0.0570  0.1882  228 LEU B CA  
137  C C   . LEU A 42  ? 0.7862 0.9799 0.7940 0.0019  0.0585  0.1969  228 LEU B C   
138  O O   . LEU A 42  ? 0.7881 1.0055 0.7937 0.0148  0.0584  0.2114  228 LEU B O   
139  C CB  . LEU A 42  ? 0.7864 0.9537 0.8113 -0.0147 0.0609  0.1976  228 LEU B CB  
140  C CG  . LEU A 42  ? 0.7863 0.9751 0.8335 -0.0060 0.0647  0.2227  228 LEU B CG  
141  C CD1 . LEU A 42  ? 0.7861 0.9931 0.8171 0.0025  0.0631  0.2304  228 LEU B CD1 
142  C CD2 . LEU A 42  ? 0.7890 0.9653 0.8680 -0.0156 0.0676  0.2300  228 LEU B CD2 
143  N N   . LEU A 43  ? 0.7858 0.9703 0.8045 -0.0032 0.0603  0.1889  229 LEU B N   
144  C CA  . LEU A 43  ? 0.7864 0.9890 0.8185 0.0062  0.0611  0.1981  229 LEU B CA  
145  C C   . LEU A 43  ? 0.7887 1.0108 0.7981 0.0159  0.0543  0.1946  229 LEU B C   
146  O O   . LEU A 43  ? 0.7922 1.0385 0.8044 0.0291  0.0532  0.2092  229 LEU B O   
147  C CB  . LEU A 43  ? 0.7862 0.9754 0.8350 -0.0009 0.0645  0.1882  229 LEU B CB  
148  C CG  . LEU A 43  ? 0.7889 0.9628 0.8659 -0.0058 0.0710  0.1946  229 LEU B CG  
149  C CD1 . LEU A 43  ? 0.7914 0.9505 0.8803 -0.0119 0.0751  0.1809  229 LEU B CD1 
150  C CD2 . LEU A 43  ? 0.7915 0.9825 0.8918 0.0053  0.0736  0.2195  229 LEU B CD2 
151  N N   . GLN A 44  ? 0.7898 1.0013 0.7757 0.0098  0.0492  0.1756  230 GLN B N   
152  C CA  . GLN A 44  ? 0.7956 1.0224 0.7597 0.0182  0.0410  0.1696  230 GLN B CA  
153  C C   . GLN A 44  ? 0.8180 1.0606 0.7661 0.0310  0.0394  0.1804  230 GLN B C   
154  O O   . GLN A 44  ? 0.8719 1.1371 0.8094 0.0442  0.0346  0.1847  230 GLN B O   
155  C CB  . GLN A 44  ? 0.7984 1.0065 0.7436 0.0076  0.0363  0.1476  230 GLN B CB  
156  C CG  . GLN A 44  ? 0.8570 1.0520 0.8165 -0.0048 0.0394  0.1370  230 GLN B CG  
157  C CD  . GLN A 44  ? 0.7963 1.0104 0.7673 -0.0006 0.0355  0.1356  230 GLN B CD  
158  O OE1 . GLN A 44  ? 0.7922 1.0097 0.7873 -0.0021 0.0406  0.1395  230 GLN B OE1 
159  N NE2 . GLN A 44  ? 0.8039 1.0303 0.7581 0.0050  0.0256  0.1292  230 GLN B NE2 
160  N N   . THR A 45  ? 0.8384 1.0715 0.7849 0.0281  0.0432  0.1849  231 THR B N   
161  C CA  . THR A 45  ? 0.8037 1.0540 0.7380 0.0407  0.0436  0.1964  231 THR B CA  
162  C C   . THR A 45  ? 0.8061 1.0839 0.7555 0.0537  0.0481  0.2201  231 THR B C   
163  O O   . THR A 45  ? 0.8211 1.1223 0.7541 0.0692  0.0464  0.2272  231 THR B O   
164  C CB  . THR A 45  ? 0.7997 1.0370 0.7373 0.0339  0.0472  0.1989  231 THR B CB  
165  O OG1 . THR A 45  ? 0.8008 1.0136 0.7205 0.0238  0.0426  0.1786  231 THR B OG1 
166  C CG2 . THR A 45  ? 0.8050 1.0641 0.7343 0.0479  0.0493  0.2130  231 THR B CG2 
167  N N   . LEU A 46  ? 0.8128 1.0875 0.7929 0.0484  0.0543  0.2330  232 LEU B N   
168  C CA  . LEU A 46  ? 0.8048 1.1036 0.8019 0.0604  0.0591  0.2579  232 LEU B CA  
169  C C   . LEU A 46  ? 0.8426 1.1584 0.8329 0.0703  0.0537  0.2567  232 LEU B C   
170  O O   . LEU A 46  ? 0.8829 1.2260 0.8702 0.0859  0.0545  0.2745  232 LEU B O   
171  C CB  . LEU A 46  ? 0.8001 1.0865 0.8339 0.0514  0.0663  0.2709  232 LEU B CB  
172  C CG  . LEU A 46  ? 0.7961 1.0680 0.8415 0.0410  0.0703  0.2736  232 LEU B CG  
173  C CD1 . LEU A 46  ? 0.8181 1.0722 0.8993 0.0304  0.0750  0.2801  232 LEU B CD1 
174  C CD2 . LEU A 46  ? 0.8006 1.0966 0.8440 0.0516  0.0744  0.2941  232 LEU B CD2 
175  N N   . PHE A 47  ? 0.8525 1.1548 0.8411 0.0618  0.0481  0.2366  233 PHE B N   
176  C CA  . PHE A 47  ? 0.8398 1.1596 0.8252 0.0699  0.0413  0.2339  233 PHE B CA  
177  C C   . PHE A 47  ? 0.8493 1.1900 0.8022 0.0834  0.0329  0.2292  233 PHE B C   
178  O O   . PHE A 47  ? 0.8365 1.2038 0.7856 0.0978  0.0290  0.2397  233 PHE B O   
179  C CB  . PHE A 47  ? 0.8366 1.1386 0.8279 0.0564  0.0376  0.2123  233 PHE B CB  
180  C CG  . PHE A 47  ? 0.8248 1.1457 0.8128 0.0627  0.0283  0.2057  233 PHE B CG  
181  C CD1 . PHE A 47  ? 0.8494 1.1861 0.8614 0.0693  0.0292  0.2188  233 PHE B CD1 
182  C CD2 . PHE A 47  ? 0.8202 1.1425 0.7832 0.0618  0.0177  0.1861  233 PHE B CD2 
183  C CE1 . PHE A 47  ? 0.8408 1.1977 0.8518 0.0751  0.0193  0.2127  233 PHE B CE1 
184  C CE2 . PHE A 47  ? 0.8393 1.1799 0.8018 0.0663  0.0074  0.1790  233 PHE B CE2 
185  C CZ  . PHE A 47  ? 0.8675 1.2270 0.8541 0.0730  0.0079  0.1923  233 PHE B CZ  
186  N N   . PHE A 48  ? 0.8282 1.1568 0.7565 0.0801  0.0294  0.2132  234 PHE B N   
187  C CA  . PHE A 48  ? 0.8636 1.2082 0.7594 0.0935  0.0213  0.2057  234 PHE B CA  
188  C C   . PHE A 48  ? 0.8588 1.2220 0.7436 0.1085  0.0278  0.2240  234 PHE B C   
189  O O   . PHE A 48  ? 0.9200 1.2960 0.7752 0.1216  0.0226  0.2174  234 PHE B O   
190  C CB  . PHE A 48  ? 0.8463 1.1675 0.7213 0.0840  0.0140  0.1788  234 PHE B CB  
191  C CG  . PHE A 48  ? 0.8442 1.1543 0.7260 0.0720  0.0064  0.1608  234 PHE B CG  
192  C CD1 . PHE A 48  ? 0.8951 1.2255 0.7733 0.0794  -0.0037 0.1563  234 PHE B CD1 
193  C CD2 . PHE A 48  ? 0.8485 1.1303 0.7409 0.0536  0.0094  0.1493  234 PHE B CD2 
194  C CE1 . PHE A 48  ? 0.8526 1.1760 0.7416 0.0677  -0.0106 0.1406  234 PHE B CE1 
195  C CE2 . PHE A 48  ? 0.9248 1.1992 0.8258 0.0425  0.0041  0.1346  234 PHE B CE2 
196  C CZ  . PHE A 48  ? 0.8411 1.1368 0.7423 0.0491  -0.0058 0.1305  234 PHE B CZ  
197  N N   . THR A 49  ? 0.8671 1.2322 0.7762 0.1068  0.0391  0.2463  235 THR B N   
198  C CA  . THR A 49  ? 0.8756 1.2676 0.7829 0.1227  0.0469  0.2715  235 THR B CA  
199  C C   . THR A 49  ? 0.8621 1.2800 0.7747 0.1354  0.0457  0.2878  235 THR B C   
200  O O   . THR A 49  ? 0.8583 1.2811 0.8000 0.1347  0.0531  0.3104  235 THR B O   
201  C CB  . THR A 49  ? 0.9134 1.2971 0.8492 0.1141  0.0585  0.2896  235 THR B CB  
202  O OG1 . THR A 49  ? 0.9782 1.3357 0.9104 0.1005  0.0573  0.2719  235 THR B OG1 
203  C CG2 . THR A 49  ? 0.8515 1.2646 0.7852 0.1298  0.0676  0.3155  235 THR B CG2 
204  N N   . ASN A 50  ? 0.8905 1.3246 0.7741 0.1476  0.0351  0.2756  236 ASN B N   
205  C CA  . ASN A 50  ? 0.8872 1.3428 0.7738 0.1573  0.0291  0.2834  236 ASN B CA  
206  C C   . ASN A 50  ? 0.8953 1.3773 0.7954 0.1712  0.0393  0.3191  236 ASN B C   
207  O O   . ASN A 50  ? 0.8947 1.3835 0.8178 0.1723  0.0397  0.3337  236 ASN B O   
208  C CB  . ASN A 50  ? 0.9073 1.3789 0.7568 0.1698  0.0148  0.2642  236 ASN B CB  
209  C CG  . ASN A 50  ? 0.9279 1.3743 0.7706 0.1549  0.0030  0.2307  236 ASN B CG  
210  O OD1 . ASN A 50  ? 0.9218 1.3383 0.7759 0.1376  0.0069  0.2200  236 ASN B OD1 
211  N ND2 . ASN A 50  ? 0.9649 1.4237 0.7889 0.1613  -0.0119 0.2144  236 ASN B ND2 
212  N N   . GLN A 51  ? 0.9046 1.4023 0.7919 0.1825  0.0481  0.3348  237 GLN B N   
213  C CA  . GLN A 51  ? 0.9144 1.4378 0.8158 0.1952  0.0597  0.3718  237 GLN B CA  
214  C C   . GLN A 51  ? 0.8979 1.4024 0.8461 0.1801  0.0696  0.3902  237 GLN B C   
215  O O   . GLN A 51  ? 0.9047 1.4221 0.8744 0.1863  0.0749  0.4171  237 GLN B O   
216  C CB  . GLN A 51  ? 0.9268 1.4706 0.8077 0.2087  0.0689  0.3839  237 GLN B CB  
217  C CG  . GLN A 51  ? 0.9424 1.5184 0.8325 0.2245  0.0814  0.4237  237 GLN B CG  
218  C CD  . GLN A 51  ? 0.9603 1.5641 0.8223 0.2425  0.0896  0.4333  237 GLN B CD  
219  O OE1 . GLN A 51  ? 0.9602 1.5561 0.7988 0.2424  0.0864  0.4099  237 GLN B OE1 
220  N NE2 . GLN A 51  ? 0.9788 1.6158 0.8426 0.2591  0.1009  0.4686  237 GLN B NE2 
221  N N   . LEU A 52  ? 0.8790 1.3525 0.8430 0.1607  0.0719  0.3760  238 LEU B N   
222  C CA  . LEU A 52  ? 0.8660 1.3171 0.8727 0.1452  0.0787  0.3870  238 LEU B CA  
223  C C   . LEU A 52  ? 0.8629 1.3042 0.8854 0.1411  0.0725  0.3807  238 LEU B C   
224  O O   . LEU A 52  ? 0.8638 1.3015 0.9193 0.1395  0.0784  0.4008  238 LEU B O   
225  C CB  . LEU A 52  ? 0.8494 1.2697 0.8639 0.1260  0.0796  0.3686  238 LEU B CB  
226  C CG  . LEU A 52  ? 0.8373 1.2277 0.8900 0.1078  0.0828  0.3682  238 LEU B CG  
227  C CD1 . LEU A 52  ? 0.8435 1.2412 0.9313 0.1094  0.0937  0.4020  238 LEU B CD1 
228  C CD2 . LEU A 52  ? 0.8245 1.1873 0.8758 0.0908  0.0813  0.3466  238 LEU B CD2 
229  N N   . ARG A 53  ? 0.8608 1.2980 0.8622 0.1396  0.0607  0.3533  239 ARG B N   
230  C CA  . ARG A 53  ? 0.8614 1.2912 0.8795 0.1351  0.0548  0.3452  239 ARG B CA  
231  C C   . ARG A 53  ? 0.9083 1.3661 0.9353 0.1521  0.0546  0.3706  239 ARG B C   
232  O O   . ARG A 53  ? 0.9331 1.3837 0.9925 0.1496  0.0581  0.3826  239 ARG B O   
233  C CB  . ARG A 53  ? 0.8540 1.2783 0.8483 0.1302  0.0420  0.3124  239 ARG B CB  
234  C CG  . ARG A 53  ? 0.8541 1.2834 0.8620 0.1303  0.0344  0.3060  239 ARG B CG  
235  C CD  . ARG A 53  ? 0.8431 1.2508 0.8483 0.1143  0.0276  0.2745  239 ARG B CD  
236  N NE  . ARG A 53  ? 0.8487 1.2575 0.8186 0.1145  0.0184  0.2533  239 ARG B NE  
237  C CZ  . ARG A 53  ? 0.8575 1.2789 0.8113 0.1178  0.0050  0.2364  239 ARG B CZ  
238  N NH1 . ARG A 53  ? 0.8683 1.3061 0.8379 0.1216  -0.0015 0.2386  239 ARG B NH1 
239  N NH2 . ARG A 53  ? 0.8652 1.2822 0.7881 0.1173  -0.0029 0.2166  239 ARG B NH2 
240  N N   . LYS A 54  ? 0.8893 1.3792 0.8867 0.1706  0.0504  0.3790  240 LYS B N   
241  C CA  . LYS A 54  ? 0.9069 1.4263 0.9085 0.1886  0.0493  0.4043  240 LYS B CA  
242  C C   . LYS A 54  ? 0.9267 1.4465 0.9603 0.1912  0.0640  0.4411  240 LYS B C   
243  O O   . LYS A 54  ? 0.9328 1.4605 0.9891 0.1983  0.0650  0.4616  240 LYS B O   
244  C CB  . LYS A 54  ? 0.9289 1.4829 0.8876 0.2089  0.0420  0.4050  240 LYS B CB  
245  C CG  . LYS A 54  ? 0.9310 1.4868 0.8621 0.2080  0.0245  0.3702  240 LYS B CG  
246  C CD  . LYS A 54  ? 0.9560 1.5419 0.8410 0.2276  0.0168  0.3661  240 LYS B CD  
247  C CE  . LYS A 54  ? 0.9807 1.6047 0.8577 0.2499  0.0131  0.3908  240 LYS B CE  
248  N NZ  . LYS A 54  ? 1.0091 1.6627 0.8370 0.2701  0.0047  0.3838  240 LYS B NZ  
249  N N   . ALA A 55  ? 0.9067 1.4181 0.9451 0.1852  0.0751  0.4504  241 ALA B N   
250  C CA  . ALA A 55  ? 0.9105 1.4181 0.9852 0.1837  0.0888  0.4841  241 ALA B CA  
251  C C   . ALA A 55  ? 0.9932 1.4675 1.1093 0.1679  0.0902  0.4800  241 ALA B C   
252  O O   . ALA A 55  ? 1.0758 1.5495 1.2234 0.1717  0.0964  0.5067  241 ALA B O   
253  C CB  . ALA A 55  ? 0.9067 1.4120 0.9814 0.1779  0.0990  0.4912  241 ALA B CB  
254  N N   . VAL A 56  ? 0.9472 1.3930 1.0631 0.1510  0.0849  0.4469  242 VAL B N   
255  C CA  . VAL A 56  ? 0.9817 1.3958 1.1327 0.1370  0.0863  0.4388  242 VAL B CA  
256  C C   . VAL A 56  ? 0.9587 1.3818 1.1218 0.1468  0.0813  0.4436  242 VAL B C   
257  O O   . VAL A 56  ? 0.9534 1.3622 1.1525 0.1454  0.0865  0.4574  242 VAL B O   
258  C CB  . VAL A 56  ? 0.9437 1.3297 1.0851 0.1187  0.0818  0.4023  242 VAL B CB  
259  C CG1 . VAL A 56  ? 0.9096 1.2668 1.0807 0.1073  0.0825  0.3903  242 VAL B CG1 
260  C CG2 . VAL A 56  ? 0.8593 1.2337 0.9982 0.1085  0.0873  0.4015  242 VAL B CG2 
261  N N   . TYR A 57  ? 1.0112 1.4584 1.1460 0.1575  0.0704  0.4323  243 TYR B N   
262  C CA  . TYR A 57  ? 0.9562 1.4169 1.1027 0.1677  0.0638  0.4365  243 TYR B CA  
263  C C   . TYR A 57  ? 1.1087 1.5877 1.2740 0.1842  0.0698  0.4763  243 TYR B C   
264  O O   . TYR A 57  ? 1.0499 1.5266 1.2433 0.1890  0.0694  0.4861  243 TYR B O   
265  C CB  . TYR A 57  ? 0.8928 1.3796 1.0044 0.1761  0.0493  0.4179  243 TYR B CB  
266  C CG  . TYR A 57  ? 0.8762 1.3448 0.9785 0.1603  0.0419  0.3800  243 TYR B CG  
267  C CD1 . TYR A 57  ? 0.8614 1.2979 0.9906 0.1437  0.0471  0.3659  243 TYR B CD1 
268  C CD2 . TYR A 57  ? 0.8781 1.3611 0.9448 0.1623  0.0299  0.3583  243 TYR B CD2 
269  C CE1 . TYR A 57  ? 0.8483 1.2695 0.9689 0.1294  0.0418  0.3337  243 TYR B CE1 
270  C CE2 . TYR A 57  ? 0.8651 1.3306 0.9256 0.1470  0.0237  0.3258  243 TYR B CE2 
271  C CZ  . TYR A 57  ? 0.8498 1.2854 0.9373 0.1306  0.0303  0.3148  243 TYR B CZ  
272  O OH  . TYR A 57  ? 0.8390 1.2587 0.9199 0.1158  0.0255  0.2851  243 TYR B OH  
273  N N   . MET A 58  ? 1.0553 1.5532 1.2065 0.1939  0.0759  0.5008  244 MET B N   
274  C CA  . MET A 58  ? 1.1072 1.6271 1.2715 0.2114  0.0818  0.5415  244 MET B CA  
275  C C   . MET A 58  ? 1.0622 1.5591 1.2668 0.2035  0.0965  0.5677  244 MET B C   
276  O O   . MET A 58  ? 1.0102 1.5243 1.2246 0.2160  0.1045  0.6056  244 MET B O   
277  C CB  . MET A 58  ? 1.0898 1.6492 1.2135 0.2297  0.0803  0.5557  244 MET B CB  
278  C CG  . MET A 58  ? 1.1035 1.6877 1.1892 0.2401  0.0636  0.5323  244 MET B CG  
279  S SD  . MET A 58  ? 1.4841 2.1167 1.5217 0.2660  0.0616  0.5515  244 MET B SD  
280  C CE  . MET A 58  ? 1.2281 1.8492 1.2510 0.2558  0.0735  0.5454  244 MET B CE  
281  N N   . MET A 59  ? 1.0630 1.5215 1.2911 0.1827  0.0998  0.5483  245 MET B N   
282  C CA  . MET A 59  ? 1.1109 1.5446 1.3799 0.1734  0.1116  0.5695  245 MET B CA  
283  C C   . MET A 59  ? 1.0687 1.4913 1.3752 0.1798  0.1133  0.5871  245 MET B C   
284  O O   . MET A 59  ? 1.0768 1.4964 1.3843 0.1827  0.1054  0.5693  245 MET B O   
285  C CB  . MET A 59  ? 1.0740 1.4704 1.3538 0.1500  0.1128  0.5410  245 MET B CB  
286  C CG  . MET A 59  ? 1.0079 1.4107 1.2567 0.1427  0.1120  0.5250  245 MET B CG  
287  S SD  . MET A 59  ? 1.0909 1.4492 1.3567 0.1161  0.1128  0.4954  245 MET B SD  
288  C CE  . MET A 59  ? 0.9493 1.2871 1.2145 0.1114  0.1044  0.4616  245 MET B CE  
289  N N   . PRO A 60  ? 1.0891 1.5046 1.4293 0.1818  0.1236  0.6223  246 PRO B N   
290  C CA  . PRO A 60  ? 1.1448 1.5460 1.5238 0.1887  0.1257  0.6410  246 PRO B CA  
291  C C   . PRO A 60  ? 1.2082 1.5627 1.6205 0.1713  0.1265  0.6167  246 PRO B C   
292  O O   . PRO A 60  ? 1.2361 1.5610 1.6866 0.1620  0.1343  0.6302  246 PRO B O   
293  C CB  . PRO A 60  ? 1.1142 1.5245 1.5151 0.1957  0.1373  0.6883  246 PRO B CB  
294  C CG  . PRO A 60  ? 1.1469 1.5514 1.5427 0.1798  0.1433  0.6836  246 PRO B CG  
295  C CD  . PRO A 60  ? 1.1154 1.5359 1.4629 0.1777  0.1343  0.6480  246 PRO B CD  
296  N N   . THR A 61  ? 1.2250 1.5718 1.6234 0.1667  0.1183  0.5796  247 THR B N   
297  C CA  . THR A 61  ? 1.2869 1.5920 1.7107 0.1518  0.1193  0.5531  247 THR B CA  
298  C C   . THR A 61  ? 1.4020 1.6988 1.8528 0.1627  0.1182  0.5546  247 THR B C   
299  O O   . THR A 61  ? 1.4172 1.6833 1.8845 0.1535  0.1187  0.5290  247 THR B O   
300  C CB  . THR A 61  ? 1.1542 1.4525 1.5478 0.1377  0.1134  0.5106  247 THR B CB  
301  O OG1 . THR A 61  ? 1.1111 1.4409 1.4734 0.1481  0.1043  0.4987  247 THR B OG1 
302  C CG2 . THR A 61  ? 1.1101 1.4081 1.4846 0.1252  0.1153  0.5073  247 THR B CG2 
303  N N   . GLU A 62  ? 1.6124 1.9370 2.0670 0.1832  0.1166  0.5837  248 GLU B N   
304  C CA  . GLU A 62  ? 1.6838 2.0010 2.1685 0.1951  0.1158  0.5884  248 GLU B CA  
305  C C   . GLU A 62  ? 1.5188 1.7931 2.0505 0.1895  0.1252  0.6009  248 GLU B C   
306  O O   . GLU A 62  ? 1.5759 1.8424 2.1231 0.1869  0.1320  0.6294  248 GLU B O   
307  C CB  . GLU A 62  ? 1.7676 2.1253 2.2465 0.2194  0.1112  0.6199  248 GLU B CB  
308  C CG  . GLU A 62  ? 1.8967 2.2983 2.3299 0.2271  0.0997  0.6076  248 GLU B CG  
309  C CD  . GLU A 62  ? 1.8271 2.2519 2.2245 0.2266  0.1003  0.6191  248 GLU B CD  
310  O OE1 . GLU A 62  ? 1.6790 2.0859 2.0865 0.2169  0.1101  0.6328  248 GLU B OE1 
311  O OE2 . GLU A 62  ? 1.8622 2.3243 2.2225 0.2365  0.0906  0.6145  248 GLU B OE2 
312  N N   . GLY A 63  ? 1.3012 1.5476 1.8567 0.1876  0.1257  0.5792  249 GLY B N   
313  C CA  . GLY A 63  ? 1.2325 1.4335 1.8318 0.1819  0.1333  0.5844  249 GLY B CA  
314  C C   . GLY A 63  ? 1.0291 1.1936 1.6303 0.1581  0.1364  0.5603  249 GLY B C   
315  O O   . GLY A 63  ? 1.0493 1.1805 1.6843 0.1511  0.1420  0.5730  249 GLY B O   
316  N N   . ASP A 64  ? 1.0055 1.1750 1.5724 0.1454  0.1322  0.5263  250 ASP B N   
317  C CA  . ASP A 64  ? 1.0639 1.2009 1.6289 0.1235  0.1335  0.5003  250 ASP B CA  
318  C C   . ASP A 64  ? 1.0711 1.1812 1.6393 0.1183  0.1333  0.4617  250 ASP B C   
319  O O   . ASP A 64  ? 1.2108 1.3360 1.7732 0.1295  0.1316  0.4509  250 ASP B O   
320  C CB  . ASP A 64  ? 1.1649 1.3243 1.6885 0.1128  0.1296  0.4901  250 ASP B CB  
321  C CG  . ASP A 64  ? 1.1895 1.3745 1.7093 0.1171  0.1317  0.5265  250 ASP B CG  
322  O OD1 . ASP A 64  ? 1.2413 1.4371 1.7824 0.1316  0.1351  0.5618  250 ASP B OD1 
323  O OD2 . ASP A 64  ? 1.0674 1.2627 1.5625 0.1068  0.1304  0.5206  250 ASP B OD2 
324  N N   . ASP A 65  ? 1.0595 1.1315 1.6369 0.1015  0.1350  0.4408  251 ASP B N   
325  C CA  . ASP A 65  ? 1.1171 1.1619 1.6956 0.0968  0.1361  0.4036  251 ASP B CA  
326  C C   . ASP A 65  ? 1.1646 1.2241 1.6995 0.0867  0.1322  0.3727  251 ASP B C   
327  O O   . ASP A 65  ? 1.1880 1.2473 1.7020 0.0723  0.1292  0.3665  251 ASP B O   
328  C CB  . ASP A 65  ? 1.0973 1.0935 1.7036 0.0842  0.1384  0.3931  251 ASP B CB  
329  C CG  . ASP A 65  ? 1.1885 1.1580 1.7849 0.0770  0.1392  0.3504  251 ASP B CG  
330  O OD1 . ASP A 65  ? 1.2030 1.1698 1.8080 0.0894  0.1429  0.3392  251 ASP B OD1 
331  O OD2 . ASP A 65  ? 1.2625 1.2157 1.8422 0.0596  0.1363  0.3287  251 ASP B OD2 
332  N N   . SER A 66  ? 1.1880 1.2609 1.7115 0.0943  0.1323  0.3546  252 SER B N   
333  C CA  . SER A 66  ? 1.1122 1.2013 1.5963 0.0857  0.1289  0.3284  252 SER B CA  
334  C C   . SER A 66  ? 1.2329 1.2903 1.7039 0.0674  0.1297  0.2991  252 SER B C   
335  O O   . SER A 66  ? 1.3379 1.4040 1.7760 0.0560  0.1258  0.2866  252 SER B O   
336  C CB  . SER A 66  ? 1.1882 1.2953 1.6705 0.0963  0.1299  0.3151  252 SER B CB  
337  O OG  . SER A 66  ? 1.1459 1.2590 1.5955 0.0853  0.1285  0.2864  252 SER B OG  
338  N N   . SER A 67  ? 1.2073 1.2271 1.7032 0.0650  0.1341  0.2876  253 SER B N   
339  C CA  . SER A 67  ? 1.2495 1.2394 1.7313 0.0493  0.1341  0.2566  253 SER B CA  
340  C C   . SER A 67  ? 1.2663 1.2469 1.7406 0.0337  0.1287  0.2618  253 SER B C   
341  O O   . SER A 67  ? 1.3160 1.2806 1.7695 0.0199  0.1262  0.2369  253 SER B O   
342  C CB  . SER A 67  ? 1.2199 1.1715 1.7304 0.0528  0.1395  0.2418  253 SER B CB  
343  O OG  . SER A 67  ? 1.1957 1.1233 1.7413 0.0522  0.1388  0.2614  253 SER B OG  
344  N N   . LYS A 68  ? 1.1921 1.1838 1.6834 0.0359  0.1271  0.2942  254 LYS B N   
345  C CA  . LYS A 68  ? 1.1978 1.1814 1.6897 0.0214  0.1230  0.3012  254 LYS B CA  
346  C C   . LYS A 68  ? 1.2189 1.2387 1.6984 0.0237  0.1210  0.3294  254 LYS B C   
347  O O   . LYS A 68  ? 1.1882 1.2057 1.6727 0.0130  0.1187  0.3393  254 LYS B O   
348  C CB  . LYS A 68  ? 1.2331 1.1820 1.7694 0.0178  0.1242  0.3117  254 LYS B CB  
349  C CG  . LYS A 68  ? 1.1802 1.0883 1.7274 0.0142  0.1252  0.2803  254 LYS B CG  
350  C CD  . LYS A 68  ? 1.2047 1.0761 1.7976 0.0103  0.1251  0.2904  254 LYS B CD  
351  C CE  . LYS A 68  ? 1.1086 0.9382 1.7095 0.0083  0.1256  0.2559  254 LYS B CE  
352  N NZ  . LYS A 68  ? 1.1250 0.9147 1.7717 0.0036  0.1240  0.2630  254 LYS B NZ  
353  N N   . SER A 69  ? 1.2125 1.2667 1.6765 0.0376  0.1215  0.3419  255 SER B N   
354  C CA  . SER A 69  ? 1.1479 1.2375 1.5995 0.0432  0.1202  0.3694  255 SER B CA  
355  C C   . SER A 69  ? 1.0776 1.1880 1.4847 0.0377  0.1153  0.3522  255 SER B C   
356  O O   . SER A 69  ? 1.1142 1.2382 1.4980 0.0426  0.1132  0.3361  255 SER B O   
357  C CB  . SER A 69  ? 1.1355 1.2511 1.5960 0.0631  0.1221  0.3945  255 SER B CB  
358  O OG  . SER A 69  ? 1.0325 1.1831 1.4776 0.0701  0.1209  0.4204  255 SER B OG  
359  N N   . VAL A 70  ? 1.0397 1.1524 1.4376 0.0274  0.1133  0.3561  256 VAL B N   
360  C CA  . VAL A 70  ? 1.0426 1.1755 1.4002 0.0239  0.1088  0.3445  256 VAL B CA  
361  C C   . VAL A 70  ? 1.0576 1.2299 1.3956 0.0393  0.1079  0.3627  256 VAL B C   
362  O O   . VAL A 70  ? 1.1037 1.2903 1.4095 0.0414  0.1036  0.3457  256 VAL B O   
363  C CB  . VAL A 70  ? 0.9720 1.0992 1.3293 0.0107  0.1072  0.3464  256 VAL B CB  
364  C CG1 . VAL A 70  ? 1.0109 1.1576 1.3269 0.0089  0.1027  0.3343  256 VAL B CG1 
365  C CG2 . VAL A 70  ? 0.9573 1.0461 1.3308 -0.0047 0.1056  0.3250  256 VAL B CG2 
366  N N   . PRO A 71  ? 0.9819 1.1730 1.3368 0.0504  0.1115  0.3967  257 PRO B N   
367  C CA  . PRO A 71  ? 0.9309 1.1605 1.2628 0.0668  0.1095  0.4114  257 PRO B CA  
368  C C   . PRO A 71  ? 1.0050 1.2427 1.3295 0.0763  0.1057  0.3990  257 PRO B C   
369  O O   . PRO A 71  ? 0.9911 1.2540 1.2846 0.0829  0.1000  0.3914  257 PRO B O   
370  C CB  . PRO A 71  ? 1.0078 1.2509 1.3654 0.0770  0.1156  0.4517  257 PRO B CB  
371  C CG  . PRO A 71  ? 1.0155 1.2338 1.4001 0.0621  0.1197  0.4569  257 PRO B CG  
372  C CD  . PRO A 71  ? 1.0165 1.1973 1.4091 0.0482  0.1171  0.4241  257 PRO B CD  
373  N N   . LEU A 72  ? 1.0287 1.2458 1.3822 0.0773  0.1085  0.3959  258 LEU B N   
374  C CA  . LEU A 72  ? 0.9139 1.1403 1.2640 0.0858  0.1054  0.3832  258 LEU B CA  
375  C C   . LEU A 72  ? 0.8854 1.1056 1.2082 0.0747  0.1014  0.3476  258 LEU B C   
376  O O   . LEU A 72  ? 0.8643 1.1066 1.1683 0.0802  0.0960  0.3379  258 LEU B O   
377  C CB  . LEU A 72  ? 0.9597 1.1640 1.3487 0.0901  0.1104  0.3871  258 LEU B CB  
378  C CG  . LEU A 72  ? 1.0171 1.2340 1.4082 0.1001  0.1081  0.3757  258 LEU B CG  
379  C CD1 . LEU A 72  ? 1.0061 1.2642 1.3871 0.1172  0.1023  0.3972  258 LEU B CD1 
380  C CD2 . LEU A 72  ? 1.0850 1.2760 1.5146 0.1043  0.1142  0.3753  258 LEU B CD2 
381  N N   . ALA A 73  ? 0.8784 1.0691 1.1997 0.0588  0.1036  0.3284  259 ALA B N   
382  C CA  . ALA A 73  ? 0.8944 1.0775 1.1895 0.0480  0.1010  0.2966  259 ALA B CA  
383  C C   . ALA A 73  ? 0.9215 1.1288 1.1798 0.0480  0.0944  0.2934  259 ALA B C   
384  O O   . ALA A 73  ? 0.9464 1.1633 1.1847 0.0471  0.0904  0.2757  259 ALA B O   
385  C CB  . ALA A 73  ? 0.8499 0.9982 1.1482 0.0322  0.1037  0.2794  259 ALA B CB  
386  N N   . LEU A 74  ? 0.8756 1.0932 1.1260 0.0493  0.0936  0.3106  260 LEU B N   
387  C CA  . LEU A 74  ? 0.8733 1.1135 1.0885 0.0517  0.0877  0.3078  260 LEU B CA  
388  C C   . LEU A 74  ? 0.8962 1.1682 1.1013 0.0668  0.0824  0.3153  260 LEU B C   
389  O O   . LEU A 74  ? 0.8868 1.1720 1.0632 0.0671  0.0755  0.3005  260 LEU B O   
390  C CB  . LEU A 74  ? 0.9042 1.1514 1.1161 0.0521  0.0896  0.3265  260 LEU B CB  
391  C CG  . LEU A 74  ? 0.8163 1.0820 0.9904 0.0542  0.0843  0.3198  260 LEU B CG  
392  C CD1 . LEU A 74  ? 0.8606 1.1054 1.0145 0.0398  0.0809  0.2901  260 LEU B CD1 
393  C CD2 . LEU A 74  ? 0.8204 1.1009 0.9941 0.0589  0.0878  0.3427  260 LEU B CD2 
394  N N   . GLN A 75  ? 0.9276 1.2120 1.1563 0.0796  0.0847  0.3385  261 GLN B N   
395  C CA  . GLN A 75  ? 0.8501 1.1653 1.0715 0.0944  0.0782  0.3447  261 GLN B CA  
396  C C   . GLN A 75  ? 0.8300 1.1425 1.0507 0.0898  0.0739  0.3192  261 GLN B C   
397  O O   . GLN A 75  ? 0.8268 1.1614 1.0270 0.0938  0.0650  0.3095  261 GLN B O   
398  C CB  . GLN A 75  ? 0.8523 1.1781 1.1028 0.1088  0.0820  0.3753  261 GLN B CB  
399  C CG  . GLN A 75  ? 0.8811 1.2206 1.1301 0.1168  0.0858  0.4056  261 GLN B CG  
400  C CD  . GLN A 75  ? 0.9750 1.3151 1.2591 0.1277  0.0919  0.4370  261 GLN B CD  
401  O OE1 . GLN A 75  ? 0.9196 1.2342 1.2356 0.1233  0.0962  0.4344  261 GLN B OE1 
402  N NE2 . GLN A 75  ? 1.0270 1.3955 1.3049 0.1428  0.0926  0.4673  261 GLN B NE2 
403  N N   . ARG A 76  ? 0.8294 1.1153 1.0733 0.0813  0.0802  0.3077  262 ARG B N   
404  C CA  . ARG A 76  ? 0.8240 1.1089 1.0708 0.0773  0.0786  0.2854  262 ARG B CA  
405  C C   . ARG A 76  ? 0.8259 1.1096 1.0407 0.0654  0.0735  0.2608  262 ARG B C   
406  O O   . ARG A 76  ? 0.9048 1.2064 1.1109 0.0664  0.0668  0.2494  262 ARG B O   
407  C CB  . ARG A 76  ? 0.8287 1.0835 1.1031 0.0712  0.0880  0.2769  262 ARG B CB  
408  C CG  . ARG A 76  ? 0.8259 1.0837 1.1092 0.0700  0.0890  0.2581  262 ARG B CG  
409  C CD  . ARG A 76  ? 0.8341 1.0611 1.1409 0.0654  0.0993  0.2479  262 ARG B CD  
410  N NE  . ARG A 76  ? 0.8489 1.0662 1.1866 0.0756  0.1038  0.2691  262 ARG B NE  
411  C CZ  . ARG A 76  ? 0.8574 1.0481 1.2030 0.0703  0.1079  0.2757  262 ARG B CZ  
412  N NH1 . ARG A 76  ? 0.8898 1.0626 1.2141 0.0557  0.1077  0.2627  262 ARG B NH1 
413  N NH2 . ARG A 76  ? 0.9443 1.1260 1.3216 0.0797  0.1117  0.2961  262 ARG B NH2 
414  N N   . VAL A 77  ? 0.8086 1.0711 1.0071 0.0538  0.0761  0.2529  263 VAL B N   
415  C CA  . VAL A 77  ? 0.8132 1.0705 0.9824 0.0425  0.0719  0.2304  263 VAL B CA  
416  C C   . VAL A 77  ? 0.8124 1.0959 0.9551 0.0495  0.0618  0.2329  263 VAL B C   
417  O O   . VAL A 77  ? 0.8294 1.1186 0.9553 0.0448  0.0554  0.2156  263 VAL B O   
418  C CB  . VAL A 77  ? 0.7983 1.0270 0.9576 0.0296  0.0764  0.2223  263 VAL B CB  
419  C CG1 . VAL A 77  ? 0.8438 1.0761 1.0021 0.0342  0.0768  0.2423  263 VAL B CG1 
420  C CG2 . VAL A 77  ? 0.7922 1.0140 0.9213 0.0188  0.0723  0.2007  263 VAL B CG2 
421  N N   . PHE A 78  ? 0.8412 1.1410 0.9800 0.0611  0.0603  0.2544  264 PHE B N   
422  C CA  . PHE A 78  ? 0.8506 1.1770 0.9625 0.0707  0.0507  0.2563  264 PHE B CA  
423  C C   . PHE A 78  ? 0.8458 1.1966 0.9625 0.0787  0.0422  0.2531  264 PHE B C   
424  O O   . PHE A 78  ? 0.8773 1.2398 0.9723 0.0779  0.0321  0.2380  264 PHE B O   
425  C CB  . PHE A 78  ? 0.8856 1.2279 0.9935 0.0836  0.0528  0.2824  264 PHE B CB  
426  C CG  . PHE A 78  ? 0.8604 1.1895 0.9538 0.0774  0.0570  0.2829  264 PHE B CG  
427  C CD1 . PHE A 78  ? 0.8721 1.1783 0.9512 0.0628  0.0563  0.2600  264 PHE B CD1 
428  C CD2 . PHE A 78  ? 0.8373 1.1794 0.9317 0.0869  0.0617  0.3077  264 PHE B CD2 
429  C CE1 . PHE A 78  ? 0.8475 1.1438 0.9147 0.0582  0.0593  0.2610  264 PHE B CE1 
430  C CE2 . PHE A 78  ? 0.8345 1.1681 0.9188 0.0816  0.0656  0.3088  264 PHE B CE2 
431  C CZ  . PHE A 78  ? 0.8254 1.1363 0.8963 0.0675  0.0637  0.2850  264 PHE B CZ  
432  N N   . TYR A 79  ? 0.8161 1.1746 0.9627 0.0864  0.0453  0.2670  265 TYR B N   
433  C CA  . TYR A 79  ? 0.8199 1.2044 0.9750 0.0945  0.0365  0.2649  265 TYR B CA  
434  C C   . TYR A 79  ? 0.8115 1.1885 0.9670 0.0807  0.0336  0.2377  265 TYR B C   
435  O O   . TYR A 79  ? 0.8285 1.2256 0.9733 0.0817  0.0219  0.2267  265 TYR B O   
436  C CB  . TYR A 79  ? 0.8263 1.2172 1.0168 0.1054  0.0417  0.2850  265 TYR B CB  
437  C CG  . TYR A 79  ? 0.8434 1.2645 1.0461 0.1152  0.0320  0.2850  265 TYR B CG  
438  C CD1 . TYR A 79  ? 0.8245 1.2429 1.0483 0.1078  0.0328  0.2682  265 TYR B CD1 
439  C CD2 . TYR A 79  ? 0.8436 1.2984 1.0367 0.1324  0.0219  0.3019  265 TYR B CD2 
440  C CE1 . TYR A 79  ? 0.8287 1.2775 1.0672 0.1164  0.0232  0.2684  265 TYR B CE1 
441  C CE2 . TYR A 79  ? 0.8492 1.3338 1.0541 0.1415  0.0110  0.3014  265 TYR B CE2 
442  C CZ  . TYR A 79  ? 0.8408 1.3226 1.0702 0.1330  0.0115  0.2847  265 TYR B CZ  
443  O OH  . TYR A 79  ? 0.9213 1.4355 1.1664 0.1416  0.0002  0.2845  265 TYR B OH  
444  N N   . GLU A 80  ? 0.8043 1.1525 0.9723 0.0677  0.0439  0.2267  266 GLU B N   
445  C CA  . GLU A 80  ? 0.7980 1.1389 0.9661 0.0542  0.0436  0.2030  266 GLU B CA  
446  C C   . GLU A 80  ? 0.7965 1.1344 0.9307 0.0454  0.0355  0.1873  266 GLU B C   
447  O O   . GLU A 80  ? 0.8565 1.2028 0.9875 0.0388  0.0286  0.1717  266 GLU B O   
448  C CB  . GLU A 80  ? 0.7945 1.1045 0.9770 0.0435  0.0572  0.1950  266 GLU B CB  
449  C CG  . GLU A 80  ? 0.7993 1.1078 1.0169 0.0521  0.0655  0.2070  266 GLU B CG  
450  C CD  . GLU A 80  ? 0.8961 1.2279 1.1379 0.0575  0.0633  0.2041  266 GLU B CD  
451  O OE1 . GLU A 80  ? 0.8151 1.1578 1.0495 0.0496  0.0580  0.1884  266 GLU B OE1 
452  O OE2 . GLU A 80  ? 0.8741 1.2134 1.1445 0.0697  0.0667  0.2182  266 GLU B OE2 
453  N N   . LEU A 81  ? 0.7972 1.1234 0.9079 0.0455  0.0362  0.1916  267 LEU B N   
454  C CA  . LEU A 81  ? 0.8007 1.1226 0.8792 0.0394  0.0286  0.1773  267 LEU B CA  
455  C C   . LEU A 81  ? 0.8077 1.1585 0.8710 0.0500  0.0142  0.1770  267 LEU B C   
456  O O   . LEU A 81  ? 0.8120 1.1600 0.8517 0.0448  0.0058  0.1612  267 LEU B O   
457  C CB  . LEU A 81  ? 0.8355 1.1401 0.8953 0.0385  0.0334  0.1829  267 LEU B CB  
458  C CG  . LEU A 81  ? 0.7913 1.0636 0.8536 0.0243  0.0434  0.1748  267 LEU B CG  
459  C CD1 . LEU A 81  ? 0.7985 1.0607 0.8457 0.0255  0.0459  0.1830  267 LEU B CD1 
460  C CD2 . LEU A 81  ? 0.7900 1.0480 0.8403 0.0102  0.0414  0.1525  267 LEU B CD2 
461  N N   . GLN A 82  ? 0.8137 1.1914 0.8893 0.0652  0.0105  0.1937  268 GLN B N   
462  C CA  . GLN A 82  ? 0.8280 1.2354 0.8868 0.0770  -0.0045 0.1933  268 GLN B CA  
463  C C   . GLN A 82  ? 0.8285 1.2566 0.9056 0.0759  -0.0146 0.1839  268 GLN B C   
464  O O   . GLN A 82  ? 0.8462 1.2909 0.9070 0.0777  -0.0296 0.1718  268 GLN B O   
465  C CB  . GLN A 82  ? 0.8359 1.2648 0.8916 0.0966  -0.0040 0.2194  268 GLN B CB  
466  C CG  . GLN A 82  ? 0.8533 1.3147 0.8858 0.1115  -0.0195 0.2198  268 GLN B CG  
467  C CD  . GLN A 82  ? 0.9325 1.4117 0.9516 0.1304  -0.0165 0.2454  268 GLN B CD  
468  O OE1 . GLN A 82  ? 0.8606 1.3246 0.8801 0.1298  -0.0037 0.2590  268 GLN B OE1 
469  N NE2 . GLN A 82  ? 0.9257 1.4388 0.9335 0.1472  -0.0283 0.2529  268 GLN B NE2 
470  N N   . HIS A 83  ? 0.8207 1.2486 0.9325 0.0729  -0.0072 0.1881  269 HIS B N   
471  C CA  . HIS A 83  ? 0.8226 1.2753 0.9582 0.0738  -0.0158 0.1828  269 HIS B CA  
472  C C   . HIS A 83  ? 0.8132 1.2523 0.9678 0.0557  -0.0106 0.1644  269 HIS B C   
473  O O   . HIS A 83  ? 0.8161 1.2736 0.9803 0.0507  -0.0213 0.1522  269 HIS B O   
474  C CB  . HIS A 83  ? 0.8251 1.2966 0.9894 0.0893  -0.0122 0.2054  269 HIS B CB  
475  C CG  . HIS A 83  ? 0.8382 1.3304 0.9866 0.1086  -0.0184 0.2264  269 HIS B CG  
476  N ND1 . HIS A 83  ? 0.8721 1.3499 1.0008 0.1131  -0.0106 0.2395  269 HIS B ND1 
477  C CD2 . HIS A 83  ? 0.8519 1.3801 1.0008 0.1250  -0.0314 0.2374  269 HIS B CD2 
478  C CE1 . HIS A 83  ? 0.8985 1.4025 1.0160 0.1316  -0.0170 0.2587  269 HIS B CE1 
479  N NE2 . HIS A 83  ? 0.8627 1.3972 0.9905 0.1396  -0.0300 0.2577  269 HIS B NE2 
480  N N   . SER A 84  ? 0.8038 1.2129 0.9650 0.0458  0.0055  0.1624  270 SER B N   
481  C CA  . SER A 84  ? 0.8403 1.2388 1.0200 0.0308  0.0131  0.1478  270 SER B CA  
482  C C   . SER A 84  ? 0.8748 1.2652 1.0350 0.0153  0.0059  0.1278  270 SER B C   
483  O O   . SER A 84  ? 0.8536 1.2282 0.9820 0.0127  0.0021  0.1232  270 SER B O   
484  C CB  . SER A 84  ? 0.8643 1.2317 1.0500 0.0254  0.0313  0.1495  270 SER B CB  
485  O OG  . SER A 84  ? 0.8878 1.2444 1.0849 0.0111  0.0398  0.1347  270 SER B OG  
486  N N   . ASP A 85  ? 1.0121 1.4134 1.1936 0.0052  0.0046  0.1166  271 ASP B N   
487  C CA  . ASP A 85  ? 1.0710 1.4612 1.2402 -0.0119 0.0000  0.0986  271 ASP B CA  
488  C C   . ASP A 85  ? 1.1066 1.4668 1.2753 -0.0267 0.0169  0.0917  271 ASP B C   
489  O O   . ASP A 85  ? 1.1835 1.5300 1.3408 -0.0415 0.0154  0.0790  271 ASP B O   
490  C CB  . ASP A 85  ? 1.1168 1.5372 1.3108 -0.0166 -0.0121 0.0906  271 ASP B CB  
491  C CG  . ASP A 85  ? 1.3014 1.7554 1.4973 -0.0007 -0.0300 0.0974  271 ASP B CG  
492  O OD1 . ASP A 85  ? 1.4226 1.8978 1.6421 0.0126  -0.0275 0.1114  271 ASP B OD1 
493  O OD2 . ASP A 85  ? 1.3221 1.7806 1.4946 -0.0004 -0.0466 0.0887  271 ASP B OD2 
494  N N   . LYS A 86  ? 0.8794 1.2285 1.0593 -0.0227 0.0326  0.0995  272 LYS B N   
495  C CA  . LYS A 86  ? 0.9074 1.2278 1.0820 -0.0342 0.0486  0.0931  272 LYS B CA  
496  C C   . LYS A 86  ? 0.8656 1.1594 1.0171 -0.0298 0.0543  0.0991  272 LYS B C   
497  O O   . LYS A 86  ? 0.8973 1.1977 1.0491 -0.0164 0.0508  0.1117  272 LYS B O   
498  C CB  . LYS A 86  ? 0.8431 1.1712 1.0508 -0.0344 0.0629  0.0934  272 LYS B CB  
499  C CG  . LYS A 86  ? 0.7904 1.1394 1.0204 -0.0448 0.0615  0.0851  272 LYS B CG  
500  C CD  . LYS A 86  ? 0.7900 1.1491 1.0532 -0.0435 0.0776  0.0855  272 LYS B CD  
501  C CE  . LYS A 86  ? 0.8323 1.2142 1.1238 -0.0252 0.0764  0.0973  272 LYS B CE  
502  N NZ  . LYS A 86  ? 0.8217 1.2404 1.1312 -0.0206 0.0586  0.1006  272 LYS B NZ  
503  N N   . PRO A 87  ? 0.8648 1.1296 0.9969 -0.0409 0.0628  0.0914  273 PRO B N   
504  C CA  . PRO A 87  ? 0.8202 1.0612 0.9304 -0.0382 0.0658  0.0960  273 PRO B CA  
505  C C   . PRO A 87  ? 0.7919 1.0307 0.9203 -0.0279 0.0740  0.1067  273 PRO B C   
506  O O   . PRO A 87  ? 0.8475 1.0914 1.0011 -0.0259 0.0830  0.1062  273 PRO B O   
507  C CB  . PRO A 87  ? 0.8608 1.0747 0.9521 -0.0525 0.0738  0.0847  273 PRO B CB  
508  C CG  . PRO A 87  ? 0.9273 1.1502 1.0212 -0.0630 0.0702  0.0755  273 PRO B CG  
509  C CD  . PRO A 87  ? 0.8647 1.1189 0.9919 -0.0569 0.0680  0.0789  273 PRO B CD  
510  N N   . VAL A 88  ? 0.7872 1.0183 0.9041 -0.0211 0.0712  0.1165  274 VAL B N   
511  C CA  . VAL A 88  ? 0.7876 1.0184 0.9231 -0.0102 0.0758  0.1303  274 VAL B CA  
512  C C   . VAL A 88  ? 0.7948 0.9959 0.9291 -0.0164 0.0868  0.1253  274 VAL B C   
513  O O   . VAL A 88  ? 0.8043 0.9857 0.9146 -0.0262 0.0875  0.1166  274 VAL B O   
514  C CB  . VAL A 88  ? 0.7864 1.0272 0.9116 0.0000  0.0672  0.1455  274 VAL B CB  
515  C CG1 . VAL A 88  ? 0.7889 1.0268 0.9346 0.0098  0.0726  0.1623  274 VAL B CG1 
516  C CG2 . VAL A 88  ? 0.7864 1.0574 0.9098 0.0074  0.0552  0.1484  274 VAL B CG2 
517  N N   . GLY A 89  ? 0.7963 0.9938 0.9564 -0.0100 0.0947  0.1302  275 GLY B N   
518  C CA  . GLY A 89  ? 0.8043 0.9735 0.9656 -0.0143 0.1036  0.1245  275 GLY B CA  
519  C C   . GLY A 89  ? 0.8463 1.0066 1.0127 -0.0088 0.1012  0.1391  275 GLY B C   
520  O O   . GLY A 89  ? 0.8033 0.9815 0.9820 0.0018  0.0963  0.1564  275 GLY B O   
521  N N   . THR A 90  ? 0.9360 1.0696 1.0936 -0.0163 0.1045  0.1324  276 THR B N   
522  C CA  . THR A 90  ? 0.8154 0.9388 0.9784 -0.0147 0.1019  0.1450  276 THR B CA  
523  C C   . THR A 90  ? 0.8529 0.9500 1.0338 -0.0166 0.1086  0.1395  276 THR B C   
524  O O   . THR A 90  ? 0.8350 0.9168 1.0172 -0.0207 0.1064  0.1437  276 THR B O   
525  C CB  . THR A 90  ? 0.8102 0.9282 0.9442 -0.0228 0.0957  0.1428  276 THR B CB  
526  O OG1 . THR A 90  ? 0.9129 1.0103 1.0274 -0.0342 0.0985  0.1233  276 THR B OG1 
527  C CG2 . THR A 90  ? 0.7997 0.9410 0.9155 -0.0196 0.0884  0.1470  276 THR B CG2 
528  N N   . LYS A 91  ? 0.8478 0.9400 1.0438 -0.0136 0.1165  0.1296  277 LYS B N   
529  C CA  . LYS A 91  ? 0.8574 0.9218 1.0672 -0.0150 0.1229  0.1197  277 LYS B CA  
530  C C   . LYS A 91  ? 0.8650 0.9224 1.1049 -0.0080 0.1215  0.1374  277 LYS B C   
531  O O   . LYS A 91  ? 0.9839 1.0171 1.2285 -0.0138 0.1204  0.1345  277 LYS B O   
532  C CB  . LYS A 91  ? 0.8669 0.9307 1.0868 -0.0106 0.1329  0.1058  277 LYS B CB  
533  C CG  . LYS A 91  ? 0.8905 0.9239 1.1199 -0.0109 0.1398  0.0911  277 LYS B CG  
534  C CD  . LYS A 91  ? 0.9009 0.9377 1.1428 -0.0034 0.1513  0.0791  277 LYS B CD  
535  C CE  . LYS A 91  ? 1.0251 1.0306 1.2660 -0.0043 0.1587  0.0585  277 LYS B CE  
536  N NZ  . LYS A 91  ? 0.9929 1.0049 1.2435 0.0041  0.1718  0.0462  277 LYS B NZ  
537  N N   . LYS A 92  ? 0.8600 0.9386 1.1215 0.0042  0.1210  0.1565  278 LYS B N   
538  C CA  . LYS A 92  ? 0.9225 0.9950 1.2146 0.0117  0.1207  0.1768  278 LYS B CA  
539  C C   . LYS A 92  ? 0.9267 0.9962 1.2121 0.0051  0.1145  0.1900  278 LYS B C   
540  O O   . LYS A 92  ? 0.9632 1.0123 1.2691 0.0026  0.1148  0.1965  278 LYS B O   
541  C CB  . LYS A 92  ? 0.8652 0.9656 1.1770 0.0270  0.1204  0.1968  278 LYS B CB  
542  N N   . LEU A 93  ? 0.8493 0.9390 1.1078 0.0023  0.1087  0.1937  279 LEU B N   
543  C CA  . LEU A 93  ? 0.9032 0.9943 1.1550 -0.0026 0.1037  0.2063  279 LEU B CA  
544  C C   . LEU A 93  ? 1.0296 1.0921 1.2750 -0.0166 0.1026  0.1904  279 LEU B C   
545  O O   . LEU A 93  ? 1.0355 1.0893 1.2960 -0.0207 0.1006  0.2016  279 LEU B O   
546  C CB  . LEU A 93  ? 0.8368 0.9543 1.0587 -0.0012 0.0981  0.2098  279 LEU B CB  
547  C CG  . LEU A 93  ? 0.9193 1.0442 1.1303 -0.0039 0.0937  0.2227  279 LEU B CG  
548  C CD1 . LEU A 93  ? 0.9627 1.0900 1.2042 0.0014  0.0959  0.2489  279 LEU B CD1 
549  C CD2 . LEU A 93  ? 0.8109 0.9635 0.9943 0.0021  0.0887  0.2261  279 LEU B CD2 
550  N N   . THR A 94  ? 1.0227 1.0721 1.2466 -0.0241 0.1037  0.1650  280 THR B N   
551  C CA  . THR A 94  ? 0.9906 1.0134 1.2061 -0.0363 0.1017  0.1482  280 THR B CA  
552  C C   . THR A 94  ? 1.0457 1.0431 1.2933 -0.0367 0.1040  0.1473  280 THR B C   
553  O O   . THR A 94  ? 1.0495 1.0307 1.3052 -0.0453 0.0992  0.1470  280 THR B O   
554  C CB  . THR A 94  ? 1.0627 1.0772 1.2485 -0.0421 0.1040  0.1227  280 THR B CB  
555  O OG1 . THR A 94  ? 1.0490 1.0815 1.2051 -0.0444 0.1001  0.1232  280 THR B OG1 
556  C CG2 . THR A 94  ? 1.0557 1.0419 1.2330 -0.0528 0.1016  0.1041  280 THR B CG2 
557  N N   . LYS A 95  ? 1.1538 1.1472 1.4217 -0.0275 0.1108  0.1462  281 LYS B N   
558  C CA  . LYS A 95  ? 1.2445 1.2131 1.5470 -0.0255 0.1131  0.1479  281 LYS B CA  
559  C C   . LYS A 95  ? 1.1502 1.1243 1.4812 -0.0237 0.1099  0.1770  281 LYS B C   
560  O O   . LYS A 95  ? 1.2293 1.1794 1.5866 -0.0285 0.1083  0.1791  281 LYS B O   
561  C CB  . LYS A 95  ? 1.2048 1.1722 1.5244 -0.0129 0.1216  0.1438  281 LYS B CB  
562  C CG  . LYS A 95  ? 1.1896 1.1317 1.5488 -0.0074 0.1245  0.1485  281 LYS B CG  
563  C CD  . LYS A 95  ? 1.2852 1.2374 1.6660 0.0090  0.1321  0.1557  281 LYS B CD  
564  C CE  . LYS A 95  ? 1.2989 1.2614 1.6575 0.0121  0.1384  0.1340  281 LYS B CE  
565  N NZ  . LYS A 95  ? 1.3328 1.2666 1.6753 0.0044  0.1413  0.1030  281 LYS B NZ  
566  N N   . SER A 96  ? 1.0572 1.0628 1.3833 -0.0171 0.1088  0.1995  282 SER B N   
567  C CA  . SER A 96  ? 1.0337 1.0494 1.3875 -0.0120 0.1084  0.2310  282 SER B CA  
568  C C   . SER A 96  ? 1.0797 1.0844 1.4420 -0.0245 0.1035  0.2369  282 SER B C   
569  O O   . SER A 96  ? 1.0358 1.0252 1.4336 -0.0263 0.1042  0.2511  282 SER B O   
570  C CB  . SER A 96  ? 0.9590 1.0131 1.2983 -0.0014 0.1079  0.2508  282 SER B CB  
571  O OG  . SER A 96  ? 1.1253 1.1907 1.4925 0.0078  0.1100  0.2826  282 SER B OG  
572  N N   . PHE A 97  ? 1.1171 1.1295 1.4498 -0.0336 0.0983  0.2270  283 PHE B N   
573  C CA  . PHE A 97  ? 1.0052 1.0111 1.3462 -0.0457 0.0928  0.2316  283 PHE B CA  
574  C C   . PHE A 97  ? 1.0521 1.0264 1.3887 -0.0592 0.0876  0.2029  283 PHE B C   
575  O O   . PHE A 97  ? 0.9849 0.9549 1.3250 -0.0707 0.0809  0.2024  283 PHE B O   
576  C CB  . PHE A 97  ? 0.8874 0.9223 1.2016 -0.0459 0.0895  0.2406  283 PHE B CB  
577  C CG  . PHE A 97  ? 0.8640 0.9051 1.1354 -0.0461 0.0875  0.2186  283 PHE B CG  
578  C CD1 . PHE A 97  ? 0.9311 0.9551 1.1819 -0.0577 0.0823  0.1944  283 PHE B CD1 
579  C CD2 . PHE A 97  ? 0.8530 0.9172 1.1052 -0.0350 0.0901  0.2231  283 PHE B CD2 
580  C CE1 . PHE A 97  ? 0.9672 0.9960 1.1798 -0.0581 0.0812  0.1770  283 PHE B CE1 
581  C CE2 . PHE A 97  ? 0.9515 1.0199 1.1678 -0.0365 0.0881  0.2040  283 PHE B CE2 
582  C CZ  . PHE A 97  ? 0.9778 1.0279 1.1745 -0.0480 0.0844  0.1820  283 PHE B CZ  
583  N N   . GLY A 98  ? 1.0820 1.0364 1.4108 -0.0576 0.0905  0.1792  284 GLY B N   
584  C CA  . GLY A 98  ? 1.1209 1.0423 1.4502 -0.0680 0.0862  0.1528  284 GLY B CA  
585  C C   . GLY A 98  ? 1.0959 1.0157 1.3934 -0.0798 0.0781  0.1347  284 GLY B C   
586  O O   . GLY A 98  ? 1.1115 1.0116 1.4190 -0.0912 0.0702  0.1245  284 GLY B O   
587  N N   . TRP A 99  ? 1.1004 1.0400 1.3607 -0.0775 0.0789  0.1304  285 TRP B N   
588  C CA  . TRP A 99  ? 1.0799 1.0159 1.3061 -0.0870 0.0720  0.1116  285 TRP B CA  
589  C C   . TRP A 99  ? 1.1258 1.0470 1.3261 -0.0853 0.0768  0.0850  285 TRP B C   
590  O O   . TRP A 99  ? 0.9953 0.9303 1.1690 -0.0806 0.0818  0.0816  285 TRP B O   
591  C CB  . TRP A 99  ? 1.0515 1.0157 1.2543 -0.0856 0.0697  0.1241  285 TRP B CB  
592  C CG  . TRP A 99  ? 0.9757 0.9550 1.2003 -0.0879 0.0651  0.1476  285 TRP B CG  
593  C CD1 . TRP A 99  ? 0.9851 0.9591 1.2509 -0.0902 0.0646  0.1634  285 TRP B CD1 
594  C CD2 . TRP A 99  ? 0.9766 0.9792 1.1844 -0.0880 0.0611  0.1584  285 TRP B CD2 
595  N NE1 . TRP A 99  ? 0.9593 0.9546 1.2356 -0.0920 0.0615  0.1847  285 TRP B NE1 
596  C CE2 . TRP A 99  ? 0.9816 0.9950 1.2220 -0.0899 0.0593  0.1813  285 TRP B CE2 
597  C CE3 . TRP A 99  ? 1.0047 1.0195 1.1744 -0.0862 0.0593  0.1515  285 TRP B CE3 
598  C CZ2 . TRP A 99  ? 1.0107 1.0490 1.2459 -0.0889 0.0566  0.1967  285 TRP B CZ2 
599  C CZ3 . TRP A 99  ? 0.9940 1.0304 1.1580 -0.0849 0.0556  0.1657  285 TRP B CZ3 
600  C CH2 . TRP A 99  ? 0.9884 1.0376 1.1845 -0.0857 0.0546  0.1878  285 TRP B CH2 
601  N N   . GLU A 100 ? 1.1421 1.0348 1.3515 -0.0892 0.0756  0.0660  286 GLU B N   
602  C CA  . GLU A 100 ? 1.1031 0.9809 1.2923 -0.0858 0.0822  0.0410  286 GLU B CA  
603  C C   . GLU A 100 ? 1.1039 0.9597 1.2692 -0.0951 0.0750  0.0142  286 GLU B C   
604  O O   . GLU A 100 ? 1.1273 0.9716 1.2707 -0.0920 0.0811  -0.0075 286 GLU B O   
605  C CB  . GLU A 100 ? 1.1947 1.0593 1.4163 -0.0765 0.0905  0.0414  286 GLU B CB  
606  C CG  . GLU A 100 ? 1.1773 1.0672 1.4126 -0.0649 0.0986  0.0643  286 GLU B CG  
607  C CD  . GLU A 100 ? 1.2811 1.1609 1.5582 -0.0558 0.1036  0.0749  286 GLU B CD  
608  O OE1 . GLU A 100 ? 1.3567 1.2198 1.6628 -0.0605 0.0980  0.0821  286 GLU B OE1 
609  O OE2 . GLU A 100 ? 1.3501 1.2388 1.6330 -0.0440 0.1129  0.0766  286 GLU B OE2 
610  N N   . THR A 101 ? 1.2044 1.0562 1.3732 -0.1058 0.0622  0.0154  287 THR B N   
611  C CA  . THR A 101 ? 1.2277 1.0632 1.3685 -0.1143 0.0533  -0.0096 287 THR B CA  
612  C C   . THR A 101 ? 1.2151 1.0666 1.3099 -0.1142 0.0545  -0.0133 287 THR B C   
613  O O   . THR A 101 ? 1.2284 1.1036 1.3178 -0.1114 0.0573  0.0054  287 THR B O   
614  C CB  . THR A 101 ? 1.2361 1.0654 1.3977 -0.1263 0.0378  -0.0065 287 THR B CB  
615  O OG1 . THR A 101 ? 1.3772 1.2062 1.5037 -0.1338 0.0272  -0.0218 287 THR B OG1 
616  C CG2 . THR A 101 ? 1.2072 1.0604 1.3969 -0.1270 0.0365  0.0257  287 THR B CG2 
617  N N   . LEU A 102 ? 1.2191 1.0565 1.2800 -0.1173 0.0519  -0.0379 288 LEU B N   
618  C CA  . LEU A 102 ? 1.2121 1.0607 1.2283 -0.1163 0.0554  -0.0424 288 LEU B CA  
619  C C   . LEU A 102 ? 1.2302 1.0982 1.2363 -0.1210 0.0467  -0.0257 288 LEU B C   
620  O O   . LEU A 102 ? 1.1938 1.0763 1.1752 -0.1181 0.0519  -0.0190 288 LEU B O   
621  C CB  . LEU A 102 ? 1.1669 0.9966 1.1486 -0.1188 0.0526  -0.0704 288 LEU B CB  
622  C CG  . LEU A 102 ? 1.1346 0.9550 1.1023 -0.1103 0.0679  -0.0869 288 LEU B CG  
623  C CD1 . LEU A 102 ? 1.1337 0.9362 1.0644 -0.1118 0.0647  -0.1147 288 LEU B CD1 
624  C CD2 . LEU A 102 ? 1.1395 0.9809 1.0921 -0.1047 0.0815  -0.0746 288 LEU B CD2 
625  N N   . ASP A 103 ? 1.2000 1.0688 1.2268 -0.1281 0.0336  -0.0187 289 ASP B N   
626  C CA  . ASP A 103 ? 1.1489 1.0366 1.1686 -0.1315 0.0250  -0.0037 289 ASP B CA  
627  C C   . ASP A 103 ? 1.2010 1.1081 1.2559 -0.1289 0.0264  0.0232  289 ASP B C   
628  O O   . ASP A 103 ? 1.2069 1.1302 1.2642 -0.1313 0.0189  0.0364  289 ASP B O   
629  C CB  . ASP A 103 ? 1.1164 0.9958 1.1301 -0.1411 0.0085  -0.0155 289 ASP B CB  
630  C CG  . ASP A 103 ? 1.2986 1.1599 1.3475 -0.1475 0.0013  -0.0243 289 ASP B CG  
631  O OD1 . ASP A 103 ? 1.3487 1.2053 1.4309 -0.1442 0.0091  -0.0164 289 ASP B OD1 
632  O OD2 . ASP A 103 ? 1.3418 1.1926 1.3851 -0.1557 -0.0130 -0.0397 289 ASP B OD2 
633  N N   . SER A 104 ? 1.1222 1.0294 1.2041 -0.1228 0.0362  0.0321  290 SER B N   
634  C CA  . SER A 104 ? 1.0969 1.0212 1.2145 -0.1200 0.0375  0.0583  290 SER B CA  
635  C C   . SER A 104 ? 1.0884 1.0398 1.1908 -0.1148 0.0389  0.0759  290 SER B C   
636  O O   . SER A 104 ? 1.1683 1.1359 1.2869 -0.1159 0.0340  0.0933  290 SER B O   
637  C CB  . SER A 104 ? 1.0161 0.9361 1.1594 -0.1123 0.0484  0.0646  290 SER B CB  
638  O OG  . SER A 104 ? 1.1683 1.0908 1.2871 -0.1048 0.0583  0.0567  290 SER B OG  
639  N N   . PHE A 105 ? 1.0164 0.9733 1.0891 -0.1088 0.0458  0.0715  291 PHE B N   
640  C CA  . PHE A 105 ? 1.0049 0.9850 1.0642 -0.1030 0.0465  0.0866  291 PHE B CA  
641  C C   . PHE A 105 ? 1.0556 1.0390 1.0896 -0.1074 0.0373  0.0832  291 PHE B C   
642  O O   . PHE A 105 ? 1.0431 1.0456 1.0771 -0.1035 0.0349  0.0982  291 PHE B O   
643  C CB  . PHE A 105 ? 0.8758 0.8610 0.9170 -0.0960 0.0558  0.0840  291 PHE B CB  
644  C CG  . PHE A 105 ? 0.9355 0.9296 1.0038 -0.0881 0.0636  0.0963  291 PHE B CG  
645  C CD1 . PHE A 105 ? 1.0435 1.0230 1.1303 -0.0874 0.0693  0.0884  291 PHE B CD1 
646  C CD2 . PHE A 105 ? 0.8688 0.8865 0.9438 -0.0800 0.0648  0.1156  291 PHE B CD2 
647  C CE1 . PHE A 105 ? 1.0085 0.9969 1.1214 -0.0789 0.0759  0.1013  291 PHE B CE1 
648  C CE2 . PHE A 105 ? 0.8629 0.8907 0.9615 -0.0717 0.0709  0.1282  291 PHE B CE2 
649  C CZ  . PHE A 105 ? 0.9708 0.9840 1.0893 -0.0712 0.0763  0.1219  291 PHE B CZ  
650  N N   . MET A 106 ? 0.9820 0.9483 0.9937 -0.1141 0.0321  0.0642  292 MET B N   
651  C CA  . MET A 106 ? 1.0167 0.9875 1.0060 -0.1172 0.0224  0.0632  292 MET B CA  
652  C C   . MET A 106 ? 1.1416 1.1173 1.1558 -0.1233 0.0110  0.0692  292 MET B C   
653  O O   . MET A 106 ? 1.1565 1.1434 1.1605 -0.1236 0.0031  0.0742  292 MET B O   
654  C CB  . MET A 106 ? 0.9883 0.9424 0.9392 -0.1207 0.0209  0.0432  292 MET B CB  
655  C CG  . MET A 106 ? 0.9355 0.8913 0.8588 -0.1154 0.0306  0.0425  292 MET B CG  
656  S SD  . MET A 106 ? 1.1360 1.0769 1.0113 -0.1189 0.0293  0.0260  292 MET B SD  
657  C CE  . MET A 106 ? 1.2163 1.1636 1.0822 -0.1212 0.0132  0.0315  292 MET B CE  
658  N N   . GLN A 107 ? 1.2922 1.2601 1.3408 -0.1282 0.0097  0.0691  293 GLN B N   
659  C CA  . GLN A 107 ? 1.2607 1.2362 1.3383 -0.1353 -0.0012 0.0772  293 GLN B CA  
660  C C   . GLN A 107 ? 1.2245 1.2258 1.3310 -0.1299 0.0031  0.1046  293 GLN B C   
661  O O   . GLN A 107 ? 1.2434 1.2606 1.3669 -0.1332 -0.0044 0.1158  293 GLN B O   
662  C CB  . GLN A 107 ? 1.2554 1.2105 1.3613 -0.1445 -0.0063 0.0659  293 GLN B CB  
663  C CG  . GLN A 107 ? 1.3076 1.2405 1.3883 -0.1514 -0.0155 0.0384  293 GLN B CG  
664  C CD  . GLN A 107 ? 1.4622 1.3767 1.5755 -0.1614 -0.0242 0.0276  293 GLN B CD  
665  O OE1 . GLN A 107 ? 1.4955 1.4168 1.6532 -0.1655 -0.0259 0.0439  293 GLN B OE1 
666  N NE2 . GLN A 107 ? 1.6673 1.5579 1.7592 -0.1653 -0.0297 0.0004  293 GLN B NE2 
667  N N   . HIS A 108 ? 1.0490 1.0568 1.1621 -0.1211 0.0151  0.1161  294 HIS B N   
668  C CA  . HIS A 108 ? 1.0101 1.0427 1.1490 -0.1147 0.0201  0.1426  294 HIS B CA  
669  C C   . HIS A 108 ? 0.9397 0.9932 1.0505 -0.1046 0.0223  0.1504  294 HIS B C   
670  O O   . HIS A 108 ? 0.9394 0.9862 1.0139 -0.1036 0.0198  0.1364  294 HIS B O   
671  C CB  . HIS A 108 ? 1.0283 1.0587 1.1893 -0.1092 0.0306  0.1524  294 HIS B CB  
672  C CG  . HIS A 108 ? 1.0568 1.0656 1.2504 -0.1175 0.0290  0.1470  294 HIS B CG  
673  N ND1 . HIS A 108 ? 1.0456 1.0263 1.2275 -0.1237 0.0257  0.1213  294 HIS B ND1 
674  C CD2 . HIS A 108 ? 1.0559 1.0659 1.2936 -0.1201 0.0306  0.1641  294 HIS B CD2 
675  C CE1 . HIS A 108 ? 1.0981 1.0621 1.3152 -0.1295 0.0245  0.1207  294 HIS B CE1 
676  N NE2 . HIS A 108 ? 1.1537 1.1341 1.4065 -0.1281 0.0273  0.1472  294 HIS B NE2 
677  N N   . ASP A 109 ? 0.9259 1.0044 1.0533 -0.0964 0.0275  0.1733  295 ASP B N   
678  C CA  . ASP A 109 ? 0.9039 1.0030 1.0072 -0.0854 0.0293  0.1810  295 ASP B CA  
679  C C   . ASP A 109 ? 0.8560 0.9652 0.9529 -0.0735 0.0390  0.1896  295 ASP B C   
680  O O   . ASP A 109 ? 0.8436 0.9506 0.9621 -0.0726 0.0448  0.1968  295 ASP B O   
681  C CB  . ASP A 109 ? 0.9326 1.0576 1.0561 -0.0831 0.0270  0.2000  295 ASP B CB  
682  C CG  . ASP A 109 ? 0.8995 1.0193 1.0299 -0.0943 0.0154  0.1919  295 ASP B CG  
683  O OD1 . ASP A 109 ? 0.8945 0.9960 0.9968 -0.0989 0.0084  0.1715  295 ASP B OD1 
684  O OD2 . ASP A 109 ? 0.8263 0.9619 0.9917 -0.0985 0.0131  0.2068  295 ASP B OD2 
685  N N   . VAL A 110 ? 0.9028 1.1363 0.8216 0.0317  0.0111  0.1946  296 VAL B N   
686  C CA  . VAL A 110 ? 0.8912 1.1280 0.8085 0.0409  0.0196  0.2058  296 VAL B CA  
687  C C   . VAL A 110 ? 0.9002 1.1436 0.8509 0.0462  0.0226  0.2223  296 VAL B C   
688  O O   . VAL A 110 ? 0.9333 1.1788 0.8983 0.0509  0.0295  0.2292  296 VAL B O   
689  C CB  . VAL A 110 ? 0.8853 1.1265 0.7710 0.0449  0.0199  0.2119  296 VAL B CB  
690  C CG1 . VAL A 110 ? 0.8942 1.1285 0.7467 0.0401  0.0188  0.1967  296 VAL B CG1 
691  C CG2 . VAL A 110 ? 0.8841 1.1304 0.7700 0.0444  0.0124  0.2200  296 VAL B CG2 
692  N N   . GLN A 111 ? 0.8812 1.1287 0.8450 0.0450  0.0171  0.2292  297 GLN B N   
693  C CA  . GLN A 111 ? 0.8738 1.1280 0.8688 0.0483  0.0193  0.2442  297 GLN B CA  
694  C C   . GLN A 111 ? 0.8840 1.1325 0.9102 0.0466  0.0222  0.2409  297 GLN B C   
695  O O   . GLN A 111 ? 0.8723 1.1253 0.9200 0.0506  0.0271  0.2541  297 GLN B O   
696  C CB  . GLN A 111 ? 0.8890 1.1473 0.8920 0.0460  0.0124  0.2484  297 GLN B CB  
697  C CG  . GLN A 111 ? 0.8702 1.1337 0.8485 0.0471  0.0083  0.2508  297 GLN B CG  
698  C CD  . GLN A 111 ? 0.8819 1.1385 0.8401 0.0413  -0.0001 0.2375  297 GLN B CD  
699  O OE1 . GLN A 111 ? 0.8894 1.1392 0.8288 0.0382  0.0002  0.2258  297 GLN B OE1 
700  N NE2 . GLN A 111 ? 0.8849 1.1443 0.8471 0.0390  -0.0080 0.2391  297 GLN B NE2 
701  N N   . GLU A 112 ? 0.8899 1.1299 0.9214 0.0399  0.0191  0.2237  298 GLU B N   
702  C CA  . GLU A 112 ? 0.9016 1.1363 0.9678 0.0376  0.0224  0.2184  298 GLU B CA  
703  C C   . GLU A 112 ? 0.9075 1.1397 0.9783 0.0417  0.0293  0.2189  298 GLU B C   
704  O O   . GLU A 112 ? 0.8898 1.1222 0.9930 0.0448  0.0329  0.2287  298 GLU B O   
705  C CB  . GLU A 112 ? 0.9067 1.1360 0.9761 0.0278  0.0191  0.1965  298 GLU B CB  
706  C CG  . GLU A 112 ? 0.9104 1.1432 0.9784 0.0229  0.0121  0.1951  298 GLU B CG  
707  C CD  . GLU A 112 ? 0.9744 1.2053 1.0531 0.0118  0.0105  0.1739  298 GLU B CD  
708  O OE1 . GLU A 112 ? 1.0505 1.2797 1.1659 0.0097  0.0145  0.1698  298 GLU B OE1 
709  O OE2 . GLU A 112 ? 1.0365 1.2690 1.0882 0.0043  0.0055  0.1614  298 GLU B OE2 
710  N N   . LEU A 113 ? 0.8930 1.1230 0.9321 0.0417  0.0307  0.2092  299 LEU B N   
711  C CA  . LEU A 113 ? 0.9177 1.1455 0.9592 0.0457  0.0373  0.2085  299 LEU B CA  
712  C C   . LEU A 113 ? 0.8997 1.1371 0.9478 0.0543  0.0414  0.2323  299 LEU B C   
713  O O   . LEU A 113 ? 0.9672 1.2050 1.0397 0.0576  0.0456  0.2395  299 LEU B O   
714  C CB  . LEU A 113 ? 0.9288 1.1532 0.9312 0.0435  0.0382  0.1931  299 LEU B CB  
715  C CG  . LEU A 113 ? 0.8926 1.1138 0.8971 0.0466  0.0449  0.1876  299 LEU B CG  
716  C CD1 . LEU A 113 ? 0.8995 1.1142 0.9442 0.0424  0.0464  0.1760  299 LEU B CD1 
717  C CD2 . LEU A 113 ? 0.8961 1.1141 0.8587 0.0436  0.0457  0.1716  299 LEU B CD2 
718  N N   . CYS A 114 ? 0.8708 1.1176 0.8990 0.0569  0.0402  0.2446  300 CYS B N   
719  C CA  . CYS A 114 ? 0.8591 1.1193 0.8944 0.0625  0.0445  0.2666  300 CYS B CA  
720  C C   . CYS A 114 ? 0.8909 1.1544 0.9669 0.0620  0.0433  0.2809  300 CYS B C   
721  O O   . CYS A 114 ? 0.8676 1.1395 0.9611 0.0649  0.0471  0.2973  300 CYS B O   
722  C CB  . CYS A 114 ? 0.8508 1.1216 0.8603 0.0637  0.0438  0.2734  300 CYS B CB  
723  S SG  . CYS A 114 ? 0.8987 1.1913 0.9122 0.0679  0.0508  0.2969  300 CYS B SG  
724  N N   . ARG A 115 ? 0.9711 1.2290 1.0625 0.0575  0.0379  0.2755  301 ARG B N   
725  C CA  . ARG A 115 ? 0.9706 1.2298 1.1016 0.0564  0.0369  0.2873  301 ARG B CA  
726  C C   . ARG A 115 ? 0.9765 1.2275 1.1388 0.0568  0.0398  0.2846  301 ARG B C   
727  O O   . ARG A 115 ? 0.9747 1.2303 1.1671 0.0585  0.0411  0.3020  301 ARG B O   
728  C CB  . ARG A 115 ? 1.0478 1.3027 1.1874 0.0514  0.0313  0.2796  301 ARG B CB  
729  C CG  . ARG A 115 ? 1.0229 1.2880 1.1475 0.0512  0.0279  0.2882  301 ARG B CG  
730  C CD  . ARG A 115 ? 1.0093 1.2882 1.1514 0.0526  0.0303  0.3109  301 ARG B CD  
731  N NE  . ARG A 115 ? 1.0588 1.3502 1.1802 0.0560  0.0350  0.3209  301 ARG B NE  
732  C CZ  . ARG A 115 ? 1.1030 1.4095 1.2363 0.0563  0.0386  0.3404  301 ARG B CZ  
733  N NH1 . ARG A 115 ? 1.1271 1.4370 1.2924 0.0535  0.0374  0.3538  301 ARG B NH1 
734  N NH2 . ARG A 115 ? 1.1101 1.4299 1.2226 0.0585  0.0438  0.3468  301 ARG B NH2 
735  N N   . VAL A 116 ? 0.8802 1.1198 1.0377 0.0544  0.0404  0.2628  302 VAL B N   
736  C CA  . VAL A 116 ? 0.9116 1.1434 1.1027 0.0543  0.0434  0.2570  302 VAL B CA  
737  C C   . VAL A 116 ? 0.8796 1.1174 1.0747 0.0606  0.0475  0.2730  302 VAL B C   
738  O O   . VAL A 116 ? 0.8808 1.1186 1.1144 0.0624  0.0485  0.2852  302 VAL B O   
739  C CB  . VAL A 116 ? 0.9019 1.1234 1.0830 0.0487  0.0440  0.2279  302 VAL B CB  
740  C CG1 . VAL A 116 ? 0.8981 1.1133 1.1101 0.0494  0.0483  0.2206  302 VAL B CG1 
741  C CG2 . VAL A 116 ? 0.9019 1.1197 1.0919 0.0408  0.0404  0.2131  302 VAL B CG2 
742  N N   . LEU A 117 ? 0.8731 1.1169 1.0295 0.0639  0.0499  0.2734  303 LEU B N   
743  C CA  . LEU A 117 ? 0.9305 1.1826 1.0871 0.0694  0.0544  0.2878  303 LEU B CA  
744  C C   . LEU A 117 ? 0.8978 1.1659 1.0689 0.0711  0.0542  0.3168  303 LEU B C   
745  O O   . LEU A 117 ? 0.9518 1.2246 1.1529 0.0730  0.0552  0.3331  303 LEU B O   
746  C CB  . LEU A 117 ? 0.9090 1.1644 1.0190 0.0718  0.0580  0.2791  303 LEU B CB  
747  C CG  . LEU A 117 ? 0.8692 1.1110 0.9596 0.0687  0.0583  0.2508  303 LEU B CG  
748  C CD1 . LEU A 117 ? 0.8640 1.1098 0.9064 0.0709  0.0617  0.2449  303 LEU B CD1 
749  C CD2 . LEU A 117 ? 0.8753 1.1084 0.9961 0.0688  0.0606  0.2414  303 LEU B CD2 
750  N N   . LEU A 118 ? 0.8528 1.1305 1.0046 0.0695  0.0527  0.3236  304 LEU B N   
751  C CA  . LEU A 118 ? 0.8441 1.1411 1.0042 0.0691  0.0535  0.3491  304 LEU B CA  
752  C C   . LEU A 118 ? 0.8494 1.1456 1.0537 0.0664  0.0498  0.3636  304 LEU B C   
753  O O   . LEU A 118 ? 0.8677 1.1779 1.0903 0.0659  0.0506  0.3866  304 LEU B O   
754  C CB  . LEU A 118 ? 0.8945 1.2019 1.0268 0.0670  0.0529  0.3494  304 LEU B CB  
755  C CG  . LEU A 118 ? 0.8755 1.1925 0.9688 0.0698  0.0583  0.3456  304 LEU B CG  
756  C CD1 . LEU A 118 ? 0.9480 1.2807 1.0261 0.0671  0.0586  0.3517  304 LEU B CD1 
757  C CD2 . LEU A 118 ? 0.8803 1.2093 0.9749 0.0728  0.0645  0.3578  304 LEU B CD2 
758  N N   . ASP A 119 ? 0.9923 1.2737 1.2144 0.0637  0.0459  0.3510  305 ASP B N   
759  C CA  . ASP A 119 ? 0.9982 1.2771 1.2647 0.0612  0.0432  0.3629  305 ASP B CA  
760  C C   . ASP A 119 ? 1.0028 1.2775 1.3027 0.0639  0.0447  0.3707  305 ASP B C   
761  O O   . ASP A 119 ? 1.0305 1.3123 1.3624 0.0629  0.0432  0.3933  305 ASP B O   
762  C CB  . ASP A 119 ? 1.0068 1.2708 1.2856 0.0578  0.0402  0.3443  305 ASP B CB  
763  C CG  . ASP A 119 ? 1.1402 1.4096 1.3966 0.0547  0.0372  0.3418  305 ASP B CG  
764  O OD1 . ASP A 119 ? 1.0635 1.3483 1.3135 0.0537  0.0368  0.3596  305 ASP B OD1 
765  O OD2 . ASP A 119 ? 1.0980 1.3577 1.3449 0.0524  0.0352  0.3216  305 ASP B OD2 
766  N N   . ASN A 120 ? 0.8949 1.1587 1.1890 0.0668  0.0472  0.3525  306 ASN B N   
767  C CA  . ASN A 120 ? 0.8850 1.1445 1.2126 0.0696  0.0485  0.3577  306 ASN B CA  
768  C C   . ASN A 120 ? 0.9156 1.1932 1.2405 0.0725  0.0497  0.3844  306 ASN B C   
769  O O   . ASN A 120 ? 0.9655 1.2467 1.3290 0.0728  0.0479  0.4046  306 ASN B O   
770  C CB  . ASN A 120 ? 0.9727 1.2191 1.2893 0.0711  0.0515  0.3300  306 ASN B CB  
771  C CG  . ASN A 120 ? 0.9453 1.1756 1.2902 0.0668  0.0508  0.3073  306 ASN B CG  
772  O OD1 . ASN A 120 ? 0.9042 1.1272 1.2955 0.0668  0.0512  0.3072  306 ASN B OD1 
773  N ND2 . ASN A 120 ? 1.0063 1.2321 1.3252 0.0624  0.0500  0.2877  306 ASN B ND2 
774  N N   . VAL A 121 ? 0.8823 1.1725 1.1630 0.0739  0.0530  0.3851  307 VAL B N   
775  C CA  . VAL A 121 ? 0.9383 1.2495 1.2131 0.0753  0.0555  0.4086  307 VAL B CA  
776  C C   . VAL A 121 ? 1.0256 1.3545 1.3187 0.0701  0.0525  0.4366  307 VAL B C   
777  O O   . VAL A 121 ? 1.0667 1.4083 1.3842 0.0692  0.0514  0.4610  307 VAL B O   
778  C CB  . VAL A 121 ? 0.9164 1.2379 1.1401 0.0773  0.0611  0.3999  307 VAL B CB  
779  C CG1 . VAL A 121 ? 1.0261 1.3754 1.2419 0.0760  0.0644  0.4251  307 VAL B CG1 
780  C CG2 . VAL A 121 ? 0.9698 1.2777 1.1791 0.0820  0.0644  0.3781  307 VAL B CG2 
781  N N   . GLU A 122 ? 1.0284 1.3594 1.3096 0.0658  0.0507  0.4338  308 GLU B N   
782  C CA  . GLU A 122 ? 1.0484 1.3966 1.3457 0.0593  0.0479  0.4577  308 GLU B CA  
783  C C   . GLU A 122 ? 1.0181 1.3580 1.3660 0.0577  0.0429  0.4718  308 GLU B C   
784  O O   . GLU A 122 ? 0.9799 1.3365 1.3488 0.0530  0.0407  0.4992  308 GLU B O   
785  C CB  . GLU A 122 ? 0.9641 1.3127 1.2416 0.0554  0.0467  0.4475  308 GLU B CB  
786  C CG  . GLU A 122 ? 0.9509 1.3167 1.2438 0.0474  0.0439  0.4683  308 GLU B CG  
787  C CD  . GLU A 122 ? 1.0757 1.4387 1.3535 0.0442  0.0422  0.4551  308 GLU B CD  
788  O OE1 . GLU A 122 ? 1.0450 1.3972 1.2958 0.0481  0.0434  0.4328  308 GLU B OE1 
789  O OE2 . GLU A 122 ? 1.0046 1.3764 1.2980 0.0374  0.0392  0.4670  308 GLU B OE2 
790  N N   . ASN A 123 ? 0.9978 1.3133 1.3672 0.0604  0.0414  0.4533  309 ASN B N   
791  C CA  . ASN A 123 ? 1.0477 1.3534 1.4697 0.0594  0.0376  0.4641  309 ASN B CA  
792  C C   . ASN A 123 ? 1.0209 1.3314 1.4686 0.0625  0.0373  0.4816  309 ASN B C   
793  O O   . ASN A 123 ? 0.9819 1.2969 1.4698 0.0599  0.0332  0.5059  309 ASN B O   
794  C CB  . ASN A 123 ? 0.9566 1.2376 1.3953 0.0609  0.0379  0.4363  309 ASN B CB  
795  C CG  . ASN A 123 ? 1.0702 1.3420 1.5617 0.0582  0.0348  0.4446  309 ASN B CG  
796  O OD1 . ASN A 123 ? 1.0954 1.3784 1.6061 0.0543  0.0314  0.4711  309 ASN B OD1 
797  N ND2 . ASN A 123 ? 1.0254 1.2779 1.5413 0.0591  0.0363  0.4214  309 ASN B ND2 
798  N N   . LYS A 124 ? 0.9994 1.3093 1.4247 0.0678  0.0411  0.4702  310 LYS B N   
799  C CA  . LYS A 124 ? 0.9803 1.2964 1.4265 0.0712  0.0409  0.4860  310 LYS B CA  
800  C C   . LYS A 124 ? 1.0220 1.3673 1.4628 0.0667  0.0396  0.5198  310 LYS B C   
801  O O   . LYS A 124 ? 1.0898 1.4428 1.5652 0.0662  0.0360  0.5444  310 LYS B O   
802  C CB  . LYS A 124 ? 1.0179 1.3278 1.4356 0.0773  0.0461  0.4636  310 LYS B CB  
803  C CG  . LYS A 124 ? 0.9974 1.3082 1.4425 0.0818  0.0457  0.4735  310 LYS B CG  
804  C CD  . LYS A 124 ? 0.9859 1.2759 1.4886 0.0830  0.0422  0.4676  310 LYS B CD  
805  C CE  . LYS A 124 ? 0.9917 1.2827 1.5294 0.0874  0.0407  0.4795  310 LYS B CE  
806  N NZ  . LYS A 124 ? 1.1109 1.3807 1.7079 0.0886  0.0383  0.4693  310 LYS B NZ  
807  N N   . MET A 125 ? 1.0430 1.4063 1.4425 0.0626  0.0425  0.5213  311 MET B N   
808  C CA  . MET A 125 ? 1.0628 1.4584 1.4538 0.0559  0.0428  0.5503  311 MET B CA  
809  C C   . MET A 125 ? 1.1410 1.5469 1.5629 0.0469  0.0366  0.5758  311 MET B C   
810  O O   . MET A 125 ? 1.1162 1.5514 1.5358 0.0390  0.0360  0.6019  311 MET B O   
811  C CB  . MET A 125 ? 1.0303 1.4431 1.3699 0.0536  0.0491  0.5405  311 MET B CB  
812  C CG  . MET A 125 ? 1.0718 1.4785 1.3762 0.0612  0.0558  0.5179  311 MET B CG  
813  S SD  . MET A 125 ? 1.1644 1.5942 1.4150 0.0577  0.0637  0.5100  311 MET B SD  
814  C CE  . MET A 125 ? 1.0175 1.4450 1.2723 0.0506  0.0593  0.5079  311 MET B CE  
815  N N   . LYS A 126 ? 1.0958 1.4805 1.5450 0.0467  0.0326  0.5684  312 LYS B N   
816  C CA  . LYS A 126 ? 1.0315 1.4244 1.5112 0.0381  0.0267  0.5925  312 LYS B CA  
817  C C   . LYS A 126 ? 1.1308 1.5348 1.6497 0.0359  0.0217  0.6248  312 LYS B C   
818  O O   . LYS A 126 ? 1.1943 1.5832 1.7403 0.0433  0.0206  0.6228  312 LYS B O   
819  C CB  . LYS A 126 ? 1.1071 1.4733 1.6123 0.0394  0.0243  0.5766  312 LYS B CB  
820  C CG  . LYS A 126 ? 1.2263 1.5851 1.6965 0.0392  0.0274  0.5498  312 LYS B CG  
821  C CD  . LYS A 126 ? 1.1000 1.4344 1.5975 0.0400  0.0255  0.5343  312 LYS B CD  
822  C CE  . LYS A 126 ? 1.0333 1.3621 1.4966 0.0395  0.0276  0.5091  312 LYS B CE  
823  N NZ  . LYS A 126 ? 1.0579 1.3652 1.5469 0.0396  0.0265  0.4930  312 LYS B NZ  
824  N N   . GLY A 127 ? 1.1478 1.5793 1.6706 0.0247  0.0183  0.6546  313 GLY B N   
825  C CA  . GLY A 127 ? 1.0495 1.4963 1.6069 0.0206  0.0125  0.6893  313 GLY B CA  
826  C C   . GLY A 127 ? 1.0675 1.5381 1.6045 0.0214  0.0156  0.7002  313 GLY B C   
827  O O   . GLY A 127 ? 1.2191 1.7014 1.7861 0.0194  0.0103  0.7283  313 GLY B O   
828  N N   . THR A 128 ? 1.0604 1.5392 1.5486 0.0240  0.0239  0.6797  314 THR B N   
