data_9FJ0
# 
_entry.id   9FJ0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FJ0         pdb_00009fj0 10.2210/pdb9fj0/pdb 
WWPDB D_1292139018 ?            ?                   
# 
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 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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                        9FJ0 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guardado@pasteur.fr 
_pdbx_contact_author.name_first         Pablo 
_pdbx_contact_author.name_last          Guardado-Calvo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7292-5270 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vernuccio, R.'      1 0009-0009-8319-0922 
'Guardado-Calvo, P.' 2 0000-0001-7292-5270 
# 
_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            'Nat Microbiol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2058-5276 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                734 
_citation.page_last                 748 
_citation.title                     'Structural insights into tecovirimat antiviral activity and poxvirus resistance.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41564-025-01936-6 
_citation.pdbx_database_id_PubMed   39939832 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vernuccio, R.'         1  0009-0009-8319-0922 
primary 'Martinez Leon, A.'     2  0009-0005-6162-7303 
primary 'Poojari, C.S.'         3  0000-0001-6575-221X 
primary 'Buchrieser, J.'        4  0000-0003-4790-7577 
primary 'Selverian, C.N.'       5  0000-0002-1047-4336 
primary 'Jaleta, Y.'            6  ?                   
primary 'Meola, A.'             7  ?                   
primary 'Guivel-Benhassine, F.' 8  ?                   
primary 'Porrot, F.'            9  0000-0001-8995-3614 
primary 'Haouz, A.'             10 0000-0003-1196-1635 
primary 'Chevreuil, M.'         11 ?                   
primary 'Raynal, B.'            12 0000-0001-5634-0408 
primary 'Mercer, J.'            13 ?                   
primary 'Simon-Loriere, E.'     14 0000-0001-8420-7743 
primary 'Chandran, K.'          15 0000-0003-0232-7077 
primary 'Schwartz, O.'          16 0000-0002-0729-1475 
primary 'Hub, J.S.'             17 0000-0001-7716-1767 
primary 'Guardado-Calvo, P.'    18 0000-0001-7292-5270 
# 
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 'Envelope phospholipase OPG057' 42312.891 1 3.1.1.-,3.1.4.4 ? ? ? 
2 non-polymer syn GLYCEROL                        92.094    1 ?               ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '37 kDa protein,Envelope phospholipase F13,Palmitoylated EV membrane protein,p37K' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;HHHHHHHHGSGSVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASE
KGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYP
PLATDLRRRFDTFKAFNSAKNSAANLASAAAALPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSI
DIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVCNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTK
LLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHHHGSGSVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASE
KGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYP
PLATDLRRRFDTFKAFNSAKNSAANLASAAAALPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSI
DIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVCNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTK
LLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        GLYCEROL 