829  C CA  . THR A 128 ? 1.1378 1.6389 1.6033 0.0254  0.0287  0.6859  314 THR B CA  
830  C C   . THR A 128 ? 1.0528 1.5935 1.4828 0.0132  0.0337  0.6963  314 THR B C   
831  O O   . THR A 128 ? 1.0411 1.5898 1.4608 0.0045  0.0339  0.6945  314 THR B O   
832  C CB  . THR A 128 ? 1.1363 1.6154 1.5755 0.0385  0.0356  0.6518  314 THR B CB  
833  O OG1 . THR A 128 ? 1.1074 1.5863 1.5030 0.0379  0.0422  0.6272  314 THR B OG1 
834  C CG2 . THR A 128 ? 1.0714 1.5116 1.5447 0.0481  0.0317  0.6350  314 THR B CG2 
835  N N   . CYS A 129 ? 1.0576 1.6245 1.4699 0.0121  0.0385  0.7060  315 CYS B N   
836  C CA  . CYS A 129 ? 1.0022 1.6104 1.3812 0.0000  0.0455  0.7134  315 CYS B CA  
837  C C   . CYS A 129 ? 1.0168 1.6200 1.3523 0.0033  0.0550  0.6804  315 CYS B C   
838  O O   . CYS A 129 ? 1.0935 1.7264 1.4070 -0.0080 0.0603  0.6818  315 CYS B O   
839  C CB  . CYS A 129 ? 1.0034 1.6413 1.3756 -0.0016 0.0491  0.7306  315 CYS B CB  
840  S SG  . CYS A 129 ? 0.8595 1.4802 1.2000 0.0151  0.0587  0.7001  315 CYS B SG  
841  N N   . VAL A 130 ? 1.0451 1.6131 1.3693 0.0176  0.0571  0.6510  316 VAL B N   
842  C CA  . VAL A 130 ? 0.9853 1.5466 1.2696 0.0215  0.0651  0.6206  316 VAL B CA  
843  C C   . VAL A 130 ? 0.9983 1.5315 1.2876 0.0233  0.0608  0.6028  316 VAL B C   
844  O O   . VAL A 130 ? 0.8186 1.3377 1.0800 0.0285  0.0650  0.5761  316 VAL B O   
845  C CB  . VAL A 130 ? 0.9038 1.4498 1.1652 0.0342  0.0713  0.5994  316 VAL B CB  
846  C CG1 . VAL A 130 ? 0.9624 1.4651 1.2412 0.0459  0.0660  0.5807  316 VAL B CG1 
847  C CG2 . VAL A 130 ? 1.0140 1.5699 1.2302 0.0345  0.0816  0.5776  316 VAL B CG2 
848  N N   . GLU A 131 ? 1.0404 1.5674 1.3648 0.0182  0.0523  0.6186  317 GLU B N   
849  C CA  . GLU A 131 ? 1.0278 1.5278 1.3614 0.0200  0.0480  0.6028  317 GLU B CA  
850  C C   . GLU A 131 ? 0.9427 1.4537 1.2468 0.0141  0.0521  0.5888  317 GLU B C   
851  O O   . GLU A 131 ? 0.8167 1.3617 1.1086 0.0031  0.0557  0.6009  317 GLU B O   
852  C CB  . GLU A 131 ? 1.0768 1.5738 1.4542 0.0137  0.0392  0.6256  317 GLU B CB  
853  C CG  . GLU A 131 ? 1.0556 1.5265 1.4459 0.0149  0.0352  0.6105  317 GLU B CG  
854  C CD  . GLU A 131 ? 1.1223 1.5926 1.5554 0.0078  0.0273  0.6342  317 GLU B CD  
855  O OE1 . GLU A 131 ? 1.1028 1.6018 1.5461 -0.0029 0.0249  0.6635  317 GLU B OE1 
856  O OE2 . GLU A 131 ? 1.1940 1.6363 1.6512 0.0122  0.0238  0.6237  317 GLU B OE2 
857  N N   . GLY A 132 ? 1.0346 1.5183 1.3289 0.0207  0.0515  0.5627  318 GLY B N   
858  C CA  . GLY A 132 ? 0.8289 1.3188 1.0995 0.0165  0.0540  0.5481  318 GLY B CA  
859  C C   . GLY A 132 ? 0.8911 1.3909 1.1228 0.0197  0.0623  0.5317  318 GLY B C   
860  O O   . GLY A 132 ? 0.9043 1.4172 1.1188 0.0144  0.0653  0.5234  318 GLY B O   
861  N N   . THR A 133 ? 0.9181 1.4127 1.1374 0.0279  0.0664  0.5266  319 THR B N   
862  C CA  . THR A 133 ? 0.8391 1.3418 1.0213 0.0313  0.0749  0.5105  319 THR B CA  
863  C C   . THR A 133 ? 0.8715 1.3498 1.0346 0.0371  0.0739  0.4834  319 THR B C   
864  O O   . THR A 133 ? 0.9050 1.3949 1.0445 0.0350  0.0789  0.4729  319 THR B O   
865  C CB  . THR A 133 ? 0.9319 1.4317 1.1057 0.0390  0.0791  0.5102  319 THR B CB  
866  O OG1 . THR A 133 ? 0.8015 1.3316 0.9881 0.0322  0.0810  0.5365  319 THR B OG1 
867  C CG2 . THR A 133 ? 0.8781 1.3792 1.0128 0.0440  0.0877  0.4895  319 THR B CG2 
868  N N   . ILE A 134 ? 0.9301 1.3760 1.1049 0.0436  0.0677  0.4716  320 ILE B N   
869  C CA  . ILE A 134 ? 0.9063 1.3305 1.0640 0.0478  0.0656  0.4471  320 ILE B CA  
870  C C   . ILE A 134 ? 0.8649 1.2982 1.0235 0.0409  0.0633  0.4467  320 ILE B C   
871  O O   . ILE A 134 ? 0.8659 1.3013 1.0005 0.0415  0.0657  0.4326  320 ILE B O   
872  C CB  . ILE A 134 ? 0.9467 1.3387 1.1203 0.0537  0.0599  0.4349  320 ILE B CB  
873  C CG1 . ILE A 134 ? 1.0217 1.4009 1.1792 0.0613  0.0634  0.4216  320 ILE B CG1 
874  C CG2 . ILE A 134 ? 0.8852 1.2599 1.0536 0.0536  0.0552  0.4168  320 ILE B CG2 
875  C CD1 . ILE A 134 ? 0.9461 1.3367 1.1158 0.0627  0.0666  0.4380  320 ILE B CD1 
876  N N   . PRO A 135 ? 0.9186 1.3578 1.1046 0.0339  0.0586  0.4612  321 PRO B N   
877  C CA  . PRO A 135 ? 0.8094 1.2592 0.9950 0.0267  0.0569  0.4590  321 PRO B CA  
878  C C   . PRO A 135 ? 0.7870 1.2683 0.9547 0.0202  0.0641  0.4619  321 PRO B C   
879  O O   . PRO A 135 ? 0.9079 1.3920 1.0640 0.0184  0.0644  0.4491  321 PRO B O   
880  C CB  . PRO A 135 ? 0.8008 1.2541 1.0198 0.0196  0.0516  0.4772  321 PRO B CB  
881  C CG  . PRO A 135 ? 0.8088 1.2405 1.0476 0.0261  0.0485  0.4804  321 PRO B CG  
882  C CD  . PRO A 135 ? 1.0263 1.4600 1.2468 0.0325  0.0540  0.4781  321 PRO B CD  
883  N N   . LYS A 136 ? 0.7865 1.2929 0.9532 0.0161  0.0700  0.4777  322 LYS B N   
884  C CA  . LYS A 136 ? 0.8460 1.3867 0.9988 0.0078  0.0783  0.4795  322 LYS B CA  
885  C C   . LYS A 136 ? 0.8601 1.3974 0.9828 0.0151  0.0851  0.4603  322 LYS B C   
886  O O   . LYS A 136 ? 0.9108 1.4734 1.0232 0.0089  0.0924  0.4564  322 LYS B O   
887  C CB  . LYS A 136 ? 0.7471 1.3203 0.9084 -0.0008 0.0830  0.5030  322 LYS B CB  
888  C CG  . LYS A 136 ? 0.8373 1.4155 0.9812 0.0057  0.0902  0.5033  322 LYS B CG  
889  C CD  . LYS A 136 ? 0.8189 1.4321 0.9736 -0.0043 0.0938  0.5286  322 LYS B CD  
890  C CE  . LYS A 136 ? 0.8075 1.4622 0.9612 -0.0204 0.1001  0.5339  322 LYS B CE  
891  N NZ  . LYS A 136 ? 1.0164 1.7098 1.1797 -0.0326 0.1036  0.5594  322 LYS B NZ  
892  N N   . LEU A 137 ? 0.7871 1.2952 0.8969 0.0269  0.0833  0.4477  323 LEU B N   
893  C CA  . LEU A 137 ? 0.8208 1.3233 0.9013 0.0335  0.0888  0.4295  323 LEU B CA  
894  C C   . LEU A 137 ? 0.8607 1.3391 0.9330 0.0379  0.0828  0.4103  323 LEU B C   
895  O O   . LEU A 137 ? 0.7956 1.2794 0.8504 0.0386  0.0868  0.3985  323 LEU B O   
896  C CB  . LEU A 137 ? 0.7797 1.2683 0.8471 0.0424  0.0914  0.4265  323 LEU B CB  
897  C CG  . LEU A 137 ? 0.8435 1.3589 0.9093 0.0397  0.0999  0.4416  323 LEU B CG  
898  C CD1 . LEU A 137 ? 0.7488 1.2461 0.8050 0.0491  0.1008  0.4370  323 LEU B CD1 
899  C CD2 . LEU A 137 ? 0.8163 1.3615 0.8635 0.0348  0.1110  0.4378  323 LEU B CD2 
900  N N   . PHE A 138 ? 0.8100 1.2637 0.8964 0.0402  0.0733  0.4073  324 PHE B N   
901  C CA  . PHE A 138 ? 0.7953 1.2252 0.8718 0.0446  0.0671  0.3889  324 PHE B CA  
902  C C   . PHE A 138 ? 0.9075 1.3345 1.0018 0.0398  0.0598  0.3882  324 PHE B C   
903  O O   . PHE A 138 ? 1.0389 1.4532 1.1242 0.0419  0.0552  0.3740  324 PHE B O   
904  C CB  . PHE A 138 ? 0.8850 1.2854 0.9574 0.0518  0.0627  0.3791  324 PHE B CB  
905  C CG  . PHE A 138 ? 0.8486 1.2475 0.9018 0.0572  0.0690  0.3761  324 PHE B CG  
906  C CD1 . PHE A 138 ? 0.7803 1.1729 0.8040 0.0613  0.0716  0.3609  324 PHE B CD1 
907  C CD2 . PHE A 138 ? 0.8309 1.2345 0.8967 0.0579  0.0719  0.3884  324 PHE B CD2 
908  C CE1 . PHE A 138 ? 0.8432 1.2341 0.8479 0.0659  0.0778  0.3569  324 PHE B CE1 
909  C CE2 . PHE A 138 ? 0.8778 1.2803 0.9262 0.0629  0.0777  0.3845  324 PHE B CE2 
910  C CZ  . PHE A 138 ? 1.0075 1.4036 1.0242 0.0669  0.0811  0.3679  324 PHE B CZ  
911  N N   . ARG A 139 ? 0.9060 1.3443 1.0252 0.0330  0.0583  0.4030  325 ARG B N   
912  C CA  . ARG A 139 ? 0.9464 1.3794 1.0824 0.0287  0.0513  0.4009  325 ARG B CA  
913  C C   . ARG A 139 ? 1.0186 1.4771 1.1565 0.0203  0.0538  0.4021  325 ARG B C   
914  O O   . ARG A 139 ? 0.9003 1.3867 1.0383 0.0139  0.0611  0.4123  325 ARG B O   
915  C CB  . ARG A 139 ? 0.9363 1.3645 1.1001 0.0257  0.0475  0.4145  325 ARG B CB  
916  C CG  . ARG A 139 ? 1.0487 1.4647 1.2286 0.0231  0.0402  0.4089  325 ARG B CG  
917  C CD  . ARG A 139 ? 1.0943 1.5054 1.3038 0.0198  0.0371  0.4225  325 ARG B CD  
918  N NE  . ARG A 139 ? 1.1321 1.5694 1.3560 0.0100  0.0393  0.4430  325 ARG B NE  
919  C CZ  . ARG A 139 ? 1.1445 1.5820 1.3951 0.0054  0.0366  0.4590  325 ARG B CZ  
920  N NH1 . ARG A 139 ? 1.1539 1.5667 1.4228 0.0102  0.0324  0.4558  325 ARG B NH1 
921  N NH2 . ARG A 139 ? 1.1473 1.6120 1.4081 -0.0054 0.0384  0.4785  325 ARG B NH2 
922  N N   . GLY A 140 ? 0.9548 1.4052 1.0957 0.0196  0.0480  0.3907  326 GLY B N   
923  C CA  . GLY A 140 ? 0.8906 1.3630 1.0372 0.0115  0.0495  0.3886  326 GLY B CA  
924  C C   . GLY A 140 ? 0.9094 1.3754 1.0746 0.0071  0.0419  0.3863  326 GLY B C   
925  O O   . GLY A 140 ? 0.9825 1.4243 1.1527 0.0118  0.0353  0.3825  326 GLY B O   
926  N N   . LYS A 141 ? 0.7684 1.2581 0.9446 -0.0029 0.0437  0.3872  327 LYS B N   
927  C CA  . LYS A 141 ? 0.8337 1.3215 1.0277 -0.0087 0.0374  0.3846  327 LYS B CA  
928  C C   . LYS A 141 ? 0.8804 1.3605 1.0706 -0.0057 0.0326  0.3666  327 LYS B C   
929  O O   . LYS A 141 ? 0.9289 1.4206 1.1110 -0.0054 0.0364  0.3590  327 LYS B O   
930  C CB  . LYS A 141 ? 0.9085 1.4280 1.1186 -0.0235 0.0415  0.3957  327 LYS B CB  
931  C CG  . LYS A 141 ? 0.8093 1.3374 1.0279 -0.0284 0.0439  0.4168  327 LYS B CG  
932  C CD  . LYS A 141 ? 0.8794 1.4427 1.1122 -0.0456 0.0475  0.4277  327 LYS B CD  
933  C CE  . LYS A 141 ? 0.9635 1.5373 1.2061 -0.0516 0.0487  0.4516  327 LYS B CE  
934  N NZ  . LYS A 141 ? 0.9329 1.5445 1.1878 -0.0708 0.0519  0.4636  327 LYS B NZ  
935  N N   . MET A 142 ? 0.9352 1.3958 1.1328 -0.0034 0.0244  0.3600  328 MET B N   
936  C CA  . MET A 142 ? 0.8412 1.2922 1.0366 0.0000  0.0179  0.3442  328 MET B CA  
937  C C   . MET A 142 ? 0.8975 1.3437 1.1103 -0.0047 0.0117  0.3409  328 MET B C   
938  O O   . MET A 142 ? 0.9680 1.4054 1.1898 -0.0058 0.0106  0.3483  328 MET B O   
939  C CB  . MET A 142 ? 0.7796 1.2050 0.9565 0.0112  0.0136  0.3364  328 MET B CB  
940  C CG  . MET A 142 ? 0.7834 1.1978 0.9575 0.0147  0.0053  0.3223  328 MET B CG  
941  S SD  . MET A 142 ? 0.8605 1.2469 1.0129 0.0246  -0.0003 0.3152  328 MET B SD  
942  C CE  . MET A 142 ? 0.7885 1.1816 0.9199 0.0287  0.0075  0.3182  328 MET B CE  
943  N N   . VAL A 143 ? 0.9049 1.3573 1.1243 -0.0074 0.0079  0.3296  329 VAL B N   
944  C CA  . VAL A 143 ? 0.8686 1.3173 1.1035 -0.0117 0.0019  0.3239  329 VAL B CA  
945  C C   . VAL A 143 ? 0.8227 1.2526 1.0522 -0.0042 -0.0070 0.3099  329 VAL B C   
946  O O   . VAL A 143 ? 0.7804 1.2120 1.0028 -0.0005 -0.0088 0.3027  329 VAL B O   
947  C CB  . VAL A 143 ? 0.7671 1.2428 1.0185 -0.0241 0.0047  0.3223  329 VAL B CB  
948  C CG1 . VAL A 143 ? 0.7545 1.2458 1.0047 -0.0246 0.0071  0.3133  329 VAL B CG1 
949  C CG2 . VAL A 143 ? 0.7730 1.2434 1.0387 -0.0278 -0.0018 0.3141  329 VAL B CG2 
950  N N   . SER A 144 ? 0.8260 1.2389 1.0598 -0.0024 -0.0123 0.3068  330 SER B N   
951  C CA  . SER A 144 ? 0.8154 1.2137 1.0465 0.0024  -0.0213 0.2941  330 SER B CA  
952  C C   . SER A 144 ? 0.8915 1.2959 1.1406 -0.0039 -0.0249 0.2874  330 SER B C   
953  O O   . SER A 144 ? 0.9342 1.3390 1.1946 -0.0090 -0.0226 0.2919  330 SER B O   
954  C CB  . SER A 144 ? 0.8971 1.2734 1.1191 0.0083  -0.0237 0.2931  330 SER B CB  
955  O OG  . SER A 144 ? 0.9246 1.2902 1.1429 0.0114  -0.0324 0.2813  330 SER B OG  
956  N N   . TYR A 145 ? 0.8602 1.2693 1.1134 -0.0038 -0.0309 0.2767  331 TYR B N   
957  C CA  . TYR A 145 ? 0.8287 1.2464 1.0997 -0.0103 -0.0340 0.2686  331 TYR B CA  
958  C C   . TYR A 145 ? 0.8393 1.2443 1.1106 -0.0057 -0.0442 0.2568  331 TYR B C   
959  O O   . TYR A 145 ? 0.8184 1.2146 1.0781 0.0012  -0.0499 0.2541  331 TYR B O   
960  C CB  . TYR A 145 ? 0.8237 1.2653 1.1069 -0.0173 -0.0309 0.2654  331 TYR B CB  
961  C CG  . TYR A 145 ? 0.8240 1.2674 1.1044 -0.0120 -0.0348 0.2589  331 TYR B CG  
962  C CD1 . TYR A 145 ? 0.9074 1.3482 1.1979 -0.0101 -0.0440 0.2470  331 TYR B CD1 
963  C CD2 . TYR A 145 ? 0.7869 1.2350 1.0563 -0.0089 -0.0292 0.2649  331 TYR B CD2 
964  C CE1 . TYR A 145 ? 0.8902 1.3324 1.1818 -0.0053 -0.0483 0.2425  331 TYR B CE1 
965  C CE2 . TYR A 145 ? 0.8457 1.2952 1.1147 -0.0042 -0.0325 0.2594  331 TYR B CE2 
966  C CZ  . TYR A 145 ? 0.8731 1.3192 1.1542 -0.0024 -0.0423 0.2487  331 TYR B CZ  
967  O OH  . TYR A 145 ? 0.8736 1.3205 1.1576 0.0022  -0.0465 0.2445  331 TYR B OH  
968  N N   . ILE A 146 ? 0.8364 1.2417 1.1207 -0.0103 -0.0467 0.2503  332 ILE B N   
969  C CA  . ILE A 146 ? 0.8575 1.2557 1.1457 -0.0079 -0.0561 0.2382  332 ILE B CA  
970  C C   . ILE A 146 ? 0.8784 1.2911 1.1865 -0.0156 -0.0572 0.2295  332 ILE B C   
971  O O   . ILE A 146 ? 0.9175 1.3345 1.2343 -0.0227 -0.0524 0.2304  332 ILE B O   
972  C CB  . ILE A 146 ? 0.8321 1.2139 1.1151 -0.0054 -0.0576 0.2364  332 ILE B CB  
973  C CG1 . ILE A 146 ? 0.8706 1.2396 1.1356 0.0006  -0.0559 0.2432  332 ILE B CG1 
974  C CG2 . ILE A 146 ? 0.8410 1.2188 1.1273 -0.0038 -0.0673 0.2241  332 ILE B CG2 
975  C CD1 . ILE A 146 ? 0.8505 1.2061 1.1141 0.0013  -0.0552 0.2402  332 ILE B CD1 
976  N N   . GLN A 147 ? 0.8918 1.3122 1.2086 -0.0150 -0.0635 0.2207  333 GLN B N   
977  C CA  . GLN A 147 ? 0.8634 1.2997 1.2015 -0.0229 -0.0644 0.2100  333 GLN B CA  
978  C C   . GLN A 147 ? 0.8592 1.2894 1.2052 -0.0198 -0.0753 0.1975  333 GLN B C   
979  O O   . GLN A 147 ? 0.8656 1.2906 1.2092 -0.0129 -0.0836 0.1957  333 GLN B O   
980  C CB  . GLN A 147 ? 0.8505 1.3054 1.1993 -0.0264 -0.0612 0.2087  333 GLN B CB  
981  C CG  . GLN A 147 ? 0.7756 1.2487 1.1498 -0.0352 -0.0626 0.1944  333 GLN B CG  
982  C CD  . GLN A 147 ? 0.7803 1.2663 1.1623 -0.0479 -0.0554 0.1934  333 GLN B CD  
983  O OE1 . GLN A 147 ? 0.8089 1.3081 1.1887 -0.0551 -0.0461 0.2021  333 GLN B OE1 
984  N NE2 . GLN A 147 ? 0.7776 1.2614 1.1690 -0.0514 -0.0598 0.1828  333 GLN B NE2 
985  N N   . CYS A 148 ? 0.8630 1.2949 1.2188 -0.0254 -0.0756 0.1893  334 CYS B N   
986  C CA  . CYS A 148 ? 0.8771 1.3066 1.2428 -0.0238 -0.0853 0.1762  334 CYS B CA  
987  C C   . CYS A 148 ? 0.9165 1.3623 1.3045 -0.0277 -0.0890 0.1656  334 CYS B C   
988  O O   . CYS A 148 ? 0.9545 1.4168 1.3538 -0.0362 -0.0818 0.1643  334 CYS B O   
989  C CB  . CYS A 148 ? 0.8778 1.3046 1.2471 -0.0291 -0.0829 0.1698  334 CYS B CB  
990  S SG  . CYS A 148 ? 0.8329 1.2410 1.1837 -0.0252 -0.0782 0.1786  334 CYS B SG  
991  N N   . LYS A 149 ? 0.9054 1.3481 1.3017 -0.0224 -0.1005 0.1579  335 LYS B N   
992  C CA  . LYS A 149 ? 0.9262 1.3832 1.3481 -0.0249 -0.1049 0.1475  335 LYS B CA  
993  C C   . LYS A 149 ? 0.9422 1.4088 1.3855 -0.0321 -0.1076 0.1306  335 LYS B C   
994  O O   . LYS A 149 ? 0.9815 1.4656 1.4481 -0.0399 -0.1050 0.1203  335 LYS B O   
995  C CB  . LYS A 149 ? 0.9826 1.4325 1.4064 -0.0152 -0.1170 0.1499  335 LYS B CB  
996  C CG  . LYS A 149 ? 1.1094 1.5487 1.5304 -0.0101 -0.1293 0.1460  335 LYS B CG  
997  C CD  . LYS A 149 ? 1.2026 1.6371 1.6265 -0.0021 -0.1421 0.1510  335 LYS B CD  
998  C CE  . LYS A 149 ? 1.1313 1.5585 1.5520 0.0013  -0.1547 0.1482  335 LYS B CE  
999  N NZ  . LYS A 149 ? 1.0481 1.4730 1.4750 0.0076  -0.1690 0.1541  335 LYS B NZ  
1000 N N   . GLU A 150 ? 0.9240 1.3809 1.3611 -0.0306 -0.1120 0.1259  336 GLU B N   
1001 C CA  . GLU A 150 ? 0.8929 1.3577 1.3486 -0.0369 -0.1148 0.1088  336 GLU B CA  
1002 C C   . GLU A 150 ? 0.8580 1.3266 1.3095 -0.0469 -0.1044 0.1059  336 GLU B C   
1003 O O   . GLU A 150 ? 0.9109 1.3927 1.3803 -0.0565 -0.1028 0.0916  336 GLU B O   
1004 C CB  . GLU A 150 ? 0.8880 1.3426 1.3422 -0.0299 -0.1266 0.1034  336 GLU B CB  
1005 C CG  . GLU A 150 ? 0.8892 1.3409 1.3497 -0.0210 -0.1392 0.1073  336 GLU B CG  
1006 C CD  . GLU A 150 ? 1.0906 1.5339 1.5459 -0.0152 -0.1510 0.1051  336 GLU B CD  
1007 O OE1 . GLU A 150 ? 1.1553 1.5949 1.6015 -0.0177 -0.1480 0.0994  336 GLU B OE1 
1008 O OE2 . GLU A 150 ? 1.1474 1.5890 1.6083 -0.0089 -0.1631 0.1093  336 GLU B OE2 
1009 N N   . VAL A 151 ? 0.9266 1.3841 1.3566 -0.0454 -0.0976 0.1186  337 VAL B N   
1010 C CA  . VAL A 151 ? 0.9668 1.4268 1.3934 -0.0547 -0.0878 0.1195  337 VAL B CA  
1011 C C   . VAL A 151 ? 0.9005 1.3693 1.3229 -0.0605 -0.0782 0.1327  337 VAL B C   
1012 O O   . VAL A 151 ? 0.8354 1.3025 1.2504 -0.0546 -0.0779 0.1433  337 VAL B O   
1013 C CB  . VAL A 151 ? 0.9315 1.3738 1.3421 -0.0497 -0.0866 0.1240  337 VAL B CB  
1014 C CG1 . VAL A 151 ? 0.9345 1.3780 1.3450 -0.0591 -0.0771 0.1252  337 VAL B CG1 
1015 C CG2 . VAL A 151 ? 0.8315 1.2683 1.2455 -0.0445 -0.0961 0.1111  337 VAL B CG2 
1016 N N   . ASP A 152 ? 0.9531 1.4330 1.3805 -0.0730 -0.0705 0.1319  338 ASP B N   
1017 C CA  . ASP A 152 ? 1.0586 1.5528 1.4850 -0.0820 -0.0615 0.1435  338 ASP B CA  
1018 C C   . ASP A 152 ? 1.0105 1.4912 1.4191 -0.0786 -0.0556 0.1626  338 ASP B C   
1019 O O   . ASP A 152 ? 0.9841 1.4673 1.3925 -0.0873 -0.0497 0.1686  338 ASP B O   
1020 C CB  . ASP A 152 ? 1.1672 1.6828 1.6089 -0.0994 -0.0570 0.1332  338 ASP B CB  
1021 C CG  . ASP A 152 ? 1.3395 1.8771 1.7835 -0.1115 -0.0485 0.1427  338 ASP B CG  
1022 O OD1 . ASP A 152 ? 1.4243 1.9584 1.8564 -0.1058 -0.0451 0.1590  338 ASP B OD1 
1023 O OD2 . ASP A 152 ? 1.3343 1.8940 1.7917 -0.1280 -0.0449 0.1333  338 ASP B OD2 
1024 N N   . TYR A 153 ? 0.8895 1.3559 1.2845 -0.0662 -0.0575 0.1724  339 TYR B N   
1025 C CA  . TYR A 153 ? 0.8933 1.3480 1.2742 -0.0627 -0.0518 0.1898  339 TYR B CA  
1026 C C   . TYR A 153 ? 0.8590 1.3114 1.2285 -0.0549 -0.0512 0.2006  339 TYR B C   
1027 O O   . TYR A 153 ? 0.8222 1.2713 1.1896 -0.0471 -0.0576 0.1951  339 TYR B O   
1028 C CB  . TYR A 153 ? 0.8934 1.3270 1.2677 -0.0555 -0.0539 0.1883  339 TYR B CB  
1029 C CG  . TYR A 153 ? 0.8536 1.2749 1.2183 -0.0521 -0.0478 0.2044  339 TYR B CG  
1030 C CD1 . TYR A 153 ? 0.8331 1.2570 1.2037 -0.0604 -0.0408 0.2138  339 TYR B CD1 
1031 C CD2 . TYR A 153 ? 0.8350 1.2426 1.1866 -0.0414 -0.0495 0.2099  339 TYR B CD2 
1032 C CE1 . TYR A 153 ? 0.8675 1.2801 1.2338 -0.0571 -0.0358 0.2286  339 TYR B CE1 
1033 C CE2 . TYR A 153 ? 0.8410 1.2378 1.1870 -0.0386 -0.0438 0.2227  339 TYR B CE2 
1034 C CZ  . TYR A 153 ? 0.8849 1.2840 1.2397 -0.0460 -0.0370 0.2321  339 TYR B CZ  
1035 O OH  . TYR A 153 ? 0.8770 1.2652 1.2305 -0.0430 -0.0319 0.2451  339 TYR B OH  
1036 N N   . ARG A 154 ? 0.8111 1.2656 1.1739 -0.0573 -0.0438 0.2166  340 ARG B N   
1037 C CA  . ARG A 154 ? 0.8016 1.2536 1.1518 -0.0504 -0.0417 0.2279  340 ARG B CA  
1038 C C   . ARG A 154 ? 0.8088 1.2505 1.1507 -0.0489 -0.0359 0.2439  340 ARG B C   
1039 O O   . ARG A 154 ? 0.8184 1.2639 1.1677 -0.0572 -0.0317 0.2499  340 ARG B O   
1040 C CB  . ARG A 154 ? 0.7870 1.2628 1.1432 -0.0578 -0.0373 0.2292  340 ARG B CB  
1041 C CG  . ARG A 154 ? 0.7826 1.2570 1.1258 -0.0503 -0.0349 0.2385  340 ARG B CG  
1042 C CD  . ARG A 154 ? 0.7677 1.2691 1.1188 -0.0598 -0.0282 0.2396  340 ARG B CD  
1043 N NE  . ARG A 154 ? 0.7626 1.2638 1.1021 -0.0525 -0.0253 0.2464  340 ARG B NE  
1044 C CZ  . ARG A 154 ? 0.7566 1.2597 1.0989 -0.0472 -0.0284 0.2379  340 ARG B CZ  
1045 N NH1 . ARG A 154 ? 0.7547 1.2605 1.1129 -0.0479 -0.0351 0.2228  340 ARG B NH1 
1046 N NH2 . ARG A 154 ? 0.7528 1.2550 1.0830 -0.0410 -0.0250 0.2449  340 ARG B NH2 
1047 N N   . SER A 155 ? 0.8122 1.2407 1.1400 -0.0389 -0.0361 0.2508  341 SER B N   
1048 C CA  . SER A 155 ? 0.8611 1.2790 1.1833 -0.0364 -0.0309 0.2649  341 SER B CA  
1049 C C   . SER A 155 ? 0.8121 1.2354 1.1231 -0.0333 -0.0270 0.2758  341 SER B C   
1050 O O   . SER A 155 ? 0.8119 1.2274 1.1104 -0.0247 -0.0301 0.2725  341 SER B O   
1051 C CB  . SER A 155 ? 0.8315 1.2268 1.1485 -0.0279 -0.0340 0.2602  341 SER B CB  
1052 O OG  . SER A 155 ? 0.8376 1.2231 1.1537 -0.0259 -0.0286 0.2724  341 SER B OG  
1053 N N   . ASP A 156 ? 0.8071 1.2445 1.1221 -0.0410 -0.0204 0.2892  342 ASP B N   
1054 C CA  . ASP A 156 ? 0.8389 1.2842 1.1442 -0.0394 -0.0153 0.3006  342 ASP B CA  
1055 C C   . ASP A 156 ? 0.9142 1.3484 1.2180 -0.0369 -0.0116 0.3158  342 ASP B C   
1056 O O   . ASP A 156 ? 0.9617 1.3996 1.2779 -0.0444 -0.0093 0.3251  342 ASP B O   
1057 C CB  . ASP A 156 ? 0.7872 1.2622 1.0995 -0.0516 -0.0103 0.3041  342 ASP B CB  
1058 C CG  . ASP A 156 ? 0.7931 1.2800 1.1084 -0.0527 -0.0127 0.2888  342 ASP B CG  
1059 O OD1 . ASP A 156 ? 0.7888 1.2615 1.0956 -0.0418 -0.0176 0.2808  342 ASP B OD1 
1060 O OD2 . ASP A 156 ? 0.8456 1.3566 1.1735 -0.0651 -0.0100 0.2845  342 ASP B OD2 
1061 N N   . ARG A 157 ? 0.8822 1.3029 1.1725 -0.0268 -0.0112 0.3182  343 ARG B N   
1062 C CA  . ARG A 157 ? 0.9788 1.3895 1.2693 -0.0237 -0.0075 0.3315  343 ARG B CA  
1063 C C   . ARG A 157 ? 1.0509 1.4670 1.3267 -0.0195 -0.0035 0.3388  343 ARG B C   
1064 O O   . ARG A 157 ? 0.9305 1.3449 1.1918 -0.0137 -0.0052 0.3299  343 ARG B O   
1065 C CB  . ARG A 157 ? 0.9813 1.3670 1.2727 -0.0160 -0.0105 0.3241  343 ARG B CB  
1066 C CG  . ARG A 157 ? 1.0903 1.4653 1.3659 -0.0080 -0.0156 0.3095  343 ARG B CG  
1067 C CD  . ARG A 157 ? 1.0753 1.4306 1.3540 -0.0038 -0.0182 0.3004  343 ARG B CD  
1068 N NE  . ARG A 157 ? 1.1075 1.4542 1.3693 0.0024  -0.0234 0.2886  343 ARG B NE  
1069 C CZ  . ARG A 157 ? 1.0478 1.3866 1.2951 0.0079  -0.0226 0.2892  343 ARG B CZ  
1070 N NH1 . ARG A 157 ? 1.1379 1.4756 1.3858 0.0089  -0.0166 0.3003  343 ARG B NH1 
1071 N NH2 . ARG A 157 ? 1.1432 1.4754 1.3751 0.0117  -0.0283 0.2788  343 ARG B NH2 
1072 N N   . ARG A 158 ? 1.2074 1.6303 1.4877 -0.0226 0.0016  0.3556  344 ARG B N   
1073 C CA  . ARG A 158 ? 1.2180 1.6483 1.4854 -0.0196 0.0064  0.3639  344 ARG B CA  
1074 C C   . ARG A 158 ? 1.2657 1.6728 1.5242 -0.0086 0.0059  0.3625  344 ARG B C   
1075 O O   . ARG A 158 ? 1.3353 1.7266 1.6056 -0.0066 0.0048  0.3647  344 ARG B O   
1076 C CB  . ARG A 158 ? 1.3961 1.8469 1.6734 -0.0291 0.0116  0.3836  344 ARG B CB  
1077 C CG  . ARG A 158 ? 1.5347 1.9954 1.7998 -0.0267 0.0174  0.3936  344 ARG B CG  
1078 C CD  . ARG A 158 ? 1.6269 2.1117 1.9032 -0.0380 0.0217  0.4145  344 ARG B CD  
1079 N NE  . ARG A 158 ? 1.4945 1.9664 1.7884 -0.0384 0.0193  0.4278  344 ARG B NE  
1080 C CZ  . ARG A 158 ? 1.5249 1.9796 1.8209 -0.0298 0.0195  0.4348  344 ARG B CZ  
1081 N NH1 . ARG A 158 ? 1.3737 1.8212 1.6522 -0.0203 0.0220  0.4295  344 ARG B NH1 
1082 N NH2 . ARG A 158 ? 1.5229 1.9668 1.8405 -0.0310 0.0174  0.4464  344 ARG B NH2 
1083 N N   . GLU A 159 ? 1.0680 1.4738 1.3070 -0.0022 0.0072  0.3577  345 GLU B N   
1084 C CA  . GLU A 159 ? 1.0226 1.4096 1.2508 0.0068  0.0075  0.3556  345 GLU B CA  
1085 C C   . GLU A 159 ? 1.0747 1.4719 1.2913 0.0084  0.0138  0.3656  345 GLU B C   
1086 O O   . GLU A 159 ? 1.0484 1.4668 1.2594 0.0042  0.0177  0.3694  345 GLU B O   
1087 C CB  . GLU A 159 ? 0.8754 1.2475 1.0874 0.0133  0.0022  0.3384  345 GLU B CB  
1088 C CG  . GLU A 159 ? 0.8942 1.2555 1.1160 0.0124  -0.0041 0.3274  345 GLU B CG  
1089 C CD  . GLU A 159 ? 0.8611 1.2076 1.0670 0.0180  -0.0097 0.3128  345 GLU B CD  
1090 O OE1 . GLU A 159 ? 0.9595 1.2964 1.1520 0.0227  -0.0083 0.3112  345 GLU B OE1 
1091 O OE2 . GLU A 159 ? 1.0503 1.3959 1.2573 0.0170  -0.0157 0.3031  345 GLU B OE2 
1092 N N   . ASP A 160 ? 1.0246 1.4079 1.2396 0.0140  0.0154  0.3688  346 ASP B N   
1093 C CA  . ASP A 160 ? 0.9513 1.3402 1.1529 0.0173  0.0209  0.3756  346 ASP B CA  
1094 C C   . ASP A 160 ? 0.9462 1.3172 1.1266 0.0258  0.0194  0.3611  346 ASP B C   
1095 O O   . ASP A 160 ? 0.9084 1.2605 1.0902 0.0285  0.0146  0.3498  346 ASP B O   
1096 C CB  . ASP A 160 ? 1.0133 1.4018 1.2316 0.0165  0.0238  0.3915  346 ASP B CB  
1097 C CG  . ASP A 160 ? 1.0783 1.4906 1.3127 0.0066  0.0261  0.4099  346 ASP B CG  
1098 O OD1 . ASP A 160 ? 1.0802 1.5134 1.3086 0.0002  0.0278  0.4096  346 ASP B OD1 
1099 O OD2 . ASP A 160 ? 1.0648 1.4761 1.3192 0.0043  0.0262  0.4246  346 ASP B OD2 
1100 N N   . TYR A 161 ? 0.9670 1.3455 1.1272 0.0287  0.0239  0.3611  347 TYR B N   
1101 C CA  . TYR A 161 ? 0.9642 1.3275 1.1018 0.0355  0.0228  0.3484  347 TYR B CA  
1102 C C   . TYR A 161 ? 0.9977 1.3661 1.1221 0.0388  0.0299  0.3543  347 TYR B C   
1103 O O   . TYR A 161 ? 0.9538 1.3432 1.0796 0.0357  0.0360  0.3659  347 TYR B O   
1104 C CB  . TYR A 161 ? 0.8819 1.2473 1.0041 0.0362  0.0192  0.3373  347 TYR B CB  
1105 C CG  . TYR A 161 ? 0.8353 1.2237 0.9523 0.0337  0.0250  0.3421  347 TYR B CG  
1106 C CD1 . TYR A 161 ? 0.8506 1.2581 0.9846 0.0265  0.0258  0.3471  347 TYR B CD1 
1107 C CD2 . TYR A 161 ? 0.8680 1.2605 0.9644 0.0375  0.0304  0.3401  347 TYR B CD2 
1108 C CE1 . TYR A 161 ? 0.8683 1.2997 1.0005 0.0224  0.0321  0.3493  347 TYR B CE1 
1109 C CE2 . TYR A 161 ? 0.8503 1.2658 0.9446 0.0344  0.0371  0.3428  347 TYR B CE2 
1110 C CZ  . TYR A 161 ? 0.8243 1.2601 0.9376 0.0265  0.0381  0.3471  347 TYR B CZ  
1111 O OH  . TYR A 161 ? 0.7791 1.2406 0.8931 0.0218  0.0459  0.3478  347 TYR B OH  
1112 N N   . TYR A 162 ? 1.0027 1.3534 1.1144 0.0442  0.0293  0.3453  348 TYR B N   
1113 C CA  . TYR A 162 ? 0.8757 1.2284 0.9703 0.0482  0.0356  0.3467  348 TYR B CA  
1114 C C   . TYR A 162 ? 0.9096 1.2556 0.9745 0.0519  0.0350  0.3329  348 TYR B C   
1115 O O   . TYR A 162 ? 0.9540 1.3032 1.0011 0.0551  0.0410  0.3327  348 TYR B O   
1116 C CB  . TYR A 162 ? 0.9343 1.2728 1.0396 0.0506  0.0361  0.3471  348 TYR B CB  
1117 C CG  . TYR A 162 ? 0.9957 1.3433 1.1294 0.0477  0.0382  0.3649  348 TYR B CG  
1118 C CD1 . TYR A 162 ? 1.0378 1.3797 1.1987 0.0442  0.0337  0.3683  348 TYR B CD1 
1119 C CD2 . TYR A 162 ? 0.9889 1.3518 1.1227 0.0479  0.0445  0.3790  348 TYR B CD2 
1120 C CE1 . TYR A 162 ? 1.0384 1.3885 1.2265 0.0409  0.0349  0.3863  348 TYR B CE1 
1121 C CE2 . TYR A 162 ? 1.0096 1.3821 1.1701 0.0443  0.0452  0.3977  348 TYR B CE2 
1122 C CZ  . TYR A 162 ? 1.0741 1.4396 1.2621 0.0407  0.0400  0.4017  348 TYR B CZ  
1123 O OH  . TYR A 162 ? 1.1926 1.5674 1.4082 0.0365  0.0401  0.4219  348 TYR B OH  
1124 N N   . ASP A 163 ? 0.8766 1.2140 0.9360 0.0512  0.0279  0.3222  349 ASP B N   
1125 C CA  . ASP A 163 ? 0.8163 1.1467 0.8493 0.0538  0.0256  0.3106  349 ASP B CA  
1126 C C   . ASP A 163 ? 0.8179 1.1480 0.8540 0.0516  0.0176  0.3055  349 ASP B C   
1127 O O   . ASP A 163 ? 0.8212 1.1504 0.8770 0.0485  0.0130  0.3067  349 ASP B O   
1128 C CB  . ASP A 163 ? 0.8286 1.1398 0.8484 0.0554  0.0233  0.2992  349 ASP B CB  
1129 C CG  . ASP A 163 ? 0.9716 1.2712 1.0120 0.0525  0.0185  0.2952  349 ASP B CG  
1130 O OD1 . ASP A 163 ? 1.0255 1.3313 1.0911 0.0506  0.0186  0.3043  349 ASP B OD1 
1131 O OD2 . ASP A 163 ? 1.0248 1.3105 1.0572 0.0513  0.0151  0.2823  349 ASP B OD2 
1132 N N   . ILE A 164 ? 0.8522 1.1829 0.8695 0.0532  0.0159  0.2999  350 ILE B N   
1133 C CA  . ILE A 164 ? 0.8167 1.1485 0.8373 0.0517  0.0080  0.2960  350 ILE B CA  
1134 C C   . ILE A 164 ? 0.8282 1.1451 0.8268 0.0526  0.0004  0.2858  350 ILE B C   
1135 O O   . ILE A 164 ? 0.8277 1.1423 0.8045 0.0552  0.0036  0.2833  350 ILE B O   
1136 C CB  . ILE A 164 ? 0.8021 1.1531 0.8274 0.0515  0.0129  0.3005  350 ILE B CB  
1137 C CG1 . ILE A 164 ? 0.7913 1.1606 0.8383 0.0478  0.0199  0.3106  350 ILE B CG1 
1138 C CG2 . ILE A 164 ? 0.8037 1.1545 0.8352 0.0505  0.0039  0.2955  350 ILE B CG2 
1139 C CD1 . ILE A 164 ? 0.8915 1.2600 0.9610 0.0437  0.0136  0.3116  350 ILE B CD1 
1140 N N   . GLN A 165 ? 0.8389 1.1470 0.8425 0.0498  -0.0096 0.2801  351 GLN B N   
1141 C CA  . GLN A 165 ? 0.8512 1.1480 0.8352 0.0483  -0.0185 0.2716  351 GLN B CA  
1142 C C   . GLN A 165 ? 0.8489 1.1512 0.8348 0.0486  -0.0256 0.2730  351 GLN B C   
1143 O O   . GLN A 165 ? 0.9292 1.2364 0.9348 0.0470  -0.0307 0.2744  351 GLN B O   
1144 C CB  . GLN A 165 ? 0.8646 1.1515 0.8536 0.0434  -0.0250 0.2639  351 GLN B CB  
1145 C CG  . GLN A 165 ? 0.8678 1.1485 0.8595 0.0427  -0.0182 0.2607  351 GLN B CG  
1146 C CD  . GLN A 165 ? 0.8629 1.1498 0.8814 0.0441  -0.0118 0.2690  351 GLN B CD  
1147 O OE1 . GLN A 165 ? 0.9739 1.2633 1.0123 0.0418  -0.0153 0.2703  351 GLN B OE1 
1148 N NE2 . GLN A 165 ? 0.8673 1.1578 0.8862 0.0472  -0.0025 0.2754  351 GLN B NE2 
1149 N N   . LEU A 166 ? 0.8499 1.1512 0.8168 0.0506  -0.0261 0.2724  352 LEU B N   
1150 C CA  . LEU A 166 ? 0.8452 1.1525 0.8174 0.0517  -0.0316 0.2748  352 LEU B CA  
1151 C C   . LEU A 166 ? 0.8607 1.1581 0.8201 0.0486  -0.0454 0.2713  352 LEU B C   
1152 O O   . LEU A 166 ? 0.9014 1.1889 0.8366 0.0463  -0.0477 0.2669  352 LEU B O   
1153 C CB  . LEU A 166 ? 0.8338 1.1489 0.7978 0.0557  -0.0221 0.2775  352 LEU B CB  
1154 C CG  . LEU A 166 ? 0.8164 1.1480 0.7961 0.0571  -0.0089 0.2823  352 LEU B CG  
1155 C CD1 . LEU A 166 ? 0.9036 1.2443 0.8743 0.0601  0.0004  0.2830  352 LEU B CD1 
1156 C CD2 . LEU A 166 ? 0.8091 1.1526 0.8189 0.0548  -0.0114 0.2846  352 LEU B CD2 
1157 N N   . SER A 167 ? 0.8618 1.1630 0.8381 0.0478  -0.0549 0.2732  353 SER B N   
1158 C CA  . SER A 167 ? 0.8761 1.1711 0.8431 0.0445  -0.0693 0.2726  353 SER B CA  
1159 C C   . SER A 167 ? 0.8761 1.1698 0.8289 0.0470  -0.0699 0.2758  353 SER B C   
1160 O O   . SER A 167 ? 0.8622 1.1638 0.8242 0.0517  -0.0612 0.2784  353 SER B O   
1161 C CB  . SER A 167 ? 0.8765 1.1770 0.8689 0.0434  -0.0793 0.2743  353 SER B CB  
1162 O OG  . SER A 167 ? 1.0380 1.3339 1.0225 0.0395  -0.0943 0.2753  353 SER B OG  
1163 N N   . ILE A 168 ? 0.8920 1.1772 0.8229 0.0426  -0.0802 0.2751  354 ILE B N   
1164 C CA  . ILE A 168 ? 0.8952 1.1768 0.8081 0.0438  -0.0812 0.2780  354 ILE B CA  
1165 C C   . ILE A 168 ? 0.9076 1.1877 0.8238 0.0406  -0.0980 0.2839  354 ILE B C   
1166 O O   . ILE A 168 ? 0.9094 1.1917 0.8341 0.0443  -0.0994 0.2895  354 ILE B O   
1167 C CB  . ILE A 168 ? 0.9388 1.2116 0.8174 0.0404  -0.0767 0.2722  354 ILE B CB  
1168 C CG1 . ILE A 168 ? 0.9183 1.1931 0.7953 0.0447  -0.0598 0.2680  354 ILE B CG1 
1169 C CG2 . ILE A 168 ? 0.9106 1.1787 0.7682 0.0399  -0.0803 0.2752  354 ILE B CG2 
1170 C CD1 . ILE A 168 ? 0.9685 1.2441 0.8306 0.0495  -0.0488 0.2684  354 ILE B CD1 
1171 N N   . LYS A 169 ? 0.9250 1.2024 0.8356 0.0331  -0.1107 0.2830  355 LYS B N   
1172 C CA  . LYS A 169 ? 0.9373 1.2145 0.8490 0.0286  -0.1283 0.2902  355 LYS B CA  
1173 C C   . LYS A 169 ? 0.9279 1.2121 0.8753 0.0345  -0.1326 0.2965  355 LYS B C   
1174 O O   . LYS A 169 ? 0.9194 1.2095 0.8905 0.0365  -0.1305 0.2938  355 LYS B O   
1175 C CB  . LYS A 169 ? 0.9536 1.2312 0.8563 0.0184  -0.1396 0.2870  355 LYS B CB  
1176 C CG  . LYS A 169 ? 0.9705 1.2501 0.8720 0.0117  -0.1592 0.2957  355 LYS B CG  
1177 C CD  . LYS A 169 ? 0.9816 1.2556 0.8569 0.0080  -0.1639 0.3011  355 LYS B CD  
1178 C CE  . LYS A 169 ? 1.0004 1.2778 0.8746 -0.0003 -0.1848 0.3120  355 LYS B CE  
1179 N NZ  . LYS A 169 ? 1.0239 1.2959 0.8737 -0.0044 -0.1905 0.3190  355 LYS B NZ  
1180 N N   . GLY A 170 ? 0.9291 1.2128 0.8821 0.0371  -0.1379 0.3041  356 GLY B N   
1181 C CA  . GLY A 170 ? 0.9200 1.2106 0.9101 0.0424  -0.1416 0.3088  356 GLY B CA  
1182 C C   . GLY A 170 ? 0.8979 1.1957 0.9076 0.0501  -0.1246 0.3050  356 GLY B C   
1183 O O   . GLY A 170 ? 1.0394 1.3443 1.0817 0.0537  -0.1262 0.3072  356 GLY B O   
1184 N N   . LYS A 171 ? 0.9283 1.2263 0.9211 0.0517  -0.1084 0.2988  357 LYS B N   
1185 C CA  . LYS A 171 ? 0.9074 1.2154 0.9156 0.0571  -0.0912 0.2953  357 LYS B CA  
1186 C C   . LYS A 171 ? 0.9598 1.2640 0.9453 0.0593  -0.0823 0.2956  357 LYS B C   
1187 O O   . LYS A 171 ? 1.0473 1.3420 0.9985 0.0569  -0.0813 0.2941  357 LYS B O   
1188 C CB  . LYS A 171 ? 0.8967 1.2104 0.9060 0.0570  -0.0792 0.2895  357 LYS B CB  
1189 C CG  . LYS A 171 ? 0.8934 1.2139 0.9312 0.0556  -0.0845 0.2881  357 LYS B CG  
1190 C CD  . LYS A 171 ? 0.9108 1.2222 0.9380 0.0508  -0.0984 0.2884  357 LYS B CD  
1191 C CE  . LYS A 171 ? 0.9981 1.3163 1.0551 0.0497  -0.1048 0.2869  357 LYS B CE  
1192 N NZ  . LYS A 171 ? 1.1089 1.4209 1.1567 0.0445  -0.1162 0.2857  357 LYS B NZ  
1193 N N   . LYS A 172 ? 0.8540 1.1666 0.8598 0.0634  -0.0752 0.2962  358 LYS B N   
1194 C CA  . LYS A 172 ? 0.9750 1.2842 0.9613 0.0655  -0.0674 0.2965  358 LYS B CA  
1195 C C   . LYS A 172 ? 0.9204 1.2382 0.8963 0.0681  -0.0463 0.2900  358 LYS B C   
1196 O O   . LYS A 172 ? 0.9489 1.2607 0.8958 0.0689  -0.0395 0.2885  358 LYS B O   
1197 C CB  . LYS A 172 ? 0.8957 1.2093 0.9101 0.0681  -0.0706 0.3003  358 LYS B CB  
1198 C CG  . LYS A 172 ? 0.9141 1.2456 0.9732 0.0702  -0.0628 0.2960  358 LYS B CG  
1199 C CD  . LYS A 172 ? 1.0879 1.4222 1.1816 0.0720  -0.0701 0.2997  358 LYS B CD  
1200 C CE  . LYS A 172 ? 1.1085 1.4319 1.2093 0.0698  -0.0940 0.3088  358 LYS B CE  
1201 N NZ  . LYS A 172 ? 0.9988 1.3056 1.0664 0.0676  -0.1064 0.3180  358 LYS B NZ  
1202 N N   . ASN A 173 ? 0.8203 1.1531 0.8185 0.0686  -0.0359 0.2862  359 ASN B N   
1203 C CA  . ASN A 173 ? 0.8048 1.1488 0.7946 0.0700  -0.0165 0.2818  359 ASN B CA  
1204 C C   . ASN A 173 ? 0.8322 1.1846 0.8324 0.0678  -0.0126 0.2806  359 ASN B C   
1205 O O   . ASN A 173 ? 0.8141 1.1636 0.8286 0.0656  -0.0238 0.2819  359 ASN B O   
1206 C CB  . ASN A 173 ? 0.8366 1.1980 0.8480 0.0719  -0.0028 0.2787  359 ASN B CB  
1207 C CG  . ASN A 173 ? 0.8226 1.1986 0.8792 0.0705  -0.0052 0.2773  359 ASN B CG  
1208 O OD1 . ASN A 173 ? 0.8584 1.2400 0.9314 0.0678  -0.0088 0.2768  359 ASN B OD1 
1209 N ND2 . ASN A 173 ? 0.8725 1.2549 0.9513 0.0720  -0.0030 0.2757  359 ASN B ND2 
1210 N N   . ILE A 174 ? 0.8550 1.2185 0.8482 0.0680  0.0035  0.2786  360 ILE B N   
1211 C CA  . ILE A 174 ? 0.8369 1.2085 0.8384 0.0654  0.0077  0.2793  360 ILE B CA  
1212 C C   . ILE A 174 ? 0.7679 1.1562 0.8077 0.0622  0.0071  0.2785  360 ILE B C   
1213 O O   . ILE A 174 ? 0.7701 1.1584 0.8203 0.0594  0.0021  0.2796  360 ILE B O   
1214 C CB  . ILE A 174 ? 0.7678 1.1500 0.7552 0.0659  0.0247  0.2791  360 ILE B CB  
1215 C CG1 . ILE A 174 ? 0.7810 1.1444 0.7322 0.0680  0.0230  0.2788  360 ILE B CG1 
1216 C CG2 . ILE A 174 ? 0.8104 1.2078 0.8152 0.0621  0.0307  0.2817  360 ILE B CG2 
1217 C CD1 . ILE A 174 ? 0.9478 1.3190 0.8882 0.0683  0.0362  0.2799  360 ILE B CD1 
1218 N N   . PHE A 175 ? 0.7693 1.1725 0.8319 0.0620  0.0127  0.2753  361 PHE B N   
1219 C CA  . PHE A 175 ? 0.7732 1.1939 0.8748 0.0578  0.0125  0.2721  361 PHE B CA  
1220 C C   . PHE A 175 ? 0.8170 1.2240 0.9298 0.0576  -0.0060 0.2733  361 PHE B C   
1221 O O   . PHE A 175 ? 0.7562 1.1692 0.8849 0.0539  -0.0085 0.2725  361 PHE B O   
1222 C CB  . PHE A 175 ? 0.7316 1.1690 0.8585 0.0574  0.0206  0.2666  361 PHE B CB  
1223 C CG  . PHE A 175 ? 0.8109 1.2634 0.9809 0.0530  0.0174  0.2612  361 PHE B CG  
1224 C CD1 . PHE A 175 ? 0.8059 1.2831 0.9971 0.0456  0.0278  0.2567  361 PHE B CD1 
1225 C CD2 . PHE A 175 ? 0.7931 1.2362 0.9834 0.0554  0.0036  0.2606  361 PHE B CD2 
1226 C CE1 . PHE A 175 ? 0.6996 1.1916 0.9308 0.0404  0.0251  0.2497  361 PHE B CE1 
1227 C CE2 . PHE A 175 ? 0.7229 1.1799 0.9550 0.0513  0.0005  0.2542  361 PHE B CE2 
1228 C CZ  . PHE A 175 ? 0.7279 1.2093 0.9802 0.0437  0.0116  0.2477  361 PHE B CZ  
1229 N N   . GLU A 176 ? 0.7984 1.1880 0.9028 0.0610  -0.0192 0.2758  362 GLU B N   
1230 C CA  . GLU A 176 ? 0.7872 1.1646 0.8991 0.0604  -0.0374 0.2779  362 GLU B CA  
1231 C C   . GLU A 176 ? 0.7975 1.1640 0.8880 0.0588  -0.0416 0.2797  362 GLU B C   
1232 O O   . GLU A 176 ? 0.8020 1.1673 0.9060 0.0565  -0.0504 0.2790  362 GLU B O   
1233 C CB  . GLU A 176 ? 0.8024 1.1646 0.9057 0.0631  -0.0510 0.2823  362 GLU B CB  
1234 C CG  . GLU A 176 ? 0.8066 1.1776 0.9419 0.0646  -0.0518 0.2812  362 GLU B CG  
1235 C CD  . GLU A 176 ? 0.8909 1.2464 1.0227 0.0662  -0.0695 0.2883  362 GLU B CD  
1236 O OE1 . GLU A 176 ? 0.9437 1.2832 1.0420 0.0653  -0.0788 0.2934  362 GLU B OE1 
1237 O OE2 . GLU A 176 ? 1.0438 1.4043 1.2080 0.0675  -0.0745 0.2888  362 GLU B OE2 
1238 N N   . SER A 177 ? 0.8086 1.1674 0.8676 0.0598  -0.0350 0.2810  363 SER B N   
1239 C CA  . SER A 177 ? 0.8105 1.1594 0.8528 0.0581  -0.0376 0.2815  363 SER B CA  
1240 C C   . SER A 177 ? 0.8293 1.1908 0.8919 0.0552  -0.0311 0.2807  363 SER B C   
1241 O O   . SER A 177 ? 0.8074 1.1632 0.8741 0.0530  -0.0381 0.2803  363 SER B O   
1242 C CB  . SER A 177 ? 0.8144 1.1549 0.8237 0.0595  -0.0301 0.2816  363 SER B CB  
1243 O OG  . SER A 177 ? 0.8244 1.1547 0.8214 0.0574  -0.0334 0.2808  363 SER B OG  
1244 N N   . PHE A 178 ? 0.8197 1.1999 0.8952 0.0543  -0.0172 0.2803  364 PHE B N   
1245 C CA  . PHE A 178 ? 0.7727 1.1675 0.8675 0.0497  -0.0110 0.2806  364 PHE B CA  
1246 C C   . PHE A 178 ? 0.7707 1.1723 0.8959 0.0466  -0.0191 0.2769  364 PHE B C   
1247 O O   . PHE A 178 ? 0.7715 1.1753 0.9076 0.0430  -0.0211 0.2768  364 PHE B O   
1248 C CB  . PHE A 178 ? 0.7550 1.1717 0.8548 0.0474  0.0059  0.2814  364 PHE B CB  
1249 C CG  . PHE A 178 ? 0.7553 1.1704 0.8341 0.0479  0.0145  0.2865  364 PHE B CG  
1250 C CD1 . PHE A 178 ? 0.7553 1.1740 0.8408 0.0440  0.0160  0.2908  364 PHE B CD1 
1251 C CD2 . PHE A 178 ? 0.7603 1.1704 0.8143 0.0519  0.0211  0.2872  364 PHE B CD2 
1252 C CE1 . PHE A 178 ? 0.7561 1.1732 0.8264 0.0446  0.0231  0.2966  364 PHE B CE1 
1253 C CE2 . PHE A 178 ? 0.8154 1.2243 0.8524 0.0525  0.0287  0.2916  364 PHE B CE2 
1254 C CZ  . PHE A 178 ? 0.7563 1.1687 0.8028 0.0490  0.0294  0.2968  364 PHE B CZ  
1255 N N   . VAL A 179 ? 0.7794 1.1845 0.9204 0.0478  -0.0237 0.2736  365 VAL B N   
1256 C CA  . VAL A 179 ? 0.7670 1.1779 0.9389 0.0452  -0.0324 0.2691  365 VAL B CA  
1257 C C   . VAL A 179 ? 0.7836 1.1772 0.9484 0.0458  -0.0471 0.2704  365 VAL B C   
1258 O O   . VAL A 179 ? 0.8224 1.2208 1.0056 0.0422  -0.0508 0.2672  365 VAL B O   
1259 C CB  . VAL A 179 ? 0.7637 1.1785 0.9549 0.0474  -0.0363 0.2660  365 VAL B CB  
1260 C CG1 . VAL A 179 ? 0.7659 1.1827 0.9880 0.0456  -0.0484 0.2617  365 VAL B CG1 
1261 C CG2 . VAL A 179 ? 0.7444 1.1817 0.9509 0.0448  -0.0197 0.2617  365 VAL B CG2 
1262 N N   . ASP A 180 ? 0.7990 1.1739 0.9366 0.0491  -0.0549 0.2742  366 ASP B N   
1263 C CA  . ASP A 180 ? 0.8149 1.1759 0.9440 0.0482  -0.0674 0.2745  366 ASP B CA  
1264 C C   . ASP A 180 ? 0.8145 1.1754 0.9398 0.0454  -0.0614 0.2739  366 ASP B C   
1265 O O   . ASP A 180 ? 0.8214 1.1787 0.9545 0.0431  -0.0687 0.2715  366 ASP B O   
1266 C CB  . ASP A 180 ? 0.8308 1.1754 0.9304 0.0500  -0.0753 0.2777  366 ASP B CB  
1267 C CG  . ASP A 180 ? 0.8471 1.1806 0.9368 0.0471  -0.0868 0.2768  366 ASP B CG  
1268 O OD1 . ASP A 180 ? 0.9076 1.2420 1.0132 0.0458  -0.0987 0.2761  366 ASP B OD1 
1269 O OD2 . ASP A 180 ? 0.9468 1.2720 1.0143 0.0457  -0.0836 0.2761  366 ASP B OD2 
1270 N N   . TYR A 181 ? 0.8070 1.1719 0.9214 0.0455  -0.0483 0.2763  367 TYR B N   
1271 C CA  . TYR A 181 ? 0.8070 1.1717 0.9209 0.0429  -0.0427 0.2775  367 TYR B CA  
1272 C C   . TYR A 181 ? 0.7977 1.1769 0.9398 0.0382  -0.0408 0.2757  367 TYR B C   
1273 O O   . TYR A 181 ? 0.8128 1.1882 0.9605 0.0356  -0.0432 0.2750  367 TYR B O   
1274 C CB  . TYR A 181 ? 0.8007 1.1684 0.8993 0.0440  -0.0298 0.2819  367 TYR B CB  
1275 C CG  . TYR A 181 ? 0.8063 1.1667 0.8978 0.0428  -0.0262 0.2845  367 TYR B CG  
1276 C CD1 . TYR A 181 ? 0.8209 1.1635 0.8939 0.0442  -0.0317 0.2822  367 TYR B CD1 
1277 C CD2 . TYR A 181 ? 0.7972 1.1699 0.9018 0.0395  -0.0172 0.2894  367 TYR B CD2 
1278 C CE1 . TYR A 181 ? 0.8257 1.1619 0.8969 0.0431  -0.0278 0.2834  367 TYR B CE1 
1279 C CE2 . TYR A 181 ? 0.8030 1.1683 0.9048 0.0388  -0.0143 0.2930  367 TYR B CE2 
1280 C CZ  . TYR A 181 ? 0.8928 1.2395 0.9795 0.0410  -0.0194 0.2894  367 TYR B CZ  
1281 O OH  . TYR A 181 ? 0.8297 1.1693 0.9184 0.0402  -0.0161 0.2916  367 TYR B OH  
1282 N N   . VAL A 182 ? 0.8482 1.2450 1.0091 0.0363  -0.0359 0.2737  368 VAL B N   
1283 C CA  . VAL A 182 ? 0.7743 1.1876 0.9628 0.0300  -0.0337 0.2701  368 VAL B CA  
1284 C C   . VAL A 182 ? 0.7782 1.1899 0.9863 0.0298  -0.0459 0.2632  368 VAL B C   
1285 O O   . VAL A 182 ? 0.7709 1.1959 1.0033 0.0243  -0.0453 0.2579  368 VAL B O   
1286 C CB  . VAL A 182 ? 0.7561 1.1937 0.9577 0.0256  -0.0206 0.2696  368 VAL B CB  
1287 C CG1 . VAL A 182 ? 0.8222 1.2789 1.0460 0.0163  -0.0154 0.2676  368 VAL B CG1 
1288 C CG2 . VAL A 182 ? 0.8014 1.2396 0.9806 0.0276  -0.0098 0.2766  368 VAL B CG2 
1289 N N   . ALA A 183 ? 0.7900 1.1867 0.9885 0.0349  -0.0574 0.2632  369 ALA B N   
1290 C CA  . ALA A 183 ? 0.7977 1.1928 1.0150 0.0350  -0.0705 0.2582  369 ALA B CA  
1291 C C   . ALA A 183 ? 0.8542 1.2459 1.0772 0.0317  -0.0754 0.2550  369 ALA B C   
1292 O O   . ALA A 183 ? 0.9276 1.3097 1.1331 0.0315  -0.0736 0.2578  369 ALA B O   
1293 C CB  . ALA A 183 ? 0.8088 1.1890 1.0113 0.0399  -0.0826 0.2616  369 ALA B CB  
1294 N N   . VAL A 184 ? 0.7983 1.1983 1.0479 0.0290  -0.0812 0.2481  370 VAL B N   
1295 C CA  . VAL A 184 ? 0.8834 1.2822 1.1412 0.0254  -0.0850 0.2434  370 VAL B CA  
1296 C C   . VAL A 184 ? 0.9110 1.2940 1.1557 0.0283  -0.0981 0.2440  370 VAL B C   
1297 O O   . VAL A 184 ? 0.9029 1.2827 1.1517 0.0311  -0.1096 0.2442  370 VAL B O   
1298 C CB  . VAL A 184 ? 0.8236 1.2381 1.1147 0.0208  -0.0864 0.2340  370 VAL B CB  
1299 C CG1 . VAL A 184 ? 0.7993 1.2114 1.0975 0.0174  -0.0914 0.2282  370 VAL B CG1 
1300 C CG2 . VAL A 184 ? 0.8394 1.2736 1.1435 0.0149  -0.0723 0.2322  370 VAL B CG2 
1301 N N   . GLU A 185 ? 1.0115 1.3863 1.2427 0.0268  -0.0965 0.2443  371 GLU B N   
1302 C CA  . GLU A 185 ? 1.0637 1.4277 1.2849 0.0271  -0.1072 0.2426  371 GLU B CA  
1303 C C   . GLU A 185 ? 1.1093 1.4784 1.3512 0.0241  -0.1130 0.2346  371 GLU B C   
1304 O O   . GLU A 185 ? 1.1279 1.5050 1.3850 0.0206  -0.1058 0.2304  371 GLU B O   
1305 C CB  . GLU A 185 ? 1.1440 1.4977 1.3436 0.0263  -0.1016 0.2447  371 GLU B CB  
1306 C CG  . GLU A 185 ? 1.1199 1.4662 1.3107 0.0244  -0.1109 0.2408  371 GLU B CG  
1307 C CD  . GLU A 185 ? 1.2566 1.5942 1.4304 0.0225  -0.1043 0.2405  371 GLU B CD  
1308 O OE1 . GLU A 185 ? 1.2371 1.5712 1.3992 0.0243  -0.0957 0.2453  371 GLU B OE1 
1309 O OE2 . GLU A 185 ? 1.1302 1.4655 1.3043 0.0190  -0.1071 0.2345  371 GLU B OE2 
1310 N N   . GLN A 186 ? 1.0913 1.4568 1.3332 0.0246  -0.1262 0.2326  372 GLN B N   
1311 C CA  . GLN A 186 ? 0.9808 1.3512 1.2416 0.0223  -0.1333 0.2245  372 GLN B CA  
1312 C C   . GLN A 186 ? 1.0243 1.3885 1.2726 0.0194  -0.1342 0.2210  372 GLN B C   
1313 O O   . GLN A 186 ? 1.0176 1.3748 1.2453 0.0193  -0.1376 0.2245  372 GLN B O   
1314 C CB  . GLN A 186 ? 0.9619 1.3353 1.2357 0.0245  -0.1481 0.2248  372 GLN B CB  
1315 C CG  . GLN A 186 ? 1.0601 1.4445 1.3662 0.0233  -0.1509 0.2162  372 GLN B CG  
1316 C CD  . GLN A 186 ? 0.9857 1.3797 1.3075 0.0223  -0.1396 0.2143  372 GLN B CD  
1317 O OE1 . GLN A 186 ? 0.8336 1.2262 1.1426 0.0238  -0.1313 0.2209  372 GLN B OE1 
1318 N NE2 . GLN A 186 ? 1.0243 1.4299 1.3742 0.0189  -0.1390 0.2042  372 GLN B NE2 
1319 N N   . LEU A 187 ? 1.0225 1.3904 1.2840 0.0162  -0.1303 0.2131  373 LEU B N   
1320 C CA  . LEU A 187 ? 1.0584 1.4224 1.3135 0.0130  -0.1298 0.2076  373 LEU B CA  
1321 C C   . LEU A 187 ? 1.2056 1.5760 1.4769 0.0115  -0.1399 0.1991  373 LEU B C   
1322 O O   . LEU A 187 ? 1.1195 1.4951 1.4077 0.0092  -0.1362 0.1915  373 LEU B O   
1323 C CB  . LEU A 187 ? 1.0195 1.3817 1.2767 0.0104  -0.1159 0.2060  373 LEU B CB  
1324 C CG  . LEU A 187 ? 0.9861 1.3426 1.2296 0.0118  -0.1058 0.2146  373 LEU B CG  
1325 C CD1 . LEU A 187 ? 0.9689 1.3253 1.2203 0.0087  -0.0938 0.2145  373 LEU B CD1 
1326 C CD2 . LEU A 187 ? 1.0688 1.4165 1.2909 0.0124  -0.1081 0.2167  373 LEU B CD2 
1327 N N   . ASP A 188 ? 1.2958 1.6668 1.5616 0.0121  -0.1530 0.2008  374 ASP B N   
1328 C CA  . ASP A 188 ? 1.3566 1.7344 1.6369 0.0108  -0.1644 0.1942  374 ASP B CA  
1329 C C   . ASP A 188 ? 1.4039 1.7821 1.6742 0.0062  -0.1644 0.1877  374 ASP B C   
1330 O O   . ASP A 188 ? 1.4104 1.7834 1.6668 0.0038  -0.1543 0.1870  374 ASP B O   
1331 C CB  . ASP A 188 ? 1.2726 1.6529 1.5561 0.0136  -0.1798 0.2016  374 ASP B CB  
1332 C CG  . ASP A 188 ? 1.3111 1.6943 1.6146 0.0176  -0.1800 0.2038  374 ASP B CG  
1333 O OD1 . ASP A 188 ? 1.4139 1.8024 1.7369 0.0168  -0.1732 0.1956  374 ASP B OD1 
1334 O OD2 . ASP A 188 ? 1.2730 1.6543 1.5735 0.0206  -0.1864 0.2132  374 ASP B OD2 
1335 N N   . GLY A 189 ? 1.3904 1.7761 1.6699 0.0045  -0.1754 0.1823  375 GLY B N   
1336 C CA  . GLY A 189 ? 1.3616 1.7512 1.6332 -0.0009 -0.1757 0.1750  375 GLY B CA  
1337 C C   . GLY A 189 ? 1.4752 1.8626 1.7225 -0.0047 -0.1751 0.1803  375 GLY B C   
1338 O O   . GLY A 189 ? 1.5004 1.8856 1.7369 -0.0033 -0.1822 0.1908  375 GLY B O   
1339 N N   . ASP A 190 ? 1.6115 1.9999 1.8515 -0.0102 -0.1661 0.1720  376 ASP B N   
1340 C CA  . ASP A 190 ? 1.6122 1.9996 1.8326 -0.0157 -0.1615 0.1725  376 ASP B CA  
1341 C C   . ASP A 190 ? 1.5462 1.9213 1.7603 -0.0121 -0.1493 0.1775  376 ASP B C   
1342 O O   . ASP A 190 ? 1.6485 2.0209 1.8501 -0.0163 -0.1422 0.1756  376 ASP B O   
1343 C CB  . ASP A 190 ? 1.6822 2.0764 1.8865 -0.0198 -0.1760 0.1803  376 ASP B CB  
1344 C CG  . ASP A 190 ? 1.7548 2.1534 1.9403 -0.0292 -0.1717 0.1761  376 ASP B CG  
1345 O OD1 . ASP A 190 ? 1.8142 2.2107 2.0019 -0.0322 -0.1574 0.1661  376 ASP B OD1 
1346 O OD2 . ASP A 190 ? 1.7214 2.1268 1.8915 -0.0346 -0.1829 0.1826  376 ASP B OD2 
1347 N N   . ASN A 191 ? 1.4440 1.8132 1.6681 -0.0054 -0.1461 0.1827  377 ASN B N   
1348 C CA  . ASN A 191 ? 1.3699 1.7297 1.5906 -0.0025 -0.1337 0.1874  377 ASN B CA  
1349 C C   . ASN A 191 ? 1.2656 1.6245 1.5049 0.0001  -0.1256 0.1856  377 ASN B C   
1350 O O   . ASN A 191 ? 1.1675 1.5214 1.4066 0.0025  -0.1168 0.1916  377 ASN B O   
1351 C CB  . ASN A 191 ? 1.3646 1.7204 1.5730 0.0016  -0.1379 0.1988  377 ASN B CB  
1352 C CG  . ASN A 191 ? 1.4356 1.7908 1.6220 -0.0024 -0.1430 0.2013  377 ASN B CG  
1353 O OD1 . ASN A 191 ? 1.4662 1.8223 1.6454 -0.0084 -0.1383 0.1944  377 ASN B OD1 
1354 N ND2 . ASN A 191 ? 1.4423 1.7970 1.6192 0.0000  -0.1524 0.2105  377 ASN B ND2 
1355 N N   . LYS A 192 ? 1.2470 1.6120 1.5019 -0.0014 -0.1283 0.1773  378 LYS B N   
1356 C CA  . LYS A 192 ? 1.1277 1.4942 1.4002 -0.0007 -0.1221 0.1748  378 LYS B CA  
1357 C C   . LYS A 192 ? 0.9998 1.3601 1.2732 -0.0023 -0.1074 0.1761  378 LYS B C   
1358 O O   . LYS A 192 ? 1.0134 1.3697 1.2828 -0.0051 -0.1014 0.1722  378 LYS B O   
1359 C CB  . LYS A 192 ? 1.1211 1.4948 1.4083 -0.0032 -0.1268 0.1633  378 LYS B CB  
1360 C CG  . LYS A 192 ? 1.1691 1.5501 1.4664 -0.0008 -0.1404 0.1627  378 LYS B CG  
1361 C CD  . LYS A 192 ? 1.0469 1.4350 1.3625 -0.0031 -0.1427 0.1503  378 LYS B CD  
1362 C CE  . LYS A 192 ? 1.0187 1.4114 1.3307 -0.0057 -0.1491 0.1427  378 LYS B CE  
1363 N NZ  . LYS A 192 ? 1.1443 1.5422 1.4539 -0.0038 -0.1653 0.1479  378 LYS B NZ  
1364 N N   . TYR A 193 ? 0.9303 1.2913 1.2109 -0.0014 -0.1016 0.1819  379 TYR B N   
1365 C CA  . TYR A 193 ? 0.9392 1.2957 1.2228 -0.0032 -0.0889 0.1862  379 TYR B CA  
1366 C C   . TYR A 193 ? 0.8840 1.2410 1.1809 -0.0077 -0.0836 0.1773  379 TYR B C   
1367 O O   . TYR A 193 ? 0.8824 1.2459 1.1899 -0.0097 -0.0879 0.1688  379 TYR B O   
1368 C CB  . TYR A 193 ? 0.9192 1.2807 1.2080 -0.0031 -0.0849 0.1945  379 TYR B CB  
1369 C CG  . TYR A 193 ? 0.8658 1.2253 1.1599 -0.0061 -0.0731 0.2011  379 TYR B CG  
1370 C CD1 . TYR A 193 ? 0.9257 1.2773 1.2103 -0.0041 -0.0668 0.2099  379 TYR B CD1 
1371 C CD2 . TYR A 193 ? 0.8609 1.2272 1.1703 -0.0117 -0.0688 0.1989  379 TYR B CD2 
1372 C CE1 . TYR A 193 ? 0.9656 1.3158 1.2577 -0.0068 -0.0571 0.2178  379 TYR B CE1 
1373 C CE2 . TYR A 193 ? 0.8594 1.2248 1.1745 -0.0155 -0.0591 0.2072  379 TYR B CE2 
1374 C CZ  . TYR A 193 ? 0.8704 1.2277 1.1777 -0.0126 -0.0536 0.2174  379 TYR B CZ  
1375 O OH  . TYR A 193 ? 0.9108 1.2675 1.2263 -0.0163 -0.0451 0.2275  379 TYR B OH  
1376 N N   . ASP A 194 ? 0.8886 1.2385 1.1865 -0.0094 -0.0742 0.1787  380 ASP B N   
1377 C CA  . ASP A 194 ? 0.8917 1.2408 1.2038 -0.0137 -0.0673 0.1714  380 ASP B CA  
1378 C C   . ASP A 194 ? 0.8835 1.2355 1.2070 -0.0167 -0.0615 0.1783  380 ASP B C   
1379 O O   . ASP A 194 ? 0.9513 1.2989 1.2769 -0.0173 -0.0538 0.1890  380 ASP B O   
1380 C CB  . ASP A 194 ? 0.9041 1.2451 1.2170 -0.0147 -0.0592 0.1700  380 ASP B CB  
1381 C CG  . ASP A 194 ? 0.9038 1.2435 1.2336 -0.0191 -0.0513 0.1620  380 ASP B CG  
1382 O OD1 . ASP A 194 ? 0.9102 1.2554 1.2478 -0.0216 -0.0532 0.1561  380 ASP B OD1 
1383 O OD2 . ASP A 194 ? 0.9615 1.2948 1.2983 -0.0205 -0.0429 0.1610  380 ASP B OD2 
1384 N N   . ALA A 195 ? 0.8782 1.2391 1.2098 -0.0196 -0.0654 0.1723  381 ALA B N   
1385 C CA  . ALA A 195 ? 0.8705 1.2378 1.2124 -0.0251 -0.0603 0.1777  381 ALA B CA  
1386 C C   . ALA A 195 ? 0.8752 1.2397 1.2296 -0.0308 -0.0524 0.1751  381 ALA B C   
1387 O O   . ALA A 195 ? 0.8704 1.2419 1.2338 -0.0374 -0.0490 0.1783  381 ALA B O   
1388 C CB  . ALA A 195 ? 0.8621 1.2420 1.2098 -0.0274 -0.0672 0.1708  381 ALA B CB  
1389 N N   . GLY A 196 ? 0.8847 1.2404 1.2406 -0.0294 -0.0492 0.1690  382 GLY B N   
1390 C CA  . GLY A 196 ? 0.8899 1.2417 1.2598 -0.0344 -0.0407 0.1668  382 GLY B CA  
1391 C C   . GLY A 196 ? 0.8887 1.2479 1.2671 -0.0400 -0.0421 0.1549  382 GLY B C   
1392 O O   . GLY A 196 ? 0.8921 1.2530 1.2698 -0.0390 -0.0461 0.1400  382 GLY B O   
1393 N N   . GLU A 197 ? 0.8857 1.2505 1.2721 -0.0470 -0.0388 0.1613  383 GLU B N   
1394 C CA  . GLU A 197 ? 0.8827 1.2557 1.2773 -0.0542 -0.0397 0.1497  383 GLU B CA  
1395 C C   . GLU A 197 ? 0.8861 1.2681 1.2765 -0.0524 -0.0495 0.1364  383 GLU B C   
1396 O O   . GLU A 197 ? 0.9714 1.3570 1.3670 -0.0551 -0.0517 0.1210  383 GLU B O   
1397 C CB  . GLU A 197 ? 0.8779 1.2591 1.2794 -0.0638 -0.0357 0.1607  383 GLU B CB  
1398 C CG  . GLU A 197 ? 0.8764 1.2675 1.2861 -0.0737 -0.0358 0.1490  383 GLU B CG  
1399 C CD  . GLU A 197 ? 0.9894 1.3928 1.4041 -0.0853 -0.0328 0.1606  383 GLU B CD  
1400 O OE1 . GLU A 197 ? 0.8945 1.2984 1.3067 -0.0849 -0.0304 0.1789  383 GLU B OE1 
1401 O OE2 . GLU A 197 ? 1.0811 1.4952 1.5021 -0.0957 -0.0329 0.1512  383 GLU B OE2 
1402 N N   . HIS A 198 ? 0.9120 1.2976 1.2945 -0.0477 -0.0557 0.1421  384 HIS B N   
1403 C CA  . HIS A 198 ? 0.8848 1.2787 1.2672 -0.0455 -0.0658 0.1317  384 HIS B CA  
1404 C C   . HIS A 198 ? 0.8724 1.2604 1.2464 -0.0373 -0.0729 0.1262  384 HIS B C   
1405 O O   . HIS A 198 ? 0.8695 1.2634 1.2440 -0.0343 -0.0827 0.1203  384 HIS B O   
1406 C CB  . HIS A 198 ? 0.9236 1.3266 1.3054 -0.0460 -0.0683 0.1404  384 HIS B CB  
1407 C CG  . HIS A 198 ? 0.9326 1.3462 1.3223 -0.0563 -0.0617 0.1459  384 HIS B CG  
1408 N ND1 . HIS A 198 ? 0.9879 1.4075 1.3745 -0.0580 -0.0582 0.1602  384 HIS B ND1 
1409 C CD2 . HIS A 198 ? 0.9422 1.3633 1.3421 -0.0667 -0.0580 0.1391  384 HIS B CD2 
1410 C CE1 . HIS A 198 ? 0.9723 1.4040 1.3671 -0.0697 -0.0528 0.1628  384 HIS B CE1 
1411 N NE2 . HIS A 198 ? 0.9815 1.4140 1.3843 -0.0754 -0.0528 0.1502  384 HIS B NE2 
1412 N N   . GLY A 199 ? 0.8812 1.2593 1.2491 -0.0344 -0.0682 0.1283  385 GLY B N   
1413 C CA  . GLY A 199 ? 0.8882 1.2638 1.2475 -0.0293 -0.0743 0.1228  385 GLY B CA  
1414 C C   . GLY A 199 ? 0.8861 1.2610 1.2335 -0.0236 -0.0814 0.1327  385 GLY B C   
1415 O O   . GLY A 199 ? 0.9147 1.2892 1.2595 -0.0227 -0.0796 0.1443  385 GLY B O   
1416 N N   . LEU A 200 ? 0.8923 1.2684 1.2321 -0.0205 -0.0897 0.1279  386 LEU B N   
1417 C CA  . LEU A 200 ? 0.8921 1.2677 1.2200 -0.0157 -0.0979 0.1367  386 LEU B CA  
1418 C C   . LEU A 200 ? 0.8830 1.2656 1.2181 -0.0140 -0.1060 0.1384  386 LEU B C   
1419 O O   . LEU A 200 ? 0.8807 1.2706 1.2281 -0.0157 -0.1114 0.1284  386 LEU B O   
1420 C CB  . LEU A 200 ? 0.9024 1.2800 1.2211 -0.0149 -0.1055 0.1316  386 LEU B CB  
1421 C CG  . LEU A 200 ? 0.9088 1.2805 1.2121 -0.0142 -0.1026 0.1385  386 LEU B CG  
1422 C CD1 . LEU A 200 ? 0.9106 1.2754 1.2179 -0.0170 -0.0883 0.1373  386 LEU B CD1 
1423 C CD2 . LEU A 200 ? 0.9191 1.2971 1.2132 -0.0159 -0.1113 0.1331  386 LEU B CD2 
1424 N N   . GLN A 201 ? 0.8774 1.2585 1.2065 -0.0111 -0.1063 0.1500  387 GLN B N   
1425 C CA  . GLN A 201 ? 0.8669 1.2558 1.2063 -0.0106 -0.1106 0.1514  387 GLN B CA  
1426 C C   . GLN A 201 ? 1.0243 1.4115 1.3541 -0.0051 -0.1176 0.1609  387 GLN B C   
1427 O O   . GLN A 201 ? 1.0740 1.4535 1.3869 -0.0026 -0.1155 0.1691  387 GLN B O   
1428 C CB  . GLN A 201 ? 0.8569 1.2497 1.2033 -0.0153 -0.1000 0.1555  387 GLN B CB  
1429 C CG  . GLN A 201 ? 0.8904 1.2880 1.2499 -0.0223 -0.0950 0.1455  387 GLN B CG  
1430 C CD  . GLN A 201 ? 0.8532 1.2599 1.2279 -0.0240 -0.1036 0.1312  387 GLN B CD  
1431 O OE1 . GLN A 201 ? 0.8469 1.2606 1.2302 -0.0222 -0.1109 0.1299  387 GLN B OE1 
1432 N NE2 . GLN A 201 ? 0.8580 1.2648 1.2383 -0.0276 -0.1023 0.1197  387 GLN B NE2 
1433 N N   . GLU A 202 ? 0.9830 1.3779 1.3256 -0.0038 -0.1256 0.1589  388 GLU B N   
1434 C CA  . GLU A 202 ? 1.0813 1.4755 1.4191 0.0012  -0.1328 0.1675  388 GLU B CA  
1435 C C   . GLU A 202 ? 0.9781 1.3764 1.3192 0.0004  -0.1241 0.1737  388 GLU B C   
1436 O O   . GLU A 202 ? 0.9592 1.3681 1.3195 -0.0015 -0.1248 0.1693  388 GLU B O   
1437 C CB  . GLU A 202 ? 1.1766 1.5770 1.5307 0.0032  -0.1470 0.1620  388 GLU B CB  
1438 C CG  . GLU A 202 ? 1.2065 1.6037 1.5511 0.0046  -0.1578 0.1612  388 GLU B CG  
1439 C CD  . GLU A 202 ? 1.4166 1.8209 1.7802 0.0063  -0.1728 0.1567  388 GLU B CD  
1440 O OE1 . GLU A 202 ? 1.3871 1.7986 1.7746 0.0060  -0.1739 0.1507  388 GLU B OE1 
1441 O OE2 . GLU A 202 ? 1.4453 1.8494 1.8012 0.0072  -0.1838 0.1593  388 GLU B OE2 
1442 N N   . ALA A 203 ? 0.9503 1.3419 1.2740 0.0011  -0.1151 0.1832  389 ALA B N   
1443 C CA  . ALA A 203 ? 0.8364 1.2333 1.1611 -0.0007 -0.1052 0.1899  389 ALA B CA  
1444 C C   . ALA A 203 ? 0.8668 1.2614 1.1808 0.0046  -0.1072 0.1990  389 ALA B C   
1445 O O   . ALA A 203 ? 0.9421 1.3309 1.2489 0.0093  -0.1171 0.2007  389 ALA B O   
1446 C CB  . ALA A 203 ? 0.8415 1.2333 1.1568 -0.0037 -0.0938 0.1951  389 ALA B CB  
1447 N N   . GLU A 204 ? 0.9309 1.3314 1.2439 0.0031  -0.0975 0.2053  390 GLU B N   
1448 C CA  . GLU A 204 ? 0.9339 1.3324 1.2347 0.0076  -0.0960 0.2141  390 GLU B CA  
1449 C C   . GLU A 204 ? 0.8416 1.2361 1.1262 0.0070  -0.0846 0.2233  390 GLU B C   
1450 O O   . GLU A 204 ? 0.8990 1.3006 1.1907 0.0013  -0.0759 0.2242  390 GLU B O   
1451 C CB  . GLU A 204 ? 0.9731 1.3866 1.2924 0.0060  -0.0945 0.2116  390 GLU B CB  
1452 C CG  . GLU A 204 ? 0.9926 1.4099 1.3319 0.0076  -0.1065 0.2034  390 GLU B CG  
1453 C CD  . GLU A 204 ? 0.9879 1.4202 1.3490 0.0059  -0.1039 0.2000  390 GLU B CD  
1454 O OE1 . GLU A 204 ? 0.9071 1.3496 1.2671 0.0022  -0.0918 0.2030  390 GLU B OE1 
1455 O OE2 . GLU A 204 ? 1.0281 1.4634 1.4094 0.0079  -0.1137 0.1941  390 GLU B OE2 
1456 N N   . LYS A 205 ? 0.9843 1.3682 1.2481 0.0121  -0.0849 0.2305  391 LYS B N   
1457 C CA  . LYS A 205 ? 0.9390 1.3181 1.1882 0.0124  -0.0749 0.2389  391 LYS B CA  
1458 C C   . LYS A 205 ? 0.8560 1.2385 1.0954 0.0155  -0.0708 0.2457  391 LYS B C   
1459 O O   . LYS A 205 ? 0.8217 1.2011 1.0551 0.0197  -0.0776 0.2453  391 LYS B O   
1460 C CB  . LYS A 205 ? 0.9301 1.2936 1.1630 0.0147  -0.0771 0.2394  391 LYS B CB  
1461 C CG  . LYS A 205 ? 1.0393 1.3975 1.2620 0.0148  -0.0668 0.2471  391 LYS B CG  
1462 C CD  . LYS A 205 ? 1.1129 1.4577 1.3258 0.0154  -0.0677 0.2444  391 LYS B CD  
1463 C CE  . LYS A 205 ? 1.1767 1.5144 1.3712 0.0183  -0.0757 0.2422  391 LYS B CE  
1464 N NZ  . LYS A 205 ? 1.1481 1.4842 1.3268 0.0218  -0.0723 0.2492  391 LYS B NZ  
1465 N N   . GLY A 206 ? 0.9212 1.3112 1.1598 0.0130  -0.0596 0.2523  392 GLY B N   
1466 C CA  . GLY A 206 ? 0.8970 1.2920 1.1260 0.0155  -0.0540 0.2581  392 GLY B CA  
1467 C C   . GLY A 206 ? 0.7991 1.1976 1.0210 0.0135  -0.0425 0.2673  392 GLY B C   
1468 O O   . GLY A 206 ? 0.8022 1.1993 1.0288 0.0100  -0.0392 0.2703  392 GLY B O   
1469 N N   . VAL A 207 ? 0.7923 1.1958 1.0037 0.0158  -0.0366 0.2722  393 VAL B N   
1470 C CA  . VAL A 207 ? 0.7893 1.1987 0.9935 0.0143  -0.0258 0.2818  393 VAL B CA  
1471 C C   . VAL A 207 ? 0.7728 1.2009 0.9788 0.0126  -0.0183 0.2830  393 VAL B C   
1472 O O   . VAL A 207 ? 0.7981 1.2244 0.9995 0.0170  -0.0212 0.2786  393 VAL B O   
1473 C CB  . VAL A 207 ? 0.7978 1.1883 0.9803 0.0204  -0.0257 0.2861  393 VAL B CB  
1474 C CG1 . VAL A 207 ? 0.8312 1.2055 1.0010 0.0258  -0.0359 0.2792  393 VAL B CG1 
1475 C CG2 . VAL A 207 ? 0.8097 1.2064 0.9791 0.0222  -0.0163 0.2935  393 VAL B CG2 
1476 N N   . LYS A 208 ? 0.7625 1.2101 0.9767 0.0053  -0.0084 0.2890  394 LYS B N   
1477 C CA  . LYS A 208 ? 0.7488 1.2183 0.9654 0.0020  0.0010  0.2899  394 LYS B CA  
1478 C C   . LYS A 208 ? 0.7590 1.2368 0.9657 -0.0005 0.0111  0.3022  394 LYS B C   
1479 O O   . LYS A 208 ? 0.8523 1.3255 1.0598 -0.0028 0.0111  0.3103  394 LYS B O   
1480 C CB  . LYS A 208 ? 0.7356 1.2300 0.9780 -0.0081 0.0034  0.2824  394 LYS B CB  
1481 C CG  . LYS A 208 ? 0.7613 1.2661 1.0172 -0.0182 0.0045  0.2854  394 LYS B CG  
1482 C CD  . LYS A 208 ? 0.9139 1.4452 1.1951 -0.0298 0.0072  0.2756  394 LYS B CD  
1483 C CE  . LYS A 208 ? 0.9023 1.4244 1.1975 -0.0267 -0.0032 0.2618  394 LYS B CE  
1484 N NZ  . LYS A 208 ? 0.7833 1.3325 1.1061 -0.0389 0.0001  0.2503  394 LYS B NZ  
1485 N N   . PHE A 209 ? 0.7346 1.2253 0.9334 0.0001  0.0198  0.3039  395 PHE B N   
1486 C CA  . PHE A 209 ? 0.8086 1.3071 0.9959 -0.0010 0.0290  0.3157  395 PHE B CA  
1487 C C   . PHE A 209 ? 0.7973 1.3272 1.0006 -0.0145 0.0374  0.3222  395 PHE B C   
1488 O O   . PHE A 209 ? 0.8151 1.3701 1.0327 -0.0227 0.0427  0.3153  395 PHE B O   
1489 C CB  . PHE A 209 ? 0.7557 1.2555 0.9258 0.0049  0.0354  0.3143  395 PHE B CB  
1490 C CG  . PHE A 209 ? 0.7433 1.2131 0.8921 0.0166  0.0283  0.3116  395 PHE B CG  
1491 C CD1 . PHE A 209 ? 0.7483 1.2021 0.8812 0.0213  0.0283  0.3187  395 PHE B CD1 
1492 C CD2 . PHE A 209 ? 0.7563 1.2151 0.9028 0.0218  0.0214  0.3019  395 PHE B CD2 
1493 C CE1 . PHE A 209 ? 0.7601 1.1887 0.8736 0.0299  0.0221  0.3144  395 PHE B CE1 
1494 C CE2 . PHE A 209 ? 0.7545 1.1881 0.8801 0.0304  0.0144  0.2998  395 PHE B CE2 
1495 C CZ  . PHE A 209 ? 0.7635 1.1825 0.8719 0.0338  0.0151  0.3052  395 PHE B CZ  
1496 N N   . LEU A 210 ? 0.7577 1.2873 0.9607 -0.0178 0.0385  0.3352  396 LEU B N   
1497 C CA  . LEU A 210 ? 0.7745 1.3355 0.9894 -0.0316 0.0464  0.3450  396 LEU B CA  
1498 C C   . LEU A 210 ? 0.7770 1.3564 0.9803 -0.0326 0.0574  0.3529  396 LEU B C   
1499 O O   . LEU A 210 ? 0.8206 1.4325 1.0314 -0.0430 0.0666  0.3508  396 LEU B O   
1500 C CB  . LEU A 210 ? 0.7277 1.2811 0.9497 -0.0353 0.0421  0.3576  396 LEU B CB  
1501 C CG  . LEU A 210 ? 0.7893 1.3308 1.0253 -0.0373 0.0331  0.3503  396 LEU B CG  
1502 C CD1 . LEU A 210 ? 0.7817 1.3125 1.0242 -0.0393 0.0297  0.3634  396 LEU B CD1 
1503 C CD2 . LEU A 210 ? 0.7241 1.2938 0.9778 -0.0508 0.0355  0.3418  396 LEU B CD2 
1504 N N   . THR A 211 ? 0.7972 1.3576 0.9831 -0.0227 0.0572  0.3608  397 THR B N   
1505 C CA  . THR A 211 ? 0.7318 1.3073 0.9050 -0.0225 0.0673  0.3686  397 THR B CA  
1506 C C   . THR A 211 ? 0.7309 1.2785 0.8815 -0.0076 0.0656  0.3641  397 THR B C   
1507 O O   . THR A 211 ? 0.7653 1.2820 0.9106 0.0012  0.0563  0.3597  397 THR B O   
1508 C CB  . THR A 211 ? 0.7594 1.3475 0.9377 -0.0296 0.0699  0.3882  397 THR B CB  
1509 O OG1 . THR A 211 ? 0.7266 1.2836 0.9043 -0.0214 0.0612  0.3942  397 THR B OG1 
1510 C CG2 . THR A 211 ? 0.7301 1.3492 0.9293 -0.0469 0.0717  0.3936  397 THR B CG2 
1511 N N   . LEU A 212 ? 0.7597 1.3203 0.8967 -0.0060 0.0753  0.3646  398 LEU B N   
1512 C CA  . LEU A 212 ? 0.7747 1.3130 0.8883 0.0065  0.0755  0.3601  398 LEU B CA  
1513 C C   . LEU A 212 ? 0.8044 1.3498 0.9072 0.0074  0.0827  0.3725  398 LEU B C   
1514 O O   . LEU A 212 ? 0.7888 1.3664 0.8964 -0.0015 0.0925  0.3803  398 LEU B O   
1515 C CB  . LEU A 212 ? 0.7916 1.3360 0.8972 0.0091  0.0806  0.3467  398 LEU B CB  
1516 C CG  . LEU A 212 ? 0.7570 1.2874 0.8701 0.0118  0.0716  0.3337  398 LEU B CG  
1517 C CD1 . LEU A 212 ? 0.7914 1.3364 0.9050 0.0116  0.0788  0.3231  398 LEU B CD1 
1518 C CD2 . LEU A 212 ? 0.7223 1.2153 0.8205 0.0226  0.0601  0.3298  398 LEU B CD2 
1519 N N   . PRO A 213 ? 0.8477 1.3659 0.9374 0.0171  0.0783  0.3739  399 PRO B N   
1520 C CA  . PRO A 213 ? 0.7870 1.3101 0.8709 0.0182  0.0836  0.3863  399 PRO B CA  
1521 C C   . PRO A 213 ? 0.8252 1.3638 0.8901 0.0202  0.0951  0.3831  399 PRO B C   
1522 O O   . PRO A 213 ? 0.7857 1.3229 0.8393 0.0233  0.0978  0.3698  399 PRO B O   
1523 C CB  . PRO A 213 ? 0.8281 1.3149 0.9055 0.0281  0.0751  0.3833  399 PRO B CB  
1524 C CG  . PRO A 213 ? 0.8702 1.3375 0.9534 0.0296  0.0651  0.3723  399 PRO B CG  
1525 C CD  . PRO A 213 ? 0.8541 1.3372 0.9360 0.0262  0.0679  0.3637  399 PRO B CD  
1526 N N   . PRO A 214 ? 0.7829 1.3371 0.8450 0.0183  0.1021  0.3955  400 PRO B N   
1527 C CA  . PRO A 214 ? 0.7593 1.3270 0.8014 0.0210  0.1137  0.3916  400 PRO B CA  
1528 C C   . PRO A 214 ? 0.8568 1.3937 0.8745 0.0336  0.1117  0.3778  400 PRO B C   
1529 O O   . PRO A 214 ? 0.8640 1.4079 0.8645 0.0361  0.1201  0.3684  400 PRO B O   
1530 C CB  . PRO A 214 ? 0.8695 1.4557 0.9159 0.0169  0.1185  0.4097  400 PRO B CB  
1531 C CG  . PRO A 214 ? 0.7936 1.3883 0.8661 0.0077  0.1117  0.4243  400 PRO B CG  
1532 C CD  . PRO A 214 ? 0.8192 1.3817 0.8980 0.0129  0.0999  0.4146  400 PRO B CD  
1533 N N   . VAL A 215 ? 0.8574 1.3620 0.8736 0.0405  0.1014  0.3758  401 VAL B N   
1534 C CA  . VAL A 215 ? 0.8377 1.3133 0.8309 0.0502  0.0983  0.3618  401 VAL B CA  
1535 C C   . VAL A 215 ? 0.7954 1.2465 0.7933 0.0520  0.0862  0.3525  401 VAL B C   
1536 O O   . VAL A 215 ? 0.7903 1.2308 0.8058 0.0505  0.0782  0.3574  401 VAL B O   
1537 C CB  . VAL A 215 ? 0.7723 1.2337 0.7589 0.0556  0.0981  0.3652  401 VAL B CB  
1538 C CG1 . VAL A 215 ? 0.8176 1.2523 0.7785 0.0635  0.0959  0.3487  401 VAL B CG1 
1539 C CG2 . VAL A 215 ? 0.7488 1.2374 0.7336 0.0531  0.1094  0.3768  401 VAL B CG2 
1540 N N   . LEU A 216 ? 0.7420 1.1850 0.7252 0.0549  0.0849  0.3397  402 LEU B N   
1541 C CA  . LEU A 216 ? 0.7515 1.1771 0.7395 0.0553  0.0737  0.3316  402 LEU B CA  
1542 C C   . LEU A 216 ? 0.8100 1.2068 0.7767 0.0614  0.0671  0.3204  402 LEU B C   
1543 O O   . LEU A 216 ? 0.8542 1.2476 0.7981 0.0650  0.0711  0.3130  402 LEU B O   
1544 C CB  . LEU A 216 ? 0.7572 1.1972 0.7488 0.0527  0.0758  0.3264  402 LEU B CB  
1545 C CG  . LEU A 216 ? 0.7456 1.1771 0.7512 0.0510  0.0649  0.3214  402 LEU B CG  
1546 C CD1 . LEU A 216 ? 0.7447 1.1856 0.7764 0.0446  0.0619  0.3299  402 LEU B CD1 
1547 C CD2 . LEU A 216 ? 0.7454 1.1900 0.7538 0.0498  0.0681  0.3149  402 LEU B CD2 
1548 N N   . HIS A 217 ? 0.7904 1.1681 0.7648 0.0615  0.0577  0.3186  403 HIS B N   
1549 C CA  . HIS A 217 ? 0.7918 1.1446 0.7482 0.0645  0.0509  0.3066  403 HIS B CA  
1550 C C   . HIS A 217 ? 0.8336 1.1774 0.7912 0.0629  0.0405  0.2997  403 HIS B C   
1551 O O   . HIS A 217 ? 0.8386 1.1798 0.8158 0.0600  0.0338  0.3016  403 HIS B O   
1552 C CB  . HIS A 217 ? 0.8433 1.1827 0.8096 0.0645  0.0482  0.3068  403 HIS B CB  
1553 C CG  . HIS A 217 ? 0.8655 1.2077 0.8254 0.0673  0.0566  0.3101  403 HIS B CG  
1554 N ND1 . HIS A 217 ? 0.7974 1.1529 0.7398 0.0696  0.0660  0.3117  403 HIS B ND1 
1555 C CD2 . HIS A 217 ? 0.8054 1.1397 0.7763 0.0681  0.0570  0.3117  403 HIS B CD2 
1556 C CE1 . HIS A 217 ? 0.7953 1.1510 0.7361 0.0718  0.0716  0.3146  403 HIS B CE1 
1557 N NE2 . HIS A 217 ? 0.8533 1.1959 0.8124 0.0711  0.0659  0.3148  403 HIS B NE2 
1558 N N   . LEU A 218 ? 0.8358 1.1751 0.7730 0.0646  0.0389  0.2923  404 LEU B N   
1559 C CA  . LEU A 218 ? 0.8065 1.1384 0.7441 0.0631  0.0282  0.2871  404 LEU B CA  
1560 C C   . LEU A 218 ? 0.8224 1.1340 0.7376 0.0627  0.0205  0.2769  404 LEU B C   
1561 O O   . LEU A 218 ? 0.8241 1.1312 0.7149 0.0645  0.0241  0.2720  404 LEU B O   
1562 C CB  . LEU A 218 ? 0.7962 1.1408 0.7328 0.0641  0.0312  0.2878  404 LEU B CB  
1563 C CG  . LEU A 218 ? 0.7792 1.1484 0.7378 0.0622  0.0401  0.2955  404 LEU B CG  
1564 C CD1 . LEU A 218 ? 0.8409 1.2220 0.8012 0.0626  0.0433  0.2930  404 LEU B CD1 
1565 C CD2 . LEU A 218 ? 0.7799 1.1526 0.7649 0.0582  0.0342  0.2998  404 LEU B CD2 
1566 N N   . GLN A 219 ? 0.8774 1.1785 0.8005 0.0592  0.0104  0.2730  405 GLN B N   
1567 C CA  . GLN A 219 ? 0.8499 1.1354 0.7539 0.0559  0.0021  0.2626  405 GLN B CA  
1568 C C   . GLN A 219 ? 0.8555 1.1396 0.7554 0.0539  -0.0087 0.2618  405 GLN B C   
1569 O O   . GLN A 219 ? 0.8921 1.1818 0.8127 0.0532  -0.0139 0.2661  405 GLN B O   
1570 C CB  . GLN A 219 ? 0.8595 1.1369 0.7761 0.0518  -0.0015 0.2575  405 GLN B CB  
1571 C CG  . GLN A 219 ? 0.8596 1.1330 0.7759 0.0528  0.0067  0.2547  405 GLN B CG  
1572 C CD  . GLN A 219 ? 0.8478 1.1317 0.7880 0.0562  0.0146  0.2664  405 GLN B CD  
1573 O OE1 . GLN A 219 ? 0.8419 1.1345 0.8021 0.0559  0.0130  0.2745  405 GLN B OE1 
1574 N NE2 . GLN A 219 ? 0.8448 1.1288 0.7837 0.0587  0.0228  0.2675  405 GLN B NE2 
1575 N N   . LEU A 220 ? 0.8636 1.1406 0.7377 0.0525  -0.0124 0.2566  406 LEU B N   
1576 C CA  . LEU A 220 ? 0.8699 1.1456 0.7393 0.0507  -0.0232 0.2579  406 LEU B CA  
1577 C C   . LEU A 220 ? 0.9349 1.2013 0.7963 0.0428  -0.0356 0.2512  406 LEU B C   
1578 O O   . LEU A 220 ? 1.0034 1.2619 0.8406 0.0381  -0.0373 0.2434  406 LEU B O   
1579 C CB  . LEU A 220 ? 0.8682 1.1433 0.7153 0.0532  -0.0197 0.2580  406 LEU B CB  
1580 C CG  . LEU A 220 ? 0.8500 1.1373 0.7036 0.0598  -0.0059 0.2629  406 LEU B CG  
1581 C CD1 . LEU A 220 ? 0.8497 1.1364 0.6851 0.0617  -0.0044 0.2625  406 LEU B CD1 
1582 C CD2 . LEU A 220 ? 0.8371 1.1385 0.7233 0.0615  -0.0043 0.2700  406 LEU B CD2 
1583 N N   . MET A 221 ? 0.8953 1.1645 0.7767 0.0404  -0.0443 0.2535  407 MET B N   
1584 C CA  . MET A 221 ? 0.9228 1.1871 0.8010 0.0319  -0.0549 0.2468  407 MET B CA  
1585 C C   . MET A 221 ? 1.0054 1.2673 0.8647 0.0267  -0.0675 0.2477  407 MET B C   
1586 O O   . MET A 221 ? 1.0235 1.2889 0.8937 0.0248  -0.0786 0.2524  407 MET B O   
1587 C CB  . MET A 221 ? 0.9089 1.1781 0.8156 0.0313  -0.0585 0.2488  407 MET B CB  
1588 C CG  . MET A 221 ? 0.8988 1.1702 0.8254 0.0347  -0.0476 0.2491  407 MET B CG  
1589 S SD  . MET A 221 ? 1.0270 1.2905 0.9481 0.0289  -0.0430 0.2370  407 MET B SD  
1590 C CE  . MET A 221 ? 0.8956 1.1590 0.8138 0.0363  -0.0282 0.2407  407 MET B CE  
1591 N N   . ARG A 222 ? 0.9261 1.1823 0.7569 0.0239  -0.0661 0.2431  408 ARG B N   
1592 C CA  . ARG A 222 ? 0.9399 1.1938 0.7498 0.0177  -0.0781 0.2449  408 ARG B CA  
1593 C C   . ARG A 222 ? 0.9577 1.2098 0.7512 0.0043  -0.0858 0.2347  408 ARG B C   
1594 O O   . ARG A 222 ? 0.9932 1.2409 0.7601 -0.0019 -0.0844 0.2268  408 ARG B O   
1595 C CB  . ARG A 222 ? 0.9523 1.2023 0.7405 0.0219  -0.0719 0.2466  408 ARG B CB  
1596 C CG  . ARG A 222 ? 0.9291 1.1759 0.7055 0.0251  -0.0570 0.2386  408 ARG B CG  
1597 C CD  . ARG A 222 ? 0.9294 1.1721 0.6786 0.0270  -0.0523 0.2380  408 ARG B CD  
1598 N NE  . ARG A 222 ? 0.9162 1.1641 0.6765 0.0362  -0.0476 0.2479  408 ARG B NE  
1599 C CZ  . ARG A 222 ? 0.9208 1.1685 0.6784 0.0360  -0.0556 0.2550  408 ARG B CZ  
1600 N NH1 . ARG A 222 ? 0.9393 1.1820 0.6815 0.0269  -0.0702 0.2557  408 ARG B NH1 
1601 N NH2 . ARG A 222 ? 0.9068 1.1607 0.6792 0.0443  -0.0488 0.2616  408 ARG B NH2 
1602 N N   . PHE A 223 ? 0.9634 1.2205 0.7734 -0.0011 -0.0937 0.2339  409 PHE B N   
1603 C CA  . PHE A 223 ? 1.0068 1.2669 0.8052 -0.0157 -0.1016 0.2240  409 PHE B CA  
1604 C C   . PHE A 223 ? 1.0571 1.3250 0.8760 -0.0195 -0.1120 0.2276  409 PHE B C   
1605 O O   . PHE A 223 ? 1.0821 1.3517 0.9261 -0.0104 -0.1110 0.2351  409 PHE B O   
1606 C CB  . PHE A 223 ? 0.9796 1.2374 0.7767 -0.0198 -0.0905 0.2087  409 PHE B CB  
1607 C CG  . PHE A 223 ? 0.9693 1.2286 0.7977 -0.0145 -0.0829 0.2067  409 PHE B CG  
1608 C CD1 . PHE A 223 ? 0.9654 1.2219 0.8102 -0.0012 -0.0726 0.2139  409 PHE B CD1 
1609 C CD2 . PHE A 223 ? 0.9766 1.2416 0.8182 -0.0239 -0.0856 0.1974  409 PHE B CD2 
1610 C CE1 . PHE A 223 ? 1.0336 1.2917 0.9069 0.0026  -0.0662 0.2134  409 PHE B CE1 
1611 C CE2 . PHE A 223 ? 0.9759 1.2416 0.8472 -0.0191 -0.0784 0.1957  409 PHE B CE2 
1612 C CZ  . PHE A 223 ? 1.0195 1.2811 0.9063 -0.0059 -0.0692 0.2044  409 PHE B CZ  
1613 N N   . MET A 224 ? 1.1520 1.4266 0.9599 -0.0342 -0.1220 0.2214  410 MET B N   
1614 C CA  . MET A 224 ? 1.0423 1.3264 0.8677 -0.0393 -0.1321 0.2240  410 MET B CA  
1615 C C   . MET A 224 ? 1.1488 1.4427 0.9644 -0.0572 -0.1363 0.2106  410 MET B C   
1616 O O   . MET A 224 ? 1.1571 1.4523 0.9467 -0.0686 -0.1379 0.2035  410 MET B O   
1617 C CB  . MET A 224 ? 1.0455 1.3325 0.8708 -0.0377 -0.1472 0.2398  410 MET B CB  
1618 C CG  . MET A 224 ? 1.0820 1.3701 0.8770 -0.0484 -0.1581 0.2436  410 MET B CG  
1619 S SD  . MET A 224 ? 1.4068 1.7015 1.2075 -0.0506 -0.1794 0.2624  410 MET B SD  
1620 C CE  . MET A 224 ? 1.2297 1.5161 1.0584 -0.0295 -0.1735 0.2738  410 MET B CE  
1621 N N   . TYR A 225 ? 1.2258 1.5280 1.0630 -0.0605 -0.1375 0.2064  411 TYR B N   
1622 C CA  . TYR A 225 ? 1.3061 1.6226 1.1388 -0.0788 -0.1429 0.1948  411 TYR B CA  
1623 C C   . TYR A 225 ? 1.3282 1.6537 1.1860 -0.0780 -0.1482 0.1979  411 TYR B C   
1624 O O   . TYR A 225 ? 1.4079 1.7439 1.2767 -0.0878 -0.1453 0.1853  411 TYR B O   
1625 C CB  . TYR A 225 ? 1.3832 1.7001 1.2162 -0.0864 -0.1295 0.1746  411 TYR B CB  
1626 C CG  . TYR A 225 ? 1.4288 1.7635 1.2592 -0.1074 -0.1329 0.1592  411 TYR B CG  
1627 C CD1 . TYR A 225 ? 1.5124 1.8594 1.3160 -0.1246 -0.1452 0.1591  411 TYR B CD1 
1628 C CD2 . TYR A 225 ? 1.4582 1.7991 1.3141 -0.1110 -0.1234 0.1448  411 TYR B CD2 
1629 C CE1 . TYR A 225 ? 1.5898 1.9570 1.3913 -0.1459 -0.1477 0.1443  411 TYR B CE1 
1630 C CE2 . TYR A 225 ? 1.5169 1.8769 1.3729 -0.1312 -0.1249 0.1289  411 TYR B CE2 
1631 C CZ  . TYR A 225 ? 1.5573 1.9315 1.3856 -0.1492 -0.1369 0.1283  411 TYR B CZ  
1632 O OH  . TYR A 225 ? 1.4641 1.8610 1.2928 -0.1715 -0.1377 0.1116  411 TYR B OH  
1633 N N   . GLN A 228 ? 1.4281 1.8537 1.2137 -0.1791 -0.2117 0.1910  414 GLN B N   
1634 C CA  . GLN A 228 ? 1.5502 1.9670 1.3066 -0.1820 -0.2158 0.1970  414 GLN B CA  
1635 C C   . GLN A 228 ? 1.7412 2.1587 1.4844 -0.1930 -0.2013 0.1737  414 GLN B C   
1636 O O   . GLN A 228 ? 1.7736 2.1865 1.5367 -0.1875 -0.1850 0.1572  414 GLN B O   
1637 C CB  . GLN A 228 ? 1.5984 1.9894 1.3599 -0.1573 -0.2141 0.2126  414 GLN B CB  
1638 C CG  . GLN A 228 ? 1.5554 1.9284 1.3289 -0.1421 -0.1938 0.2003  414 GLN B CG  
1639 C CD  . GLN A 228 ? 1.5397 1.8913 1.3145 -0.1212 -0.1914 0.2144  414 GLN B CD  
1640 O OE1 . GLN A 228 ? 1.6339 1.9830 1.4079 -0.1155 -0.2040 0.2329  414 GLN B OE1 
1641 N NE2 . GLN A 228 ? 1.4397 1.7770 1.2172 -0.1105 -0.1751 0.2054  414 GLN B NE2 
1642 N N   . THR A 229 ? 1.9555 2.3788 1.6666 -0.2088 -0.2080 0.1731  415 THR B N   
1643 C CA  . THR A 229 ? 1.9721 2.3978 1.6647 -0.2228 -0.1975 0.1516  415 THR B CA  
1644 C C   . THR A 229 ? 1.9999 2.4267 1.7180 -0.2220 -0.1785 0.1270  415 THR B C   
1645 O O   . THR A 229 ? 1.9735 2.4184 1.7106 -0.2312 -0.1775 0.1185  415 THR B O   
1646 C CB  . THR A 229 ? 1.8645 2.2670 1.5371 -0.2102 -0.1950 0.1589  415 THR B CB  
1647 O OG1 . THR A 229 ? 2.0128 2.4152 1.6659 -0.2116 -0.2130 0.1821  415 THR B OG1 
1648 C CG2 . THR A 229 ? 1.8223 2.2285 1.4710 -0.2268 -0.1869 0.1374  415 THR B CG2 
1649 N N   . ASP A 230 ? 1.7465 2.1562 1.4664 -0.2127 -0.1632 0.1146  416 ASP B N   
1650 C CA  . ASP A 230 ? 1.7123 2.1168 1.4647 -0.2044 -0.1458 0.0983  416 ASP B CA  
1651 C C   . ASP A 230 ? 1.6628 2.0409 1.4204 -0.1830 -0.1332 0.0992  416 ASP B C   
1652 O O   . ASP A 230 ? 1.5626 1.9366 1.3406 -0.1807 -0.1182 0.0820  416 ASP B O   
1653 C CB  . ASP A 230 ? 1.7166 2.1428 1.4742 -0.2288 -0.1376 0.0694  416 ASP B CB  
1654 C CG  . ASP A 230 ? 1.6960 2.1196 1.4936 -0.2216 -0.1210 0.0536  416 ASP B CG  
1655 O OD1 . ASP A 230 ? 1.5552 1.9842 1.3756 -0.2163 -0.1223 0.0594  416 ASP B OD1 
1656 O OD2 . ASP A 230 ? 1.5771 1.9931 1.3841 -0.2211 -0.1070 0.0358  416 ASP B OD2 
1657 N N   . GLN A 231 ? 1.6248 1.9859 1.3670 -0.1675 -0.1384 0.1186  417 GLN B N   
1658 C CA  . GLN A 231 ? 1.5491 1.8895 1.2913 -0.1514 -0.1260 0.1169  417 GLN B CA  
1659 C C   . GLN A 231 ? 1.4771 1.8005 1.2291 -0.1268 -0.1264 0.1388  417 GLN B C   
1660 O O   . GLN A 231 ? 1.4143 1.7398 1.1666 -0.1225 -0.1383 0.1566  417 GLN B O   
1661 C CB  . GLN A 231 ? 1.4510 1.7885 1.1572 -0.1607 -0.1277 0.1119  417 GLN B CB  
1662 C CG  . GLN A 231 ? 1.4895 1.8438 1.1840 -0.1861 -0.1255 0.0874  417 GLN B CG  
1663 C CD  . GLN A 231 ? 1.5709 1.9220 1.2275 -0.1954 -0.1283 0.0835  417 GLN B CD  
1664 O OE1 . GLN A 231 ? 1.5830 1.9216 1.2201 -0.1846 -0.1344 0.1016  417 GLN B OE1 
1665 N NE2 . GLN A 231 ? 1.5764 1.9397 1.2235 -0.2164 -0.1233 0.0587  417 GLN B NE2 
1666 N N   . ASN A 232 ? 1.3745 1.6825 1.1357 -0.1116 -0.1130 0.1368  418 ASN B N   
1667 C CA  . ASN A 232 ? 1.2749 1.5686 1.0423 -0.0902 -0.1110 0.1550  418 ASN B CA  
1668 C C   . ASN A 232 ? 1.1922 1.4779 0.9278 -0.0885 -0.1134 0.1609  418 ASN B C   
1669 O O   . ASN A 232 ? 1.1552 1.4361 0.8757 -0.0919 -0.1052 0.1484  418 ASN B O   
1670 C CB  . ASN A 232 ? 1.2333 1.5173 1.0267 -0.0760 -0.0955 0.1513  418 ASN B CB  
1671 C CG  . ASN A 232 ? 1.2819 1.5726 1.1080 -0.0776 -0.0920 0.1449  418 ASN B CG  
1672 O OD1 . ASN A 232 ? 1.4010 1.7037 1.2317 -0.0871 -0.1008 0.1446  418 ASN B OD1 
1673 N ND2 . ASN A 232 ? 1.1418 1.4253 0.9916 -0.0684 -0.0790 0.1404  418 ASN B ND2 
1674 N N   . ILE A 233 ? 1.1897 1.4742 0.9166 -0.0836 -0.1245 0.1790  419 ILE B N   
1675 C CA  . ILE A 233 ? 1.1983 1.4763 0.8959 -0.0831 -0.1282 0.1859  419 ILE B CA  
1676 C C   . ILE A 233 ? 1.1242 1.3902 0.8323 -0.0619 -0.1210 0.1990  419 ILE B C   
1677 O O   . ILE A 233 ? 1.1181 1.3830 0.8547 -0.0499 -0.1164 0.2046  419 ILE B O   
1678 C CB  . ILE A 233 ? 1.2433 1.5304 0.9238 -0.0958 -0.1469 0.1967  419 ILE B CB  
1679 C CG1 . ILE A 233 ? 1.3638 1.6445 1.0115 -0.0986 -0.1508 0.2018  419 ILE B CG1 
1680 C CG2 . ILE A 233 ? 1.0650 1.3542 0.7695 -0.0862 -0.1564 0.2148  419 ILE B CG2 
1681 C CD1 . ILE A 233 ? 1.1278 1.4190 0.7555 -0.1155 -0.1697 0.2109  419 ILE B CD1 
1682 N N   . LYS A 234 ? 0.9467 1.4013 0.7787 -0.0349 -0.1303 0.1426  420 LYS B N   
1683 C CA  . LYS A 234 ? 0.9253 1.3638 0.7890 -0.0289 -0.1193 0.1496  420 LYS B CA  
1684 C C   . LYS A 234 ? 0.9864 1.4309 0.8803 -0.0261 -0.1292 0.1704  420 LYS B C   
1685 O O   . LYS A 234 ? 1.0409 1.5011 0.9278 -0.0269 -0.1408 0.1885  420 LYS B O   
1686 C CB  . LYS A 234 ? 0.9181 1.3487 0.7704 -0.0255 -0.1037 0.1554  420 LYS B CB  
1687 C CG  . LYS A 234 ? 0.9378 1.3613 0.7673 -0.0264 -0.0909 0.1366  420 LYS B CG  
1688 C CD  . LYS A 234 ? 1.0562 1.4864 0.8598 -0.0260 -0.0828 0.1455  420 LYS B CD  
1689 C CE  . LYS A 234 ? 1.0519 1.4784 0.8742 -0.0223 -0.0777 0.1668  420 LYS B CE  
1690 N NZ  . LYS A 234 ? 1.0570 1.4943 0.8560 -0.0231 -0.0723 0.1806  420 LYS B NZ  
1691 N N   . ILE A 235 ? 0.9279 1.3608 0.8564 -0.0225 -0.1242 0.1683  421 ILE B N   
1692 C CA  . ILE A 235 ? 0.8797 1.3144 0.8433 -0.0182 -0.1287 0.1859  421 ILE B CA  
1693 C C   . ILE A 235 ? 0.9355 1.3568 0.9063 -0.0135 -0.1144 0.1933  421 ILE B C   
1694 O O   . ILE A 235 ? 0.8618 1.2685 0.8437 -0.0112 -0.1016 0.1821  421 ILE B O   
1695 C CB  . ILE A 235 ? 0.8609 1.2924 0.8586 -0.0172 -0.1299 0.1778  421 ILE B CB  
1696 C CG1 . ILE A 235 ? 0.8739 1.3194 0.8675 -0.0233 -0.1451 0.1698  421 ILE B CG1 
1697 C CG2 . ILE A 235 ? 0.8536 1.2861 0.8907 -0.0116 -0.1318 0.1943  421 ILE B CG2 
1698 C CD1 . ILE A 235 ? 0.8594 1.3043 0.8901 -0.0230 -0.1462 0.1638  421 ILE B CD1 
1699 N N   . ASN A 236 ? 0.9306 1.3580 0.8956 -0.0125 -0.1171 0.2129  422 ASN B N   
1700 C CA  . ASN A 236 ? 0.8722 1.2877 0.8453 -0.0094 -0.1044 0.2203  422 ASN B CA  
1701 C C   . ASN A 236 ? 0.8604 1.2675 0.8772 -0.0044 -0.1025 0.2290  422 ASN B C   
1702 O O   . ASN A 236 ? 0.8594 1.2583 0.8894 -0.0023 -0.0950 0.2386  422 ASN B O   
1703 C CB  . ASN A 236 ? 0.8945 1.3202 0.8455 -0.0111 -0.1063 0.2390  422 ASN B CB  
1704 C CG  . ASN A 236 ? 0.9115 1.3463 0.8177 -0.0157 -0.1059 0.2285  422 ASN B CG  
1705 O OD1 . ASN A 236 ? 0.9281 1.3551 0.8221 -0.0169 -0.0981 0.2064  422 ASN B OD1 
1706 N ND2 . ASN A 236 ? 0.9381 1.3902 0.8202 -0.0182 -0.1137 0.2444  422 ASN B ND2 
1707 N N   . ASP A 237 ? 0.8758 1.2845 0.9178 -0.0026 -0.1078 0.2244  423 ASP B N   
1708 C CA  . ASP A 237 ? 0.8528 1.2553 0.9391 0.0029  -0.1057 0.2320  423 ASP B CA  
1709 C C   . ASP A 237 ? 0.8287 1.2127 0.9260 0.0051  -0.0887 0.2182  423 ASP B C   
1710 O O   . ASP A 237 ? 0.8192 1.1967 0.8942 0.0027  -0.0800 0.2010  423 ASP B O   
1711 C CB  . ASP A 237 ? 0.8401 1.2505 0.9517 0.0043  -0.1135 0.2286  423 ASP B CB  
1712 C CG  . ASP A 237 ? 0.8581 1.2896 0.9626 0.0015  -0.1333 0.2422  423 ASP B CG  
1713 O OD1 . ASP A 237 ? 0.8956 1.3358 0.9678 -0.0020 -0.1400 0.2516  423 ASP B OD1 
1714 O OD2 . ASP A 237 ? 0.8566 1.2974 0.9880 0.0025  -0.1422 0.2434  423 ASP B OD2 
1715 N N   . ARG A 238 ? 0.8280 1.2042 0.9618 0.0096  -0.0845 0.2259  424 ARG B N   
1716 C CA  . ARG A 238 ? 0.8517 1.2116 0.9985 0.0112  -0.0695 0.2112  424 ARG B CA  
1717 C C   . ARG A 238 ? 0.8698 1.2274 1.0234 0.0125  -0.0629 0.1914  424 ARG B C   
1718 O O   . ARG A 238 ? 0.8938 1.2586 1.0689 0.0149  -0.0677 0.1934  424 ARG B O   
1719 C CB  . ARG A 238 ? 0.8238 1.1753 1.0118 0.0155  -0.0667 0.2228  424 ARG B CB  
1720 C CG  . ARG A 238 ? 0.8588 1.1938 1.0621 0.0164  -0.0521 0.2052  424 ARG B CG  
1721 C CD  . ARG A 238 ? 0.8884 1.2146 1.1415 0.0216  -0.0492 0.2130  424 ARG B CD  
1722 N NE  . ARG A 238 ? 0.8688 1.1790 1.1359 0.0213  -0.0356 0.1940  424 ARG B NE  
1723 C CZ  . ARG A 238 ? 0.8624 1.1631 1.1306 0.0180  -0.0319 0.1956  424 ARG B CZ  
1724 N NH1 . ARG A 238 ? 0.9744 1.2796 1.2302 0.0151  -0.0386 0.2167  424 ARG B NH1 
1725 N NH2 . ARG A 238 ? 0.8391 1.1265 1.1212 0.0170  -0.0209 0.1752  424 ARG B NH2 
1726 N N   . PHE A 239 ? 0.8304 1.1797 0.9666 0.0107  -0.0519 0.1737  425 PHE B N   
1727 C CA  . PHE A 239 ? 0.8254 1.1732 0.9643 0.0115  -0.0438 0.1565  425 PHE B CA  
1728 C C   . PHE A 239 ? 0.7819 1.1188 0.9175 0.0113  -0.0311 0.1418  425 PHE B C   
1729 O O   . PHE A 239 ? 0.8145 1.1482 0.9264 0.0081  -0.0296 0.1393  425 PHE B O   
1730 C CB  . PHE A 239 ? 0.8282 1.1830 0.9388 0.0079  -0.0473 0.1507  425 PHE B CB  
1731 C CG  . PHE A 239 ? 0.7724 1.1268 0.8870 0.0084  -0.0386 0.1368  425 PHE B CG  
1732 C CD1 . PHE A 239 ? 0.7714 1.1331 0.9106 0.0101  -0.0404 0.1380  425 PHE B CD1 
1733 C CD2 . PHE A 239 ? 0.7856 1.1345 0.8809 0.0071  -0.0286 0.1243  425 PHE B CD2 
1734 C CE1 . PHE A 239 ? 0.7910 1.1536 0.9348 0.0104  -0.0307 0.1272  425 PHE B CE1 
1735 C CE2 . PHE A 239 ? 0.7632 1.1135 0.8607 0.0075  -0.0201 0.1146  425 PHE B CE2 
1736 C CZ  . PHE A 239 ? 0.7626 1.1195 0.8841 0.0090  -0.0203 0.1161  425 PHE B CZ  
1737 N N   . GLU A 240 ? 0.7819 1.1146 0.9413 0.0146  -0.0219 0.1313  426 GLU B N   
1738 C CA  . GLU A 240 ? 0.7838 1.1075 0.9425 0.0141  -0.0107 0.1157  426 GLU B CA  
1739 C C   . GLU A 240 ? 0.7930 1.1204 0.9310 0.0129  -0.0027 0.1004  426 GLU B C   
1740 O O   . GLU A 240 ? 0.7760 1.1099 0.9195 0.0146  -0.0006 0.0994  426 GLU B O   
1741 C CB  . GLU A 240 ? 0.7924 1.1087 0.9912 0.0184  -0.0042 0.1117  426 GLU B CB  
1742 C CG  . GLU A 240 ? 0.8068 1.1188 1.0318 0.0201  -0.0118 0.1300  426 GLU B CG  
1743 C CD  . GLU A 240 ? 0.9043 1.2079 1.1760 0.0255  -0.0048 0.1266  426 GLU B CD  
1744 O OE1 . GLU A 240 ? 0.9718 1.2741 1.2539 0.0280  0.0066  0.1084  426 GLU B OE1 
1745 O OE2 . GLU A 240 ? 0.8175 1.1158 1.1165 0.0273  -0.0098 0.1426  426 GLU B OE2 
1746 N N   . PHE A 241 ? 0.7795 1.1039 0.8952 0.0097  0.0015  0.0903  427 PHE B N   
1747 C CA  . PHE A 241 ? 0.7787 1.1074 0.8741 0.0086  0.0092  0.0777  427 PHE B CA  
1748 C C   . PHE A 241 ? 0.7882 1.1124 0.8821 0.0070  0.0163  0.0621  427 PHE B C   
1749 O O   . PHE A 241 ? 0.7904 1.1091 0.8840 0.0044  0.0124  0.0626  427 PHE B O   
1750 C CB  . PHE A 241 ? 0.7714 1.1048 0.8361 0.0056  0.0042  0.0828  427 PHE B CB  
1751 C CG  . PHE A 241 ? 0.7703 1.1007 0.8227 0.0028  -0.0020 0.0882  427 PHE B CG  
1752 C CD1 . PHE A 241 ? 0.7688 1.0992 0.8232 0.0026  -0.0103 0.1017  427 PHE B CD1 
1753 C CD2 . PHE A 241 ? 0.8206 1.1505 0.8596 0.0002  0.0004  0.0802  427 PHE B CD2 
1754 C CE1 . PHE A 241 ? 0.7696 1.0989 0.8132 0.0001  -0.0138 0.1074  427 PHE B CE1 
1755 C CE2 . PHE A 241 ? 0.7716 1.1004 0.8036 -0.0024 -0.0043 0.0858  427 PHE B CE2 
1756 C CZ  . PHE A 241 ? 0.7935 1.1216 0.8279 -0.0023 -0.0103 0.0995  427 PHE B CZ  
1757 N N   . PRO A 242 ? 0.7964 1.1235 0.8903 0.0082  0.0269  0.0476  428 PRO B N   
1758 C CA  . PRO A 242 ? 0.8101 1.1341 0.9021 0.0060  0.0332  0.0294  428 PRO B CA  
1759 C C   . PRO A 242 ? 0.8153 1.1463 0.8723 0.0014  0.0313  0.0242  428 PRO B C   
1760 O O   . PRO A 242 ? 0.8099 1.1489 0.8450 0.0012  0.0295  0.0323  428 PRO B O   
1761 C CB  . PRO A 242 ? 0.8214 1.1483 0.9265 0.0096  0.0465  0.0161  428 PRO B CB  
1762 C CG  . PRO A 242 ? 0.8120 1.1485 0.9083 0.0115  0.0476  0.0270  428 PRO B CG  
1763 C CD  . PRO A 242 ? 0.7962 1.1307 0.8946 0.0112  0.0344  0.0467  428 PRO B CD  
1764 N N   . GLU A 243 ? 0.8231 1.1513 0.8786 -0.0023 0.0312  0.0107  429 GLU B N   
1765 C CA  . GLU A 243 ? 0.8565 1.1941 0.8817 -0.0068 0.0285  0.0045  429 GLU B CA  
1766 C C   . GLU A 243 ? 0.8655 1.2151 0.8688 -0.0059 0.0370  -0.0034 429 GLU B C   
1767 O O   . GLU A 243 ? 0.8382 1.1987 0.8145 -0.0076 0.0340  0.0021  429 GLU B O   
1768 C CB  . GLU A 243 ? 0.9116 1.2452 0.9438 -0.0120 0.0262  -0.0110 429 GLU B CB  
1769 C CG  . GLU A 243 ? 0.9792 1.3250 0.9830 -0.0173 0.0207  -0.0171 429 GLU B CG  
1770 C CD  . GLU A 243 ? 1.0442 1.3864 1.0590 -0.0237 0.0167  -0.0330 429 GLU B CD  
1771 O OE1 . GLU A 243 ? 0.9451 1.2766 0.9845 -0.0240 0.0225  -0.0478 429 GLU B OE1 
1772 O OE2 . GLU A 243 ? 1.0200 1.3703 1.0224 -0.0284 0.0078  -0.0310 429 GLU B OE2 
1773 N N   . GLN A 244 ? 0.8781 1.2268 0.8945 -0.0030 0.0484  -0.0149 430 GLN B N   
1774 C CA  . GLN A 244 ? 0.8629 1.2241 0.8604 -0.0019 0.0594  -0.0215 430 GLN B CA  
1775 C C   . GLN A 244 ? 0.8548 1.2148 0.8735 0.0036  0.0673  -0.0127 430 GLN B C   
1776 O O   . GLN A 244 ? 0.8546 1.2055 0.9059 0.0070  0.0710  -0.0167 430 GLN B O   
1777 C CB  . GLN A 244 ? 0.8902 1.2546 0.8821 -0.0043 0.0682  -0.0480 430 GLN B CB  
1778 C CG  . GLN A 244 ? 0.9955 1.3625 0.9699 -0.0110 0.0581  -0.0578 430 GLN B CG  
1779 C CD  . GLN A 244 ? 1.1434 1.5142 1.1108 -0.0147 0.0652  -0.0873 430 GLN B CD  
1780 O OE1 . GLN A 244 ? 1.2252 1.5886 1.2147 -0.0120 0.0772  -0.1034 430 GLN B OE1 
1781 N NE2 . GLN A 244 ? 1.2127 1.5957 1.1511 -0.0211 0.0575  -0.0955 430 GLN B NE2 
1782 N N   . LEU A 245 ? 0.8492 1.2190 0.8531 0.0045  0.0696  0.0000  431 LEU B N   
1783 C CA  . LEU A 245 ? 0.8391 1.2093 0.8645 0.0085  0.0743  0.0112  431 LEU B CA  
1784 C C   . LEU A 245 ? 0.8733 1.2563 0.8914 0.0099  0.0904  0.0063  431 LEU B C   
1785 O O   . LEU A 245 ? 0.8920 1.2854 0.8857 0.0081  0.0920  0.0153  431 LEU B O   
1786 C CB  . LEU A 245 ? 0.8197 1.1889 0.8408 0.0077  0.0630  0.0315  431 LEU B CB  
1787 C CG  . LEU A 245 ? 0.8090 1.1786 0.8549 0.0104  0.0640  0.0429  431 LEU B CG  
1788 C CD1 . LEU A 245 ? 0.8048 1.1663 0.8847 0.0134  0.0610  0.0414  431 LEU B CD1 
1789 C CD2 . LEU A 245 ? 0.7949 1.1638 0.8328 0.0084  0.0534  0.0587  431 LEU B CD2 
1790 N N   . PRO A 246 ? 0.9297 1.3131 0.9701 0.0134  0.1037  -0.0066 432 PRO B N   
1791 C CA  . PRO A 246 ? 0.8868 1.2842 0.9231 0.0151  0.1215  -0.0100 432 PRO B CA  
1792 C C   . PRO A 246 ? 0.8649 1.2657 0.9239 0.0172  0.1225  0.0088  432 PRO B C   
1793 O O   . PRO A 246 ? 0.8502 1.2433 0.9436 0.0200  0.1164  0.0148  432 PRO B O   
1794 C CB  . PRO A 246 ? 0.8990 1.2937 0.9573 0.0186  0.1354  -0.0325 432 PRO B CB  
1795 C CG  . PRO A 246 ? 0.9357 1.3135 1.0285 0.0207  0.1238  -0.0307 432 PRO B CG  
1796 C CD  . PRO A 246 ? 0.9068 1.2782 0.9795 0.0162  0.1043  -0.0187 432 PRO B CD  
1797 N N   . LEU A 247 ? 0.8823 1.2955 0.9232 0.0155  0.1294  0.0191  433 LEU B N   
1798 C CA  . LEU A 247 ? 0.8564 1.2733 0.9195 0.0160  0.1299  0.0367  433 LEU B CA  
1799 C C   . LEU A 247 ? 0.9111 1.3441 0.9760 0.0169  0.1507  0.0379  433 LEU B C   
1800 O O   . LEU A 247 ? 0.9235 1.3621 1.0000 0.0156  0.1523  0.0542  433 LEU B O   
1801 C CB  . LEU A 247 ? 0.8420 1.2554 0.8892 0.0122  0.1152  0.0539  433 LEU B CB  
1802 C CG  . LEU A 247 ? 0.8255 1.2248 0.8719 0.0112  0.0958  0.0556  433 LEU B CG  
1803 C CD1 . LEU A 247 ? 0.8338 1.2311 0.8660 0.0081  0.0851  0.0707  433 LEU B CD1 
1804 C CD2 . LEU A 247 ? 0.8131 1.2053 0.8964 0.0138  0.0897  0.0560  433 LEU B CD2 
1805 N N   . ASP A 248 ? 0.9615 1.4026 1.0154 0.0187  0.1673  0.0203  434 ASP B N   
1806 C CA  . ASP A 248 ? 0.9830 1.4417 1.0364 0.0196  0.1897  0.0212  434 ASP B CA  
1807 C C   . ASP A 248 ? 0.9970 1.4581 1.1005 0.0231  0.1975  0.0279  434 ASP B C   
1808 O O   . ASP A 248 ? 0.9693 1.4429 1.0813 0.0220  0.2085  0.0416  434 ASP B O   
1809 C CB  . ASP A 248 ? 0.9766 1.4435 1.0089 0.0210  0.2065  -0.0034 434 ASP B CB  
1810 C CG  . ASP A 248 ? 1.0164 1.4992 0.9965 0.0169  0.2127  -0.0016 434 ASP B CG  
1811 O OD1 . ASP A 248 ? 1.0888 1.5775 1.0549 0.0139  0.2079  0.0214  434 ASP B OD1 
1812 O OD2 . ASP A 248 ? 1.0305 1.5206 0.9844 0.0164  0.2223  -0.0234 434 ASP B OD2 
1813 N N   . GLU A 249 ? 0.9551 1.4054 1.0953 0.0271  0.1911  0.0204  435 GLU B N   
1814 C CA  . GLU A 249 ? 0.9714 1.4269 1.1630 0.0310  0.1983  0.0257  435 GLU B CA  
1815 C C   . GLU A 249 ? 0.9308 1.3873 1.1415 0.0275  0.1852  0.0485  435 GLU B C   
1816 O O   . GLU A 249 ? 0.9428 1.4088 1.1934 0.0291  0.1926  0.0556  435 GLU B O   
1817 C CB  . GLU A 249 ? 0.8801 1.3242 1.1079 0.0365  0.1929  0.0146  435 GLU B CB  
1818 C CG  . GLU A 249 ? 0.9198 1.3472 1.1431 0.0347  0.1671  0.0205  435 GLU B CG  
1819 C CD  . GLU A 249 ? 0.9985 1.4152 1.2583 0.0402  0.1629  0.0123  435 GLU B CD  
1820 O OE1 . GLU A 249 ? 0.8679 1.2902 1.1659 0.0462  0.1780  0.0050  435 GLU B OE1 
1821 O OE2 . GLU A 249 ? 1.0806 1.4836 1.3333 0.0389  0.1453  0.0143  435 GLU B OE2 
1822 N N   . PHE A 250 ? 0.8647 1.3123 1.0502 0.0227  0.1665  0.0588  436 PHE B N   
1823 C CA  . PHE A 250 ? 0.8349 1.2824 1.0357 0.0185  0.1546  0.0771  436 PHE B CA  
1824 C C   . PHE A 250 ? 0.8441 1.3014 1.0275 0.0142  0.1649  0.0894  436 PHE B C   
1825 O O   . PHE A 250 ? 0.8338 1.2911 1.0336 0.0101  0.1576  0.1038  436 PHE B O   
1826 C CB  . PHE A 250 ? 0.8179 1.2504 1.0053 0.0159  0.1299  0.0811  436 PHE B CB  
1827 C CG  . PHE A 250 ? 0.8471 1.2705 1.0529 0.0196  0.1185  0.0738  436 PHE B CG  
1828 C CD1 . PHE A 250 ? 0.7990 1.2244 1.0466 0.0210  0.1098  0.0802  436 PHE B CD1 
1829 C CD2 . PHE A 250 ? 0.8478 1.2618 1.0315 0.0214  0.1160  0.0619  436 PHE B CD2 
1830 C CE1 . PHE A 250 ? 0.7939 1.2121 1.0597 0.0247  0.0990  0.0773  436 PHE B CE1 
1831 C CE2 . PHE A 250 ? 0.8090 1.2140 1.0131 0.0247  0.1063  0.0580  436 PHE B CE2 
1832 C CZ  . PHE A 250 ? 0.7990 1.2062 1.0436 0.0267  0.0980  0.0668  436 PHE B CZ  
1833 N N   . LEU A 251 ? 0.8657 1.3319 1.0172 0.0148  0.1815  0.0843  437 LEU B N   
1834 C CA  . LEU A 251 ? 0.8794 1.3581 1.0173 0.0114  0.1946  0.0988  437 LEU B CA  
1835 C C   . LEU A 251 ? 0.8952 1.3897 1.0685 0.0129  0.2159  0.1019  437 LEU B C   
1836 O O   . LEU A 251 ? 0.8964 1.3963 1.0866 0.0178  0.2283  0.0870  437 LEU B O   
1837 C CB  . LEU A 251 ? 0.9121 1.3977 0.9990 0.0112  0.2032  0.0935  437 LEU B CB  
1838 C CG  . LEU A 251 ? 0.8971 1.3711 0.9482 0.0094  0.1840  0.0927  437 LEU B CG  
1839 C CD1 . LEU A 251 ? 0.9247 1.4105 0.9286 0.0088  0.1932  0.0871  437 LEU B CD1 
1840 C CD2 . LEU A 251 ? 0.8818 1.3483 0.9377 0.0055  0.1703  0.1131  437 LEU B CD2 
1841 N N   . GLN A 252 ? 0.8890 1.3911 1.0772 0.0086  0.2211  0.1213  438 GLN B N   
1842 C CA  . GLN A 252 ? 0.9051 1.4241 1.1301 0.0092  0.2426  0.1266  438 GLN B CA  
1843 C C   . GLN A 252 ? 0.9525 1.4882 1.1528 0.0128  0.2695  0.1169  438 GLN B C   
1844 O O   . GLN A 252 ? 0.9379 1.4844 1.1668 0.0171  0.2872  0.1072  438 GLN B O   
1845 C CB  . GLN A 252 ? 0.8966 1.4203 1.1404 0.0028  0.2440  0.1504  438 GLN B CB  
1846 C CG  . GLN A 252 ? 0.9485 1.4886 1.2435 0.0024  0.2618  0.1572  438 GLN B CG  
1847 C CD  . GLN A 252 ? 0.9911 1.5332 1.3130 -0.0052 0.2606  0.1801  438 GLN B CD  
1848 O OE1 . GLN A 252 ? 0.9085 1.4411 1.2066 -0.0094 0.2510  0.1918  438 GLN B OE1 
1849 N NE2 . GLN A 252 ? 0.9672 1.5213 1.3436 -0.0070 0.2697  0.1862  438 GLN B NE2 
1850 N N   . LYS A 253 ? 1.0345 1.5740 1.1823 0.0112  0.2732  0.1192  439 LYS B N   
1851 C CA  . LYS A 253 ? 0.9973 1.5528 1.1109 0.0139  0.2958  0.1061  439 LYS B CA  
1852 C C   . LYS A 253 ? 0.9898 1.5383 1.0487 0.0132  0.2827  0.0959  439 LYS B C   
1853 O O   . LYS A 253 ? 0.9896 1.5362 1.0208 0.0093  0.2715  0.1125  439 LYS B O   
1854 C CB  . LYS A 253 ? 1.0078 1.5859 1.1137 0.0114  0.3202  0.1247  439 LYS B CB  
1855 C CG  . LYS A 253 ? 1.0667 1.6648 1.1382 0.0143  0.3462  0.1087  439 LYS B CG  
1856 C CD  . LYS A 253 ? 1.1218 1.7449 1.1845 0.0117  0.3722  0.1294  439 LYS B CD  
1857 C CE  . LYS A 253 ? 1.1188 1.7637 1.1444 0.0147  0.3993  0.1102  439 LYS B CE  
1858 N NZ  . LYS A 253 ? 1.2272 1.8995 1.2384 0.0120  0.4262  0.1323  439 LYS B NZ  
1859 N N   . THR A 254 ? 0.9974 1.5417 1.0453 0.0169  0.2837  0.0689  440 THR B N   
1860 C CA  . THR A 254 ? 1.0065 1.5452 1.0070 0.0156  0.2710  0.0564  440 THR B CA  
1861 C C   . THR A 254 ? 1.1029 1.6631 1.0513 0.0130  0.2853  0.0596  440 THR B C   
1862 O O   . THR A 254 ? 1.0682 1.6482 1.0155 0.0134  0.3095  0.0654  440 THR B O   
1863 C CB  . THR A 254 ? 1.0086 1.5374 1.0167 0.0196  0.2705  0.0255  440 THR B CB  
1864 O OG1 . THR A 254 ? 1.0438 1.5894 1.0402 0.0221  0.2969  0.0065  440 THR B OG1 
1865 C CG2 . THR A 254 ? 0.9790 1.4932 1.0447 0.0234  0.2631  0.0248  440 THR B CG2 
1866 N N   . ASP A 255 ? 1.1810 1.7390 1.0861 0.0103  0.2699  0.0565  441 ASP B N   
1867 C CA  . ASP A 255 ? 1.1415 1.7215 0.9923 0.0073  0.2785  0.0597  441 ASP B CA  
1868 C C   . ASP A 255 ? 1.1927 1.7742 1.0091 0.0069  0.2757  0.0276  441 ASP B C   
1869 O O   . ASP A 255 ? 1.2105 1.7766 1.0210 0.0056  0.2531  0.0198  441 ASP B O   
1870 C CB  . ASP A 255 ? 1.1010 1.6814 0.9311 0.0037  0.2615  0.0890  441 ASP B CB  
1871 C CG  . ASP A 255 ? 1.1585 1.7636 0.9318 0.0007  0.2670  0.0956  441 ASP B CG  
1872 O OD1 . ASP A 255 ? 1.2427 1.8696 1.0049 0.0004  0.2894  0.1072  441 ASP B OD1 
1873 O OD2 . ASP A 255 ? 1.1973 1.8022 0.9376 -0.0014 0.2492  0.0901  441 ASP B OD2 
1874 N N   . PRO A 256 ? 1.3663 1.9658 1.1618 0.0077  0.2985  0.0070  442 PRO B N   
1875 C CA  . PRO A 256 ? 1.3865 1.9905 1.1425 0.0056  0.2955  -0.0242 442 PRO B CA  
1876 C C   . PRO A 256 ? 1.3153 1.9314 1.0191 0.0000  0.2781  -0.0114 442 PRO B C   
1877 O O   . PRO A 256 ? 1.3805 2.0086 1.0702 -0.0016 0.2765  0.0212  442 PRO B O   
1878 C CB  . PRO A 256 ? 1.3234 1.9491 1.0650 0.0073  0.3273  -0.0441 442 PRO B CB  
1879 C CG  . PRO A 256 ? 1.2031 1.8262 0.9976 0.0123  0.3452  -0.0310 442 PRO B CG  
1880 C CD  . PRO A 256 ? 1.1685 1.7843 0.9807 0.0107  0.3290  0.0080  442 PRO B CD  
1881 N N   . LYS A 257 ? 1.4733 2.0857 1.1529 -0.0030 0.2639  -0.0366 443 LYS B N   
1882 C CA  . LYS A 257 ? 1.5393 2.1614 1.1753 -0.0084 0.2425  -0.0294 443 LYS B CA  
1883 C C   . LYS A 257 ? 1.5925 2.1968 1.2504 -0.0083 0.2178  -0.0019 443 LYS B C   
1884 O O   . LYS A 257 ? 1.5691 2.1790 1.1999 -0.0119 0.1980  0.0060  443 LYS B O   
1885 C CB  . LYS A 257 ? 1.5447 2.2009 1.1276 -0.0116 0.2526  -0.0132 443 LYS B CB  
1886 C CG  . LYS A 257 ? 1.6743 2.3467 1.2064 -0.0176 0.2323  -0.0156 443 LYS B CG  
1887 C CD  . LYS A 257 ? 1.8728 2.5811 1.3530 -0.0203 0.2411  0.0059  443 LYS B CD  
1888 C CE  . LYS A 257 ? 1.7362 2.4611 1.1726 -0.0260 0.2157  0.0114  443 LYS B CE  
1889 N NZ  . LYS A 257 ? 1.7304 2.4943 1.1110 -0.0290 0.2236  0.0309  443 LYS B NZ  
1890 N N   . ASP A 258 ? 1.3970 1.9809 1.1041 -0.0042 0.2179  0.0113  444 ASP B N   
1891 C CA  . ASP A 258 ? 1.2012 1.7649 0.9324 -0.0039 0.1951  0.0296  444 ASP B CA  
1892 C C   . ASP A 258 ? 1.0577 1.5976 0.8420 0.0000  0.1962  0.0239  444 ASP B C   
1893 O O   . ASP A 258 ? 1.0643 1.5980 0.8786 0.0020  0.1989  0.0448  444 ASP B O   
1894 C CB  . ASP A 258 ? 1.1551 1.7270 0.8806 -0.0044 0.1919  0.0673  444 ASP B CB  
1895 C CG  . ASP A 258 ? 1.1824 1.7386 0.9189 -0.0049 0.1672  0.0826  444 ASP B CG  
1896 O OD1 . ASP A 258 ? 1.1862 1.7219 0.9452 -0.0041 0.1549  0.0683  444 ASP B OD1 
1897 O OD2 . ASP A 258 ? 1.2187 1.7833 0.9426 -0.0057 0.1610  0.1098  444 ASP B OD2 
1898 N N   . PRO A 259 ? 1.0535 1.5802 0.8522 0.0009  0.1937  -0.0039 445 PRO B N   
1899 C CA  . PRO A 259 ? 1.0323 1.5373 0.8815 0.0048  0.1915  -0.0067 445 PRO B CA  
1900 C C   . PRO A 259 ? 0.9860 1.4748 0.8509 0.0042  0.1695  0.0127  445 PRO B C   
1901 O O   . PRO A 259 ? 1.0943 1.5834 0.9351 0.0012  0.1538  0.0191  445 PRO B O   
1902 C CB  . PRO A 259 ? 1.0312 1.5267 0.8869 0.0053  0.1919  -0.0397 445 PRO B CB  
1903 C CG  . PRO A 259 ? 1.0730 1.5878 0.8824 0.0016  0.1999  -0.0581 445 PRO B CG  
1904 C CD  . PRO A 259 ? 1.0984 1.6291 0.8701 -0.0020 0.1910  -0.0335 445 PRO B CD  
1905 N N   . ALA A 260 ? 0.9592 1.4349 0.8657 0.0072  0.1684  0.0215  446 ALA B N   
1906 C CA  . ALA A 260 ? 0.9441 1.4040 0.8665 0.0066  0.1486  0.0365  446 ALA B CA  
1907 C C   . ALA A 260 ? 0.9166 1.3610 0.8462 0.0066  0.1347  0.0208  446 ALA B C   
1908 O O   . ALA A 260 ? 0.8961 1.3264 0.8581 0.0087  0.1283  0.0206  446 ALA B O   
1909 C CB  . ALA A 260 ? 0.9113 1.3656 0.8730 0.0087  0.1512  0.0504  446 ALA B CB  
1910 N N   . ASN A 261 ? 0.9323 1.3811 0.8311 0.0036  0.1293  0.0091  447 ASN B N   
1911 C CA  . ASN A 261 ? 0.9253 1.3610 0.8294 0.0022  0.1165  -0.0051 447 ASN B CA  
1912 C C   . ASN A 261 ? 0.9092 1.3410 0.8011 -0.0003 0.0979  0.0098  447 ASN B C   
1913 O O   . ASN A 261 ? 0.9193 1.3637 0.7824 -0.0025 0.0947  0.0197  447 ASN B O   
1914 C CB  . ASN A 261 ? 0.9553 1.3983 0.8382 -0.0004 0.1222  -0.0314 447 ASN B CB  
1915 C CG  . ASN A 261 ? 0.9719 1.4153 0.8730 0.0029  0.1415  -0.0508 447 ASN B CG  
1916 O OD1 . ASN A 261 ? 1.0358 1.4698 0.9744 0.0075  0.1467  -0.0464 447 ASN B OD1 
1917 N ND2 . ASN A 261 ? 1.1105 1.5663 0.9861 0.0007  0.1521  -0.0731 447 ASN B ND2 
1918 N N   . TYR A 262 ? 0.8863 1.3018 0.8010 0.0003  0.0861  0.0123  448 TYR B N   
1919 C CA  . TYR A 262 ? 0.8695 1.2802 0.7785 -0.0013 0.0705  0.0265  448 TYR B CA  
1920 C C   . TYR A 262 ? 0.8643 1.2649 0.7803 -0.0033 0.0599  0.0156  448 TYR B C   
1921 O O   . TYR A 262 ? 0.8657 1.2573 0.8024 -0.0025 0.0630  0.0022  448 TYR B O   
1922 C CB  . TYR A 262 ? 0.8471 1.2496 0.7765 0.0011  0.0672  0.0444  448 TYR B CB  
1923 C CG  . TYR A 262 ? 0.8512 1.2633 0.7730 0.0016  0.0741  0.0596  448 TYR B CG  
1924 C CD1 . TYR A 262 ? 0.8617 1.2815 0.7909 0.0030  0.0892  0.0585  448 TYR B CD1 
1925 C CD2 . TYR A 262 ? 0.8462 1.2601 0.7567 0.0008  0.0666  0.0757  448 TYR B CD2 
1926 C CE1 . TYR A 262 ? 0.8671 1.2959 0.7920 0.0029  0.0965  0.0744  448 TYR B CE1 
1927 C CE2 . TYR A 262 ? 0.8518 1.2732 0.7595 0.0011  0.0733  0.0913  448 TYR B CE2 
1928 C CZ  . TYR A 262 ? 0.8623 1.2913 0.7769 0.0018  0.0881  0.0913  448 TYR B CZ  
1929 O OH  . TYR A 262 ? 0.8692 1.3058 0.7838 0.0015  0.0956  0.1089  448 TYR B OH  
1930 N N   . ILE A 263 ? 0.8594 1.2621 0.7615 -0.0058 0.0479  0.0226  449 ILE B N   
1931 C CA  . ILE A 263 ? 0.8549 1.2503 0.7637 -0.0087 0.0376  0.0152  449 ILE B CA  
1932 C C   . ILE A 263 ? 0.8323 1.2197 0.7507 -0.0075 0.0280  0.0322  449 ILE B C   
1933 O O   . ILE A 263 ? 0.8269 1.2196 0.7346 -0.0064 0.0253  0.0468  449 ILE B O   
1934 C CB  . ILE A 263 ? 0.8734 1.2820 0.7579 -0.0135 0.0321  0.0056  449 ILE B CB  
1935 C CG1 . ILE A 263 ? 0.9010 1.3189 0.7719 -0.0151 0.0426  -0.0144 449 ILE B CG1 
1936 C CG2 . ILE A 263 ? 0.8700 1.2717 0.7663 -0.0172 0.0213  -0.0010 449 ILE B CG2 
1937 C CD1 . ILE A 263 ? 0.9674 1.4006 0.8123 -0.0209 0.0359  -0.0268 449 ILE B CD1 
1938 N N   . LEU A 264 ? 0.8217 1.1966 0.7612 -0.0076 0.0238  0.0306  450 LEU B N   
1939 C CA  . LEU A 264 ? 0.8041 1.1726 0.7505 -0.0067 0.0160  0.0450  450 LEU B CA  
1940 C C   . LEU A 264 ? 0.8036 1.1793 0.7358 -0.0090 0.0082  0.0496  450 LEU B C   
1941 O O   . LEU A 264 ? 0.8129 1.1934 0.7413 -0.0127 0.0046  0.0400  450 LEU B O   
1942 C CB  . LEU A 264 ? 0.7979 1.1542 0.7674 -0.0068 0.0133  0.0435  450 LEU B CB  
1943 C CG  . LEU A 264 ? 0.7839 1.1353 0.7578 -0.0062 0.0064  0.0576  450 LEU B CG  
1944 C CD1 . LEU A 264 ? 0.7758 1.1275 0.7470 -0.0033 0.0072  0.0681  450 LEU B CD1 
1945 C CD2 . LEU A 264 ? 0.7893 1.1311 0.7850 -0.0067 0.0042  0.0584  450 LEU B CD2 
1946 N N   . HIS A 265 ? 0.7940 1.1709 0.7213 -0.0069 0.0056  0.0637  451 HIS B N   
1947 C CA  . HIS A 265 ? 0.7930 1.1773 0.7117 -0.0077 -0.0009 0.0704  451 HIS B CA  
1948 C C   . HIS A 265 ? 0.7864 1.1637 0.7155 -0.0068 -0.0049 0.0782  451 HIS B C   
1949 O O   . HIS A 265 ? 0.8193 1.1993 0.7522 -0.0090 -0.0098 0.0772  451 HIS B O   
1950 C CB  . HIS A 265 ? 0.7975 1.1908 0.7030 -0.0054 0.0009  0.0808  451 HIS B CB  
1951 C CG  . HIS A 265 ? 0.8014 1.2062 0.6991 -0.0058 -0.0060 0.0873  451 HIS B CG  
1952 N ND1 . HIS A 265 ? 0.7983 1.2055 0.6963 -0.0023 -0.0069 0.1020  451 HIS B ND1 
1953 C CD2 . HIS A 265 ? 0.8092 1.2241 0.7024 -0.0093 -0.0129 0.0812  451 HIS B CD2 
1954 C CE1 . HIS A 265 ? 0.8239 1.2432 0.7185 -0.0029 -0.0140 0.1063  451 HIS B CE1 
1955 N NE2 . HIS A 265 ? 0.8441 1.2692 0.7350 -0.0076 -0.0184 0.0938  451 HIS B NE2 
1956 N N   . ALA A 266 ? 0.7717 1.1414 0.7057 -0.0040 -0.0028 0.0852  452 ALA B N   
1957 C CA  . ALA A 266 ? 0.7637 1.1285 0.7030 -0.0032 -0.0054 0.0914  452 ALA B CA  
1958 C C   . ALA A 266 ? 0.7597 1.1155 0.7076 -0.0029 -0.0049 0.0916  452 ALA B C   
1959 O O   . ALA A 266 ? 0.7599 1.1129 0.7110 -0.0020 -0.0025 0.0908  452 ALA B O   
1960 C CB  . ALA A 266 ? 0.7618 1.1280 0.6972 -0.0002 -0.0047 0.0995  452 ALA B CB  
1961 N N   . VAL A 267 ? 0.7782 1.1312 0.7307 -0.0039 -0.0074 0.0943  453 VAL B N   
1962 C CA  . VAL A 267 ? 0.7567 1.1039 0.7155 -0.0038 -0.0087 0.0977  453 VAL B CA  
1963 C C   . VAL A 267 ? 0.7566 1.1045 0.7084 -0.0033 -0.0096 0.1033  453 VAL B C   
1964 O O   . VAL A 267 ? 0.7575 1.1082 0.7096 -0.0044 -0.0093 0.1059  453 VAL B O   
1965 C CB  . VAL A 267 ? 0.7595 1.1035 0.7315 -0.0057 -0.0098 0.0970  453 VAL B CB  
1966 C CG1 . VAL A 267 ? 0.7609 1.1011 0.7399 -0.0051 -0.0124 0.1043  453 VAL B CG1 
1967 C CG2 . VAL A 267 ? 0.7632 1.1064 0.7422 -0.0062 -0.0072 0.0875  453 VAL B CG2 
1968 N N   . LEU A 268 ? 0.7573 1.1034 0.7041 -0.0021 -0.0099 0.1040  454 LEU B N   
1969 C CA  . LEU A 268 ? 0.7611 1.1079 0.6996 -0.0015 -0.0095 0.1056  454 LEU B CA  
1970 C C   . LEU A 268 ? 0.7672 1.1142 0.7032 -0.0031 -0.0130 0.1096  454 LEU B C   
1971 O O   . LEU A 268 ? 0.7838 1.1295 0.7237 -0.0037 -0.0173 0.1103  454 LEU B O   
1972 C CB  . LEU A 268 ? 0.7624 1.1065 0.6984 -0.0001 -0.0082 0.1022  454 LEU B CB  
1973 C CG  . LEU A 268 ? 0.7602 1.1054 0.6981 0.0022  -0.0044 0.1022  454 LEU B CG  
1974 C CD1 . LEU A 268 ? 0.7567 1.1044 0.6981 0.0021  -0.0042 0.1031  454 LEU B CD1 
1975 C CD2 . LEU A 268 ? 0.7646 1.1049 0.7043 0.0035  -0.0025 0.0999  454 LEU B CD2 
1976 N N   . VAL A 269 ? 0.7725 1.1230 0.7030 -0.0038 -0.0113 0.1138  455 VAL B N   
1977 C CA  . VAL A 269 ? 0.7814 1.1346 0.7084 -0.0055 -0.0144 0.1214  455 VAL B CA  
1978 C C   . VAL A 269 ? 0.7935 1.1516 0.7029 -0.0057 -0.0122 0.1207  455 VAL B C   
1979 O O   . VAL A 269 ? 0.7940 1.1531 0.6988 -0.0042 -0.0060 0.1154  455 VAL B O   
1980 C CB  . VAL A 269 ? 0.7810 1.1350 0.7195 -0.0070 -0.0132 0.1294  455 VAL B CB  
1981 C CG1 . VAL A 269 ? 0.7917 1.1484 0.7305 -0.0084 -0.0170 0.1414  455 VAL B CG1 
1982 C CG2 . VAL A 269 ? 0.7880 1.1369 0.7429 -0.0070 -0.0140 0.1250  455 VAL B CG2 
1983 N N   . HIS A 270 ? 0.8287 1.1910 0.7289 -0.0074 -0.0173 0.1260  456 HIS B N   
1984 C CA  . HIS A 270 ? 0.8234 1.1929 0.7023 -0.0085 -0.0160 0.1249  456 HIS B CA  
1985 C C   . HIS A 270 ? 0.8401 1.2173 0.7148 -0.0104 -0.0180 0.1405  456 HIS B C   
1986 O O   . HIS A 270 ? 0.8739 1.2498 0.7622 -0.0108 -0.0246 0.1504  456 HIS B O   
1987 C CB  . HIS A 270 ? 0.8312 1.2005 0.7014 -0.0098 -0.0230 0.1157  456 HIS B CB  
1988 C CG  . HIS A 270 ? 0.8866 1.2654 0.7322 -0.0123 -0.0250 0.1137  456 HIS B CG  
1989 N ND1 . HIS A 270 ? 0.8928 1.2721 0.7236 -0.0122 -0.0185 0.0996  456 HIS B ND1 
1990 C CD2 . HIS A 270 ? 0.8722 1.2615 0.7051 -0.0149 -0.0330 0.1236  456 HIS B CD2 
1991 C CE1 . HIS A 270 ? 0.8919 1.2819 0.6986 -0.0152 -0.0219 0.0986  456 HIS B CE1 
1992 N NE2 . HIS A 270 ? 0.9142 1.3114 0.7205 -0.0170 -0.0314 0.1144  456 HIS B NE2 
1993 N N   . SER A 271 ? 0.8507 1.2364 0.7084 -0.0112 -0.0115 0.1440  457 SER B N   
1994 C CA  . SER A 271 ? 0.8774 1.2721 0.7300 -0.0132 -0.0126 0.1621  457 SER B CA  
1995 C C   . SER A 271 ? 1.1764 1.5833 0.9991 -0.0153 -0.0164 0.1628  457 SER B C   
1996 O O   . SER A 271 ? 1.0644 1.4748 0.8669 -0.0153 -0.0109 0.1487  457 SER B O   
1997 C CB  . SER A 271 ? 0.8656 1.2635 0.7246 -0.0133 -0.0011 0.1700  457 SER B CB  
1998 O OG  . SER A 271 ? 0.9400 1.3289 0.8278 -0.0131 -0.0015 0.1732  457 SER B OG  
1999 N N   . GLY A 272 ? 1.5486 1.9624 1.3701 -0.0170 -0.0261 0.1793  458 GLY B N   
2000 C CA  . GLY A 272 ? 1.5115 1.9370 1.3096 -0.0194 -0.0369 0.1799  458 GLY B CA  
2001 C C   . GLY A 272 ? 1.6359 2.0799 1.4067 -0.0221 -0.0389 0.1960  458 GLY B C   
2002 O O   . GLY A 272 ? 1.7811 2.2340 1.5504 -0.0236 -0.0527 0.2095  458 GLY B O   
2003 N N   . ASP A 273 ? 1.7757 2.2278 1.5262 -0.0227 -0.0257 0.1970  459 ASP B N   
2004 C CA  . ASP A 273 ? 1.9822 2.4550 1.6986 -0.0259 -0.0275 0.2099  459 ASP B CA  
2005 C C   . ASP A 273 ? 1.8205 2.3021 1.5070 -0.0288 -0.0379 0.1912  459 ASP B C   
2006 O O   . ASP A 273 ? 1.7752 2.2453 1.4730 -0.0284 -0.0437 0.1711  459 ASP B O   
2007 C CB  . ASP A 273 ? 1.9641 2.4458 1.6639 -0.0260 -0.0086 0.2134  459 ASP B CB  
2008 C CG  . ASP A 273 ? 1.9820 2.4571 1.6751 -0.0242 0.0045  0.1854  459 ASP B CG  
2009 O OD1 . ASP A 273 ? 1.9132 2.3764 1.6144 -0.0232 -0.0020 0.1651  459 ASP B OD1 
2010 O OD2 . ASP A 273 ? 1.8046 2.2874 1.4861 -0.0236 0.0214  0.1848  459 ASP B OD2 
2011 N N   . ASN A 274 ? 1.8113 2.3140 1.4593 -0.0323 -0.0403 0.1971  460 ASN B N   
2012 C CA  . ASN A 274 ? 1.8002 2.3139 1.4218 -0.0365 -0.0553 0.1823  460 ASN B CA  
2013 C C   . ASN A 274 ? 1.6746 2.1769 1.2919 -0.0368 -0.0496 0.1459  460 ASN B C   
2014 O O   . ASN A 274 ? 1.5155 2.0109 1.1441 -0.0385 -0.0623 0.1312  460 ASN B O   
2015 C CB  . ASN A 274 ? 1.7254 2.2662 1.3008 -0.0406 -0.0566 0.1934  460 ASN B CB  
2016 C CG  . ASN A 274 ? 1.7432 2.2952 1.3250 -0.0399 -0.0586 0.2332  460 ASN B CG  
2017 O OD1 . ASN A 274 ? 1.7965 2.3377 1.4175 -0.0371 -0.0659 0.2516  460 ASN B OD1 
2018 N ND2 . ASN A 274 ? 1.6538 2.2272 1.1986 -0.0422 -0.0506 0.2466  460 ASN B ND2 
2019 N N   . HIS A 275 ? 1.6069 2.1065 1.2123 -0.0350 -0.0300 0.1319  461 HIS B N   
2020 C CA  . HIS A 275 ? 1.4924 1.9778 1.1033 -0.0342 -0.0240 0.0996  461 HIS B CA  
2021 C C   . HIS A 275 ? 1.5611 2.0258 1.2106 -0.0284 -0.0124 0.0991  461 HIS B C   
2022 O O   . HIS A 275 ? 1.5190 1.9683 1.1967 -0.0271 -0.0195 0.0933  461 HIS B O   
2023 C CB  . HIS A 275 ? 1.4312 1.9270 1.0056 -0.0357 -0.0103 0.0785  461 HIS B CB  
2024 C CG  . HIS A 275 ? 1.4675 1.9763 1.0088 -0.0422 -0.0238 0.0607  461 HIS B CG  
2025 N ND1 . HIS A 275 ? 1.4643 1.9612 1.0161 -0.0447 -0.0323 0.0337  461 HIS B ND1 
2026 C CD2 . HIS A 275 ? 1.5096 2.0435 1.0084 -0.0476 -0.0318 0.0667  461 HIS B CD2 
2027 C CE1 . HIS A 275 ? 1.5028 2.0165 1.0208 -0.0518 -0.0453 0.0213  461 HIS B CE1 
2028 N NE2 . HIS A 275 ? 1.5315 2.0687 1.0149 -0.0536 -0.0457 0.0410  461 HIS B NE2 
2029 N N   . GLY A 276 ? 1.4953 1.9623 1.1451 -0.0253 0.0051  0.1061  462 GLY B N   
2030 C CA  . GLY A 276 ? 1.3316 1.7850 1.0156 -0.0204 0.0156  0.1113  462 GLY B CA  
2031 C C   . GLY A 276 ? 1.3568 1.7907 1.0700 -0.0176 0.0130  0.0963  462 GLY B C   
2032 O O   . GLY A 276 ? 1.6157 2.0435 1.3246 -0.0174 0.0146  0.0734  462 GLY B O   
2033 N N   . GLY A 277 ? 1.1689 1.5932 0.9116 -0.0159 0.0083  0.1096  463 GLY B N   
2034 C CA  . GLY A 277 ? 1.0751 1.4832 0.8448 -0.0133 0.0062  0.0998  463 GLY B CA  
2035 C C   . GLY A 277 ? 0.9865 1.3884 0.7767 -0.0089 0.0190  0.0992  463 GLY B C   
2036 O O   . GLY A 277 ? 1.0042 1.4076 0.7899 -0.0065 0.0313  0.0878  463 GLY B O   
2037 N N   . HIS A 278 ? 0.9567 1.3524 0.7714 -0.0079 0.0157  0.1105  464 HIS B N   
2038 C CA  . HIS A 278 ? 0.8829 1.2749 0.7193 -0.0047 0.0242  0.1119  464 HIS B CA  
2039 C C   . HIS A 278 ? 0.8642 1.2456 0.7225 -0.0039 0.0162  0.1123  464 HIS B C   
2040 O O   . HIS A 278 ? 0.9445 1.3240 0.8087 -0.0060 0.0078  0.1212  464 HIS B O   
2041 C CB  . HIS A 278 ? 0.9088 1.3098 0.7502 -0.0059 0.0305  0.1280  464 HIS B CB  
2042 C CG  . HIS A 278 ? 0.9098 1.3112 0.7727 -0.0033 0.0394  0.1279  464 HIS B CG  
2043 N ND1 . HIS A 278 ? 1.0329 1.4398 0.9119 -0.0051 0.0429  0.1415  464 HIS B ND1 
2044 C CD2 . HIS A 278 ? 0.8743 1.2724 0.7482 0.0008  0.0449  0.1168  464 HIS B CD2 
2045 C CE1 . HIS A 278 ? 0.9927 1.4011 0.8906 -0.0026 0.0490  0.1379  464 HIS B CE1 
2046 N NE2 . HIS A 278 ? 0.9013 1.3047 0.7964 0.0015  0.0503  0.1240  464 HIS B NE2 
2047 N N   . TYR A 279 ? 0.8328 1.2079 0.7036 -0.0006 0.0197  0.1034  465 TYR B N   
2048 C CA  . TYR A 279 ? 0.8149 1.1815 0.7014 0.0002  0.0131  0.1024  465 TYR B CA  
2049 C C   . TYR A 279 ? 0.8009 1.1693 0.7052 0.0016  0.0157  0.1082  465 TYR B C   
2050 O O   . TYR A 279 ? 0.8005 1.1719 0.7123 0.0047  0.0227  0.1059  465 TYR B O   
2051 C CB  . TYR A 279 ? 0.8165 1.1757 0.7046 0.0024  0.0138  0.0903  465 TYR B CB  
2052 C CG  . TYR A 279 ? 0.8582 1.2165 0.7298 0.0000  0.0109  0.0809  465 TYR B CG  
2053 C CD1 . TYR A 279 ? 0.8541 1.2172 0.7104 0.0002  0.0182  0.0726  465 TYR B CD1 
2054 C CD2 . TYR A 279 ? 0.9014 1.2560 0.7731 -0.0029 0.0009  0.0795  465 TYR B CD2 
2055 C CE1 . TYR A 279 ? 0.8738 1.2380 0.7126 -0.0030 0.0145  0.0616  465 TYR B CE1 
2056 C CE2 . TYR A 279 ? 0.8498 1.2059 0.7076 -0.0061 -0.0039 0.0702  465 TYR B CE2 
2057 C CZ  . TYR A 279 ? 0.8715 1.2323 0.7113 -0.0065 0.0023  0.0606  465 TYR B CZ  
2058 O OH  . TYR A 279 ? 0.9546 1.3185 0.7780 -0.0107 -0.0035 0.0489  465 TYR B OH  
2059 N N   . VAL A 280 ? 0.8213 1.1887 0.7342 -0.0007 0.0098  0.1150  466 VAL B N   
2060 C CA  . VAL A 280 ? 0.8016 1.1710 0.7307 -0.0009 0.0096  0.1179  466 VAL B CA  
2061 C C   . VAL A 280 ? 0.7710 1.1345 0.7054 -0.0013 0.0029  0.1151  466 VAL B C   
2062 O O   . VAL A 280 ? 0.7718 1.1302 0.7017 -0.0020 -0.0012 0.1139  466 VAL B O   
2063 C CB  . VAL A 280 ? 0.7819 1.1566 0.7194 -0.0043 0.0108  0.1267  466 VAL B CB  
2064 C CG1 . VAL A 280 ? 0.7944 1.1766 0.7241 -0.0042 0.0190  0.1313  466 VAL B CG1 
2065 C CG2 . VAL A 280 ? 0.7822 1.1517 0.7221 -0.0072 0.0046  0.1314  466 VAL B CG2 
2066 N N   . VAL A 281 ? 0.7867 1.1530 0.7310 -0.0010 0.0018  0.1142  467 VAL B N   
2067 C CA  . VAL A 281 ? 0.7588 1.1222 0.7053 -0.0014 -0.0027 0.1108  467 VAL B CA  
2068 C C   . VAL A 281 ? 0.7570 1.1244 0.7135 -0.0048 -0.0055 0.1103  467 VAL B C   
2069 O O   . VAL A 281 ? 0.7569 1.1317 0.7211 -0.0057 -0.0050 0.1122  467 VAL B O   
2070 C CB  . VAL A 281 ? 0.7573 1.1216 0.7026 0.0020  -0.0019 0.1093  467 VAL B CB  
2071 C CG1 . VAL A 281 ? 0.7574 1.1299 0.7100 0.0041  0.0003  0.1123  467 VAL B CG1 
2072 C CG2 . VAL A 281 ? 0.7553 1.1200 0.7004 0.0012  -0.0052 0.1073  467 VAL B CG2 
2073 N N   . TYR A 282 ? 0.7570 1.1198 0.7160 -0.0068 -0.0082 0.1067  468 TYR B N   
2074 C CA  . TYR A 282 ? 0.7587 1.1236 0.7275 -0.0104 -0.0108 0.1018  468 TYR B CA  
2075 C C   . TYR A 282 ? 0.7600 1.1289 0.7220 -0.0099 -0.0126 0.0951  468 TYR B C   
2076 O O   . TYR A 282 ? 0.7598 1.1250 0.7147 -0.0076 -0.0111 0.0936  468 TYR B O   
2077 C CB  . TYR A 282 ? 0.7618 1.1185 0.7407 -0.0126 -0.0111 0.1009  468 TYR B CB  
2078 C CG  . TYR A 282 ? 0.7644 1.1196 0.7523 -0.0143 -0.0099 0.1102  468 TYR B CG  
2079 C CD1 . TYR A 282 ? 0.7659 1.1201 0.7449 -0.0121 -0.0085 0.1186  468 TYR B CD1 
2080 C CD2 . TYR A 282 ? 0.8084 1.1640 0.8138 -0.0188 -0.0102 0.1107  468 TYR B CD2 
2081 C CE1 . TYR A 282 ? 0.7952 1.1504 0.7791 -0.0138 -0.0068 0.1293  468 TYR B CE1 
2082 C CE2 . TYR A 282 ? 0.8321 1.1870 0.8470 -0.0205 -0.0079 0.1222  468 TYR B CE2 
2083 C CZ  . TYR A 282 ? 0.7859 1.1414 0.7886 -0.0178 -0.0059 0.1324  468 TYR B CZ  
2084 O OH  . TYR A 282 ? 0.7831 1.1402 0.7923 -0.0198 -0.0031 0.1459  468 TYR B OH  
2085 N N   . LEU A 283 ? 0.7673 1.1454 0.7317 -0.0124 -0.0161 0.0917  469 LEU B N   
2086 C CA  . LEU A 283 ? 0.7685 1.1547 0.7225 -0.0120 -0.0185 0.0878  469 LEU B CA  
2087 C C   . LEU A 283 ? 0.7777 1.1713 0.7353 -0.0176 -0.0235 0.0775  469 LEU B C   
2088 O O   . LEU A 283 ? 0.8409 1.2377 0.8119 -0.0214 -0.0267 0.0766  469 LEU B O   
2089 C CB  . LEU A 283 ? 0.7665 1.1616 0.7170 -0.0084 -0.0197 0.0968  469 LEU B CB  
2090 C CG  . LEU A 283 ? 0.7639 1.1540 0.7072 -0.0032 -0.0154 0.1033  469 LEU B CG  
2091 C CD1 . LEU A 283 ? 0.7619 1.1570 0.7110 0.0008  -0.0150 0.1121  469 LEU B CD1 
2092 C CD2 . LEU A 283 ? 0.7710 1.1650 0.7029 -0.0029 -0.0155 0.1022  469 LEU B CD2 
2093 N N   . ASN A 284 ? 0.7874 1.1844 0.7332 -0.0185 -0.0237 0.0689  470 ASN B N   
2094 C CA  . ASN A 284 ? 0.8227 1.2316 0.7642 -0.0237 -0.0297 0.0578  470 ASN B CA  
2095 C C   . ASN A 284 ? 0.8081 1.2318 0.7309 -0.0213 -0.0327 0.0645  470 ASN B C   
2096 O O   . ASN A 284 ? 0.8170 1.2430 0.7237 -0.0200 -0.0290 0.0619  470 ASN B O   
2097 C CB  . ASN A 284 ? 0.8147 1.2174 0.7563 -0.0271 -0.0265 0.0406  470 ASN B CB  
2098 C CG  . ASN A 284 ? 0.8707 1.2685 0.8005 -0.0228 -0.0184 0.0400  470 ASN B CG  
2099 O OD1 . ASN A 284 ? 0.8356 1.2271 0.7655 -0.0178 -0.0144 0.0519  470 ASN B OD1 
2100 N ND2 . ASN A 284 ? 0.9108 1.3124 0.8314 -0.0251 -0.0155 0.0248  470 ASN B ND2 
2101 N N   . PRO A 285 ? 0.8053 1.2404 0.7318 -0.0203 -0.0389 0.0750  471 PRO B N   
2102 C CA  . PRO A 285 ? 0.8104 1.2579 0.7241 -0.0163 -0.0411 0.0873  471 PRO B CA  
2103 C C   . PRO A 285 ? 0.9505 1.4129 0.8427 -0.0193 -0.0451 0.0812  471 PRO B C   
2104 O O   . PRO A 285 ? 1.0131 1.4807 0.8908 -0.0157 -0.0423 0.0910  471 PRO B O   
2105 C CB  . PRO A 285 ? 0.8056 1.2641 0.7344 -0.0154 -0.0481 0.0973  471 PRO B CB  
2106 C CG  . PRO A 285 ? 0.7931 1.2398 0.7412 -0.0168 -0.0446 0.0939  471 PRO B CG  
2107 C CD  . PRO A 285 ? 0.7977 1.2351 0.7443 -0.0223 -0.0429 0.0782  471 PRO B CD  
2108 N N   . LYS A 286 ? 0.9380 1.4078 0.8279 -0.0264 -0.0511 0.0648  472 LYS B N   
2109 C CA  . LYS A 286 ? 0.9163 1.4023 0.7818 -0.0303 -0.0550 0.0553  472 LYS B CA  
2110 C C   . LYS A 286 ? 0.8772 1.3528 0.7312 -0.0310 -0.0442 0.0401  472 LYS B C   
2111 O O   . LYS A 286 ? 0.9125 1.4011 0.7441 -0.0345 -0.0446 0.0288  472 LYS B O   
2112 C CB  . LYS A 286 ? 0.8823 1.3833 0.7513 -0.0386 -0.0679 0.0420  472 LYS B CB  
2113 C CG  . LYS A 286 ? 0.8774 1.3945 0.7589 -0.0381 -0.0799 0.0573  472 LYS B CG  
2114 C CD  . LYS A 286 ? 0.8854 1.4193 0.7497 -0.0327 -0.0834 0.0776  472 LYS B CD  
2115 C CE  . LYS A 286 ? 0.9243 1.4762 0.8055 -0.0316 -0.0959 0.0932  472 LYS B CE  
2116 N NZ  . LYS A 286 ? 0.8664 1.4040 0.7771 -0.0256 -0.0898 0.1053  472 LYS B NZ  
2117 N N   . GLY A 287 ? 0.8913 1.3457 0.7600 -0.0277 -0.0343 0.0397  473 GLY B N   
2118 C CA  . GLY A 287 ? 0.8976 1.3428 0.7620 -0.0277 -0.0237 0.0259  473 GLY B CA  
2119 C C   . GLY A 287 ? 0.8846 1.3286 0.7532 -0.0343 -0.0249 0.0011  473 GLY B C   
2120 O O   . GLY A 287 ? 0.8974 1.3372 0.7609 -0.0344 -0.0157 -0.0136 473 GLY B O   
2121 N N   . ASP A 288 ? 0.8857 1.3333 0.7665 -0.0399 -0.0352 -0.0047 474 ASP B N   
2122 C CA  . ASP A 288 ? 0.9040 1.3510 0.7922 -0.0477 -0.0381 -0.0298 474 ASP B CA  
2123 C C   . ASP A 288 ? 0.8929 1.3169 0.8141 -0.0482 -0.0328 -0.0363 474 ASP B C   
2124 O O   . ASP A 288 ? 0.9223 1.3422 0.8577 -0.0548 -0.0346 -0.0566 474 ASP B O   
2125 C CB  . ASP A 288 ? 0.9138 1.3790 0.8014 -0.0548 -0.0535 -0.0327 474 ASP B CB  
2126 C CG  . ASP A 288 ? 0.9053 1.3697 0.8138 -0.0528 -0.0597 -0.0121 474 ASP B CG  
2127 O OD1 . ASP A 288 ? 0.8881 1.3374 0.8082 -0.0464 -0.0520 0.0028  474 ASP B OD1 
2128 O OD2 . ASP A 288 ? 0.8970 1.3774 0.8105 -0.0579 -0.0722 -0.0113 474 ASP B OD2 
2129 N N   . GLY A 289 ? 0.8701 1.2797 0.8048 -0.0419 -0.0268 -0.0193 475 GLY B N   
2130 C CA  . GLY A 289 ? 0.8613 1.2520 0.8273 -0.0424 -0.0235 -0.0202 475 GLY B CA  
2131 C C   . GLY A 289 ? 0.8653 1.2561 0.8518 -0.0467 -0.0313 -0.0132 475 GLY B C   
2132 O O   . GLY A 289 ? 0.8490 1.2254 0.8630 -0.0483 -0.0289 -0.0132 475 GLY B O   
2133 N N   . LYS A 290 ? 1.0044 1.4119 0.9810 -0.0486 -0.0401 -0.0060 476 LYS B N   
2134 C CA  . LYS A 290 ? 0.9321 1.3425 0.9295 -0.0519 -0.0462 0.0035  476 LYS B CA  
2135 C C   . LYS A 290 ? 0.9462 1.3535 0.9419 -0.0443 -0.0420 0.0266  476 LYS B C   
2136 O O   . LYS A 290 ? 0.9480 1.3669 0.9278 -0.0403 -0.0444 0.0370  476 LYS B O   
2137 C CB  . LYS A 290 ? 0.9434 1.3756 0.9352 -0.0578 -0.0585 -0.0016 476 LYS B CB  
2138 N N   . TRP A 291 ? 0.8416 1.2339 0.8546 -0.0425 -0.0358 0.0344  477 TRP B N   
2139 C CA  . TRP A 291 ? 0.8795 1.2669 0.8870 -0.0356 -0.0306 0.0521  477 TRP B CA  
2140 C C   . TRP A 291 ? 0.7957 1.1889 0.8157 -0.0361 -0.0316 0.0651  477 TRP B C   
2141 O O   . TRP A 291 ? 0.7909 1.1855 0.8323 -0.0419 -0.0337 0.0636  477 TRP B O   
2142 C CB  . TRP A 291 ? 0.8404 1.2110 0.8558 -0.0329 -0.0238 0.0546  477 TRP B CB  
2143 C CG  . TRP A 291 ? 0.8303 1.1958 0.8347 -0.0301 -0.0202 0.0453  477 TRP B CG  
2144 C CD1 . TRP A 291 ? 0.8748 1.2377 0.8833 -0.0332 -0.0192 0.0276  477 TRP B CD1 
2145 C CD2 . TRP A 291 ? 0.7939 1.1573 0.7832 -0.0239 -0.0161 0.0522  477 TRP B CD2 
2146 N NE1 . TRP A 291 ? 0.9074 1.2674 0.9042 -0.0287 -0.0134 0.0242  477 TRP B NE1 
2147 C CE2 . TRP A 291 ? 0.8285 1.1891 0.8147 -0.0233 -0.0120 0.0399  477 TRP B CE2 
2148 C CE3 . TRP A 291 ? 0.7796 1.1434 0.7598 -0.0192 -0.0149 0.0661  477 TRP B CE3 
2149 C CZ2 . TRP A 291 ? 0.8346 1.1937 0.8108 -0.0183 -0.0070 0.0433  477 TRP B CZ2 
2150 C CZ3 . TRP A 291 ? 0.7770 1.1380 0.7474 -0.0149 -0.0112 0.0681  477 TRP B CZ3 
2151 C CH2 . TRP A 291 ? 0.8051 1.1643 0.7745 -0.0146 -0.0074 0.0579  477 TRP B CH2 
2152 N N   . CYS A 292 ? 0.7829 1.1794 0.7913 -0.0300 -0.0289 0.0773  478 CYS B N   
2153 C CA  . CYS A 292 ? 0.8232 1.2248 0.8415 -0.0288 -0.0265 0.0895  478 CYS B CA  
2154 C C   . CYS A 292 ? 0.8153 1.2078 0.8244 -0.0230 -0.0189 0.0991  478 CYS B C   
2155 O O   . CYS A 292 ? 0.7634 1.1494 0.7573 -0.0191 -0.0175 0.0978  478 CYS B O   
2156 C CB  . CYS A 292 ? 0.7702 1.1882 0.7868 -0.0269 -0.0309 0.0933  478 CYS B CB  
2157 S SG  . CYS A 292 ? 0.8281 1.2629 0.8577 -0.0349 -0.0426 0.0840  478 CYS B SG  
2158 N N   . LYS A 293 ? 0.7890 1.1824 0.8076 -0.0231 -0.0140 0.1084  479 LYS B N   
2159 C CA  . LYS A 293 ? 0.7617 1.1502 0.7690 -0.0184 -0.0073 0.1165  479 LYS B CA  
2160 C C   . LYS A 293 ? 0.7595 1.1575 0.7648 -0.0141 -0.0036 0.1207  479 LYS B C   
2161 O O   . LYS A 293 ? 0.7600 1.1683 0.7807 -0.0158 -0.0022 0.1244  479 LYS B O   
2162 C CB  . LYS A 293 ? 0.7665 1.1507 0.7824 -0.0210 -0.0028 0.1249  479 LYS B CB  
2163 C CG  . LYS A 293 ? 0.7693 1.1535 0.7703 -0.0169 0.0039  0.1327  479 LYS B CG  
2164 C CD  . LYS A 293 ? 0.7770 1.1555 0.7778 -0.0187 0.0058  0.1419  479 LYS B CD  
2165 C CE  . LYS A 293 ? 0.7836 1.1673 0.8026 -0.0231 0.0104  0.1526  479 LYS B CE  
2166 N NZ  . LYS A 293 ? 0.7941 1.1737 0.8108 -0.0241 0.0123  0.1655  479 LYS B NZ  
2167 N N   . PHE A 294 ? 0.7581 1.1525 0.7484 -0.0087 -0.0015 0.1199  480 PHE B N   
2168 C CA  . PHE A 294 ? 0.7579 1.1586 0.7490 -0.0036 0.0031  0.1226  480 PHE B CA  
2169 C C   . PHE A 294 ? 0.7635 1.1597 0.7451 -0.0012 0.0117  0.1245  480 PHE B C   
2170 O O   . PHE A 294 ? 0.7657 1.1536 0.7329 0.0012  0.0126  0.1211  480 PHE B O   
2171 C CB  . PHE A 294 ? 0.7560 1.1554 0.7404 0.0005  -0.0002 0.1202  480 PHE B CB  
2172 C CG  . PHE A 294 ? 0.7552 1.1631 0.7446 -0.0016 -0.0087 0.1192  480 PHE B CG  
2173 C CD1 . PHE A 294 ? 0.7564 1.1610 0.7395 -0.0060 -0.0141 0.1131  480 PHE B CD1 
2174 C CD2 . PHE A 294 ? 0.7557 1.1764 0.7564 0.0009  -0.0114 0.1239  480 PHE B CD2 
2175 C CE1 . PHE A 294 ? 0.7603 1.1745 0.7437 -0.0086 -0.0218 0.1099  480 PHE B CE1 
2176 C CE2 . PHE A 294 ? 0.7585 1.1903 0.7607 -0.0017 -0.0209 0.1234  480 PHE B CE2 
2177 C CZ  . PHE A 294 ? 0.7619 1.1907 0.7530 -0.0068 -0.0261 0.1154  480 PHE B CZ  
2178 N N   . ASP A 295 ? 0.8028 1.2061 0.7926 -0.0027 0.0182  0.1298  481 ASP B N   
2179 C CA  . ASP A 295 ? 0.7781 1.1812 0.7562 -0.0008 0.0278  0.1316  481 ASP B CA  
2180 C C   . ASP A 295 ? 0.7815 1.1920 0.7665 0.0045  0.0366  0.1297  481 ASP B C   
2181 O O   . ASP A 295 ? 0.7855 1.2068 0.7833 0.0045  0.0445  0.1344  481 ASP B O   
2182 C CB  . ASP A 295 ? 0.7878 1.1949 0.7696 -0.0057 0.0315  0.1405  481 ASP B CB  
2183 C CG  . ASP A 295 ? 0.8423 1.2505 0.8046 -0.0046 0.0400  0.1432  481 ASP B CG  
2184 O OD1 . ASP A 295 ? 0.8376 1.2424 0.7841 -0.0005 0.0422  0.1350  481 ASP B OD1 
2185 O OD2 . ASP A 295 ? 0.8888 1.3020 0.8518 -0.0081 0.0444  0.1535  481 ASP B OD2 
2186 N N   . ASP A 296 ? 0.7810 1.1855 0.7610 0.0095  0.0360  0.1231  482 ASP B N   
2187 C CA  . ASP A 296 ? 0.7847 1.1939 0.7767 0.0158  0.0440  0.1206  482 ASP B CA  
2188 C C   . ASP A 296 ? 0.8992 1.3217 0.9177 0.0166  0.0423  0.1273  482 ASP B C   
2189 O O   . ASP A 296 ? 0.9014 1.3259 0.9275 0.0155  0.0316  0.1300  482 ASP B O   
2190 C CB  . ASP A 296 ? 0.8000 1.2119 0.7837 0.0177  0.0579  0.1167  482 ASP B CB  
2191 C CG  . ASP A 296 ? 0.8703 1.2713 0.8283 0.0174  0.0586  0.1078  482 ASP B CG  
2192 O OD1 . ASP A 296 ? 0.8199 1.2104 0.7750 0.0187  0.0522  0.1024  482 ASP B OD1 
2193 O OD2 . ASP A 296 ? 0.9913 1.3959 0.9326 0.0153  0.0654  0.1067  482 ASP B OD2 
2194 N N   . ASP A 297 ? 0.8699 1.3035 0.9024 0.0181  0.0529  0.1301  483 ASP B N   
2195 C CA  . ASP A 297 ? 0.7892 1.2385 0.8517 0.0186  0.0516  0.1371  483 ASP B CA  
2196 C C   . ASP A 297 ? 0.7829 1.2387 0.8533 0.0102  0.0428  0.1426  483 ASP B C   
2197 O O   . ASP A 297 ? 0.8683 1.3376 0.9633 0.0089  0.0370  0.1472  483 ASP B O   
2198 C CB  . ASP A 297 ? 0.7986 1.2585 0.8766 0.0231  0.0679  0.1379  483 ASP B CB  
2199 C CG  . ASP A 297 ? 0.8716 1.3347 0.9385 0.0182  0.0780  0.1403  483 ASP B CG  
2200 O OD1 . ASP A 297 ? 0.9363 1.3886 0.9758 0.0144  0.0756  0.1381  483 ASP B OD1 
2201 O OD2 . ASP A 297 ? 0.8885 1.3661 0.9756 0.0182  0.0885  0.1458  483 ASP B OD2 
2202 N N   . VAL A 298 ? 0.7730 1.2202 0.8261 0.0045  0.0412  0.1423  484 VAL B N   
2203 C CA  . VAL A 298 ? 0.7697 1.2200 0.8337 -0.0037 0.0343  0.1463  484 VAL B CA  
2204 C C   . VAL A 298 ? 0.7636 1.2046 0.8175 -0.0065 0.0204  0.1407  484 VAL B C   
2205 O O   . VAL A 298 ? 0.7645 1.1922 0.7969 -0.0061 0.0191  0.1371  484 VAL B O   
2206 C CB  . VAL A 298 ? 0.7782 1.2254 0.8349 -0.0079 0.0422  0.1520  484 VAL B CB  
2207 C CG1 . VAL A 298 ? 0.7763 1.2253 0.8520 -0.0165 0.0358  0.1566  484 VAL B CG1 
2208 C CG2 . VAL A 298 ? 0.7884 1.2461 0.8494 -0.0048 0.0584  0.1569  484 VAL B CG2 
2209 N N   . VAL A 299 ? 0.7593 1.2091 0.8291 -0.0096 0.0101  0.1394  485 VAL B N   
2210 C CA  . VAL A 299 ? 0.7573 1.2018 0.8184 -0.0133 -0.0020 0.1326  485 VAL B CA  
2211 C C   . VAL A 299 ? 0.7596 1.2077 0.8385 -0.0223 -0.0074 0.1308  485 VAL B C   
2212 O O   . VAL A 299 ? 0.7881 1.2510 0.8910 -0.0256 -0.0102 0.1332  485 VAL B O   
2213 C CB  . VAL A 299 ? 0.7558 1.2090 0.8167 -0.0098 -0.0106 0.1315  485 VAL B CB  
2214 C CG1 . VAL A 299 ? 0.7578 1.2063 0.8042 -0.0136 -0.0209 0.1236  485 VAL B CG1 
2215 C CG2 . VAL A 299 ? 0.7551 1.2042 0.8071 -0.0008 -0.0039 0.1346  485 VAL B CG2 
2216 N N   . SER A 300 ? 0.7620 1.1968 0.8331 -0.0263 -0.0089 0.1265  486 SER B N   
2217 C CA  . SER A 300 ? 0.7665 1.2008 0.8583 -0.0350 -0.0121 0.1243  486 SER B CA  
2218 C C   . SER A 300 ? 0.7700 1.1934 0.8535 -0.0383 -0.0196 0.1123  486 SER B C   
2219 O O   . SER A 300 ? 0.7683 1.1830 0.8293 -0.0338 -0.0198 0.1086  486 SER B O   
2220 C CB  . SER A 300 ? 0.7702 1.1987 0.8703 -0.0366 -0.0018 0.1351  486 SER B CB  
2221 O OG  . SER A 300 ? 0.7710 1.1862 0.8479 -0.0322 0.0026  0.1375  486 SER B OG  
2222 N N   . ARG A 301 ? 0.7926 1.2170 0.8971 -0.0466 -0.0253 0.1051  487 ARG B N   
2223 C CA  . ARG A 301 ? 0.7835 1.1967 0.8848 -0.0503 -0.0302 0.0913  487 ARG B CA  
2224 C C   . ARG A 301 ? 0.7852 1.1806 0.8906 -0.0497 -0.0230 0.0967  487 ARG B C   
2225 O O   . ARG A 301 ? 0.7853 1.1792 0.9042 -0.0505 -0.0163 0.1103  487 ARG B O   
2226 C CB  . ARG A 301 ? 0.8398 1.2601 0.9643 -0.0600 -0.0390 0.0788  487 ARG B CB  
2227 C CG  . ARG A 301 ? 0.8859 1.3238 0.9999 -0.0610 -0.0500 0.0698  487 ARG B CG  
2228 C CD  . ARG A 301 ? 0.9458 1.3784 1.0356 -0.0604 -0.0540 0.0545  487 ARG B CD  
2229 N NE  . ARG A 301 ? 0.9852 1.4056 1.0894 -0.0675 -0.0546 0.0387  487 ARG B NE  
2230 C CZ  . ARG A 301 ? 0.8933 1.3064 0.9820 -0.0677 -0.0551 0.0227  487 ARG B CZ  
2231 N NH1 . ARG A 301 ? 0.9124 1.3301 0.9696 -0.0616 -0.0551 0.0219  487 ARG B NH1 
2232 N NH2 . ARG A 301 ? 0.9012 1.3022 1.0089 -0.0740 -0.0545 0.0072  487 ARG B NH2 
2233 N N   . CYS A 302 ? 0.8912 1.2748 0.9855 -0.0482 -0.0241 0.0872  488 CYS B N   
2234 C CA  . CYS A 302 ? 0.8403 1.2081 0.9411 -0.0468 -0.0188 0.0930  488 CYS B CA  
2235 C C   . CYS A 302 ? 0.7994 1.1565 0.9055 -0.0488 -0.0213 0.0763  488 CYS B C   
2236 O O   . CYS A 302 ? 0.8027 1.1651 0.8956 -0.0494 -0.0258 0.0607  488 CYS B O   
2237 C CB  . CYS A 302 ? 0.7835 1.1485 0.8606 -0.0388 -0.0141 0.1044  488 CYS B CB  
2238 S SG  . CYS A 302 ? 0.8271 1.1940 0.8738 -0.0328 -0.0167 0.0945  488 CYS B SG  
2239 N N   . THR A 303 ? 0.8053 1.1482 0.9314 -0.0495 -0.0177 0.0803  489 THR B N   
2240 C CA  . THR A 303 ? 0.8152 1.1463 0.9521 -0.0505 -0.0178 0.0641  489 THR B CA  
2241 C C   . THR A 303 ? 0.8104 1.1392 0.9223 -0.0430 -0.0159 0.0609  489 THR B C   
2242 O O   . THR A 303 ? 0.8003 1.1316 0.8942 -0.0372 -0.0143 0.0748  489 THR B O   
2243 C CB  . THR A 303 ? 0.8237 1.1397 0.9953 -0.0524 -0.0141 0.0723  489 THR B CB  
2244 O OG1 . THR A 303 ? 0.8801 1.1926 1.0449 -0.0459 -0.0105 0.0933  489 THR B OG1 
2245 C CG2 . THR A 303 ? 0.8545 1.1732 1.0537 -0.0602 -0.0146 0.0791  489 THR B CG2 
2246 N N   . LYS A 304 ? 0.8198 1.1444 0.9318 -0.0435 -0.0156 0.0412  490 LYS B N   
2247 C CA  . LYS A 304 ? 0.8368 1.1593 0.9309 -0.0368 -0.0121 0.0384  490 LYS B CA  
2248 C C   . LYS A 304 ? 0.8140 1.1248 0.9239 -0.0319 -0.0083 0.0524  490 LYS B C   
2249 O O   . LYS A 304 ? 0.8067 1.1187 0.9019 -0.0260 -0.0068 0.0586  490 LYS B O   
2250 C CB  . LYS A 304 ? 0.8313 1.1533 0.9230 -0.0387 -0.0104 0.0136  490 LYS B CB  
2251 C CG  . LYS A 304 ? 0.8302 1.1562 0.8980 -0.0326 -0.0062 0.0104  490 LYS B CG  
2252 C CD  . LYS A 304 ? 0.8969 1.2319 0.9472 -0.0356 -0.0058 -0.0120 490 LYS B CD  
2253 C CE  . LYS A 304 ? 0.9428 1.2681 1.0165 -0.0399 -0.0023 -0.0346 490 LYS B CE  
2254 N NZ  . LYS A 304 ? 1.1252 1.4363 1.2203 -0.0340 0.0068  -0.0350 490 LYS B NZ  
2255 N N   . GLU A 305 ? 0.8209 1.1215 0.9629 -0.0345 -0.0074 0.0587  491 GLU B N   
2256 C CA  . GLU A 305 ? 0.8198 1.1123 0.9772 -0.0298 -0.0057 0.0775  491 GLU B CA  
2257 C C   . GLU A 305 ? 0.8089 1.1106 0.9440 -0.0272 -0.0080 0.0989  491 GLU B C   
2258 O O   . GLU A 305 ? 0.8057 1.1072 0.9351 -0.0220 -0.0085 0.1109  491 GLU B O   
2259 C CB  . GLU A 305 ? 0.8319 1.1123 1.0306 -0.0335 -0.0043 0.0832  491 GLU B CB  
2260 C CG  . GLU A 305 ? 0.8927 1.1599 1.1205 -0.0346 -0.0005 0.0620  491 GLU B CG  
2261 C CD  . GLU A 305 ? 0.8833 1.1533 1.1085 -0.0421 -0.0016 0.0361  491 GLU B CD  
2262 O OE1 . GLU A 305 ? 0.9313 1.2147 1.1330 -0.0458 -0.0061 0.0366  491 GLU B OE1 
2263 O OE2 . GLU A 305 ? 0.9532 1.2131 1.2009 -0.0443 0.0018  0.0146  491 GLU B OE2 
2264 N N   . GLU A 306 ? 0.8306 1.1413 0.9548 -0.0309 -0.0092 0.1032  492 GLU B N   
2265 C CA  . GLU A 306 ? 0.8097 1.1292 0.9125 -0.0284 -0.0094 0.1204  492 GLU B CA  
2266 C C   . GLU A 306 ? 0.7889 1.1146 0.8609 -0.0235 -0.0105 0.1156  492 GLU B C   
2267 O O   . GLU A 306 ? 0.7862 1.1155 0.8429 -0.0202 -0.0110 0.1272  492 GLU B O   
2268 C CB  . GLU A 306 ? 0.7975 1.1258 0.9006 -0.0331 -0.0086 0.1246  492 GLU B CB  
2269 C CG  . GLU A 306 ? 0.7978 1.1355 0.8814 -0.0308 -0.0062 0.1409  492 GLU B CG  
2270 C CD  . GLU A 306 ? 0.9624 1.3094 1.0528 -0.0351 -0.0033 0.1454  492 GLU B CD  
2271 O OE1 . GLU A 306 ? 0.8272 1.1730 0.9409 -0.0408 -0.0046 0.1379  492 GLU B OE1 
2272 O OE2 . GLU A 306 ? 1.0331 1.3894 1.1071 -0.0331 0.0005  0.1555  492 GLU B OE2 
2273 N N   . ALA A 307 ? 0.7865 1.1138 0.8498 -0.0234 -0.0110 0.0986  493 ALA B N   
2274 C CA  . ALA A 307 ? 0.7791 1.1120 0.8169 -0.0193 -0.0112 0.0957  493 ALA B CA  
2275 C C   . ALA A 307 ? 0.8086 1.1361 0.8478 -0.0152 -0.0102 0.0943  493 ALA B C   
2276 O O   . ALA A 307 ? 0.7879 1.1187 0.8113 -0.0119 -0.0108 0.0985  493 ALA B O   
2277 C CB  . ALA A 307 ? 0.7790 1.1192 0.8053 -0.0210 -0.0121 0.0820  493 ALA B CB  
2278 N N   . ILE A 308 ? 0.8080 1.1274 0.8691 -0.0153 -0.0084 0.0878  494 ILE B N   
2279 C CA  . ILE A 308 ? 0.7866 1.1027 0.8530 -0.0110 -0.0062 0.0844  494 ILE B CA  
2280 C C   . ILE A 308 ? 0.7901 1.0996 0.8804 -0.0087 -0.0078 0.0980  494 ILE B C   
2281 O O   . ILE A 308 ? 0.8221 1.1351 0.9067 -0.0056 -0.0111 0.1095  494 ILE B O   
2282 C CB  . ILE A 308 ? 0.7948 1.1086 0.8675 -0.0118 -0.0011 0.0642  494 ILE B CB  
2283 C CG1 . ILE A 308 ? 0.7940 1.1178 0.8401 -0.0141 -0.0013 0.0543  494 ILE B CG1 
2284 C CG2 . ILE A 308 ? 0.7959 1.1078 0.8771 -0.0069 0.0034  0.0609  494 ILE B CG2 
2285 C CD1 . ILE A 308 ? 0.9119 1.2374 0.9557 -0.0155 0.0035  0.0338  494 ILE B CD1 
2286 N N   . GLU A 309 ? 0.7993 1.1000 0.9180 -0.0105 -0.0064 0.0977  495 GLU B N   
2287 C CA  . GLU A 309 ? 0.8052 1.0995 0.9520 -0.0074 -0.0079 0.1123  495 GLU B CA  
2288 C C   . GLU A 309 ? 0.8045 1.1046 0.9423 -0.0077 -0.0136 0.1360  495 GLU B C   
2289 O O   . GLU A 309 ? 0.8071 1.1092 0.9522 -0.0041 -0.0179 0.1511  495 GLU B O   
2290 C CB  . GLU A 309 ? 0.8176 1.0993 1.0015 -0.0093 -0.0041 0.1065  495 GLU B CB  
2291 C CG  . GLU A 309 ? 0.8890 1.1632 1.0942 -0.0063 0.0023  0.0875  495 GLU B CG  
2292 C CD  . GLU A 309 ? 0.9564 1.2330 1.1435 -0.0096 0.0070  0.0608  495 GLU B CD  
2293 O OE1 . GLU A 309 ? 0.8258 1.1070 0.9957 -0.0153 0.0045  0.0562  495 GLU B OE1 
2294 O OE2 . GLU A 309 ? 1.0323 1.3081 1.2231 -0.0064 0.0135  0.0451  495 GLU B OE2 
2295 N N   . HIS A 310 ? 0.8031 1.1077 0.9250 -0.0119 -0.0137 0.1396  496 HIS B N   
2296 C CA  . HIS A 310 ? 0.8065 1.1180 0.9180 -0.0125 -0.0168 0.1609  496 HIS B CA  
2297 C C   . HIS A 310 ? 0.8013 1.1231 0.8807 -0.0101 -0.0206 0.1644  496 HIS B C   
2298 O O   . HIS A 310 ? 0.8082 1.1372 0.8760 -0.0103 -0.0237 0.1809  496 HIS B O   
2299 C CB  . HIS A 310 ? 0.8276 1.1417 0.9362 -0.0178 -0.0136 0.1624  496 HIS B CB  
2300 C CG  . HIS A 310 ? 0.8286 1.1330 0.9731 -0.0215 -0.0110 0.1648  496 HIS B CG  
2301 N ND1 . HIS A 310 ? 0.8521 1.1585 1.0037 -0.0272 -0.0081 0.1663  496 HIS B ND1 
2302 C CD2 . HIS A 310 ? 0.8900 1.1824 1.0697 -0.0205 -0.0105 0.1659  496 HIS B CD2 
2303 C CE1 . HIS A 310 ? 0.8507 1.1460 1.0399 -0.0304 -0.0064 0.1677  496 HIS B CE1 
2304 N NE2 . HIS A 310 ? 0.8343 1.1202 1.0415 -0.0261 -0.0075 0.1672  496 HIS B NE2 
2305 N N   . ASN A 311 ? 0.7922 1.1154 0.8576 -0.0083 -0.0203 0.1495  497 ASN B N   
2306 C CA  . ASN A 311 ? 0.7886 1.1197 0.8289 -0.0066 -0.0238 0.1507  497 ASN B CA  
2307 C C   . ASN A 311 ? 0.7890 1.1207 0.8393 -0.0033 -0.0285 0.1529  497 ASN B C   
2308 O O   . ASN A 311 ? 0.8067 1.1440 0.8407 -0.0026 -0.0317 0.1504  497 ASN B O   
2309 C CB  . ASN A 311 ? 0.7795 1.1127 0.7999 -0.0071 -0.0204 0.1359  497 ASN B CB  
2310 C CG  . ASN A 311 ? 0.7795 1.1166 0.7871 -0.0097 -0.0175 0.1369  497 ASN B CG  
2311 O OD1 . ASN A 311 ? 0.7839 1.1269 0.7763 -0.0100 -0.0181 0.1451  497 ASN B OD1 
2312 N ND2 . ASN A 311 ? 0.8562 1.1916 0.8703 -0.0117 -0.0143 0.1278  497 ASN B ND2 
2313 N N   . TYR A 312 ? 0.7936 1.1196 0.8742 -0.0013 -0.0288 0.1574  498 TYR B N   
2314 C CA  . TYR A 312 ? 0.7942 1.1222 0.8905 0.0024  -0.0330 0.1605  498 TYR B CA  
2315 C C   . TYR A 312 ? 0.8020 1.1403 0.8902 0.0026  -0.0434 0.1786  498 TYR B C   
2316 O O   . TYR A 312 ? 0.8370 1.1817 0.9281 0.0043  -0.0492 0.1794  498 TYR B O   
2317 C CB  . TYR A 312 ? 0.7991 1.1178 0.9344 0.0053  -0.0293 0.1601  498 TYR B CB  
2318 C CG  . TYR A 312 ? 0.7950 1.1064 0.9367 0.0054  -0.0195 0.1377  498 TYR B CG  
2319 C CD1 . TYR A 312 ? 0.7868 1.1022 0.9013 0.0038  -0.0160 0.1233  498 TYR B CD1 
2320 C CD2 . TYR A 312 ? 0.8024 1.1035 0.9776 0.0070  -0.0137 0.1311  498 TYR B CD2 
2321 C CE1 . TYR A 312 ? 0.7871 1.0989 0.9032 0.0036  -0.0075 0.1042  498 TYR B CE1 
2322 C CE2 . TYR A 312 ? 0.8032 1.0995 0.9802 0.0066  -0.0045 0.1084  498 TYR B CE2 
2323 C CZ  . TYR A 312 ? 0.7961 1.0990 0.9413 0.0047  -0.0019 0.0957  498 TYR B CZ  
2324 O OH  . TYR A 312 ? 0.8008 1.1019 0.9440 0.0039  0.0067  0.0745  498 TYR B OH  
2325 N N   . GLY A 313 ? 0.8117 1.1535 0.8893 0.0003  -0.0459 0.1932  499 GLY B N   
2326 C CA  . GLY A 313 ? 0.8240 1.1785 0.8870 -0.0003 -0.0560 0.2100  499 GLY B CA  
2327 C C   . GLY A 313 ? 0.8380 1.1952 0.9269 0.0018  -0.0626 0.2336  499 GLY B C   
2328 O O   . GLY A 313 ? 0.8365 1.1850 0.9626 0.0052  -0.0606 0.2355  499 GLY B O   
2329 N N   . HIS A 323 ? 1.6571 2.1156 1.4589 -0.0234 -0.0227 0.2743  509 HIS B N   
2330 C CA  . HIS A 323 ? 1.5793 2.0197 1.4048 -0.0213 -0.0170 0.2534  509 HIS B CA  
2331 C C   . HIS A 323 ? 1.5073 1.9330 1.3652 -0.0193 -0.0273 0.2504  509 HIS B C   
2332 O O   . HIS A 323 ? 1.3178 1.7312 1.2078 -0.0185 -0.0235 0.2528  509 HIS B O   
2333 C CB  . HIS A 323 ? 1.6109 2.0477 1.4547 -0.0219 -0.0023 0.2592  509 HIS B CB  
2334 C CG  . HIS A 323 ? 1.8309 2.2794 1.6487 -0.0227 0.0120  0.2533  509 HIS B CG  
2335 N ND1 . HIS A 323 ? 1.8688 2.3157 1.6706 -0.0209 0.0168  0.2277  509 HIS B ND1 
2336 C CD2 . HIS A 323 ? 1.9403 2.4026 1.7480 -0.0247 0.0238  0.2698  509 HIS B CD2 
2337 C CE1 . HIS A 323 ? 1.9753 2.4341 1.7586 -0.0213 0.0313  0.2270  509 HIS B CE1 
2338 N NE2 . HIS A 323 ? 1.9574 2.4266 1.7426 -0.0238 0.0361  0.2523  509 HIS B NE2 
2339 N N   . CYS A 324 ? 1.3783 1.8063 1.2285 -0.0187 -0.0401 0.2447  510 CYS B N   
2340 C CA  . CYS A 324 ? 1.1766 1.5927 1.0573 -0.0164 -0.0487 0.2412  510 CYS B CA  
2341 C C   . CYS A 324 ? 1.1015 1.5045 0.9890 -0.0150 -0.0432 0.2159  510 CYS B C   
2342 O O   . CYS A 324 ? 1.0865 1.4911 0.9551 -0.0154 -0.0446 0.1989  510 CYS B O   
2343 C CB  . CYS A 324 ? 0.9944 1.4206 0.8676 -0.0167 -0.0645 0.2459  510 CYS B CB  
2344 S SG  . CYS A 324 ? 1.0219 1.4363 0.9323 -0.0135 -0.0733 0.2386  510 CYS B SG  
2345 N N   . THR A 325 ? 0.9696 1.3599 0.8847 -0.0137 -0.0374 0.2135  511 THR B N   
2346 C CA  . THR A 325 ? 1.0027 1.3828 0.9236 -0.0124 -0.0328 0.1926  511 THR B CA  
2347 C C   . THR A 325 ? 0.8660 1.2403 0.8015 -0.0105 -0.0404 0.1850  511 THR B C   
2348 O O   . THR A 325 ? 0.8344 1.2064 0.7923 -0.0094 -0.0457 0.1950  511 THR B O   
2349 C CB  . THR A 325 ? 0.9757 1.3478 0.9170 -0.0127 -0.0243 0.1917  511 THR B CB  
2350 O OG1 . THR A 325 ? 1.0900 1.4528 1.0612 -0.0117 -0.0275 0.1938  511 THR B OG1 
2351 C CG2 . THR A 325 ? 0.8656 1.2446 0.8045 -0.0150 -0.0180 0.2072  511 THR B CG2 
2352 N N   . ASN A 326 ? 0.8286 1.2005 0.7545 -0.0101 -0.0401 0.1681  512 ASN B N   
2353 C CA  . ASN A 326 ? 0.8163 1.1839 0.7567 -0.0087 -0.0453 0.1608  512 ASN B CA  
2354 C C   . ASN A 326 ? 0.8008 1.1605 0.7442 -0.0076 -0.0381 0.1452  512 ASN B C   
2355 O O   . ASN A 326 ? 0.8007 1.1603 0.7285 -0.0080 -0.0330 0.1371  512 ASN B O   
2356 C CB  . ASN A 326 ? 0.8268 1.2028 0.7549 -0.0103 -0.0550 0.1589  512 ASN B CB  
2357 C CG  . ASN A 326 ? 0.8442 1.2312 0.7704 -0.0113 -0.0649 0.1764  512 ASN B CG  
2358 O OD1 . ASN A 326 ? 0.8425 1.2297 0.7928 -0.0095 -0.0709 0.1870  512 ASN B OD1 
2359 N ND2 . ASN A 326 ? 0.8635 1.2609 0.7613 -0.0138 -0.0664 0.1801  512 ASN B ND2 
2360 N N   . ALA A 327 ? 0.7902 1.1439 0.7542 -0.0060 -0.0374 0.1417  513 ALA B N   
2361 C CA  . ALA A 327 ? 0.7788 1.1274 0.7446 -0.0050 -0.0315 0.1292  513 ALA B CA  
2362 C C   . ALA A 327 ? 0.7971 1.1472 0.7620 -0.0051 -0.0349 0.1233  513 ALA B C   
2363 O O   . ALA A 327 ? 0.7872 1.1401 0.7652 -0.0050 -0.0409 0.1270  513 ALA B O   
2364 C CB  . ALA A 327 ? 0.7722 1.1155 0.7581 -0.0036 -0.0276 0.1267  513 ALA B CB  
2365 N N   . TYR A 328 ? 0.7760 1.1246 0.7295 -0.0055 -0.0313 0.1151  514 TYR B N   
2366 C CA  . TYR A 328 ? 0.7774 1.1263 0.7325 -0.0067 -0.0342 0.1094  514 TYR B CA  
2367 C C   . TYR A 328 ? 0.7691 1.1138 0.7317 -0.0056 -0.0275 0.1037  514 TYR B C   
2368 O O   . TYR A 328 ? 0.7692 1.1142 0.7415 -0.0067 -0.0291 0.1011  514 TYR B O   
2369 C CB  . TYR A 328 ? 0.7887 1.1396 0.7260 -0.0088 -0.0366 0.1046  514 TYR B CB  
2370 C CG  . TYR A 328 ? 0.7883 1.1354 0.7146 -0.0074 -0.0284 0.0997  514 TYR B CG  
2371 C CD1 . TYR A 328 ? 0.7902 1.1396 0.7074 -0.0065 -0.0247 0.1041  514 TYR B CD1 
2372 C CD2 . TYR A 328 ? 0.7870 1.1289 0.7162 -0.0069 -0.0242 0.0921  514 TYR B CD2 
2373 C CE1 . TYR A 328 ? 0.7899 1.1377 0.7014 -0.0047 -0.0173 0.1003  514 TYR B CE1 
2374 C CE2 . TYR A 328 ? 0.7874 1.1267 0.7113 -0.0047 -0.0170 0.0892  514 TYR B CE2 
2375 C CZ  . TYR A 328 ? 0.7884 1.1313 0.7036 -0.0034 -0.0137 0.0929  514 TYR B CZ  
2376 O OH  . TYR A 328 ? 0.8169 1.1589 0.7310 -0.0008 -0.0066 0.0907  514 TYR B OH  
2377 N N   . MET A 329 ? 0.7638 1.1061 0.7230 -0.0038 -0.0206 0.1027  515 MET B N   
2378 C CA  . MET A 329 ? 0.7595 1.1003 0.7229 -0.0027 -0.0146 0.1002  515 MET B CA  
2379 C C   . MET A 329 ? 0.7560 1.0981 0.7199 -0.0014 -0.0101 0.1001  515 MET B C   
2380 O O   . MET A 329 ? 0.7559 1.0986 0.7145 -0.0014 -0.0104 0.1008  515 MET B O   
2381 C CB  . MET A 329 ? 0.7620 1.1003 0.7181 -0.0022 -0.0118 0.0982  515 MET B CB  
2382 C CG  . MET A 329 ? 0.7602 1.0981 0.7211 -0.0009 -0.0059 0.0996  515 MET B CG  
2383 S SD  . MET A 329 ? 0.7655 1.0984 0.7264 0.0003  -0.0030 0.0993  515 MET B SD  
2384 C CE  . MET A 329 ? 0.7652 1.1008 0.7318 0.0021  0.0033  0.1070  515 MET B CE  
2385 N N   . LEU A 330 ? 0.7552 1.0989 0.7258 -0.0007 -0.0054 0.0985  516 LEU B N   
2386 C CA  . LEU A 330 ? 0.7564 1.1028 0.7254 -0.0002 -0.0009 0.0952  516 LEU B CA  
2387 C C   . LEU A 330 ? 0.7595 1.1103 0.7219 0.0005  0.0048  0.0959  516 LEU B C   
2388 O O   . LEU A 330 ? 0.7601 1.1109 0.7278 0.0006  0.0074  0.0991  516 LEU B O   
2389 C CB  . LEU A 330 ? 0.7577 1.1039 0.7414 0.0003  0.0008  0.0918  516 LEU B CB  
2390 C CG  . LEU A 330 ? 0.7568 1.0997 0.7516 0.0002  -0.0054 0.0952  516 LEU B CG  
2391 C CD1 . LEU A 330 ? 0.7589 1.1016 0.7747 0.0018  -0.0030 0.0931  516 LEU B CD1 
2392 C CD2 . LEU A 330 ? 0.7577 1.0985 0.7466 -0.0009 -0.0080 0.0962  516 LEU B CD2 
2393 N N   . VAL A 331 ? 0.7634 1.1190 0.7154 0.0004  0.0062  0.0939  517 VAL B N   
2394 C CA  . VAL A 331 ? 0.7702 1.1332 0.7129 0.0009  0.0107  0.0968  517 VAL B CA  
2395 C C   . VAL A 331 ? 0.7876 1.1573 0.7242 -0.0001 0.0146  0.0886  517 VAL B C   
2396 O O   . VAL A 331 ? 0.8108 1.1814 0.7445 -0.0016 0.0113  0.0816  517 VAL B O   
2397 C CB  . VAL A 331 ? 0.7707 1.1370 0.7050 0.0017  0.0073  0.1030  517 VAL B CB  
2398 C CG1 . VAL A 331 ? 0.7803 1.1556 0.7061 0.0026  0.0111  0.1100  517 VAL B CG1 
2399 C CG2 . VAL A 331 ? 0.7647 1.1232 0.7057 0.0029  0.0050  0.1073  517 VAL B CG2 
2400 N N   . TYR A 332 ? 0.7870 1.1620 0.7226 0.0004  0.0224  0.0886  518 TYR B N   
2401 C CA  . TYR A 332 ? 0.8006 1.1835 0.7276 -0.0005 0.0285  0.0787  518 TYR B CA  
2402 C C   . TYR A 332 ? 0.8143 1.2102 0.7220 -0.0007 0.0324  0.0854  518 TYR B C   
2403 O O   . TYR A 332 ? 0.8618 1.2588 0.7711 0.0005  0.0344  0.0988  518 TYR B O   
2404 C CB  . TYR A 332 ? 0.8024 1.1831 0.7449 0.0006  0.0370  0.0725  518 TYR B CB  
2405 C CG  . TYR A 332 ? 0.7949 1.1657 0.7566 0.0010  0.0335  0.0653  518 TYR B CG  
2406 C CD1 . TYR A 332 ? 0.7819 1.1449 0.7594 0.0019  0.0276  0.0728  518 TYR B CD1 
2407 C CD2 . TYR A 332 ? 0.8037 1.1733 0.7682 0.0003  0.0355  0.0514  518 TYR B CD2 
2408 C CE1 . TYR A 332 ? 0.7777 1.1335 0.7725 0.0025  0.0236  0.0700  518 TYR B CE1 
2409 C CE2 . TYR A 332 ? 0.7985 1.1583 0.7848 0.0011  0.0325  0.0478  518 TYR B CE2 
2410 C CZ  . TYR A 332 ? 0.7854 1.1390 0.7863 0.0024  0.0264  0.0589  518 TYR B CZ  
2411 O OH  . TYR A 332 ? 0.7827 1.1285 0.8050 0.0033  0.0226  0.0591  518 TYR B OH  
2412 N N   . ILE A 333 ? 0.8299 1.2363 0.7203 -0.0026 0.0331  0.0762  519 ILE B N   
2413 C CA  . ILE A 333 ? 0.8481 1.2708 0.7160 -0.0032 0.0359  0.0829  519 ILE B CA  
2414 C C   . ILE A 333 ? 0.8772 1.3091 0.7338 -0.0044 0.0469  0.0695  519 ILE B C   
2415 O O   . ILE A 333 ? 0.8731 1.3021 0.7320 -0.0061 0.0473  0.0506  519 ILE B O   
2416 C CB  . ILE A 333 ? 0.8536 1.2853 0.7066 -0.0051 0.0246  0.0846  519 ILE B CB  
2417 C CG1 . ILE A 333 ? 0.8642 1.2873 0.7308 -0.0031 0.0163  0.0972  519 ILE B CG1 
2418 C CG2 . ILE A 333 ? 0.9144 1.3661 0.7424 -0.0058 0.0262  0.0933  519 ILE B CG2 
2419 C CD1 . ILE A 333 ? 0.8439 1.2771 0.7021 -0.0042 0.0056  0.1010  519 ILE B CD1 
2420 N N   . ARG A 334 ? 0.9407 1.3838 0.7871 -0.0035 0.0570  0.0792  520 ARG B N   
2421 C CA  . ARG A 334 ? 0.9042 1.3582 0.7386 -0.0042 0.0705  0.0668  520 ARG B CA  
2422 C C   . ARG A 334 ? 0.9279 1.3956 0.7337 -0.0079 0.0666  0.0516  520 ARG B C   
2423 O O   . ARG A 334 ? 0.9776 1.4558 0.7647 -0.0097 0.0559  0.0603  520 ARG B O   
2424 C CB  . ARG A 334 ? 0.9598 1.4254 0.7878 -0.0030 0.0827  0.0839  520 ARG B CB  
2425 C CG  . ARG A 334 ? 0.9353 1.4095 0.7607 -0.0027 0.1009  0.0721  520 ARG B CG  
2426 C CD  . ARG A 334 ? 0.9858 1.4741 0.8040 -0.0021 0.1138  0.0920  520 ARG B CD  
2427 N NE  . ARG A 334 ? 1.1260 1.6222 0.9481 -0.0012 0.1337  0.0822  520 ARG B NE  
2428 C CZ  . ARG A 334 ? 0.9536 1.4437 0.8079 0.0009  0.1440  0.0877  520 ARG B CZ  
2429 N NH1 . ARG A 334 ? 0.9632 1.4391 0.8463 0.0015  0.1359  0.1021  520 ARG B NH1 
2430 N NH2 . ARG A 334 ? 0.9703 1.4699 0.8287 0.0020  0.1632  0.0774  520 ARG B NH2 
2431 N N   . GLU A 335 ? 0.9423 1.4104 0.7470 -0.0090 0.0751  0.0281  521 GLU B N   
2432 C CA  . GLU A 335 ? 0.9672 1.4466 0.7474 -0.0136 0.0709  0.0080  521 GLU B CA  
2433 C C   . GLU A 335 ? 0.9969 1.5021 0.7379 -0.0158 0.0724  0.0164  521 GLU B C   
2434 O O   . GLU A 335 ? 1.0511 1.5691 0.7698 -0.0199 0.0597  0.0134  521 GLU B O   
2435 C CB  . GLU A 335 ? 0.9801 1.4534 0.7706 -0.0139 0.0826  -0.0202 521 GLU B CB  
2436 C CG  . GLU A 335 ? 1.1228 1.5946 0.9087 -0.0190 0.0740  -0.0454 521 GLU B CG  
2437 C CD  . GLU A 335 ? 1.3267 1.7868 1.1337 -0.0183 0.0859  -0.0727 521 GLU B CD  
2438 O OE1 . GLU A 335 ? 1.2611 1.7228 1.0741 -0.0144 0.1034  -0.0760 521 GLU B OE1 
2439 O OE2 . GLU A 335 ? 1.4431 1.8923 1.2647 -0.0216 0.0783  -0.0903 521 GLU B OE2 
2440 N N   . SER A 336 ? 1.0081 1.5229 0.7414 -0.0133 0.0873  0.0288  522 SER B N   
2441 C CA  . SER A 336 ? 1.0396 1.5809 0.7346 -0.0152 0.0900  0.0409  522 SER B CA  
2442 C C   . SER A 336 ? 1.1373 1.6844 0.8267 -0.0149 0.0742  0.0687  522 SER B C   
2443 O O   . SER A 336 ? 1.2295 1.7999 0.8861 -0.0174 0.0686  0.0775  522 SER B O   
2444 C CB  . SER A 336 ? 1.0524 1.6019 0.7458 -0.0125 0.1113  0.0514  522 SER B CB  
2445 O OG  . SER A 336 ? 1.0231 1.5579 0.7497 -0.0086 0.1137  0.0737  522 SER B OG  
2446 N N   . LYS A 337 ? 1.0721 1.5997 0.7933 -0.0118 0.0668  0.0828  523 LYS B N   
2447 C CA  . LYS A 337 ? 1.0829 1.6132 0.8062 -0.0104 0.0541  0.1088  523 LYS B CA  
2448 C C   . LYS A 337 ? 1.0597 1.5836 0.7910 -0.0118 0.0357  0.1020  523 LYS B C   
2449 O O   . LYS A 337 ? 0.9775 1.5017 0.7167 -0.0098 0.0254  0.1218  523 LYS B O   
2450 C CB  . LYS A 337 ? 0.9683 1.4824 0.7223 -0.0061 0.0598  0.1292  523 LYS B CB  
2451 C CG  . LYS A 337 ? 0.9762 1.4957 0.7305 -0.0051 0.0786  0.1373  523 LYS B CG  
2452 C CD  . LYS A 337 ? 1.1062 1.6515 0.8296 -0.0059 0.0827  0.1567  523 LYS B CD  
2453 C CE  . LYS A 337 ? 1.0938 1.6456 0.8197 -0.0052 0.1033  0.1673  523 LYS B CE  
2454 N NZ  . LYS A 337 ? 1.1245 1.7033 0.8182 -0.0061 0.1081  0.1894  523 LYS B NZ  
2455 N N   . LEU A 338 ? 1.0420 1.5599 0.7748 -0.0152 0.0325  0.0750  524 LEU B N   
2456 C CA  . LEU A 338 ? 0.9874 1.4956 0.7365 -0.0165 0.0175  0.0695  524 LEU B CA  
2457 C C   . LEU A 338 ? 0.9756 1.5036 0.7084 -0.0187 0.0019  0.0802  524 LEU B C   
2458 O O   . LEU A 338 ? 0.9987 1.5213 0.7494 -0.0169 -0.0085 0.0925  524 LEU B O   
2459 C CB  . LEU A 338 ? 1.0050 1.5037 0.7614 -0.0203 0.0181  0.0396  524 LEU B CB  
2460 C CG  . LEU A 338 ? 0.9345 1.4220 0.7119 -0.0223 0.0049  0.0340  524 LEU B CG  
2461 C CD1 . LEU A 338 ? 0.9091 1.3789 0.7133 -0.0174 0.0040  0.0516  524 LEU B CD1 
2462 C CD2 . LEU A 338 ? 0.9382 1.4147 0.7272 -0.0260 0.0075  0.0063  524 LEU B CD2 
2463 N N   . SER A 339 ? 1.0194 1.5719 0.7186 -0.0226 0.0000  0.0755  525 SER B N   
2464 C CA  . SER A 339 ? 1.0135 1.5882 0.6976 -0.0252 -0.0173 0.0857  525 SER B CA  
2465 C C   . SER A 339 ? 1.0085 1.5897 0.6976 -0.0195 -0.0202 0.1215  525 SER B C   
2466 O O   . SER A 339 ? 1.0378 1.6250 0.7380 -0.0185 -0.0347 0.1348  525 SER B O   
2467 C CB  . SER A 339 ? 1.0558 1.6579 0.6990 -0.0314 -0.0192 0.0714  525 SER B CB  
2468 O OG  . SER A 339 ? 1.0868 1.6828 0.7296 -0.0373 -0.0190 0.0361  525 SER B OG  
2469 N N   . GLU A 340 ? 1.0132 1.5932 0.6984 -0.0157 -0.0061 0.1376  526 GLU B N   
2470 C CA  . GLU A 340 ? 1.0115 1.5961 0.7056 -0.0104 -0.0075 0.1722  526 GLU B CA  
2471 C C   . GLU A 340 ? 1.0064 1.5650 0.7412 -0.0054 -0.0085 0.1808  526 GLU B C   
2472 O O   . GLU A 340 ? 0.9699 1.5311 0.7196 -0.0015 -0.0169 0.2026  526 GLU B O   
2473 C CB  . GLU A 340 ? 1.0303 1.6216 0.7101 -0.0089 0.0091  0.1867  526 GLU B CB  
2474 C CG  . GLU A 340 ? 1.0475 1.6470 0.7343 -0.0043 0.0082  0.2246  526 GLU B CG  
2475 C CD  . GLU A 340 ? 1.0678 1.6742 0.7434 -0.0036 0.0261  0.2401  526 GLU B CD  
2476 O OE1 . GLU A 340 ? 1.2478 1.8445 0.9234 -0.0050 0.0412  0.2222  526 GLU B OE1 
2477 O OE2 . GLU A 340 ? 1.0774 1.7003 0.7462 -0.0014 0.0253  0.2716  526 GLU B OE2 
2478 N N   . VAL A 341 ? 1.0876 1.6221 0.8413 -0.0052 -0.0001 0.1636  527 VAL B N   
2479 C CA  . VAL A 341 ? 0.9748 1.4861 0.7626 -0.0012 -0.0011 0.1685  527 VAL B CA  
2480 C C   . VAL A 341 ? 0.9160 1.4277 0.7143 -0.0018 -0.0156 0.1634  527 VAL B C   
2481 O O   . VAL A 341 ? 0.8947 1.3985 0.7156 0.0023  -0.0196 0.1764  527 VAL B O   
2482 C CB  . VAL A 341 ? 0.9030 1.3925 0.7056 -0.0015 0.0098  0.1521  527 VAL B CB  
2483 C CG1 . VAL A 341 ? 0.8976 1.3659 0.7297 0.0013  0.0067  0.1531  527 VAL B CG1 
2484 C CG2 . VAL A 341 ? 0.9410 1.4302 0.7421 -0.0003 0.0243  0.1613  527 VAL B CG2 
2485 N N   . LEU A 342 ? 0.9354 1.4563 0.7198 -0.0072 -0.0226 0.1437  528 LEU B N   
2486 C CA  . LEU A 342 ? 0.9464 1.4693 0.7429 -0.0091 -0.0359 0.1373  528 LEU B CA  
2487 C C   . LEU A 342 ? 1.0210 1.5722 0.8012 -0.0115 -0.0501 0.1456  528 LEU B C   
2488 O O   . LEU A 342 ? 1.0971 1.6577 0.8748 -0.0170 -0.0609 0.1303  528 LEU B O   
2489 C CB  . LEU A 342 ? 0.9454 1.4573 0.7457 -0.0142 -0.0351 0.1097  528 LEU B CB  
2490 C CG  . LEU A 342 ? 0.8792 1.3646 0.6994 -0.0120 -0.0245 0.1020  528 LEU B CG  
2491 C CD1 . LEU A 342 ? 0.8735 1.3499 0.7034 -0.0168 -0.0269 0.0797  528 LEU B CD1 
2492 C CD2 . LEU A 342 ? 0.8577 1.3304 0.7005 -0.0064 -0.0239 0.1186  528 LEU B CD2 
2493 N N   . GLN A 343 ? 1.0186 1.5848 0.7892 -0.0079 -0.0512 0.1703  529 GLN B N   
2494 C CA  . GLN A 343 ? 0.9703 1.5665 0.7264 -0.0096 -0.0666 0.1828  529 GLN B CA  
2495 C C   . GLN A 343 ? 0.9914 1.5909 0.7720 -0.0098 -0.0810 0.1822  529 GLN B C   
2496 O O   . GLN A 343 ? 1.0196 1.5989 0.8312 -0.0059 -0.0775 0.1829  529 GLN B O   
2497 C CB  . GLN A 343 ? 0.9833 1.5907 0.7380 -0.0035 -0.0654 0.2168  529 GLN B CB  
2498 C CG  . GLN A 343 ? 1.0457 1.6593 0.7728 -0.0041 -0.0529 0.2230  529 GLN B CG  
2499 C CD  . GLN A 343 ? 1.0901 1.7091 0.8259 0.0024  -0.0498 0.2595  529 GLN B CD  
2500 O OE1 . GLN A 343 ? 1.0157 1.6451 0.7677 0.0064  -0.0616 0.2814  529 GLN B OE1 
2501 N NE2 . GLN A 343 ? 1.0208 1.6330 0.7500 0.0036  -0.0335 0.2674  529 GLN B NE2 
2502 N N   . ALA A 344 ? 0.9780 1.6051 0.7444 -0.0149 -0.0974 0.1805  530 ALA B N   
2503 C CA  . ALA A 344 ? 0.9682 1.6044 0.7613 -0.0145 -0.1121 0.1863  530 ALA B CA  
2504 C C   . ALA A 344 ? 0.9613 1.5991 0.7783 -0.0047 -0.1127 0.2195  530 ALA B C   
2505 O O   . ALA A 344 ? 0.9788 1.6269 0.7825 -0.0009 -0.1109 0.2419  530 ALA B O   
2506 C CB  . ALA A 344 ? 1.0634 1.7326 0.8369 -0.0226 -0.1316 0.1789  530 ALA B CB  
2507 N N   . VAL A 345 ? 0.9371 1.5638 0.7917 -0.0005 -0.1137 0.2228  531 VAL B N   
2508 C CA  . VAL A 345 ? 0.9964 1.6217 0.8812 0.0094  -0.1130 0.2507  531 VAL B CA  
2509 C C   . VAL A 345 ? 1.0338 1.6803 0.9438 0.0099  -0.1294 0.2581  531 VAL B C   
2510 O O   . VAL A 345 ? 0.9485 1.5885 0.8781 0.0071  -0.1304 0.2417  531 VAL B O   
2511 C CB  . VAL A 345 ? 0.9028 1.4940 0.8124 0.0154  -0.0957 0.2476  531 VAL B CB  
2512 C CG1 . VAL A 345 ? 0.8833 1.4577 0.7963 0.0101  -0.0911 0.2193  531 VAL B CG1 
2513 C CG2 . VAL A 345 ? 1.0089 1.5984 0.9581 0.0248  -0.0960 0.2686  531 VAL B CG2 
2514 N N   . THR A 346 ? 1.0064 1.6798 0.9183 0.0134  -0.1422 0.2844  532 THR B N   
2515 C CA  . THR A 346 ? 0.9977 1.6962 0.9363 0.0143  -0.1598 0.2954  532 THR B CA  
2516 C C   . THR A 346 ? 1.0219 1.7118 1.0069 0.0267  -0.1543 0.3196  532 THR B C   
2517 O O   . THR A 346 ? 1.0640 1.7327 1.0564 0.0341  -0.1397 0.3314  532 THR B O   
2518 C CB  . THR A 346 ? 0.9886 1.7268 0.9012 0.0101  -0.1803 0.3099  532 THR B CB  
2519 O OG1 . THR A 346 ? 1.0506 1.7942 0.9561 0.0175  -0.1774 0.3412  532 THR B OG1 
2520 C CG2 . THR A 346 ? 1.0067 1.7536 0.8722 -0.0024 -0.1845 0.2823  532 THR B CG2 
2521 N N   . ASP A 347 ? 0.9705 1.6775 0.9902 0.0287  -0.1658 0.3259  533 ASP B N   
2522 C CA  . ASP A 347 ? 0.9239 1.6244 0.9929 0.0410  -0.1601 0.3465  533 ASP B CA  
2523 C C   . ASP A 347 ? 0.9445 1.6573 1.0214 0.0498  -0.1646 0.3825  533 ASP B C   
2524 O O   . ASP A 347 ? 0.9369 1.6341 1.0515 0.0609  -0.1538 0.3986  533 ASP B O   
2525 C CB  . ASP A 347 ? 0.9166 1.6368 1.0225 0.0408  -0.1717 0.3454  533 ASP B CB  
2526 C CG  . ASP A 347 ? 1.0034 1.7052 1.1162 0.0351  -0.1617 0.3152  533 ASP B CG  
2527 O OD1 . ASP A 347 ? 0.9810 1.6544 1.0702 0.0321  -0.1465 0.2961  533 ASP B OD1 
2528 O OD2 . ASP A 347 ? 1.1274 1.8442 1.2710 0.0337  -0.1690 0.3123  533 ASP B OD2 
2529 N N   . HIS A 348 ? 1.0235 1.7645 1.0667 0.0450  -0.1800 0.3956  534 HIS B N   
2530 C CA  . HIS A 348 ? 1.0476 1.8028 1.0932 0.0524  -0.1846 0.4330  534 HIS B CA  
2531 C C   . HIS A 348 ? 1.0536 1.7830 1.0791 0.0546  -0.1659 0.4378  534 HIS B C   
2532 O O   . HIS A 348 ? 1.0817 1.8149 1.1196 0.0622  -0.1648 0.4708  534 HIS B O   
2533 C CB  . HIS A 348 ? 1.0978 1.8976 1.1122 0.0457  -0.2095 0.4457  534 HIS B CB  
2534 C CG  . HIS A 348 ? 1.1538 1.9829 1.1968 0.0444  -0.2303 0.4474  534 HIS B CG  
2535 N ND1 . HIS A 348 ? 1.1771 2.0263 1.2657 0.0546  -0.2415 0.4813  534 HIS B ND1 
2536 C CD2 . HIS A 348 ? 1.1372 1.9780 1.1758 0.0343  -0.2412 0.4197  534 HIS B CD2 
2537 C CE1 . HIS A 348 ? 1.3237 2.1980 1.4336 0.0507  -0.2590 0.4746  534 HIS B CE1 
2538 N NE2 . HIS A 348 ? 1.3049 2.1744 1.3851 0.0380  -0.2592 0.4372  534 HIS B NE2 
2539 N N   . ASP A 349 ? 1.0129 1.7170 1.0112 0.0480  -0.1515 0.4075  535 ASP B N   
2540 C CA  . ASP A 349 ? 1.0289 1.7071 1.0160 0.0500  -0.1328 0.4105  535 ASP B CA  
2541 C C   . ASP A 349 ? 0.9729 1.6236 1.0089 0.0611  -0.1187 0.4234  535 ASP B C   
2542 O O   . ASP A 349 ? 1.0207 1.6548 1.0588 0.0645  -0.1061 0.4364  535 ASP B O   
2543 C CB  . ASP A 349 ? 0.9929 1.6500 0.9488 0.0414  -0.1211 0.3743  535 ASP B CB  
2544 C CG  . ASP A 349 ? 1.0587 1.7387 0.9630 0.0309  -0.1300 0.3621  535 ASP B CG  
2545 O OD1 . ASP A 349 ? 1.0715 1.7740 0.9516 0.0306  -0.1357 0.3842  535 ASP B OD1 
2546 O OD2 . ASP A 349 ? 0.9898 1.6655 0.8781 0.0230  -0.1308 0.3306  535 ASP B OD2 
2547 N N   . ILE A 350 ? 0.9523 1.5981 1.0289 0.0665  -0.1197 0.4188  536 ILE B N   
2548 C CA  . ILE A 350 ? 0.9757 1.5963 1.1010 0.0772  -0.1058 0.4271  536 ILE B CA  
2549 C C   . ILE A 350 ? 1.0731 1.7125 1.2331 0.0871  -0.1149 0.4671  536 ILE B C   
2550 O O   . ILE A 350 ? 0.9695 1.6399 1.1397 0.0881  -0.1326 0.4793  536 ILE B O   
2551 C CB  . ILE A 350 ? 0.9224 1.5305 1.0748 0.0787  -0.1004 0.4032  536 ILE B CB  
2552 C CG1 . ILE A 350 ? 0.9000 1.4984 1.0155 0.0677  -0.0968 0.3680  536 ILE B CG1 
2553 C CG2 . ILE A 350 ? 0.9059 1.4829 1.0996 0.0881  -0.0822 0.4032  536 ILE B CG2 
2554 C CD1 . ILE A 350 ? 0.8777 1.4641 1.0150 0.0681  -0.0900 0.3454  536 ILE B CD1 
2555 N N   . PRO A 351 ? 1.0743 1.6970 1.2563 0.0943  -0.1040 0.4888  537 PRO B N   
2556 C CA  . PRO A 351 ? 1.1080 1.7477 1.3278 0.1046  -0.1122 0.5304  537 PRO B CA  
2557 C C   . PRO A 351 ? 1.0378 1.6811 1.3130 0.1142  -0.1153 0.5336  537 PRO B C   
2558 O O   . PRO A 351 ? 0.9938 1.6142 1.2895 0.1158  -0.1028 0.5064  537 PRO B O   
2559 C CB  . PRO A 351 ? 0.9993 1.6099 1.2379 0.1096  -0.0948 0.5448  537 PRO B CB  
2560 C CG  . PRO A 351 ? 0.9898 1.5822 1.1819 0.0991  -0.0838 0.5175  537 PRO B CG  
2561 C CD  . PRO A 351 ? 0.9804 1.5702 1.1528 0.0924  -0.0851 0.4784  537 PRO B CD  
2562 N N   . GLN A 352 ? 1.0024 1.6771 1.3020 0.1206  -0.1322 0.5682  538 GLN B N   
2563 C CA  . GLN A 352 ? 1.1138 1.7985 1.4686 0.1299  -0.1371 0.5738  538 GLN B CA  
2564 C C   . GLN A 352 ? 1.0834 1.7333 1.4973 0.1421  -0.1159 0.5733  538 GLN B C   
2565 O O   . GLN A 352 ? 1.0535 1.6957 1.5021 0.1468  -0.1087 0.5551  538 GLN B O   
2566 C CB  . GLN A 352 ? 1.1842 1.9114 1.5556 0.1348  -0.1608 0.6150  538 GLN B CB  
2567 C CG  . GLN A 352 ? 1.2154 1.9827 1.5393 0.1231  -0.1848 0.6098  538 GLN B CG  
2568 C CD  . GLN A 352 ? 1.3773 2.1895 1.7169 0.1277  -0.2103 0.6521  538 GLN B CD  
2569 O OE1 . GLN A 352 ? 1.2493 2.0629 1.6225 0.1385  -0.2099 0.6909  538 GLN B OE1 
2570 N NE2 . GLN A 352 ? 1.4969 2.3466 1.8141 0.1192  -0.2333 0.6455  538 GLN B NE2 
2571 N N   . GLN A 353 ? 1.0095 1.6380 1.4369 0.1470  -0.1047 0.5920  539 GLN B N   
2572 C CA  . GLN A 353 ? 1.0693 1.6622 1.5534 0.1576  -0.0839 0.5871  539 GLN B CA  
2573 C C   . GLN A 353 ? 1.0448 1.6045 1.5134 0.1520  -0.0651 0.5402  539 GLN B C   
2574 O O   . GLN A 353 ? 1.0922 1.6313 1.6041 0.1597  -0.0506 0.5248  539 GLN B O   
2575 C CB  . GLN A 353 ? 1.2516 1.8281 1.7576 0.1631  -0.0762 0.6175  539 GLN B CB  
2576 C CG  . GLN A 353 ? 1.4106 2.0168 1.9510 0.1726  -0.0921 0.6689  539 GLN B CG  
2577 C CD  . GLN A 353 ? 1.5418 2.1302 2.1096 0.1782  -0.0830 0.7017  539 GLN B CD  
2578 O OE1 . GLN A 353 ? 1.5664 2.1287 2.1104 0.1715  -0.0694 0.6893  539 GLN B OE1 
2579 N NE2 . GLN A 353 ? 1.4109 2.0136 2.0333 0.1907  -0.0906 0.7452  539 GLN B NE2 
2580 N N   . LEU A 354 ? 1.0089 1.5639 1.4173 0.1391  -0.0647 0.5175  540 LEU B N   
2581 C CA  . LEU A 354 ? 0.9367 1.4657 1.3281 0.1333  -0.0502 0.4748  540 LEU B CA  
2582 C C   . LEU A 354 ? 0.9210 1.4639 1.3213 0.1337  -0.0539 0.4564  540 LEU B C   
2583 O O   . LEU A 354 ? 0.9083 1.4309 1.3288 0.1366  -0.0388 0.4315  540 LEU B O   
2584 C CB  . LEU A 354 ? 0.9383 1.4632 1.2668 0.1200  -0.0509 0.4572  540 LEU B CB  
2585 C CG  . LEU A 354 ? 0.9091 1.4074 1.2187 0.1137  -0.0368 0.4163  540 LEU B CG  
2586 C CD1 . LEU A 354 ? 0.9099 1.3730 1.2549 0.1197  -0.0178 0.4075  540 LEU B CD1 
2587 C CD2 . LEU A 354 ? 0.9046 1.4026 1.1568 0.1015  -0.0391 0.4026  540 LEU B CD2 
2588 N N   . VAL A 355 ? 0.9836 1.5625 1.3688 0.1302  -0.0738 0.4678  541 VAL B N   
2589 C CA  . VAL A 355 ? 0.9717 1.5672 1.3695 0.1296  -0.0786 0.4532  541 VAL B CA  
2590 C C   . VAL A 355 ? 0.9226 1.5161 1.3886 0.1438  -0.0705 0.4633  541 VAL B C   
2591 O O   . VAL A 355 ? 0.8978 1.4852 1.3832 0.1456  -0.0598 0.4411  541 VAL B O   
2592 C CB  . VAL A 355 ? 0.9174 1.5538 1.2896 0.1224  -0.1037 0.4654  541 VAL B CB  
2593 C CG1 . VAL A 355 ? 0.9726 1.6277 1.3665 0.1217  -0.1093 0.4531  541 VAL B CG1 
2594 C CG2 . VAL A 355 ? 0.9513 1.5873 1.2570 0.1084  -0.1086 0.4493  541 VAL B CG2 
2595 N N   . GLU A 356 ? 0.9310 1.5300 1.4363 0.1544  -0.0743 0.4977  542 GLU B N   
2596 C CA  . GLU A 356 ? 0.9353 1.5335 1.5117 0.1692  -0.0667 0.5094  542 GLU B CA  
2597 C C   . GLU A 356 ? 0.9277 1.4858 1.5283 0.1744  -0.0392 0.4814  542 GLU B C   
2598 O O   . GLU A 356 ? 0.9218 1.4785 1.5628 0.1818  -0.0282 0.4691  542 GLU B O   
2599 C CB  . GLU A 356 ? 1.0236 1.6337 1.6384 0.1796  -0.0762 0.5545  542 GLU B CB  
2600 C CG  . GLU A 356 ? 1.0269 1.6838 1.6324 0.1776  -0.1049 0.5861  542 GLU B CG  
2601 C CD  . GLU A 356 ? 1.2135 1.8817 1.8479 0.1867  -0.1145 0.6338  542 GLU B CD  
2602 O OE1 . GLU A 356 ? 1.3334 1.9709 1.9824 0.1914  -0.0992 0.6411  542 GLU B OE1 
2603 O OE2 . GLU A 356 ? 1.3016 2.0101 1.9456 0.1888  -0.1377 0.6648  542 GLU B OE2 
2604 N N   . ARG A 357 ? 0.9299 1.4566 1.5071 0.1703  -0.0275 0.4705  543 ARG B N   
2605 C CA  . ARG A 357 ? 0.9275 1.4171 1.5279 0.1747  -0.0029 0.4434  543 ARG B CA  
2606 C C   . ARG A 357 ? 0.9081 1.3918 1.4810 0.1678  0.0070  0.4036  543 ARG B C   
2607 O O   . ARG A 357 ? 0.9075 1.3770 1.5125 0.1745  0.0246  0.3839  543 ARG B O   
2608 C CB  . ARG A 357 ? 0.9356 1.3953 1.5189 0.1706  0.0052  0.4416  543 ARG B CB  
2609 C CG  . ARG A 357 ? 1.0080 1.4296 1.6178 0.1745  0.0291  0.4130  543 ARG B CG  
2610 C CD  . ARG A 357 ? 1.0314 1.4240 1.6322 0.1701  0.0363  0.4118  543 ARG B CD  
2611 N NE  . ARG A 357 ? 1.0133 1.3713 1.6383 0.1726  0.0575  0.3804  543 ARG B NE  
2612 C CZ  . ARG A 357 ? 1.0457 1.3743 1.6695 0.1682  0.0667  0.3701  543 ARG B CZ  
2613 N NH1 . ARG A 357 ? 1.0657 1.3943 1.6679 0.1616  0.0585  0.3902  543 ARG B NH1 
2614 N NH2 . ARG A 357 ? 1.0204 1.3202 1.6654 0.1699  0.0849  0.3380  543 ARG B NH2 
2615 N N   . LEU A 358 ? 0.8947 1.3889 1.4087 0.1546  -0.0032 0.3913  544 LEU B N   
2616 C CA  . LEU A 358 ? 0.8779 1.3665 1.3652 0.1475  0.0057  0.3568  544 LEU B CA  
2617 C C   . LEU A 358 ? 0.8721 1.3831 1.3908 0.1525  0.0057  0.3554  544 LEU B C   
2618 O O   . LEU A 358 ? 0.8930 1.3932 1.4218 0.1543  0.0227  0.3311  544 LEU B O   
2619 C CB  . LEU A 358 ? 0.8668 1.3616 1.2901 0.1329  -0.0057 0.3468  544 LEU B CB  
2620 C CG  . LEU A 358 ? 0.8653 1.3318 1.2515 0.1256  0.0026  0.3300  544 LEU B CG  
2621 C CD1 . LEU A 358 ? 0.8798 1.3397 1.2690 0.1274  -0.0016 0.3538  544 LEU B CD1 
2622 C CD2 . LEU A 358 ? 0.8516 1.3251 1.1832 0.1126  -0.0050 0.3135  544 LEU B CD2 
2623 N N   . GLN A 359 ? 0.8756 1.4197 1.4108 0.1545  -0.0132 0.3817  545 GLN B N   
2624 C CA  . GLN A 359 ? 0.8701 1.4381 1.4427 0.1594  -0.0140 0.3828  545 GLN B CA  
2625 C C   . GLN A 359 ? 0.8794 1.4360 1.5167 0.1749  0.0047  0.3845  545 GLN B C   
2626 O O   . GLN A 359 ? 0.8740 1.4363 1.5373 0.1786  0.0169  0.3702  545 GLN B O   
2627 C CB  . GLN A 359 ? 0.8742 1.4819 1.4532 0.1579  -0.0406 0.4116  545 GLN B CB  
2628 C CG  . GLN A 359 ? 0.9064 1.5282 1.4239 0.1420  -0.0581 0.4044  545 GLN B CG  
2629 C CD  . GLN A 359 ? 1.0429 1.7056 1.5647 0.1396  -0.0855 0.4305  545 GLN B CD  
2630 O OE1 . GLN A 359 ? 1.2764 1.9556 1.8390 0.1498  -0.0944 0.4609  545 GLN B OE1 
2631 N NE2 . GLN A 359 ? 0.8952 1.5753 1.3765 0.1260  -0.0998 0.4186  545 GLN B NE2 
2632 N N   . GLU A 360 ? 0.8952 1.4355 1.5614 0.1841  0.0086  0.4017  546 GLU B N   
2633 C CA  . GLU A 360 ? 0.9069 1.4314 1.6367 0.1990  0.0287  0.3997  546 GLU B CA  
2634 C C   . GLU A 360 ? 0.9035 1.3982 1.6204 0.1972  0.0545  0.3588  546 GLU B C   
2635 O O   . GLU A 360 ? 0.9073 1.4004 1.6642 0.2059  0.0723  0.3452  546 GLU B O   
2636 C CB  . GLU A 360 ? 0.9262 1.4356 1.6885 0.2078  0.0278  0.4258  546 GLU B CB  
2637 C CG  . GLU A 360 ? 0.9415 1.4275 1.7711 0.2230  0.0509  0.4199  546 GLU B CG  
2638 C CD  . GLU A 360 ? 0.9829 1.4937 1.8775 0.2362  0.0524  0.4332  546 GLU B CD  
2639 O OE1 . GLU A 360 ? 0.9426 1.4895 1.8476 0.2371  0.0301  0.4641  546 GLU B OE1 
2640 O OE2 . GLU A 360 ? 0.9706 1.4659 1.9069 0.2456  0.0762  0.4122  546 GLU B OE2 
2641 N N   . GLU A 361 ? 0.8987 1.3711 1.5601 0.1859  0.0571  0.3388  547 GLU B N   
2642 C CA  . GLU A 361 ? 0.8978 1.3452 1.5403 0.1827  0.0789  0.3003  547 GLU B CA  
2643 C C   . GLU A 361 ? 0.8854 1.3511 1.5152 0.1789  0.0839  0.2829  547 GLU B C   
2644 O O   . GLU A 361 ? 0.8917 1.3489 1.5404 0.1840  0.1053  0.2605  547 GLU B O   
2645 C CB  . GLU A 361 ? 0.8938 1.3194 1.4784 0.1703  0.0766  0.2855  547 GLU B CB  
2646 C CG  . GLU A 361 ? 0.9089 1.3091 1.5095 0.1736  0.0791  0.2945  547 GLU B CG  
2647 C CD  . GLU A 361 ? 0.9058 1.2829 1.4554 0.1617  0.0814  0.2733  547 GLU B CD  
2648 O OE1 . GLU A 361 ? 0.8915 1.2741 1.3922 0.1514  0.0789  0.2549  547 GLU B OE1 
2649 O OE2 . GLU A 361 ? 0.9423 1.2960 1.5045 0.1627  0.0857  0.2756  547 GLU B OE2 
2650 N N   . LYS A 362 ? 0.8701 1.3617 1.4694 0.1696  0.0651  0.2928  548 LYS B N   
2651 C CA  . LYS A 362 ? 0.8588 1.3687 1.4501 0.1650  0.0691  0.2792  548 LYS B CA  
2652 C C   . LYS A 362 ? 0.9007 1.4300 1.5561 0.1774  0.0775  0.2880  548 LYS B C   
2653 O O   . LYS A 362 ? 0.9726 1.5073 1.6348 0.1776  0.0933  0.2703  548 LYS B O   
2654 C CB  . LYS A 362 ? 0.8440 1.3766 1.3953 0.1522  0.0461  0.2882  548 LYS B CB  
2655 C CG  . LYS A 362 ? 0.9130 1.4275 1.3999 0.1392  0.0425  0.2725  548 LYS B CG  
2656 C CD  . LYS A 362 ? 0.8429 1.3782 1.2937 0.1264  0.0248  0.2738  548 LYS B CD  
2657 C CE  . LYS A 362 ? 0.8487 1.4079 1.3046 0.1256  0.0003  0.3011  548 LYS B CE  
2658 N NZ  . LYS A 362 ? 0.8279 1.4066 1.2493 0.1125  -0.0170 0.2987  548 LYS B NZ  
2659 N N   . ARG A 363 ? 0.8726 1.4137 1.5770 0.1880  0.0678  0.3167  549 ARG B N   
2660 C CA  . ARG A 363 ? 0.8796 1.4374 1.6534 0.2017  0.0775  0.3258  549 ARG B CA  
2661 C C   . ARG A 363 ? 0.8937 1.4248 1.6953 0.2116  0.1090  0.3005  549 ARG B C   
2662 O O   . ARG A 363 ? 0.9823 1.5237 1.8158 0.2176  0.1264  0.2891  549 ARG B O   
2663 C CB  . ARG A 363 ? 0.8888 1.4631 1.7114 0.2119  0.0601  0.3640  549 ARG B CB  
2664 C CG  . ARG A 363 ? 0.8804 1.4891 1.6845 0.2037  0.0283  0.3902  549 ARG B CG  
2665 C CD  . ARG A 363 ? 0.8934 1.5240 1.7554 0.2160  0.0129  0.4296  549 ARG B CD  
2666 N NE  . ARG A 363 ? 0.8923 1.5514 1.7254 0.2072  -0.0192 0.4552  549 ARG B NE  
2667 C CZ  . ARG A 363 ? 0.9021 1.5546 1.7077 0.2047  -0.0328 0.4739  549 ARG B CZ  
2668 N NH1 . ARG A 363 ? 0.9123 1.5304 1.7209 0.2102  -0.0183 0.4724  549 ARG B NH1 
2669 N NH2 . ARG A 363 ? 1.0562 1.7382 1.8308 0.1958  -0.0610 0.4938  549 ARG B NH2 
2670 N N   . ILE A 364 ? 0.9056 1.4029 1.6966 0.2131  0.1174  0.2906  550 ILE B N   
2671 C CA  . ILE A 364 ? 0.9238 1.3941 1.7413 0.2219  0.1467  0.2639  550 ILE B CA  
2672 C C   . ILE A 364 ? 0.9678 1.4336 1.7438 0.2140  0.1647  0.2279  550 ILE B C   
2673 O O   . ILE A 364 ? 1.0456 1.5082 1.8507 0.2221  0.1896  0.2078  550 ILE B O   
2674 C CB  . ILE A 364 ? 1.0150 1.4503 1.8288 0.2229  0.1491  0.2607  550 ILE B CB  
2675 C CG1 . ILE A 364 ? 0.9691 1.4111 1.8258 0.2310  0.1317  0.3010  550 ILE B CG1 
2676 C CG2 . ILE A 364 ? 0.9606 1.3673 1.8034 0.2313  0.1789  0.2296  550 ILE B CG2 
2677 C CD1 . ILE A 364 ? 0.9565 1.3664 1.8111 0.2306  0.1320  0.3036  550 ILE B CD1 
2678 N N   . GLU A 365 ? 0.9060 1.3724 1.6144 0.1985  0.1533  0.2200  551 GLU B N   
2679 C CA  . GLU A 365 ? 0.9145 1.3790 1.5825 0.1906  0.1688  0.1902  551 GLU B CA  
2680 C C   . GLU A 365 ? 1.0433 1.5389 1.7338 0.1924  0.1747  0.1938  551 GLU B C   
2681 O O   . GLU A 365 ? 1.0062 1.5013 1.6939 0.1935  0.1978  0.1708  551 GLU B O   
2682 C CB  . GLU A 365 ? 0.8909 1.3489 1.4869 0.1743  0.1544  0.1838  551 GLU B CB  
2683 C CG  . GLU A 365 ? 1.0577 1.4838 1.6272 0.1709  0.1539  0.1727  551 GLU B CG  
2684 C CD  . GLU A 365 ? 1.2266 1.6486 1.7301 0.1556  0.1395  0.1680  551 GLU B CD  
2685 O OE1 . GLU A 365 ? 1.2480 1.6912 1.7291 0.1481  0.1273  0.1769  551 GLU B OE1 
2686 O OE2 . GLU A 365 ? 1.3170 1.7144 1.7943 0.1511  0.1407  0.1550  551 GLU B OE2 
2687 N N   . ALA A 366 ? 1.0241 1.5484 1.7378 0.1925  0.1544  0.2224  552 ALA B N   
2688 C CA  . ALA A 366 ? 0.9253 1.4811 1.6626 0.1925  0.1577  0.2269  552 ALA B CA  
2689 C C   . ALA A 366 ? 0.8918 1.4541 1.6955 0.2082  0.1821  0.2229  552 ALA B C   
2690 O O   . ALA A 366 ? 0.8885 1.4755 1.7143 0.2088  0.1913  0.2224  552 ALA B O   
2691 C CB  . ALA A 366 ? 0.8604 1.4464 1.6093 0.1882  0.1277  0.2575  552 ALA B CB  
2692 N N   . GLN A 367 ? 0.9095 1.4508 1.7489 0.2208  0.1934  0.2203  553 GLN B N   
2693 C CA  . GLN A 367 ? 0.9403 1.4853 1.8486 0.2374  0.2180  0.2154  553 GLN B CA  
2694 C C   . GLN A 367 ? 0.9495 1.4679 1.8416 0.2398  0.2507  0.1763  553 GLN B C   
2695 O O   . GLN A 367 ? 0.9644 1.4509 1.8476 0.2419  0.2565  0.1623  553 GLN B O   
2696 C CB  . GLN A 367 ? 1.0412 1.5815 2.0104 0.2512  0.2091  0.2403  553 GLN B CB  
2697 C CG  . GLN A 367 ? 0.9400 1.5076 1.9197 0.2484  0.1745  0.2800  553 GLN B CG  
2698 C CD  . GLN A 367 ? 0.9451 1.5021 1.9638 0.2587  0.1623  0.3061  553 GLN B CD  
2699 O OE1 . GLN A 367 ? 1.0221 1.5576 2.0872 0.2721  0.1816  0.2994  553 GLN B OE1 
2700 N NE2 . GLN A 367 ? 0.9185 1.4903 1.9180 0.2521  0.1308  0.3358  553 GLN B NE2 
2701 N N   . LYS B 23  ? 0.8060 1.0289 0.9689 0.0711  0.0125  0.2257  209 LYS A N   
2702 C CA  . LYS B 23  ? 1.1513 1.4000 1.3383 0.0748  -0.0004 0.2368  209 LYS A CA  
2703 C C   . LYS B 23  ? 1.3318 1.5570 1.5188 0.0946  -0.0077 0.2403  209 LYS A C   
2704 O O   . LYS B 23  ? 1.4387 1.6256 1.6035 0.1038  -0.0050 0.2332  209 LYS A O   
2705 C CB  . LYS B 23  ? 1.1934 1.4821 1.4087 0.0733  0.0049  0.2427  209 LYS A CB  
2706 C CG  . LYS B 23  ? 1.1561 1.4390 1.3764 0.0895  0.0186  0.2413  209 LYS A CG  
2707 C CD  . LYS B 23  ? 1.0637 1.3890 1.3165 0.0888  0.0223  0.2504  209 LYS A CD  
2708 C CE  . LYS B 23  ? 1.0772 1.3973 1.3351 0.1073  0.0369  0.2503  209 LYS A CE  
2709 N NZ  . LYS B 23  ? 0.9520 1.2445 1.2032 0.1293  0.0326  0.2499  209 LYS A NZ  
2710 N N   . HIS B 24  ? 1.5010 1.7496 1.7139 0.1006  -0.0178 0.2513  210 HIS A N   
2711 C CA  . HIS B 24  ? 1.4966 1.7294 1.7175 0.1182  -0.0280 0.2569  210 HIS A CA  
2712 C C   . HIS B 24  ? 1.6971 1.9079 1.9066 0.1159  -0.0427 0.2598  210 HIS A C   
2713 O O   . HIS B 24  ? 1.6332 1.8374 1.8553 0.1265  -0.0554 0.2679  210 HIS A O   
2714 C CB  . HIS B 24  ? 1.5291 1.7300 1.7373 0.1371  -0.0182 0.2483  210 HIS A CB  
2715 C CG  . HIS B 24  ? 1.7078 1.8632 1.8940 0.1466  -0.0263 0.2432  210 HIS A CG  
2716 N ND1 . HIS B 24  ? 1.7528 1.8948 1.9499 0.1601  -0.0404 0.2490  210 HIS A ND1 
2717 C CD2 . HIS B 24  ? 1.6987 1.8195 1.8544 0.1439  -0.0233 0.2337  210 HIS A CD2 
2718 C CE1 . HIS B 24  ? 1.7393 1.8396 1.9133 0.1650  -0.0465 0.2430  210 HIS A CE1 
2719 N NE2 . HIS B 24  ? 1.6650 1.7522 1.8133 0.1554  -0.0361 0.2339  210 HIS A NE2 
2720 N N   . THR B 25  ? 1.3992 1.6004 1.5877 0.1017  -0.0411 0.2546  211 THR A N   
2721 C CA  . THR B 25  ? 1.2112 1.3958 1.3899 0.0978  -0.0538 0.2591  211 THR A CA  
2722 C C   . THR B 25  ? 1.0118 1.2156 1.1836 0.0785  -0.0540 0.2597  211 THR A C   
2723 O O   . THR B 25  ? 0.9487 1.1433 1.1129 0.0745  -0.0633 0.2648  211 THR A O   
2724 C CB  . THR B 25  ? 1.1411 1.2769 1.2932 0.1056  -0.0523 0.2506  211 THR A CB  
2725 O OG1 . THR B 25  ? 1.0598 1.1811 1.2040 0.1005  -0.0640 0.2565  211 THR A OG1 
2726 C CG2 . THR B 25  ? 1.0866 1.2105 1.2161 0.0989  -0.0355 0.2375  211 THR A CG2 
2727 N N   . GLY B 26  ? 0.9746 1.2047 1.1493 0.0668  -0.0444 0.2549  212 GLY A N   
2728 C CA  . GLY B 26  ? 0.9192 1.1629 1.0837 0.0489  -0.0438 0.2521  212 GLY A CA  
2729 C C   . GLY B 26  ? 0.9465 1.1588 1.0825 0.0424  -0.0341 0.2403  212 GLY A C   
2730 O O   . GLY B 26  ? 1.0551 1.2761 1.1814 0.0275  -0.0318 0.2359  212 GLY A O   
2731 N N   . TYR B 27  ? 0.9067 1.0827 1.0288 0.0533  -0.0287 0.2348  213 TYR A N   
2732 C CA  . TYR B 27  ? 0.8775 1.0222 0.9731 0.0482  -0.0199 0.2251  213 TYR A CA  
2733 C C   . TYR B 27  ? 0.7952 0.9246 0.8842 0.0556  -0.0057 0.2164  213 TYR A C   
2734 O O   . TYR B 27  ? 0.7853 0.9051 0.8793 0.0714  -0.0062 0.2176  213 TYR A O   
2735 C CB  . TYR B 27  ? 0.9335 1.0448 1.0146 0.0540  -0.0292 0.2289  213 TYR A CB  
2736 C CG  . TYR B 27  ? 0.8044 0.9308 0.8948 0.0505  -0.0438 0.2409  213 TYR A CG  
2737 C CD1 . TYR B 27  ? 0.7717 0.9229 0.8614 0.0359  -0.0439 0.2418  213 TYR A CD1 
2738 C CD2 . TYR B 27  ? 0.7866 0.9027 0.8867 0.0624  -0.0576 0.2516  213 TYR A CD2 
2739 C CE1 . TYR B 27  ? 0.7274 0.8944 0.8244 0.0339  -0.0563 0.2537  213 TYR A CE1 
2740 C CE2 . TYR B 27  ? 0.7363 0.8685 0.8471 0.0598  -0.0705 0.2648  213 TYR A CE2 
2741 C CZ  . TYR B 27  ? 0.7199 0.8784 0.8283 0.0459  -0.0692 0.2662  213 TYR A CZ  
2742 O OH  . TYR B 27  ? 0.7113 0.8879 0.8291 0.0445  -0.0812 0.2802  213 TYR A OH  
2743 N N   . VAL B 28  ? 0.7843 0.9117 0.8623 0.0447  0.0070  0.2079  214 VAL A N   
2744 C CA  . VAL B 28  ? 0.7979 0.9138 0.8697 0.0506  0.0219  0.2009  214 VAL A CA  
2745 C C   . VAL B 28  ? 0.8011 0.8762 0.8455 0.0530  0.0262  0.1951  214 VAL A C   
2746 O O   . VAL B 28  ? 0.8551 0.9152 0.8869 0.0456  0.0204  0.1954  214 VAL A O   
2747 C CB  . VAL B 28  ? 0.8786 1.0212 0.9607 0.0371  0.0335  0.1972  214 VAL A CB  
2748 C CG1 . VAL B 28  ? 0.8366 0.9661 0.9018 0.0217  0.0389  0.1902  214 VAL A CG1 
2749 C CG2 . VAL B 28  ? 0.8172 0.9623 0.9053 0.0474  0.0472  0.1955  214 VAL A CG2 
2750 N N   . GLY B 29  ? 0.8672 0.9249 0.9022 0.0641  0.0369  0.1903  215 GLY A N   
2751 C CA  . GLY B 29  ? 0.8674 0.8864 0.8764 0.0687  0.0405  0.1853  215 GLY A CA  
2752 C C   . GLY B 29  ? 0.8713 0.8857 0.8694 0.0577  0.0558  0.1793  215 GLY A C   
2753 O O   . GLY B 29  ? 0.7986 0.8388 0.8098 0.0460  0.0638  0.1783  215 GLY A O   
2754 N N   . LEU B 30  ? 0.8754 0.8555 0.8500 0.0617  0.0589  0.1758  216 LEU A N   
2755 C CA  . LEU B 30  ? 0.8527 0.8228 0.8151 0.0537  0.0733  0.1711  216 LEU A CA  
2756 C C   . LEU B 30  ? 0.9497 0.9046 0.8998 0.0691  0.0839  0.1681  216 LEU A C   
2757 O O   . LEU B 30  ? 0.9951 0.9284 0.9332 0.0849  0.0770  0.1676  216 LEU A O   
2758 C CB  . LEU B 30  ? 0.8156 0.7591 0.7602 0.0451  0.0691  0.1707  216 LEU A CB  
2759 C CG  . LEU B 30  ? 0.8167 0.7733 0.7688 0.0290  0.0624  0.1727  216 LEU A CG  
2760 C CD1 . LEU B 30  ? 0.8998 0.8268 0.8340 0.0258  0.0566  0.1746  216 LEU A CD1 
2761 C CD2 . LEU B 30  ? 0.8064 0.7841 0.7681 0.0138  0.0744  0.1685  216 LEU A CD2 
2762 N N   . LYS B 31  ? 0.9566 0.9231 0.9102 0.0649  0.1003  0.1664  217 LYS A N   
2763 C CA  . LYS B 31  ? 0.9922 0.9494 0.9349 0.0803  0.1123  0.1647  217 LYS A CA  
2764 C C   . LYS B 31  ? 0.9824 0.9018 0.8957 0.0847  0.1135  0.1616  217 LYS A C   
2765 O O   . LYS B 31  ? 0.9772 0.8840 0.8830 0.0713  0.1129  0.1614  217 LYS A O   
2766 C CB  . LYS B 31  ? 0.9138 0.8984 0.8729 0.0741  0.1298  0.1664  217 LYS A CB  
2767 C CG  . LYS B 31  ? 1.0811 1.0839 1.0504 0.0908  0.1386  0.1689  217 LYS A CG  
2768 C CD  . LYS B 31  ? 1.1889 1.1626 1.1318 0.1122  0.1402  0.1656  217 LYS A CD  
2769 C CE  . LYS B 31  ? 1.1882 1.1774 1.1385 0.1314  0.1491  0.1675  217 LYS A CE  
2770 N NZ  . LYS B 31  ? 1.1865 1.1439 1.1076 0.1533  0.1479  0.1621  217 LYS A NZ  
2771 N N   . ASN B 32  ? 1.0521 0.9533 0.9485 0.1041  0.1149  0.1592  218 ASN A N   
2772 C CA  . ASN B 32  ? 1.0530 0.9206 0.9205 0.1103  0.1175  0.1562  218 ASN A CA  
2773 C C   . ASN B 32  ? 1.0770 0.9545 0.9433 0.1063  0.1379  0.1572  218 ASN A C   
2774 O O   . ASN B 32  ? 1.1039 0.9978 0.9751 0.1173  0.1505  0.1580  218 ASN A O   
2775 C CB  . ASN B 32  ? 1.1426 0.9881 0.9917 0.1331  0.1109  0.1521  218 ASN A CB  
2776 C CG  . ASN B 32  ? 1.2493 1.0567 1.0665 0.1390  0.1084  0.1487  218 ASN A CG  
2777 O OD1 . ASN B 32  ? 1.2577 1.0593 1.0662 0.1291  0.1177  0.1501  218 ASN A OD1 
2778 N ND2 . ASN B 32  ? 1.2844 1.0653 1.0849 0.1549  0.0951  0.1444  218 ASN A ND2 
2779 N N   . GLN B 33  ? 1.1199 0.9884 0.9815 0.0909  0.1417  0.1584  219 GLN A N   
2780 C CA  . GLN B 33  ? 1.1413 1.0198 1.0060 0.0842  0.1603  0.1608  219 GLN A CA  
2781 C C   . GLN B 33  ? 1.0980 0.9451 0.9363 0.0849  0.1630  0.1605  219 GLN A C   
2782 O O   . GLN B 33  ? 1.1777 1.0214 1.0183 0.0697  0.1684  0.1627  219 GLN A O   
2783 C CB  . GLN B 33  ? 1.1247 1.0277 1.0153 0.0626  0.1640  0.1629  219 GLN A CB  
2784 C CG  . GLN B 33  ? 1.1216 1.0599 1.0400 0.0609  0.1636  0.1643  219 GLN A CG  
2785 C CD  . GLN B 33  ? 1.0560 1.0168 0.9982 0.0392  0.1666  0.1653  219 GLN A CD  
2786 O OE1 . GLN B 33  ? 1.1034 1.0514 1.0408 0.0252  0.1644  0.1636  219 GLN A OE1 
2787 N NE2 . GLN B 33  ? 1.0401 1.0342 1.0083 0.0366  0.1714  0.1681  219 GLN A NE2 
2788 N N   . GLY B 34  ? 1.1006 0.9245 0.9139 0.1032  0.1591  0.1577  220 GLY A N   
2789 C CA  . GLY B 34  ? 1.1398 0.9336 0.9263 0.1056  0.1598  0.1576  220 GLY A CA  
2790 C C   . GLY B 34  ? 1.0772 0.8407 0.8500 0.1032  0.1400  0.1562  220 GLY A C   
2791 O O   . GLY B 34  ? 1.0117 0.7767 0.7945 0.1020  0.1254  0.1554  220 GLY A O   
2792 N N   . ALA B 35  ? 1.0672 0.8040 0.8184 0.1022  0.1396  0.1576  221 ALA A N   
2793 C CA  . ALA B 35  ? 1.0862 0.7919 0.8233 0.1007  0.1212  0.1581  221 ALA A CA  
2794 C C   . ALA B 35  ? 1.0255 0.7367 0.7807 0.0808  0.1163  0.1628  221 ALA A C   
2795 O O   . ALA B 35  ? 1.0511 0.7483 0.8008 0.0700  0.1178  0.1672  221 ALA A O   
2796 C CB  . ALA B 35  ? 1.1478 0.8253 0.8572 0.1052  0.1228  0.1592  221 ALA A CB  
2797 N N   . THR B 36  ? 1.0338 0.7665 0.8105 0.0767  0.1109  0.1622  222 THR A N   
2798 C CA  . THR B 36  ? 0.9148 0.6553 0.7076 0.0601  0.1053  0.1659  222 THR A CA  
2799 C C   . THR B 36  ? 0.9967 0.7142 0.7829 0.0612  0.0854  0.1695  222 THR A C   
2800 O O   . THR B 36  ? 1.0568 0.7758 0.8519 0.0484  0.0808  0.1741  222 THR A O   
2801 C CB  . THR B 36  ? 1.0115 0.7865 0.8294 0.0557  0.1072  0.1642  222 THR A CB  
2802 O OG1 . THR B 36  ? 1.1097 0.8978 0.9419 0.0373  0.1105  0.1661  222 THR A OG1 
2803 C CG2 . THR B 36  ? 0.9281 0.7042 0.7514 0.0649  0.0898  0.1643  222 THR A CG2 
2804 N N   . CYS B 37  ? 0.9754 0.6718 0.7468 0.0766  0.0733  0.1679  223 CYS A N   
2805 C CA  . CYS B 37  ? 0.9954 0.6665 0.7607 0.0790  0.0529  0.1724  223 CYS A CA  
2806 C C   . CYS B 37  ? 1.0071 0.6960 0.7949 0.0720  0.0426  0.1770  223 CYS A C   
2807 O O   . CYS B 37  ? 1.0614 0.7729 0.8637 0.0767  0.0419  0.1742  223 CYS A O   
2808 C CB  . CYS B 37  ? 1.0223 0.6682 0.7728 0.0714  0.0531  0.1777  223 CYS A CB  
2809 S SG  . CYS B 37  ? 1.1709 0.7876 0.8903 0.0837  0.0561  0.1739  223 CYS A SG  
2810 N N   . TYR B 38  ? 1.0603 0.7413 0.8520 0.0614  0.0350  0.1851  224 TYR A N   
2811 C CA  . TYR B 38  ? 1.0062 0.7020 0.8166 0.0559  0.0240  0.1915  224 TYR A CA  
2812 C C   . TYR B 38  ? 0.9630 0.6939 0.7908 0.0448  0.0355  0.1893  224 TYR A C   
2813 O O   . TYR B 38  ? 0.9921 0.7401 0.8352 0.0414  0.0271  0.1938  224 TYR A O   
2814 C CB  . TYR B 38  ? 0.9021 0.5781 0.7093 0.0485  0.0150  0.2018  224 TYR A CB  
2815 C CG  . TYR B 38  ? 0.9629 0.6270 0.7578 0.0393  0.0287  0.2020  224 TYR A CG  
2816 C CD1 . TYR B 38  ? 1.0021 0.6851 0.8049 0.0258  0.0434  0.2009  224 TYR A CD1 
2817 C CD2 . TYR B 38  ? 0.9383 0.5721 0.7138 0.0443  0.0266  0.2030  224 TYR A CD2 
2818 C CE1 . TYR B 38  ? 0.9918 0.6638 0.7858 0.0176  0.0562  0.2016  224 TYR A CE1 
2819 C CE2 . TYR B 38  ? 0.9578 0.5820 0.7238 0.0359  0.0394  0.2045  224 TYR A CE2 
2820 C CZ  . TYR B 38  ? 0.9931 0.6365 0.7694 0.0226  0.0545  0.2041  224 TYR A CZ  
2821 O OH  . TYR B 38  ? 1.0418 0.6758 0.8112 0.0143  0.0675  0.2060  224 TYR A OH  
2822 N N   . MET B 39  ? 0.9478 0.6900 0.7741 0.0391  0.0535  0.1831  225 MET A N   
2823 C CA  . MET B 39  ? 0.9442 0.7157 0.7863 0.0260  0.0632  0.1811  225 MET A CA  
2824 C C   . MET B 39  ? 0.9505 0.7509 0.8108 0.0287  0.0569  0.1801  225 MET A C   
2825 O O   . MET B 39  ? 0.9177 0.7368 0.7903 0.0195  0.0535  0.1825  225 MET A O   
2826 C CB  . MET B 39  ? 0.8991 0.6779 0.7397 0.0209  0.0824  0.1752  225 MET A CB  
2827 C CG  . MET B 39  ? 0.9112 0.7189 0.7691 0.0070  0.0913  0.1719  225 MET A CG  
2828 S SD  . MET B 39  ? 0.9609 0.7763 0.8215 0.0003  0.1128  0.1671  225 MET A SD  
2829 C CE  . MET B 39  ? 1.0617 0.9096 0.9447 -0.0163 0.1166  0.1630  225 MET A CE  
2830 N N   . ASN B 40  ? 0.9164 0.7210 0.7784 0.0419  0.0552  0.1770  226 ASN A N   
2831 C CA  . ASN B 40  ? 0.9033 0.7359 0.7845 0.0449  0.0491  0.1775  226 ASN A CA  
2832 C C   . ASN B 40  ? 0.8488 0.6800 0.7371 0.0455  0.0311  0.1854  226 ASN A C   
2833 O O   . ASN B 40  ? 0.8437 0.7012 0.7481 0.0388  0.0274  0.1883  226 ASN A O   
2834 C CB  . ASN B 40  ? 0.9432 0.7774 0.8245 0.0611  0.0505  0.1735  226 ASN A CB  
2835 C CG  . ASN B 40  ? 0.9081 0.7537 0.7884 0.0607  0.0693  0.1679  226 ASN A CG  
2836 O OD1 . ASN B 40  ? 0.8379 0.7001 0.7262 0.0468  0.0801  0.1668  226 ASN A OD1 
2837 N ND2 . ASN B 40  ? 1.0608 0.8975 0.9319 0.0765  0.0732  0.1645  226 ASN A ND2 
2838 N N   . SER B 41  ? 0.9082 0.7093 0.7851 0.0533  0.0193  0.1899  227 SER A N   
2839 C CA  . SER B 41  ? 0.9242 0.7237 0.8104 0.0544  0.0017  0.1998  227 SER A CA  
2840 C C   . SER B 41  ? 0.8615 0.6720 0.7521 0.0398  0.0029  0.2057  227 SER A C   
2841 O O   . SER B 41  ? 0.8162 0.6477 0.7217 0.0372  -0.0053 0.2122  227 SER A O   
2842 C CB  . SER B 41  ? 0.9495 0.7125 0.8234 0.0642  -0.0116 0.2039  227 SER A CB  
2843 O OG  . SER B 41  ? 0.9739 0.7266 0.8434 0.0794  -0.0149 0.1977  227 SER A OG  
2844 N N   . LEU B 42  ? 0.8219 0.6190 0.6995 0.0309  0.0136  0.2037  228 LEU A N   
2845 C CA  . LEU B 42  ? 0.8244 0.6299 0.7043 0.0182  0.0161  0.2083  228 LEU A CA  
2846 C C   . LEU B 42  ? 0.8397 0.6807 0.7322 0.0094  0.0233  0.2028  228 LEU A C   
2847 O O   . LEU B 42  ? 0.8424 0.7001 0.7422 0.0035  0.0186  0.2078  228 LEU A O   
2848 C CB  . LEU B 42  ? 0.7984 0.5814 0.6629 0.0110  0.0272  0.2068  228 LEU A CB  
2849 C CG  . LEU B 42  ? 0.7892 0.5757 0.6538 -0.0008 0.0308  0.2114  228 LEU A CG  
2850 C CD1 . LEU B 42  ? 0.7847 0.5649 0.6533 0.0029  0.0154  0.2253  228 LEU A CD1 
2851 C CD2 . LEU B 42  ? 0.7938 0.5595 0.6454 -0.0077 0.0437  0.2091  228 LEU A CD2 
2852 N N   . LEU B 43  ? 0.8701 0.7238 0.7654 0.0087  0.0344  0.1932  229 LEU A N   
2853 C CA  . LEU B 43  ? 0.7962 0.6828 0.7043 -0.0009 0.0405  0.1877  229 LEU A CA  
2854 C C   . LEU B 43  ? 0.8097 0.7224 0.7337 0.0027  0.0280  0.1929  229 LEU A C   
2855 O O   . LEU B 43  ? 0.8951 0.8311 0.8265 -0.0062 0.0266  0.1931  229 LEU A O   
2856 C CB  . LEU B 43  ? 0.7965 0.6916 0.7076 -0.0012 0.0539  0.1789  229 LEU A CB  
2857 C CG  . LEU B 43  ? 0.7909 0.6712 0.6917 -0.0095 0.0689  0.1737  229 LEU A CG  
2858 C CD1 . LEU B 43  ? 0.8286 0.7176 0.7342 -0.0070 0.0812  0.1679  229 LEU A CD1 
2859 C CD2 . LEU B 43  ? 0.7840 0.6753 0.6880 -0.0251 0.0732  0.1708  229 LEU A CD2 
2860 N N   . GLN B 44  ? 0.7927 0.7019 0.7220 0.0160  0.0185  0.1969  230 GLN A N   
2861 C CA  . GLN B 44  ? 0.7736 0.7072 0.7203 0.0200  0.0060  0.2037  230 GLN A CA  
2862 C C   . GLN B 44  ? 0.8522 0.7841 0.7995 0.0176  -0.0055 0.2147  230 GLN A C   
2863 O O   . GLN B 44  ? 0.9021 0.8618 0.8616 0.0141  -0.0116 0.2197  230 GLN A O   
2864 C CB  . GLN B 44  ? 0.8407 0.7677 0.7937 0.0356  -0.0015 0.2055  230 GLN A CB  
2865 C CG  . GLN B 44  ? 0.9802 0.9413 0.9545 0.0385  -0.0051 0.2070  230 GLN A CG  
2866 C CD  . GLN B 44  ? 0.8773 0.8547 0.8560 0.0369  0.0088  0.1978  230 GLN A CD  
2867 O OE1 . GLN B 44  ? 0.9021 0.9120 0.8952 0.0290  0.0114  0.1969  230 GLN A OE1 
2868 N NE2 . GLN B 44  ? 0.8778 0.8337 0.8448 0.0448  0.0174  0.1918  230 GLN A NE2 
2869 N N   . THR B 45  ? 0.9458 0.8466 0.8803 0.0198  -0.0086 0.2197  231 THR A N   
2870 C CA  . THR B 45  ? 0.8583 0.7567 0.7942 0.0182  -0.0185 0.2322  231 THR A CA  
2871 C C   . THR B 45  ? 0.8377 0.7556 0.7711 0.0054  -0.0110 0.2305  231 THR A C   
2872 O O   . THR B 45  ? 0.8089 0.7477 0.7507 0.0041  -0.0184 0.2391  231 THR A O   
2873 C CB  . THR B 45  ? 0.8120 0.6725 0.7347 0.0216  -0.0216 0.2376  231 THR A CB  
2874 O OG1 . THR B 45  ? 0.8843 0.7253 0.8082 0.0341  -0.0310 0.2385  231 THR A OG1 
2875 C CG2 . THR B 45  ? 0.8481 0.7076 0.7743 0.0198  -0.0307 0.2526  231 THR A CG2 
2876 N N   . LEU B 46  ? 0.8700 0.7811 0.7917 -0.0036 0.0038  0.2195  232 LEU A N   
2877 C CA  . LEU B 46  ? 0.8850 0.8117 0.8030 -0.0156 0.0114  0.2152  232 LEU A CA  
2878 C C   . LEU B 46  ? 0.9732 0.9369 0.9032 -0.0204 0.0110  0.2093  232 LEU A C   
2879 O O   . LEU B 46  ? 0.9807 0.9639 0.9107 -0.0269 0.0097  0.2098  232 LEU A O   
2880 C CB  . LEU B 46  ? 0.8483 0.7557 0.7531 -0.0237 0.0267  0.2052  232 LEU A CB  
2881 C CG  . LEU B 46  ? 0.8525 0.7243 0.7448 -0.0207 0.0279  0.2115  232 LEU A CG  
2882 C CD1 . LEU B 46  ? 0.7695 0.6247 0.6517 -0.0279 0.0436  0.2018  232 LEU A CD1 
2883 C CD2 . LEU B 46  ? 0.8798 0.7487 0.7690 -0.0219 0.0228  0.2229  232 LEU A CD2 
2884 N N   . PHE B 47  ? 0.9162 0.8903 0.8562 -0.0168 0.0118  0.2041  233 PHE A N   
2885 C CA  . PHE B 47  ? 0.8845 0.8945 0.8382 -0.0216 0.0108  0.1996  233 PHE A CA  
2886 C C   . PHE B 47  ? 0.8879 0.9220 0.8521 -0.0183 -0.0030 0.2107  233 PHE A C   
2887 O O   . PHE B 47  ? 0.9100 0.9722 0.8781 -0.0260 -0.0043 0.2084  233 PHE A O   
2888 C CB  . PHE B 47  ? 0.9142 0.9298 0.8786 -0.0159 0.0140  0.1953  233 PHE A CB  
2889 C CG  . PHE B 47  ? 0.8565 0.9099 0.8388 -0.0190 0.0109  0.1939  233 PHE A CG  
2890 C CD1 . PHE B 47  ? 0.8211 0.8927 0.8068 -0.0315 0.0189  0.1841  233 PHE A CD1 
2891 C CD2 . PHE B 47  ? 0.8157 0.8862 0.8135 -0.0096 -0.0008 0.2030  233 PHE A CD2 
2892 C CE1 . PHE B 47  ? 0.7915 0.8983 0.7947 -0.0350 0.0149  0.1837  233 PHE A CE1 
2893 C CE2 . PHE B 47  ? 0.8016 0.9077 0.8170 -0.0126 -0.0038 0.2030  233 PHE A CE2 
2894 C CZ  . PHE B 47  ? 0.7566 0.8813 0.7745 -0.0255 0.0039  0.1935  233 PHE A CZ  
2895 N N   . PHE B 48  ? 0.8171 0.8408 0.7863 -0.0068 -0.0139 0.2230  234 PHE A N   
2896 C CA  . PHE B 48  ? 0.8331 0.8789 0.8149 -0.0024 -0.0275 0.2363  234 PHE A CA  
2897 C C   . PHE B 48  ? 0.8515 0.8926 0.8243 -0.0047 -0.0306 0.2456  234 PHE A C   
2898 O O   . PHE B 48  ? 0.7995 0.8573 0.7827 0.0001  -0.0419 0.2596  234 PHE A O   
2899 C CB  . PHE B 48  ? 0.8288 0.8667 0.8244 0.0112  -0.0387 0.2458  234 PHE A CB  
2900 C CG  . PHE B 48  ? 0.8508 0.9020 0.8589 0.0152  -0.0369 0.2393  234 PHE A CG  
2901 C CD1 . PHE B 48  ? 0.8136 0.9029 0.8366 0.0112  -0.0388 0.2393  234 PHE A CD1 
2902 C CD2 . PHE B 48  ? 0.8804 0.9068 0.8848 0.0234  -0.0330 0.2336  234 PHE A CD2 
2903 C CE1 . PHE B 48  ? 0.7296 0.8325 0.7661 0.0152  -0.0365 0.2350  234 PHE A CE1 
2904 C CE2 . PHE B 48  ? 0.8849 0.9246 0.9009 0.0284  -0.0300 0.2286  234 PHE A CE2 
2905 C CZ  . PHE B 48  ? 0.7375 0.8157 0.7708 0.0242  -0.0315 0.2298  234 PHE A CZ  
2906 N N   . THR B 49  ? 0.8638 0.8832 0.8188 -0.0110 -0.0205 0.2396  235 THR A N   
2907 C CA  . THR B 49  ? 0.8595 0.8818 0.8045 -0.0155 -0.0193 0.2449  235 THR A CA  
2908 C C   . THR B 49  ? 0.9255 0.9778 0.8678 -0.0255 -0.0144 0.2341  235 THR A C   
2909 O O   . THR B 49  ? 0.9041 0.9499 0.8338 -0.0350 -0.0031 0.2208  235 THR A O   
2910 C CB  . THR B 49  ? 0.7807 0.7686 0.7091 -0.0182 -0.0098 0.2424  235 THR A CB  
2911 O OG1 . THR B 49  ? 0.9493 0.9088 0.8800 -0.0096 -0.0152 0.2500  235 THR A OG1 
2912 C CG2 . THR B 49  ? 0.8087 0.7989 0.7289 -0.0197 -0.0096 0.2515  235 THR A CG2 
2913 N N   . ASN B 50  ? 0.8804 0.9663 0.8357 -0.0234 -0.0242 0.2403  236 ASN A N   
2914 C CA  . ASN B 50  ? 0.8765 0.9936 0.8332 -0.0324 -0.0225 0.2294  236 ASN A CA  
2915 C C   . ASN B 50  ? 0.8507 0.9697 0.7887 -0.0418 -0.0150 0.2203  236 ASN A C   
2916 O O   . ASN B 50  ? 0.8490 0.9756 0.7826 -0.0522 -0.0086 0.2044  236 ASN A O   
2917 C CB  . ASN B 50  ? 0.8495 1.0024 0.8233 -0.0275 -0.0356 0.2412  236 ASN A CB  
2918 C CG  . ASN B 50  ? 0.8000 0.9551 0.7941 -0.0196 -0.0417 0.2460  236 ASN A CG  
2919 O OD1 . ASN B 50  ? 0.7510 0.8814 0.7490 -0.0106 -0.0445 0.2534  236 ASN A OD1 
2920 N ND2 . ASN B 50  ? 0.8944 1.0791 0.9017 -0.0229 -0.0442 0.2418  236 ASN A ND2 
2921 N N   . GLN B 51  ? 0.7812 0.8936 0.7089 -0.0380 -0.0159 0.2304  237 GLN A N   
2922 C CA  . GLN B 51  ? 0.8841 0.9955 0.7923 -0.0452 -0.0076 0.2212  237 GLN A CA  
2923 C C   . GLN B 51  ? 0.9212 1.0016 0.8183 -0.0528 0.0060  0.2062  237 GLN A C   
2924 O O   . GLN B 51  ? 0.8754 0.9585 0.7618 -0.0626 0.0132  0.1906  237 GLN A O   
2925 C CB  . GLN B 51  ? 0.8606 0.9698 0.7612 -0.0377 -0.0099 0.2374  237 GLN A CB  
2926 C CG  . GLN B 51  ? 0.9126 1.0241 0.7919 -0.0430 -0.0017 0.2287  237 GLN A CG  
2927 C CD  . GLN B 51  ? 0.9106 1.0308 0.7844 -0.0341 -0.0048 0.2468  237 GLN A CD  
2928 O OE1 . GLN B 51  ? 0.9974 1.1192 0.8851 -0.0246 -0.0133 0.2672  237 GLN A OE1 
2929 N NE2 . GLN B 51  ? 0.9479 1.0737 0.8020 -0.0366 0.0021  0.2397  237 GLN A NE2 
2930 N N   . LEU B 52  ? 0.9313 0.9819 0.8312 -0.0484 0.0091  0.2108  238 LEU A N   
2931 C CA  . LEU B 52  ? 0.8753 0.8984 0.7677 -0.0551 0.0218  0.1981  238 LEU A CA  
2932 C C   . LEU B 52  ? 0.9322 0.9676 0.8322 -0.0634 0.0254  0.1827  238 LEU A C   
2933 O O   . LEU B 52  ? 0.9340 0.9605 0.8277 -0.0731 0.0356  0.1687  238 LEU A O   
2934 C CB  . LEU B 52  ? 0.7977 0.7901 0.6922 -0.0476 0.0222  0.2073  238 LEU A CB  
2935 C CG  . LEU B 52  ? 0.8441 0.8108 0.7346 -0.0523 0.0338  0.1966  238 LEU A CG  
2936 C CD1 . LEU B 52  ? 0.7956 0.7467 0.6721 -0.0608 0.0461  0.1886  238 LEU A CD1 
2937 C CD2 . LEU B 52  ? 0.7929 0.7337 0.6855 -0.0431 0.0307  0.2064  238 LEU A CD2 
2938 N N   . ARG B 53  ? 0.9095 0.9658 0.8252 -0.0595 0.0169  0.1862  239 ARG A N   
2939 C CA  . ARG B 53  ? 0.9498 1.0197 0.8762 -0.0664 0.0200  0.1744  239 ARG A CA  
2940 C C   . ARG B 53  ? 0.9264 1.0174 0.8490 -0.0786 0.0212  0.1615  239 ARG A C   
2941 O O   . ARG B 53  ? 0.9483 1.0344 0.8715 -0.0885 0.0295  0.1481  239 ARG A O   
2942 C CB  . ARG B 53  ? 0.8910 0.9810 0.8358 -0.0585 0.0102  0.1827  239 ARG A CB  
2943 C CG  . ARG B 53  ? 0.8469 0.9610 0.8060 -0.0652 0.0111  0.1737  239 ARG A CG  
2944 C CD  . ARG B 53  ? 0.9389 1.0538 0.9139 -0.0556 0.0091  0.1796  239 ARG A CD  
2945 N NE  . ARG B 53  ? 0.9216 1.0459 0.9052 -0.0440 -0.0032 0.1941  239 ARG A NE  
2946 C CZ  . ARG B 53  ? 0.8142 0.9691 0.8156 -0.0412 -0.0118 0.1995  239 ARG A CZ  
2947 N NH1 . ARG B 53  ? 0.8176 0.9979 0.8298 -0.0493 -0.0103 0.1922  239 ARG A NH1 
2948 N NH2 . ARG B 53  ? 0.7434 0.9035 0.7539 -0.0301 -0.0228 0.2137  239 ARG A NH2 
2949 N N   . LYS B 54  ? 0.9016 1.0162 0.8205 -0.0780 0.0125  0.1656  240 LYS A N   
2950 C CA  . LYS B 54  ? 0.8552 0.9901 0.7680 -0.0890 0.0117  0.1524  240 LYS A CA  
2951 C C   . LYS B 54  ? 0.9159 1.0267 0.8111 -0.0968 0.0229  0.1397  240 LYS A C   
2952 O O   . LYS B 54  ? 0.9588 1.0746 0.8523 -0.1084 0.0258  0.1239  240 LYS A O   
2953 C CB  . LYS B 54  ? 0.8827 1.0468 0.7918 -0.0849 0.0004  0.1609  240 LYS A CB  
2954 C CG  . LYS B 54  ? 1.0300 1.2174 0.9306 -0.0954 -0.0027 0.1471  240 LYS A CG  
2955 C CD  . LYS B 54  ? 0.9913 1.2082 0.8862 -0.0896 -0.0134 0.1572  240 LYS A CD  
2956 C CE  . LYS B 54  ? 1.1303 1.3704 1.0139 -0.0996 -0.0177 0.1425  240 LYS A CE  
2957 N NZ  . LYS B 54  ? 1.2851 1.5571 1.1625 -0.0931 -0.0281 0.1533  240 LYS A NZ  
2958 N N   . ALA B 55  ? 0.9807 1.0650 0.8640 -0.0905 0.0287  0.1469  241 ALA A N   
2959 C CA  . ALA B 55  ? 0.9693 1.0281 0.8376 -0.0967 0.0404  0.1364  241 ALA A CA  
2960 C C   . ALA B 55  ? 0.9461 0.9868 0.8224 -0.1049 0.0502  0.1255  241 ALA A C   
2961 O O   . ALA B 55  ? 0.9981 1.0309 0.8692 -0.1152 0.0573  0.1108  241 ALA A O   
2962 C CB  . ALA B 55  ? 0.8882 0.9233 0.7458 -0.0875 0.0443  0.1496  241 ALA A CB  
2963 N N   . VAL B 56  ? 0.8957 0.9296 0.7848 -0.0998 0.0506  0.1329  242 VAL A N   
2964 C CA  . VAL B 56  ? 1.0099 1.0297 0.9077 -0.1060 0.0602  0.1250  242 VAL A CA  
2965 C C   . VAL B 56  ? 0.9991 1.0418 0.9086 -0.1177 0.0588  0.1118  242 VAL A C   
2966 O O   . VAL B 56  ? 0.9812 1.0138 0.8940 -0.1277 0.0674  0.1007  242 VAL A O   
2967 C CB  . VAL B 56  ? 1.0331 1.0444 0.9404 -0.0961 0.0599  0.1359  242 VAL A CB  
2968 C CG1 . VAL B 56  ? 0.9332 0.9378 0.8513 -0.1013 0.0694  0.1289  242 VAL A CG1 
2969 C CG2 . VAL B 56  ? 0.9895 0.9728 0.8853 -0.0868 0.0616  0.1473  242 VAL A CG2 
2970 N N   . TYR B 57  ? 1.0264 1.1008 0.9438 -0.1169 0.0472  0.1138  243 TYR A N   
2971 C CA  . TYR B 57  ? 0.9536 1.0523 0.8840 -0.1282 0.0436  0.1030  243 TYR A CA  
2972 C C   . TYR B 57  ? 1.0004 1.0963 0.9205 -0.1408 0.0456  0.0867  243 TYR A C   
2973 O O   . TYR B 57  ? 0.9359 1.0387 0.8678 -0.1525 0.0466  0.0756  243 TYR A O   
2974 C CB  . TYR B 57  ? 0.8612 0.9952 0.8006 -0.1244 0.0298  0.1098  243 TYR A CB  
2975 C CG  . TYR B 57  ? 0.7976 0.9397 0.7544 -0.1146 0.0273  0.1224  243 TYR A CG  
2976 C CD1 . TYR B 57  ? 0.8701 0.9965 0.8369 -0.1130 0.0368  0.1228  243 TYR A CD1 
2977 C CD2 . TYR B 57  ? 0.7868 0.9527 0.7500 -0.1063 0.0157  0.1339  243 TYR A CD2 
2978 C CE1 . TYR B 57  ? 0.8719 1.0046 0.8525 -0.1026 0.0350  0.1331  243 TYR A CE1 
2979 C CE2 . TYR B 57  ? 0.7713 0.9430 0.7508 -0.0965 0.0135  0.1445  243 TYR A CE2 
2980 C CZ  . TYR B 57  ? 0.8253 0.9797 0.8124 -0.0944 0.0233  0.1434  243 TYR A CZ  
2981 O OH  . TYR B 57  ? 0.8740 1.0329 0.8751 -0.0834 0.0217  0.1527  243 TYR A OH  
2982 N N   . MET B 58  ? 0.9832 1.0689 0.8821 -0.1384 0.0460  0.0852  244 MET A N   
2983 C CA  . MET B 58  ? 0.9694 1.0546 0.8555 -0.1485 0.0461  0.0689  244 MET A CA  
2984 C C   . MET B 58  ? 1.0460 1.0969 0.9245 -0.1537 0.0597  0.0600  244 MET A C   
2985 O O   . MET B 58  ? 1.0054 1.0491 0.8685 -0.1587 0.0612  0.0477  244 MET A O   
2986 C CB  . MET B 58  ? 0.8641 0.9626 0.7306 -0.1421 0.0386  0.0718  244 MET A CB  
2987 C CG  . MET B 58  ? 0.9843 1.1200 0.8587 -0.1389 0.0244  0.0794  244 MET A CG  
2988 S SD  . MET B 58  ? 1.3477 1.5029 1.1982 -0.1327 0.0160  0.0815  244 MET A SD  
2989 C CE  . MET B 58  ? 1.0959 1.2250 0.9344 -0.1179 0.0245  0.0986  244 MET A CE  
2990 N N   . MET B 59  ? 0.9048 1.0275 1.0859 -0.0762 -0.1046 0.2498  245 MET A N   
2991 C CA  . MET B 59  ? 0.9631 1.0597 1.1365 -0.0770 -0.0923 0.2524  245 MET A CA  
2992 C C   . MET B 59  ? 0.9710 1.0657 1.1705 -0.0830 -0.0721 0.2359  245 MET A C   
2993 O O   . MET B 59  ? 1.0115 1.1090 1.2264 -0.0854 -0.0633 0.2270  245 MET A O   
2994 C CB  . MET B 59  ? 1.0627 1.1183 1.2044 -0.0726 -0.0883 0.2698  245 MET A CB  
2995 C CG  . MET B 59  ? 0.9594 1.0135 1.0731 -0.0665 -0.1076 0.2873  245 MET A CG  
2996 S SD  . MET B 59  ? 0.9986 1.0040 1.0748 -0.0612 -0.1030 0.3079  245 MET A SD  
2997 C CE  . MET B 59  ? 0.9072 0.9030 0.9894 -0.0619 -0.0927 0.3043  245 MET A CE  
2998 N N   . PRO B 60  ? 1.0455 1.1352 1.2507 -0.0855 -0.0643 0.2315  246 PRO A N   
2999 C CA  . PRO B 60  ? 1.0743 1.1615 1.3045 -0.0913 -0.0447 0.2158  246 PRO A CA  
3000 C C   . PRO B 60  ? 1.0944 1.1416 1.3136 -0.0915 -0.0264 0.2203  246 PRO A C   
3001 O O   . PRO B 60  ? 1.0693 1.0926 1.2826 -0.0925 -0.0150 0.2223  246 PRO A O   
3002 C CB  . PRO B 60  ? 0.9916 1.0876 1.2280 -0.0932 -0.0458 0.2117  246 PRO A CB  
3003 C CG  . PRO B 60  ? 1.0219 1.1331 1.2420 -0.0890 -0.0672 0.2224  246 PRO A CG  
3004 C CD  . PRO B 60  ? 1.0129 1.1045 1.2053 -0.0836 -0.0745 0.2389  246 PRO A CD  
3005 N N   . THR B 61  ? 1.1102 1.1503 1.3275 -0.0906 -0.0232 0.2216  247 THR A N   
3006 C CA  . THR B 61  ? 1.1904 1.1936 1.3964 -0.0905 -0.0070 0.2265  247 THR A CA  
3007 C C   . THR B 61  ? 1.1513 1.1568 1.3846 -0.0960 0.0112  0.2100  247 THR A C   
3008 O O   . THR B 61  ? 1.1613 1.1407 1.3883 -0.0962 0.0241  0.2124  247 THR A O   
3009 C CB  . THR B 61  ? 1.1776 1.1678 1.3602 -0.0854 -0.0154 0.2407  247 THR A CB  
3010 O OG1 . THR B 61  ? 1.0894 1.1108 1.2866 -0.0856 -0.0258 0.2339  247 THR A OG1 
3011 C CG2 . THR B 61  ? 1.1050 1.0848 1.2573 -0.0799 -0.0305 0.2587  247 THR A CG2 
3012 N N   . GLU B 62  ? 1.0758 1.1116 1.3389 -0.1005 0.0125  0.1933  248 GLU A N   
3013 C CA  . GLU B 62  ? 1.1353 1.1752 1.4256 -0.1058 0.0291  0.1771  248 GLU A CA  
3014 C C   . GLU B 62  ? 1.1468 1.1524 1.4337 -0.1081 0.0496  0.1769  248 GLU A C   
3015 O O   . GLU B 62  ? 1.1888 1.1776 1.4800 -0.1099 0.0639  0.1735  248 GLU A O   
3016 C CB  . GLU B 62  ? 1.0676 1.1455 1.3895 -0.1101 0.0264  0.1598  248 GLU A CB  
3017 C CG  . GLU B 62  ? 1.1410 1.2557 1.4684 -0.1084 0.0058  0.1587  248 GLU A CG  
3018 C CD  . GLU B 62  ? 1.1265 1.2472 1.4374 -0.1053 -0.0095 0.1686  248 GLU A CD  
3019 O OE1 . GLU B 62  ? 1.1378 1.2311 1.4299 -0.1038 -0.0046 0.1782  248 GLU A OE1 
3020 O OE2 . GLU B 62  ? 1.0588 1.2112 1.3757 -0.1045 -0.0262 0.1667  248 GLU A OE2 
3021 N N   . GLY B 63  ? 1.0532 1.0475 1.3322 -0.1082 0.0513  0.1807  249 GLY A N   
3022 C CA  . GLY B 63  ? 1.1773 1.1411 1.4548 -0.1108 0.0702  0.1796  249 GLY A CA  
3023 C C   . GLY B 63  ? 1.2423 1.1656 1.4864 -0.1069 0.0730  0.1976  249 GLY A C   
3024 O O   . GLY B 63  ? 1.2691 1.1683 1.5055 -0.1080 0.0829  0.2007  249 GLY A O   
3025 N N   . ASP B 64  ? 1.1775 1.0929 1.4016 -0.1025 0.0642  0.2096  250 ASP A N   
3026 C CA  . ASP B 64  ? 1.2252 1.1025 1.4165 -0.0985 0.0658  0.2274  250 ASP A CA  
3027 C C   . ASP B 64  ? 1.1789 1.0309 1.3675 -0.0995 0.0812  0.2275  250 ASP A C   
3028 O O   . ASP B 64  ? 1.2179 1.0847 1.4267 -0.1021 0.0863  0.2163  250 ASP A O   
3029 C CB  . ASP B 64  ? 1.2163 1.0990 1.3840 -0.0923 0.0452  0.2424  250 ASP A CB  
3030 C CG  . ASP B 64  ? 1.2529 1.1577 1.4199 -0.0910 0.0298  0.2440  250 ASP A CG  
3031 O OD1 . ASP B 64  ? 1.2447 1.1700 1.4350 -0.0950 0.0327  0.2308  250 ASP A OD1 
3032 O OD2 . ASP B 64  ? 1.3289 1.2306 1.4722 -0.0859 0.0145  0.2586  250 ASP A OD2 
3033 N N   . ASP B 65  ? 1.1111 0.9246 1.2743 -0.0975 0.0884  0.2406  251 ASP A N   
3034 C CA  . ASP B 65  ? 1.2017 0.9867 1.3586 -0.0982 0.1035  0.2426  251 ASP A CA  
3035 C C   . ASP B 65  ? 1.2073 0.9896 1.3459 -0.0934 0.0926  0.2539  251 ASP A C   
3036 O O   . ASP B 65  ? 1.2127 0.9851 1.3250 -0.0882 0.0798  0.2696  251 ASP A O   
3037 C CB  . ASP B 65  ? 1.1293 0.8738 1.2669 -0.0984 0.1160  0.2516  251 ASP A CB  
3038 C CG  . ASP B 65  ? 1.2179 0.9295 1.3417 -0.0981 0.1287  0.2579  251 ASP A CG  
3039 O OD1 . ASP B 65  ? 1.2460 0.9429 1.3444 -0.0932 0.1205  0.2725  251 ASP A OD1 
3040 O OD2 . ASP B 65  ? 1.3277 1.0286 1.4663 -0.1027 0.1470  0.2479  251 ASP A OD2 
3041 N N   . SER B 66  ? 1.1875 0.9781 1.3402 -0.0950 0.0978  0.2459  252 SER A N   
3042 C CA  . SER B 66  ? 1.1835 0.9767 1.3227 -0.0906 0.0867  0.2546  252 SER A CA  
3043 C C   . SER B 66  ? 1.2013 0.9556 1.3060 -0.0863 0.0879  0.2732  252 SER A C   
3044 O O   . SER B 66  ? 1.2632 1.0173 1.3473 -0.0810 0.0729  0.2862  252 SER A O   
3045 C CB  . SER B 66  ? 1.2917 1.0972 1.4531 -0.0937 0.0949  0.2419  252 SER A CB  
3046 O OG  . SER B 66  ? 1.3578 1.1570 1.5037 -0.0898 0.0881  0.2512  252 SER A OG  
3047 N N   . SER B 67  ? 1.1970 0.9179 1.2948 -0.0884 0.1056  0.2748  253 SER A N   
3048 C CA  . SER B 67  ? 1.2498 0.9324 1.3156 -0.0847 0.1082  0.2919  253 SER A CA  
3049 C C   . SER B 67  ? 1.2452 0.9151 1.2849 -0.0805 0.0968  0.3072  253 SER A C   
3050 O O   . SER B 67  ? 1.2823 0.9258 1.2930 -0.0761 0.0933  0.3234  253 SER A O   
3051 C CB  . SER B 67  ? 1.3122 0.9630 1.3790 -0.0886 0.1309  0.2886  253 SER A CB  
3052 O OG  . SER B 67  ? 1.2418 0.8822 1.3108 -0.0913 0.1386  0.2864  253 SER A OG  
3053 N N   . LYS B 68  ? 1.2077 0.8957 1.2569 -0.0816 0.0907  0.3027  254 LYS A N   
3054 C CA  . LYS B 68  ? 1.2010 0.8752 1.2270 -0.0782 0.0819  0.3162  254 LYS A CA  
3055 C C   . LYS B 68  ? 1.1851 0.8923 1.2147 -0.0758 0.0618  0.3165  254 LYS A C   
3056 O O   . LYS B 68  ? 1.2161 0.9155 1.2291 -0.0733 0.0539  0.3263  254 LYS A O   
3057 C CB  . LYS B 68  ? 1.1731 0.8264 1.2018 -0.0820 0.0969  0.3129  254 LYS A CB  
3058 C CG  . LYS B 68  ? 1.2918 0.9074 1.3120 -0.0839 0.1164  0.3153  254 LYS A CG  
3059 C CD  . LYS B 68  ? 1.3532 0.9492 1.3763 -0.0878 0.1304  0.3120  254 LYS A CD  
3060 C CE  . LYS B 68  ? 1.3941 0.9523 1.4082 -0.0899 0.1495  0.3146  254 LYS A CE  
3061 N NZ  . LYS B 68  ? 1.4714 1.0097 1.4876 -0.0936 0.1628  0.3120  254 LYS A NZ  
3062 N N   . SER B 69  ? 1.1713 0.9149 1.2218 -0.0767 0.0533  0.3061  255 SER A N   
3063 C CA  . SER B 69  ? 1.0929 0.8699 1.1486 -0.0749 0.0344  0.3053  255 SER A CA  
3064 C C   . SER B 69  ? 1.0475 0.8281 1.0822 -0.0689 0.0167  0.3189  255 SER A C   
3065 O O   . SER B 69  ? 0.9929 0.7851 1.0342 -0.0685 0.0142  0.3158  255 SER A O   
3066 C CB  . SER B 69  ? 1.1429 0.9585 1.2341 -0.0795 0.0347  0.2858  255 SER A CB  
3067 O OG  . SER B 69  ? 1.0831 0.9312 1.1792 -0.0780 0.0164  0.2850  255 SER A OG  
3068 N N   . VAL B 70  ? 1.1666 0.9370 1.1760 -0.0643 0.0045  0.3340  256 VAL A N   
3069 C CA  . VAL B 70  ? 1.1017 0.8777 1.0911 -0.0584 -0.0140 0.3472  256 VAL A CA  
3070 C C   . VAL B 70  ? 0.9875 0.8075 0.9960 -0.0586 -0.0294 0.3386  256 VAL A C   
3071 O O   . VAL B 70  ? 0.9569 0.7872 0.9624 -0.0561 -0.0384 0.3415  256 VAL A O   
3072 C CB  . VAL B 70  ? 0.9818 0.7363 0.9404 -0.0536 -0.0229 0.3651  256 VAL A CB  
3073 C CG1 . VAL B 70  ? 0.9976 0.7572 0.9352 -0.0474 -0.0420 0.3791  256 VAL A CG1 
3074 C CG2 . VAL B 70  ? 1.0038 0.7141 0.9443 -0.0537 -0.0070 0.3732  256 VAL A CG2 
3075 N N   . PRO B 71  ? 0.9279 0.7753 0.9555 -0.0614 -0.0337 0.3283  257 PRO A N   
3076 C CA  . PRO B 71  ? 0.9252 0.8149 0.9728 -0.0622 -0.0472 0.3188  257 PRO A CA  
3077 C C   . PRO B 71  ? 1.0205 0.9243 1.0914 -0.0655 -0.0394 0.3054  257 PRO A C   
3078 O O   . PRO B 71  ? 1.0585 0.9857 1.1342 -0.0640 -0.0518 0.3043  257 PRO A O   
3079 C CB  . PRO B 71  ? 1.0161 0.9265 1.0814 -0.0656 -0.0480 0.3086  257 PRO A CB  
3080 C CG  . PRO B 71  ? 1.0206 0.9014 1.0647 -0.0639 -0.0441 0.3196  257 PRO A CG  
3081 C CD  . PRO B 71  ? 0.9706 0.8123 1.0003 -0.0635 -0.0286 0.3261  257 PRO A CD  
3082 N N   . LEU B 72  ? 1.0311 0.9211 1.1167 -0.0701 -0.0192 0.2951  258 LEU A N   
3083 C CA  . LEU B 72  ? 0.9737 0.8765 1.0818 -0.0734 -0.0113 0.2822  258 LEU A CA  
3084 C C   . LEU B 72  ? 0.9393 0.8258 1.0302 -0.0697 -0.0130 0.2922  258 LEU A C   
3085 O O   . LEU B 72  ? 0.9762 0.8837 1.0791 -0.0698 -0.0188 0.2866  258 LEU A O   
3086 C CB  . LEU B 72  ? 0.9987 0.8894 1.1259 -0.0791 0.0110  0.2693  258 LEU A CB  
3087 C CG  . LEU B 72  ? 1.0695 0.9741 1.2222 -0.0829 0.0203  0.2546  258 LEU A CG  
3088 C CD1 . LEU B 72  ? 1.0371 0.9862 1.2152 -0.0848 0.0084  0.2420  258 LEU A CD1 
3089 C CD2 . LEU B 72  ? 1.1366 1.0252 1.3051 -0.0882 0.0429  0.2435  258 LEU A CD2 
3090 N N   . ALA B 73  ? 0.9424 0.7915 1.0053 -0.0665 -0.0082 0.3070  259 ALA A N   
3091 C CA  . ALA B 73  ? 0.9991 0.8309 1.0441 -0.0628 -0.0098 0.3173  259 ALA A CA  
3092 C C   . ALA B 73  ? 0.9714 0.8240 1.0058 -0.0579 -0.0322 0.3258  259 ALA A C   
3093 O O   . ALA B 73  ? 1.0222 0.8834 1.0594 -0.0568 -0.0364 0.3252  259 ALA A O   
3094 C CB  . ALA B 73  ? 1.0508 0.8382 1.0665 -0.0603 -0.0011 0.3322  259 ALA A CB  
3095 N N   . LEU B 74  ? 0.9501 0.8118 0.9729 -0.0551 -0.0470 0.3337  260 LEU A N   
3096 C CA  . LEU B 74  ? 0.9777 0.8601 0.9905 -0.0505 -0.0689 0.3419  260 LEU A CA  
3097 C C   . LEU B 74  ? 0.9612 0.8852 1.0026 -0.0533 -0.0764 0.3271  260 LEU A C   
3098 O O   . LEU B 74  ? 0.9414 0.8802 0.9796 -0.0505 -0.0895 0.3307  260 LEU A O   
3099 C CB  . LEU B 74  ? 0.9436 0.8271 0.9391 -0.0473 -0.0823 0.3526  260 LEU A CB  
3100 C CG  . LEU B 74  ? 0.9823 0.8805 0.9615 -0.0418 -0.1049 0.3645  260 LEU A CG  
3101 C CD1 . LEU B 74  ? 0.9634 0.8320 0.9155 -0.0370 -0.1053 0.3798  260 LEU A CD1 
3102 C CD2 . LEU B 74  ? 0.9375 0.8420 0.9041 -0.0394 -0.1182 0.3725  260 LEU A CD2 
3103 N N   . GLN B 75  ? 0.9658 0.9093 1.0353 -0.0588 -0.0686 0.3106  261 GLN A N   
3104 C CA  . GLN B 75  ? 0.9182 0.8991 1.0167 -0.0621 -0.0731 0.2953  261 GLN A CA  
3105 C C   . GLN B 75  ? 0.9300 0.9061 1.0362 -0.0630 -0.0650 0.2906  261 GLN A C   
3106 O O   . GLN B 75  ? 0.8825 0.8830 0.9980 -0.0624 -0.0757 0.2870  261 GLN A O   
3107 C CB  . GLN B 75  ? 0.8958 0.8945 1.0228 -0.0680 -0.0637 0.2782  261 GLN A CB  
3108 C CG  . GLN B 75  ? 0.8983 0.9141 1.0249 -0.0677 -0.0750 0.2791  261 GLN A CG  
3109 C CD  . GLN B 75  ? 0.9370 0.9618 1.0882 -0.0734 -0.0625 0.2638  261 GLN A CD  
3110 O OE1 . GLN B 75  ? 0.9588 0.9615 1.1151 -0.0764 -0.0436 0.2590  261 GLN A OE1 
3111 N NE2 . GLN B 75  ? 0.9097 0.9673 1.0762 -0.0751 -0.0731 0.2561  261 GLN A NE2 
3112 N N   . ARG B 76  ? 0.9361 0.8807 1.0383 -0.0644 -0.0461 0.2908  262 ARG A N   
3113 C CA  . ARG B 76  ? 0.9834 0.9219 1.0938 -0.0657 -0.0365 0.2856  262 ARG A CA  
3114 C C   . ARG B 76  ? 0.9676 0.9034 1.0583 -0.0603 -0.0501 0.2983  262 ARG A C   
3115 O O   . ARG B 76  ? 0.9482 0.9026 1.0521 -0.0609 -0.0542 0.2918  262 ARG A O   
3116 C CB  . ARG B 76  ? 0.9536 0.8554 1.0590 -0.0678 -0.0144 0.2857  262 ARG A CB  
3117 C CG  . ARG B 76  ? 0.9126 0.8085 1.0303 -0.0701 -0.0017 0.2778  262 ARG A CG  
3118 C CD  . ARG B 76  ? 1.0229 0.8814 1.1339 -0.0722 0.0199  0.2788  262 ARG A CD  
3119 N NE  . ARG B 76  ? 1.0667 0.9235 1.1917 -0.0767 0.0319  0.2696  262 ARG A NE  
3120 C CZ  . ARG B 76  ? 1.0772 0.9123 1.1853 -0.0757 0.0349  0.2781  262 ARG A CZ  
3121 N NH1 . ARG B 76  ? 1.0794 0.8919 1.1558 -0.0705 0.0269  0.2963  262 ARG A NH1 
3122 N NH2 . ARG B 76  ? 1.0271 0.8629 1.1510 -0.0802 0.0462  0.2681  262 ARG A NH2 
3123 N N   . VAL B 77  ? 0.9243 0.8371 0.9832 -0.0550 -0.0576 0.3165  263 VAL A N   
3124 C CA  . VAL B 77  ? 0.8849 0.7922 0.9233 -0.0497 -0.0699 0.3295  263 VAL A CA  
3125 C C   . VAL B 77  ? 0.8750 0.8197 0.9199 -0.0478 -0.0918 0.3287  263 VAL A C   
3126 O O   . VAL B 77  ? 0.8844 0.8391 0.9291 -0.0459 -0.1002 0.3302  263 VAL A O   
3127 C CB  . VAL B 77  ? 0.8546 0.7262 0.8571 -0.0446 -0.0716 0.3493  263 VAL A CB  
3128 C CG1 . VAL B 77  ? 1.0581 0.9342 1.0507 -0.0430 -0.0814 0.3556  263 VAL A CG1 
3129 C CG2 . VAL B 77  ? 0.9076 0.7731 0.8889 -0.0389 -0.0841 0.3629  263 VAL A CG2 
3130 N N   . PHE B 78  ? 0.8830 0.8488 0.9336 -0.0485 -0.1014 0.3263  264 PHE A N   
3131 C CA  . PHE B 78  ? 0.9176 0.9208 0.9765 -0.0474 -0.1217 0.3242  264 PHE A CA  
3132 C C   . PHE B 78  ? 0.8599 0.8915 0.9501 -0.0517 -0.1193 0.3070  264 PHE A C   
3133 O O   . PHE B 78  ? 0.8376 0.8899 0.9305 -0.0500 -0.1331 0.3075  264 PHE A O   
3134 C CB  . PHE B 78  ? 0.9707 0.9912 1.0327 -0.0481 -0.1302 0.3229  264 PHE A CB  
3135 C CG  . PHE B 78  ? 1.0070 1.0099 1.0374 -0.0427 -0.1409 0.3414  264 PHE A CG  
3136 C CD1 . PHE B 78  ? 0.9755 0.9537 0.9776 -0.0373 -0.1457 0.3580  264 PHE A CD1 
3137 C CD2 . PHE B 78  ? 0.9435 0.9547 0.9728 -0.0431 -0.1464 0.3421  264 PHE A CD2 
3138 C CE1 . PHE B 78  ? 0.9697 0.9317 0.9429 -0.0323 -0.1557 0.3750  264 PHE A CE1 
3139 C CE2 . PHE B 78  ? 0.8835 0.8787 0.8842 -0.0382 -0.1562 0.3589  264 PHE A CE2 
3140 C CZ  . PHE B 78  ? 0.8798 0.8503 0.8524 -0.0328 -0.1609 0.3754  264 PHE A CZ  
3141 N N   . TYR B 79  ? 0.9188 0.9518 1.0329 -0.0573 -0.1021 0.2917  265 TYR A N   
3142 C CA  . TYR B 79  ? 0.9224 0.9806 1.0670 -0.0617 -0.0981 0.2748  265 TYR A CA  
3143 C C   . TYR B 79  ? 0.9164 0.9632 1.0566 -0.0601 -0.0951 0.2774  265 TYR A C   
3144 O O   . TYR B 79  ? 0.9363 1.0077 1.0892 -0.0603 -0.1046 0.2719  265 TYR A O   
3145 C CB  . TYR B 79  ? 0.9162 0.9725 1.0844 -0.0678 -0.0785 0.2593  265 TYR A CB  
3146 C CG  . TYR B 79  ? 0.9234 1.0051 1.1253 -0.0729 -0.0724 0.2404  265 TYR A CG  
3147 C CD1 . TYR B 79  ? 1.0016 1.0701 1.2113 -0.0746 -0.0585 0.2350  265 TYR A CD1 
3148 C CD2 . TYR B 79  ? 0.9775 1.0959 1.2037 -0.0762 -0.0799 0.2277  265 TYR A CD2 
3149 C CE1 . TYR B 79  ? 1.0068 1.0982 1.2477 -0.0793 -0.0527 0.2176  265 TYR A CE1 
3150 C CE2 . TYR B 79  ? 0.9973 1.1388 1.2546 -0.0809 -0.0743 0.2104  265 TYR A CE2 
3151 C CZ  . TYR B 79  ? 1.0231 1.1508 1.2876 -0.0824 -0.0607 0.2054  265 TYR A CZ  
3152 O OH  . TYR B 79  ? 0.9951 1.1456 1.2906 -0.0871 -0.0551 0.1881  265 TYR A OH  
3153 N N   . GLU B 80  ? 0.8478 0.8570 0.9696 -0.0585 -0.0823 0.2861  266 GLU A N   
3154 C CA  . GLU B 80  ? 0.8377 0.8338 0.9542 -0.0569 -0.0785 0.2890  266 GLU A CA  
3155 C C   . GLU B 80  ? 0.8056 0.8107 0.9045 -0.0514 -0.0992 0.3015  266 GLU A C   
3156 O O   . GLU B 80  ? 0.8656 0.8808 0.9717 -0.0510 -0.1028 0.2984  266 GLU A O   
3157 C CB  . GLU B 80  ? 0.8958 0.8488 0.9937 -0.0561 -0.0613 0.2971  266 GLU A CB  
3158 C CG  . GLU B 80  ? 1.0118 0.9532 1.1270 -0.0618 -0.0392 0.2847  266 GLU A CG  
3159 C CD  . GLU B 80  ? 0.9833 0.9382 1.1276 -0.0665 -0.0281 0.2678  266 GLU A CD  
3160 O OE1 . GLU B 80  ? 1.0127 0.9757 1.1585 -0.0650 -0.0342 0.2681  266 GLU A OE1 
3161 O OE2 . GLU B 80  ? 1.0069 0.9641 1.1726 -0.0718 -0.0131 0.2543  266 GLU A OE2 
3162 N N   . LEU B 81  ? 0.8892 0.8910 0.9652 -0.0470 -0.1132 0.3155  267 LEU A N   
3163 C CA  . LEU B 81  ? 0.8705 0.8809 0.9291 -0.0416 -0.1336 0.3278  267 LEU A CA  
3164 C C   . LEU B 81  ? 0.7798 0.8331 0.8593 -0.0430 -0.1494 0.3184  267 LEU A C   
3165 O O   . LEU B 81  ? 0.7581 0.8217 0.8281 -0.0392 -0.1654 0.3259  267 LEU A O   
3166 C CB  . LEU B 81  ? 0.7866 0.7823 0.8155 -0.0366 -0.1443 0.3452  267 LEU A CB  
3167 C CG  . LEU B 81  ? 0.8021 0.7543 0.8016 -0.0331 -0.1353 0.3602  267 LEU A CG  
3168 C CD1 . LEU B 81  ? 0.8896 0.8314 0.8629 -0.0286 -0.1467 0.3758  267 LEU A CD1 
3169 C CD2 . LEU B 81  ? 0.8636 0.8050 0.8514 -0.0296 -0.1382 0.3676  267 LEU A CD2 
3170 N N   . GLN B 82  ? 0.7453 0.8236 0.8527 -0.0482 -0.1455 0.3023  268 GLN A N   
3171 C CA  . GLN B 82  ? 0.8250 0.9445 0.9530 -0.0499 -0.1603 0.2928  268 GLN A CA  
3172 C C   . GLN B 82  ? 0.8508 0.9861 1.0061 -0.0539 -0.1532 0.2774  268 GLN A C   
3173 O O   . GLN B 82  ? 0.9604 1.1237 1.1260 -0.0537 -0.1673 0.2737  268 GLN A O   
3174 C CB  . GLN B 82  ? 0.8361 0.9771 0.9782 -0.0531 -0.1630 0.2847  268 GLN A CB  
3175 C CG  . GLN B 82  ? 0.7903 0.9748 0.9526 -0.0549 -0.1793 0.2754  268 GLN A CG  
3176 C CD  . GLN B 82  ? 0.7818 0.9848 0.9492 -0.0563 -0.1863 0.2727  268 GLN A CD  
3177 O OE1 . GLN B 82  ? 0.9137 1.0979 1.0621 -0.0542 -0.1853 0.2826  268 GLN A OE1 
3178 N NE2 . GLN B 82  ? 0.7952 1.0351 0.9881 -0.0600 -0.1936 0.2592  268 GLN A NE2 
3179 N N   . HIS B 83  ? 0.8023 0.9203 0.9694 -0.0575 -0.1321 0.2685  269 HIS A N   
3180 C CA  . HIS B 83  ? 0.8865 1.0195 1.0815 -0.0618 -0.1239 0.2526  269 HIS A CA  
3181 C C   . HIS B 83  ? 0.9248 1.0332 1.1117 -0.0604 -0.1140 0.2564  269 HIS A C   
3182 O O   . HIS B 83  ? 0.9255 1.0490 1.1273 -0.0615 -0.1163 0.2490  269 HIS A O   
3183 C CB  . HIS B 83  ? 0.9057 1.0434 1.1267 -0.0681 -0.1066 0.2361  269 HIS A CB  
3184 C CG  . HIS B 83  ? 0.9328 1.0985 1.1671 -0.0703 -0.1151 0.2292  269 HIS A CG  
3185 N ND1 . HIS B 83  ? 0.9169 1.0765 1.1332 -0.0679 -0.1220 0.2394  269 HIS A ND1 
3186 C CD2 . HIS B 83  ? 0.9508 1.1507 1.2149 -0.0749 -0.1177 0.2132  269 HIS A CD2 
3187 C CE1 . HIS B 83  ? 0.9343 1.1232 1.1686 -0.0709 -0.1284 0.2298  269 HIS A CE1 
3188 N NE2 . HIS B 83  ? 0.9014 1.1152 1.1647 -0.0751 -0.1260 0.2139  269 HIS A NE2 
3189 N N   . SER B 84  ? 0.8181 0.8353 0.9777 -0.0350 -0.0528 0.1891  270 SER A N   
3190 C CA  . SER B 84  ? 0.8465 0.8839 1.0137 -0.0309 -0.0406 0.2062  270 SER A CA  
3191 C C   . SER B 84  ? 0.9229 0.9632 1.0508 -0.0152 -0.0386 0.2065  270 SER A C   
3192 O O   . SER B 84  ? 0.9573 0.9770 1.0471 -0.0085 -0.0405 0.2017  270 SER A O   
3193 C CB  . SER B 84  ? 0.9349 0.9643 1.1084 -0.0354 -0.0273 0.2248  270 SER A CB  
3194 O OG  . SER B 84  ? 1.0708 1.1198 1.2450 -0.0294 -0.0147 0.2413  270 SER A OG  
3195 N N   . ASP B 85  ? 0.9456 1.0120 1.0848 -0.0096 -0.0345 0.2121  271 ASP A N   
3196 C CA  . ASP B 85  ? 0.9370 1.0084 1.0438 0.0058  -0.0303 0.2149  271 ASP A CA  
3197 C C   . ASP B 85  ? 0.9646 1.0402 1.0641 0.0098  -0.0146 0.2331  271 ASP A C   
3198 O O   . ASP B 85  ? 0.9298 1.0094 1.0028 0.0229  -0.0099 0.2359  271 ASP A O   
3199 C CB  . ASP B 85  ? 1.0806 1.1796 1.2025 0.0120  -0.0351 0.2096  271 ASP A CB  
3200 C CG  . ASP B 85  ? 1.1991 1.2993 1.3335 0.0078  -0.0512 0.1920  271 ASP A CG  
3201 O OD1 . ASP B 85  ? 1.2083 1.3197 1.3832 -0.0049 -0.0549 0.1893  271 ASP A OD1 
3202 O OD2 . ASP B 85  ? 1.1981 1.2872 1.3012 0.0173  -0.0603 0.1809  271 ASP A OD2 
3203 N N   . LYS B 86  ? 1.0697 1.1439 1.1916 -0.0006 -0.0066 0.2454  272 LYS A N   
3204 C CA  . LYS B 86  ? 1.0790 1.1581 1.1981 0.0017  0.0085  0.2645  272 LYS A CA  
3205 C C   . LYS B 86  ? 1.1459 1.1973 1.2419 0.0003  0.0099  0.2678  272 LYS A C   
3206 O O   . LYS B 86  ? 1.2561 1.2878 1.3544 -0.0074 0.0011  0.2581  272 LYS A O   
3207 C CB  . LYS B 86  ? 1.1178 1.2170 1.2841 -0.0098 0.0169  0.2780  272 LYS A CB  
3208 C CG  . LYS B 86  ? 1.1963 1.3288 1.3914 -0.0089 0.0185  0.2781  272 LYS A CG  
3209 C CD  . LYS B 86  ? 1.2917 1.4416 1.5362 -0.0228 0.0277  0.2923  272 LYS A CD  
3210 C CE  . LYS B 86  ? 1.3624 1.4955 1.6354 -0.0391 0.0181  0.2843  272 LYS A CE  
3211 N NZ  . LYS B 86  ? 1.3789 1.5151 1.6637 -0.0421 0.0009  0.2620  272 LYS A NZ  
3212 N N   . PRO B 87  ? 0.9938 1.0442 1.0671 0.0083  0.0205  0.2804  273 PRO A N   
3213 C CA  . PRO B 87  ? 0.9196 0.9460 0.9716 0.0078  0.0212  0.2833  273 PRO A CA  
3214 C C   . PRO B 87  ? 0.9256 0.9444 1.0089 -0.0056 0.0225  0.2913  273 PRO A C   
3215 O O   . PRO B 87  ? 0.9232 0.9580 1.0411 -0.0127 0.0295  0.3032  273 PRO A O   
3216 C CB  . PRO B 87  ? 0.8841 0.9187 0.9122 0.0194  0.0330  0.2968  273 PRO A CB  
3217 C CG  . PRO B 87  ? 0.9572 1.0110 0.9778 0.0294  0.0343  0.2926  273 PRO A CG  
3218 C CD  . PRO B 87  ? 1.0949 1.1649 1.1540 0.0208  0.0301  0.2885  273 PRO A CD  
3219 N N   . VAL B 88  ? 0.8509 0.8452 0.9231 -0.0089 0.0161  0.2846  274 VAL A N   
3220 C CA  . VAL B 88  ? 0.8369 0.8193 0.9383 -0.0213 0.0143  0.2873  274 VAL A CA  
3221 C C   . VAL B 88  ? 0.8707 0.8473 0.9697 -0.0201 0.0246  0.3068  274 VAL A C   
3222 O O   . VAL B 88  ? 0.8758 0.8479 0.9415 -0.0099 0.0279  0.3108  274 VAL A O   
3223 C CB  . VAL B 88  ? 0.8097 0.7698 0.9017 -0.0247 0.0012  0.2678  274 VAL A CB  
3224 C CG1 . VAL B 88  ? 0.8406 0.7860 0.9605 -0.0359 -0.0009 0.2695  274 VAL A CG1 
3225 C CG2 . VAL B 88  ? 0.7596 0.7268 0.8544 -0.0254 -0.0090 0.2501  274 VAL A CG2 
3226 N N   . GLY B 89  ? 0.8427 0.8194 0.9775 -0.0304 0.0294  0.3190  275 GLY A N   
3227 C CA  . GLY B 89  ? 0.8942 0.8635 1.0299 -0.0297 0.0387  0.3389  275 GLY A CA  
3228 C C   . GLY B 89  ? 0.9159 0.8585 1.0557 -0.0349 0.0315  0.3336  275 GLY A C   
3229 O O   . GLY B 89  ? 0.7989 0.7309 0.9549 -0.0430 0.0211  0.3172  275 GLY A O   
3230 N N   . THR B 90  ? 0.9448 0.8775 1.0690 -0.0290 0.0369  0.3474  276 THR A N   
3231 C CA  . THR B 90  ? 0.9115 0.8196 1.0357 -0.0311 0.0306  0.3434  276 THR A CA  
3232 C C   . THR B 90  ? 0.9366 0.8379 1.0789 -0.0330 0.0396  0.3670  276 THR A C   
3233 O O   . THR B 90  ? 0.9499 0.8335 1.0830 -0.0295 0.0369  0.3691  276 THR A O   
3234 C CB  . THR B 90  ? 0.9106 0.8103 0.9930 -0.0201 0.0251  0.3333  276 THR A CB  
3235 O OG1 . THR B 90  ? 1.0859 0.9968 1.1429 -0.0087 0.0341  0.3488  276 THR A OG1 
3236 C CG2 . THR B 90  ? 0.7957 0.6982 0.8606 -0.0187 0.0164  0.3107  276 THR A CG2 
3237 N N   . LYS B 91  ? 0.9845 0.8997 1.1528 -0.0382 0.0507  0.3853  277 LYS A N   
3238 C CA  . LYS B 91  ? 0.9531 0.8624 1.1362 -0.0391 0.0614  0.4113  277 LYS A CA  
3239 C C   . LYS B 91  ? 0.9729 0.8563 1.1846 -0.0487 0.0553  0.4086  277 LYS A C   
3240 O O   . LYS B 91  ? 1.0395 0.9065 1.2443 -0.0437 0.0567  0.4201  277 LYS A O   
3241 C CB  . LYS B 91  ? 0.9931 0.9239 1.2020 -0.0446 0.0752  0.4305  277 LYS A CB  
3242 C CG  . LYS B 91  ? 1.0232 0.9799 1.2033 -0.0327 0.0845  0.4389  277 LYS A CG  
3243 C CD  . LYS B 91  ? 1.0318 0.9860 1.1792 -0.0191 0.0918  0.4573  277 LYS A CD  
3244 C CE  . LYS B 91  ? 1.1174 1.0992 1.2437 -0.0083 0.1045  0.4707  277 LYS A CE  
3245 N NZ  . LYS B 91  ? 1.1946 1.1958 1.3564 -0.0170 0.1183  0.4881  277 LYS A NZ  
3246 N N   . LYS B 92  ? 0.9383 0.8177 1.1822 -0.0615 0.0478  0.3927  278 LYS A N   
3247 C CA  . LYS B 92  ? 1.0229 0.8771 1.2957 -0.0706 0.0414  0.3876  278 LYS A CA  
3248 C C   . LYS B 92  ? 0.9784 0.8129 1.2244 -0.0625 0.0310  0.3731  278 LYS A C   
3249 O O   . LYS B 92  ? 1.0007 0.8140 1.2559 -0.0623 0.0302  0.3796  278 LYS A O   
3250 C CB  . LYS B 92  ? 0.9958 0.8518 1.3054 -0.0849 0.0337  0.3695  278 LYS A CB  
3251 C CG  . LYS B 92  ? 0.9600 0.8295 1.3110 -0.0966 0.0442  0.3860  278 LYS A CG  
3252 C CD  . LYS B 92  ? 1.0724 0.9403 1.4650 -0.1118 0.0347  0.3669  278 LYS A CD  
3253 C CE  . LYS B 92  ? 1.0761 0.9600 1.5130 -0.1244 0.0455  0.3832  278 LYS A CE  
3254 N NZ  . LYS B 92  ? 1.0809 0.9647 1.5616 -0.1398 0.0352  0.3634  278 LYS A NZ  
3255 N N   . LEU B 93  ? 0.9273 0.7685 1.1410 -0.0557 0.0233  0.3537  279 LEU A N   
3256 C CA  . LEU B 93  ? 0.9527 0.7782 1.1414 -0.0485 0.0143  0.3395  279 LEU A CA  
3257 C C   . LEU B 93  ? 1.0023 0.8230 1.1688 -0.0370 0.0202  0.3578  279 LEU A C   
3258 O O   . LEU B 93  ? 0.9393 0.7420 1.1043 -0.0338 0.0154  0.3553  279 LEU A O   
3259 C CB  . LEU B 93  ? 0.9318 0.7668 1.0903 -0.0439 0.0070  0.3180  279 LEU A CB  
3260 C CG  . LEU B 93  ? 0.9554 0.7777 1.0870 -0.0371 -0.0016 0.3017  279 LEU A CG  
3261 C CD1 . LEU B 93  ? 0.9908 0.7917 1.1448 -0.0425 -0.0085 0.2923  279 LEU A CD1 
3262 C CD2 . LEU B 93  ? 0.8691 0.6998 0.9782 -0.0356 -0.0080 0.2810  279 LEU A CD2 
3263 N N   . THR B 94  ? 1.0653 0.9035 1.2141 -0.0298 0.0301  0.3756  280 THR A N   
3264 C CA  . THR B 94  ? 1.0031 0.8393 1.1307 -0.0181 0.0359  0.3947  280 THR A CA  
3265 C C   . THR B 94  ? 0.9699 0.7896 1.1259 -0.0217 0.0409  0.4145  280 THR A C   
3266 O O   . THR B 94  ? 0.9122 0.7174 1.0596 -0.0144 0.0381  0.4192  280 THR A O   
3267 C CB  . THR B 94  ? 1.0447 0.9046 1.1504 -0.0102 0.0464  0.4097  280 THR A CB  
3268 O OG1 . THR B 94  ? 1.0663 0.9370 1.1402 -0.0038 0.0408  0.3914  280 THR A OG1 
3269 C CG2 . THR B 94  ? 1.0563 0.9163 1.1457 0.0012  0.0541  0.4337  280 THR A CG2 
3270 N N   . LYS B 95  ? 1.0532 0.8744 1.2451 -0.0333 0.0479  0.4256  281 LYS A N   
3271 C CA  . LYS B 95  ? 1.0623 0.8641 1.2870 -0.0393 0.0523  0.4428  281 LYS A CA  
3272 C C   . LYS B 95  ? 1.0086 0.7847 1.2484 -0.0434 0.0398  0.4239  281 LYS A C   
3273 O O   . LYS B 95  ? 1.0037 0.7590 1.2565 -0.0417 0.0405  0.4356  281 LYS A O   
3274 C CB  . LYS B 95  ? 1.0284 0.8383 1.2926 -0.0534 0.0615  0.4541  281 LYS A CB  
3275 C CG  . LYS B 95  ? 1.0583 0.8459 1.3648 -0.0636 0.0656  0.4691  281 LYS A CG  
3276 C CD  . LYS B 95  ? 1.0358 0.8218 1.3383 -0.0568 0.0803  0.5048  281 LYS A CD  
3277 C CE  . LYS B 95  ? 1.0568 0.8313 1.4084 -0.0714 0.0897  0.5236  281 LYS A CE  
3278 N NZ  . LYS B 95  ? 1.0079 0.8042 1.3864 -0.0850 0.0944  0.5189  281 LYS A NZ  
3279 N N   . SER B 96  ? 1.0423 0.8195 1.2794 -0.0475 0.0285  0.3947  282 SER A N   
3280 C CA  . SER B 96  ? 0.9915 0.7466 1.2466 -0.0527 0.0172  0.3747  282 SER A CA  
3281 C C   . SER B 96  ? 1.0339 0.7738 1.2690 -0.0408 0.0126  0.3743  282 SER A C   
3282 O O   . SER B 96  ? 1.0818 0.7993 1.3383 -0.0419 0.0105  0.3776  282 SER A O   
3283 C CB  . SER B 96  ? 0.9688 0.7319 1.2190 -0.0576 0.0069  0.3447  282 SER A CB  
3284 O OG  . SER B 96  ? 1.0316 0.7759 1.3079 -0.0654 -0.0024 0.3264  282 SER A OG  
3285 N N   . PHE B 97  ? 1.0478 0.7996 1.2429 -0.0291 0.0108  0.3697  283 PHE A N   
3286 C CA  . PHE B 97  ? 1.0302 0.7722 1.2056 -0.0170 0.0064  0.3696  283 PHE A CA  
3287 C C   . PHE B 97  ? 1.0764 0.8238 1.2352 -0.0056 0.0152  0.3978  283 PHE A C   
3288 O O   . PHE B 97  ? 1.0830 0.8279 1.2204 0.0065  0.0115  0.3988  283 PHE A O   
3289 C CB  . PHE B 97  ? 0.9328 0.6831 1.0774 -0.0116 -0.0022 0.3453  283 PHE A CB  
3290 C CG  . PHE B 97  ? 0.8740 0.6471 0.9899 -0.0086 0.0012  0.3442  283 PHE A CG  
3291 C CD1 . PHE B 97  ? 0.8780 0.6632 0.9652 0.0031  0.0060  0.3585  283 PHE A CD1 
3292 C CD2 . PHE B 97  ? 0.9300 0.7120 1.0466 -0.0164 -0.0015 0.3275  283 PHE A CD2 
3293 C CE1 . PHE B 97  ? 0.8903 0.6949 0.9514 0.0064  0.0086  0.3557  283 PHE A CE1 
3294 C CE2 . PHE B 97  ? 0.9441 0.7452 1.0347 -0.0127 0.0013  0.3261  283 PHE A CE2 
3295 C CZ  . PHE B 97  ? 0.9507 0.7625 1.0139 -0.0015 0.0065  0.3398  283 PHE A CZ  
3296 N N   . GLY B 98  ? 1.0198 0.7764 1.1877 -0.0088 0.0267  0.4202  284 GLY A N   
3297 C CA  . GLY B 98  ? 1.0059 0.7649 1.1639 0.0010  0.0365  0.4506  284 GLY A CA  
3298 C C   . GLY B 98  ? 1.0415 0.8178 1.1554 0.0167  0.0368  0.4542  284 GLY A C   
3299 O O   . GLY B 98  ? 1.0042 0.7762 1.1047 0.0288  0.0379  0.4702  284 GLY A O   
3300 N N   . TRP B 99  ? 1.0620 0.8575 1.1533 0.0172  0.0351  0.4393  285 TRP A N   
3301 C CA  . TRP B 99  ? 1.0410 0.8551 1.0920 0.0311  0.0365  0.4429  285 TRP A CA  
3302 C C   . TRP B 99  ? 1.0482 0.8824 1.0940 0.0312  0.0492  0.4604  285 TRP A C   
3303 O O   . TRP B 99  ? 1.1374 0.9872 1.1725 0.0290  0.0497  0.4486  285 TRP A O   
3304 C CB  . TRP B 99  ? 1.0026 0.8228 1.0309 0.0325  0.0262  0.4141  285 TRP A CB  
3305 C CG  . TRP B 99  ? 0.9767 0.7827 1.0032 0.0353  0.0149  0.3977  285 TRP A CG  
3306 C CD1 . TRP B 99  ? 0.9189 0.7054 0.9662 0.0353  0.0117  0.4022  285 TRP A CD1 
3307 C CD2 . TRP B 99  ? 0.9796 0.7901 0.9830 0.0389  0.0058  0.3741  285 TRP A CD2 
3308 N NE1 . TRP B 99  ? 0.9990 0.7798 1.0375 0.0392  0.0012  0.3822  285 TRP A NE1 
3309 C CE2 . TRP B 99  ? 0.9570 0.7526 0.9691 0.0408  -0.0022 0.3652  285 TRP A CE2 
3310 C CE3 . TRP B 99  ? 0.9379 0.7631 0.9152 0.0405  0.0041  0.3600  285 TRP A CE3 
3311 C CZ2 . TRP B 99  ? 0.9554 0.7525 0.9520 0.0436  -0.0111 0.3431  285 TRP A CZ2 
3312 C CZ3 . TRP B 99  ? 0.9388 0.7630 0.9006 0.0428  -0.0049 0.3386  285 TRP A CZ3 
3313 C CH2 . TRP B 99  ? 0.9765 0.7878 0.9484 0.0439  -0.0120 0.3304  285 TRP A CH2 
3314 N N   . GLU B 100 ? 1.0387 0.8731 1.0903 0.0353  0.0601  0.4897  286 GLU A N   
3315 C CA  . GLU B 100 ? 1.1409 0.9951 1.1920 0.0346  0.0741  0.5080  286 GLU A CA  
3316 C C   . GLU B 100 ? 1.2003 1.0700 1.2172 0.0514  0.0818  0.5287  286 GLU A C   
3317 O O   . GLU B 100 ? 1.2127 1.1018 1.2244 0.0530  0.0942  0.5435  286 GLU A O   
3318 C CB  . GLU B 100 ? 1.1055 0.9507 1.1997 0.0215  0.0842  0.5269  286 GLU A CB  
3319 C CG  . GLU B 100 ? 1.0631 0.9010 1.1926 0.0039  0.0787  0.5071  286 GLU A CG  
3320 C CD  . GLU B 100 ? 1.1437 0.9647 1.3188 -0.0091 0.0848  0.5224  286 GLU A CD  
3321 O OE1 . GLU B 100 ? 1.1731 0.9730 1.3552 -0.0057 0.0844  0.5352  286 GLU A OE1 
3322 O OE2 . GLU B 100 ? 1.1234 0.9520 1.3282 -0.0226 0.0898  0.5215  286 GLU A OE2 
3323 N N   . THR B 101 ? 1.1978 1.0612 1.1916 0.0644  0.0749  0.5300  287 THR A N   
3324 C CA  . THR B 101 ? 1.1545 1.0350 1.1106 0.0821  0.0794  0.5447  287 THR A CA  
3325 C C   . THR B 101 ? 1.1867 1.0867 1.1099 0.0883  0.0740  0.5229  287 THR A C   
3326 O O   . THR B 101 ? 1.1273 1.0236 1.0533 0.0810  0.0643  0.4958  287 THR A O   
3327 C CB  . THR B 101 ? 1.2202 1.0885 1.1639 0.0946  0.0724  0.5524  287 THR A CB  
3328 O OG1 . THR B 101 ? 1.3537 1.2405 1.2545 0.1119  0.0689  0.5501  287 THR A OG1 
3329 C CG2 . THR B 101 ? 1.1561 1.0036 1.1161 0.0882  0.0579  0.5289  287 THR A CG2 
3330 N N   . LEU B 102 ? 1.1843 1.1049 1.0759 0.1022  0.0809  0.5353  288 LEU A N   
3331 C CA  . LEU B 102 ? 1.1841 1.1230 1.0444 0.1090  0.0766  0.5156  288 LEU A CA  
3332 C C   . LEU B 102 ? 1.1990 1.1305 1.0428 0.1128  0.0600  0.4893  288 LEU A C   
3333 O O   . LEU B 102 ? 1.2480 1.1855 1.0791 0.1110  0.0540  0.4659  288 LEU A O   
3334 C CB  . LEU B 102 ? 1.1823 1.1437 1.0092 0.1256  0.0857  0.5330  288 LEU A CB  
3335 C CG  . LEU B 102 ? 1.2095 1.1904 1.0387 0.1239  0.1011  0.5449  288 LEU A CG  
3336 C CD1 . LEU B 102 ? 1.1711 1.1738 0.9672 0.1400  0.1072  0.5513  288 LEU A CD1 
3337 C CD2 . LEU B 102 ? 1.1641 1.1512 0.9940 0.1166  0.0966  0.5181  288 LEU A CD2 
3338 N N   . ASP B 103 ? 1.1760 1.0946 1.0208 0.1179  0.0526  0.4930  289 ASP A N   
3339 C CA  . ASP B 103 ? 1.1167 1.0316 0.9464 0.1226  0.0376  0.4698  289 ASP A CA  
3340 C C   . ASP B 103 ? 1.0471 0.9408 0.9051 0.1098  0.0289  0.4531  289 ASP A C   
3341 O O   . ASP B 103 ? 1.1449 1.0347 0.9952 0.1127  0.0172  0.4349  289 ASP A O   
3342 C CB  . ASP B 103 ? 1.2833 1.2024 1.0916 0.1397  0.0336  0.4825  289 ASP A CB  
3343 C CG  . ASP B 103 ? 1.3352 1.2406 1.1636 0.1411  0.0398  0.5105  289 ASP A CG  
3344 O OD1 . ASP B 103 ? 1.3534 1.2433 1.2158 0.1271  0.0452  0.5162  289 ASP A OD1 
3345 O OD2 . ASP B 103 ? 1.2970 1.2067 1.1075 0.1565  0.0384  0.5262  289 ASP A OD2 
3346 N N   . SER B 104 ? 1.1179 0.9993 1.0089 0.0958  0.0344  0.4577  290 SER A N   
3347 C CA  . SER B 104 ? 1.0959 0.9568 1.0142 0.0848  0.0265  0.4428  290 SER A CA  
3348 C C   . SER B 104 ? 0.9813 0.8434 0.8902 0.0802  0.0165  0.4116  290 SER A C   
3349 O O   . SER B 104 ? 1.0474 0.8995 0.9596 0.0799  0.0067  0.3964  290 SER A O   
3350 C CB  . SER B 104 ? 1.1273 0.9772 1.0822 0.0703  0.0340  0.4516  290 SER A CB  
3351 O OG  . SER B 104 ? 1.1376 1.0016 1.0920 0.0642  0.0414  0.4505  290 SER A OG  
3352 N N   . PHE B 105 ? 1.0149 0.8893 0.9125 0.0767  0.0195  0.4024  291 PHE A N   
3353 C CA  . PHE B 105 ? 1.0496 0.9238 0.9377 0.0720  0.0114  0.3748  291 PHE A CA  
3354 C C   . PHE B 105 ? 1.0829 0.9669 0.9390 0.0832  0.0046  0.3638  291 PHE A C   
3355 O O   . PHE B 105 ? 1.1435 1.0229 0.9952 0.0800  -0.0039 0.3419  291 PHE A O   
3356 C CB  . PHE B 105 ? 0.9378 0.8201 0.8272 0.0648  0.0168  0.3697  291 PHE A CB  
3357 C CG  . PHE B 105 ? 1.0040 0.8760 0.9272 0.0510  0.0191  0.3699  291 PHE A CG  
3358 C CD1 . PHE B 105 ? 0.9486 0.8214 0.8939 0.0476  0.0286  0.3918  291 PHE A CD1 
3359 C CD2 . PHE B 105 ? 0.9675 0.8295 0.9011 0.0413  0.0118  0.3481  291 PHE A CD2 
3360 C CE1 . PHE B 105 ? 0.9488 0.8128 0.9276 0.0343  0.0298  0.3903  291 PHE A CE1 
3361 C CE2 . PHE B 105 ? 0.9336 0.7874 0.8979 0.0293  0.0126  0.3465  291 PHE A CE2 
3362 C CZ  . PHE B 105 ? 0.9264 0.7812 0.9144 0.0254  0.0211  0.3669  291 PHE A CZ  
3363 N N   . MET B 106 ? 1.0516 0.9495 0.8856 0.0962  0.0082  0.3782  292 MET A N   
3364 C CA  . MET B 106 ? 1.0436 0.9527 0.8473 0.1074  0.0011  0.3672  292 MET A CA  
3365 C C   . MET B 106 ? 1.1335 1.0372 0.9385 0.1132  -0.0084 0.3641  292 MET A C   
3366 O O   . MET B 106 ? 1.1111 1.0218 0.8981 0.1188  -0.0170 0.3481  292 MET A O   
3367 C CB  . MET B 106 ? 1.1270 1.0543 0.9061 0.1206  0.0080  0.3840  292 MET A CB  
3368 C CG  . MET B 106 ? 1.1322 1.0698 0.9027 0.1184  0.0158  0.3822  292 MET A CG  
3369 S SD  . MET B 106 ? 1.2084 1.1698 0.9452 0.1364  0.0231  0.3979  292 MET A SD  
3370 C CE  . MET B 106 ? 1.3519 1.3192 1.0596 0.1486  0.0088  0.3802  292 MET A CE  
3371 N N   . GLN B 107 ? 1.1568 1.0483 0.9844 0.1119  -0.0070 0.3786  293 GLN A N   
3372 C CA  . GLN B 107 ? 1.0799 0.9652 0.9125 0.1182  -0.0157 0.3770  293 GLN A CA  
3373 C C   . GLN B 107 ? 1.0395 0.9128 0.8891 0.1080  -0.0235 0.3535  293 GLN A C   
3374 O O   . GLN B 107 ? 1.1232 0.9979 0.9702 0.1135  -0.0326 0.3430  293 GLN A O   
3375 C CB  . GLN B 107 ? 1.0585 0.9331 0.9095 0.1214  -0.0103 0.4030  293 GLN A CB  
3376 C CG  . GLN B 107 ? 1.1483 1.0350 0.9791 0.1367  -0.0053 0.4279  293 GLN A CG  
3377 C CD  . GLN B 107 ? 1.2132 1.0867 1.0648 0.1368  0.0033  0.4562  293 GLN A CD  
3378 O OE1 . GLN B 107 ? 1.2463 1.1000 1.1285 0.1272  0.0028  0.4555  293 GLN A OE1 
3379 N NE2 . GLN B 107 ? 1.3251 1.2092 1.1602 0.1477  0.0118  0.4815  293 GLN A NE2 
3380 N N   . HIS B 108 ? 0.9445 0.8076 0.8118 0.0939  -0.0203 0.3452  294 HIS A N   
3381 C CA  . HIS B 108 ? 0.9551 0.8065 0.8389 0.0844  -0.0264 0.3244  294 HIS A CA  
3382 C C   . HIS B 108 ? 0.9625 0.8206 0.8300 0.0796  -0.0300 0.3012  294 HIS A C   
3383 O O   . HIS B 108 ? 0.9889 0.8597 0.8330 0.0841  -0.0287 0.3000  294 HIS A O   
3384 C CB  . HIS B 108 ? 0.9390 0.7748 0.8518 0.0725  -0.0219 0.3279  294 HIS A CB  
3385 C CG  . HIS B 108 ? 0.9732 0.7981 0.9061 0.0756  -0.0187 0.3492  294 HIS A CG  
3386 N ND1 . HIS B 108 ? 1.0530 0.8834 0.9810 0.0822  -0.0109 0.3748  294 HIS A ND1 
3387 C CD2 . HIS B 108 ? 1.0048 0.8130 0.9627 0.0735  -0.0219 0.3491  294 HIS A CD2 
3388 C CE1 . HIS B 108 ? 1.1168 0.9329 1.0665 0.0834  -0.0091 0.3906  294 HIS A CE1 
3389 N NE2 . HIS B 108 ? 1.0984 0.9002 1.0668 0.0783  -0.0162 0.3749  294 HIS A NE2 
3390 N N   . ASP B 109 ? 0.9111 0.7598 0.7913 0.0707  -0.0342 0.2827  295 ASP A N   
3391 C CA  . ASP B 109 ? 0.8536 0.7051 0.7219 0.0648  -0.0372 0.2608  295 ASP A CA  
3392 C C   . ASP B 109 ? 0.8774 0.7198 0.7562 0.0527  -0.0335 0.2542  295 ASP A C   
3393 O O   . ASP B 109 ? 0.9418 0.7750 0.8417 0.0478  -0.0306 0.2622  295 ASP A O   
3394 C CB  . ASP B 109 ? 0.9800 0.8300 0.8531 0.0649  -0.0446 0.2445  295 ASP A CB  
3395 C CG  . ASP B 109 ? 0.9950 0.8566 0.8583 0.0774  -0.0500 0.2486  295 ASP A CG  
3396 O OD1 . ASP B 109 ? 0.9998 0.8733 0.8423 0.0851  -0.0494 0.2556  295 ASP A OD1 
3397 O OD2 . ASP B 109 ? 1.0089 0.8686 0.8848 0.0804  -0.0552 0.2441  295 ASP A OD2 
3398 N N   . VAL B 110 ? 0.8533 0.6981 0.7175 0.0481  -0.0339 0.2392  296 VAL A N   
3399 C CA  . VAL B 110 ? 0.8385 0.6750 0.7113 0.0376  -0.0321 0.2305  296 VAL A CA  
3400 C C   . VAL B 110 ? 0.9312 0.7563 0.8245 0.0316  -0.0355 0.2208  296 VAL A C   
3401 O O   . VAL B 110 ? 0.9645 0.7815 0.8747 0.0247  -0.0342 0.2202  296 VAL A O   
3402 C CB  . VAL B 110 ? 0.8387 0.6779 0.6908 0.0349  -0.0323 0.2163  296 VAL A CB  
3403 C CG1 . VAL B 110 ? 0.9280 0.7765 0.7635 0.0400  -0.0281 0.2253  296 VAL A CG1 
3404 C CG2 . VAL B 110 ? 0.9260 0.7677 0.7666 0.0367  -0.0371 0.2026  296 VAL A CG2 
3405 N N   . GLN B 111 ? 0.9124 0.7380 0.8054 0.0347  -0.0401 0.2120  297 GLN A N   
3406 C CA  . GLN B 111 ? 0.9551 0.7715 0.8671 0.0306  -0.0431 0.2019  297 GLN A CA  
3407 C C   . GLN B 111 ? 0.9742 0.7814 0.9102 0.0314  -0.0424 0.2147  297 GLN A C   
3408 O O   . GLN B 111 ? 0.9367 0.7335 0.8904 0.0246  -0.0428 0.2085  297 GLN A O   
3409 C CB  . GLN B 111 ? 1.0032 0.8252 0.9120 0.0357  -0.0477 0.1926  297 GLN A CB  
3410 C CG  . GLN B 111 ? 0.9936 0.8250 0.8810 0.0350  -0.0485 0.1808  297 GLN A CG  
3411 C CD  . GLN B 111 ? 0.9515 0.7948 0.8224 0.0439  -0.0498 0.1901  297 GLN A CD  
3412 O OE1 . GLN B 111 ? 0.9452 0.7906 0.8072 0.0465  -0.0464 0.2025  297 GLN A OE1 
3413 N NE2 . GLN B 111 ? 1.0336 0.8864 0.9013 0.0493  -0.0547 0.1837  297 GLN A NE2 
3414 N N   . GLU B 112 ? 0.9671 0.7777 0.9039 0.0397  -0.0415 0.2327  298 GLU A N   
3415 C CA  . GLU B 112 ? 0.9703 0.7702 0.9307 0.0408  -0.0403 0.2468  298 GLU A CA  
3416 C C   . GLU B 112 ? 0.9297 0.7232 0.9038 0.0319  -0.0356 0.2528  298 GLU A C   
3417 O O   . GLU B 112 ? 0.9557 0.7361 0.9545 0.0268  -0.0362 0.2524  298 GLU A O   
3418 C CB  . GLU B 112 ? 1.0408 0.8463 0.9955 0.0523  -0.0393 0.2673  298 GLU A CB  
3419 C CG  . GLU B 112 ? 0.8387 0.6518 0.7836 0.0624  -0.0454 0.2621  298 GLU A CG  
3420 C CD  . GLU B 112 ? 0.9479 0.7643 0.8900 0.0749  -0.0452 0.2837  298 GLU A CD  
3421 O OE1 . GLU B 112 ? 0.9173 0.7435 0.8426 0.0793  -0.0410 0.2977  298 GLU A OE1 
3422 O OE2 . GLU B 112 ? 1.0394 0.8489 0.9957 0.0811  -0.0491 0.2872  298 GLU A OE2 
3423 N N   . LEU B 113 ? 0.9616 0.7645 0.9212 0.0302  -0.0311 0.2578  299 LEU A N   
3424 C CA  . LEU B 113 ? 1.0113 0.8114 0.9852 0.0218  -0.0269 0.2625  299 LEU A CA  
3425 C C   . LEU B 113 ? 0.8914 0.6840 0.8750 0.0124  -0.0308 0.2424  299 LEU A C   
3426 O O   . LEU B 113 ? 0.9283 0.7126 0.9360 0.0053  -0.0308 0.2425  299 LEU A O   
3427 C CB  . LEU B 113 ? 0.9505 0.7644 0.9060 0.0234  -0.0215 0.2702  299 LEU A CB  
3428 C CG  . LEU B 113 ? 0.8665 0.6808 0.8403 0.0156  -0.0167 0.2776  299 LEU A CG  
3429 C CD1 . LEU B 113 ? 0.8835 0.6901 0.8837 0.0146  -0.0131 0.2959  299 LEU A CD1 
3430 C CD2 . LEU B 113 ? 0.8673 0.6968 0.8236 0.0182  -0.0110 0.2845  299 LEU A CD2 
3431 N N   . CYS B 114 ? 0.8865 0.6821 0.8518 0.0121  -0.0341 0.2248  300 CYS A N   
3432 C CA  . CYS B 114 ? 0.9275 0.7167 0.8984 0.0045  -0.0375 0.2059  300 CYS A CA  
3433 C C   . CYS B 114 ? 0.9717 0.7488 0.9650 0.0032  -0.0414 0.1990  300 CYS A C   
3434 O O   . CYS B 114 ? 1.0292 0.7989 1.0377 -0.0034 -0.0438 0.1890  300 CYS A O   
3435 C CB  . CYS B 114 ? 0.8831 0.6774 0.8290 0.0050  -0.0389 0.1909  300 CYS A CB  
3436 S SG  . CYS B 114 ? 1.1563 0.9446 1.1024 -0.0030 -0.0418 0.1698  300 CYS A SG  
3437 N N   . ARG B 115 ? 0.9206 0.6960 0.9161 0.0103  -0.0429 0.2031  301 ARG A N   
3438 C CA  . ARG B 115 ? 0.9642 0.7275 0.9821 0.0107  -0.0465 0.1972  301 ARG A CA  
3439 C C   . ARG B 115 ? 0.9996 0.7515 1.0447 0.0071  -0.0453 0.2092  301 ARG A C   
3440 O O   . ARG B 115 ? 1.0635 0.8038 1.1292 0.0022  -0.0484 0.1988  301 ARG A O   
3441 C CB  . ARG B 115 ? 1.0468 0.8122 1.0618 0.0206  -0.0485 0.2010  301 ARG A CB  
3442 C CG  . ARG B 115 ? 1.1060 0.8806 1.1035 0.0230  -0.0508 0.1848  301 ARG A CG  
3443 C CD  . ARG B 115 ? 1.3299 1.1143 1.3169 0.0333  -0.0520 0.1946  301 ARG A CD  
3444 N NE  . ARG B 115 ? 1.3051 1.1008 1.2768 0.0351  -0.0541 0.1803  301 ARG A NE  
3445 C CZ  . ARG B 115 ? 1.2429 1.0509 1.2017 0.0428  -0.0559 0.1847  301 ARG A CZ  
3446 N NH1 . ARG B 115 ? 1.1283 0.9392 1.0841 0.0507  -0.0558 0.2035  301 ARG A NH1 
3447 N NH2 . ARG B 115 ? 1.2075 1.0256 1.1564 0.0426  -0.0579 0.1699  301 ARG A NH2 
3448 N N   . VAL B 116 ? 0.9699 0.7250 1.0158 0.0094  -0.0404 0.2310  302 VAL A N   
3449 C CA  . VAL B 116 ? 0.9299 0.6744 1.0035 0.0051  -0.0378 0.2450  302 VAL A CA  
3450 C C   . VAL B 116 ? 0.9682 0.7106 1.0561 -0.0064 -0.0386 0.2346  302 VAL A C   
3451 O O   . VAL B 116 ? 0.9902 0.7193 1.1061 -0.0122 -0.0408 0.2311  302 VAL A O   
3452 C CB  . VAL B 116 ? 1.0544 0.8062 1.1223 0.0098  -0.0308 0.2711  302 VAL A CB  
3453 C CG1 . VAL B 116 ? 1.0670 0.8112 1.1629 0.0023  -0.0260 0.2856  302 VAL A CG1 
3454 C CG2 . VAL B 116 ? 1.0868 0.8368 1.1480 0.0219  -0.0315 0.2827  302 VAL A CG2 
3455 N N   . LEU B 117 ? 0.9277 0.6832 0.9972 -0.0093 -0.0374 0.2288  303 LEU A N   
3456 C CA  . LEU B 117 ? 0.9577 0.7137 1.0392 -0.0189 -0.0392 0.2185  303 LEU A CA  
3457 C C   . LEU B 117 ? 1.0001 0.7473 1.0873 -0.0222 -0.0464 0.1945  303 LEU A C   
3458 O O   . LEU B 117 ? 1.0605 0.7988 1.1731 -0.0289 -0.0498 0.1875  303 LEU A O   
3459 C CB  . LEU B 117 ? 0.9102 0.6820 0.9685 -0.0192 -0.0366 0.2181  303 LEU A CB  
3460 C CG  . LEU B 117 ? 0.8024 0.5853 0.8542 -0.0156 -0.0289 0.2402  303 LEU A CG  
3461 C CD1 . LEU B 117 ? 0.7907 0.5880 0.8174 -0.0142 -0.0272 0.2363  303 LEU A CD1 
3462 C CD2 . LEU B 117 ? 0.8130 0.5939 0.8961 -0.0221 -0.0249 0.2545  303 LEU A CD2 
3463 N N   . LEU B 118 ? 0.9597 0.7097 1.0242 -0.0176 -0.0486 0.1814  304 LEU A N   
3464 C CA  . LEU B 118 ? 0.9225 0.6672 0.9880 -0.0201 -0.0541 0.1584  304 LEU A CA  
3465 C C   . LEU B 118 ? 0.9972 0.7270 1.0878 -0.0192 -0.0577 0.1531  304 LEU A C   
3466 O O   . LEU B 118 ? 1.0367 0.7596 1.1408 -0.0236 -0.0625 0.1367  304 LEU A O   
3467 C CB  . LEU B 118 ? 0.8312 0.5833 0.8672 -0.0158 -0.0539 0.1474  304 LEU A CB  
3468 C CG  . LEU B 118 ? 0.9211 0.6832 0.9330 -0.0183 -0.0528 0.1418  304 LEU A CG  
3469 C CD1 . LEU B 118 ? 0.8990 0.6689 0.9082 -0.0193 -0.0491 0.1579  304 LEU A CD1 
3470 C CD2 . LEU B 118 ? 0.9338 0.7013 0.9191 -0.0141 -0.0511 0.1355  304 LEU A CD2 
3471 N N   . ASP B 119 ? 1.0246 0.7493 1.1211 -0.0127 -0.0559 0.1660  305 ASP A N   
3472 C CA  . ASP B 119 ? 1.0174 0.7262 1.1390 -0.0107 -0.0592 0.1623  305 ASP A CA  
3473 C C   . ASP B 119 ? 1.0738 0.7704 1.2266 -0.0187 -0.0605 0.1657  305 ASP A C   
3474 O O   . ASP B 119 ? 1.1353 0.8188 1.3087 -0.0209 -0.0654 0.1515  305 ASP A O   
3475 C CB  . ASP B 119 ? 1.0843 0.7904 1.2058 -0.0009 -0.0572 0.1786  305 ASP A CB  
3476 C CG  . ASP B 119 ? 1.1170 0.8340 1.2147 0.0069  -0.0580 0.1704  305 ASP A CG  
3477 O OD1 . ASP B 119 ? 1.1516 0.8714 1.2422 0.0056  -0.0605 0.1495  305 ASP A OD1 
3478 O OD2 . ASP B 119 ? 1.0568 0.7807 1.1431 0.0143  -0.0559 0.1849  305 ASP A OD2 
3479 N N   . ASN B 120 ? 1.0712 0.7725 1.2291 -0.0232 -0.0558 0.1837  306 ASN A N   
3480 C CA  . ASN B 120 ? 0.9711 0.6631 1.1613 -0.0325 -0.0564 0.1872  306 ASN A CA  
3481 C C   . ASN B 120 ? 1.0615 0.7553 1.2572 -0.0401 -0.0629 0.1633  306 ASN A C   
3482 O O   . ASN B 120 ? 1.1624 0.8429 1.3857 -0.0454 -0.0679 0.1524  306 ASN A O   
3483 C CB  . ASN B 120 ? 0.8876 0.5892 1.0799 -0.0359 -0.0490 0.2104  306 ASN A CB  
3484 C CG  . ASN B 120 ? 0.9651 0.6575 1.1697 -0.0316 -0.0430 0.2358  306 ASN A CG  
3485 O OD1 . ASN B 120 ? 0.9954 0.6733 1.2322 -0.0372 -0.0421 0.2438  306 ASN A OD1 
3486 N ND2 . ASN B 120 ? 1.0358 0.7364 1.2150 -0.0215 -0.0391 0.2488  306 ASN A ND2 
3487 N N   . VAL B 121 ? 1.0643 0.7740 1.2335 -0.0403 -0.0632 0.1547  307 VAL A N   
3488 C CA  . VAL B 121 ? 0.9394 0.6530 1.1094 -0.0460 -0.0697 0.1330  307 VAL A CA  
3489 C C   . VAL B 121 ? 1.0676 0.7717 1.2369 -0.0429 -0.0757 0.1103  307 VAL A C   
3490 O O   . VAL B 121 ? 1.0145 0.7118 1.2027 -0.0477 -0.0823 0.0936  307 VAL A O   
3491 C CB  . VAL B 121 ? 0.9196 0.6511 1.0584 -0.0451 -0.0680 0.1314  307 VAL A CB  
3492 C CG1 . VAL B 121 ? 0.9853 0.7203 1.1165 -0.0475 -0.0750 0.1074  307 VAL A CG1 
3493 C CG2 . VAL B 121 ? 1.0376 0.7796 1.1829 -0.0492 -0.0632 0.1494  307 VAL A CG2 
3494 N N   . GLU B 122 ? 1.0770 0.7818 1.2257 -0.0346 -0.0736 0.1086  308 GLU A N   
3495 C CA  . GLU B 122 ? 1.0268 0.7253 1.1736 -0.0306 -0.0779 0.0874  308 GLU A CA  
3496 C C   . GLU B 122 ? 1.0585 0.7383 1.2392 -0.0312 -0.0820 0.0830  308 GLU A C   
3497 O O   . GLU B 122 ? 1.0461 0.7197 1.2359 -0.0321 -0.0880 0.0613  308 GLU A O   
3498 C CB  . GLU B 122 ? 1.0324 0.7366 1.1560 -0.0220 -0.0740 0.0897  308 GLU A CB  
3499 C CG  . GLU B 122 ? 1.1261 0.8263 1.2483 -0.0168 -0.0767 0.0695  308 GLU A CG  
3500 C CD  . GLU B 122 ? 1.2080 0.9153 1.3132 -0.0088 -0.0727 0.0737  308 GLU A CD  
3501 O OE1 . GLU B 122 ? 1.1993 0.9159 1.2883 -0.0078 -0.0684 0.0891  308 GLU A OE1 
3502 O OE2 . GLU B 122 ? 1.2351 0.9396 1.3440 -0.0032 -0.0740 0.0608  308 GLU A OE2 
3503 N N   . ASN B 123 ? 1.0768 0.7467 1.2761 -0.0302 -0.0788 0.1033  309 ASN A N   
3504 C CA  . ASN B 123 ? 1.1629 0.8119 1.3967 -0.0311 -0.0822 0.1015  309 ASN A CA  
3505 C C   . ASN B 123 ? 1.1238 0.7673 1.3840 -0.0423 -0.0867 0.0941  309 ASN A C   
3506 O O   . ASN B 123 ? 1.1514 0.7801 1.4352 -0.0443 -0.0930 0.0778  309 ASN A O   
3507 C CB  . ASN B 123 ? 1.1962 0.8358 1.4415 -0.0268 -0.0769 0.1281  309 ASN A CB  
3508 C CG  . ASN B 123 ? 1.3519 0.9675 1.6278 -0.0239 -0.0801 0.1259  309 ASN A CG  
3509 O OD1 . ASN B 123 ? 1.3430 0.9501 1.6277 -0.0226 -0.0862 0.1027  309 ASN A OD1 
3510 N ND2 . ASN B 123 ? 1.3908 0.9947 1.6830 -0.0223 -0.0757 0.1506  309 ASN A ND2 
3511 N N   . LYS B 124 ? 1.1233 0.7793 1.3809 -0.0496 -0.0841 0.1047  310 LYS A N   
3512 C CA  . LYS B 124 ? 1.0602 0.7146 1.3445 -0.0607 -0.0889 0.0971  310 LYS A CA  
3513 C C   . LYS B 124 ? 1.0517 0.7106 1.3288 -0.0618 -0.0980 0.0666  310 LYS A C   
3514 O O   . LYS B 124 ? 0.9820 0.6318 1.2864 -0.0681 -0.1053 0.0512  310 LYS A O   
3515 C CB  . LYS B 124 ? 1.0472 0.7179 1.3285 -0.0668 -0.0837 0.1147  310 LYS A CB  
3516 C CG  . LYS B 124 ? 1.0274 0.6970 1.3441 -0.0792 -0.0872 0.1123  310 LYS A CG  
3517 C CD  . LYS B 124 ? 0.9596 0.6080 1.3146 -0.0837 -0.0846 0.1261  310 LYS A CD  
3518 C CE  . LYS B 124 ? 1.0128 0.6593 1.4077 -0.0975 -0.0884 0.1218  310 LYS A CE  
3519 N NZ  . LYS B 124 ? 0.9501 0.5748 1.3833 -0.1029 -0.0840 0.1390  310 LYS A NZ  
3520 N N   . MET B 125 ? 1.0336 0.7063 1.2742 -0.0555 -0.0975 0.0574  311 MET A N   
3521 C CA  . MET B 125 ? 1.0089 0.6875 1.2367 -0.0549 -0.1049 0.0302  311 MET A CA  
3522 C C   . MET B 125 ? 1.0324 0.6977 1.2657 -0.0490 -0.1091 0.0105  311 MET A C   
3523 O O   . MET B 125 ? 0.9829 0.6516 1.2089 -0.0481 -0.1156 -0.0138 311 MET A O   
3524 C CB  . MET B 125 ? 0.9384 0.6351 1.1247 -0.0503 -0.1013 0.0301  311 MET A CB  
3525 C CG  . MET B 125 ? 1.0071 0.7177 1.1857 -0.0546 -0.0976 0.0472  311 MET A CG  
3526 S SD  . MET B 125 ? 0.9912 0.7192 1.1223 -0.0489 -0.0940 0.0458  311 MET A SD  
3527 C CE  . MET B 125 ? 1.0638 0.7852 1.1778 -0.0401 -0.0892 0.0437  311 MET A CE  
3528 N N   . LYS B 126 ? 1.0535 0.7048 1.2984 -0.0439 -0.1056 0.0201  312 LYS A N   
3529 C CA  . LYS B 126 ? 1.0865 0.7247 1.3403 -0.0375 -0.1096 0.0012  312 LYS A CA  
3530 C C   . LYS B 126 ? 1.0499 0.6746 1.3364 -0.0439 -0.1187 -0.0166 312 LYS A C   
3531 O O   . LYS B 126 ? 1.0582 0.6734 1.3746 -0.0524 -0.1197 -0.0055 312 LYS A O   
3532 C CB  . LYS B 126 ? 1.1610 0.7865 1.4241 -0.0302 -0.1047 0.0170  312 LYS A CB  
3533 C CG  . LYS B 126 ? 1.1593 0.7989 1.3908 -0.0225 -0.0975 0.0290  312 LYS A CG  
3534 C CD  . LYS B 126 ? 1.0830 0.7115 1.3250 -0.0144 -0.0941 0.0448  312 LYS A CD  
3535 C CE  . LYS B 126 ? 1.2065 0.8511 1.4186 -0.0072 -0.0881 0.0552  312 LYS A CE  
3536 N NZ  . LYS B 126 ? 1.2282 0.8646 1.4495 0.0018  -0.0858 0.0712  312 LYS A NZ  
3537 N N   . GLY B 127 ? 1.0761 0.7003 1.3571 -0.0399 -0.1251 -0.0448 313 GLY A N   
3538 C CA  . GLY B 127 ? 1.0586 0.6719 1.3674 -0.0452 -0.1351 -0.0664 313 GLY A CA  
3539 C C   . GLY B 127 ? 1.0303 0.6585 1.3352 -0.0533 -0.1415 -0.0767 313 GLY A C   
3540 O O   . GLY B 127 ? 0.9814 0.6021 1.3131 -0.0594 -0.1509 -0.0939 313 GLY A O   
3541 N N   . THR B 128 ? 1.0881 0.7370 1.3616 -0.0532 -0.1373 -0.0674 314 THR A N   
3542 C CA  . THR B 128 ? 1.0105 0.6759 1.2766 -0.0591 -0.1432 -0.0756 314 THR A CA  
3543 C C   . THR B 128 ? 1.0385 0.7194 1.2634 -0.0512 -0.1443 -0.0924 314 THR A C   
3544 O O   . THR B 128 ? 1.0631 0.7435 1.2659 -0.0425 -0.1389 -0.0953 314 THR A O   
3545 C CB  . THR B 128 ? 0.9697 0.6462 1.2343 -0.0653 -0.1372 -0.0492 314 THR A CB  
3546 O OG1 . THR B 128 ? 0.9543 0.6424 1.1803 -0.0585 -0.1285 -0.0364 314 THR A OG1 
3547 C CG2 . THR B 128 ? 0.9261 0.5875 1.2251 -0.0711 -0.1323 -0.0271 314 THR A CG2 
3548 N N   . CYS B 129 ? 1.0218 0.7176 1.2369 -0.0541 -0.1511 -0.1028 315 CYS A N   
3549 C CA  . CYS B 129 ? 1.0790 0.7897 1.2528 -0.0465 -0.1515 -0.1159 315 CYS A CA  
3550 C C   . CYS B 129 ? 1.0274 0.7475 1.1674 -0.0427 -0.1400 -0.0951 315 CYS A C   
3551 O O   . CYS B 129 ? 1.0664 0.7942 1.1721 -0.0355 -0.1367 -0.1024 315 CYS A O   
3552 C CB  . CYS B 129 ? 1.1006 0.8254 1.2714 -0.0496 -0.1621 -0.1300 315 CYS A CB  
3553 S SG  . CYS B 129 ? 0.9803 0.7202 1.1497 -0.0563 -0.1596 -0.1060 315 CYS A SG  
3554 N N   . VAL B 130 ? 0.9861 0.7055 1.1354 -0.0473 -0.1337 -0.0697 316 VAL A N   
3555 C CA  . VAL B 130 ? 0.9981 0.7263 1.1176 -0.0442 -0.1238 -0.0504 316 VAL A CA  
3556 C C   . VAL B 130 ? 1.0298 0.7485 1.1496 -0.0403 -0.1150 -0.0374 316 VAL A C   
3557 O O   . VAL B 130 ? 0.9334 0.6572 1.0363 -0.0389 -0.1069 -0.0189 316 VAL A O   
3558 C CB  . VAL B 130 ? 0.9052 0.6425 1.0297 -0.0502 -0.1228 -0.0321 316 VAL A CB  
3559 C CG1 . VAL B 130 ? 0.9427 0.6706 1.0990 -0.0557 -0.1186 -0.0122 316 VAL A CG1 
3560 C CG2 . VAL B 130 ? 1.0093 0.7587 1.0960 -0.0461 -0.1159 -0.0207 316 VAL A CG2 
3561 N N   . GLU B 131 ? 1.0066 0.7122 1.1449 -0.0377 -0.1170 -0.0482 317 GLU A N   
3562 C CA  . GLU B 131 ? 1.0577 0.7546 1.2000 -0.0330 -0.1101 -0.0370 317 GLU A CA  
3563 C C   . GLU B 131 ? 1.0780 0.7856 1.1850 -0.0264 -0.1025 -0.0353 317 GLU A C   
3564 O O   . GLU B 131 ? 1.0555 0.7714 1.1392 -0.0232 -0.1030 -0.0512 317 GLU A O   
3565 C CB  . GLU B 131 ? 1.1185 0.7998 1.2857 -0.0298 -0.1148 -0.0530 317 GLU A CB  
3566 C CG  . GLU B 131 ? 1.0062 0.6786 1.1795 -0.0231 -0.1090 -0.0437 317 GLU A CG  
3567 C CD  . GLU B 131 ? 1.0690 0.7259 1.2657 -0.0186 -0.1141 -0.0621 317 GLU A CD  
3568 O OE1 . GLU B 131 ? 1.0848 0.7276 1.3121 -0.0238 -0.1208 -0.0672 317 GLU A OE1 
3569 O OE2 . GLU B 131 ? 1.1442 0.8032 1.3298 -0.0098 -0.1113 -0.0722 317 GLU A OE2 
3570 N N   . GLY B 132 ? 1.0959 0.8035 1.1994 -0.0243 -0.0953 -0.0157 318 GLY A N   
3571 C CA  . GLY B 132 ? 0.9406 0.6580 1.0156 -0.0191 -0.0882 -0.0133 318 GLY A CA  
3572 C C   . GLY B 132 ? 0.9822 0.7124 1.0276 -0.0214 -0.0842 -0.0051 318 GLY A C   
3573 O O   . GLY B 132 ? 0.9756 0.7136 0.9961 -0.0181 -0.0786 -0.0070 318 GLY A O   
3574 N N   . THR B 133 ? 1.0790 0.8115 1.1274 -0.0268 -0.0867 0.0038  319 THR A N   
3575 C CA  . THR B 133 ? 0.9991 0.7426 1.0195 -0.0277 -0.0831 0.0116  319 THR A CA  
3576 C C   . THR B 133 ? 0.9186 0.6652 0.9272 -0.0256 -0.0754 0.0295  319 THR A C   
3577 O O   . THR B 133 ? 0.8945 0.6478 0.8758 -0.0238 -0.0706 0.0299  319 THR A O   
3578 C CB  . THR B 133 ? 0.8970 0.6440 0.9263 -0.0330 -0.0877 0.0170  319 THR A CB  
3579 O OG1 . THR B 133 ? 0.8340 0.5818 0.8672 -0.0343 -0.0957 -0.0024 319 THR A OG1 
3580 C CG2 . THR B 133 ? 0.8085 0.5653 0.8112 -0.0327 -0.0833 0.0285  319 THR A CG2 
3581 N N   . ILE B 134 ? 0.9775 0.7188 1.0060 -0.0257 -0.0742 0.0444  320 ILE A N   
3582 C CA  . ILE B 134 ? 0.9449 0.6904 0.9620 -0.0227 -0.0680 0.0605  320 ILE A CA  
3583 C C   . ILE B 134 ? 0.8853 0.6335 0.8890 -0.0179 -0.0646 0.0526  320 ILE A C   
3584 O O   . ILE B 134 ? 0.9166 0.6724 0.8972 -0.0170 -0.0599 0.0568  320 ILE A O   
3585 C CB  . ILE B 134 ? 0.9854 0.7249 1.0261 -0.0225 -0.0676 0.0781  320 ILE A CB  
3586 C CG1 . ILE B 134 ? 1.0123 0.7564 1.0551 -0.0267 -0.0666 0.0927  320 ILE A CG1 
3587 C CG2 . ILE B 134 ? 0.8962 0.6380 0.9297 -0.0165 -0.0633 0.0885  320 ILE A CG2 
3588 C CD1 . ILE B 134 ? 0.9490 0.6916 1.0076 -0.0329 -0.0720 0.0846  320 ILE A CD1 
3589 N N   . PRO B 135 ? 0.9754 0.7181 0.9930 -0.0147 -0.0665 0.0409  321 PRO A N   
3590 C CA  . PRO B 135 ? 0.9421 0.6908 0.9475 -0.0102 -0.0624 0.0328  321 PRO A CA  
3591 C C   . PRO B 135 ? 0.9367 0.6934 0.9146 -0.0119 -0.0590 0.0220  321 PRO A C   
3592 O O   . PRO B 135 ? 1.0418 0.8062 1.0034 -0.0109 -0.0534 0.0235  321 PRO A O   
3593 C CB  . PRO B 135 ? 0.8996 0.6405 0.9273 -0.0062 -0.0659 0.0199  321 PRO A CB  
3594 C CG  . PRO B 135 ? 0.9058 0.6347 0.9599 -0.0078 -0.0707 0.0289  321 PRO A CG  
3595 C CD  . PRO B 135 ? 1.0194 0.7503 1.0668 -0.0145 -0.0719 0.0354  321 PRO A CD  
3596 N N   . LYS B 136 ? 0.8501 0.6055 0.8225 -0.0146 -0.0622 0.0117  322 LYS A N   
3597 C CA  . LYS B 136 ? 0.8149 0.5771 0.7597 -0.0151 -0.0586 0.0023  322 LYS A CA  
3598 C C   . LYS B 136 ? 0.8842 0.6507 0.8064 -0.0177 -0.0547 0.0150  322 LYS A C   
3599 O O   . LYS B 136 ? 1.0256 0.7965 0.9235 -0.0180 -0.0498 0.0111  322 LYS A O   
3600 C CB  . LYS B 136 ? 0.8439 0.6042 0.7879 -0.0155 -0.0642 -0.0131 322 LYS A CB  
3601 C CG  . LYS B 136 ? 1.0125 0.7734 0.9502 -0.0191 -0.0686 -0.0074 322 LYS A CG  
3602 C CD  . LYS B 136 ? 1.0799 0.8405 1.0198 -0.0189 -0.0762 -0.0244 322 LYS A CD  
3603 C CE  . LYS B 136 ? 1.1643 0.9301 1.0791 -0.0150 -0.0732 -0.0397 322 LYS A CE  
3604 N NZ  . LYS B 136 ? 1.0880 0.8547 1.0035 -0.0137 -0.0818 -0.0571 322 LYS A NZ  
3605 N N   . LEU B 137 ? 0.8975 0.6625 0.8270 -0.0194 -0.0562 0.0305  323 LEU A N   
3606 C CA  . LEU B 137 ? 0.8777 0.6462 0.7870 -0.0208 -0.0529 0.0421  323 LEU A CA  
3607 C C   . LEU B 137 ? 0.9390 0.7105 0.8442 -0.0195 -0.0481 0.0529  323 LEU A C   
3608 O O   . LEU B 137 ? 0.9346 0.7091 0.8184 -0.0203 -0.0437 0.0563  323 LEU A O   
3609 C CB  . LEU B 137 ? 0.8922 0.6599 0.8103 -0.0228 -0.0572 0.0518  323 LEU A CB  
3610 C CG  . LEU B 137 ? 0.8912 0.6593 0.8078 -0.0244 -0.0627 0.0427  323 LEU A CG  
3611 C CD1 . LEU B 137 ? 0.8280 0.5975 0.7601 -0.0268 -0.0663 0.0536  323 LEU A CD1 
3612 C CD2 . LEU B 137 ? 0.9277 0.6989 0.8131 -0.0234 -0.0601 0.0383  323 LEU A CD2 
3613 N N   . PHE B 138 ? 0.9629 0.7335 0.8883 -0.0171 -0.0492 0.0581  324 PHE A N   
3614 C CA  . PHE B 138 ? 0.9264 0.7012 0.8497 -0.0148 -0.0466 0.0700  324 PHE A CA  
3615 C C   . PHE B 138 ? 0.9534 0.7319 0.8839 -0.0113 -0.0452 0.0648  324 PHE A C   
3616 O O   . PHE B 138 ? 1.0274 0.8120 0.9524 -0.0095 -0.0432 0.0715  324 PHE A O   
3617 C CB  . PHE B 138 ? 0.9031 0.6756 0.8420 -0.0134 -0.0492 0.0856  324 PHE A CB  
3618 C CG  . PHE B 138 ? 0.8710 0.6428 0.8063 -0.0165 -0.0502 0.0924  324 PHE A CG  
3619 C CD1 . PHE B 138 ? 0.8029 0.5795 0.7197 -0.0163 -0.0473 0.1016  324 PHE A CD1 
3620 C CD2 . PHE B 138 ? 0.8839 0.6509 0.8360 -0.0193 -0.0543 0.0887  324 PHE A CD2 
3621 C CE1 . PHE B 138 ? 0.8780 0.6559 0.7929 -0.0182 -0.0481 0.1075  324 PHE A CE1 
3622 C CE2 . PHE B 138 ? 0.8702 0.6393 0.8216 -0.0221 -0.0556 0.0944  324 PHE A CE2 
3623 C CZ  . PHE B 138 ? 0.9154 0.6904 0.8481 -0.0211 -0.0522 0.1042  324 PHE A CZ  
3624 N N   . ARG B 139 ? 0.9745 0.7508 0.9180 -0.0098 -0.0465 0.0524  325 ARG A N   
3625 C CA  . ARG B 139 ? 0.9186 0.6996 0.8728 -0.0053 -0.0456 0.0472  325 ARG A CA  
3626 C C   . ARG B 139 ? 0.8300 0.6198 0.7688 -0.0070 -0.0398 0.0355  325 ARG A C   
3627 O O   . ARG B 139 ? 0.8343 0.6232 0.7589 -0.0105 -0.0372 0.0269  325 ARG A O   
3628 C CB  . ARG B 139 ? 1.0556 0.8296 1.0333 -0.0017 -0.0497 0.0389  325 ARG A CB  
3629 C CG  . ARG B 139 ? 1.0692 0.8475 1.0620 0.0050  -0.0499 0.0360  325 ARG A CG  
3630 C CD  . ARG B 139 ? 1.1066 0.8763 1.1206 0.0087  -0.0535 0.0247  325 ARG A CD  
3631 N NE  . ARG B 139 ? 1.1193 0.8923 1.1235 0.0068  -0.0508 0.0063  325 ARG A NE  
3632 C CZ  . ARG B 139 ? 1.2624 1.0299 1.2796 0.0099  -0.0532 -0.0087 325 ARG A CZ  
3633 N NH1 . ARG B 139 ? 1.2778 1.0342 1.3203 0.0145  -0.0586 -0.0079 325 ARG A NH1 
3634 N NH2 . ARG B 139 ? 1.3470 1.1197 1.3508 0.0087  -0.0500 -0.0248 325 ARG A NH2 
3635 N N   . GLY B 140 ? 0.9272 0.7264 0.8694 -0.0045 -0.0378 0.0356  326 GLY A N   
3636 C CA  . GLY B 140 ? 0.9733 0.7824 0.9062 -0.0066 -0.0314 0.0248  326 GLY A CA  
3637 C C   . GLY B 140 ? 0.9481 0.7666 0.8999 -0.0010 -0.0315 0.0177  326 GLY A C   
3638 O O   . GLY B 140 ? 0.8871 0.7052 0.8558 0.0050  -0.0367 0.0241  326 GLY A O   
3639 N N   . LYS B 141 ? 0.9883 0.8158 0.9367 -0.0026 -0.0252 0.0048  327 LYS A N   
3640 C CA  . LYS B 141 ? 0.9699 0.8094 0.9364 0.0028  -0.0242 -0.0042 327 LYS A CA  
3641 C C   . LYS B 141 ? 0.9002 0.7548 0.8647 0.0003  -0.0207 -0.0023 327 LYS A C   
3642 O O   . LYS B 141 ? 0.9297 0.7865 0.8763 -0.0075 -0.0150 -0.0012 327 LYS A O   
3643 C CB  . LYS B 141 ? 0.9807 0.8238 0.9474 0.0034  -0.0187 -0.0207 327 LYS A CB  
3644 C CG  . LYS B 141 ? 1.0504 0.8802 1.0231 0.0071  -0.0234 -0.0268 327 LYS A CG  
3645 C CD  . LYS B 141 ? 1.2644 1.1004 1.2333 0.0084  -0.0173 -0.0445 327 LYS A CD  
3646 C CE  . LYS B 141 ? 1.2516 1.0751 1.2261 0.0123  -0.0227 -0.0539 327 LYS A CE  
3647 N NZ  . LYS B 141 ? 1.0564 0.8873 1.0238 0.0146  -0.0167 -0.0721 327 LYS A NZ  
3648 N N   . MET B 142 ? 0.9632 0.8279 0.9469 0.0070  -0.0247 -0.0020 328 MET A N   
3649 C CA  . MET B 142 ? 0.9145 0.7955 0.9005 0.0057  -0.0237 -0.0012 328 MET A CA  
3650 C C   . MET B 142 ? 0.9454 0.8420 0.9553 0.0136  -0.0249 -0.0104 328 MET A C   
3651 O O   . MET B 142 ? 0.9792 0.8701 1.0046 0.0227  -0.0302 -0.0106 328 MET A O   
3652 C CB  . MET B 142 ? 0.8339 0.7116 0.8154 0.0074  -0.0307 0.0136  328 MET A CB  
3653 C CG  . MET B 142 ? 0.8389 0.7338 0.8231 0.0070  -0.0320 0.0137  328 MET A CG  
3654 S SD  . MET B 142 ? 1.0221 0.9138 1.0008 0.0127  -0.0414 0.0305  328 MET A SD  
3655 C CE  . MET B 142 ? 0.9466 0.8210 0.8985 0.0038  -0.0378 0.0387  328 MET A CE  
3656 N N   . VAL B 143 ? 0.9253 0.8414 0.9400 0.0102  -0.0199 -0.0181 329 VAL A N   
3657 C CA  . VAL B 143 ? 0.8965 0.8317 0.9354 0.0178  -0.0208 -0.0276 329 VAL A CA  
3658 C C   . VAL B 143 ? 0.8627 0.8138 0.9093 0.0194  -0.0265 -0.0232 329 VAL A C   
3659 O O   . VAL B 143 ? 0.8522 0.8082 0.8873 0.0102  -0.0237 -0.0215 329 VAL A O   
3660 C CB  . VAL B 143 ? 0.8938 0.8431 0.9363 0.0131  -0.0094 -0.0427 329 VAL A CB  
3661 C CG1 . VAL B 143 ? 0.8661 0.8205 0.8922 -0.0006 -0.0006 -0.0426 329 VAL A CG1 
3662 C CG2 . VAL B 143 ? 0.8339 0.8062 0.9036 0.0214  -0.0104 -0.0526 329 VAL A CG2 
3663 N N   . SER B 144 ? 0.8641 0.8223 0.9298 0.0317  -0.0350 -0.0216 330 SER A N   
3664 C CA  . SER B 144 ? 0.8837 0.8604 0.9591 0.0361  -0.0420 -0.0193 330 SER A CA  
3665 C C   . SER B 144 ? 0.9049 0.9067 1.0054 0.0412  -0.0405 -0.0333 330 SER A C   
3666 O O   . SER B 144 ? 0.9223 0.9232 1.0382 0.0510  -0.0413 -0.0382 330 SER A O   
3667 C CB  . SER B 144 ? 0.8848 0.8519 0.9615 0.0479  -0.0535 -0.0048 330 SER A CB  
3668 O OG  . SER B 144 ? 1.0729 1.0591 1.1563 0.0534  -0.0613 -0.0028 330 SER A OG  
3669 N N   . TYR B 145 ? 0.8680 0.8925 0.9742 0.0346  -0.0381 -0.0403 331 TYR A N   
3670 C CA  . TYR B 145 ? 0.8738 0.9258 1.0051 0.0371  -0.0348 -0.0548 331 TYR A CA  
3671 C C   . TYR B 145 ? 0.8991 0.9752 1.0463 0.0432  -0.0450 -0.0556 331 TYR A C   
3672 O O   . TYR B 145 ? 0.9174 0.9928 1.0527 0.0392  -0.0507 -0.0487 331 TYR A O   
3673 C CB  . TYR B 145 ? 0.8491 0.9106 0.9775 0.0220  -0.0203 -0.0653 331 TYR A CB  
3674 C CG  . TYR B 145 ? 0.8619 0.9273 0.9789 0.0081  -0.0184 -0.0631 331 TYR A CG  
3675 C CD1 . TYR B 145 ? 0.9175 1.0105 1.0531 0.0050  -0.0204 -0.0708 331 TYR A CD1 
3676 C CD2 . TYR B 145 ? 0.8707 0.9124 0.9599 -0.0016 -0.0149 -0.0542 331 TYR A CD2 
3677 C CE1 . TYR B 145 ? 0.8711 0.9662 0.9980 -0.0079 -0.0191 -0.0702 331 TYR A CE1 
3678 C CE2 . TYR B 145 ? 0.9285 0.9717 1.0078 -0.0136 -0.0132 -0.0529 331 TYR A CE2 
3679 C CZ  . TYR B 145 ? 0.9059 0.9750 1.0043 -0.0170 -0.0153 -0.0612 331 TYR A CZ  
3680 O OH  . TYR B 145 ? 1.0110 1.0803 1.1013 -0.0293 -0.0142 -0.0613 331 TYR A OH  
3681 N N   . ILE B 146 ? 0.8413 0.9394 1.0154 0.0538  -0.0477 -0.0648 332 ILE A N   
3682 C CA  . ILE B 146 ? 0.8384 0.9656 1.0321 0.0601  -0.0571 -0.0692 332 ILE A CA  
3683 C C   . ILE B 146 ? 0.8501 1.0071 1.0704 0.0575  -0.0488 -0.0866 332 ILE A C   
3684 O O   . ILE B 146 ? 0.8560 1.0160 1.0912 0.0670  -0.0457 -0.0929 332 ILE A O   
3685 C CB  . ILE B 146 ? 0.8707 0.9960 1.0724 0.0802  -0.0715 -0.0604 332 ILE A CB  
3686 C CG1 . ILE B 146 ? 0.8462 0.9414 1.0217 0.0823  -0.0774 -0.0418 332 ILE A CG1 
3687 C CG2 . ILE B 146 ? 0.9236 1.0816 1.1446 0.0876  -0.0823 -0.0657 332 ILE A CG2 
3688 C CD1 . ILE B 146 ? 0.7838 0.8719 0.9647 0.1016  -0.0895 -0.0301 332 ILE A CD1 
3689 N N   . GLN B 147 ? 0.9303 1.1091 1.1576 0.0446  -0.0447 -0.0947 333 GLN A N   
3690 C CA  . GLN B 147 ? 0.9929 1.2013 1.2456 0.0389  -0.0343 -0.1107 333 GLN A CA  
3691 C C   . GLN B 147 ? 0.9887 1.2335 1.2692 0.0433  -0.0442 -0.1191 333 GLN A C   
3692 O O   . GLN B 147 ? 1.0082 1.2587 1.2840 0.0361  -0.0508 -0.1176 333 GLN A O   
3693 C CB  . GLN B 147 ? 1.0038 1.2073 1.2439 0.0176  -0.0182 -0.1137 333 GLN A CB  
3694 C CG  . GLN B 147 ? 0.9446 1.1807 1.2116 0.0096  -0.0058 -0.1289 333 GLN A CG  
3695 C CD  . GLN B 147 ? 1.0073 1.2491 1.2859 0.0188  0.0030  -0.1364 333 GLN A CD  
3696 O OE1 . GLN B 147 ? 1.0138 1.2333 1.2725 0.0161  0.0130  -0.1336 333 GLN A OE1 
3697 N NE2 . GLN B 147 ? 1.0327 1.3051 1.3437 0.0309  -0.0013 -0.1468 333 GLN A NE2 
3698 N N   . CYS B 148 ? 0.9305 1.2007 1.2406 0.0557  -0.0456 -0.1291 334 CYS A N   
3699 C CA  . CYS B 148 ? 0.8978 1.2074 1.2385 0.0604  -0.0546 -0.1394 334 CYS A CA  
3700 C C   . CYS B 148 ? 0.9646 1.2997 1.3214 0.0406  -0.0421 -0.1522 334 CYS A C   
3701 O O   . CYS B 148 ? 1.0662 1.3971 1.4205 0.0290  -0.0245 -0.1561 334 CYS A O   
3702 C CB  . CYS B 148 ? 0.8894 1.2182 1.2576 0.0808  -0.0594 -0.1462 334 CYS A CB  
3703 S SG  . CYS B 148 ? 0.7848 1.0855 1.1400 0.1055  -0.0751 -0.1307 334 CYS A SG  
3704 N N   . LYS B 149 ? 1.0188 1.3809 1.3925 0.0367  -0.0513 -0.1587 335 LYS A N   
3705 C CA  . LYS B 149 ? 1.0564 1.4412 1.4469 0.0159  -0.0404 -0.1702 335 LYS A CA  
3706 C C   . LYS B 149 ? 0.9921 1.4221 1.4262 0.0182  -0.0361 -0.1868 335 LYS A C   
3707 O O   . LYS B 149 ? 1.0108 1.4549 1.4587 0.0018  -0.0189 -0.1950 335 LYS A O   
3708 C CB  . LYS B 149 ? 1.0491 1.4369 1.4341 0.0070  -0.0520 -0.1699 335 LYS A CB  
3709 C CG  . LYS B 149 ? 1.1863 1.6044 1.5927 0.0220  -0.0727 -0.1760 335 LYS A CG  
3710 C CD  . LYS B 149 ? 1.2691 1.6894 1.6674 0.0132  -0.0842 -0.1773 335 LYS A CD  
3711 C CE  . LYS B 149 ? 1.2317 1.6844 1.6499 0.0300  -0.1060 -0.1839 335 LYS A CE  
3712 N NZ  . LYS B 149 ? 1.2110 1.6715 1.6249 0.0216  -0.1180 -0.1891 335 LYS A NZ  
3713 N N   . GLU B 150 ? 0.9433 1.3973 1.3999 0.0384  -0.0508 -0.1914 336 GLU A N   
3714 C CA  . GLU B 150 ? 1.0084 1.5089 1.5091 0.0424  -0.0484 -0.2079 336 GLU A CA  
3715 C C   . GLU B 150 ? 0.9111 1.4140 1.4223 0.0577  -0.0406 -0.2108 336 GLU A C   
3716 O O   . GLU B 150 ? 0.9593 1.4925 1.4995 0.0537  -0.0276 -0.2237 336 GLU A O   
3717 C CB  . GLU B 150 ? 1.0185 1.5499 1.5414 0.0553  -0.0706 -0.2137 336 GLU A CB  
3718 C CG  . GLU B 150 ? 1.0237 1.5549 1.5371 0.0407  -0.0794 -0.2135 336 GLU A CG  
3719 C CD  . GLU B 150 ? 1.0914 1.6496 1.6196 0.0558  -0.1035 -0.2181 336 GLU A CD  
3720 O OE1 . GLU B 150 ? 1.2102 1.7859 1.7551 0.0783  -0.1137 -0.2196 336 GLU A OE1 
3721 O OE2 . GLU B 150 ? 1.0882 1.6497 1.6105 0.0459  -0.1127 -0.2204 336 GLU A OE2 
3722 N N   . VAL B 151 ? 0.8977 1.3697 1.3871 0.0753  -0.0479 -0.1994 337 VAL A N   
3723 C CA  . VAL B 151 ? 0.8361 1.3029 1.3312 0.0894  -0.0405 -0.2021 337 VAL A CA  
3724 C C   . VAL B 151 ? 0.8678 1.2931 1.3278 0.0795  -0.0263 -0.1933 337 VAL A C   
3725 O O   . VAL B 151 ? 0.9105 1.3044 1.3386 0.0698  -0.0284 -0.1808 337 VAL A O   
3726 C CB  . VAL B 151 ? 0.8097 1.2718 1.3096 0.1170  -0.0589 -0.1968 337 VAL A CB  
3727 C CG1 . VAL B 151 ? 0.7819 1.2383 1.2905 0.1321  -0.0516 -0.2017 337 VAL A CG1 
3728 C CG2 . VAL B 151 ? 0.7793 1.2844 1.3124 0.1269  -0.0738 -0.2056 337 VAL A CG2 
3729 N N   . ASP B 152 ? 0.7916 1.2183 1.2575 0.0826  -0.0120 -0.2006 338 ASP A N   
3730 C CA  . ASP B 152 ? 0.8828 1.2769 1.3183 0.0726  0.0031  -0.1955 338 ASP A CA  
3731 C C   . ASP B 152 ? 0.9065 1.2625 1.3205 0.0887  -0.0052 -0.1860 338 ASP A C   
3732 O O   . ASP B 152 ? 0.8019 1.1541 1.2214 0.1008  -0.0005 -0.1923 338 ASP A O   
3733 C CB  . ASP B 152 ? 0.9423 1.3594 1.3934 0.0668  0.0237  -0.2091 338 ASP A CB  
3734 C CG  . ASP B 152 ? 1.0429 1.4322 1.4617 0.0526  0.0405  -0.2042 338 ASP A CG  
3735 O OD1 . ASP B 152 ? 1.0622 1.4125 1.4476 0.0499  0.0352  -0.1911 338 ASP A OD1 
3736 O OD2 . ASP B 152 ? 1.0307 1.4385 1.4575 0.0445  0.0593  -0.2133 338 ASP A OD2 
3737 N N   . TYR B 153 ? 0.8827 1.2102 1.2728 0.0885  -0.0178 -0.1709 339 TYR A N   
3738 C CA  . TYR B 153 ? 0.7854 1.0734 1.1532 0.0998  -0.0249 -0.1594 339 TYR A CA  
3739 C C   . TYR B 153 ? 0.7868 1.0418 1.1186 0.0856  -0.0247 -0.1450 339 TYR A C   
3740 O O   . TYR B 153 ? 0.7876 1.0485 1.1135 0.0749  -0.0287 -0.1404 339 TYR A O   
3741 C CB  . TYR B 153 ? 0.7993 1.0872 1.1794 0.1214  -0.0439 -0.1534 339 TYR A CB  
3742 C CG  . TYR B 153 ? 0.7962 1.0421 1.1553 0.1317  -0.0506 -0.1401 339 TYR A CG  
3743 C CD1 . TYR B 153 ? 0.8068 1.0391 1.1716 0.1435  -0.0469 -0.1456 339 TYR A CD1 
3744 C CD2 . TYR B 153 ? 0.7941 1.0142 1.1285 0.1290  -0.0600 -0.1227 339 TYR A CD2 
3745 C CE1 . TYR B 153 ? 0.8200 1.0135 1.1686 0.1514  -0.0529 -0.1341 339 TYR A CE1 
3746 C CE2 . TYR B 153 ? 0.8018 0.9847 1.1196 0.1370  -0.0650 -0.1101 339 TYR A CE2 
3747 C CZ  . TYR B 153 ? 0.8685 1.0378 1.1945 0.1476  -0.0616 -0.1159 339 TYR A CZ  
3748 O OH  . TYR B 153 ? 0.9412 1.0731 1.2538 0.1544  -0.0666 -0.1041 339 TYR A OH  
3749 N N   . ARG B 154 ? 0.8927 1.1134 1.2016 0.0862  -0.0208 -0.1389 340 ARG A N   
3750 C CA  . ARG B 154 ? 0.8470 1.0352 1.1221 0.0746  -0.0206 -0.1253 340 ARG A CA  
3751 C C   . ARG B 154 ? 0.7850 0.9384 1.0461 0.0857  -0.0271 -0.1160 340 ARG A C   
3752 O O   . ARG B 154 ? 0.7938 0.9431 1.0652 0.0968  -0.0252 -0.1232 340 ARG A O   
3753 C CB  . ARG B 154 ? 0.8414 1.0259 1.0999 0.0560  -0.0033 -0.1294 340 ARG A CB  
3754 C CG  . ARG B 154 ? 0.9204 1.0740 1.1450 0.0438  -0.0030 -0.1160 340 ARG A CG  
3755 C CD  . ARG B 154 ? 0.9496 1.0976 1.1570 0.0285  0.0141  -0.1195 340 ARG A CD  
3756 N NE  . ARG B 154 ? 1.0155 1.1354 1.1914 0.0176  0.0140  -0.1070 340 ARG A NE  
3757 C CZ  . ARG B 154 ? 1.0044 1.1262 1.1711 0.0035  0.0164  -0.1026 340 ARG A CZ  
3758 N NH1 . ARG B 154 ? 0.8461 0.9963 1.0332 -0.0031 0.0190  -0.1099 340 ARG A NH1 
3759 N NH2 . ARG B 154 ? 1.0620 1.1568 1.2000 -0.0042 0.0159  -0.0913 340 ARG A NH2 
3760 N N   . SER B 155 ? 0.8429 0.9716 1.0817 0.0825  -0.0347 -0.1004 341 SER A N   
3761 C CA  . SER B 155 ? 0.8842 0.9791 1.1101 0.0907  -0.0409 -0.0894 341 SER A CA  
3762 C C   . SER B 155 ? 0.8239 0.8928 1.0187 0.0761  -0.0357 -0.0804 341 SER A C   
3763 O O   . SER B 155 ? 0.7859 0.8520 0.9660 0.0680  -0.0389 -0.0707 341 SER A O   
3764 C CB  . SER B 155 ? 0.8057 0.8970 1.0376 0.1047  -0.0566 -0.0768 341 SER A CB  
3765 O OG  . SER B 155 ? 0.9460 1.0042 1.1677 0.1114  -0.0614 -0.0652 341 SER A OG  
3766 N N   . ASP B 156 ? 0.8729 0.9241 1.0578 0.0734  -0.0279 -0.0847 342 ASP A N   
3767 C CA  . ASP B 156 ? 0.8376 0.8637 0.9941 0.0616  -0.0237 -0.0770 342 ASP A CA  
3768 C C   . ASP B 156 ? 0.8935 0.8903 1.0457 0.0699  -0.0310 -0.0689 342 ASP A C   
3769 O O   . ASP B 156 ? 0.9445 0.9356 1.1087 0.0790  -0.0308 -0.0774 342 ASP A O   
3770 C CB  . ASP B 156 ? 0.7943 0.8240 0.9408 0.0512  -0.0091 -0.0884 342 ASP A CB  
3771 C CG  . ASP B 156 ? 0.9144 0.9669 1.0600 0.0386  -0.0003 -0.0923 342 ASP A CG  
3772 O OD1 . ASP B 156 ? 0.9526 1.0096 1.0958 0.0337  -0.0057 -0.0843 342 ASP A OD1 
3773 O OD2 . ASP B 156 ? 1.0006 1.0670 1.1488 0.0336  0.0124  -0.1037 342 ASP A OD2 
3774 N N   . ARG B 157 ? 0.8923 0.8708 1.0286 0.0667  -0.0373 -0.0530 343 ARG A N   
3775 C CA  . ARG B 157 ? 0.9297 0.8797 1.0616 0.0717  -0.0431 -0.0435 343 ARG A CA  
3776 C C   . ARG B 157 ? 0.9586 0.8909 1.0641 0.0590  -0.0401 -0.0348 343 ARG A C   
3777 O O   . ARG B 157 ? 0.9617 0.9001 1.0531 0.0506  -0.0390 -0.0283 343 ARG A O   
3778 C CB  . ARG B 157 ? 0.9149 0.8600 1.0574 0.0837  -0.0549 -0.0295 343 ARG A CB  
3779 C CG  . ARG B 157 ? 0.8929 0.8476 1.0246 0.0805  -0.0593 -0.0176 343 ARG A CG  
3780 C CD  . ARG B 157 ? 0.9623 0.9163 1.1049 0.0949  -0.0707 -0.0049 343 ARG A CD  
3781 N NE  . ARG B 157 ? 1.0849 1.0457 1.2135 0.0927  -0.0756 0.0071  343 ARG A NE  
3782 C CZ  . ARG B 157 ? 1.1215 1.0644 1.2313 0.0887  -0.0771 0.0225  343 ARG A CZ  
3783 N NH1 . ARG B 157 ? 1.0895 1.0071 1.1934 0.0854  -0.0743 0.0281  343 ARG A NH1 
3784 N NH2 . ARG B 157 ? 1.1979 1.1497 1.2950 0.0881  -0.0815 0.0315  343 ARG A NH2 
3785 N N   . ARG B 158 ? 1.0071 0.9182 1.1067 0.0579  -0.0391 -0.0357 344 ARG A N   
3786 C CA  . ARG B 158 ? 1.0222 0.9169 1.0985 0.0473  -0.0372 -0.0277 344 ARG A CA  
3787 C C   . ARG B 158 ? 1.0112 0.8889 1.0862 0.0504  -0.0457 -0.0097 344 ARG A C   
3788 O O   . ARG B 158 ? 1.1021 0.9692 1.1934 0.0600  -0.0520 -0.0057 344 ARG A O   
3789 C CB  . ARG B 158 ? 1.1181 1.0009 1.1878 0.0440  -0.0324 -0.0385 344 ARG A CB  
3790 C CG  . ARG B 158 ? 1.0689 0.9353 1.1159 0.0343  -0.0317 -0.0304 344 ARG A CG  
3791 C CD  . ARG B 158 ? 1.2300 1.0884 1.2683 0.0313  -0.0273 -0.0428 344 ARG A CD  
3792 N NE  . ARG B 158 ? 1.3361 1.1819 1.3914 0.0394  -0.0326 -0.0499 344 ARG A NE  
3793 C CZ  . ARG B 158 ? 1.2581 1.0841 1.3188 0.0404  -0.0399 -0.0417 344 ARG A CZ  
3794 N NH1 . ARG B 158 ? 1.1848 1.0026 1.2349 0.0346  -0.0426 -0.0255 344 ARG A NH1 
3795 N NH2 . ARG B 158 ? 1.2542 1.0682 1.3322 0.0471  -0.0443 -0.0506 344 ARG A NH2 
3796 N N   . GLU B 159 ? 0.9585 0.8331 1.0142 0.0423  -0.0453 0.0014  345 GLU A N   
3797 C CA  . GLU B 159 ? 1.0164 0.8758 1.0672 0.0436  -0.0512 0.0189  345 GLU A CA  
3798 C C   . GLU B 159 ? 1.0066 0.8517 1.0389 0.0336  -0.0478 0.0217  345 GLU A C   
3799 O O   . GLU B 159 ? 1.0257 0.8754 1.0434 0.0253  -0.0413 0.0134  345 GLU A O   
3800 C CB  . GLU B 159 ? 0.9619 0.8323 1.0062 0.0452  -0.0548 0.0308  345 GLU A CB  
3801 C CG  . GLU B 159 ? 0.9866 0.8724 1.0482 0.0564  -0.0603 0.0302  345 GLU A CG  
3802 C CD  . GLU B 159 ? 1.1334 1.0270 1.1869 0.0599  -0.0659 0.0438  345 GLU A CD  
3803 O OE1 . GLU B 159 ? 1.1416 1.0218 1.1828 0.0587  -0.0675 0.0585  345 GLU A OE1 
3804 O OE2 . GLU B 159 ? 1.1795 1.0938 1.2390 0.0640  -0.0688 0.0392  345 GLU A OE2 
3805 N N   . ASP B 160 ? 0.8816 0.7101 0.9156 0.0347  -0.0520 0.0338  346 ASP A N   
3806 C CA  . ASP B 160 ? 0.9552 0.7718 0.9739 0.0263  -0.0501 0.0380  346 ASP A CA  
3807 C C   . ASP B 160 ? 0.9347 0.7506 0.9413 0.0248  -0.0519 0.0556  346 ASP A C   
3808 O O   . ASP B 160 ? 0.9035 0.7215 0.9175 0.0319  -0.0561 0.0672  346 ASP A O   
3809 C CB  . ASP B 160 ? 1.0778 0.8768 1.1094 0.0272  -0.0530 0.0364  346 ASP A CB  
3810 C CG  . ASP B 160 ? 1.0662 0.8653 1.1025 0.0270  -0.0505 0.0165  346 ASP A CG  
3811 O OD1 . ASP B 160 ? 1.0883 0.9001 1.1124 0.0236  -0.0447 0.0060  346 ASP A OD1 
3812 O OD2 . ASP B 160 ? 1.0873 0.8736 1.1393 0.0300  -0.0540 0.0113  346 ASP A OD2 
3813 N N   . TYR B 161 ? 0.8379 0.6514 0.8249 0.0166  -0.0485 0.0574  347 TYR A N   
3814 C CA  . TYR B 161 ? 0.8164 0.6297 0.7900 0.0152  -0.0493 0.0723  347 TYR A CA  
3815 C C   . TYR B 161 ? 0.9091 0.7116 0.8723 0.0086  -0.0478 0.0757  347 TYR A C   
3816 O O   . TYR B 161 ? 0.9913 0.7904 0.9490 0.0035  -0.0452 0.0645  347 TYR A O   
3817 C CB  . TYR B 161 ? 0.8752 0.7021 0.8331 0.0128  -0.0469 0.0702  347 TYR A CB  
3818 C CG  . TYR B 161 ? 0.8862 0.7143 0.8288 0.0041  -0.0407 0.0589  347 TYR A CG  
3819 C CD1 . TYR B 161 ? 0.8960 0.7313 0.8438 0.0025  -0.0368 0.0443  347 TYR A CD1 
3820 C CD2 . TYR B 161 ? 0.8701 0.6926 0.7929 -0.0018 -0.0382 0.0636  347 TYR A CD2 
3821 C CE1 . TYR B 161 ? 0.8798 0.7157 0.8124 -0.0052 -0.0301 0.0359  347 TYR A CE1 
3822 C CE2 . TYR B 161 ? 0.8530 0.6749 0.7607 -0.0089 -0.0324 0.0550  347 TYR A CE2 
3823 C CZ  . TYR B 161 ? 0.8776 0.7058 0.7897 -0.0108 -0.0281 0.0418  347 TYR A CZ  
3824 O OH  . TYR B 161 ? 0.8883 0.7155 0.7842 -0.0177 -0.0212 0.0350  347 TYR A OH  
3825 N N   . TYR B 162 ? 0.9703 0.7686 0.9308 0.0095  -0.0494 0.0912  348 TYR A N   
3826 C CA  . TYR B 162 ? 0.8609 0.6527 0.8111 0.0038  -0.0480 0.0959  348 TYR A CA  
3827 C C   . TYR B 162 ? 0.8142 0.6120 0.7426 0.0021  -0.0457 0.1027  348 TYR A C   
3828 O O   . TYR B 162 ? 0.9338 0.7279 0.8511 -0.0021 -0.0441 0.1050  348 TYR A O   
3829 C CB  . TYR B 162 ? 0.8692 0.6517 0.8358 0.0053  -0.0507 0.1082  348 TYR A CB  
3830 C CG  . TYR B 162 ? 0.9288 0.7013 0.9157 0.0045  -0.0532 0.0991  348 TYR A CG  
3831 C CD1 . TYR B 162 ? 0.9475 0.7145 0.9334 -0.0015 -0.0534 0.0902  348 TYR A CD1 
3832 C CD2 . TYR B 162 ? 0.9385 0.7071 0.9454 0.0106  -0.0559 0.0985  348 TYR A CD2 
3833 C CE1 . TYR B 162 ? 1.0356 0.7938 1.0398 -0.0020 -0.0565 0.0797  348 TYR A CE1 
3834 C CE2 . TYR B 162 ? 1.0575 0.8156 1.0835 0.0103  -0.0584 0.0886  348 TYR A CE2 
3835 C CZ  . TYR B 162 ? 1.1199 0.8729 1.1444 0.0037  -0.0588 0.0786  348 TYR A CZ  
3836 O OH  . TYR B 162 ? 1.2323 0.9750 1.2757 0.0037  -0.0622 0.0667  348 TYR A OH  
3837 N N   . ASP B 163 ? 0.7968 0.6042 0.7194 0.0058  -0.0460 0.1048  349 ASP A N   
3838 C CA  . ASP B 163 ? 0.8012 0.6140 0.7038 0.0050  -0.0445 0.1097  349 ASP A CA  
3839 C C   . ASP B 163 ? 0.8107 0.6351 0.7103 0.0071  -0.0453 0.1034  349 ASP A C   
3840 O O   . ASP B 163 ? 0.7936 0.6236 0.7080 0.0114  -0.0478 0.0997  349 ASP A O   
3841 C CB  . ASP B 163 ? 0.8480 0.6604 0.7492 0.0096  -0.0458 0.1268  349 ASP A CB  
3842 C CG  . ASP B 163 ? 0.9787 0.7919 0.8974 0.0171  -0.0492 0.1364  349 ASP A CG  
3843 O OD1 . ASP B 163 ? 1.0521 0.8628 0.9874 0.0183  -0.0510 0.1295  349 ASP A OD1 
3844 O OD2 . ASP B 163 ? 1.0445 0.8605 0.9603 0.0224  -0.0497 0.1512  349 ASP A OD2 
3845 N N   . ILE B 164 ? 0.7710 0.5991 0.6526 0.0041  -0.0434 0.1014  350 ILE A N   
3846 C CA  . ILE B 164 ? 0.7521 0.5916 0.6308 0.0040  -0.0442 0.0936  350 ILE A CA  
3847 C C   . ILE B 164 ? 0.8191 0.6642 0.6847 0.0084  -0.0469 0.1014  350 ILE A C   
3848 O O   . ILE B 164 ? 0.9020 0.7413 0.7513 0.0060  -0.0447 0.1049  350 ILE A O   
3849 C CB  . ILE B 164 ? 0.7506 0.5883 0.6207 -0.0051 -0.0387 0.0808  350 ILE A CB  
3850 C CG1 . ILE B 164 ? 0.8012 0.6359 0.6828 -0.0080 -0.0357 0.0721  350 ILE A CG1 
3851 C CG2 . ILE B 164 ? 0.8851 0.7348 0.7541 -0.0066 -0.0393 0.0730  350 ILE A CG2 
3852 C CD1 . ILE B 164 ? 0.9353 0.7811 0.8370 -0.0035 -0.0381 0.0660  350 ILE A CD1 
3853 N N   . GLN B 165 ? 0.8514 0.7085 0.7234 0.0157  -0.0521 0.1035  351 GLN A N   
3854 C CA  . GLN B 165 ? 0.7881 0.6533 0.6469 0.0213  -0.0557 0.1089  351 GLN A CA  
3855 C C   . GLN B 165 ? 0.8820 0.7562 0.7357 0.0167  -0.0566 0.0949  351 GLN A C   
3856 O O   . GLN B 165 ? 0.9089 0.7938 0.7763 0.0168  -0.0591 0.0859  351 GLN A O   
3857 C CB  . GLN B 165 ? 0.7696 0.6436 0.6366 0.0330  -0.0616 0.1197  351 GLN A CB  
3858 C CG  . GLN B 165 ? 0.8547 0.7191 0.7286 0.0373  -0.0603 0.1356  351 GLN A CG  
3859 C CD  . GLN B 165 ? 0.8879 0.7441 0.7826 0.0349  -0.0592 0.1325  351 GLN A CD  
3860 O OE1 . GLN B 165 ? 0.9718 0.8343 0.8807 0.0388  -0.0626 0.1270  351 GLN A OE1 
3861 N NE2 . GLN B 165 ? 0.8625 0.7055 0.7596 0.0292  -0.0550 0.1352  351 GLN A NE2 
3862 N N   . LEU B 166 ? 0.8510 0.7210 0.6868 0.0128  -0.0547 0.0927  352 LEU A N   
3863 C CA  . LEU B 166 ? 0.8545 0.7290 0.6863 0.0060  -0.0544 0.0789  352 LEU A CA  
3864 C C   . LEU B 166 ? 0.8453 0.7319 0.6688 0.0125  -0.0612 0.0776  352 LEU A C   
3865 O O   . LEU B 166 ? 0.9229 0.8079 0.7320 0.0194  -0.0629 0.0870  352 LEU A O   
3866 C CB  . LEU B 166 ? 0.8503 0.7093 0.6680 -0.0031 -0.0476 0.0757  352 LEU A CB  
3867 C CG  . LEU B 166 ? 0.8142 0.6629 0.6374 -0.0105 -0.0409 0.0731  352 LEU A CG  
3868 C CD1 . LEU B 166 ? 0.8886 0.7228 0.6950 -0.0178 -0.0350 0.0709  352 LEU A CD1 
3869 C CD2 . LEU B 166 ? 0.7608 0.6193 0.6013 -0.0149 -0.0398 0.0621  352 LEU A CD2 
3870 N N   . SER B 167 ? 0.9072 0.8073 0.7400 0.0105  -0.0652 0.0652  353 SER A N   
3871 C CA  . SER B 167 ? 0.9359 0.8486 0.7612 0.0154  -0.0727 0.0598  353 SER A CA  
3872 C C   . SER B 167 ? 0.9172 0.8190 0.7258 0.0083  -0.0697 0.0531  353 SER A C   
3873 O O   . SER B 167 ? 0.8590 0.7481 0.6678 -0.0030 -0.0625 0.0474  353 SER A O   
3874 C CB  . SER B 167 ? 0.8774 0.8094 0.7214 0.0146  -0.0784 0.0470  353 SER A CB  
3875 O OG  . SER B 167 ? 0.9421 0.8885 0.7799 0.0202  -0.0874 0.0405  353 SER A OG  
3876 N N   . ILE B 168 ? 0.8656 0.7722 0.6588 0.0158  -0.0753 0.0537  354 ILE A N   
3877 C CA  . ILE B 168 ? 0.8868 0.7813 0.6621 0.0119  -0.0730 0.0486  354 ILE A CA  
3878 C C   . ILE B 168 ? 0.9566 0.8626 0.7296 0.0124  -0.0809 0.0338  354 ILE A C   
3879 O O   . ILE B 168 ? 0.9871 0.8838 0.7581 0.0026  -0.0787 0.0220  354 ILE A O   
3880 C CB  . ILE B 168 ? 0.9907 0.8773 0.7470 0.0207  -0.0710 0.0628  354 ILE A CB  
3881 C CG1 . ILE B 168 ? 0.9263 0.8005 0.6868 0.0180  -0.0634 0.0749  354 ILE A CG1 
3882 C CG2 . ILE B 168 ? 0.9599 0.8357 0.6977 0.0190  -0.0698 0.0562  354 ILE A CG2 
3883 C CD1 . ILE B 168 ? 1.0096 0.8786 0.7558 0.0257  -0.0610 0.0886  354 ILE A CD1 
3884 N N   . LYS B 169 ? 0.9569 0.8825 0.7295 0.0241  -0.0903 0.0344  355 LYS A N   
3885 C CA  . LYS B 169 ? 0.9236 0.8621 0.6920 0.0265  -0.0996 0.0196  355 LYS A CA  
3886 C C   . LYS B 169 ? 0.8557 0.7972 0.6436 0.0125  -0.1000 0.0016  355 LYS A C   
3887 O O   . LYS B 169 ? 0.9586 0.9111 0.7679 0.0090  -0.1003 -0.0007 355 LYS A O   
3888 C CB  . LYS B 169 ? 0.9258 0.8877 0.6932 0.0420  -0.1102 0.0238  355 LYS A CB  
3889 C CG  . LYS B 169 ? 0.9758 0.9547 0.7381 0.0466  -0.1219 0.0074  355 LYS A CG  
3890 C CD  . LYS B 169 ? 0.9802 0.9489 0.7181 0.0493  -0.1218 0.0034  355 LYS A CD  
3891 C CE  . LYS B 169 ? 1.0653 1.0521 0.7980 0.0551  -0.1347 -0.0143 355 LYS A CE  
3892 N NZ  . LYS B 169 ? 1.0601 1.0360 0.7694 0.0579  -0.1348 -0.0207 355 LYS A NZ  
3893 N N   . GLY B 170 ? 0.8709 0.8022 0.6525 0.0044  -0.0994 -0.0111 356 GLY A N   
3894 C CA  . GLY B 170 ? 0.8529 0.7843 0.6532 -0.0108 -0.0980 -0.0276 356 GLY A CA  
3895 C C   . GLY B 170 ? 0.8785 0.7886 0.6842 -0.0250 -0.0847 -0.0243 356 GLY A C   
3896 O O   . GLY B 170 ? 0.9552 0.8615 0.7742 -0.0390 -0.0812 -0.0365 356 GLY A O   
3897 N N   . LYS B 171 ? 0.9696 0.8659 0.7653 -0.0219 -0.0771 -0.0083 357 LYS A N   
3898 C CA  . LYS B 171 ? 0.9099 0.7865 0.7071 -0.0333 -0.0650 -0.0041 357 LYS A CA  
3899 C C   . LYS B 171 ? 0.9421 0.7948 0.7164 -0.0330 -0.0603 0.0011  357 LYS A C   
3900 O O   . LYS B 171 ? 0.9926 0.8437 0.7505 -0.0214 -0.0629 0.0106  357 LYS A O   
3901 C CB  . LYS B 171 ? 0.8424 0.7212 0.6465 -0.0302 -0.0605 0.0084  357 LYS A CB  
3902 C CG  . LYS B 171 ? 0.9188 0.8180 0.7476 -0.0316 -0.0627 0.0032  357 LYS A CG  
3903 C CD  . LYS B 171 ? 0.9394 0.8603 0.7721 -0.0178 -0.0742 0.0050  357 LYS A CD  
3904 C CE  . LYS B 171 ? 0.9784 0.9210 0.8372 -0.0188 -0.0776 -0.0026 357 LYS A CE  
3905 N NZ  . LYS B 171 ? 1.1367 1.0992 0.9984 -0.0036 -0.0888 0.0016  357 LYS A NZ  
3906 N N   . LYS B 172 ? 0.9516 0.7861 0.7251 -0.0452 -0.0530 -0.0045 358 LYS A N   
3907 C CA  . LYS B 172 ? 1.0373 0.8482 0.7897 -0.0445 -0.0492 -0.0011 358 LYS A CA  
3908 C C   . LYS B 172 ? 1.0472 0.8422 0.7902 -0.0444 -0.0403 0.0131  358 LYS A C   
3909 O O   . LYS B 172 ? 1.0983 0.8799 0.8228 -0.0379 -0.0392 0.0201  358 LYS A O   
3910 C CB  . LYS B 172 ? 1.0015 0.7979 0.7565 -0.0569 -0.0464 -0.0140 358 LYS A CB  
3911 C CG  . LYS B 172 ? 1.0186 0.8093 0.7892 -0.0721 -0.0367 -0.0160 358 LYS A CG  
3912 C CD  . LYS B 172 ? 1.1353 0.9129 0.9117 -0.0851 -0.0342 -0.0289 358 LYS A CD  
3913 C CE  . LYS B 172 ? 1.1918 0.9898 0.9842 -0.0865 -0.0449 -0.0458 358 LYS A CE  
3914 N NZ  . LYS B 172 ? 1.1654 0.9599 0.9426 -0.0772 -0.0547 -0.0529 358 LYS A NZ  
3915 N N   . ASN B 173 ? 0.9784 0.7759 0.7336 -0.0506 -0.0343 0.0166  359 ASN A N   
3916 C CA  . ASN B 173 ? 0.9770 0.7612 0.7236 -0.0503 -0.0270 0.0283  359 ASN A CA  
3917 C C   . ASN B 173 ? 0.9710 0.7692 0.7323 -0.0492 -0.0261 0.0327  359 ASN A C   
3918 O O   . ASN B 173 ? 0.9081 0.7252 0.6863 -0.0488 -0.0306 0.0272  359 ASN A O   
3919 C CB  . ASN B 173 ? 0.9268 0.6894 0.6673 -0.0613 -0.0174 0.0268  359 ASN A CB  
3920 C CG  . ASN B 173 ? 1.0208 0.7888 0.7793 -0.0743 -0.0127 0.0172  359 ASN A CG  
3921 O OD1 . ASN B 173 ? 0.9913 0.7777 0.7671 -0.0755 -0.0133 0.0150  359 ASN A OD1 
3922 N ND2 . ASN B 173 ? 1.1887 0.9406 0.9443 -0.0841 -0.0076 0.0116  359 ASN A ND2 
3923 N N   . ILE B 174 ? 1.0435 0.8322 0.7985 -0.0480 -0.0210 0.0421  360 ILE A N   
3924 C CA  . ILE B 174 ? 0.9877 0.7868 0.7557 -0.0465 -0.0202 0.0457  360 ILE A CA  
3925 C C   . ILE B 174 ? 0.9364 0.7425 0.7203 -0.0562 -0.0151 0.0368  360 ILE A C   
3926 O O   . ILE B 174 ? 0.9413 0.7632 0.7422 -0.0543 -0.0172 0.0347  360 ILE A O   
3927 C CB  . ILE B 174 ? 0.8895 0.6764 0.6468 -0.0437 -0.0164 0.0556  360 ILE A CB  
3928 C CG1 . ILE B 174 ? 0.8878 0.6761 0.6378 -0.0329 -0.0221 0.0651  360 ILE A CG1 
3929 C CG2 . ILE B 174 ? 0.9106 0.7038 0.6808 -0.0452 -0.0137 0.0557  360 ILE A CG2 
3930 C CD1 . ILE B 174 ? 1.0306 0.8143 0.7791 -0.0296 -0.0205 0.0739  360 ILE A CD1 
3931 N N   . PHE B 175 ? 0.9342 0.7287 0.7138 -0.0666 -0.0079 0.0318  361 PHE A N   
3932 C CA  . PHE B 175 ? 0.8999 0.7024 0.6956 -0.0767 -0.0014 0.0238  361 PHE A CA  
3933 C C   . PHE B 175 ? 1.0080 0.8335 0.8252 -0.0766 -0.0082 0.0142  361 PHE A C   
3934 O O   . PHE B 175 ? 0.9392 0.7813 0.7743 -0.0765 -0.0077 0.0108  361 PHE A O   
3935 C CB  . PHE B 175 ? 0.9066 0.6919 0.6943 -0.0882 0.0075  0.0211  361 PHE A CB  
3936 C CG  . PHE B 175 ? 1.0129 0.8086 0.8196 -0.1000 0.0143  0.0120  361 PHE A CG  
3937 C CD1 . PHE B 175 ? 1.0212 0.8217 0.8340 -0.1040 0.0233  0.0129  361 PHE A CD1 
3938 C CD2 . PHE B 175 ? 1.0162 0.8185 0.8359 -0.1071 0.0116  0.0016  361 PHE A CD2 
3939 C CE1 . PHE B 175 ? 0.9231 0.7355 0.7549 -0.1148 0.0308  0.0048  361 PHE A CE1 
3940 C CE2 . PHE B 175 ? 0.9278 0.7418 0.7683 -0.1188 0.0183  -0.0069 361 PHE A CE2 
3941 C CZ  . PHE B 175 ? 0.8859 0.7053 0.7326 -0.1227 0.0285  -0.0047 361 PHE A CZ  
3942 N N   . GLU B 176 ? 0.9662 0.7938 0.7817 -0.0754 -0.0153 0.0091  362 GLU A N   
3943 C CA  . GLU B 176 ? 0.8604 0.7117 0.6949 -0.0734 -0.0237 -0.0004 362 GLU A CA  
3944 C C   . GLU B 176 ? 0.8528 0.7193 0.6925 -0.0603 -0.0313 0.0058  362 GLU A C   
3945 O O   . GLU B 176 ? 0.9604 0.8478 0.8199 -0.0584 -0.0355 0.0001  362 GLU A O   
3946 C CB  . GLU B 176 ? 0.8620 0.7121 0.6906 -0.0731 -0.0311 -0.0076 362 GLU A CB  
3947 C CG  . GLU B 176 ? 0.9636 0.8033 0.7962 -0.0875 -0.0252 -0.0175 362 GLU A CG  
3948 C CD  . GLU B 176 ? 1.0405 0.8844 0.8733 -0.0869 -0.0348 -0.0287 362 GLU A CD  
3949 O OE1 . GLU B 176 ? 0.9863 0.8377 0.8093 -0.0739 -0.0449 -0.0266 362 GLU A OE1 
3950 O OE2 . GLU B 176 ? 1.1560 0.9963 0.9991 -0.0993 -0.0322 -0.0398 362 GLU A OE2 
3951 N N   . SER B 177 ? 0.9368 0.7930 0.7602 -0.0512 -0.0331 0.0177  363 SER A N   
3952 C CA  . SER B 177 ? 0.9521 0.8197 0.7808 -0.0393 -0.0392 0.0254  363 SER A CA  
3953 C C   . SER B 177 ? 0.9363 0.8106 0.7818 -0.0409 -0.0350 0.0251  363 SER A C   
3954 O O   . SER B 177 ? 0.8525 0.7433 0.7135 -0.0342 -0.0406 0.0243  363 SER A O   
3955 C CB  . SER B 177 ? 0.8233 0.6777 0.6333 -0.0314 -0.0398 0.0386  363 SER A CB  
3956 O OG  . SER B 177 ? 0.8463 0.7106 0.6620 -0.0204 -0.0455 0.0472  363 SER A OG  
3957 N N   . PHE B 178 ? 1.0045 0.8661 0.8463 -0.0488 -0.0253 0.0253  364 PHE A N   
3958 C CA  . PHE B 178 ? 0.9347 0.8027 0.7909 -0.0500 -0.0207 0.0232  364 PHE A CA  
3959 C C   . PHE B 178 ? 0.8662 0.7533 0.7440 -0.0555 -0.0196 0.0111  364 PHE A C   
3960 O O   . PHE B 178 ? 0.8408 0.7421 0.7363 -0.0513 -0.0208 0.0083  364 PHE A O   
3961 C CB  . PHE B 178 ? 0.9248 0.7757 0.7687 -0.0563 -0.0106 0.0259  364 PHE A CB  
3962 C CG  . PHE B 178 ? 0.8440 0.6854 0.6799 -0.0492 -0.0119 0.0353  364 PHE A CG  
3963 C CD1 . PHE B 178 ? 0.8288 0.6770 0.6781 -0.0449 -0.0123 0.0346  364 PHE A CD1 
3964 C CD2 . PHE B 178 ? 0.8925 0.7187 0.7093 -0.0466 -0.0130 0.0439  364 PHE A CD2 
3965 C CE1 . PHE B 178 ? 0.8751 0.7143 0.7197 -0.0393 -0.0140 0.0420  364 PHE A CE1 
3966 C CE2 . PHE B 178 ? 0.8872 0.7065 0.6998 -0.0409 -0.0145 0.0518  364 PHE A CE2 
3967 C CZ  . PHE B 178 ? 0.8677 0.6932 0.6946 -0.0378 -0.0151 0.0507  364 PHE A CZ  
3968 N N   . VAL B 179 ? 0.9136 0.8017 0.7922 -0.0648 -0.0175 0.0034  365 VAL A N   
3969 C CA  . VAL B 179 ? 0.8660 0.7747 0.7681 -0.0711 -0.0167 -0.0089 365 VAL A CA  
3970 C C   . VAL B 179 ? 0.7933 0.7244 0.7113 -0.0603 -0.0289 -0.0118 365 VAL A C   
3971 O O   . VAL B 179 ? 0.8623 0.8130 0.8025 -0.0592 -0.0292 -0.0184 365 VAL A O   
3972 C CB  . VAL B 179 ? 0.7973 0.7012 0.6980 -0.0833 -0.0136 -0.0165 365 VAL A CB  
3973 C CG1 . VAL B 179 ? 0.7954 0.7240 0.7237 -0.0896 -0.0149 -0.0301 365 VAL A CG1 
3974 C CG2 . VAL B 179 ? 0.8191 0.7012 0.7060 -0.0938 -0.0002 -0.0127 365 VAL A CG2 
3975 N N   . ASP B 180 ? 0.7940 0.7231 0.7000 -0.0511 -0.0388 -0.0064 366 ASP A N   
3976 C CA  . ASP B 180 ? 0.8384 0.7874 0.7553 -0.0388 -0.0507 -0.0067 366 ASP A CA  
3977 C C   . ASP B 180 ? 0.8749 0.8268 0.8001 -0.0293 -0.0511 0.0009  366 ASP A C   
3978 O O   . ASP B 180 ? 0.8954 0.8668 0.8388 -0.0217 -0.0575 -0.0024 366 ASP A O   
3979 C CB  . ASP B 180 ? 0.8873 0.8318 0.7854 -0.0303 -0.0596 -0.0006 366 ASP A CB  
3980 C CG  . ASP B 180 ? 0.9335 0.8971 0.8385 -0.0156 -0.0716 0.0022  366 ASP A CG  
3981 O OD1 . ASP B 180 ? 0.8936 0.8791 0.8149 -0.0149 -0.0784 -0.0089 366 ASP A OD1 
3982 O OD2 . ASP B 180 ? 1.0060 0.9631 0.9006 -0.0048 -0.0742 0.0158  366 ASP A OD2 
3983 N N   . TYR B 181 ? 0.8756 0.8082 0.7884 -0.0291 -0.0449 0.0105  367 TYR A N   
3984 C CA  . TYR B 181 ? 0.8496 0.7820 0.7709 -0.0208 -0.0454 0.0168  367 TYR A CA  
3985 C C   . TYR B 181 ? 0.8261 0.7718 0.7695 -0.0241 -0.0405 0.0065  367 TYR A C   
3986 O O   . TYR B 181 ? 0.8501 0.8068 0.8097 -0.0149 -0.0450 0.0065  367 TYR A O   
3987 C CB  . TYR B 181 ? 0.7934 0.7030 0.6979 -0.0216 -0.0399 0.0268  367 TYR A CB  
3988 C CG  . TYR B 181 ? 0.7535 0.6589 0.6633 -0.0116 -0.0432 0.0361  367 TYR A CG  
3989 C CD1 . TYR B 181 ? 0.7548 0.6596 0.6600 -0.0013 -0.0508 0.0476  367 TYR A CD1 
3990 C CD2 . TYR B 181 ? 0.7513 0.6530 0.6707 -0.0125 -0.0381 0.0334  367 TYR A CD2 
3991 C CE1 . TYR B 181 ? 0.7737 0.6727 0.6856 0.0067  -0.0530 0.0570  367 TYR A CE1 
3992 C CE2 . TYR B 181 ? 0.7740 0.6698 0.7001 -0.0041 -0.0414 0.0408  367 TYR A CE2 
3993 C CZ  . TYR B 181 ? 0.7813 0.6751 0.7047 0.0050  -0.0486 0.0530  367 TYR A CZ  
3994 O OH  . TYR B 181 ? 0.7832 0.6694 0.7152 0.0123  -0.0511 0.0612  367 TYR A OH  
3995 N N   . VAL B 182 ? 0.9010 0.8625 0.8980 0.0370  -0.0999 -0.1353 368 VAL A N   
3996 C CA  . VAL B 182 ? 0.8846 0.8443 0.9009 0.0189  -0.0970 -0.1148 368 VAL A CA  
3997 C C   . VAL B 182 ? 0.8957 0.8431 0.9360 0.0244  -0.1186 -0.1249 368 VAL A C   
3998 O O   . VAL B 182 ? 0.8841 0.8285 0.9466 0.0104  -0.1176 -0.1100 368 VAL A O   
3999 C CB  . VAL B 182 ? 0.8696 0.8293 0.9220 0.0009  -0.0974 -0.0947 368 VAL A CB  
4000 C CG1 . VAL B 182 ? 0.8844 0.8437 0.9410 -0.0207 -0.0827 -0.0699 368 VAL A CG1 
4001 C CG2 . VAL B 182 ? 0.8651 0.8351 0.9030 0.0002  -0.0856 -0.0909 368 VAL A CG2 
4002 N N   . ALA B 183 ? 0.9195 0.8586 0.9562 0.0440  -0.1379 -0.1501 369 ALA A N   
4003 C CA  . ALA B 183 ? 0.9327 0.8595 0.9925 0.0500  -0.1612 -0.1612 369 ALA A CA  
4004 C C   . ALA B 183 ? 0.9791 0.9073 1.0172 0.0468  -0.1518 -0.1547 369 ALA A C   
4005 O O   . ALA B 183 ? 1.0081 0.9434 0.9992 0.0498  -0.1319 -0.1531 369 ALA A O   
4006 C CB  . ALA B 183 ? 0.9633 0.8794 1.0132 0.0721  -0.1821 -0.1905 369 ALA A CB  
4007 N N   . VAL B 184 ? 1.0042 0.9256 1.0796 0.0404  -0.1655 -0.1503 370 VAL A N   
4008 C CA  . VAL B 184 ? 1.0527 0.9749 1.1180 0.0364  -0.1586 -0.1431 370 VAL A CA  
4009 C C   . VAL B 184 ? 1.0982 1.0120 1.1350 0.0569  -0.1753 -0.1661 370 VAL A C   
4010 O O   . VAL B 184 ? 1.0476 0.9496 1.1049 0.0683  -0.2034 -0.1847 370 VAL A O   
4011 C CB  . VAL B 184 ? 1.0335 0.9509 1.1544 0.0216  -0.1665 -0.1301 370 VAL A CB  
4012 C CG1 . VAL B 184 ? 0.9611 0.8784 1.0771 0.0198  -0.1624 -0.1254 370 VAL A CG1 
4013 C CG2 . VAL B 184 ? 0.9500 0.8722 1.0903 0.0002  -0.1472 -0.1060 370 VAL A CG2 
4014 N N   . GLU B 185 ? 1.1442 1.0624 1.1321 0.0611  -0.1584 -0.1647 371 GLU A N   
4015 C CA  . GLU B 185 ? 1.1395 1.0474 1.0951 0.0789  -0.1729 -0.1836 371 GLU A CA  
4016 C C   . GLU B 185 ? 1.1113 1.0157 1.0926 0.0739  -0.1829 -0.1770 371 GLU A C   
4017 O O   . GLU B 185 ? 1.1014 1.0146 1.1017 0.0571  -0.1652 -0.1553 371 GLU A O   
4018 C CB  . GLU B 185 ? 1.2571 1.1694 1.1459 0.0866  -0.1496 -0.1858 371 GLU A CB  
4019 C CG  . GLU B 185 ? 1.3658 1.2644 1.2136 0.1046  -0.1630 -0.2039 371 GLU A CG  
4020 C CD  . GLU B 185 ? 1.4854 1.3865 1.2659 0.1121  -0.1382 -0.2062 371 GLU A CD  
4021 O OE1 . GLU B 185 ? 1.4738 1.3848 1.2383 0.1089  -0.1164 -0.2023 371 GLU A OE1 
4022 O OE2 . GLU B 185 ? 1.4898 1.3823 1.2343 0.1212  -0.1407 -0.2118 371 GLU A OE2 
4023 N N   . GLN B 186 ? 1.1697 1.0601 1.1522 0.0885  -0.2117 -0.1960 372 GLN A N   
4024 C CA  . GLN B 186 ? 1.0999 0.9859 1.1132 0.0857  -0.2266 -0.1924 372 GLN A CA  
4025 C C   . GLN B 186 ? 1.1945 1.0769 1.1577 0.0959  -0.2231 -0.1961 372 GLN A C   
4026 O O   . GLN B 186 ? 1.3288 1.2015 1.2396 0.1125  -0.2287 -0.2136 372 GLN A O   
4027 C CB  . GLN B 186 ? 1.0595 0.9316 1.1155 0.0937  -0.2647 -0.2101 372 GLN A CB  
4028 C CG  . GLN B 186 ? 1.0955 0.9690 1.2207 0.0800  -0.2742 -0.1981 372 GLN A CG  
4029 C CD  . GLN B 186 ? 1.0724 0.9560 1.2366 0.0600  -0.2540 -0.1778 372 GLN A CD  
4030 O OE1 . GLN B 186 ? 1.0990 0.9877 1.2455 0.0575  -0.2396 -0.1750 372 GLN A OE1 
4031 N NE2 . GLN B 186 ? 1.2131 1.0981 1.4308 0.0454  -0.2529 -0.1635 372 GLN A NE2 
4032 N N   . LEU B 187 ? 1.2177 1.1064 1.1966 0.0855  -0.2123 -0.1792 373 LEU A N   
4033 C CA  . LEU B 187 ? 1.2626 1.1482 1.2021 0.0932  -0.2091 -0.1793 373 LEU A CA  
4034 C C   . LEU B 187 ? 1.3766 1.2540 1.3615 0.0948  -0.2376 -0.1823 373 LEU A C   
4035 O O   . LEU B 187 ? 1.3670 1.2523 1.3923 0.0808  -0.2277 -0.1646 373 LEU A O   
4036 C CB  . LEU B 187 ? 1.2536 1.1541 1.1734 0.0794  -0.1702 -0.1562 373 LEU A CB  
4037 C CG  . LEU B 187 ? 1.2081 1.1188 1.0852 0.0756  -0.1393 -0.1504 373 LEU A CG  
4038 C CD1 . LEU B 187 ? 1.1303 1.0549 0.9989 0.0592  -0.1037 -0.1261 373 LEU A CD1 
4039 C CD2 . LEU B 187 ? 1.3039 1.2058 1.1147 0.0950  -0.1413 -0.1693 373 LEU A CD2 
4040 N N   . ASP B 188 ? 1.4234 1.2841 1.4030 0.1114  -0.2727 -0.2048 374 ASP A N   
4041 C CA  . ASP B 188 ? 1.3826 1.2341 1.4038 0.1149  -0.3043 -0.2102 374 ASP A CA  
4042 C C   . ASP B 188 ? 1.4830 1.3260 1.4564 0.1269  -0.3096 -0.2139 374 ASP A C   
4043 O O   . ASP B 188 ? 1.4806 1.3270 1.3947 0.1295  -0.2839 -0.2087 374 ASP A O   
4044 C CB  . ASP B 188 ? 1.4643 1.3013 1.5113 0.1247  -0.3419 -0.2323 374 ASP A CB  
4045 C CG  . ASP B 188 ? 1.4759 1.3205 1.5872 0.1109  -0.3407 -0.2259 374 ASP A CG  
4046 O OD1 . ASP B 188 ? 1.4771 1.3338 1.6350 0.0935  -0.3237 -0.2054 374 ASP A OD1 
4047 O OD2 . ASP B 188 ? 1.4384 1.2754 1.5524 0.1174  -0.3559 -0.2414 374 ASP A OD2 
4048 N N   . GLY B 189 ? 1.5236 1.3549 1.5238 0.1340  -0.3433 -0.2224 375 GLY A N   
4049 C CA  . GLY B 189 ? 1.3818 1.2020 1.3386 0.1463  -0.3536 -0.2265 375 GLY A CA  
4050 C C   . GLY B 189 ? 1.6144 1.4206 1.4843 0.1624  -0.3506 -0.2421 375 GLY A C   
4051 O O   . GLY B 189 ? 1.7706 1.5681 1.6258 0.1693  -0.3603 -0.2586 375 GLY A O   
4052 N N   . ASP B 190 ? 1.5910 1.3941 1.4039 0.1682  -0.3356 -0.2371 376 ASP A N   
4053 C CA  . ASP B 190 ? 1.6934 1.4848 1.4191 0.1810  -0.3220 -0.2473 376 ASP A CA  
4054 C C   . ASP B 190 ? 1.6732 1.4832 1.3816 0.1708  -0.2791 -0.2360 376 ASP A C   
4055 O O   . ASP B 190 ? 1.7214 1.5267 1.3622 0.1782  -0.2587 -0.2399 376 ASP A O   
4056 C CB  . ASP B 190 ? 1.8388 1.6041 1.5291 0.1985  -0.3532 -0.2755 376 ASP A CB  
4057 C CG  . ASP B 190 ? 1.8753 1.6217 1.4710 0.2137  -0.3429 -0.2874 376 ASP A CG  
4058 O OD1 . ASP B 190 ? 1.9088 1.6619 1.4652 0.2119  -0.3138 -0.2744 376 ASP A OD1 
4059 O OD2 . ASP B 190 ? 1.7473 1.4706 1.3073 0.2272  -0.3631 -0.3104 376 ASP A OD2 
4060 N N   . ASN B 191 ? 1.5970 1.4271 1.3642 0.1535  -0.2645 -0.2213 377 ASN A N   
4061 C CA  . ASN B 191 ? 1.5458 1.3941 1.3014 0.1417  -0.2251 -0.2078 377 ASN A CA  
4062 C C   . ASN B 191 ? 1.4813 1.3499 1.2883 0.1206  -0.2024 -0.1818 377 ASN A C   
4063 O O   . ASN B 191 ? 1.3847 1.2683 1.1947 0.1078  -0.1733 -0.1691 377 ASN A O   
4064 C CB  . ASN B 191 ? 1.5601 1.4082 1.3262 0.1425  -0.2293 -0.2192 377 ASN A CB  
4065 C CG  . ASN B 191 ? 1.7375 1.5667 1.4428 0.1616  -0.2396 -0.2431 377 ASN A CG  
4066 O OD1 . ASN B 191 ? 1.8520 1.6723 1.4939 0.1715  -0.2293 -0.2473 377 ASN A OD1 
4067 N ND2 . ASN B 191 ? 1.7143 1.5353 1.4378 0.1668  -0.2594 -0.2594 377 ASN A ND2 
4068 N N   . LYS B 192 ? 1.4409 1.3091 1.2879 0.1165  -0.2149 -0.1739 378 LYS A N   
4069 C CA  . LYS B 192 ? 1.2971 1.1812 1.1993 0.0960  -0.1950 -0.1507 378 LYS A CA  
4070 C C   . LYS B 192 ? 1.1826 1.0810 1.0490 0.0850  -0.1508 -0.1321 378 LYS A C   
4071 O O   . LYS B 192 ? 1.0715 0.9673 0.8807 0.0934  -0.1386 -0.1327 378 LYS A O   
4072 C CB  . LYS B 192 ? 1.3176 1.1974 1.2603 0.0962  -0.2140 -0.1469 378 LYS A CB  
4073 C CG  . LYS B 192 ? 1.3224 1.1940 1.3288 0.0982  -0.2519 -0.1580 378 LYS A CG  
4074 C CD  . LYS B 192 ? 1.2641 1.1363 1.3273 0.0931  -0.2640 -0.1492 378 LYS A CD  
4075 C CE  . LYS B 192 ? 1.2837 1.1409 1.3196 0.1113  -0.2937 -0.1617 378 LYS A CE  
4076 N NZ  . LYS B 192 ? 1.2579 1.0976 1.2986 0.1262  -0.3381 -0.1860 378 LYS A NZ  
4077 N N   . TYR B 193 ? 1.1813 1.0930 1.0795 0.0660  -0.1271 -0.1157 379 TYR A N   
4078 C CA  . TYR B 193 ? 1.0792 1.0040 0.9468 0.0535  -0.0856 -0.0974 379 TYR A CA  
4079 C C   . TYR B 193 ? 1.0679 0.9958 0.9392 0.0476  -0.0709 -0.0826 379 TYR A C   
4080 O O   . TYR B 193 ? 1.1090 1.0350 1.0345 0.0422  -0.0834 -0.0773 379 TYR A O   
4081 C CB  . TYR B 193 ? 0.9759 0.9110 0.8778 0.0335  -0.0666 -0.0828 379 TYR A CB  
4082 C CG  . TYR B 193 ? 0.9712 0.9186 0.8477 0.0180  -0.0248 -0.0622 379 TYR A CG  
4083 C CD1 . TYR B 193 ? 0.9588 0.9117 0.7757 0.0222  -0.0045 -0.0639 379 TYR A CD1 
4084 C CD2 . TYR B 193 ? 1.0434 0.9959 0.9563 -0.0015 -0.0049 -0.0413 379 TYR A CD2 
4085 C CE1 . TYR B 193 ? 1.0342 0.9980 0.8281 0.0075  0.0329  -0.0455 379 TYR A CE1 
4086 C CE2 . TYR B 193 ? 1.0495 1.0115 0.9371 -0.0165 0.0334  -0.0228 379 TYR A CE2 
4087 C CZ  . TYR B 193 ? 1.0193 0.9872 0.8474 -0.0119 0.0513  -0.0250 379 TYR A CZ  
4088 O OH  . TYR B 193 ? 1.1109 1.0880 0.9144 -0.0273 0.0884  -0.0071 379 TYR A OH  
4089 N N   . ASP B 194 ? 1.1056 1.0383 0.9207 0.0488  -0.0435 -0.0762 380 ASP A N   
4090 C CA  . ASP B 194 ? 1.0494 0.9859 0.8618 0.0427  -0.0243 -0.0610 380 ASP A CA  
4091 C C   . ASP B 194 ? 1.0569 1.0059 0.9011 0.0180  0.0088  -0.0379 380 ASP A C   
4092 O O   . ASP B 194 ? 1.0427 1.0006 0.8521 0.0087  0.0408  -0.0278 380 ASP A O   
4093 C CB  . ASP B 194 ? 1.1685 1.1034 0.9061 0.0540  -0.0079 -0.0640 380 ASP A CB  
4094 C CG  . ASP B 194 ? 1.2072 1.1450 0.9405 0.0491  0.0112  -0.0489 380 ASP A CG  
4095 O OD1 . ASP B 194 ? 1.1820 1.1216 0.9721 0.0390  0.0080  -0.0380 380 ASP A OD1 
4096 O OD2 . ASP B 194 ? 1.3709 1.3086 1.0449 0.0552  0.0306  -0.0479 380 ASP A OD2 
4097 N N   . ALA B 195 ? 1.0381 0.9863 0.9490 0.0067  0.0012  -0.0297 381 ALA A N   
4098 C CA  . ALA B 195 ? 0.9837 0.9394 0.9273 -0.0177 0.0318  -0.0080 381 ALA A CA  
4099 C C   . ALA B 195 ? 0.9751 0.9352 0.9092 -0.0264 0.0612  0.0085  381 ALA A C   
4100 O O   . ALA B 195 ? 0.8447 0.8080 0.8109 -0.0471 0.0862  0.0267  381 ALA A O   
4101 C CB  . ALA B 195 ? 0.8821 0.8333 0.9021 -0.0272 0.0145  -0.0062 381 ALA A CB  
4102 N N   . GLY B 196 ? 1.0183 0.9768 0.9091 -0.0113 0.0591  0.0027  382 GLY A N   
4103 C CA  . GLY B 196 ? 1.0572 1.0199 0.9340 -0.0186 0.0884  0.0181  382 GLY A CA  
4104 C C   . GLY B 196 ? 0.9976 0.9582 0.9407 -0.0277 0.0860  0.0283  382 GLY A C   
4105 O O   . GLY B 196 ? 0.9662 0.9200 0.9330 -0.0144 0.0569  0.0194  382 GLY A O   
4106 N N   . GLU B 197 ? 0.9960 0.9610 0.9688 -0.0510 0.1171  0.0472  383 GLU A N   
4107 C CA  . GLU B 197 ? 0.9690 0.9314 1.0090 -0.0624 0.1206  0.0581  383 GLU A CA  
4108 C C   . GLU B 197 ? 0.9414 0.8969 1.0443 -0.0553 0.0807  0.0459  383 GLU A C   
4109 O O   . GLU B 197 ? 1.0414 0.9937 1.1954 -0.0538 0.0687  0.0472  383 GLU A O   
4110 C CB  . GLU B 197 ? 0.9746 0.9391 1.0322 -0.0897 0.1602  0.0784  383 GLU A CB  
4111 C CG  . GLU B 197 ? 1.0268 0.9873 1.1519 -0.1044 0.1720  0.0913  383 GLU A CG  
4112 C CD  . GLU B 197 ? 1.1245 1.0826 1.2630 -0.1319 0.2097  0.1098  383 GLU A CD  
4113 O OE1 . GLU B 197 ? 1.0357 0.9960 1.1297 -0.1392 0.2246  0.1129  383 GLU A OE1 
4114 O OE2 . GLU B 197 ? 1.2805 1.2332 1.4739 -0.1466 0.2244  0.1212  383 GLU A OE2 
4115 N N   . HIS B 198 ? 0.9005 0.8538 1.0030 -0.0508 0.0596  0.0337  384 HIS A N   
4116 C CA  . HIS B 198 ? 0.8444 0.7909 1.0038 -0.0438 0.0212  0.0208  384 HIS A CA  
4117 C C   . HIS B 198 ? 0.9215 0.8622 1.0567 -0.0178 -0.0202 -0.0015 384 HIS A C   
4118 O O   . HIS B 198 ? 0.9386 0.8728 1.1169 -0.0105 -0.0552 -0.0144 384 HIS A O   
4119 C CB  . HIS B 198 ? 0.9198 0.8651 1.0983 -0.0548 0.0211  0.0206  384 HIS A CB  
4120 C CG  . HIS B 198 ? 1.0261 0.9727 1.2258 -0.0811 0.0592  0.0418  384 HIS A CG  
4121 N ND1 . HIS B 198 ? 1.0954 1.0427 1.2739 -0.0931 0.0756  0.0477  384 HIS A ND1 
4122 C CD2 . HIS B 198 ? 1.0885 1.0336 1.3279 -0.0980 0.0841  0.0585  384 HIS A CD2 
4123 C CE1 . HIS B 198 ? 1.0513 0.9962 1.2515 -0.1165 0.1084  0.0672  384 HIS A CE1 
4124 N NE2 . HIS B 198 ? 1.0930 1.0363 1.3303 -0.1201 0.1154  0.0738  384 HIS A NE2 
4125 N N   . GLY B 199 ? 0.9649 0.9059 1.0312 -0.0040 -0.0171 -0.0068 385 GLY A N   
4126 C CA  . GLY B 199 ? 0.9551 0.8865 0.9932 0.0202  -0.0555 -0.0281 385 GLY A CA  
4127 C C   . GLY B 199 ? 0.9963 0.9237 1.0196 0.0280  -0.0763 -0.0450 385 GLY A C   
4128 O O   . GLY B 199 ? 1.1132 1.0464 1.1347 0.0165  -0.0585 -0.0400 385 GLY A O   
4129 N N   . LEU B 200 ? 1.0071 0.9225 1.0190 0.0482  -0.1155 -0.0654 386 LEU A N   
4130 C CA  . LEU B 200 ? 1.0480 0.9571 1.0506 0.0570  -0.1389 -0.0835 386 LEU A CA  
4131 C C   . LEU B 200 ? 1.0397 0.9507 1.1180 0.0447  -0.1498 -0.0816 386 LEU A C   
4132 O O   . LEU B 200 ? 1.0137 0.9235 1.1548 0.0393  -0.1618 -0.0770 386 LEU A O   
4133 C CB  . LEU B 200 ? 1.1455 1.0382 1.1190 0.0806  -0.1789 -0.1058 386 LEU A CB  
4134 C CG  . LEU B 200 ? 1.1788 1.0643 1.0631 0.0961  -0.1721 -0.1148 386 LEU A CG  
4135 C CD1 . LEU B 200 ? 1.1055 0.9964 0.9581 0.0930  -0.1434 -0.0992 386 LEU A CD1 
4136 C CD2 . LEU B 200 ? 1.2352 1.0998 1.0940 0.1181  -0.2150 -0.1384 386 LEU A CD2 
4137 N N   . GLN B 201 ? 1.0384 0.9516 1.1125 0.0401  -0.1454 -0.0851 387 GLN A N   
4138 C CA  . GLN B 201 ? 1.1055 1.0213 1.2471 0.0242  -0.1452 -0.0780 387 GLN A CA  
4139 C C   . GLN B 201 ? 1.1775 1.0872 1.3364 0.0294  -0.1706 -0.0936 387 GLN A C   
4140 O O   . GLN B 201 ? 1.1699 1.0793 1.3898 0.0170  -0.1739 -0.0883 387 GLN A O   
4141 C CB  . GLN B 201 ? 1.0477 0.9742 1.1857 0.0025  -0.1015 -0.0556 387 GLN A CB  
4142 C CG  . GLN B 201 ? 1.0278 0.9592 1.1841 -0.0106 -0.0755 -0.0363 387 GLN A CG  
4143 C CD  . GLN B 201 ? 0.9807 0.9074 1.2155 -0.0158 -0.0926 -0.0345 387 GLN A CD  
4144 O OE1 . GLN B 201 ? 0.9613 0.8837 1.2458 -0.0203 -0.1090 -0.0391 387 GLN A OE1 
4145 N NE2 . GLN B 201 ? 0.9272 0.8547 1.1761 -0.0153 -0.0887 -0.0279 387 GLN A NE2 
4146 N N   . GLU B 202 ? 1.2382 1.1416 1.3482 0.0465  -0.1874 -0.1124 388 GLU A N   
4147 C CA  . GLU B 202 ? 1.2774 1.1751 1.4035 0.0510  -0.2090 -0.1270 388 GLU A CA  
4148 C C   . GLU B 202 ? 1.2237 1.1301 1.3687 0.0327  -0.1835 -0.1124 388 GLU A C   
4149 O O   . GLU B 202 ? 1.3042 1.2098 1.5097 0.0205  -0.1878 -0.1063 388 GLU A O   
4150 C CB  . GLU B 202 ? 1.3107 1.1982 1.4979 0.0561  -0.2481 -0.1395 388 GLU A CB  
4151 C CG  . GLU B 202 ? 1.3819 1.2550 1.5412 0.0785  -0.2849 -0.1627 388 GLU A CG  
4152 C CD  . GLU B 202 ? 1.4774 1.3410 1.7007 0.0823  -0.3239 -0.1739 388 GLU A CD  
4153 O OE1 . GLU B 202 ? 1.6386 1.5077 1.9318 0.0673  -0.3204 -0.1624 388 GLU A OE1 
4154 O OE2 . GLU B 202 ? 1.3303 1.1796 1.5326 0.1001  -0.3578 -0.1946 388 GLU A OE2 
4155 N N   . ALA B 203 ? 1.1819 1.0956 1.2730 0.0309  -0.1567 -0.1067 389 ALA A N   
4156 C CA  . ALA B 203 ? 1.1388 1.0604 1.2377 0.0135  -0.1309 -0.0913 389 ALA A CA  
4157 C C   . ALA B 203 ? 1.1187 1.0379 1.2028 0.0215  -0.1425 -0.1050 389 ALA A C   
4158 O O   . ALA B 203 ? 1.1470 1.0574 1.2207 0.0393  -0.1705 -0.1267 389 ALA A O   
4159 C CB  . ALA B 203 ? 1.1456 1.0778 1.2003 0.0036  -0.0918 -0.0736 389 ALA A CB  
4160 N N   . GLU B 204 ? 1.1564 1.0822 1.2410 0.0074  -0.1209 -0.0918 390 GLU A N   
4161 C CA  . GLU B 204 ? 1.1486 1.0745 1.2169 0.0130  -0.1257 -0.1013 390 GLU A CA  
4162 C C   . GLU B 204 ? 0.9795 0.9163 0.9979 0.0073  -0.0936 -0.0903 390 GLU A C   
4163 O O   . GLU B 204 ? 1.0041 0.9477 1.0225 -0.0103 -0.0663 -0.0690 390 GLU A O   
4164 C CB  . GLU B 204 ? 1.0994 1.0214 1.2228 0.0014  -0.1346 -0.0962 390 GLU A CB  
4165 C CG  . GLU B 204 ? 1.0866 0.9976 1.2619 0.0081  -0.1685 -0.1099 390 GLU A CG  
4166 C CD  . GLU B 204 ? 1.0923 0.9987 1.3170 -0.0025 -0.1758 -0.1056 390 GLU A CD  
4167 O OE1 . GLU B 204 ? 1.0375 0.9486 1.2561 -0.0164 -0.1539 -0.0898 390 GLU A OE1 
4168 O OE2 . GLU B 204 ? 0.9930 0.8902 1.2615 0.0030  -0.2040 -0.1181 390 GLU A OE2 
4169 N N   . LYS B 205 ? 1.0157 0.9531 0.9928 0.0218  -0.0966 -0.1052 391 LYS A N   
4170 C CA  . LYS B 205 ? 1.1084 1.0562 1.0382 0.0189  -0.0685 -0.0981 391 LYS A CA  
4171 C C   . LYS B 205 ? 1.0116 0.9611 0.9483 0.0191  -0.0723 -0.1025 391 LYS A C   
4172 O O   . LYS B 205 ? 1.0393 0.9806 0.9885 0.0324  -0.0972 -0.1212 391 LYS A O   
4173 C CB  . LYS B 205 ? 1.0995 1.0466 0.9697 0.0362  -0.0639 -0.1114 391 LYS A CB  
4174 C CG  . LYS B 205 ? 1.1937 1.1519 1.0147 0.0336  -0.0330 -0.1046 391 LYS A CG  
4175 C CD  . LYS B 205 ? 1.1626 1.1179 0.9260 0.0489  -0.0259 -0.1155 391 LYS A CD  
4176 C CE  . LYS B 205 ? 1.1932 1.1348 0.9374 0.0714  -0.0511 -0.1425 391 LYS A CE  
4177 N NZ  . LYS B 205 ? 1.2186 1.1624 0.9556 0.0760  -0.0492 -0.1520 391 LYS A NZ  
4178 N N   . GLY B 206 ? 0.8941 0.8532 0.8227 0.0042  -0.0478 -0.0852 392 GLY A N   
4179 C CA  . GLY B 206 ? 1.0058 0.9671 0.9437 0.0030  -0.0508 -0.0867 392 GLY A CA  
4180 C C   . GLY B 206 ? 0.9650 0.9383 0.8723 -0.0081 -0.0215 -0.0716 392 GLY A C   
4181 O O   . GLY B 206 ? 0.9777 0.9575 0.8557 -0.0154 0.0022  -0.0599 392 GLY A O   
4182 N N   . VAL B 207 ? 0.8662 0.8422 0.7822 -0.0092 -0.0242 -0.0722 393 VAL A N   
4183 C CA  . VAL B 207 ? 0.8839 0.8711 0.7755 -0.0190 -0.0007 -0.0594 393 VAL A CA  
4184 C C   . VAL B 207 ? 0.8293 0.8146 0.7570 -0.0308 -0.0084 -0.0491 393 VAL A C   
4185 O O   . VAL B 207 ? 0.8837 0.8626 0.8404 -0.0216 -0.0316 -0.0617 393 VAL A O   
4186 C CB  . VAL B 207 ? 0.8988 0.8925 0.7490 -0.0014 0.0057  -0.0766 393 VAL A CB  
4187 C CG1 . VAL B 207 ? 0.8766 0.8799 0.7230 -0.0079 0.0172  -0.0693 393 VAL A CG1 
4188 C CG2 . VAL B 207 ? 1.0075 1.0054 0.8110 0.0026  0.0257  -0.0769 393 VAL A CG2 
4189 N N   . LYS B 208 ? 0.8133 0.8026 0.7373 -0.0512 0.0106  -0.0262 394 LYS A N   
4190 C CA  . LYS B 208 ? 0.8086 0.7944 0.7609 -0.0638 0.0045  -0.0141 394 LYS A CA  
4191 C C   . LYS B 208 ? 0.8401 0.8367 0.7633 -0.0730 0.0249  -0.0019 394 LYS A C   
4192 O O   . LYS B 208 ? 0.9009 0.9054 0.7876 -0.0780 0.0484  0.0051  394 LYS A O   
4193 C CB  . LYS B 208 ? 0.8456 0.8191 0.8296 -0.0834 0.0037  0.0044  394 LYS A CB  
4194 C CG  . LYS B 208 ? 0.9718 0.9364 0.9899 -0.0943 -0.0086 0.0146  394 LYS A CG  
4195 C CD  . LYS B 208 ? 0.8943 0.8546 0.9446 -0.0770 -0.0375 -0.0054 394 LYS A CD  
4196 C CE  . LYS B 208 ? 0.8352 0.7796 0.9329 -0.0835 -0.0546 -0.0023 394 LYS A CE  
4197 N NZ  . LYS B 208 ? 0.8939 0.8280 1.0092 -0.1051 -0.0506 0.0206  394 LYS A NZ  
4198 N N   . PHE B 209 ? 0.8014 0.7980 0.7426 -0.0753 0.0153  0.0007  395 PHE A N   
4199 C CA  . PHE B 209 ? 0.8383 0.8454 0.7572 -0.0827 0.0304  0.0106  395 PHE A CA  
4200 C C   . PHE B 209 ? 0.9076 0.9086 0.8246 -0.1093 0.0437  0.0384  395 PHE A C   
4201 O O   . PHE B 209 ? 0.9641 0.9515 0.9118 -0.1210 0.0316  0.0495  395 PHE A O   
4202 C CB  . PHE B 209 ? 0.8207 0.8303 0.7615 -0.0730 0.0133  0.0012  395 PHE A CB  
4203 C CG  . PHE B 209 ? 0.8814 0.8982 0.8126 -0.0482 0.0080  -0.0255 395 PHE A CG  
4204 C CD1 . PHE B 209 ? 0.8118 0.8421 0.7080 -0.0414 0.0265  -0.0314 395 PHE A CD1 
4205 C CD2 . PHE B 209 ? 0.8688 0.8771 0.8247 -0.0320 -0.0145 -0.0449 395 PHE A CD2 
4206 C CE1 . PHE B 209 ? 0.8251 0.8589 0.7098 -0.0191 0.0239  -0.0561 395 PHE A CE1 
4207 C CE2 . PHE B 209 ? 0.8405 0.8519 0.7834 -0.0099 -0.0182 -0.0698 395 PHE A CE2 
4208 C CZ  . PHE B 209 ? 0.8405 0.8639 0.7471 -0.0035 0.0017  -0.0753 395 PHE A CZ  
4209 N N   . LEU B 210 ? 0.8774 0.8866 0.7565 -0.1192 0.0692  0.0494  396 LEU A N   
4210 C CA  . LEU B 210 ? 0.9229 0.9252 0.7934 -0.1451 0.0835  0.0753  396 LEU A CA  
4211 C C   . LEU B 210 ? 0.9520 0.9577 0.8244 -0.1513 0.0786  0.0832  396 LEU A C   
4212 O O   . LEU B 210 ? 0.9959 0.9883 0.8877 -0.1661 0.0689  0.0983  396 LEU A O   
4213 C CB  . LEU B 210 ? 0.9090 0.9177 0.7385 -0.1539 0.1131  0.0839  396 LEU A CB  
4214 C CG  . LEU B 210 ? 0.9468 0.9506 0.7752 -0.1521 0.1203  0.0812  396 LEU A CG  
4215 C CD1 . LEU B 210 ? 0.8894 0.9014 0.6755 -0.1586 0.1502  0.0882  396 LEU A CD1 
4216 C CD2 . LEU B 210 ? 0.9500 0.9350 0.8092 -0.1685 0.1148  0.0954  396 LEU A CD2 
4217 N N   . THR B 211 ? 0.9405 0.9628 0.7934 -0.1400 0.0849  0.0730  397 THR A N   
4218 C CA  . THR B 211 ? 0.8944 0.9223 0.7513 -0.1442 0.0800  0.0788  397 THR A CA  
4219 C C   . THR B 211 ? 0.8076 0.8496 0.6719 -0.1201 0.0716  0.0552  397 THR A C   
4220 O O   . THR B 211 ? 0.8547 0.9035 0.7042 -0.1031 0.0780  0.0369  397 THR A O   
4221 C CB  . THR B 211 ? 0.9865 1.0208 0.8072 -0.1616 0.1036  0.0958  397 THR A CB  
4222 O OG1 . THR B 211 ? 0.8616 0.9112 0.6497 -0.1508 0.1242  0.0841  397 THR A OG1 
4223 C CG2 . THR B 211 ? 0.9851 1.0029 0.7945 -0.1865 0.1150  0.1191  397 THR A CG2 
4224 N N   . LEU B 212 ? 0.8495 0.8941 0.7365 -0.1190 0.0576  0.0560  398 LEU A N   
4225 C CA  . LEU B 212 ? 0.8318 0.8886 0.7302 -0.0980 0.0507  0.0350  398 LEU A CA  
4226 C C   . LEU B 212 ? 0.8465 0.9166 0.7355 -0.1042 0.0604  0.0425  398 LEU A C   
4227 O O   . LEU B 212 ? 0.8482 0.9130 0.7446 -0.1224 0.0550  0.0629  398 LEU A O   
4228 C CB  . LEU B 212 ? 0.8129 0.8609 0.7573 -0.0879 0.0221  0.0259  398 LEU A CB  
4229 C CG  . LEU B 212 ? 0.8021 0.8395 0.7618 -0.0756 0.0090  0.0111  398 LEU A CG  
4230 C CD1 . LEU B 212 ? 0.8111 0.8375 0.8176 -0.0724 -0.0185 0.0089  398 LEU A CD1 
4231 C CD2 . LEU B 212 ? 0.8076 0.8536 0.7501 -0.0526 0.0154  -0.0151 398 LEU A CD2 
4232 N N   . PRO B 213 ? 0.9156 1.0012 0.7882 -0.0900 0.0741  0.0267  399 PRO A N   
4233 C CA  . PRO B 213 ? 0.7917 0.8911 0.6536 -0.0971 0.0866  0.0341  399 PRO A CA  
4234 C C   . PRO B 213 ? 0.7807 0.8816 0.6832 -0.0967 0.0657  0.0365  399 PRO A C   
4235 O O   . PRO B 213 ? 0.7886 0.8820 0.7264 -0.0862 0.0438  0.0274  399 PRO A O   
4236 C CB  . PRO B 213 ? 0.7757 0.8890 0.6141 -0.0783 0.1060  0.0125  399 PRO A CB  
4237 C CG  . PRO B 213 ? 0.7914 0.8959 0.6175 -0.0654 0.1060  -0.0020 399 PRO A CG  
4238 C CD  . PRO B 213 ? 0.8548 0.9443 0.7165 -0.0670 0.0793  0.0011  399 PRO A CD  
4239 N N   . PRO B 214 ? 0.7773 0.8873 0.6776 -0.1084 0.0706  0.0492  400 PRO A N   
4240 C CA  . PRO B 214 ? 0.7831 0.8964 0.7247 -0.1058 0.0503  0.0498  400 PRO A CA  
4241 C C   . PRO B 214 ? 0.7877 0.9114 0.7540 -0.0804 0.0475  0.0231  400 PRO A C   
4242 O O   . PRO B 214 ? 0.7951 0.9158 0.8040 -0.0730 0.0255  0.0185  400 PRO A O   
4243 C CB  . PRO B 214 ? 0.7786 0.9014 0.7052 -0.1224 0.0607  0.0665  400 PRO A CB  
4244 C CG  . PRO B 214 ? 0.7726 0.8895 0.6533 -0.1398 0.0804  0.0814  400 PRO A CG  
4245 C CD  . PRO B 214 ? 0.7694 0.8856 0.6313 -0.1254 0.0933  0.0644  400 PRO A CD  
4246 N N   . VAL B 215 ? 0.7792 0.7144 0.6333 -0.0814 -0.0110 0.1359  401 VAL A N   
4247 C CA  . VAL B 215 ? 0.8331 0.7696 0.6962 -0.0679 -0.0150 0.1464  401 VAL A CA  
4248 C C   . VAL B 215 ? 0.8300 0.7486 0.7049 -0.0573 -0.0138 0.1334  401 VAL A C   
4249 O O   . VAL B 215 ? 0.8533 0.7621 0.7308 -0.0597 -0.0157 0.1208  401 VAL A O   
4250 C CB  . VAL B 215 ? 0.8825 0.8310 0.7437 -0.0712 -0.0220 0.1553  401 VAL A CB  
4251 C CG1 . VAL B 215 ? 0.7577 0.7095 0.6271 -0.0570 -0.0235 0.1662  401 VAL A CG1 
4252 C CG2 . VAL B 215 ? 0.7902 0.7589 0.6413 -0.0830 -0.0254 0.1659  401 VAL A CG2 
4253 N N   . LEU B 216 ? 0.7551 0.6688 0.6374 -0.0453 -0.0115 0.1362  402 LEU A N   
4254 C CA  . LEU B 216 ? 0.7504 0.6485 0.6441 -0.0354 -0.0114 0.1230  402 LEU A CA  
4255 C C   . LEU B 216 ? 0.7459 0.6416 0.6406 -0.0221 -0.0164 0.1295  402 LEU A C   
4256 O O   . LEU B 216 ? 0.8225 0.7239 0.7167 -0.0146 -0.0152 0.1413  402 LEU A O   
4257 C CB  . LEU B 216 ? 0.8083 0.7008 0.7095 -0.0337 -0.0046 0.1187  402 LEU A CB  
4258 C CG  . LEU B 216 ? 0.7744 0.6538 0.6913 -0.0284 -0.0035 0.1007  402 LEU A CG  
4259 C CD1 . LEU B 216 ? 0.7517 0.6290 0.6738 -0.0368 -0.0019 0.0844  402 LEU A CD1 
4260 C CD2 . LEU B 216 ? 0.7534 0.6287 0.6778 -0.0277 0.0038  0.1008  402 LEU A CD2 
4261 N N   . HIS B 217 ? 0.7461 0.6326 0.6413 -0.0185 -0.0216 0.1221  403 HIS A N   
4262 C CA  . HIS B 217 ? 0.7637 0.6458 0.6558 -0.0062 -0.0257 0.1272  403 HIS A CA  
4263 C C   . HIS B 217 ? 0.8188 0.6860 0.7182 0.0054  -0.0282 0.1142  403 HIS A C   
4264 O O   . HIS B 217 ? 0.8179 0.6742 0.7226 0.0057  -0.0326 0.1006  403 HIS A O   
4265 C CB  . HIS B 217 ? 0.7772 0.6564 0.6617 -0.0098 -0.0304 0.1296  403 HIS A CB  
4266 C CG  . HIS B 217 ? 0.8328 0.7290 0.7114 -0.0184 -0.0290 0.1448  403 HIS A CG  
4267 N ND1 . HIS B 217 ? 0.7806 0.6948 0.6605 -0.0201 -0.0254 0.1563  403 HIS A ND1 
4268 C CD2 . HIS B 217 ? 0.7972 0.6953 0.6702 -0.0259 -0.0314 0.1504  403 HIS A CD2 
4269 C CE1 . HIS B 217 ? 0.7799 0.7095 0.6570 -0.0281 -0.0264 0.1675  403 HIS A CE1 
4270 N NE2 . HIS B 217 ? 0.8012 0.7212 0.6743 -0.0327 -0.0294 0.1640  403 HIS A NE2 
4271 N N   . LEU B 218 ? 0.7569 0.6239 0.6577 0.0154  -0.0264 0.1177  404 LEU A N   
4272 C CA  . LEU B 218 ? 0.7495 0.6035 0.6573 0.0259  -0.0295 0.1050  404 LEU A CA  
4273 C C   . LEU B 218 ? 0.7568 0.6057 0.6534 0.0390  -0.0339 0.1088  404 LEU A C   
4274 O O   . LEU B 218 ? 0.8079 0.6637 0.6984 0.0443  -0.0297 0.1203  404 LEU A O   
4275 C CB  . LEU B 218 ? 0.7486 0.6023 0.6661 0.0264  -0.0235 0.1038  404 LEU A CB  
4276 C CG  . LEU B 218 ? 0.7460 0.6043 0.6713 0.0131  -0.0168 0.1019  404 LEU A CG  
4277 C CD1 . LEU B 218 ? 0.7501 0.6042 0.6829 0.0144  -0.0105 0.1031  404 LEU A CD1 
4278 C CD2 . LEU B 218 ? 0.7792 0.6327 0.7151 0.0078  -0.0189 0.0846  404 LEU A CD2 
4279 N N   . GLN B 219 ? 0.7638 0.6007 0.6572 0.0450  -0.0422 0.0990  405 GLN A N   
4280 C CA  . GLN B 219 ? 0.7759 0.6053 0.6550 0.0579  -0.0469 0.1005  405 GLN A CA  
4281 C C   . GLN B 219 ? 0.8349 0.6545 0.7209 0.0675  -0.0513 0.0860  405 GLN A C   
4282 O O   . GLN B 219 ? 0.8407 0.6547 0.7411 0.0660  -0.0569 0.0713  405 GLN A O   
4283 C CB  . GLN B 219 ? 0.7865 0.6066 0.6534 0.0590  -0.0548 0.1007  405 GLN A CB  
4284 C CG  . GLN B 219 ? 0.8559 0.6833 0.7104 0.0521  -0.0503 0.1171  405 GLN A CG  
4285 C CD  . GLN B 219 ? 0.8811 0.7148 0.7449 0.0372  -0.0481 0.1185  405 GLN A CD  
4286 O OE1 . GLN B 219 ? 0.9002 0.7290 0.7765 0.0332  -0.0509 0.1059  405 GLN A OE1 
4287 N NE2 . GLN B 219 ? 0.8785 0.7242 0.7367 0.0285  -0.0428 0.1327  405 GLN A NE2 
4288 N N   . LEU B 220 ? 0.8902 0.7085 0.7676 0.0773  -0.0487 0.0891  406 LEU A N   
4289 C CA  . LEU B 220 ? 0.8109 0.6194 0.6942 0.0858  -0.0522 0.0752  406 LEU A CA  
4290 C C   . LEU B 220 ? 0.9609 0.7581 0.8269 0.0974  -0.0629 0.0678  406 LEU A C   
4291 O O   . LEU B 220 ? 0.9591 0.7556 0.8040 0.1054  -0.0607 0.0759  406 LEU A O   
4292 C CB  . LEU B 220 ? 0.7983 0.6096 0.6822 0.0900  -0.0427 0.0817  406 LEU A CB  
4293 C CG  . LEU B 220 ? 0.7853 0.6064 0.6830 0.0799  -0.0332 0.0912  406 LEU A CG  
4294 C CD1 . LEU B 220 ? 0.7923 0.6102 0.6931 0.0869  -0.0264 0.0945  406 LEU A CD1 
4295 C CD2 . LEU B 220 ? 0.7874 0.6065 0.7031 0.0689  -0.0347 0.0807  406 LEU A CD2 
4296 N N   . MET B 221 ? 0.9290 0.7184 0.8041 0.0987  -0.0746 0.0523  407 MET A N   
4297 C CA  . MET B 221 ? 0.9148 0.6930 0.7727 0.1094  -0.0882 0.0454  407 MET A CA  
4298 C C   . MET B 221 ? 0.9894 0.7598 0.8395 0.1203  -0.0921 0.0345  407 MET A C   
4299 O O   . MET B 221 ? 1.0748 0.8395 0.9368 0.1236  -0.1030 0.0169  407 MET A O   
4300 C CB  . MET B 221 ? 0.8895 0.6645 0.7640 0.1074  -0.1005 0.0327  407 MET A CB  
4301 C CG  . MET B 221 ? 0.8928 0.6724 0.7739 0.0974  -0.0973 0.0407  407 MET A CG  
4302 S SD  . MET B 221 ? 1.0019 0.7735 0.8511 0.1004  -0.0999 0.0580  407 MET A SD  
4303 C CE  . MET B 221 ? 0.8231 0.6089 0.6735 0.0866  -0.0825 0.0756  407 MET A CE  
4304 N N   . ARG B 222 ? 0.8781 0.6490 0.7089 0.1261  -0.0831 0.0441  408 ARG A N   
4305 C CA  . ARG B 222 ? 1.0007 0.7626 0.8199 0.1373  -0.0855 0.0333  408 ARG A CA  
4306 C C   . ARG B 222 ? 1.0642 0.8177 0.8482 0.1481  -0.0931 0.0348  408 ARG A C   
4307 O O   . ARG B 222 ? 1.1396 0.8941 0.9003 0.1543  -0.0840 0.0441  408 ARG A O   
4308 C CB  . ARG B 222 ? 0.9934 0.7597 0.8152 0.1386  -0.0700 0.0405  408 ARG A CB  
4309 C CG  . ARG B 222 ? 0.9997 0.7799 0.8156 0.1346  -0.0572 0.0621  408 ARG A CG  
4310 C CD  . ARG B 222 ? 0.9684 0.7531 0.7838 0.1407  -0.0439 0.0686  408 ARG A CD  
4311 N NE  . ARG B 222 ? 0.8993 0.6830 0.7400 0.1363  -0.0392 0.0654  408 ARG A NE  
4312 C CZ  . ARG B 222 ? 0.9515 0.7222 0.7979 0.1426  -0.0394 0.0523  408 ARG A CZ  
4313 N NH1 . ARG B 222 ? 1.0095 0.7683 0.8385 0.1538  -0.0449 0.0390  408 ARG A NH1 
4314 N NH2 . ARG B 222 ? 0.8674 0.6355 0.7362 0.1370  -0.0341 0.0525  408 ARG A NH2 
4315 N N   . PHE B 223 ? 1.1157 0.8614 0.8958 0.1509  -0.1101 0.0253  409 PHE A N   
4316 C CA  . PHE B 223 ? 1.1928 0.9276 0.9362 0.1616  -0.1197 0.0263  409 PHE A CA  
4317 C C   . PHE B 223 ? 1.2012 0.9274 0.9482 0.1662  -0.1420 0.0107  409 PHE A C   
4318 O O   . PHE B 223 ? 1.1699 0.9010 0.9498 0.1600  -0.1484 0.0019  409 PHE A O   
4319 C CB  . PHE B 223 ? 1.2066 0.9426 0.9282 0.1589  -0.1133 0.0478  409 PHE A CB  
4320 C CG  . PHE B 223 ? 1.1727 0.9072 0.9069 0.1521  -0.1219 0.0518  409 PHE A CG  
4321 C CD1 . PHE B 223 ? 1.1133 0.8586 0.8789 0.1399  -0.1148 0.0545  409 PHE A CD1 
4322 C CD2 . PHE B 223 ? 1.1762 0.8970 0.8889 0.1585  -0.1372 0.0529  409 PHE A CD2 
4323 C CE1 . PHE B 223 ? 1.1135 0.8563 0.8904 0.1342  -0.1217 0.0563  409 PHE A CE1 
4324 C CE2 . PHE B 223 ? 1.1876 0.9046 0.9129 0.1536  -0.1450 0.0560  409 PHE A CE2 
4325 C CZ  . PHE B 223 ? 1.1410 0.8692 0.8993 0.1414  -0.1368 0.0568  409 PHE A CZ  
4326 N N   . MET B 224 ? 1.3113 1.0259 1.0239 0.1777  -0.1537 0.0074  410 MET A N   
4327 C CA  . MET B 224 ? 1.2964 1.0027 1.0070 0.1846  -0.1779 -0.0060 410 MET A CA  
4328 C C   . MET B 224 ? 1.2950 0.9872 0.9556 0.1960  -0.1873 0.0012  410 MET A C   
4329 O O   . MET B 224 ? 1.4510 1.1344 1.1020 0.2022  -0.2073 -0.0013 410 MET A O   
4330 C CB  . MET B 224 ? 1.2966 1.0044 1.0295 0.1867  -0.1880 -0.0308 410 MET A CB  
4331 C CG  . MET B 224 ? 1.2752 0.9767 0.9845 0.1935  -0.1828 -0.0388 410 MET A CG  
4332 S SD  . MET B 224 ? 1.7112 1.4097 1.4402 0.1967  -0.2011 -0.0705 410 MET A SD  
4333 C CE  . MET B 224 ? 1.3531 1.0654 1.1442 0.1813  -0.1927 -0.0765 410 MET A CE  
4334 N N   . GLN B 228 ? 1.8176 1.4428 1.3006 0.2803  -0.3723 -0.0807 414 GLN A N   
4335 C CA  . GLN B 228 ? 1.8180 1.4265 1.2369 0.2840  -0.3572 -0.0598 414 GLN A CA  
4336 C C   . GLN B 228 ? 1.9170 1.5281 1.3470 0.2729  -0.3256 -0.0360 414 GLN A C   
4337 O O   . GLN B 228 ? 1.8770 1.5032 1.3564 0.2619  -0.3093 -0.0404 414 GLN A O   
4338 C CB  . GLN B 228 ? 1.7922 1.3978 1.1776 0.2869  -0.3499 -0.0749 414 GLN A CB  
4339 C CG  . GLN B 228 ? 1.8687 1.4856 1.2854 0.2761  -0.3204 -0.0809 414 GLN A CG  
4340 C CD  . GLN B 228 ? 1.9145 1.5250 1.2936 0.2807  -0.3111 -0.0940 414 GLN A CD  
4341 O OE1 . GLN B 228 ? 1.9861 1.5852 1.3185 0.2911  -0.3290 -0.1034 414 GLN A OE1 
4342 N NE2 . GLN B 228 ? 1.5399 1.1569 0.9372 0.2738  -0.2830 -0.0943 414 GLN A NE2 
4343 N N   . THR B 229 ? 1.9750 1.5714 1.3598 0.2750  -0.3176 -0.0104 415 THR A N   
4344 C CA  . THR B 229 ? 2.0555 1.6549 1.4497 0.2638  -0.2891 0.0122  415 THR A CA  
4345 C C   . THR B 229 ? 2.1622 1.7448 1.4943 0.2665  -0.2781 0.0365  415 THR A C   
4346 O O   . THR B 229 ? 2.1691 1.7334 1.4595 0.2762  -0.2975 0.0439  415 THR A O   
4347 C CB  . THR B 229 ? 2.0311 1.6336 1.4696 0.2579  -0.2947 0.0201  415 THR A CB  
4348 O OG1 . THR B 229 ? 1.9757 1.5959 1.4734 0.2537  -0.3009 -0.0018 415 THR A OG1 
4349 C CG2 . THR B 229 ? 1.9961 1.6006 1.4411 0.2455  -0.2671 0.0436  415 THR A CG2 
4350 N N   . ASP B 230 ? 2.4059 1.9953 1.7320 0.2581  -0.2472 0.0491  416 ASP A N   
4351 C CA  . ASP B 230 ? 2.3647 1.9419 1.6487 0.2553  -0.2325 0.0770  416 ASP A CA  
4352 C C   . ASP B 230 ? 2.2677 1.8605 1.5808 0.2411  -0.2019 0.0907  416 ASP A C   
4353 O O   . ASP B 230 ? 2.1780 1.7650 1.4695 0.2348  -0.1865 0.1144  416 ASP A O   
4354 C CB  . ASP B 230 ? 2.3002 1.8669 1.5188 0.2639  -0.2277 0.0786  416 ASP A CB  
4355 C CG  . ASP B 230 ? 2.4256 1.9770 1.5966 0.2611  -0.2150 0.1083  416 ASP A CG  
4356 O OD1 . ASP B 230 ? 2.5592 2.0899 1.7077 0.2651  -0.2341 0.1210  416 ASP A OD1 
4357 O OD2 . ASP B 230 ? 2.4471 2.0074 1.6067 0.2542  -0.1854 0.1195  416 ASP A OD2 
4358 N N   . GLN B 231 ? 2.0621 1.6745 1.4252 0.2354  -0.1939 0.0761  417 GLN A N   
4359 C CA  . GLN B 231 ? 1.8492 1.4790 1.2413 0.2230  -0.1667 0.0868  417 GLN A CA  
4360 C C   . GLN B 231 ? 1.7060 1.3508 1.1592 0.2160  -0.1690 0.0738  417 GLN A C   
4361 O O   . GLN B 231 ? 1.7805 1.4246 1.2549 0.2205  -0.1884 0.0544  417 GLN A O   
4362 C CB  . GLN B 231 ? 1.8573 1.4974 1.2306 0.2247  -0.1432 0.0860  417 GLN A CB  
4363 C CG  . GLN B 231 ? 1.8939 1.5236 1.2082 0.2288  -0.1326 0.1015  417 GLN A CG  
4364 C CD  . GLN B 231 ? 1.7784 1.4212 1.0807 0.2317  -0.1083 0.0971  417 GLN A CD  
4365 O OE1 . GLN B 231 ? 1.6988 1.3534 1.0307 0.2338  -0.1045 0.0794  417 GLN A OE1 
4366 N NE2 . GLN B 231 ? 1.7948 1.4357 1.0556 0.2315  -0.0906 0.1137  417 GLN A NE2 
4367 N N   . ASN B 232 ? 1.5994 1.2588 1.0805 0.2040  -0.1488 0.0852  418 ASN A N   
4368 C CA  . ASN B 232 ? 1.5178 1.1933 1.0518 0.1961  -0.1447 0.0752  418 ASN A CA  
4369 C C   . ASN B 232 ? 1.4142 1.1022 0.9549 0.1980  -0.1290 0.0660  418 ASN A C   
4370 O O   . ASN B 232 ? 1.3655 1.0612 0.8915 0.1966  -0.1088 0.0783  418 ASN A O   
4371 C CB  . ASN B 232 ? 1.4293 1.1131 0.9872 0.1823  -0.1327 0.0923  418 ASN A CB  
4372 C CG  . ASN B 232 ? 1.3820 1.0506 0.9352 0.1805  -0.1471 0.1011  418 ASN A CG  
4373 O OD1 . ASN B 232 ? 1.3349 1.0005 0.9136 0.1815  -0.1634 0.0895  418 ASN A OD1 
4374 N ND2 . ASN B 232 ? 1.3547 1.0135 0.8769 0.1776  -0.1401 0.1218  418 ASN A ND2 
4375 N N   . ILE B 233 ? 1.3374 1.0274 0.9018 0.2012  -0.1378 0.0445  419 ILE A N   
4376 C CA  . ILE B 233 ? 1.3122 1.0086 0.8821 0.2046  -0.1255 0.0335  419 ILE A CA  
4377 C C   . ILE B 233 ? 1.3198 1.0304 0.9383 0.1944  -0.1154 0.0326  419 ILE A C   
4378 O O   . ILE B 233 ? 1.3508 1.0652 0.9988 0.1860  -0.1221 0.0332  419 ILE A O   
4379 C CB  . ILE B 233 ? 1.3872 1.0722 0.9451 0.2149  -0.1428 0.0091  419 ILE A CB  
4380 C CG1 . ILE B 233 ? 1.4610 1.1476 1.0190 0.2199  -0.1299 -0.0033 419 ILE A CG1 
4381 C CG2 . ILE B 233 ? 1.3564 1.0413 0.9508 0.2113  -0.1626 -0.0062 419 ILE A CG2 
4382 C CD1 . ILE B 233 ? 1.3481 1.0213 0.8850 0.2303  -0.1459 -0.0273 419 ILE A CD1 
4383 N N   . LYS B 234 ? 1.2433 0.9610 0.8691 0.1961  -0.0992 0.0306  420 LYS A N   
4384 C CA  . LYS B 234 ? 1.2102 0.9400 0.8768 0.1875  -0.0884 0.0323  420 LYS A CA  
4385 C C   . LYS B 234 ? 1.2184 0.9419 0.9081 0.1890  -0.0953 0.0107  420 LYS A C   
4386 O O   . LYS B 234 ? 1.2368 0.9493 0.9091 0.1985  -0.1010 -0.0052 420 LYS A O   
4387 C CB  . LYS B 234 ? 1.1664 0.9087 0.8313 0.1883  -0.0661 0.0462  420 LYS A CB  
4388 C CG  . LYS B 234 ? 1.1869 0.9392 0.8382 0.1831  -0.0569 0.0684  420 LYS A CG  
4389 C CD  . LYS B 234 ? 1.1642 0.9245 0.7932 0.1904  -0.0389 0.0771  420 LYS A CD  
4390 C CE  . LYS B 234 ? 1.2363 1.0071 0.8892 0.1941  -0.0250 0.0741  420 LYS A CE  
4391 N NZ  . LYS B 234 ? 1.1465 0.9044 0.7854 0.2077  -0.0252 0.0550  420 LYS A NZ  
4392 N N   . ILE B 235 ? 1.1535 0.8835 0.8816 0.1786  -0.0946 0.0097  421 ILE A N   
4393 C CA  . ILE B 235 ? 1.1571 0.8823 0.9129 0.1766  -0.0968 -0.0073 421 ILE A CA  
4394 C C   . ILE B 235 ? 1.2250 0.9553 0.9937 0.1755  -0.0777 0.0014  421 ILE A C   
4395 O O   . ILE B 235 ? 1.2147 0.9564 1.0039 0.1662  -0.0688 0.0153  421 ILE A O   
4396 C CB  . ILE B 235 ? 1.1034 0.8324 0.8926 0.1655  -0.1065 -0.0136 421 ILE A CB  
4397 C CG1 . ILE B 235 ? 1.2088 0.9332 0.9879 0.1690  -0.1272 -0.0229 421 ILE A CG1 
4398 C CG2 . ILE B 235 ? 1.0474 0.7722 0.8669 0.1608  -0.1054 -0.0287 421 ILE A CG2 
4399 C CD1 . ILE B 235 ? 1.1035 0.8337 0.9186 0.1597  -0.1368 -0.0316 421 ILE A CD1 
4400 N N   . ASN B 236 ? 1.1829 0.9045 0.9392 0.1858  -0.0719 -0.0069 422 ASN A N   
4401 C CA  . ASN B 236 ? 1.1571 0.8817 0.9253 0.1880  -0.0547 0.0008  422 ASN A CA  
4402 C C   . ASN B 236 ? 1.1902 0.9063 0.9912 0.1819  -0.0542 -0.0085 422 ASN A C   
4403 O O   . ASN B 236 ? 1.2672 0.9779 1.0756 0.1869  -0.0430 -0.0074 422 ASN A O   
4404 C CB  . ASN B 236 ? 1.1836 0.9016 0.9244 0.2030  -0.0470 -0.0044 422 ASN A CB  
4405 C CG  . ASN B 236 ? 1.3027 1.0296 1.0098 0.2082  -0.0437 0.0070  422 ASN A CG  
4406 O OD1 . ASN B 236 ? 1.3189 1.0604 1.0284 0.2009  -0.0401 0.0256  422 ASN A OD1 
4407 N ND2 . ASN B 236 ? 1.2974 1.0144 0.9714 0.2201  -0.0446 -0.0043 422 ASN A ND2 
4408 N N   . ASP B 237 ? 1.1418 0.8561 0.9633 0.1713  -0.0654 -0.0173 423 ASP A N   
4409 C CA  . ASP B 237 ? 1.1394 0.8445 0.9914 0.1636  -0.0646 -0.0271 423 ASP A CA  
4410 C C   . ASP B 237 ? 1.0615 0.7737 0.9328 0.1566  -0.0498 -0.0084 423 ASP A C   
4411 O O   . ASP B 237 ? 1.0312 0.7594 0.8987 0.1537  -0.0437 0.0107  423 ASP A O   
4412 C CB  . ASP B 237 ? 1.1958 0.9021 1.0676 0.1532  -0.0787 -0.0403 423 ASP A CB  
4413 C CG  . ASP B 237 ? 1.2149 0.9146 1.0699 0.1604  -0.0966 -0.0596 423 ASP A CG  
4414 O OD1 . ASP B 237 ? 1.2077 0.9019 1.0303 0.1729  -0.0974 -0.0608 423 ASP A OD1 
4415 O OD2 . ASP B 237 ? 1.1781 0.8794 1.0523 0.1537  -0.1099 -0.0734 423 ASP A OD2 
4416 N N   . ARG B 238 ? 1.0173 0.7163 0.9088 0.1534  -0.0448 -0.0139 424 ARG A N   
4417 C CA  . ARG B 238 ? 1.0129 0.7155 0.9219 0.1466  -0.0324 0.0036  424 ARG A CA  
4418 C C   . ARG B 238 ? 1.0897 0.8038 1.0166 0.1301  -0.0342 0.0093  424 ARG A C   
4419 O O   . ARG B 238 ? 1.0505 0.7618 0.9912 0.1219  -0.0427 -0.0059 424 ARG A O   
4420 C CB  . ARG B 238 ? 0.9912 0.6718 0.9150 0.1478  -0.0268 -0.0036 424 ARG A CB  
4421 C CG  . ARG B 238 ? 0.9886 0.6698 0.9278 0.1415  -0.0151 0.0160  424 ARG A CG  
4422 C CD  . ARG B 238 ? 1.0085 0.6641 0.9654 0.1385  -0.0111 0.0081  424 ARG A CD  
4423 N NE  . ARG B 238 ? 0.9658 0.6190 0.9329 0.1346  -0.0003 0.0292  424 ARG A NE  
4424 C CZ  . ARG B 238 ? 1.1264 0.7755 1.0885 0.1474  0.0075  0.0427  424 ARG A CZ  
4425 N NH1 . ARG B 238 ? 1.1936 0.8416 1.1414 0.1647  0.0080  0.0368  424 ARG A NH1 
4426 N NH2 . ARG B 238 ? 1.1204 0.7671 1.0917 0.1434  0.0150  0.0625  424 ARG A NH2 
4427 N N   . PHE B 239 ? 1.0588 0.7873 0.9863 0.1254  -0.0260 0.0304  425 PHE A N   
4428 C CA  . PHE B 239 ? 0.9681 0.7083 0.9091 0.1101  -0.0256 0.0368  425 PHE A CA  
4429 C C   . PHE B 239 ? 0.9150 0.6612 0.8603 0.1055  -0.0143 0.0580  425 PHE A C   
4430 O O   . PHE B 239 ? 1.0000 0.7560 0.9333 0.1132  -0.0099 0.0729  425 PHE A O   
4431 C CB  . PHE B 239 ? 0.9543 0.7098 0.8833 0.1090  -0.0329 0.0385  425 PHE A CB  
4432 C CG  . PHE B 239 ? 0.9206 0.6876 0.8622 0.0944  -0.0324 0.0427  425 PHE A CG  
4433 C CD1 . PHE B 239 ? 0.8852 0.6502 0.8443 0.0863  -0.0386 0.0267  425 PHE A CD1 
4434 C CD2 . PHE B 239 ? 0.9044 0.6856 0.8407 0.0890  -0.0259 0.0615  425 PHE A CD2 
4435 C CE1 . PHE B 239 ? 0.8921 0.6680 0.8627 0.0737  -0.0366 0.0291  425 PHE A CE1 
4436 C CE2 . PHE B 239 ? 0.8394 0.6301 0.7847 0.0756  -0.0250 0.0637  425 PHE A CE2 
4437 C CZ  . PHE B 239 ? 0.8629 0.6504 0.8248 0.0684  -0.0295 0.0473  425 PHE A CZ  
4438 N N   . GLU B 240 ? 0.8517 0.5931 0.8138 0.0928  -0.0096 0.0594  426 GLU A N   
4439 C CA  . GLU B 240 ? 0.8514 0.5948 0.8158 0.0884  0.0000  0.0795  426 GLU A CA  
4440 C C   . GLU B 240 ? 0.8980 0.6598 0.8618 0.0750  0.0015  0.0899  426 GLU A C   
4441 O O   . GLU B 240 ? 0.9644 0.7301 0.9360 0.0646  -0.0016 0.0787  426 GLU A O   
4442 C CB  . GLU B 240 ? 0.8838 0.6056 0.8632 0.0829  0.0060  0.0766  426 GLU A CB  
4443 C CG  . GLU B 240 ? 0.9101 0.6099 0.8911 0.0954  0.0051  0.0653  426 GLU A CG  
4444 C CD  . GLU B 240 ? 1.0458 0.7214 1.0435 0.0875  0.0110  0.0616  426 GLU A CD  
4445 O OE1 . GLU B 240 ? 1.0948 0.7722 1.1021 0.0717  0.0162  0.0677  426 GLU A OE1 
4446 O OE2 . GLU B 240 ? 1.0381 0.6919 1.0384 0.0965  0.0111  0.0524  426 GLU A OE2 
4447 N N   . PHE B 241 ? 0.8283 0.6022 0.7837 0.0757  0.0057  0.1103  427 PHE A N   
4448 C CA  . PHE B 241 ? 0.8478 0.6377 0.8003 0.0625  0.0074  0.1210  427 PHE A CA  
4449 C C   . PHE B 241 ? 0.8918 0.6817 0.8423 0.0605  0.0139  0.1413  427 PHE A C   
4450 O O   . PHE B 241 ? 0.8856 0.6759 0.8328 0.0730  0.0146  0.1528  427 PHE A O   
4451 C CB  . PHE B 241 ? 0.7998 0.6097 0.7409 0.0640  0.0024  0.1252  427 PHE A CB  
4452 C CG  . PHE B 241 ? 0.8865 0.7042 0.8189 0.0780  0.0022  0.1359  427 PHE A CG  
4453 C CD1 . PHE B 241 ? 0.8557 0.6677 0.7829 0.0908  -0.0008 0.1261  427 PHE A CD1 
4454 C CD2 . PHE B 241 ? 0.9508 0.7834 0.8802 0.0782  0.0051  0.1556  427 PHE A CD2 
4455 C CE1 . PHE B 241 ? 0.9234 0.7444 0.8433 0.1034  0.0015  0.1353  427 PHE A CE1 
4456 C CE2 . PHE B 241 ? 0.8897 0.7332 0.8155 0.0911  0.0060  0.1649  427 PHE A CE2 
4457 C CZ  . PHE B 241 ? 0.9163 0.7541 0.8376 0.1036  0.0054  0.1546  427 PHE A CZ  
4458 N N   . PRO B 242 ? 0.8270 0.6166 0.7790 0.0458  0.0186  0.1462  428 PRO A N   
4459 C CA  . PRO B 242 ? 0.8418 0.6286 0.7888 0.0436  0.0236  0.1665  428 PRO A CA  
4460 C C   . PRO B 242 ? 0.8649 0.6753 0.7992 0.0418  0.0206  0.1835  428 PRO A C   
4461 O O   . PRO B 242 ? 0.8165 0.6443 0.7463 0.0366  0.0167  0.1790  428 PRO A O   
4462 C CB  . PRO B 242 ? 0.8981 0.6742 0.8496 0.0267  0.0309  0.1621  428 PRO A CB  
4463 C CG  . PRO B 242 ? 0.8313 0.6198 0.7865 0.0177  0.0285  0.1451  428 PRO A CG  
4464 C CD  . PRO B 242 ? 0.8193 0.6104 0.7777 0.0308  0.0200  0.1326  428 PRO A CD  
4465 N N   . GLU B 243 ? 0.8981 0.7083 0.8278 0.0464  0.0216  0.2034  429 GLU A N   
4466 C CA  . GLU B 243 ? 0.8938 0.7275 0.8127 0.0431  0.0175  0.2203  429 GLU A CA  
4467 C C   . GLU B 243 ? 0.9301 0.7707 0.8387 0.0236  0.0194  0.2192  429 GLU A C   
4468 O O   . GLU B 243 ? 0.9484 0.8104 0.8488 0.0173  0.0147  0.2226  429 GLU A O   
4469 C CB  . GLU B 243 ? 0.9464 0.7774 0.8635 0.0526  0.0169  0.2420  429 GLU A CB  
4470 C CG  . GLU B 243 ? 1.0707 0.9289 0.9789 0.0507  0.0102  0.2600  429 GLU A CG  
4471 C CD  . GLU B 243 ? 1.1611 1.0177 1.0703 0.0631  0.0074  0.2818  429 GLU A CD  
4472 O OE1 . GLU B 243 ? 1.1292 0.9591 1.0384 0.0657  0.0121  0.2869  429 GLU A OE1 
4473 O OE2 . GLU B 243 ? 1.0383 0.9201 0.9500 0.0705  0.0004  0.2938  429 GLU A OE2 
4474 N N   . GLN B 244 ? 0.9926 0.8152 0.9019 0.0132  0.0270  0.2136  430 GLN A N   
4475 C CA  . GLN B 244 ? 0.9000 0.7273 0.7999 -0.0054 0.0317  0.2100  430 GLN A CA  
4476 C C   . GLN B 244 ? 0.8863 0.7038 0.8002 -0.0123 0.0372  0.1868  430 GLN A C   
4477 O O   . GLN B 244 ? 0.8576 0.6556 0.7841 -0.0097 0.0418  0.1803  430 GLN A O   
4478 C CB  . GLN B 244 ? 0.9044 0.7220 0.7908 -0.0131 0.0374  0.2277  430 GLN A CB  
4479 C CG  . GLN B 244 ? 0.9763 0.8048 0.8500 -0.0053 0.0298  0.2516  430 GLN A CG  
4480 C CD  . GLN B 244 ? 1.2076 1.0238 1.0645 -0.0125 0.0343  0.2704  430 GLN A CD  
4481 O OE1 . GLN B 244 ? 1.2666 1.0584 1.1259 -0.0175 0.0440  0.2691  430 GLN A OE1 
4482 N NE2 . GLN B 244 ? 1.3382 1.1709 1.1770 -0.0140 0.0269  0.2883  430 GLN A NE2 
4483 N N   . LEU B 245 ? 0.8879 0.7188 0.8011 -0.0210 0.0362  0.1739  431 LEU A N   
4484 C CA  . LEU B 245 ? 0.8224 0.6490 0.7521 -0.0251 0.0387  0.1507  431 LEU A CA  
4485 C C   . LEU B 245 ? 0.9095 0.7403 0.8371 -0.0426 0.0479  0.1432  431 LEU A C   
4486 O O   . LEU B 245 ? 0.9023 0.7477 0.8201 -0.0492 0.0461  0.1408  431 LEU A O   
4487 C CB  . LEU B 245 ? 0.8012 0.6382 0.7349 -0.0169 0.0288  0.1399  431 LEU A CB  
4488 C CG  . LEU B 245 ? 0.8008 0.6336 0.7523 -0.0170 0.0275  0.1165  431 LEU A CG  
4489 C CD1 . LEU B 245 ? 0.8571 0.6731 0.8241 -0.0102 0.0285  0.1090  431 LEU A CD1 
4490 C CD2 . LEU B 245 ? 0.7757 0.6172 0.7251 -0.0091 0.0171  0.1104  431 LEU A CD2 
4491 N N   . PRO B 246 ? 0.9224 0.7407 0.8591 -0.0513 0.0588  0.1387  432 PRO A N   
4492 C CA  . PRO B 246 ? 0.8483 0.6722 0.7856 -0.0680 0.0700  0.1287  432 PRO A CA  
4493 C C   . PRO B 246 ? 0.8295 0.6604 0.7898 -0.0677 0.0680  0.1032  432 PRO A C   
4494 O O   . PRO B 246 ? 0.9165 0.7401 0.8984 -0.0602 0.0641  0.0912  432 PRO A O   
4495 C CB  . PRO B 246 ? 0.8726 0.6796 0.8142 -0.0766 0.0829  0.1342  432 PRO A CB  
4496 C CG  . PRO B 246 ? 0.8712 0.6625 0.8283 -0.0634 0.0770  0.1337  432 PRO A CG  
4497 C CD  . PRO B 246 ? 0.9063 0.7040 0.8533 -0.0471 0.0627  0.1425  432 PRO A CD  
4498 N N   . LEU B 247 ? 0.8259 0.6706 0.7814 -0.0753 0.0697  0.0945  433 LEU A N   
4499 C CA  . LEU B 247 ? 0.8079 0.6596 0.7853 -0.0734 0.0666  0.0711  433 LEU A CA  
4500 C C   . LEU B 247 ? 0.8996 0.7598 0.8831 -0.0880 0.0801  0.0576  433 LEU A C   
4501 O O   . LEU B 247 ? 0.9352 0.8038 0.9329 -0.0867 0.0774  0.0396  433 LEU A O   
4502 C CB  . LEU B 247 ? 0.8122 0.6708 0.7816 -0.0637 0.0525  0.0705  433 LEU A CB  
4503 C CG  . LEU B 247 ? 0.7832 0.6366 0.7483 -0.0483 0.0397  0.0805  433 LEU A CG  
4504 C CD1 . LEU B 247 ? 0.7710 0.6318 0.7279 -0.0423 0.0288  0.0795  433 LEU A CD1 
4505 C CD2 . LEU B 247 ? 0.7799 0.6230 0.7666 -0.0391 0.0360  0.0694  433 LEU A CD2 
4506 N N   . ASP B 248 ? 0.9526 0.8103 0.9250 -0.1015 0.0950  0.0661  434 ASP A N   
4507 C CA  . ASP B 248 ? 0.9579 0.8248 0.9349 -0.1160 0.1106  0.0527  434 ASP A CA  
4508 C C   . ASP B 248 ? 0.9489 0.8198 0.9659 -0.1159 0.1149  0.0288  434 ASP A C   
4509 O O   . ASP B 248 ? 0.9872 0.8703 1.0179 -0.1205 0.1210  0.0102  434 ASP A O   
4510 C CB  . ASP B 248 ? 0.9946 0.8560 0.9500 -0.1307 0.1269  0.0680  434 ASP A CB  
4511 C CG  . ASP B 248 ? 1.0897 0.9590 1.0099 -0.1394 0.1302  0.0762  434 ASP A CG  
4512 O OD1 . ASP B 248 ? 1.0089 0.8886 0.9266 -0.1361 0.1225  0.0658  434 ASP A OD1 
4513 O OD2 . ASP B 248 ? 1.1482 1.0121 1.0422 -0.1497 0.1400  0.0929  434 ASP A OD2 
4514 N N   . GLU B 249 ? 0.9075 0.7687 0.9451 -0.1105 0.1114  0.0279  435 GLU A N   
4515 C CA  . GLU B 249 ? 0.9787 0.8453 1.0568 -0.1117 0.1147  0.0053  435 GLU A CA  
4516 C C   . GLU B 249 ? 0.9084 0.7850 1.0065 -0.0988 0.0996  -0.0137 435 GLU A C   
4517 O O   . GLU B 249 ? 0.9674 0.8539 1.1006 -0.0997 0.1017  -0.0350 435 GLU A O   
4518 C CB  . GLU B 249 ? 0.8549 0.7069 0.9482 -0.1099 0.1134  0.0088  435 GLU A CB  
4519 C CG  . GLU B 249 ? 0.9020 0.7415 0.9839 -0.0934 0.0953  0.0194  435 GLU A CG  
4520 C CD  . GLU B 249 ? 1.0232 0.8455 1.1183 -0.0928 0.0958  0.0218  435 GLU A CD  
4521 O OE1 . GLU B 249 ? 0.8672 0.6894 0.9881 -0.1045 0.1073  0.0108  435 GLU A OE1 
4522 O OE2 . GLU B 249 ? 1.0294 0.8383 1.1100 -0.0811 0.0856  0.0342  435 GLU A OE2 
4523 N N   . PHE B 250 ? 0.8600 0.7345 0.9380 -0.0870 0.0845  -0.0063 436 PHE A N   
4524 C CA  . PHE B 250 ? 0.8880 0.7686 0.9805 -0.0752 0.0703  -0.0218 436 PHE A CA  
4525 C C   . PHE B 250 ? 0.8324 0.7229 0.9180 -0.0796 0.0747  -0.0294 436 PHE A C   
4526 O O   . PHE B 250 ? 0.7906 0.6847 0.8895 -0.0703 0.0642  -0.0429 436 PHE A O   
4527 C CB  . PHE B 250 ? 0.8179 0.6889 0.8944 -0.0598 0.0518  -0.0107 436 PHE A CB  
4528 C CG  . PHE B 250 ? 0.8796 0.7394 0.9612 -0.0543 0.0476  -0.0051 436 PHE A CG  
4529 C CD1 . PHE B 250 ? 0.7949 0.6540 0.9058 -0.0481 0.0403  -0.0219 436 PHE A CD1 
4530 C CD2 . PHE B 250 ? 0.8703 0.7200 0.9283 -0.0550 0.0504  0.0161  436 PHE A CD2 
4531 C CE1 . PHE B 250 ? 0.7742 0.6214 0.8890 -0.0438 0.0366  -0.0187 436 PHE A CE1 
4532 C CE2 . PHE B 250 ? 0.8858 0.7229 0.9491 -0.0494 0.0473  0.0199  436 PHE A CE2 
4533 C CZ  . PHE B 250 ? 0.7933 0.6283 0.8841 -0.0443 0.0408  0.0019  436 PHE A CZ  
4534 N N   . LEU B 251 ? 0.8500 0.7435 0.9138 -0.0932 0.0895  -0.0213 437 LEU A N   
4535 C CA  . LEU B 251 ? 0.8897 0.7923 0.9478 -0.0995 0.0965  -0.0319 437 LEU A CA  
4536 C C   . LEU B 251 ? 0.9654 0.8801 1.0555 -0.1071 0.1120  -0.0539 437 LEU A C   
4537 O O   . LEU B 251 ? 1.0175 0.9342 1.1207 -0.1161 0.1251  -0.0540 437 LEU A O   
4538 C CB  . LEU B 251 ? 0.9522 0.8538 0.9707 -0.1113 0.1052  -0.0150 437 LEU A CB  
4539 C CG  . LEU B 251 ? 0.8537 0.7485 0.8424 -0.1049 0.0904  0.0052  437 LEU A CG  
4540 C CD1 . LEU B 251 ? 0.8645 0.7612 0.8168 -0.1175 0.0983  0.0204  437 LEU A CD1 
4541 C CD2 . LEU B 251 ? 0.8317 0.7268 0.8248 -0.0952 0.0766  -0.0046 437 LEU A CD2 
4542 N N   . GLN B 252 ? 0.9022 0.8250 1.0067 -0.1034 0.1111  -0.0728 438 GLN A N   
4543 C CA  . GLN B 252 ? 0.9772 0.9149 1.1157 -0.1093 0.1264  -0.0958 438 GLN A CA  
4544 C C   . GLN B 252 ? 0.9889 0.9325 1.1103 -0.1287 0.1517  -0.0926 438 GLN A C   
4545 O O   . GLN B 252 ? 1.0637 1.0170 1.2096 -0.1380 0.1683  -0.1015 438 GLN A O   
4546 C CB  . GLN B 252 ? 0.9560 0.8991 1.1103 -0.1001 0.1203  -0.1157 438 GLN A CB  
4547 C CG  . GLN B 252 ? 1.0170 0.9780 1.2182 -0.1004 0.1313  -0.1421 438 GLN A CG  
4548 C CD  . GLN B 252 ? 0.9866 0.9506 1.2068 -0.0877 0.1224  -0.1614 438 GLN A CD  
4549 O OE1 . GLN B 252 ? 0.9542 0.9054 1.1481 -0.0822 0.1118  -0.1555 438 GLN A OE1 
4550 N NE2 . GLN B 252 ? 1.1147 1.0952 1.3828 -0.0828 0.1261  -0.1846 438 GLN A NE2 
4551 N N   . LYS B 253 ? 1.0151 0.9532 1.0936 -0.1357 0.1549  -0.0796 439 LYS A N   
4552 C CA  . LYS B 253 ? 0.9963 0.9372 1.0482 -0.1539 0.1768  -0.0725 439 LYS A CA  
4553 C C   . LYS B 253 ? 1.0228 0.9513 1.0282 -0.1566 0.1691  -0.0446 439 LYS A C   
4554 O O   . LYS B 253 ? 1.0202 0.9454 1.0022 -0.1522 0.1566  -0.0397 439 LYS A O   
4555 C CB  . LYS B 253 ? 1.0692 1.0206 1.1164 -0.1609 0.1910  -0.0915 439 LYS A CB  
4556 C CG  . LYS B 253 ? 1.0990 1.0542 1.1164 -0.1804 0.2154  -0.0862 439 LYS A CG  
4557 C CD  . LYS B 253 ? 1.1759 1.1414 1.1888 -0.1860 0.2295  -0.1083 439 LYS A CD  
4558 C CE  . LYS B 253 ? 1.2534 1.2228 1.2327 -0.2060 0.2551  -0.1036 439 LYS A CE  
4559 N NZ  . LYS B 253 ? 1.3397 1.3185 1.3104 -0.2116 0.2698  -0.1265 439 LYS A NZ  
4560 N N   . THR B 254 ? 1.0649 0.9864 1.0594 -0.1636 0.1757  -0.0262 440 THR A N   
4561 C CA  . THR B 254 ? 1.0169 0.9277 0.9704 -0.1650 0.1682  0.0011  440 THR A CA  
4562 C C   . THR B 254 ? 1.1113 1.0259 1.0241 -0.1787 0.1793  0.0060  440 THR A C   
4563 O O   . THR B 254 ? 1.0334 0.9570 0.9478 -0.1895 0.1976  -0.0102 440 THR A O   
4564 C CB  . THR B 254 ? 0.9298 0.8292 0.8838 -0.1679 0.1725  0.0193  440 THR A CB  
4565 O OG1 . THR B 254 ? 0.9731 0.8734 0.9159 -0.1855 0.1961  0.0215  440 THR A OG1 
4566 C CG2 . THR B 254 ? 1.0287 0.9261 1.0266 -0.1583 0.1666  0.0081  440 THR A CG2 
4567 N N   . ASP B 255 ? 1.1888 1.0977 1.0652 -0.1780 0.1678  0.0277  441 ASP A N   
4568 C CA  . ASP B 255 ? 1.1155 1.0273 0.9480 -0.1907 0.1744  0.0354  441 ASP A CA  
4569 C C   . ASP B 255 ? 1.1389 1.0413 0.9407 -0.1962 0.1759  0.0644  441 ASP A C   
4570 O O   . ASP B 255 ? 1.2405 1.1370 1.0354 -0.1864 0.1586  0.0838  441 ASP A O   
4571 C CB  . ASP B 255 ? 1.1546 1.0704 0.9697 -0.1858 0.1571  0.0340  441 ASP A CB  
4572 C CG  . ASP B 255 ? 1.2581 1.1774 1.0259 -0.1989 0.1605  0.0422  441 ASP A CG  
4573 O OD1 . ASP B 255 ? 1.1906 1.1150 0.9473 -0.2107 0.1775  0.0264  441 ASP A OD1 
4574 O OD2 . ASP B 255 ? 1.3924 1.3103 1.1341 -0.1973 0.1462  0.0640  441 ASP A OD2 
4575 N N   . PRO B 256 ? 1.1523 1.0525 0.9358 -0.2111 0.1964  0.0689  442 PRO A N   
4576 C CA  . PRO B 256 ? 1.1733 1.0629 0.9186 -0.2168 0.1965  0.0984  442 PRO A CA  
4577 C C   . PRO B 256 ? 1.2924 1.1875 0.9972 -0.2170 0.1814  0.1096  442 PRO A C   
4578 O O   . PRO B 256 ? 1.3420 1.2482 1.0411 -0.2190 0.1784  0.0923  442 PRO A O   
4579 C CB  . PRO B 256 ? 1.1213 1.0091 0.8532 -0.2349 0.2241  0.0963  442 PRO A CB  
4580 C CG  . PRO B 256 ? 1.0722 0.9680 0.8523 -0.2352 0.2375  0.0681  442 PRO A CG  
4581 C CD  . PRO B 256 ? 1.2041 1.1107 1.0049 -0.2226 0.2212  0.0482  442 PRO A CD  
4582 N N   . LYS B 257 ? 1.2782 1.1654 0.9570 -0.2144 0.1709  0.1383  443 LYS A N   
4583 C CA  . LYS B 257 ? 1.2831 1.1766 0.9279 -0.2124 0.1523  0.1536  443 LYS A CA  
4584 C C   . LYS B 257 ? 1.3475 1.2493 1.0157 -0.1978 0.1306  0.1481  443 LYS A C   
4585 O O   . LYS B 257 ? 1.4348 1.3444 1.0823 -0.1952 0.1136  0.1601  443 LYS A O   
4586 C CB  . LYS B 257 ? 1.4003 1.3031 1.0041 -0.2277 0.1591  0.1460  443 LYS A CB  
4587 C CG  . LYS B 257 ? 1.3917 1.3079 1.0014 -0.2281 0.1527  0.1207  443 LYS A CG  
4588 C CD  . LYS B 257 ? 1.4272 1.3495 0.9969 -0.2449 0.1647  0.1096  443 LYS A CD  
4589 C CE  . LYS B 257 ? 1.2954 1.2117 0.8554 -0.2575 0.1930  0.1061  443 LYS A CE  
4590 N NZ  . LYS B 257 ? 1.3773 1.2997 0.8929 -0.2735 0.2046  0.0956  443 LYS A NZ  
4591 N N   . ASP B 258 ? 1.2920 1.1928 1.0022 -0.1885 0.1305  0.1310  444 ASP A N   
4592 C CA  . ASP B 258 ? 1.2584 1.1628 0.9911 -0.1732 0.1111  0.1306  444 ASP A CA  
4593 C C   . ASP B 258 ? 1.1771 1.0736 0.9515 -0.1627 0.1137  0.1207  444 ASP A C   
4594 O O   . ASP B 258 ? 1.1558 1.0557 0.9560 -0.1591 0.1139  0.0987  444 ASP A O   
4595 C CB  . ASP B 258 ? 1.1579 1.0736 0.8888 -0.1748 0.1029  0.1134  444 ASP A CB  
4596 C CG  . ASP B 258 ? 1.1858 1.1061 0.9283 -0.1620 0.0821  0.1206  444 ASP A CG  
4597 O OD1 . ASP B 258 ? 1.1667 1.0814 0.9283 -0.1493 0.0761  0.1312  444 ASP A OD1 
4598 O OD2 . ASP B 258 ? 1.2970 1.2261 1.0293 -0.1650 0.0724  0.1151  444 ASP A OD2 
4599 N N   . PRO B 259 ? 1.1436 1.0283 0.9253 -0.1574 0.1151  0.1362  445 PRO A N   
4600 C CA  . PRO B 259 ? 1.0355 0.9125 0.8554 -0.1467 0.1144  0.1269  445 PRO A CA  
4601 C C   . PRO B 259 ? 1.0637 0.9452 0.8977 -0.1313 0.0957  0.1249  445 PRO A C   
4602 O O   . PRO B 259 ? 1.0955 0.9838 0.9117 -0.1276 0.0830  0.1380  445 PRO A O   
4603 C CB  . PRO B 259 ? 1.0804 0.9415 0.8973 -0.1450 0.1183  0.1474  445 PRO A CB  
4604 C CG  . PRO B 259 ? 1.1423 1.0021 0.9195 -0.1572 0.1250  0.1656  445 PRO A CG  
4605 C CD  . PRO B 259 ? 1.1704 1.0467 0.9252 -0.1597 0.1152  0.1633  445 PRO A CD  
4606 N N   . ALA B 260 ? 1.0519 0.9308 0.9184 -0.1229 0.0939  0.1082  446 ALA A N   
4607 C CA  . ALA B 260 ? 0.9092 0.7900 0.7887 -0.1081 0.0775  0.1061  446 ALA A CA  
4608 C C   . ALA B 260 ? 0.9135 0.7856 0.7945 -0.0963 0.0701  0.1243  446 ALA A C   
4609 O O   . ALA B 260 ? 0.9457 0.8097 0.8488 -0.0861 0.0669  0.1184  446 ALA A O   
4610 C CB  . ALA B 260 ? 0.9763 0.8567 0.8866 -0.1030 0.0772  0.0822  446 ALA A CB  
4611 N N   . ASN B 261 ? 0.9444 0.8183 0.8011 -0.0974 0.0668  0.1462  447 ASN A N   
4612 C CA  . ASN B 261 ? 0.8837 0.7506 0.7404 -0.0852 0.0597  0.1650  447 ASN A CA  
4613 C C   . ASN B 261 ? 0.8746 0.7541 0.7277 -0.0752 0.0448  0.1721  447 ASN A C   
4614 O O   . ASN B 261 ? 0.9228 0.8163 0.7593 -0.0818 0.0401  0.1755  447 ASN A O   
4615 C CB  . ASN B 261 ? 0.8949 0.7550 0.7296 -0.0911 0.0651  0.1864  447 ASN A CB  
4616 C CG  . ASN B 261 ? 1.0005 0.8446 0.8406 -0.1006 0.0813  0.1825  447 ASN A CG  
4617 O OD1 . ASN B 261 ? 1.1268 0.9693 0.9460 -0.1141 0.0915  0.1892  447 ASN A OD1 
4618 N ND2 . ASN B 261 ? 0.9958 0.8282 0.8635 -0.0943 0.0839  0.1715  447 ASN A ND2 
4619 N N   . TYR B 262 ? 0.8348 0.7098 0.7033 -0.0601 0.0381  0.1735  448 TYR A N   
4620 C CA  . TYR B 262 ? 0.8794 0.7667 0.7486 -0.0504 0.0262  0.1782  448 TYR A CA  
4621 C C   . TYR B 262 ? 0.8652 0.7502 0.7367 -0.0362 0.0216  0.1957  448 TYR A C   
4622 O O   . TYR B 262 ? 0.8608 0.7295 0.7392 -0.0305 0.0264  0.1985  448 TYR A O   
4623 C CB  . TYR B 262 ? 0.8006 0.6863 0.6861 -0.0448 0.0228  0.1594  448 TYR A CB  
4624 C CG  . TYR B 262 ? 0.8255 0.7175 0.7082 -0.0562 0.0238  0.1446  448 TYR A CG  
4625 C CD1 . TYR B 262 ? 0.8478 0.7342 0.7349 -0.0662 0.0338  0.1304  448 TYR A CD1 
4626 C CD2 . TYR B 262 ? 0.8023 0.7054 0.6791 -0.0572 0.0158  0.1444  448 TYR A CD2 
4627 C CE1 . TYR B 262 ? 0.8224 0.7140 0.7083 -0.0753 0.0355  0.1156  448 TYR A CE1 
4628 C CE2 . TYR B 262 ? 0.8747 0.7803 0.7491 -0.0671 0.0168  0.1302  448 TYR A CE2 
4629 C CZ  . TYR B 262 ? 0.8419 0.7416 0.7208 -0.0753 0.0266  0.1154  448 TYR A CZ  
4630 O OH  . TYR B 262 ? 0.7952 0.6970 0.6731 -0.0838 0.0282  0.0999  448 TYR A OH  
4631 N N   . ILE B 263 ? 0.8170 0.7188 0.6839 -0.0309 0.0125  0.2068  449 ILE A N   
4632 C CA  . ILE B 263 ? 0.8387 0.7434 0.7095 -0.0164 0.0079  0.2235  449 ILE A CA  
4633 C C   . ILE B 263 ? 0.8017 0.7151 0.6839 -0.0053 0.0025  0.2185  449 ILE A C   
4634 O O   . ILE B 263 ? 0.8048 0.7311 0.6850 -0.0113 -0.0015 0.2125  449 ILE A O   
4635 C CB  . ILE B 263 ? 0.8353 0.7561 0.6918 -0.0198 0.0021  0.2439  449 ILE A CB  
4636 C CG1 . ILE B 263 ? 0.8695 0.7794 0.7092 -0.0316 0.0082  0.2495  449 ILE A CG1 
4637 C CG2 . ILE B 263 ? 0.8399 0.7652 0.7049 -0.0027 -0.0028 0.2606  449 ILE A CG2 
4638 C CD1 . ILE B 263 ? 1.1180 1.0416 0.9397 -0.0348 0.0011  0.2701  449 ILE A CD1 
4639 N N   . LEU B 264 ? 0.8017 0.7061 0.6949 0.0103  0.0033  0.2201  450 LEU A N   
4640 C CA  . LEU B 264 ? 0.7884 0.6995 0.6896 0.0218  0.0001  0.2158  450 LEU A CA  
4641 C C   . LEU B 264 ? 0.8011 0.7387 0.7013 0.0233  -0.0057 0.2299  450 LEU A C   
4642 O O   . LEU B 264 ? 0.8618 0.8093 0.7618 0.0271  -0.0081 0.2464  450 LEU A O   
4643 C CB  . LEU B 264 ? 0.7947 0.6898 0.7054 0.0382  0.0032  0.2142  450 LEU A CB  
4644 C CG  . LEU B 264 ? 0.8083 0.7080 0.7242 0.0512  0.0017  0.2087  450 LEU A CG  
4645 C CD1 . LEU B 264 ? 0.7742 0.6702 0.6873 0.0450  -0.0001 0.1919  450 LEU A CD1 
4646 C CD2 . LEU B 264 ? 0.8716 0.7534 0.7947 0.0670  0.0053  0.2057  450 LEU A CD2 
4647 N N   . HIS B 265 ? 0.8397 0.7886 0.7402 0.0204  -0.0085 0.2238  451 HIS A N   
4648 C CA  . HIS B 265 ? 0.8365 0.8122 0.7389 0.0192  -0.0134 0.2354  451 HIS A CA  
4649 C C   . HIS B 265 ? 0.8063 0.7891 0.7173 0.0319  -0.0119 0.2355  451 HIS A C   
4650 O O   . HIS B 265 ? 0.8314 0.8324 0.7515 0.0411  -0.0124 0.2482  451 HIS A O   
4651 C CB  . HIS B 265 ? 0.7774 0.7621 0.6716 0.0013  -0.0173 0.2301  451 HIS A CB  
4652 C CG  . HIS B 265 ? 0.7632 0.7765 0.6592 -0.0047 -0.0235 0.2426  451 HIS A CG  
4653 N ND1 . HIS B 265 ? 0.7569 0.7815 0.6529 -0.0146 -0.0264 0.2389  451 HIS A ND1 
4654 C CD2 . HIS B 265 ? 0.8173 0.8505 0.7165 -0.0025 -0.0283 0.2589  451 HIS A CD2 
4655 C CE1 . HIS B 265 ? 0.8537 0.9055 0.7542 -0.0195 -0.0324 0.2512  451 HIS A CE1 
4656 N NE2 . HIS B 265 ? 0.8187 0.8775 0.7215 -0.0117 -0.0343 0.2635  451 HIS A NE2 
4657 N N   . ALA B 266 ? 0.7712 0.7409 0.6795 0.0332  -0.0099 0.2220  452 ALA A N   
4658 C CA  . ALA B 266 ? 0.7719 0.7470 0.6831 0.0436  -0.0075 0.2217  452 ALA A CA  
4659 C C   . ALA B 266 ? 0.8457 0.7961 0.7537 0.0547  -0.0045 0.2081  452 ALA A C   
4660 O O   . ALA B 266 ? 0.8023 0.7338 0.7066 0.0497  -0.0060 0.1955  452 ALA A O   
4661 C CB  . ALA B 266 ? 0.7812 0.7667 0.6880 0.0324  -0.0099 0.2207  452 ALA A CB  
4662 N N   . VAL B 267 ? 0.9381 0.8903 0.8486 0.0699  -0.0003 0.2097  453 VAL A N   
4663 C CA  . VAL B 267 ? 0.8578 0.7882 0.7629 0.0813  0.0017  0.1962  453 VAL A CA  
4664 C C   . VAL B 267 ? 0.8073 0.7455 0.7049 0.0880  0.0048  0.1967  453 VAL A C   
4665 O O   . VAL B 267 ? 0.8525 0.8064 0.7555 0.0978  0.0105  0.2055  453 VAL A O   
4666 C CB  . VAL B 267 ? 0.8286 0.7476 0.7408 0.0948  0.0054  0.1957  453 VAL A CB  
4667 C CG1 . VAL B 267 ? 0.9070 0.8030 0.8127 0.1050  0.0061  0.1792  453 VAL A CG1 
4668 C CG2 . VAL B 267 ? 0.7811 0.6921 0.6988 0.0868  0.0037  0.1985  453 VAL A CG2 
4669 N N   . LEU B 268 ? 0.7823 0.7095 0.6676 0.0832  0.0013  0.1877  454 LEU A N   
4670 C CA  . LEU B 268 ? 0.8086 0.7398 0.6821 0.0874  0.0043  0.1892  454 LEU A CA  
4671 C C   . LEU B 268 ? 0.8107 0.7227 0.6722 0.1022  0.0055  0.1770  454 LEU A C   
4672 O O   . LEU B 268 ? 0.8164 0.7073 0.6728 0.1025  -0.0012 0.1633  454 LEU A O   
4673 C CB  . LEU B 268 ? 0.8175 0.7451 0.6819 0.0740  -0.0010 0.1881  454 LEU A CB  
4674 C CG  . LEU B 268 ? 0.8609 0.8086 0.7326 0.0585  -0.0014 0.1998  454 LEU A CG  
4675 C CD1 . LEU B 268 ? 0.8680 0.8192 0.7508 0.0492  -0.0054 0.1998  454 LEU A CD1 
4676 C CD2 . LEU B 268 ? 0.8078 0.7473 0.6680 0.0483  -0.0050 0.1984  454 LEU A CD2 
4677 N N   . VAL B 269 ? 0.8208 0.7414 0.6784 0.1144  0.0138  0.1810  455 VAL A N   
4678 C CA  . VAL B 269 ? 0.8625 0.7661 0.7071 0.1295  0.0158  0.1689  455 VAL A CA  
4679 C C   . VAL B 269 ? 0.9374 0.8454 0.7617 0.1336  0.0214  0.1716  455 VAL A C   
4680 O O   . VAL B 269 ? 0.8474 0.7762 0.6739 0.1273  0.0274  0.1850  455 VAL A O   
4681 C CB  . VAL B 269 ? 0.8386 0.7434 0.6955 0.1432  0.0223  0.1681  455 VAL A CB  
4682 C CG1 . VAL B 269 ? 0.8971 0.8032 0.7743 0.1368  0.0190  0.1729  455 VAL A CG1 
4683 C CG2 . VAL B 269 ? 0.8417 0.7701 0.7020 0.1518  0.0340  0.1791  455 VAL A CG2 
4684 N N   . HIS B 270 ? 0.9486 0.8365 0.7521 0.1436  0.0193  0.1585  456 HIS A N   
4685 C CA  . HIS B 270 ? 0.8873 0.7748 0.6650 0.1485  0.0246  0.1601  456 HIS A CA  
4686 C C   . HIS B 270 ? 0.9559 0.8349 0.7194 0.1661  0.0311  0.1492  456 HIS A C   
4687 O O   . HIS B 270 ? 1.0057 0.8670 0.7710 0.1736  0.0253  0.1344  456 HIS A O   
4688 C CB  . HIS B 270 ? 0.9169 0.7851 0.6738 0.1420  0.0128  0.1551  456 HIS A CB  
4689 C CG  . HIS B 270 ? 0.9678 0.8262 0.6910 0.1501  0.0154  0.1531  456 HIS A CG  
4690 N ND1 . HIS B 270 ? 1.0088 0.8748 0.7160 0.1439  0.0220  0.1669  456 HIS A ND1 
4691 C CD2 . HIS B 270 ? 0.9524 0.7932 0.6528 0.1631  0.0124  0.1391  456 HIS A CD2 
4692 C CE1 . HIS B 270 ? 0.9896 0.8427 0.6636 0.1532  0.0236  0.1627  456 HIS A CE1 
4693 N NE2 . HIS B 270 ? 1.0023 0.8405 0.6708 0.1652  0.0173  0.1452  456 HIS A NE2 
4694 N N   . SER B 271 ? 0.9752 0.8679 0.7259 0.1720  0.0443  0.1563  457 SER A N   
4695 C CA  . SER B 271 ? 0.9826 0.8670 0.7100 0.1878  0.0523  0.1460  457 SER A CA  
4696 C C   . SER B 271 ? 1.0887 0.9736 0.7838 0.1852  0.0573  0.1526  457 SER A C   
4697 O O   . SER B 271 ? 1.1757 1.0790 0.8762 0.1741  0.0637  0.1691  457 SER A O   
4698 C CB  . SER B 271 ? 0.9634 0.8665 0.7092 0.2001  0.0677  0.1480  457 SER A CB  
4699 O OG  . SER B 271 ? 1.0991 0.9916 0.8658 0.2063  0.0625  0.1387  457 SER A OG  
4700 N N   . GLY B 272 ? 1.1641 1.0281 0.8243 0.1945  0.0544  0.1403  458 GLY A N   
4701 C CA  . GLY B 272 ? 1.1661 1.0219 0.7897 0.1907  0.0541  0.1464  458 GLY A CA  
4702 C C   . GLY B 272 ? 1.1667 1.0319 0.7653 0.2005  0.0733  0.1485  458 GLY A C   
4703 O O   . GLY B 272 ? 1.2825 1.1490 0.8812 0.2148  0.0817  0.1364  458 GLY A O   
4704 N N   . ASP B 273 ? 1.2313 1.1018 0.8076 0.1926  0.0813  0.1635  459 ASP A N   
4705 C CA  . ASP B 273 ? 1.2689 1.1488 0.8178 0.2003  0.1017  0.1664  459 ASP A CA  
4706 C C   . ASP B 273 ? 1.2684 1.1415 0.7830 0.1895  0.1045  0.1821  459 ASP A C   
4707 O O   . ASP B 273 ? 1.2675 1.1260 0.7793 0.1778  0.0892  0.1894  459 ASP A O   
4708 C CB  . ASP B 273 ? 1.2950 1.2107 0.8792 0.2026  0.1227  0.1735  459 ASP A CB  
4709 C CG  . ASP B 273 ? 1.1523 1.0928 0.7707 0.1850  0.1251  0.1933  459 ASP A CG  
4710 O OD1 . ASP B 273 ? 1.2194 1.1485 0.8309 0.1703  0.1136  0.2023  459 ASP A OD1 
4711 O OD2 . ASP B 273 ? 1.0637 1.0349 0.7178 0.1863  0.1373  0.1988  459 ASP A OD2 
4712 N N   . ASN B 274 ? 1.2406 1.1236 0.7287 0.1938  0.1254  0.1874  460 ASN A N   
4713 C CA  . ASN B 274 ? 1.2317 1.1043 0.6779 0.1855  0.1310  0.2020  460 ASN A CA  
4714 C C   . ASN B 274 ? 1.2318 1.1175 0.6982 0.1649  0.1348  0.2246  460 ASN A C   
4715 O O   . ASN B 274 ? 1.2376 1.1028 0.6740 0.1554  0.1288  0.2364  460 ASN A O   
4716 C CB  . ASN B 274 ? 1.2760 1.1586 0.6901 0.1948  0.1558  0.2016  460 ASN A CB  
4717 C CG  . ASN B 274 ? 1.3171 1.1724 0.6840 0.2113  0.1482  0.1825  460 ASN A CG  
4718 O OD1 . ASN B 274 ? 1.3927 1.2186 0.7403 0.2127  0.1237  0.1748  460 ASN A OD1 
4719 N ND2 . ASN B 274 ? 1.3773 1.2428 0.7249 0.2239  0.1691  0.1740  460 ASN A ND2 
4720 N N   . HIS B 275 ? 1.2422 1.1608 0.7571 0.1579  0.1446  0.2313  461 HIS A N   
4721 C CA  . HIS B 275 ? 1.2244 1.1589 0.7605 0.1373  0.1497  0.2514  461 HIS A CA  
4722 C C   . HIS B 275 ? 1.3053 1.2320 0.8709 0.1258  0.1283  0.2524  461 HIS A C   
4723 O O   . HIS B 275 ? 1.2923 1.2371 0.8856 0.1091  0.1316  0.2657  461 HIS A O   
4724 C CB  . HIS B 275 ? 1.2099 1.1889 0.7834 0.1350  0.1725  0.2586  461 HIS A CB  
4725 C CG  . HIS B 275 ? 1.2499 1.2497 0.8743 0.1377  0.1650  0.2522  461 HIS A CG  
4726 N ND1 . HIS B 275 ? 1.3779 1.3970 1.0412 0.1213  0.1600  0.2630  461 HIS A ND1 
4727 C CD2 . HIS B 275 ? 1.3172 1.3175 0.9570 0.1544  0.1599  0.2363  461 HIS A CD2 
4728 C CE1 . HIS B 275 ? 1.2477 1.2804 0.9468 0.1284  0.1528  0.2552  461 HIS A CE1 
4729 N NE2 . HIS B 275 ? 1.3176 1.3385 1.0041 0.1484  0.1531  0.2395  461 HIS A NE2 
4730 N N   . GLY B 276 ? 1.3175 1.2191 0.8784 0.1335  0.1071  0.2379  462 GLY A N   
4731 C CA  . GLY B 276 ? 1.1874 1.0799 0.7720 0.1229  0.0881  0.2376  462 GLY A CA  
4732 C C   . GLY B 276 ? 1.1662 1.0691 0.7886 0.1279  0.0796  0.2255  462 GLY A C   
4733 O O   . GLY B 276 ? 1.2544 1.1588 0.9023 0.1165  0.0690  0.2279  462 GLY A O   
4734 N N   . GLY B 277 ? 1.1202 1.0290 0.7462 0.1440  0.0847  0.2130  463 GLY A N   
4735 C CA  . GLY B 277 ? 1.0701 0.9828 0.7281 0.1491  0.0760  0.2019  463 GLY A CA  
4736 C C   . GLY B 277 ? 1.0903 1.0377 0.7880 0.1469  0.0875  0.2098  463 GLY A C   
4737 O O   . GLY B 277 ? 1.2091 1.1824 0.9151 0.1412  0.1027  0.2230  463 GLY A O   
4738 N N   . HIS B 278 ? 1.0438 0.9920 0.7675 0.1517  0.0796  0.2015  464 HIS A N   
4739 C CA  . HIS B 278 ? 0.9341 0.9123 0.6965 0.1508  0.0858  0.2088  464 HIS A CA  
4740 C C   . HIS B 278 ? 0.9512 0.9210 0.7338 0.1434  0.0696  0.2057  464 HIS A C   
4741 O O   . HIS B 278 ? 0.9038 0.8530 0.6847 0.1515  0.0609  0.1923  464 HIS A O   
4742 C CB  . HIS B 278 ? 0.9444 0.9326 0.7149 0.1701  0.0978  0.2016  464 HIS A CB  
4743 C CG  . HIS B 278 ? 0.9384 0.9611 0.7480 0.1714  0.1056  0.2116  464 HIS A CG  
4744 N ND1 . HIS B 278 ? 0.9289 0.9593 0.7556 0.1890  0.1125  0.2057  464 HIS A ND1 
4745 C CD2 . HIS B 278 ? 0.9189 0.9704 0.7545 0.1576  0.1063  0.2268  464 HIS A CD2 
4746 C CE1 . HIS B 278 ? 1.0599 1.1231 0.9219 0.1871  0.1165  0.2178  464 HIS A CE1 
4747 N NE2 . HIS B 278 ? 1.0216 1.0993 0.8895 0.1677  0.1125  0.2304  464 HIS A NE2 
4748 N N   . TYR B 279 ? 0.9515 0.9376 0.7527 0.1272  0.0664  0.2176  465 TYR A N   
4749 C CA  . TYR B 279 ? 0.8612 0.8409 0.6779 0.1169  0.0524  0.2161  465 TYR A CA  
4750 C C   . TYR B 279 ? 0.8418 0.8512 0.6913 0.1149  0.0551  0.2255  465 TYR A C   
4751 O O   . TYR B 279 ? 0.8377 0.8744 0.7006 0.1058  0.0611  0.2382  465 TYR A O   
4752 C CB  . TYR B 279 ? 0.8589 0.8292 0.6661 0.0993  0.0445  0.2206  465 TYR A CB  
4753 C CG  . TYR B 279 ? 0.9095 0.8503 0.6840 0.1019  0.0398  0.2135  465 TYR A CG  
4754 C CD1 . TYR B 279 ? 0.9324 0.8728 0.6835 0.1048  0.0497  0.2192  465 TYR A CD1 
4755 C CD2 . TYR B 279 ? 0.9998 0.9140 0.7671 0.1012  0.0251  0.2017  465 TYR A CD2 
4756 C CE1 . TYR B 279 ? 1.0346 0.9468 0.7527 0.1079  0.0437  0.2141  465 TYR A CE1 
4757 C CE2 . TYR B 279 ? 0.9396 0.8280 0.6784 0.1048  0.0184  0.1956  465 TYR A CE2 
4758 C CZ  . TYR B 279 ? 0.9699 0.8564 0.6826 0.1084  0.0269  0.2025  465 TYR A CZ  
4759 O OH  . TYR B 279 ? 0.9548 0.8147 0.6356 0.1126  0.0189  0.1980  465 TYR A OH  
4760 N N   . VAL B 280 ? 0.8324 0.8363 0.6950 0.1228  0.0503  0.2198  466 VAL A N   
4761 C CA  . VAL B 280 ? 0.8504 0.8785 0.7415 0.1206  0.0493  0.2295  466 VAL A CA  
4762 C C   . VAL B 280 ? 0.8341 0.8462 0.7284 0.1117  0.0364  0.2255  466 VAL A C   
4763 O O   . VAL B 280 ? 0.8619 0.8454 0.7424 0.1127  0.0304  0.2130  466 VAL A O   
4764 C CB  . VAL B 280 ? 0.8638 0.9028 0.7699 0.1399  0.0577  0.2298  466 VAL A CB  
4765 C CG1 . VAL B 280 ? 0.8420 0.8934 0.7412 0.1503  0.0726  0.2300  466 VAL A CG1 
4766 C CG2 . VAL B 280 ? 0.8528 0.8617 0.7533 0.1511  0.0529  0.2169  466 VAL A CG2 
4767 N N   . VAL B 281 ? 0.8268 0.8592 0.7398 0.1023  0.0322  0.2359  467 VAL A N   
4768 C CA  . VAL B 281 ? 0.8429 0.8641 0.7579 0.0920  0.0217  0.2337  467 VAL A CA  
4769 C C   . VAL B 281 ? 0.7738 0.8091 0.7078 0.0980  0.0205  0.2424  467 VAL A C   
4770 O O   . VAL B 281 ? 0.8222 0.8875 0.7728 0.1004  0.0234  0.2544  467 VAL A O   
4771 C CB  . VAL B 281 ? 0.8225 0.8503 0.7348 0.0714  0.0157  0.2372  467 VAL A CB  
4772 C CG1 . VAL B 281 ? 0.8443 0.9070 0.7712 0.0645  0.0191  0.2509  467 VAL A CG1 
4773 C CG2 . VAL B 281 ? 0.7947 0.8137 0.7087 0.0610  0.0067  0.2345  467 VAL A CG2 
4774 N N   . TYR B 282 ? 0.8034 0.8175 0.7357 0.1005  0.0161  0.2369  468 TYR A N   
4775 C CA  . TYR B 282 ? 0.8578 0.8785 0.8040 0.1054  0.0136  0.2461  468 TYR A CA  
4776 C C   . TYR B 282 ? 0.9143 0.9389 0.8588 0.0876  0.0049  0.2511  468 TYR A C   
4777 O O   . TYR B 282 ? 0.8068 0.8124 0.7391 0.0765  0.0017  0.2412  468 TYR A O   
4778 C CB  . TYR B 282 ? 0.8684 0.8605 0.8126 0.1186  0.0156  0.2378  468 TYR A CB  
4779 C CG  . TYR B 282 ? 0.8308 0.8199 0.7778 0.1384  0.0243  0.2332  468 TYR A CG  
4780 C CD1 . TYR B 282 ? 0.8690 0.8456 0.8013 0.1422  0.0286  0.2202  468 TYR A CD1 
4781 C CD2 . TYR B 282 ? 0.9022 0.8999 0.8654 0.1541  0.0279  0.2416  468 TYR A CD2 
4782 C CE1 . TYR B 282 ? 0.9390 0.9123 0.8704 0.1602  0.0373  0.2144  468 TYR A CE1 
4783 C CE2 . TYR B 282 ? 0.9556 0.9500 0.9215 0.1730  0.0370  0.2355  468 TYR A CE2 
4784 C CZ  . TYR B 282 ? 1.0005 0.9829 0.9494 0.1755  0.0422  0.2214  468 TYR A CZ  
4785 O OH  . TYR B 282 ? 0.9265 0.9053 0.8749 0.1941  0.0520  0.2140  468 TYR A OH  
4786 N N   . LEU B 283 ? 0.8737 0.9239 0.8307 0.0854  0.0009  0.2657  469 LEU A N   
4787 C CA  . LEU B 283 ? 0.7812 0.8399 0.7344 0.0679  -0.0077 0.2710  469 LEU A CA  
4788 C C   . LEU B 283 ? 0.8087 0.8777 0.7702 0.0727  -0.0130 0.2851  469 LEU A C   
4789 O O   . LEU B 283 ? 0.8607 0.9471 0.8386 0.0873  -0.0118 0.2950  469 LEU A O   
4790 C CB  . LEU B 283 ? 0.7739 0.8599 0.7312 0.0545  -0.0103 0.2750  469 LEU A CB  
4791 C CG  . LEU B 283 ? 0.7982 0.8713 0.7416 0.0399  -0.0101 0.2635  469 LEU A CG  
4792 C CD1 . LEU B 283 ? 0.8163 0.9152 0.7675 0.0313  -0.0093 0.2689  469 LEU A CD1 
4793 C CD2 . LEU B 283 ? 0.7742 0.8350 0.7058 0.0242  -0.0168 0.2583  469 LEU A CD2 
4794 N N   . ASN B 284 ? 0.8528 0.9111 0.8025 0.0611  -0.0187 0.2861  470 ASN A N   
4795 C CA  . ASN B 284 ? 0.8756 0.9490 0.8276 0.0597  -0.0269 0.3018  470 ASN A CA  
4796 C C   . ASN B 284 ? 0.8379 0.9288 0.7813 0.0385  -0.0347 0.3021  470 ASN A C   
4797 O O   . ASN B 284 ? 0.7928 0.8674 0.7185 0.0247  -0.0359 0.2955  470 ASN A O   
4798 C CB  . ASN B 284 ? 0.8611 0.9070 0.8031 0.0634  -0.0264 0.3048  470 ASN A CB  
4799 C CG  . ASN B 284 ? 0.9493 0.9683 0.8731 0.0491  -0.0231 0.2910  470 ASN A CG  
4800 O OD1 . ASN B 284 ? 0.9628 0.9730 0.8840 0.0442  -0.0189 0.2757  470 ASN A OD1 
4801 N ND2 . ASN B 284 ? 0.9717 0.9775 0.8830 0.0428  -0.0246 0.2967  470 ASN A ND2 
4802 N N   . PRO B 285 ? 0.9059 1.0300 0.8623 0.0346  -0.0392 0.3083  471 PRO A N   
4803 C CA  . PRO B 285 ? 0.8256 0.9635 0.7744 0.0130  -0.0458 0.3048  471 PRO A CA  
4804 C C   . PRO B 285 ? 0.8574 0.9956 0.7901 0.0009  -0.0552 0.3095  471 PRO A C   
4805 O O   . PRO B 285 ? 0.9123 1.0441 0.8295 -0.0170 -0.0571 0.2998  471 PRO A O   
4806 C CB  . PRO B 285 ? 0.7729 0.9497 0.7444 0.0137  -0.0491 0.3134  471 PRO A CB  
4807 C CG  . PRO B 285 ? 0.7694 0.9462 0.7569 0.0345  -0.0393 0.3151  471 PRO A CG  
4808 C CD  . PRO B 285 ? 0.8248 0.9754 0.8055 0.0493  -0.0373 0.3169  471 PRO A CD  
4809 N N   . LYS B 286 ? 0.8280 0.9722 0.7622 0.0106  -0.0609 0.3241  472 LYS A N   
4810 C CA  . LYS B 286 ? 0.9003 1.0438 0.8145 -0.0003 -0.0698 0.3305  472 LYS A CA  
4811 C C   . LYS B 286 ? 0.9423 1.0486 0.8356 -0.0006 -0.0626 0.3259  472 LYS A C   
4812 O O   . LYS B 286 ? 1.0525 1.1544 0.9258 -0.0087 -0.0677 0.3323  472 LYS A O   
4813 C CB  . LYS B 286 ? 0.8635 1.0337 0.7883 0.0095  -0.0819 0.3509  472 LYS A CB  
4814 C CG  . LYS B 286 ? 0.9305 1.1437 0.8775 0.0059  -0.0910 0.3555  472 LYS A CG  
4815 C CD  . LYS B 286 ? 1.1031 1.3451 1.0634 0.0170  -0.1048 0.3755  472 LYS A CD  
4816 C CE  . LYS B 286 ? 1.0278 1.2640 1.0081 0.0436  -0.0989 0.3849  472 LYS A CE  
4817 N NZ  . LYS B 286 ? 1.1493 1.4168 1.1480 0.0565  -0.1133 0.4045  472 LYS A NZ  
4818 N N   . GLY B 287 ? 0.8956 0.9758 0.7926 0.0072  -0.0509 0.3149  473 GLY A N   
4819 C CA  . GLY B 287 ? 0.8482 0.8949 0.7302 0.0063  -0.0433 0.3096  473 GLY A CA  
4820 C C   . GLY B 287 ? 0.9436 0.9796 0.8231 0.0178  -0.0445 0.3260  473 GLY A C   
4821 O O   . GLY B 287 ? 1.0098 1.0197 0.8743 0.0134  -0.0387 0.3246  473 GLY A O   
4822 N N   . ASP B 288 ? 0.9456 1.0004 0.8405 0.0327  -0.0513 0.3416  474 ASP A N   
4823 C CA  . ASP B 288 ? 0.9389 0.9833 0.8317 0.0452  -0.0544 0.3596  474 ASP A CA  
4824 C C   . ASP B 288 ? 0.9914 1.0097 0.8977 0.0638  -0.0448 0.3575  474 ASP A C   
4825 O O   . ASP B 288 ? 1.0094 1.0155 0.9170 0.0766  -0.0467 0.3725  474 ASP A O   
4826 C CB  . ASP B 288 ? 0.9904 1.0699 0.8953 0.0534  -0.0685 0.3782  474 ASP A CB  
4827 C CG  . ASP B 288 ? 1.0488 1.1570 0.9833 0.0636  -0.0685 0.3745  474 ASP A CG  
4828 O OD1 . ASP B 288 ? 0.9951 1.0938 0.9370 0.0647  -0.0577 0.3587  474 ASP A OD1 
4829 O OD2 . ASP B 288 ? 0.9958 1.1372 0.9462 0.0703  -0.0795 0.3879  474 ASP A OD2 
4830 N N   . GLY B 289 ? 0.9542 0.9623 0.8694 0.0659  -0.0353 0.3394  475 GLY A N   
4831 C CA  . GLY B 289 ? 1.0122 0.9982 0.9405 0.0840  -0.0272 0.3355  475 GLY A CA  
4832 C C   . GLY B 289 ? 1.0631 1.0696 1.0146 0.1045  -0.0292 0.3432  475 GLY A C   
4833 O O   . GLY B 289 ? 0.9758 0.9638 0.9380 0.1217  -0.0229 0.3411  475 GLY A O   
4834 N N   . LYS B 290 ? 1.0987 1.1435 1.0597 0.1029  -0.0374 0.3514  476 LYS A N   
4835 C CA  . LYS B 290 ? 1.0376 1.1094 1.0248 0.1208  -0.0378 0.3570  476 LYS A CA  
4836 C C   . LYS B 290 ? 1.0137 1.0972 1.0071 0.1168  -0.0302 0.3411  476 LYS A C   
4837 O O   . LYS B 290 ? 0.9649 1.0726 0.9571 0.1017  -0.0343 0.3392  476 LYS A O   
4838 C CB  . LYS B 290 ? 1.0075 1.1169 1.0046 0.1207  -0.0515 0.3752  476 LYS A CB  
4839 C CG  . LYS B 290 ? 1.0351 1.1334 1.0254 0.1280  -0.0605 0.3941  476 LYS A CG  
4840 C CD  . LYS B 290 ? 1.1522 1.2920 1.1552 0.1301  -0.0763 0.4117  476 LYS A CD  
4841 C CE  . LYS B 290 ? 1.2430 1.3705 1.2357 0.1380  -0.0871 0.4325  476 LYS A CE  
4842 N NZ  . LYS B 290 ? 1.2213 1.3915 1.2284 0.1424  -0.1050 0.4500  476 LYS A NZ  
4843 N N   . TRP B 291 ? 0.9088 0.9740 0.9076 0.1302  -0.0195 0.3299  477 TRP A N   
4844 C CA  . TRP B 291 ? 0.9176 0.9825 0.9137 0.1258  -0.0114 0.3135  477 TRP A CA  
4845 C C   . TRP B 291 ? 0.8825 0.9787 0.8993 0.1375  -0.0067 0.3156  477 TRP A C   
4846 O O   . TRP B 291 ? 0.8968 1.0032 0.9322 0.1565  -0.0051 0.3238  477 TRP A O   
4847 C CB  . TRP B 291 ? 0.9278 0.9531 0.9136 0.1318  -0.0030 0.2980  477 TRP A CB  
4848 C CG  . TRP B 291 ? 0.9059 0.9038 0.8731 0.1164  -0.0052 0.2916  477 TRP A CG  
4849 C CD1 . TRP B 291 ? 0.9304 0.9114 0.8914 0.1139  -0.0084 0.3002  477 TRP A CD1 
4850 C CD2 . TRP B 291 ? 0.8536 0.8381 0.8070 0.1020  -0.0033 0.2756  477 TRP A CD2 
4851 N NE1 . TRP B 291 ? 0.9830 0.9433 0.9283 0.0977  -0.0072 0.2897  477 TRP A NE1 
4852 C CE2 . TRP B 291 ? 0.9398 0.9024 0.8819 0.0910  -0.0046 0.2740  477 TRP A CE2 
4853 C CE3 . TRP B 291 ? 0.8591 0.8475 0.8086 0.0977  -0.0006 0.2631  477 TRP A CE3 
4854 C CZ2 . TRP B 291 ? 0.9515 0.8991 0.8823 0.0768  -0.0032 0.2590  477 TRP A CZ2 
4855 C CZ3 . TRP B 291 ? 0.8983 0.8692 0.8350 0.0843  -0.0009 0.2492  477 TRP A CZ3 
4856 C CH2 . TRP B 291 ? 0.9149 0.8671 0.8443 0.0745  -0.0022 0.2466  477 TRP A CH2 
4857 N N   . CYS B 292 ? 0.9005 1.0108 0.9142 0.1260  -0.0037 0.3083  478 CYS A N   
4858 C CA  . CYS B 292 ? 0.8528 0.9912 0.8830 0.1336  0.0039  0.3086  478 CYS A CA  
4859 C C   . CYS B 292 ? 0.8586 0.9784 0.8734 0.1317  0.0137  0.2928  478 CYS A C   
4860 O O   . CYS B 292 ? 0.8481 0.9438 0.8425 0.1187  0.0115  0.2831  478 CYS A O   
4861 C CB  . CYS B 292 ? 0.7783 0.9577 0.8214 0.1194  -0.0024 0.3182  478 CYS A CB  
4862 S SG  . CYS B 292 ? 0.8116 1.0236 0.8768 0.1238  -0.0159 0.3379  478 CYS A SG  
4863 N N   . LYS B 293 ? 0.7888 0.9208 0.8133 0.1453  0.0247  0.2904  479 LYS A N   
4864 C CA  . LYS B 293 ? 0.7900 0.9084 0.7980 0.1447  0.0342  0.2776  479 LYS A CA  
4865 C C   . LYS B 293 ? 0.7833 0.9337 0.7979 0.1336  0.0384  0.2829  479 LYS A C   
4866 O O   . LYS B 293 ? 0.8594 1.0450 0.8981 0.1401  0.0430  0.2922  479 LYS A O   
4867 C CB  . LYS B 293 ? 0.8060 0.9114 0.8146 0.1674  0.0453  0.2695  479 LYS A CB  
4868 C CG  . LYS B 293 ? 0.8121 0.9091 0.8024 0.1680  0.0555  0.2580  479 LYS A CG  
4869 C CD  . LYS B 293 ? 0.9268 0.9952 0.9059 0.1867  0.0626  0.2440  479 LYS A CD  
4870 C CE  . LYS B 293 ? 0.9193 1.0066 0.9188 0.2082  0.0737  0.2468  479 LYS A CE  
4871 N NZ  . LYS B 293 ? 0.9035 0.9617 0.8894 0.2259  0.0816  0.2307  479 LYS A NZ  
4872 N N   . PHE B 294 ? 0.7780 0.9163 0.7733 0.1170  0.0371  0.2770  480 PHE A N   
4873 C CA  . PHE B 294 ? 0.7847 0.9467 0.7830 0.1034  0.0413  0.2819  480 PHE A CA  
4874 C C   . PHE B 294 ? 0.7874 0.9357 0.7676 0.1095  0.0538  0.2738  480 PHE A C   
4875 O O   . PHE B 294 ? 0.7901 0.9106 0.7454 0.1017  0.0517  0.2655  480 PHE A O   
4876 C CB  . PHE B 294 ? 0.7994 0.9559 0.7881 0.0799  0.0305  0.2822  480 PHE A CB  
4877 C CG  . PHE B 294 ? 0.7836 0.9580 0.7871 0.0717  0.0186  0.2907  480 PHE A CG  
4878 C CD1 . PHE B 294 ? 0.8039 0.9597 0.8024 0.0767  0.0109  0.2892  480 PHE A CD1 
4879 C CD2 . PHE B 294 ? 0.7890 0.9986 0.8101 0.0580  0.0148  0.3003  480 PHE A CD2 
4880 C CE1 . PHE B 294 ? 0.8067 0.9778 0.8139 0.0690  -0.0002 0.2980  480 PHE A CE1 
4881 C CE2 . PHE B 294 ? 0.7489 0.9753 0.7803 0.0503  0.0021  0.3077  480 PHE A CE2 
4882 C CZ  . PHE B 294 ? 0.7824 0.9892 0.8051 0.0562  -0.0054 0.3070  480 PHE A CZ  
4883 N N   . ASP B 295 ? 0.8401 1.0089 0.8327 0.1240  0.0668  0.2763  481 ASP A N   
4884 C CA  . ASP B 295 ? 0.8144 0.9741 0.7880 0.1305  0.0806  0.2697  481 ASP A CA  
4885 C C   . ASP B 295 ? 0.8425 1.0326 0.8242 0.1166  0.0891  0.2795  481 ASP A C   
4886 O O   . ASP B 295 ? 0.8707 1.0924 0.8714 0.1239  0.1023  0.2850  481 ASP A O   
4887 C CB  . ASP B 295 ? 0.8287 0.9897 0.8087 0.1553  0.0916  0.2643  481 ASP A CB  
4888 C CG  . ASP B 295 ? 0.9543 1.0980 0.9065 0.1634  0.1045  0.2542  481 ASP A CG  
4889 O OD1 . ASP B 295 ? 1.0336 1.1635 0.9612 0.1501  0.1039  0.2531  481 ASP A OD1 
4890 O OD2 . ASP B 295 ? 1.0279 1.1705 0.9816 0.1835  0.1149  0.2473  481 ASP A OD2 
4891 N N   . ASP B 296 ? 0.9047 1.0839 0.8726 0.0958  0.0821  0.2812  482 ASP A N   
4892 C CA  . ASP B 296 ? 0.8836 1.0866 0.8588 0.0777  0.0878  0.2909  482 ASP A CA  
4893 C C   . ASP B 296 ? 0.8231 1.0734 0.8384 0.0733  0.0874  0.3020  482 ASP A C   
4894 O O   . ASP B 296 ? 0.8187 1.0761 0.8476 0.0656  0.0728  0.3049  482 ASP A O   
4895 C CB  . ASP B 296 ? 0.9583 1.1603 0.9166 0.0822  0.1059  0.2908  482 ASP A CB  
4896 C CG  . ASP B 296 ? 1.0364 1.1935 0.9529 0.0817  0.1035  0.2821  482 ASP A CG  
4897 O OD1 . ASP B 296 ? 0.9204 1.0542 0.8253 0.0688  0.0897  0.2799  482 ASP A OD1 
4898 O OD2 . ASP B 296 ? 1.1125 1.2584 1.0078 0.0947  0.1151  0.2771  482 ASP A OD2 
4899 N N   . ASP B 297 ? 0.8920 1.1762 0.9264 0.0776  0.1031  0.3082  483 ASP A N   
4900 C CA  . ASP B 297 ? 0.8791 1.2133 0.9562 0.0744  0.1026  0.3184  483 ASP A CA  
4901 C C   . ASP B 297 ? 0.7949 1.1429 0.8954 0.0960  0.0975  0.3185  483 ASP A C   
4902 O O   . ASP B 297 ? 0.7859 1.1729 0.9217 0.0943  0.0913  0.3272  483 ASP A O   
4903 C CB  . ASP B 297 ? 0.8149 1.1836 0.9082 0.0717  0.1229  0.3245  483 ASP A CB  
4904 C CG  . ASP B 297 ? 0.9098 1.2786 0.9988 0.0964  0.1411  0.3189  483 ASP A CG  
4905 O OD1 . ASP B 297 ? 1.0106 1.3387 1.0670 0.1094  0.1406  0.3085  483 ASP A OD1 
4906 O OD2 . ASP B 297 ? 0.8566 1.2674 0.9760 0.1027  0.1559  0.3238  483 ASP A OD2 
4907 N N   . VAL B 298 ? 0.8252 1.1417 0.9073 0.1160  0.0990  0.3093  484 VAL A N   
4908 C CA  . VAL B 298 ? 0.8002 1.1229 0.9020 0.1379  0.0953  0.3093  484 VAL A CA  
4909 C C   . VAL B 298 ? 0.8319 1.1263 0.9219 0.1337  0.0759  0.3081  484 VAL A C   
4910 O O   . VAL B 298 ? 0.8524 1.1044 0.9113 0.1330  0.0726  0.2983  484 VAL A O   
4911 C CB  . VAL B 298 ? 0.8182 1.1223 0.9079 0.1620  0.1100  0.2989  484 VAL A CB  
4912 C CG1 . VAL B 298 ? 0.8207 1.1303 0.9339 0.1854  0.1069  0.2996  484 VAL A CG1 
4913 C CG2 . VAL B 298 ? 0.8326 1.1609 0.9261 0.1638  0.1314  0.2990  484 VAL A CG2 
4914 N N   . VAL B 299 ? 0.7801 1.0991 0.8949 0.1307  0.0629  0.3181  485 VAL A N   
4915 C CA  . VAL B 299 ? 0.7741 1.0703 0.8788 0.1275  0.0458  0.3189  485 VAL A CA  
4916 C C   . VAL B 299 ? 0.8187 1.1245 0.9456 0.1495  0.0420  0.3251  485 VAL A C   
4917 O O   . VAL B 299 ? 0.9955 1.3431 1.1556 0.1543  0.0397  0.3358  485 VAL A O   
4918 C CB  . VAL B 299 ? 0.7837 1.0957 0.8913 0.1029  0.0316  0.3256  485 VAL A CB  
4919 C CG1 . VAL B 299 ? 0.7970 1.0830 0.8889 0.0993  0.0162  0.3254  485 VAL A CG1 
4920 C CG2 . VAL B 299 ? 0.7605 1.0635 0.8498 0.0821  0.0363  0.3202  485 VAL A CG2 
4921 N N   . SER B 300 ? 0.8274 1.0944 0.9375 0.1626  0.0408  0.3187  486 SER A N   
4922 C CA  . SER B 300 ? 0.8655 1.1327 0.9936 0.1853  0.0386  0.3240  486 SER A CA  
4923 C C   . SER B 300 ? 0.8033 1.0309 0.9114 0.1844  0.0274  0.3232  486 SER A C   
4924 O O   . SER B 300 ? 0.8405 1.0372 0.9206 0.1703  0.0251  0.3144  486 SER A O   
4925 C CB  . SER B 300 ? 0.8276 1.0885 0.9609 0.2088  0.0556  0.3151  486 SER A CB  
4926 O OG  . SER B 300 ? 0.8188 1.0390 0.9192 0.2071  0.0626  0.2996  486 SER A OG  
4927 N N   . ARG B 301 ? 0.8148 1.0438 0.9387 0.1998  0.0207  0.3329  487 ARG A N   
4928 C CA  . ARG B 301 ? 0.8245 1.0151 0.9314 0.2012  0.0122  0.3342  487 ARG A CA  
4929 C C   . ARG B 301 ? 0.8372 0.9856 0.9302 0.2151  0.0227  0.3199  487 ARG A C   
4930 O O   . ARG B 301 ? 0.8459 0.9976 0.9491 0.2325  0.0350  0.3129  487 ARG A O   
4931 C CB  . ARG B 301 ? 0.8377 1.0432 0.9655 0.2137  0.0011  0.3517  487 ARG A CB  
4932 C CG  . ARG B 301 ? 0.8547 1.0881 0.9849 0.1962  -0.0151 0.3653  487 ARG A CG  
4933 C CD  . ARG B 301 ? 0.9516 1.1497 1.0518 0.1825  -0.0242 0.3667  487 ARG A CD  
4934 N NE  . ARG B 301 ? 1.0543 1.2215 1.1528 0.2000  -0.0255 0.3728  487 ARG A NE  
4935 C CZ  . ARG B 301 ? 1.0067 1.1377 1.0809 0.1924  -0.0300 0.3746  487 ARG A CZ  
4936 N NH1 . ARG B 301 ? 1.0427 1.1645 1.0925 0.1686  -0.0334 0.3695  487 ARG A NH1 
4937 N NH2 . ARG B 301 ? 0.9421 1.0450 1.0174 0.2090  -0.0303 0.3816  487 ARG A NH2 
4938 N N   . CYS B 302 ? 0.7527 0.9016 1.0584 0.1266  -0.0584 0.1417  488 CYS A N   
4939 C CA  . CYS B 302 ? 0.8180 0.9525 1.1318 0.1358  -0.0492 0.1316  488 CYS A CA  
4940 C C   . CYS B 302 ? 0.7581 0.8584 1.0681 0.1438  -0.0541 0.1440  488 CYS A C   
4941 O O   . CYS B 302 ? 0.7701 0.8528 1.0549 0.1390  -0.0624 0.1610  488 CYS A O   
4942 C CB  . CYS B 302 ? 0.7432 0.8704 1.0255 0.1268  -0.0372 0.1215  488 CYS A CB  
4943 S SG  . CYS B 302 ? 0.8024 0.8983 1.0328 0.1111  -0.0399 0.1356  488 CYS A SG  
4944 N N   . THR B 303 ? 0.7533 0.8447 1.0900 0.1560  -0.0473 0.1339  489 THR A N   
4945 C CA  . THR B 303 ? 0.7626 0.8194 1.1028 0.1642  -0.0470 0.1440  489 THR A CA  
4946 C C   . THR B 303 ? 0.8370 0.8625 1.1366 0.1538  -0.0423 0.1453  489 THR A C   
4947 O O   . THR B 303 ? 0.8618 0.8921 1.1391 0.1445  -0.0379 0.1334  489 THR A O   
4948 C CB  . THR B 303 ? 0.7582 0.8159 1.1474 0.1797  -0.0388 0.1289  489 THR A CB  
4949 O OG1 . THR B 303 ? 0.7456 0.8078 1.1325 0.1778  -0.0290 0.1048  489 THR A OG1 
4950 C CG2 . THR B 303 ? 0.7561 0.8476 1.1900 0.1891  -0.0428 0.1241  489 THR A CG2 
4951 N N   . LYS B 304 ? 0.8359 0.8278 1.1256 0.1559  -0.0428 0.1607  490 LYS A N   
4952 C CA  . LYS B 304 ? 0.8490 0.8086 1.1073 0.1465  -0.0371 0.1600  490 LYS A CA  
4953 C C   . LYS B 304 ? 0.8603 0.8121 1.1387 0.1518  -0.0263 0.1359  490 LYS A C   
4954 O O   . LYS B 304 ? 0.8529 0.7905 1.1065 0.1431  -0.0233 0.1267  490 LYS A O   
4955 C CB  . LYS B 304 ? 0.8064 0.7316 1.0526 0.1485  -0.0369 0.1812  490 LYS A CB  
4956 C CG  . LYS B 304 ? 0.9257 0.8204 1.1335 0.1348  -0.0330 0.1836  490 LYS A CG  
4957 C CD  . LYS B 304 ? 1.0272 0.9004 1.2072 0.1326  -0.0368 0.2086  490 LYS A CD  
4958 C CE  . LYS B 304 ? 0.9036 0.7527 1.1077 0.1489  -0.0293 0.2219  490 LYS A CE  
4959 N NZ  . LYS B 304 ? 1.1891 1.0072 1.4152 0.1513  -0.0120 0.2080  490 LYS A NZ  
4960 N N   . GLU B 305 ? 0.8854 0.8480 1.2115 0.1667  -0.0212 0.1235  491 GLU A N   
4961 C CA  . GLU B 305 ? 0.7759 0.7400 1.1259 0.1734  -0.0126 0.0950  491 GLU A CA  
4962 C C   . GLU B 305 ? 0.8047 0.7968 1.1329 0.1679  -0.0148 0.0782  491 GLU A C   
4963 O O   . GLU B 305 ? 0.7951 0.7805 1.1118 0.1675  -0.0118 0.0599  491 GLU A O   
4964 C CB  . GLU B 305 ? 0.7671 0.7423 1.1783 0.1903  -0.0067 0.0834  491 GLU A CB  
4965 C CG  . GLU B 305 ? 0.8349 0.7763 1.2748 0.1988  0.0008  0.0965  491 GLU A CG  
4966 C CD  . GLU B 305 ? 0.8454 0.7812 1.2761 0.2002  -0.0064 0.1294  491 GLU A CD  
4967 O OE1 . GLU B 305 ? 0.8412 0.8004 1.2455 0.1935  -0.0184 0.1398  491 GLU A OE1 
4968 O OE2 . GLU B 305 ? 0.8228 0.7310 1.2747 0.2092  0.0005  0.1445  491 GLU A OE2 
4969 N N   . GLU B 306 ? 0.8031 0.8263 1.1261 0.1646  -0.0193 0.0839  492 GLU A N   
4970 C CA  . GLU B 306 ? 0.8056 0.8531 1.1054 0.1594  -0.0178 0.0712  492 GLU A CA  
4971 C C   . GLU B 306 ? 0.7971 0.8265 1.0451 0.1447  -0.0200 0.0803  492 GLU A C   
4972 O O   . GLU B 306 ? 0.7967 0.8328 1.0213 0.1429  -0.0171 0.0686  492 GLU A O   
4973 C CB  . GLU B 306 ? 0.7947 0.8777 1.1058 0.1581  -0.0190 0.0748  492 GLU A CB  
4974 C CG  . GLU B 306 ? 0.8323 0.9407 1.1223 0.1541  -0.0128 0.0622  492 GLU A CG  
4975 C CD  . GLU B 306 ? 1.0046 1.1478 1.3133 0.1525  -0.0107 0.0627  492 GLU A CD  
4976 O OE1 . GLU B 306 ? 0.9322 1.0827 1.2758 0.1568  -0.0162 0.0696  492 GLU A OE1 
4977 O OE2 . GLU B 306 ? 0.9721 1.1347 1.2614 0.1475  -0.0027 0.0563  492 GLU A OE2 
4978 N N   . ALA B 307 ? 0.8501 0.8565 1.0795 0.1351  -0.0249 0.1009  493 ALA A N   
4979 C CA  . ALA B 307 ? 0.8008 0.7909 0.9866 0.1199  -0.0268 0.1091  493 ALA A CA  
4980 C C   . ALA B 307 ? 0.8285 0.7860 1.0046 0.1199  -0.0246 0.1000  493 ALA A C   
4981 O O   . ALA B 307 ? 0.8574 0.8063 1.0029 0.1113  -0.0251 0.0972  493 ALA A O   
4982 C CB  . ALA B 307 ? 0.8085 0.7931 0.9794 0.1089  -0.0335 0.1319  493 ALA A CB  
4983 N N   . ILE B 308 ? 0.8401 0.7782 1.0445 0.1294  -0.0213 0.0950  494 ILE A N   
4984 C CA  . ILE B 308 ? 0.7948 0.6989 0.9948 0.1278  -0.0179 0.0862  494 ILE A CA  
4985 C C   . ILE B 308 ? 0.7846 0.6910 1.0179 0.1428  -0.0131 0.0571  494 ILE A C   
4986 O O   . ILE B 308 ? 0.8812 0.7874 1.1008 0.1436  -0.0149 0.0391  494 ILE A O   
4987 C CB  . ILE B 308 ? 0.8106 0.6839 1.0148 0.1248  -0.0148 0.1038  494 ILE A CB  
4988 C CG1 . ILE B 308 ? 0.8659 0.7408 1.0350 0.1109  -0.0217 0.1288  494 ILE A CG1 
4989 C CG2 . ILE B 308 ? 0.8407 0.6778 1.0452 0.1220  -0.0083 0.0927  494 ILE A CG2 
4990 C CD1 . ILE B 308 ? 0.9569 0.8024 1.1198 0.1084  -0.0191 0.1474  494 ILE A CD1 
4991 N N   . GLU B 309 ? 0.7981 0.7087 1.0773 0.1559  -0.0075 0.0511  495 GLU A N   
4992 C CA  . GLU B 309 ? 0.7648 0.6763 1.0847 0.1701  -0.0019 0.0201  495 GLU A CA  
4993 C C   . GLU B 309 ? 0.7485 0.6973 1.0677 0.1785  -0.0058 -0.0029 495 GLU A C   
4994 O O   . GLU B 309 ? 0.7766 0.7276 1.1048 0.1871  -0.0062 -0.0314 495 GLU A O   
4995 C CB  . GLU B 309 ? 0.8163 0.7221 1.1911 0.1816  0.0070  0.0205  495 GLU A CB  
4996 C CG  . GLU B 309 ? 0.8952 0.7572 1.2821 0.1792  0.0166  0.0290  495 GLU A CG  
4997 C CD  . GLU B 309 ? 0.9726 0.8150 1.3247 0.1680  0.0149  0.0662  495 GLU A CD  
4998 O OE1 . GLU B 309 ? 0.8792 0.7443 1.2157 0.1662  0.0066  0.0847  495 GLU A OE1 
4999 O OE2 . GLU B 309 ? 1.1515 0.9570 1.4930 0.1614  0.0219  0.0752  495 GLU A OE2 
5000 N N   . HIS B 310 ? 0.7495 0.7286 1.0580 0.1769  -0.0084 0.0075  496 HIS A N   
5001 C CA  . HIS B 310 ? 0.7841 0.7990 1.0913 0.1854  -0.0090 -0.0134 496 HIS A CA  
5002 C C   . HIS B 310 ? 0.7817 0.7965 1.0366 0.1802  -0.0135 -0.0167 496 HIS A C   
5003 O O   . HIS B 310 ? 0.8921 0.9328 1.1387 0.1895  -0.0135 -0.0355 496 HIS A O   
5004 C CB  . HIS B 310 ? 0.7871 0.8334 1.1022 0.1844  -0.0078 -0.0022 496 HIS A CB  
5005 C CG  . HIS B 310 ? 0.8167 0.8718 1.1903 0.1945  -0.0040 -0.0059 496 HIS A CG  
5006 N ND1 . HIS B 310 ? 0.8023 0.8852 1.1950 0.1955  -0.0037 0.0012  496 HIS A ND1 
5007 C CD2 . HIS B 310 ? 0.8142 0.8527 1.2349 0.2043  0.0006  -0.0155 496 HIS A CD2 
5008 C CE1 . HIS B 310 ? 0.7186 0.8019 1.1666 0.2060  -0.0006 -0.0032 496 HIS A CE1 
5009 N NE2 . HIS B 310 ? 0.7185 0.7744 1.1845 0.2115  0.0031  -0.0124 496 HIS A NE2 
5010 N N   . ASN B 311 ? 0.7398 0.7265 0.9591 0.1665  -0.0170 0.0011  497 ASN A N   
5011 C CA  . ASN B 311 ? 0.8045 0.7869 0.9772 0.1619  -0.0213 -0.0001 497 ASN A CA  
5012 C C   . ASN B 311 ? 0.8068 0.7635 0.9807 0.1665  -0.0256 -0.0190 497 ASN A C   
5013 O O   . ASN B 311 ? 0.7573 0.7028 0.8938 0.1617  -0.0308 -0.0173 497 ASN A O   
5014 C CB  . ASN B 311 ? 0.8154 0.7880 0.9509 0.1428  -0.0222 0.0299  497 ASN A CB  
5015 C CG  . ASN B 311 ? 0.8387 0.8414 0.9672 0.1390  -0.0182 0.0427  497 ASN A CG  
5016 O OD1 . ASN B 311 ? 0.7907 0.8143 0.8999 0.1435  -0.0150 0.0365  497 ASN A OD1 
5017 N ND2 . ASN B 311 ? 0.9040 0.9093 1.0484 0.1316  -0.0179 0.0600  497 ASN A ND2 
5018 N N   . TYR B 312 ? 0.7420 0.6882 0.9618 0.1756  -0.0227 -0.0374 498 TYR A N   
5019 C CA  . TYR B 312 ? 0.8014 0.7239 1.0311 0.1803  -0.0257 -0.0598 498 TYR A CA  
5020 C C   . TYR B 312 ? 0.8423 0.7857 1.0640 0.1967  -0.0334 -0.0907 498 TYR A C   
5021 O O   . TYR B 312 ? 0.8335 0.7596 1.0470 0.1993  -0.0403 -0.1066 498 TYR A O   
5022 C CB  . TYR B 312 ? 0.8432 0.7484 1.1305 0.1857  -0.0170 -0.0717 498 TYR A CB  
5023 C CG  . TYR B 312 ? 0.7859 0.6588 1.0722 0.1707  -0.0102 -0.0427 498 TYR A CG  
5024 C CD1 . TYR B 312 ? 0.7497 0.6104 0.9880 0.1532  -0.0141 -0.0145 498 TYR A CD1 
5025 C CD2 . TYR B 312 ? 0.8026 0.6566 1.1363 0.1748  0.0012  -0.0444 498 TYR A CD2 
5026 C CE1 . TYR B 312 ? 0.7409 0.5748 0.9750 0.1407  -0.0088 0.0098  498 TYR A CE1 
5027 C CE2 . TYR B 312 ? 0.7967 0.6202 1.1230 0.1629  0.0080  -0.0166 498 TYR A CE2 
5028 C CZ  . TYR B 312 ? 0.7435 0.5584 1.0182 0.1462  0.0021  0.0095  498 TYR A CZ  
5029 O OH  . TYR B 312 ? 0.7594 0.5469 1.0239 0.1357  0.0082  0.0351  498 TYR A OH  
5030 N N   . GLY B 313 ? 0.8080 0.7887 1.0320 0.2085  -0.0329 -0.1010 499 GLY A N   
5031 C CA  . GLY B 313 ? 0.7688 0.7731 0.9776 0.2259  -0.0406 -0.1293 499 GLY A CA  
5032 C C   . GLY B 313 ? 0.7634 0.7867 1.0284 0.2457  -0.0405 -0.1706 499 GLY A C   
5033 O O   . GLY B 313 ? 0.7481 0.7655 1.0686 0.2454  -0.0320 -0.1757 499 GLY A O   
5034 N N   . ARG B 322 ? 1.5913 1.8702 1.3242 0.3582  -0.0091 -0.1613 508 ARG A N   
5035 C CA  . ARG B 322 ? 1.6680 1.9030 1.4151 0.3364  -0.0135 -0.1325 508 ARG A CA  
5036 C C   . ARG B 322 ? 1.6250 1.8587 1.4322 0.3113  -0.0005 -0.1209 508 ARG A C   
5037 O O   . ARG B 322 ? 1.6983 1.9541 1.5654 0.3137  -0.0021 -0.1483 508 ARG A O   
5038 C CB  . ARG B 322 ? 1.6514 1.8575 1.3284 0.3304  -0.0060 -0.0910 508 ARG A CB  
5039 C CG  . ARG B 322 ? 1.6922 1.9154 1.3203 0.3309  0.0191  -0.0708 508 ARG A CG  
5040 C CD  . ARG B 322 ? 1.6894 1.8791 1.2553 0.3244  0.0283  -0.0282 508 ARG A CD  
5041 N NE  . ARG B 322 ? 1.7654 1.9664 1.2887 0.3221  0.0574  -0.0054 508 ARG A NE  
5042 C CZ  . ARG B 322 ? 1.7495 1.9259 1.2151 0.3195  0.0717  0.0316  508 ARG A CZ  
5043 N NH1 . ARG B 322 ? 1.7566 1.8970 1.1992 0.3194  0.0581  0.0501  508 ARG A NH1 
5044 N NH2 . ARG B 322 ? 1.7886 1.9756 1.2219 0.3166  0.1021  0.0503  508 ARG A NH2 
5045 N N   . HIS B 323 ? 1.5075 1.7158 1.3009 0.2883  0.0115  -0.0812 509 HIS A N   
5046 C CA  . HIS B 323 ? 1.4243 1.6331 1.2611 0.2649  0.0253  -0.0643 509 HIS A CA  
5047 C C   . HIS B 323 ? 1.3750 1.5695 1.2755 0.2553  0.0131  -0.0725 509 HIS A C   
5048 O O   . HIS B 323 ? 1.3533 1.5467 1.2904 0.2377  0.0209  -0.0586 509 HIS A O   
5049 C CB  . HIS B 323 ? 1.4686 1.7177 1.3246 0.2683  0.0417  -0.0783 509 HIS A CB  
5050 C CG  . HIS B 323 ? 1.6132 1.8752 1.4094 0.2731  0.0609  -0.0648 509 HIS A CG  
5051 N ND1 . HIS B 323 ? 1.6407 1.8815 1.3679 0.2792  0.0616  -0.0441 509 HIS A ND1 
5052 C CD2 . HIS B 323 ? 1.6433 1.9364 1.4385 0.2734  0.0818  -0.0691 509 HIS A CD2 
5053 C CE1 . HIS B 323 ? 1.5654 1.8219 1.2489 0.2833  0.0834  -0.0340 509 HIS A CE1 
5054 N NE2 . HIS B 323 ? 1.6025 1.8913 1.3264 0.2793  0.0965  -0.0499 509 HIS A NE2 
5055 N N   . CYS B 324 ? 1.3009 1.4833 1.2153 0.2665  -0.0051 -0.0941 510 CYS A N   
5056 C CA  . CYS B 324 ? 1.1368 1.3040 1.1116 0.2589  -0.0134 -0.1027 510 CYS A CA  
5057 C C   . CYS B 324 ? 1.1107 1.2405 1.0790 0.2361  -0.0134 -0.0688 510 CYS A C   
5058 O O   . CYS B 324 ? 1.1753 1.2810 1.1014 0.2330  -0.0184 -0.0537 510 CYS A O   
5059 C CB  . CYS B 324 ? 1.0898 1.2540 1.0831 0.2774  -0.0303 -0.1377 510 CYS A CB  
5060 S SG  . CYS B 324 ? 1.2647 1.4180 1.1879 0.2937  -0.0436 -0.1406 510 CYS A SG  
5061 N N   . THR B 325 ? 0.9789 1.1052 0.9895 0.2210  -0.0084 -0.0574 511 THR A N   
5062 C CA  . THR B 325 ? 1.0127 1.1095 1.0178 0.1993  -0.0077 -0.0264 511 THR A CA  
5063 C C   . THR B 325 ? 0.9663 1.0292 0.9780 0.1975  -0.0206 -0.0307 511 THR A C   
5064 O O   . THR B 325 ? 0.9270 0.9872 0.9783 0.2066  -0.0269 -0.0541 511 THR A O   
5065 C CB  . THR B 325 ? 0.9634 1.0686 1.0113 0.1873  -0.0013 -0.0158 511 THR A CB  
5066 O OG1 . THR B 325 ? 0.9385 1.0738 0.9814 0.1865  0.0118  -0.0114 511 THR A OG1 
5067 C CG2 . THR B 325 ? 0.9086 0.9858 0.9528 0.1668  -0.0030 0.0121  511 THR A CG2 
5068 N N   . ASN B 326 ? 0.8575 0.8943 0.8343 0.1851  -0.0227 -0.0090 512 ASN A N   
5069 C CA  . ASN B 326 ? 0.8385 0.8419 0.8175 0.1810  -0.0336 -0.0116 512 ASN A CA  
5070 C C   . ASN B 326 ? 0.8619 0.8422 0.8344 0.1572  -0.0305 0.0182  512 ASN A C   
5071 O O   . ASN B 326 ? 0.8428 0.8273 0.7880 0.1466  -0.0228 0.0408  512 ASN A O   
5072 C CB  . ASN B 326 ? 0.8821 0.8774 0.8217 0.1937  -0.0428 -0.0213 512 ASN A CB  
5073 C CG  . ASN B 326 ? 1.0458 1.0658 0.9910 0.2195  -0.0490 -0.0555 512 ASN A CG  
5074 O OD1 . ASN B 326 ? 1.1358 1.1791 1.0476 0.2316  -0.0454 -0.0570 512 ASN A OD1 
5075 N ND2 . ASN B 326 ? 1.0643 1.0799 1.0529 0.2283  -0.0572 -0.0846 512 ASN A ND2 
5076 N N   . ALA B 327 ? 0.8702 0.8265 0.8690 0.1490  -0.0351 0.0170  513 ALA A N   
5077 C CA  . ALA B 327 ? 0.7944 0.7283 0.7859 0.1274  -0.0340 0.0409  513 ALA A CA  
5078 C C   . ALA B 327 ? 0.8035 0.7113 0.7682 0.1233  -0.0409 0.0415  513 ALA A C   
5079 O O   . ALA B 327 ? 0.8038 0.6975 0.7772 0.1334  -0.0492 0.0200  513 ALA A O   
5080 C CB  . ALA B 327 ? 0.7747 0.6948 0.8029 0.1211  -0.0340 0.0411  513 ALA A CB  
5081 N N   . TYR B 328 ? 0.8113 0.7134 0.7480 0.1089  -0.0373 0.0642  514 TYR A N   
5082 C CA  . TYR B 328 ? 0.8227 0.7014 0.7342 0.1050  -0.0432 0.0672  514 TYR A CA  
5083 C C   . TYR B 328 ? 0.8102 0.6661 0.7251 0.0820  -0.0427 0.0828  514 TYR A C   
5084 O O   . TYR B 328 ? 0.8142 0.6466 0.7200 0.0782  -0.0492 0.0798  514 TYR A O   
5085 C CB  . TYR B 328 ? 0.8510 0.7405 0.7234 0.1108  -0.0384 0.0794  514 TYR A CB  
5086 C CG  . TYR B 328 ? 0.8533 0.7568 0.7191 0.0961  -0.0240 0.1044  514 TYR A CG  
5087 C CD1 . TYR B 328 ? 0.8525 0.7851 0.7286 0.1003  -0.0147 0.1049  514 TYR A CD1 
5088 C CD2 . TYR B 328 ? 0.8560 0.7450 0.7110 0.0779  -0.0192 0.1249  514 TYR A CD2 
5089 C CE1 . TYR B 328 ? 0.8741 0.8206 0.7502 0.0870  -0.0012 0.1242  514 TYR A CE1 
5090 C CE2 . TYR B 328 ? 0.8578 0.7614 0.7141 0.0645  -0.0051 0.1441  514 TYR A CE2 
5091 C CZ  . TYR B 328 ? 0.9127 0.8449 0.7796 0.0693  0.0038  0.1433  514 TYR A CZ  
5092 O OH  . TYR B 328 ? 0.8622 0.8100 0.7361 0.0563  0.0182  0.1590  514 TYR A OH  
5093 N N   . MET B 329 ? 0.7966 0.6602 0.7252 0.0673  -0.0362 0.0974  515 MET A N   
5094 C CA  . MET B 329 ? 0.7860 0.6321 0.7181 0.0461  -0.0362 0.1094  515 MET A CA  
5095 C C   . MET B 329 ? 0.7704 0.6205 0.7265 0.0399  -0.0350 0.1123  515 MET A C   
5096 O O   . MET B 329 ? 0.7685 0.6418 0.7355 0.0461  -0.0314 0.1153  515 MET A O   
5097 C CB  . MET B 329 ? 0.7939 0.6473 0.7097 0.0320  -0.0291 0.1295  515 MET A CB  
5098 C CG  . MET B 329 ? 0.7827 0.6229 0.7056 0.0098  -0.0293 0.1387  515 MET A CG  
5099 S SD  . MET B 329 ? 0.8207 0.6677 0.7334 -0.0065 -0.0195 0.1579  515 MET A SD  
5100 C CE  . MET B 329 ? 0.7747 0.6123 0.7047 -0.0308 -0.0222 0.1606  515 MET A CE  
5101 N N   . LEU B 330 ? 0.7623 0.5890 0.7257 0.0288  -0.0377 0.1113  516 LEU A N   
5102 C CA  . LEU B 330 ? 0.7543 0.5796 0.7337 0.0235  -0.0365 0.1166  516 LEU A CA  
5103 C C   . LEU B 330 ? 0.7516 0.5679 0.7233 0.0026  -0.0366 0.1283  516 LEU A C   
5104 O O   . LEU B 330 ? 0.8201 0.6185 0.7829 -0.0076 -0.0379 0.1254  516 LEU A O   
5105 C CB  . LEU B 330 ? 0.7519 0.5558 0.7501 0.0329  -0.0368 0.1015  516 LEU A CB  
5106 C CG  . LEU B 330 ? 0.7881 0.5998 0.8019 0.0542  -0.0373 0.0831  516 LEU A CG  
5107 C CD1 . LEU B 330 ? 0.7815 0.5678 0.8203 0.0606  -0.0355 0.0655  516 LEU A CD1 
5108 C CD2 . LEU B 330 ? 0.8230 0.6644 0.8483 0.0634  -0.0344 0.0895  516 LEU A CD2 
5109 N N   . VAL B 331 ? 0.7666 0.5966 0.7430 -0.0031 -0.0362 0.1399  517 VAL A N   
5110 C CA  . VAL B 331 ? 0.7491 0.5758 0.7194 -0.0216 -0.0373 0.1484  517 VAL A CA  
5111 C C   . VAL B 331 ? 0.7533 0.5686 0.7274 -0.0201 -0.0380 0.1513  517 VAL A C   
5112 O O   . VAL B 331 ? 0.7567 0.5858 0.7395 -0.0088 -0.0390 0.1571  517 VAL A O   
5113 C CB  . VAL B 331 ? 0.7481 0.6055 0.7188 -0.0298 -0.0371 0.1592  517 VAL A CB  
5114 C CG1 . VAL B 331 ? 0.7471 0.6032 0.7145 -0.0486 -0.0391 0.1631  517 VAL A CG1 
5115 C CG2 . VAL B 331 ? 0.7498 0.6160 0.7159 -0.0293 -0.0322 0.1592  517 VAL A CG2 
5116 N N   . TYR B 332 ? 0.7557 0.5451 0.7236 -0.0311 -0.0367 0.1479  518 TYR A N   
5117 C CA  . TYR B 332 ? 0.7661 0.5401 0.7318 -0.0311 -0.0344 0.1527  518 TYR A CA  
5118 C C   . TYR B 332 ? 0.7884 0.5675 0.7395 -0.0487 -0.0369 0.1595  518 TYR A C   
5119 O O   . TYR B 332 ? 0.7995 0.5797 0.7476 -0.0638 -0.0377 0.1547  518 TYR A O   
5120 C CB  . TYR B 332 ? 0.8152 0.5524 0.7880 -0.0284 -0.0274 0.1401  518 TYR A CB  
5121 C CG  . TYR B 332 ? 0.7682 0.5009 0.7612 -0.0086 -0.0242 0.1318  518 TYR A CG  
5122 C CD1 . TYR B 332 ? 0.7589 0.4968 0.7612 0.0000  -0.0268 0.1176  518 TYR A CD1 
5123 C CD2 . TYR B 332 ? 0.7793 0.5031 0.7831 0.0025  -0.0182 0.1378  518 TYR A CD2 
5124 C CE1 . TYR B 332 ? 0.7581 0.4959 0.7821 0.0185  -0.0244 0.1060  518 TYR A CE1 
5125 C CE2 . TYR B 332 ? 0.7775 0.4988 0.8072 0.0201  -0.0142 0.1279  518 TYR A CE2 
5126 C CZ  . TYR B 332 ? 0.7654 0.4955 0.8065 0.0277  -0.0176 0.1102  518 TYR A CZ  
5127 O OH  . TYR B 332 ? 0.7731 0.5046 0.8430 0.0456  -0.0141 0.0965  518 TYR A OH  
5128 N N   . ILE B 333 ? 0.7916 0.5747 0.7343 -0.0457 -0.0383 0.1704  519 ILE A N   
5129 C CA  . ILE B 333 ? 0.8096 0.6000 0.7361 -0.0598 -0.0417 0.1750  519 ILE A CA  
5130 C C   . ILE B 333 ? 0.8527 0.6137 0.7646 -0.0585 -0.0349 0.1792  519 ILE A C   
5131 O O   . ILE B 333 ? 0.8555 0.6053 0.7691 -0.0426 -0.0311 0.1874  519 ILE A O   
5132 C CB  . ILE B 333 ? 0.8191 0.6485 0.7452 -0.0560 -0.0519 0.1843  519 ILE A CB  
5133 C CG1 . ILE B 333 ? 0.7797 0.6356 0.7230 -0.0586 -0.0542 0.1798  519 ILE A CG1 
5134 C CG2 . ILE B 333 ? 0.8172 0.6573 0.7271 -0.0688 -0.0571 0.1854  519 ILE A CG2 
5135 C CD1 . ILE B 333 ? 0.8141 0.7095 0.7651 -0.0562 -0.0628 0.1846  519 ILE A CD1 
5136 N N   . ARG B 334 ? 0.8657 0.6131 0.7651 -0.0756 -0.0315 0.1733  520 ARG A N   
5137 C CA  . ARG B 334 ? 0.8596 0.5764 0.7424 -0.0769 -0.0214 0.1765  520 ARG A CA  
5138 C C   . ARG B 334 ? 0.9694 0.6983 0.8300 -0.0657 -0.0257 0.1949  520 ARG A C   
5139 O O   . ARG B 334 ? 0.9845 0.7485 0.8374 -0.0664 -0.0387 0.1995  520 ARG A O   
5140 C CB  . ARG B 334 ? 0.9595 0.6656 0.8341 -0.0992 -0.0176 0.1647  520 ARG A CB  
5141 C CG  . ARG B 334 ? 1.0297 0.6959 0.8936 -0.1035 -0.0020 0.1621  520 ARG A CG  
5142 C CD  . ARG B 334 ? 1.0560 0.7176 0.9132 -0.1268 0.0009  0.1489  520 ARG A CD  
5143 N NE  . ARG B 334 ? 1.1932 0.8140 1.0455 -0.1330 0.0185  0.1425  520 ARG A NE  
5144 C CZ  . ARG B 334 ? 1.1200 0.7137 0.9953 -0.1426 0.0269  0.1238  520 ARG A CZ  
5145 N NH1 . ARG B 334 ? 1.0160 0.6180 0.9164 -0.1460 0.0180  0.1112  520 ARG A NH1 
5146 N NH2 . ARG B 334 ? 1.1826 0.7393 1.0559 -0.1480 0.0451  0.1174  520 ARG A NH2 
5147 N N   . GLU B 335 ? 0.9499 0.6490 0.8021 -0.0544 -0.0144 0.2049  521 GLU A N   
5148 C CA  . GLU B 335 ? 0.9321 0.6379 0.7612 -0.0397 -0.0179 0.2257  521 GLU A CA  
5149 C C   . GLU B 335 ? 0.9832 0.7036 0.7781 -0.0502 -0.0244 0.2287  521 GLU A C   
5150 O O   . GLU B 335 ? 1.0514 0.8021 0.8310 -0.0410 -0.0390 0.2393  521 GLU A O   
5151 C CB  . GLU B 335 ? 0.9920 0.6562 0.8198 -0.0273 0.0002  0.2365  521 GLU A CB  
5152 C CG  . GLU B 335 ? 1.1658 0.8348 0.9861 -0.0042 -0.0032 0.2598  521 GLU A CG  
5153 C CD  . GLU B 335 ? 1.2747 0.9003 1.1051 0.0082  0.0182  0.2692  521 GLU A CD  
5154 O OE1 . GLU B 335 ? 1.2725 0.8621 1.1030 -0.0026 0.0371  0.2605  521 GLU A OE1 
5155 O OE2 . GLU B 335 ? 1.3117 0.9389 1.1544 0.0285  0.0172  0.2841  521 GLU A OE2 
5156 N N   . SER B 336 ? 1.0473 0.7485 0.8322 -0.0690 -0.0145 0.2169  522 SER A N   
5157 C CA  . SER B 336 ? 1.1126 0.8289 0.8661 -0.0801 -0.0195 0.2159  522 SER A CA  
5158 C C   . SER B 336 ? 1.0481 0.8130 0.8123 -0.0889 -0.0387 0.2051  522 SER A C   
5159 O O   . SER B 336 ? 1.0886 0.8798 0.8300 -0.0908 -0.0491 0.2055  522 SER A O   
5160 C CB  . SER B 336 ? 1.1137 0.7980 0.8606 -0.0998 -0.0026 0.2025  522 SER A CB  
5161 O OG  . SER B 336 ? 1.0238 0.7044 0.8047 -0.1153 -0.0010 0.1820  522 SER A OG  
5162 N N   . LYS B 337 ? 0.9817 0.7591 0.7806 -0.0937 -0.0427 0.1945  523 LYS A N   
5163 C CA  . LYS B 337 ? 1.0296 0.8495 0.8459 -0.1030 -0.0564 0.1839  523 LYS A CA  
5164 C C   . LYS B 337 ? 1.0130 0.8642 0.8445 -0.0867 -0.0688 0.1919  523 LYS A C   
5165 O O   . LYS B 337 ? 0.9538 0.8394 0.8060 -0.0935 -0.0775 0.1828  523 LYS A O   
5166 C CB  . LYS B 337 ? 0.9375 0.7501 0.7817 -0.1210 -0.0504 0.1673  523 LYS A CB  
5167 C CG  . LYS B 337 ? 1.0641 0.8463 0.9025 -0.1388 -0.0385 0.1555  523 LYS A CG  
5168 C CD  . LYS B 337 ? 1.0885 0.8903 0.9109 -0.1531 -0.0424 0.1474  523 LYS A CD  
5169 C CE  . LYS B 337 ? 1.1178 0.8901 0.9392 -0.1724 -0.0293 0.1332  523 LYS A CE  
5170 N NZ  . LYS B 337 ? 1.2961 1.0898 1.1028 -0.1870 -0.0323 0.1224  523 LYS A NZ  
5171 N N   . LEU B 338 ? 1.0377 0.8774 0.8636 -0.0658 -0.0682 0.2077  524 LEU A N   
5172 C CA  . LEU B 338 ? 0.8878 0.7529 0.7357 -0.0512 -0.0773 0.2125  524 LEU A CA  
5173 C C   . LEU B 338 ? 0.9738 0.8855 0.8227 -0.0488 -0.0951 0.2108  524 LEU A C   
5174 O O   . LEU B 338 ? 0.9685 0.9103 0.8455 -0.0506 -0.1010 0.2031  524 LEU A O   
5175 C CB  . LEU B 338 ? 0.9055 0.7490 0.7503 -0.0293 -0.0730 0.2289  524 LEU A CB  
5176 C CG  . LEU B 338 ? 0.8927 0.7585 0.7644 -0.0134 -0.0801 0.2327  524 LEU A CG  
5177 C CD1 . LEU B 338 ? 0.8568 0.7281 0.7567 -0.0223 -0.0750 0.2186  524 LEU A CD1 
5178 C CD2 . LEU B 338 ? 0.9114 0.7536 0.7845 0.0074  -0.0742 0.2478  524 LEU A CD2 
5179 N N   . SER B 339 ? 1.0309 0.9496 0.8496 -0.0442 -0.1032 0.2167  525 SER A N   
5180 C CA  . SER B 339 ? 0.9356 0.9012 0.7564 -0.0392 -0.1228 0.2120  525 SER A CA  
5181 C C   . SER B 339 ? 0.9619 0.9570 0.8045 -0.0611 -0.1255 0.1896  525 SER A C   
5182 O O   . SER B 339 ? 1.0229 1.0592 0.8919 -0.0603 -0.1373 0.1796  525 SER A O   
5183 C CB  . SER B 339 ? 0.9826 0.9482 0.7603 -0.0265 -0.1318 0.2238  525 SER A CB  
5184 O OG  . SER B 339 ? 1.0733 1.0160 0.8377 -0.0036 -0.1301 0.2467  525 SER A OG  
5185 N N   . GLU B 340 ? 1.0063 0.9809 0.8427 -0.0811 -0.1138 0.1801  526 GLU A N   
5186 C CA  . GLU B 340 ? 0.9082 0.9080 0.7706 -0.1026 -0.1144 0.1589  526 GLU A CA  
5187 C C   . GLU B 340 ? 0.9599 0.9639 0.8626 -0.1089 -0.1074 0.1541  526 GLU A C   
5188 O O   . GLU B 340 ? 1.0064 1.0441 0.9406 -0.1182 -0.1110 0.1407  526 GLU A O   
5189 C CB  . GLU B 340 ? 1.0106 0.9860 0.8584 -0.1220 -0.1034 0.1499  526 GLU A CB  
5190 C CG  . GLU B 340 ? 1.0329 1.0357 0.9101 -0.1445 -0.1042 0.1271  526 GLU A CG  
5191 C CD  . GLU B 340 ? 1.1120 1.0906 0.9803 -0.1646 -0.0930 0.1164  526 GLU A CD  
5192 O OE1 . GLU B 340 ? 1.1297 1.0644 0.9784 -0.1638 -0.0810 0.1253  526 GLU A OE1 
5193 O OE2 . GLU B 340 ? 1.0699 1.0744 0.9557 -0.1815 -0.0955 0.0967  526 GLU A OE2 
5194 N N   . VAL B 341 ? 1.0188 0.9889 0.9217 -0.1036 -0.0963 0.1641  527 VAL A N   
5195 C CA  . VAL B 341 ? 0.8962 0.8700 0.8300 -0.1061 -0.0897 0.1617  527 VAL A CA  
5196 C C   . VAL B 341 ? 0.8902 0.8977 0.8427 -0.0919 -0.0984 0.1649  527 VAL A C   
5197 O O   . VAL B 341 ? 0.8739 0.9037 0.8568 -0.0980 -0.0956 0.1576  527 VAL A O   
5198 C CB  . VAL B 341 ? 0.8404 0.7725 0.7680 -0.1017 -0.0777 0.1685  527 VAL A CB  
5199 C CG1 . VAL B 341 ? 0.8135 0.7520 0.7657 -0.0996 -0.0722 0.1679  527 VAL A CG1 
5200 C CG2 . VAL B 341 ? 0.9032 0.8044 0.8214 -0.1178 -0.0689 0.1610  527 VAL A CG2 
5201 N N   . LEU B 342 ? 0.8271 0.8380 0.7636 -0.0728 -0.1081 0.1758  528 LEU A N   
5202 C CA  . LEU B 342 ? 0.8726 0.9134 0.8288 -0.0573 -0.1175 0.1785  528 LEU A CA  
5203 C C   . LEU B 342 ? 0.9642 1.0456 0.9229 -0.0533 -0.1356 0.1713  528 LEU A C   
5204 O O   . LEU B 342 ? 0.9603 1.0569 0.9166 -0.0341 -0.1486 0.1786  528 LEU A O   
5205 C CB  . LEU B 342 ? 0.8775 0.8961 0.8224 -0.0366 -0.1167 0.1947  528 LEU A CB  
5206 C CG  . LEU B 342 ? 0.8223 0.8085 0.7725 -0.0375 -0.1008 0.1972  528 LEU A CG  
5207 C CD1 . LEU B 342 ? 0.8307 0.8060 0.7839 -0.0162 -0.1006 0.2087  528 LEU A CD1 
5208 C CD2 . LEU B 342 ? 0.7964 0.7962 0.7732 -0.0491 -0.0928 0.1868  528 LEU A CD2 
5209 N N   . GLN B 343 ? 0.9180 1.0182 0.8833 -0.0705 -0.1375 0.1555  529 GLN A N   
5210 C CA  . GLN B 343 ? 0.8898 1.0346 0.8638 -0.0678 -0.1555 0.1422  529 GLN A CA  
5211 C C   . GLN B 343 ? 0.8984 1.0787 0.9093 -0.0563 -0.1639 0.1373  529 GLN A C   
5212 O O   . GLN B 343 ? 0.8433 1.0213 0.8829 -0.0597 -0.1516 0.1374  529 GLN A O   
5213 C CB  . GLN B 343 ? 0.8749 1.0389 0.8695 -0.0912 -0.1519 0.1205  529 GLN A CB  
5214 C CG  . GLN B 343 ? 0.9200 1.0593 0.8836 -0.1041 -0.1466 0.1191  529 GLN A CG  
5215 C CD  . GLN B 343 ? 0.8640 1.0186 0.8590 -0.1291 -0.1391 0.0975  529 GLN A CD  
5216 O OE1 . GLN B 343 ? 0.9263 1.1203 0.9631 -0.1348 -0.1429 0.0802  529 GLN A OE1 
5217 N NE2 . GLN B 343 ? 1.0392 1.1619 1.0192 -0.1443 -0.1272 0.0972  529 GLN A NE2 
5218 N N   . ALA B 344 ? 0.9627 1.1770 0.9725 -0.0421 -0.1852 0.1319  530 ALA A N   
5219 C CA  . ALA B 344 ? 0.8603 1.1159 0.9138 -0.0339 -0.1950 0.1198  530 ALA A CA  
5220 C C   . ALA B 344 ? 0.8351 1.1202 0.9364 -0.0552 -0.1866 0.0949  530 ALA A C   
5221 O O   . ALA B 344 ? 0.8346 1.1280 0.9344 -0.0702 -0.1866 0.0812  530 ALA A O   
5222 C CB  . ALA B 344 ? 0.9043 1.1910 0.9457 -0.0125 -0.2226 0.1174  530 ALA A CB  
5223 N N   . VAL B 345 ? 0.8157 1.1161 0.9619 -0.0567 -0.1775 0.0887  531 VAL A N   
5224 C CA  . VAL B 345 ? 0.7939 1.1190 0.9913 -0.0762 -0.1647 0.0674  531 VAL A CA  
5225 C C   . VAL B 345 ? 0.8458 1.2206 1.0916 -0.0671 -0.1774 0.0474  531 VAL A C   
5226 O O   . VAL B 345 ? 0.7940 1.1725 1.0558 -0.0548 -0.1766 0.0530  531 VAL A O   
5227 C CB  . VAL B 345 ? 0.8199 1.1157 1.0290 -0.0884 -0.1368 0.0775  531 VAL A CB  
5228 C CG1 . VAL B 345 ? 0.7554 1.0763 1.0208 -0.1067 -0.1210 0.0578  531 VAL A CG1 
5229 C CG2 . VAL B 345 ? 0.8985 1.1477 1.0652 -0.0973 -0.1264 0.0929  531 VAL A CG2 
5230 N N   . THR B 346 ? 0.8695 1.2841 1.1425 -0.0732 -0.1891 0.0214  532 THR A N   
5231 C CA  . THR B 346 ? 0.8186 1.2846 1.1440 -0.0650 -0.2030 -0.0036 532 THR A CA  
5232 C C   . THR B 346 ? 0.8253 1.3113 1.2183 -0.0860 -0.1801 -0.0253 532 THR A C   
5233 O O   . THR B 346 ? 0.7861 1.2510 1.1827 -0.1069 -0.1579 -0.0232 532 THR A O   
5234 C CB  . THR B 346 ? 0.8829 1.3861 1.1983 -0.0547 -0.2335 -0.0225 532 THR A CB  
5235 O OG1 . THR B 346 ? 0.8897 1.4012 1.2138 -0.0755 -0.2270 -0.0402 532 THR A OG1 
5236 C CG2 . THR B 346 ? 0.8548 1.3323 1.0977 -0.0340 -0.2521 0.0034  532 THR A CG2 
5237 N N   . ASP B 347 ? 0.8361 1.3623 1.2856 -0.0798 -0.1849 -0.0466 533 ASP A N   
5238 C CA  . ASP B 347 ? 0.7746 1.3215 1.2950 -0.0989 -0.1609 -0.0687 533 ASP A CA  
5239 C C   . ASP B 347 ? 0.7861 1.3607 1.3374 -0.1150 -0.1628 -0.0967 533 ASP A C   
5240 O O   . ASP B 347 ? 0.8211 1.3995 1.4236 -0.1356 -0.1365 -0.1092 533 ASP A O   
5241 C CB  . ASP B 347 ? 0.7546 1.3389 1.3326 -0.0882 -0.1651 -0.0877 533 ASP A CB  
5242 C CG  . ASP B 347 ? 0.8534 1.4096 1.4184 -0.0798 -0.1511 -0.0636 533 ASP A CG  
5243 O OD1 . ASP B 347 ? 0.8216 1.3306 1.3343 -0.0820 -0.1381 -0.0333 533 ASP A OD1 
5244 O OD2 . ASP B 347 ? 0.9717 1.5547 1.5819 -0.0710 -0.1529 -0.0775 533 ASP A OD2 
5245 N N   . HIS B 348 ? 0.7895 1.3839 1.3118 -0.1057 -0.1922 -0.1070 534 HIS A N   
5246 C CA  . HIS B 348 ? 0.8215 1.4432 1.3704 -0.1211 -0.1945 -0.1352 534 HIS A CA  
5247 C C   . HIS B 348 ? 0.8712 1.4501 1.3865 -0.1411 -0.1748 -0.1179 534 HIS A C   
5248 O O   . HIS B 348 ? 0.9113 1.5072 1.4603 -0.1593 -0.1677 -0.1405 534 HIS A O   
5249 C CB  . HIS B 348 ? 0.8934 1.5530 1.4182 -0.1028 -0.2334 -0.1533 534 HIS A CB  
5250 C CG  . HIS B 348 ? 0.9952 1.7016 1.5573 -0.0816 -0.2572 -0.1747 534 HIS A CG  
5251 N ND1 . HIS B 348 ? 0.9947 1.7569 1.6389 -0.0864 -0.2608 -0.2185 534 HIS A ND1 
5252 C CD2 . HIS B 348 ? 1.0378 1.7438 1.5705 -0.0551 -0.2788 -0.1597 534 HIS A CD2 
5253 C CE1 . HIS B 348 ? 1.0334 1.8282 1.6965 -0.0634 -0.2849 -0.2306 534 HIS A CE1 
5254 N NE2 . HIS B 348 ? 1.0509 1.8121 1.6465 -0.0440 -0.2966 -0.1944 534 HIS A NE2 
5255 N N   . ASP B 349 ? 0.8454 1.3708 1.2996 -0.1376 -0.1662 -0.0808 535 ASP A N   
5256 C CA  . ASP B 349 ? 0.8748 1.3576 1.3027 -0.1561 -0.1464 -0.0650 535 ASP A CA  
5257 C C   . ASP B 349 ? 0.8710 1.3466 1.3548 -0.1780 -0.1136 -0.0698 535 ASP A C   
5258 O O   . ASP B 349 ? 0.8336 1.2878 1.3165 -0.1963 -0.0988 -0.0676 535 ASP A O   
5259 C CB  . ASP B 349 ? 0.8954 1.3243 1.2541 -0.1460 -0.1437 -0.0272 535 ASP A CB  
5260 C CG  . ASP B 349 ? 0.8949 1.3182 1.1909 -0.1291 -0.1697 -0.0181 535 ASP A CG  
5261 O OD1 . ASP B 349 ? 0.9153 1.3548 1.2006 -0.1345 -0.1815 -0.0336 535 ASP A OD1 
5262 O OD2 . ASP B 349 ? 0.7898 1.1919 1.0477 -0.1104 -0.1768 0.0048  535 ASP A OD2 
5263 N N   . ILE B 350 ? 0.8369 1.3288 1.3702 -0.1765 -0.1007 -0.0757 536 ILE A N   
5264 C CA  . ILE B 350 ? 0.7766 1.2607 1.3633 -0.1959 -0.0664 -0.0781 536 ILE A CA  
5265 C C   . ILE B 350 ? 0.7269 1.2585 1.3891 -0.2099 -0.0646 -0.1174 536 ILE A C   
5266 O O   . ILE B 350 ? 0.7809 1.3606 1.4812 -0.2004 -0.0823 -0.1453 536 ILE A O   
5267 C CB  . ILE B 350 ? 0.7456 1.2232 1.3505 -0.1887 -0.0487 -0.0663 536 ILE A CB  
5268 C CG1 . ILE B 350 ? 0.7166 1.1581 1.2512 -0.1709 -0.0574 -0.0343 536 ILE A CG1 
5269 C CG2 . ILE B 350 ? 0.7334 1.1893 1.3745 -0.2074 -0.0095 -0.0586 536 ILE A CG2 
5270 C CD1 . ILE B 350 ? 0.7120 1.1461 1.2598 -0.1639 -0.0396 -0.0227 536 ILE A CD1 
5271 N N   . PRO B 351 ? 0.7068 1.2281 1.3962 -0.2317 -0.0446 -0.1227 537 PRO A N   
5272 C CA  . PRO B 351 ? 0.7065 1.2745 1.4756 -0.2460 -0.0412 -0.1630 537 PRO A CA  
5273 C C   . PRO B 351 ? 0.8119 1.4097 1.6604 -0.2477 -0.0230 -0.1821 537 PRO A C   
5274 O O   . PRO B 351 ? 0.7787 1.3492 1.6295 -0.2475 0.0022  -0.1598 537 PRO A O   
5275 C CB  . PRO B 351 ? 0.6670 1.2048 1.4468 -0.2690 -0.0169 -0.1556 537 PRO A CB  
5276 C CG  . PRO B 351 ? 0.8042 1.2884 1.4958 -0.2635 -0.0220 -0.1184 537 PRO A CG  
5277 C CD  . PRO B 351 ? 0.8114 1.2791 1.4602 -0.2430 -0.0271 -0.0940 537 PRO A CD  
5278 N N   . GLN B 352 ? 1.1713 1.2350 1.4869 -0.2351 -0.1981 -0.3009 538 GLN A N   
5279 C CA  . GLN B 352 ? 1.1619 1.2802 1.5268 -0.2286 -0.1898 -0.3305 538 GLN A CA  
5280 C C   . GLN B 352 ? 1.1546 1.2685 1.6084 -0.2357 -0.1305 -0.3151 538 GLN A C   
5281 O O   . GLN B 352 ? 1.1751 1.3121 1.6545 -0.2177 -0.1284 -0.3123 538 GLN A O   
5282 C CB  . GLN B 352 ? 1.3008 1.4746 1.6880 -0.2526 -0.1888 -0.3960 538 GLN A CB  
5283 C CG  . GLN B 352 ? 1.2758 1.4903 1.6084 -0.2312 -0.2468 -0.4225 538 GLN A CG  
5284 C CD  . GLN B 352 ? 1.3095 1.5423 1.6518 -0.1997 -0.2587 -0.4068 538 GLN A CD  
5285 O OE1 . GLN B 352 ? 1.3229 1.5268 1.6063 -0.1687 -0.2948 -0.3652 538 GLN A OE1 
5286 N NE2 . GLN B 352 ? 1.3747 1.6559 1.7912 -0.2078 -0.2281 -0.4409 538 GLN A NE2 
5287 N N   . GLN B 353 ? 1.1136 1.1977 1.6154 -0.2621 -0.0821 -0.3054 539 GLN A N   
5288 C CA  . GLN B 353 ? 1.1320 1.2070 1.7177 -0.2701 -0.0253 -0.2884 539 GLN A CA  
5289 C C   . GLN B 353 ? 1.0801 1.1156 1.6417 -0.2383 -0.0371 -0.2297 539 GLN A C   
5290 O O   . GLN B 353 ? 1.1102 1.1549 1.7232 -0.2314 -0.0104 -0.2203 539 GLN A O   
5291 C CB  . GLN B 353 ? 1.2815 1.3254 1.9138 -0.3030 0.0229  -0.2850 539 GLN A CB  
5292 C CG  . GLN B 353 ? 1.3204 1.4016 1.9917 -0.3389 0.0465  -0.3425 539 GLN A CG  
5293 C CD  . GLN B 353 ? 1.4354 1.4815 2.1501 -0.3700 0.0933  -0.3355 539 GLN A CD  
5294 O OE1 . GLN B 353 ? 1.3736 1.3638 2.0654 -0.3638 0.0938  -0.2890 539 GLN A OE1 
5295 N NE2 . GLN B 353 ? 1.3711 1.4499 2.1500 -0.4036 0.1328  -0.3819 539 GLN A NE2 
5296 N N   . LEU B 354 ? 1.1177 1.1080 1.6003 -0.2191 -0.0768 -0.1899 540 LEU A N   
5297 C CA  . LEU B 354 ? 1.0441 0.9973 1.4932 -0.1866 -0.0953 -0.1344 540 LEU A CA  
5298 C C   . LEU B 354 ? 0.9925 0.9827 1.4114 -0.1571 -0.1337 -0.1428 540 LEU A C   
5299 O O   . LEU B 354 ? 0.9364 0.9217 1.3763 -0.1394 -0.1237 -0.1174 540 LEU A O   
5300 C CB  . LEU B 354 ? 1.0648 0.9621 1.4351 -0.1746 -0.1296 -0.0928 540 LEU A CB  
5301 C CG  . LEU B 354 ? 0.9488 0.7980 1.2818 -0.1433 -0.1470 -0.0302 540 LEU A CG  
5302 C CD1 . LEU B 354 ? 0.9313 0.7521 1.3395 -0.1524 -0.0914 -0.0007 540 LEU A CD1 
5303 C CD2 . LEU B 354 ? 1.0152 0.8153 1.2667 -0.1331 -0.1846 0.0034  540 LEU A CD2 
5304 N N   . VAL B 355 ? 1.0984 1.1256 1.4689 -0.1521 -0.1776 -0.1791 541 VAL A N   
5305 C CA  . VAL B 355 ? 1.1452 1.2067 1.4817 -0.1227 -0.2194 -0.1874 541 VAL A CA  
5306 C C   . VAL B 355 ? 1.0762 1.1815 1.4918 -0.1264 -0.1835 -0.2120 541 VAL A C   
5307 O O   . VAL B 355 ? 1.0483 1.1590 1.4587 -0.1007 -0.1953 -0.1936 541 VAL A O   
5308 C CB  . VAL B 355 ? 1.1044 1.1998 1.3819 -0.1210 -0.2700 -0.2273 541 VAL A CB  
5309 C CG1 . VAL B 355 ? 1.0589 1.1943 1.3101 -0.0920 -0.3109 -0.2404 541 VAL A CG1 
5310 C CG2 . VAL B 355 ? 1.2272 1.2765 1.4190 -0.1140 -0.3093 -0.1992 541 VAL A CG2 
5311 N N   . GLU B 356 ? 1.0252 1.1617 1.5153 -0.1586 -0.1382 -0.2537 542 GLU A N   
5312 C CA  . GLU B 356 ? 1.0589 1.2398 1.6260 -0.1641 -0.1032 -0.2810 542 GLU A CA  
5313 C C   . GLU B 356 ? 0.9961 1.1441 1.6052 -0.1567 -0.0658 -0.2371 542 GLU A C   
5314 O O   . GLU B 356 ? 0.9879 1.1593 1.6216 -0.1421 -0.0610 -0.2386 542 GLU A O   
5315 C CB  . GLU B 356 ? 1.0921 1.3103 1.7284 -0.2015 -0.0622 -0.3338 542 GLU A CB  
5316 C CG  . GLU B 356 ? 1.1434 1.4072 1.7465 -0.2071 -0.0995 -0.3855 542 GLU A CG  
5317 C CD  . GLU B 356 ? 1.3251 1.6179 1.9882 -0.2458 -0.0608 -0.4342 542 GLU A CD  
5318 O OE1 . GLU B 356 ? 1.3741 1.6420 2.0918 -0.2691 -0.0095 -0.4231 542 GLU A OE1 
5319 O OE2 . GLU B 356 ? 1.4319 1.7725 2.0886 -0.2530 -0.0817 -0.4837 542 GLU A OE2 
5320 N N   . ARG B 357 ? 0.9900 1.0831 1.6078 -0.1668 -0.0391 -0.1981 543 ARG A N   
5321 C CA  . ARG B 357 ? 0.9752 1.0347 1.6341 -0.1614 -0.0030 -0.1562 543 ARG A CA  
5322 C C   . ARG B 357 ? 0.9731 1.0095 1.5716 -0.1232 -0.0424 -0.1125 543 ARG A C   
5323 O O   . ARG B 357 ? 0.9849 1.0226 1.6152 -0.1126 -0.0238 -0.0970 543 ARG A O   
5324 C CB  . ARG B 357 ? 0.9714 0.9759 1.6523 -0.1805 0.0317  -0.1239 543 ARG A CB  
5325 C CG  . ARG B 357 ? 0.9575 0.9273 1.6871 -0.1779 0.0719  -0.0829 543 ARG A CG  
5326 C CD  . ARG B 357 ? 1.0994 1.0168 1.8589 -0.1981 0.1085  -0.0536 543 ARG A CD  
5327 N NE  . ARG B 357 ? 1.1211 1.0046 1.9249 -0.1947 0.1441  -0.0138 543 ARG A NE  
5328 C CZ  . ARG B 357 ? 1.0832 0.9165 1.9186 -0.2081 0.1776  0.0197  543 ARG A CZ  
5329 N NH1 . ARG B 357 ? 0.9865 0.7972 1.8172 -0.2264 0.1826  0.0184  543 ARG A NH1 
5330 N NH2 . ARG B 357 ? 1.0484 0.8528 1.9214 -0.2035 0.2067  0.0549  543 ARG A NH2 
5331 N N   . LEU B 358 ? 0.9483 0.9623 1.4589 -0.1027 -0.0963 -0.0919 544 LEU A N   
5332 C CA  . LEU B 358 ? 0.9493 0.9413 1.3986 -0.0659 -0.1362 -0.0508 544 LEU A CA  
5333 C C   . LEU B 358 ? 0.9769 1.0233 1.4277 -0.0487 -0.1567 -0.0808 544 LEU A C   
5334 O O   . LEU B 358 ? 1.0195 1.0579 1.4659 -0.0264 -0.1606 -0.0538 544 LEU A O   
5335 C CB  . LEU B 358 ? 1.0154 0.9741 1.3702 -0.0490 -0.1902 -0.0256 544 LEU A CB  
5336 C CG  . LEU B 358 ? 0.9161 0.8046 1.2555 -0.0500 -0.1776 0.0296  544 LEU A CG  
5337 C CD1 . LEU B 358 ? 0.9172 0.7942 1.3025 -0.0857 -0.1375 0.0140  544 LEU A CD1 
5338 C CD2 . LEU B 358 ? 0.9504 0.8028 1.1915 -0.0233 -0.2346 0.0655  544 LEU A CD2 
5339 N N   . GLN B 359 ? 1.0006 1.1020 1.4571 -0.0589 -0.1706 -0.1367 545 GLN A N   
5340 C CA  . GLN B 359 ? 0.9894 1.1468 1.4559 -0.0451 -0.1873 -0.1708 545 GLN A CA  
5341 C C   . GLN B 359 ? 0.9081 1.0868 1.4628 -0.0563 -0.1331 -0.1817 545 GLN A C   
5342 O O   . GLN B 359 ? 0.8989 1.0990 1.4588 -0.0370 -0.1406 -0.1818 545 GLN A O   
5343 C CB  . GLN B 359 ? 0.9983 1.2080 1.4574 -0.0573 -0.2106 -0.2296 545 GLN A CB  
5344 C CG  . GLN B 359 ? 1.0555 1.2494 1.4223 -0.0446 -0.2697 -0.2233 545 GLN A CG  
5345 C CD  . GLN B 359 ? 1.1636 1.4069 1.5255 -0.0596 -0.2902 -0.2821 545 GLN A CD  
5346 O OE1 . GLN B 359 ? 1.2340 1.5139 1.6645 -0.0867 -0.2525 -0.3250 545 GLN A OE1 
5347 N NE2 . GLN B 359 ? 1.2238 1.4670 1.5036 -0.0425 -0.3504 -0.2839 545 GLN A NE2 
5348 N N   . GLU B 360 ? 0.8976 1.0700 1.5221 -0.0878 -0.0777 -0.1908 546 GLU A N   
5349 C CA  . GLU B 360 ? 0.8860 1.0742 1.5957 -0.1008 -0.0229 -0.1993 546 GLU A CA  
5350 C C   . GLU B 360 ? 0.8857 1.0297 1.5896 -0.0810 -0.0136 -0.1439 546 GLU A C   
5351 O O   . GLU B 360 ? 0.8718 1.0368 1.6115 -0.0740 0.0034  -0.1486 546 GLU A O   
5352 C CB  . GLU B 360 ? 0.8823 1.0657 1.6623 -0.1383 0.0323  -0.2157 546 GLU A CB  
5353 C CG  . GLU B 360 ? 0.8707 1.0631 1.7399 -0.1540 0.0924  -0.2202 546 GLU A CG  
5354 C CD  . GLU B 360 ? 0.9258 1.1859 1.8384 -0.1565 0.0993  -0.2724 546 GLU A CD  
5355 O OE1 . GLU B 360 ? 0.8775 1.1827 1.7791 -0.1621 0.0758  -0.3190 546 GLU A OE1 
5356 O OE2 . GLU B 360 ? 1.0346 1.3022 1.9922 -0.1533 0.1280  -0.2672 546 GLU A OE2 
5357 N N   . GLU B 361 ? 0.9051 0.9869 1.5643 -0.0726 -0.0241 -0.0912 547 GLU A N   
5358 C CA  . GLU B 361 ? 0.8838 0.9191 1.5319 -0.0534 -0.0181 -0.0357 547 GLU A CA  
5359 C C   . GLU B 361 ? 0.8973 0.9491 1.4955 -0.0195 -0.0610 -0.0282 547 GLU A C   
5360 O O   . GLU B 361 ? 0.9117 0.9595 1.5332 -0.0097 -0.0433 -0.0111 547 GLU A O   
5361 C CB  . GLU B 361 ? 0.9361 0.9032 1.5398 -0.0498 -0.0274 0.0172  547 GLU A CB  
5362 C CG  . GLU B 361 ? 0.9820 0.9242 1.6467 -0.0824 0.0242  0.0193  547 GLU A CG  
5363 C CD  . GLU B 361 ? 0.9545 0.8251 1.5855 -0.0777 0.0213  0.0770  547 GLU A CD  
5364 O OE1 . GLU B 361 ? 0.9542 0.7949 1.5098 -0.0493 -0.0232 0.1142  547 GLU A OE1 
5365 O OE2 . GLU B 361 ? 0.9678 0.8120 1.6490 -0.1024 0.0636  0.0848  547 GLU A OE2 
5366 N N   . LYS B 362 ? 0.8827 0.9529 1.4121 -0.0018 -0.1174 -0.0416 548 LYS A N   
5367 C CA  . LYS B 362 ? 0.8848 0.9728 1.3680 0.0305  -0.1593 -0.0369 548 LYS A CA  
5368 C C   . LYS B 362 ? 0.9398 1.0887 1.4806 0.0269  -0.1406 -0.0825 548 LYS A C   
5369 O O   . LYS B 362 ? 0.9533 1.1086 1.4846 0.0487  -0.1512 -0.0705 548 LYS A O   
5370 C CB  . LYS B 362 ? 0.8958 0.9923 1.2951 0.0492  -0.2242 -0.0444 548 LYS A CB  
5371 C CG  . LYS B 362 ? 1.1361 1.1692 1.4641 0.0623  -0.2519 0.0090  548 LYS A CG  
5372 C CD  . LYS B 362 ? 1.0323 1.0712 1.2701 0.0882  -0.3206 0.0092  548 LYS A CD  
5373 C CE  . LYS B 362 ? 1.0575 1.1359 1.2866 0.0727  -0.3402 -0.0420 548 LYS A CE  
5374 N NZ  . LYS B 362 ? 1.0813 1.1626 1.2200 0.0981  -0.4086 -0.0401 548 LYS A NZ  
5375 N N   . ARG B 363 ? 0.8814 1.0751 1.4823 -0.0006 -0.1126 -0.1350 549 ARG A N   
5376 C CA  . ARG B 363 ? 0.8774 1.1278 1.5414 -0.0068 -0.0887 -0.1784 549 ARG A CA  
5377 C C   . ARG B 363 ? 0.9000 1.1297 1.6202 -0.0115 -0.0382 -0.1533 549 ARG A C   
5378 O O   . ARG B 363 ? 0.9655 1.2193 1.7017 0.0015  -0.0359 -0.1603 549 ARG A O   
5379 C CB  . ARG B 363 ? 0.8792 1.1769 1.5986 -0.0376 -0.0652 -0.2371 549 ARG A CB  
5380 C CG  . ARG B 363 ? 0.8907 1.2188 1.5607 -0.0345 -0.1144 -0.2714 549 ARG A CG  
5381 C CD  . ARG B 363 ? 0.8926 1.2740 1.6244 -0.0643 -0.0888 -0.3332 549 ARG A CD  
5382 N NE  . ARG B 363 ? 0.9058 1.3027 1.5909 -0.0683 -0.1289 -0.3603 549 ARG A NE  
5383 C CZ  . ARG B 363 ? 0.9393 1.3133 1.6190 -0.0903 -0.1191 -0.3603 549 ARG A CZ  
5384 N NH1 . ARG B 363 ? 0.9032 1.2395 1.6247 -0.1106 -0.0702 -0.3361 549 ARG A NH1 
5385 N NH2 . ARG B 363 ? 1.0326 1.4210 1.6635 -0.0923 -0.1595 -0.3852 549 ARG A NH2 
5386 N N   . ILE B 364 ? 0.8987 1.0836 1.6505 -0.0309 0.0030  -0.1247 550 ILE A N   
5387 C CA  . ILE B 364 ? 0.8569 1.0171 1.6614 -0.0372 0.0517  -0.0985 550 ILE A CA  
5388 C C   . ILE B 364 ? 0.8578 0.9772 1.6084 -0.0062 0.0274  -0.0453 550 ILE A C   
5389 O O   . ILE B 364 ? 0.8713 0.9894 1.6522 -0.0019 0.0519  -0.0347 550 ILE A O   
5390 C CB  . ILE B 364 ? 0.8529 0.9734 1.7023 -0.0653 0.0985  -0.0806 550 ILE A CB  
5391 C CG1 . ILE B 364 ? 0.8542 1.0183 1.7568 -0.0963 0.1223  -0.1363 550 ILE A CG1 
5392 C CG2 . ILE B 364 ? 0.8475 0.9418 1.7525 -0.0729 0.1489  -0.0543 550 ILE A CG2 
5393 C CD1 . ILE B 364 ? 0.8864 1.0156 1.8325 -0.1251 0.1656  -0.1242 550 ILE A CD1 
5394 N N   . GLU B 365 ? 0.9155 0.9991 1.5851 0.0149  -0.0201 -0.0106 551 GLU A N   
5395 C CA  . GLU B 365 ? 0.9778 1.0232 1.5909 0.0455  -0.0472 0.0396  551 GLU A CA  
5396 C C   . GLU B 365 ? 0.9941 1.0851 1.5890 0.0683  -0.0766 0.0162  551 GLU A C   
5397 O O   . GLU B 365 ? 1.0561 1.1312 1.6436 0.0850  -0.0742 0.0435  551 GLU A O   
5398 C CB  . GLU B 365 ? 1.0144 1.0131 1.5451 0.0620  -0.0920 0.0794  551 GLU A CB  
5399 C CG  . GLU B 365 ? 1.0433 0.9855 1.5861 0.0441  -0.0644 0.1144  551 GLU A CG  
5400 C CD  . GLU B 365 ? 1.1780 1.0769 1.6390 0.0601  -0.1098 0.1506  551 GLU A CD  
5401 O OE1 . GLU B 365 ? 1.0718 0.9898 1.4685 0.0819  -0.1627 0.1416  551 GLU A OE1 
5402 O OE2 . GLU B 365 ? 1.2154 1.0605 1.6768 0.0511  -0.0927 0.1881  551 GLU A OE2 
5403 N N   . ALA B 366 ? 1.0725 1.2203 1.6615 0.0687  -0.1039 -0.0350 552 ALA A N   
5404 C CA  . ALA B 366 ? 1.0756 1.2690 1.6461 0.0910  -0.1362 -0.0602 552 ALA A CA  
5405 C C   . ALA B 366 ? 1.0058 1.2348 1.6488 0.0823  -0.0943 -0.0861 552 ALA A C   
5406 O O   . ALA B 366 ? 1.0067 1.2678 1.6383 0.1018  -0.1162 -0.1009 552 ALA A O   
5407 C CB  . ALA B 366 ? 0.9887 1.2329 1.5373 0.0915  -0.1759 -0.1097 552 ALA A CB  
5408 N N   . GLN B 367 ? 0.8889 1.1138 1.6062 0.0536  -0.0354 -0.0931 553 GLN A N   
5409 C CA  . GLN B 367 ? 0.8590 1.1179 1.6479 0.0429  0.0073  -0.1197 553 GLN A CA  
5410 C C   . GLN B 367 ? 0.8753 1.0844 1.6763 0.0459  0.0399  -0.0705 553 GLN A C   
5411 O O   . GLN B 367 ? 0.8559 1.0504 1.7192 0.0217  0.0937  -0.0670 553 GLN A O   
5412 C CB  . GLN B 367 ? 0.8704 1.1641 1.7385 0.0078  0.0525  -0.1661 553 GLN A CB  
5413 C CG  . GLN B 367 ? 0.8580 1.1976 1.7147 0.0019  0.0224  -0.2144 553 GLN A CG  
5414 C CD  . GLN B 367 ? 0.8549 1.2125 1.7790 -0.0342 0.0659  -0.2486 553 GLN A CD  
5415 O OE1 . GLN B 367 ? 1.0109 1.3669 2.0049 -0.0549 0.1209  -0.2520 553 GLN A OE1 
5416 N NE2 . GLN B 367 ? 0.8590 1.2327 1.7615 -0.0423 0.0415  -0.2739 553 GLN A NE2 
5420 N N   . PHE C 2   ? 0.9245 1.0308 0.9758 -0.1088 0.0114  0.0460  1   PHE D N   
5421 C CA  . PHE C 2   ? 0.8447 1.0428 0.9400 -0.0889 -0.0094 0.0486  1   PHE D CA  
5422 C C   . PHE C 2   ? 0.8448 1.0509 0.9691 -0.0530 0.0064  0.0742  1   PHE D C   
5423 O O   . PHE C 2   ? 0.8390 1.0296 0.9710 -0.0518 0.0242  0.0968  1   PHE D O   
5424 C CB  . PHE C 2   ? 0.8147 1.0870 0.9341 -0.1109 -0.0288 0.0491  1   PHE D CB  
5425 C CG  . PHE C 2   ? 0.7330 1.1020 0.8973 -0.0927 -0.0516 0.0507  1   PHE D CG  
5426 C CD1 . PHE C 2   ? 0.7422 1.1585 0.9103 -0.0960 -0.0790 0.0267  1   PHE D CD1 
5427 C CD2 . PHE C 2   ? 0.6963 1.1085 0.8988 -0.0721 -0.0459 0.0760  1   PHE D CD2 
5428 C CE1 . PHE C 2   ? 0.6510 1.1559 0.8602 -0.0792 -0.1003 0.0280  1   PHE D CE1 
5429 C CE2 . PHE C 2   ? 0.6471 1.1483 0.8910 -0.0552 -0.0669 0.0774  1   PHE D CE2 
5430 C CZ  . PHE C 2   ? 0.6123 1.1601 0.8597 -0.0588 -0.0941 0.0534  1   PHE D CZ  
5431 C C1  . MEA C 3   ? 0.7527 0.9932 0.9212 0.0120  0.0131  0.0929  2   MEA D C1  
5432 N N   . MEA C 3   ? 0.8037 1.0344 0.9442 -0.0238 -0.0003 0.0709  2   MEA D N   
5433 C CA  . MEA C 3   ? 0.7690 1.0179 0.9003 -0.0240 -0.0215 0.0446  2   MEA D CA  
5434 C C   . MEA C 3   ? 0.8241 1.0005 0.9280 -0.0057 -0.0050 0.0389  2   MEA D C   
5435 O O   . MEA C 3   ? 0.8476 1.0364 0.9695 0.0248  -0.0016 0.0458  2   MEA D O   
5436 C CB  . MEA C 3   ? 0.6841 1.0301 0.8592 -0.0056 -0.0458 0.0446  2   MEA D CB  
5437 C CG  . MEA C 3   ? 0.7056 1.0776 0.8745 -0.0039 -0.0700 0.0179  2   MEA D CG  
5438 C CD1 . MEA C 3   ? 0.7063 1.1134 0.8682 -0.0318 -0.0946 -0.0033 2   MEA D CD1 
5439 C CE1 . MEA C 3   ? 0.6092 1.0399 0.7650 -0.0303 -0.1172 -0.0277 2   MEA D CE1 
5440 C CZ  . MEA C 3   ? 0.7935 1.2124 0.9497 -0.0012 -0.1149 -0.0304 2   MEA D CZ  
5441 C CE2 . MEA C 3   ? 0.6797 1.0645 0.8434 0.0265  -0.0900 -0.0092 2   MEA D CE2 
5442 C CD2 . MEA C 3   ? 0.6227 0.9845 0.7931 0.0254  -0.0677 0.0149  2   MEA D CD2 
5443 N N   . ASN C 4   ? 0.9116 1.0119 0.9708 -0.0262 0.0051  0.0255  3   ASN D N   
5444 C CA  . ASN C 4   ? 0.8798 0.9038 0.9090 -0.0120 0.0227  0.0198  3   ASN D CA  
5445 C C   . ASN C 4   ? 0.9678 0.9612 0.9599 -0.0307 0.0101  -0.0101 3   ASN D C   
5446 O O   . ASN C 4   ? 1.0211 0.9405 0.9734 -0.0499 0.0234  -0.0177 3   ASN D O   
5447 C CB  . ASN C 4   ? 0.9461 0.8895 0.9537 -0.0146 0.0546  0.0368  3   ASN D CB  
5448 C CG  . ASN C 4   ? 0.9342 0.9080 0.9729 -0.0096 0.0639  0.0642  3   ASN D CG  
5449 O OD1 . ASN C 4   ? 0.9399 0.9642 1.0163 0.0171  0.0623  0.0795  3   ASN D OD1 
5450 N ND2 . ASN C 4   ? 0.9815 0.9255 1.0044 -0.0357 0.0732  0.0704  3   ASN D ND2 
5451 C C1  . MEA C 5   ? 0.8460 0.9821 0.8961 -0.0012 -0.0322 -0.0198 4   MEA D C1  
5452 N N   . MEA C 5   ? 0.9746 1.0235 0.9790 -0.0245 -0.0154 -0.0270 4   MEA D N   
5453 C CA  . MEA C 5   ? 1.0623 1.0927 1.0340 -0.0443 -0.0317 -0.0565 4   MEA D CA  
5454 C C   . MEA C 5   ? 1.1521 1.1556 1.1084 -0.0236 -0.0326 -0.0706 4   MEA D C   
5455 O O   . MEA C 5   ? 1.1393 1.1660 1.1191 0.0064  -0.0298 -0.0608 4   MEA D O   
5456 C CB  . MEA C 5   ? 1.0184 1.1340 1.0117 -0.0612 -0.0640 -0.0690 4   MEA D CB  
5457 C CG  . MEA C 5   ? 0.9068 1.0424 0.9100 -0.0855 -0.0627 -0.0576 4   MEA D CG  
5458 C CD1 . MEA C 5   ? 0.8280 1.0505 0.8745 -0.0822 -0.0778 -0.0467 4   MEA D CD1 
5459 C CE1 . MEA C 5   ? 0.8017 1.0421 0.8570 -0.1042 -0.0761 -0.0361 4   MEA D CE1 
5460 C CZ  . MEA C 5   ? 0.9262 1.0973 0.9469 -0.1297 -0.0593 -0.0363 4   MEA D CZ  
5461 C CE2 . MEA C 5   ? 1.0065 1.0906 0.9843 -0.1326 -0.0441 -0.0470 4   MEA D CE2 
5462 C CD2 . MEA C 5   ? 0.9687 1.0349 0.9379 -0.1104 -0.0456 -0.0575 4   MEA D CD2 
5463 N N   . PRO C 6   ? 1.2235 1.1762 1.1383 -0.0412 -0.0366 -0.0943 5   PRO D N   
5464 C CA  . PRO C 6   ? 1.3032 1.2220 1.1857 -0.0779 -0.0399 -0.1084 5   PRO D CA  
5465 C C   . PRO C 6   ? 1.4025 1.2341 1.2555 -0.0885 -0.0092 -0.0971 5   PRO D C   
5466 O O   . PRO C 6   ? 1.3826 1.1566 1.2238 -0.0690 0.0142  -0.0878 5   PRO D O   
5467 C CB  . PRO C 6   ? 1.2966 1.1960 1.1486 -0.0847 -0.0560 -0.1379 5   PRO D CB  
5468 C CG  . PRO C 6   ? 1.3832 1.2540 1.2330 -0.0529 -0.0437 -0.1348 5   PRO D CG  
5469 C CD  . PRO C 6   ? 1.3428 1.2697 1.2397 -0.0244 -0.0393 -0.1101 5   PRO D CD  
5470 N N   . ASN C 7   ? 1.3568 1.1799 1.1983 -0.1193 -0.0097 -0.0980 6   ASN D N   
5471 C CA  . ASN C 7   ? 1.3310 1.0722 1.1423 -0.1333 0.0172  -0.0890 6   ASN D CA  
5472 C C   . ASN C 7   ? 1.3895 1.1109 1.1717 -0.1723 0.0083  -0.1060 6   ASN D C   
5473 O O   . ASN C 7   ? 1.4246 1.2056 1.2173 -0.1885 -0.0182 -0.1206 6   ASN D O   
5474 C CB  . ASN C 7   ? 1.2639 1.0152 1.1023 -0.1232 0.0356  -0.0585 6   ASN D CB  
5475 C CG  . ASN C 7   ? 1.2202 1.0534 1.0930 -0.1362 0.0179  -0.0513 6   ASN D CG  
5476 O OD1 . ASN C 7   ? 1.2519 1.1121 1.1180 -0.1637 -0.0015 -0.0675 6   ASN D OD1 
5477 N ND2 . ASN C 7   ? 1.1830 1.0559 1.0931 -0.1162 0.0249  -0.0267 6   ASN D ND2 
5478 C C   . DI8 C 8   ? 1.3648 0.9903 1.0909 -0.2468 0.0299  -0.1046 7   DI8 D C   
5479 N N   . DI8 C 8   ? 1.4562 1.0952 1.1992 -0.1920 0.0275  -0.1077 7   DI8 D N   
5480 O O   . DI8 C 8   ? 1.4178 0.9841 1.1042 -0.2782 0.0353  -0.1170 7   DI8 D O   
5481 C C1  . DI8 C 8   ? 1.5428 1.0863 1.2100 -0.2445 0.0246  -0.1439 7   DI8 D C1  
5482 C C2  . DI8 C 8   ? 1.5663 1.0220 1.2118 -0.2306 0.0591  -0.1282 7   DI8 D C2  
5483 C C3  . DI8 C 8   ? 1.6186 0.9878 1.2188 -0.2518 0.0751  -0.1357 7   DI8 D C3  
5484 C C4  . DI8 C 8   ? 1.6308 0.9222 1.2122 -0.2388 0.1058  -0.1217 7   DI8 D C4  
5485 C C5  . DI8 C 8   ? 1.5833 0.8830 1.1908 -0.2052 0.1204  -0.1007 7   DI8 D C5  
5486 C C6  . DI8 C 8   ? 1.5545 0.9388 1.2063 -0.1849 0.1046  -0.0935 7   DI8 D C6  
5487 C C7  . DI8 C 8   ? 1.5311 0.9950 1.2018 -0.1984 0.0732  -0.1075 7   DI8 D C7  
5488 C C8  . DI8 C 8   ? 1.4566 1.0120 1.1755 -0.1756 0.0563  -0.0993 7   DI8 D C8  
5489 C CA  . DI8 C 8   ? 1.4362 1.0660 1.1553 -0.2297 0.0165  -0.1242 7   DI8 D CA  
5490 N N   . TYR C 9   ? 1.4032 1.0661 1.1655 -0.2309 0.0387  -0.0782 8   TYR D N   
5491 C CA  . TYR C 9   ? 1.3780 1.0427 1.1507 -0.2439 0.0510  -0.0576 8   TYR D CA  
5492 C C   . TYR C 9   ? 1.3170 1.0689 1.1187 -0.2613 0.0261  -0.0608 8   TYR D C   
5493 O O   . TYR C 9   ? 1.2351 1.0638 1.0718 -0.2453 0.0071  -0.0613 8   TYR D O   
5494 C CB  . TYR C 9   ? 1.3265 0.9875 1.1238 -0.2141 0.0722  -0.0284 8   TYR D CB  
5495 C CG  . TYR C 9   ? 1.3529 0.9563 1.1366 -0.1858 0.0908  -0.0255 8   TYR D CG  
5496 C CD1 . TYR C 9   ? 1.4686 0.9784 1.2083 -0.1937 0.1101  -0.0322 8   TYR D CD1 
5497 C CD2 . TYR C 9   ? 1.2600 0.9028 1.0754 -0.1509 0.0894  -0.0156 8   TYR D CD2 
5498 C CE1 . TYR C 9   ? 1.5025 0.9600 1.2301 -0.1679 0.1275  -0.0297 8   TYR D CE1 
5499 C CE2 . TYR C 9   ? 1.3537 0.9448 1.1575 -0.1251 0.1067  -0.0131 8   TYR D CE2 
5500 C CZ  . TYR C 9   ? 1.3799 0.8785 1.1398 -0.1338 0.1258  -0.0203 8   TYR D CZ  
5501 O OH  . TYR C 9   ? 1.3478 0.7951 1.0960 -0.1084 0.1433  -0.0182 8   TYR D OH  
5502 N N   . ARG C 10  ? 1.2947 1.0352 1.0819 -0.2941 0.0263  -0.0631 9   ARG D N   
5503 C CA  . ARG C 10  ? 1.2585 1.0775 1.0708 -0.3140 0.0041  -0.0665 9   ARG D CA  
5504 C C   . ARG C 10  ? 1.2570 1.0979 1.0939 -0.3153 0.0162  -0.0395 9   ARG D C   
5505 O O   . ARG C 10  ? 1.2920 1.1782 1.1408 -0.3390 0.0041  -0.0406 9   ARG D O   
5506 C CB  . ARG C 10  ? 1.3241 1.1260 1.1059 -0.3517 -0.0080 -0.0905 9   ARG D CB  
5507 C CG  . ARG C 10  ? 1.4373 1.3274 1.2417 -0.3643 -0.0416 -0.1087 9   ARG D CG  
5508 C CD  . ARG C 10  ? 1.4803 1.3851 1.2778 -0.4028 -0.0497 -0.1158 9   ARG D CD  
5509 N NE  . ARG C 10  ? 1.4128 1.3683 1.2432 -0.4058 -0.0472 -0.0940 9   ARG D NE  
5510 C CZ  . ARG C 10  ? 1.3612 1.4078 1.2277 -0.4099 -0.0700 -0.0959 9   ARG D CZ  
5511 N NH1 . ARG C 10  ? 1.3573 1.4581 1.2333 -0.4108 -0.0979 -0.1184 9   ARG D NH1 
5512 N NH2 . ARG C 10  ? 1.3007 1.3846 1.1937 -0.4131 -0.0647 -0.0749 9   ARG D NH2 
5513 N N   . ARG C 11  ? 1.2955 1.1055 1.1402 -0.2904 0.0396  -0.0156 10  ARG D N   
5514 C CA  . ARG C 11  ? 1.2562 1.0925 1.1283 -0.2861 0.0501  0.0115  10  ARG D CA  
5515 C C   . ARG C 11  ? 1.1773 1.1006 1.0983 -0.2595 0.0362  0.0222  10  ARG D C   
5516 O O   . ARG C 11  ? 1.1590 1.1176 1.1080 -0.2546 0.0411  0.0441  10  ARG D O   
5517 C CB  . ARG C 11  ? 1.3096 1.0647 1.1640 -0.2733 0.0831  0.0324  10  ARG D CB  
5518 C CG  . ARG C 11  ? 1.3162 1.0820 1.1899 -0.2740 0.0968  0.0599  10  ARG D CG  
5519 C CD  . ARG C 11  ? 1.3931 1.0912 1.2581 -0.2514 0.1270  0.0816  10  ARG D CD  
5520 N NE  . ARG C 11  ? 1.4400 1.1632 1.3320 -0.2447 0.1368  0.1092  10  ARG D NE  
5521 C CZ  . ARG C 11  ? 1.4029 1.0719 1.2892 -0.2306 0.1630  0.1312  10  ARG D CZ  
5522 N NH1 . ARG C 11  ? 1.4278 1.0136 1.2829 -0.2216 0.1830  0.1295  10  ARG D NH1 
5523 N NH2 . ARG C 11  ? 1.4030 1.1017 1.3153 -0.2255 0.1691  0.1552  10  ARG D NH2 
5524 N N   . CYS C 12  ? 1.1405 1.1003 1.0720 -0.2433 0.0182  0.0068  11  CYS D N   
5525 C CA  . CYS C 12  ? 1.0800 1.1223 1.0572 -0.2172 0.0040  0.0154  11  CYS D CA  
5526 C C   . CYS C 12  ? 1.0208 1.1496 1.0237 -0.2370 -0.0224 0.0081  11  CYS D C   
5527 O O   . CYS C 12  ? 1.0933 1.2349 1.0814 -0.2604 -0.0413 -0.0160 11  CYS D O   
5528 C CB  . CYS C 12  ? 1.0805 1.1263 1.0571 -0.1930 -0.0053 0.0010  11  CYS D CB  
5529 S SG  . CYS C 12  ? 1.1783 1.1269 1.1272 -0.1669 0.0251  0.0086  11  CYS D SG  
5530 N N   . GLY C 13  ? 0.9696 1.1589 1.0115 -0.2270 -0.0242 0.0285  12  GLY D N   
5531 C CA  . GLY C 13  ? 0.9270 1.2006 0.9956 -0.2448 -0.0482 0.0231  12  GLY D CA  
5532 C C   . GLY C 13  ? 0.9747 1.2292 1.0234 -0.2834 -0.0456 0.0199  12  GLY D C   
5533 O O   . GLY C 13  ? 1.1015 1.3686 1.1357 -0.3093 -0.0634 -0.0035 12  GLY D O   
5534 N N   . LYS C 14  ? 1.0109 1.2329 1.0575 -0.2877 -0.0236 0.0428  13  LYS D N   
5535 C CA  . LYS C 14  ? 1.1034 1.3040 1.1307 -0.3242 -0.0189 0.0420  13  LYS D CA  
5536 C C   . LYS C 14  ? 1.0747 1.2695 1.1157 -0.3221 0.0005  0.0718  13  LYS D C   
5537 O O   . LYS C 14  ? 1.0359 1.3001 1.1094 -0.3257 -0.0097 0.0819  13  LYS D O   
5538 C CB  . LYS C 14  ? 1.1767 1.2847 1.1533 -0.3428 -0.0058 0.0277  13  LYS D CB  
5539 C CG  . LYS C 14  ? 1.2001 1.2211 1.1550 -0.3275 0.0260  0.0463  13  LYS D CG  
5540 C CD  . LYS C 14  ? 1.2754 1.2047 1.1794 -0.3476 0.0388  0.0319  13  LYS D CD  
5541 C CE  . LYS C 14  ? 1.3250 1.2702 1.2117 -0.3736 0.0158  0.0006  13  LYS D CE  
5542 N NZ  . LYS C 14  ? 1.3305 1.1867 1.1675 -0.3927 0.0277  -0.0139 13  LYS D NZ  
5546 N N   . PHE D 2   ? 0.9447 0.9242 0.8427 0.1928  0.0851  0.2857  1   PHE C N   
5547 C CA  . PHE D 2   ? 0.8799 0.9042 0.8130 0.1976  0.0651  0.2843  1   PHE C CA  
5548 C C   . PHE D 2   ? 0.8325 0.9350 0.7725 0.1820  0.1026  0.2693  1   PHE C C   
5549 O O   . PHE D 2   ? 0.8014 0.9446 0.7697 0.1561  0.1431  0.2634  1   PHE C O   
5550 C CB  . PHE D 2   ? 0.8350 0.8647 0.8428 0.1884  0.0463  0.2947  1   PHE C CB  
5551 C CG  . PHE D 2   ? 0.7895 0.8647 0.8374 0.1917  0.0251  0.2942  1   PHE C CG  
5552 C CD1 . PHE D 2   ? 0.8056 0.8488 0.8454 0.2172  -0.0247 0.3024  1   PHE C CD1 
5553 C CD2 . PHE D 2   ? 0.7310 0.8809 0.8245 0.1689  0.0549  0.2856  1   PHE C CD2 
5554 C CE1 . PHE D 2   ? 0.7642 0.8490 0.8408 0.2200  -0.0447 0.3021  1   PHE C CE1 
5555 C CE2 . PHE D 2   ? 0.6898 0.8814 0.8198 0.1713  0.0352  0.2854  1   PHE C CE2 
5556 C CZ  . PHE D 2   ? 0.7064 0.8653 0.8280 0.1970  -0.0148 0.2936  1   PHE C CZ  
5557 C C1  . MEA D 3   ? 0.7917 0.9891 0.7143 0.1862  0.1168  0.2500  2   MEA C C1  
5558 N N   . MEA D 3   ? 0.8308 0.9552 0.7468 0.1974  0.0887  0.2633  2   MEA C N   
5559 C CA  . MEA D 3   ? 0.8666 0.9448 0.7495 0.2280  0.0408  0.2697  2   MEA C CA  
5560 C C   . MEA D 3   ? 0.9128 0.9757 0.7185 0.2431  0.0499  0.2606  2   MEA C C   
5561 O O   . MEA D 3   ? 0.9006 1.0015 0.6914 0.2489  0.0532  0.2514  2   MEA C O   
5562 C CB  . MEA D 3   ? 0.8245 0.9410 0.7481 0.2343  0.0131  0.2708  2   MEA C CB  
5563 C CG  . MEA D 3   ? 0.8577 0.9309 0.7502 0.2660  -0.0378 0.2771  2   MEA C CG  
5564 C CD1 . MEA D 3   ? 0.8741 0.8933 0.7839 0.2787  -0.0800 0.2920  2   MEA C CD1 
5565 C CE1 . MEA D 3   ? 0.9046 0.8841 0.7860 0.3072  -0.1263 0.2978  2   MEA C CE1 
5566 C CZ  . MEA D 3   ? 0.9476 0.9414 0.7838 0.3232  -0.1303 0.2883  2   MEA C CZ  
5567 C CE2 . MEA D 3   ? 0.9021 0.9502 0.7220 0.3108  -0.0882 0.2733  2   MEA C CE2 
5568 C CD2 . MEA D 3   ? 0.8714 0.9593 0.7194 0.2821  -0.0422 0.2679  2   MEA C CD2 
5569 N N   . ASN D 4   ? 0.9664 0.9722 0.7243 0.2489  0.0537  0.2635  3   ASN C N   
5570 C CA  . ASN D 4   ? 1.0141 1.0013 0.6965 0.2621  0.0641  0.2551  3   ASN C CA  
5571 C C   . ASN D 4   ? 1.0766 0.9842 0.7093 0.2894  0.0232  0.2643  3   ASN C C   
5572 O O   . ASN D 4   ? 1.1511 1.0117 0.7390 0.2911  0.0325  0.2660  3   ASN C O   
5573 C CB  . ASN D 4   ? 1.0249 1.0210 0.6849 0.2419  0.1139  0.2475  3   ASN C CB  
5574 C CG  . ASN D 4   ? 0.9654 1.0260 0.6848 0.2112  0.1524  0.2426  3   ASN C CG  
5575 O OD1 . ASN D 4   ? 0.9757 1.0253 0.7197 0.1936  0.1705  0.2470  3   ASN C OD1 
5576 N ND2 . ASN D 4   ? 0.9202 1.0482 0.6623 0.2044  0.1654  0.2331  3   ASN C ND2 
5577 C C1  . MEA D 5   ? 1.0303 0.9717 0.7102 0.3135  -0.0384 0.2683  4   MEA C C1  
5578 N N   . MEA D 5   ? 1.0781 0.9697 0.7167 0.3106  -0.0219 0.2704  4   MEA C N   
5579 C CA  . MEA D 5   ? 1.1355 0.9491 0.7332 0.3355  -0.0636 0.2810  4   MEA C CA  
5580 C C   . MEA D 5   ? 1.2204 1.0162 0.7507 0.3604  -0.0789 0.2741  4   MEA C C   
5581 O O   . MEA D 5   ? 1.1853 1.0292 0.7127 0.3630  -0.0711 0.2637  4   MEA C O   
5582 C CB  . MEA D 5   ? 1.1726 0.9671 0.8220 0.3431  -0.1079 0.2950  4   MEA C CB  
5583 C CG  . MEA D 5   ? 1.1100 0.9131 0.8218 0.3196  -0.0936 0.3023  4   MEA C CG  
5584 C CD1 . MEA D 5   ? 1.0386 0.8820 0.8218 0.3097  -0.1032 0.3062  4   MEA C CD1 
5585 C CE1 . MEA D 5   ? 1.0551 0.9061 0.8947 0.2883  -0.0894 0.3123  4   MEA C CE1 
5586 C CZ  . MEA D 5   ? 1.0634 0.8812 0.8886 0.2772  -0.0667 0.3147  4   MEA C CZ  
5587 C CE2 . MEA D 5   ? 1.1343 0.9117 0.8879 0.2870  -0.0576 0.3112  4   MEA C CE2 
5588 C CD2 . MEA D 5   ? 1.1287 0.8985 0.8252 0.3081  -0.0711 0.3050  4   MEA C CD2 
5589 N N   . PRO D 6   ? 1.2466 0.9701 0.7216 0.3785  -0.1011 0.2804  5   PRO C N   
5590 C CA  . PRO D 6   ? 1.2779 0.9384 0.7509 0.3764  -0.1118 0.2933  5   PRO C CA  
5591 C C   . PRO D 6   ? 1.3185 0.9746 0.7657 0.3582  -0.0674 0.2883  5   PRO C C   
5592 O O   . PRO D 6   ? 1.2998 0.9847 0.7088 0.3541  -0.0345 0.2750  5   PRO C O   
5593 C CB  . PRO D 6   ? 1.3587 0.9615 0.7939 0.3935  -0.1512 0.2922  5   PRO C CB  
5594 C CG  . PRO D 6   ? 1.3423 0.9645 0.7214 0.4076  -0.1409 0.2793  5   PRO C CG  
5595 C CD  . PRO D 6   ? 1.3453 1.0426 0.7550 0.4042  -0.1211 0.2753  5   PRO C CD  
5596 N N   . ASN D 7   ? 1.3614 0.9823 0.8305 0.3473  -0.0668 0.2989  6   ASN C N   
5597 C CA  . ASN D 7   ? 1.3693 0.9783 0.8141 0.3306  -0.0283 0.2959  6   ASN C CA  
5598 C C   . ASN D 7   ? 1.4322 0.9729 0.8811 0.3309  -0.0475 0.3111  6   ASN C C   
5599 O O   . ASN D 7   ? 1.4630 0.9653 0.9314 0.3447  -0.0909 0.3237  6   ASN C O   
5600 C CB  . ASN D 7   ? 1.3168 0.9980 0.8079 0.3013  0.0200  0.2866  6   ASN C CB  
5601 C CG  . ASN D 7   ? 1.2705 0.9777 0.8448 0.2871  0.0129  0.2943  6   ASN C CG  
5602 O OD1 . ASN D 7   ? 1.3782 1.0401 0.9771 0.2921  -0.0174 0.3081  6   ASN C OD1 
5603 N ND2 . ASN D 7   ? 1.2124 0.9938 0.8306 0.2689  0.0416  0.2851  6   ASN C ND2 
5604 C C   . DI8 D 8   ? 1.4226 0.8910 0.8998 0.2940  -0.0115 0.3279  7   DI8 C C   
5605 N N   . DI8 D 8   ? 1.4668 0.9721 0.8801 0.3224  -0.0252 0.3119  7   DI8 C N   
5606 O O   . DI8 D 8   ? 1.5016 0.9078 0.9562 0.2922  -0.0139 0.3371  7   DI8 C O   
5607 C C1  . DI8 D 8   ? 1.4997 0.8697 0.8474 0.3352  -0.0547 0.3309  7   DI8 C C1  
5608 C C2  . DI8 D 8   ? 1.5286 0.9223 0.8289 0.3223  -0.0054 0.3170  7   DI8 C C2  
5609 C C3  . DI8 D 8   ? 1.5789 0.9219 0.8337 0.3181  0.0071  0.3203  7   DI8 C C3  
5610 C C4  . DI8 D 8   ? 1.5991 0.9644 0.8117 0.3061  0.0513  0.3078  7   DI8 C C4  
5611 C C5  . DI8 D 8   ? 1.5577 0.9949 0.7741 0.2986  0.0829  0.2923  7   DI8 C C5  
5612 C C6  . DI8 D 8   ? 1.5345 1.0207 0.7960 0.3027  0.0703  0.2893  7   DI8 C C6  
5613 C C7  . DI8 D 8   ? 1.5468 1.0098 0.8509 0.3148  0.0247  0.3021  7   DI8 C C7  
5614 C C8  . DI8 D 8   ? 1.4935 1.0104 0.8462 0.3187  0.0110  0.2989  7   DI8 C C8  
5615 C CA  . DI8 D 8   ? 1.4843 0.9256 0.9079 0.3228  -0.0466 0.3273  7   DI8 C CA  
5616 N N   . TYR D 9   ? 1.3570 0.8997 0.8828 0.2727  0.0238  0.3184  8   TYR C N   
5617 C CA  . TYR D 9   ? 1.3392 0.9120 0.9256 0.2460  0.0528  0.3193  8   TYR C CA  
5618 C C   . TYR D 9   ? 1.3080 0.8772 0.9644 0.2467  0.0206  0.3312  8   TYR C C   
5619 O O   . TYR D 9   ? 1.2714 0.8694 0.9544 0.2555  -0.0014 0.3309  8   TYR C O   
5620 C CB  . TYR D 9   ? 1.3552 1.0092 0.9591 0.2257  0.0997  0.3036  8   TYR C CB  
5621 C CG  . TYR D 9   ? 1.3683 1.0349 0.9032 0.2317  0.1218  0.2907  8   TYR C CG  
5622 C CD1 . TYR D 9   ? 1.3817 1.0066 0.8566 0.2318  0.1379  0.2896  8   TYR C CD1 
5623 C CD2 . TYR D 9   ? 1.3916 1.1116 0.9216 0.2370  0.1263  0.2797  8   TYR C CD2 
5624 C CE1 . TYR D 9   ? 1.4158 1.0518 0.8273 0.2371  0.1584  0.2777  8   TYR C CE1 
5625 C CE2 . TYR D 9   ? 1.4105 1.1422 0.8782 0.2427  0.1467  0.2677  8   TYR C CE2 
5626 C CZ  . TYR D 9   ? 1.4208 1.1104 0.8295 0.2427  0.1629  0.2667  8   TYR C CZ  
5627 O OH  . TYR D 9   ? 1.3548 1.0556 0.7017 0.2481  0.1834  0.2547  8   TYR C OH  
5628 N N   . ARG D 10  ? 1.3174 0.8517 1.0042 0.2372  0.0178  0.3418  9   ARG C N   
5629 C CA  . ARG D 10  ? 1.3556 0.8796 1.1073 0.2381  -0.0135 0.3541  9   ARG C CA  
5630 C C   . ARG D 10  ? 1.2941 0.8721 1.1202 0.2108  0.0167  0.3513  9   ARG C C   
5631 O O   . ARG D 10  ? 1.2630 0.8282 1.1450 0.2073  -0.0026 0.3618  9   ARG C O   
5632 C CB  . ARG D 10  ? 1.4057 0.8475 1.1429 0.2492  -0.0449 0.3696  9   ARG C CB  
5633 C CG  . ARG D 10  ? 1.4965 0.8801 1.1512 0.2715  -0.0648 0.3713  9   ARG C CG  
5634 C CD  . ARG D 10  ? 1.7478 1.0585 1.3971 0.2777  -0.0964 0.3844  9   ARG C CD  
5635 N NE  . ARG D 10  ? 1.9560 1.2456 1.5600 0.2877  -0.1215 0.3765  9   ARG C NE  
5636 C CZ  . ARG D 10  ? 1.9048 1.1688 1.5205 0.2834  -0.1436 0.3772  9   ARG C CZ  
5637 N NH1 . ARG D 10  ? 1.8105 1.0669 1.4812 0.2699  -0.1460 0.3851  9   ARG C NH1 
5638 N NH2 . ARG D 10  ? 1.9968 1.2456 1.5688 0.2939  -0.1601 0.3702  9   ARG C NH2 
5639 N N   . ARG D 11  ? 1.2904 0.9285 1.1190 0.1913  0.0635  0.3374  10  ARG C N   
5640 C CA  . ARG D 11  ? 1.1541 0.8516 1.0528 0.1656  0.0923  0.3332  10  ARG C CA  
5641 C C   . ARG D 11  ? 1.0954 0.8581 1.0279 0.1649  0.0895  0.3263  10  ARG C C   
5642 O O   . ARG D 11  ? 1.0650 0.8829 1.0555 0.1435  0.1131  0.3219  10  ARG C O   
5643 C CB  . ARG D 11  ? 1.0749 0.8002 0.9620 0.1419  0.1468  0.3226  10  ARG C CB  
5644 C CG  . ARG D 11  ? 1.2561 1.0174 1.0901 0.1420  0.1751  0.3081  10  ARG C CG  
5645 C CD  . ARG D 11  ? 1.2230 1.0189 1.0581 0.1154  0.2299  0.2981  10  ARG C CD  
5646 N NE  . ARG D 11  ? 1.1451 0.9975 1.0542 0.0914  0.2522  0.2952  10  ARG C NE  
5647 C CZ  . ARG D 11  ? 1.1089 0.9934 1.0367 0.0655  0.2975  0.2882  10  ARG C CZ  
5648 N NH1 . ARG D 11  ? 1.2554 1.1221 1.1349 0.0595  0.3262  0.2835  10  ARG C NH1 
5649 N NH2 . ARG D 11  ? 0.9547 0.8903 0.9509 0.0449  0.3144  0.2858  10  ARG C NH2 
5650 N N   . CYS D 12  ? 1.0427 0.7999 0.9408 0.1874  0.0608  0.3255  11  CYS C N   
5651 C CA  . CYS D 12  ? 1.0465 0.8646 0.9712 0.1879  0.0573  0.3187  11  CYS C CA  
5652 C C   . CYS D 12  ? 0.9655 0.7875 0.9570 0.1895  0.0240  0.3290  11  CYS C C   
5653 O O   . CYS D 12  ? 1.0712 0.8362 1.0629 0.2063  -0.0170 0.3421  11  CYS C O   
5654 C CB  . CYS D 12  ? 1.1206 0.9283 0.9842 0.2125  0.0368  0.3143  11  CYS C CB  
5655 S SG  . CYS D 12  ? 1.1836 0.9941 0.9664 0.2124  0.0750  0.3006  11  CYS C SG  
5656 N N   . GLY D 13  ? 0.9278 0.8175 0.9760 0.1715  0.0419  0.3232  12  GLY C N   
5657 C CA  . GLY D 13  ? 0.8866 0.7897 1.0008 0.1705  0.0143  0.3314  12  GLY C CA  
5658 C C   . GLY D 13  ? 0.9479 0.8272 1.1143 0.1577  0.0127  0.3414  12  GLY C C   
5659 O O   . GLY D 13  ? 1.0296 0.9363 1.2605 0.1489  0.0028  0.3455  12  GLY C O   
5660 N N   . LYS D 14  ? 0.9721 0.8012 1.1136 0.1562  0.0217  0.3457  13  LYS C N   
5661 C CA  . LYS D 14  ? 1.0153 0.8174 1.2049 0.1450  0.0193  0.3556  13  LYS C CA  
5662 C C   . LYS D 14  ? 1.1696 1.0358 1.4286 0.1163  0.0524  0.3496  13  LYS C C   
5663 O O   . LYS D 14  ? 1.1446 1.0506 1.3998 0.0961  0.0985  0.3382  13  LYS C O   
5664 C CB  . LYS D 14  ? 0.9922 0.7422 1.1405 0.1432  0.0355  0.3577  13  LYS C CB  
5665 C CG  . LYS D 14  ? 1.0723 0.7521 1.1525 0.1704  0.0022  0.3648  13  LYS C CG  
5666 C CD  . LYS D 14  ? 1.2300 0.8593 1.3319 0.1890  -0.0512 0.3808  13  LYS C CD  
5667 C CE  . LYS D 14  ? 1.3065 0.9034 1.4545 0.1778  -0.0528 0.3913  13  LYS C CE  
5668 N NZ  . LYS D 14  ? 1.3291 0.8932 1.4743 0.1874  -0.1001 0.3804  13  LYS C NZ  
5669 N N   . LYS D 15  ? 1.2546 1.1303 1.5764 0.1146  0.0282  0.3573  14  LYS C N   
5670 C CA  . LYS D 15  ? 1.1122 1.0391 1.5076 0.0884  0.0522  0.3545  14  LYS C CA  
5671 C C   . LYS D 15  ? 1.0988 1.0050 1.5499 0.0951  0.0117  0.3678  14  LYS C C   
5672 O O   . LYS D 15  ? 1.0671 0.9301 1.4989 0.1196  -0.0335 0.3776  14  LYS C O   
5673 C CB  . LYS D 15  ? 1.0014 1.0090 1.4124 0.0743  0.0788  0.3413  14  LYS C CB  
5674 C CG  . LYS D 15  ? 1.1258 1.1730 1.5154 0.0534  0.1338  0.3272  14  LYS C CG  
5675 C CD  . LYS D 15  ? 1.1043 1.1328 1.5136 0.0346  0.1624  0.3284  14  LYS C CD  
5676 C CE  . LYS D 15  ? 1.1187 1.1780 1.4967 0.0166  0.2148  0.3151  14  LYS C CE  
5677 N NZ  . LYS D 15  ? 0.9106 0.9394 1.2072 0.0336  0.2152  0.3116  14  LYS C NZ  
# 