_pdbx_entity_nonpoly.comp_id     GOL 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   GLY n 
1 10  SER n 
1 11  GLY n 
1 12  SER n 
1 13  VAL n 
1 14  PRO n 
1 15  ALA n 
1 16  GLY n 
1 17  ALA n 
1 18  LYS n 
1 19  CYS n 
1 20  ARG n 
1 21  LEU n 
1 22  VAL n 
1 23  GLU n 
1 24  THR n 
1 25  LEU n 
1 26  PRO n 
1 27  GLU n 
1 28  ASN n 
1 29  MET n 
1 30  ASP n 
1 31  PHE n 
1 32  ARG n 
1 33  SER n 
1 34  ASP n 
1 35  HIS n 
1 36  LEU n 
1 37  THR n 
1 38  THR n 
1 39  PHE n 
1 40  GLU n 
1 41  CYS n 
1 42  PHE n 
1 43  ASN n 
1 44  GLU n 
1 45  ILE n 
1 46  ILE n 
1 47  THR n 
1 48  LEU n 
1 49  ALA n 
1 50  LYS n 
1 51  LYS n 
1 52  TYR n 
1 53  ILE n 
1 54  TYR n 
1 55  ILE n 
1 56  ALA n 
1 57  SER n 
1 58  PHE n 
1 59  CYS n 
1 60  CYS n 
1 61  ASN n 
1 62  PRO n 
1 63  LEU n 
1 64  SER n 
1 65  THR n 
1 66  THR n 
1 67  ARG n 
1 68  GLY n 
1 69  ALA n 
1 70  LEU n 
1 71  ILE n 
1 72  PHE n 
1 73  ASP n 
1 74  LYS n 
1 75  LEU n 
1 76  LYS n 
1 77  GLU n 
1 78  ALA n 
1 79  SER n 
1 80  GLU n 
1 81  LYS n 
1 82  GLY n 
1 83  ILE n 
1 84  LYS n 
1 85  ILE n 
1 86  ILE n 
1 87  VAL n 
1 88  LEU n 
1 89  LEU n 
1 90  ASP n 
1 91  GLU n 
1 92  ARG n 
1 93  GLY n 
1 94  LYS n 
1 95  ARG n 
1 96  ASN n 
1 97  LEU n 
1 98  GLY n 
1 99  GLU n 
1 100 LEU n 
1 101 GLN n 
1 102 SER n 
1 103 HIS n 
1 104 CYS n 
1 105 PRO n 
1 106 ASP n 
1 107 ILE n 
1 108 ASN n 
1 109 PHE n 
1 110 ILE n 
1 111 THR n 
1 112 VAL n 
1 113 ASN n 
1 114 ILE n 
1 115 ASP n 
1 116 LYS n 
1 117 LYS n 
1 118 ASN n 
1 119 ASN n 
1 120 VAL n 
1 121 GLY n 
1 122 LEU n 
1 123 LEU n 
1 124 LEU n 
1 125 GLY n 
1 126 CYS n 
1 127 PHE n 
1 128 TRP n 
1 129 VAL n 
1 130 SER n 
1 131 ASP n 
1 132 ASP n 
1 133 GLU n 
1 134 ARG n 
1 135 CYS n 
1 136 TYR n 
1 137 VAL n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 SER n 
1 142 PHE n 
1 143 THR n 
1 144 GLY n 
1 145 GLY n 
1 146 SER n 
1 147 ILE n 
1 148 HIS n 
1 149 THR n 
1 150 ILE n 
1 151 LYS n 
1 152 THR n 
1 153 LEU n 
1 154 GLY n 
1 155 VAL n 
1 156 TYR n 
1 157 SER n 
1 158 ASP n 
1 159 TYR n 
1 160 PRO n 
1 161 PRO n 
1 162 LEU n 
1 163 ALA n 
1 164 THR n 
1 165 ASP n 
1 166 LEU n 
1 167 ARG n 
1 168 ARG n 
1 169 ARG n 
1 170 PHE n 
1 171 ASP n 
1 172 THR n 
1 173 PHE n 
1 174 LYS n 
1 175 ALA n 
1 176 PHE n 
1 177 ASN n 
1 178 SER n 
1 179 ALA n 
1 180 LYS n 
1 181 ASN n 
1 182 SER n 
1 183 ALA n 
1 184 ALA n 
1 185 ASN n 
1 186 LEU n 
1 187 ALA n 
1 188 SER n 
1 189 ALA n 
1 190 ALA n 
1 191 ALA n 
1 192 ALA n 
1 193 LEU n 
1 194 PRO n 
1 195 VAL n 
1 196 SER n 
1 197 THR n 
1 198 ALA n 
1 199 TYR n 
1 200 HIS n 
1 201 ILE n 
1 202 LYS n 
1 203 ASN n 
1 204 PRO n 
1 205 ILE n 
1 206 GLY n 
1 207 GLY n 
1 208 VAL n 
1 209 PHE n 
1 210 PHE n 
1 211 THR n 
1 212 ASP n 
1 213 SER n 
1 214 PRO n 
1 215 GLU n 
1 216 HIS n 
1 217 LEU n 
1 218 LEU n 
1 219 GLY n 
1 220 TYR n 
1 221 SER n 
1 222 ARG n 
1 223 ASP n 
1 224 LEU n 
1 225 ASP n 
1 226 THR n 
1 227 ASP n 
1 228 VAL n 
1 229 VAL n 
1 230 ILE n 
1 231 ASP n 
1 232 LYS n 
1 233 LEU n 
1 234 LYS n 
1 235 SER n 
1 236 ALA n 
1 237 LYS n 
1 238 THR n 
1 239 SER n 
1 240 ILE n 
1 241 ASP n 
1 242 ILE n 
1 243 GLU n 
1 244 HIS n 
1 245 LEU n 
1 246 ALA n 
1 247 ILE n 
1 248 VAL n 
1 249 PRO n 
1 250 THR n 
1 251 THR n 
1 252 ARG n 
1 253 VAL n 
1 254 ASP n 
1 255 GLY n 
1 256 ASN n 
1 257 SER n 
1 258 TYR n 
1 259 TYR n 
1 260 TRP n 
1 261 PRO n 
1 262 ASP n 
1 263 ILE n 
1 264 TYR n 
1 265 ASN n 
1 266 SER n 
1 267 ILE n 
1 268 ILE n 
1 269 GLU n 
1 270 ALA n 
1 271 ALA n 
1 272 ILE n 
1 273 ASN n 
1 274 ARG n 
1 275 GLY n 
1 276 VAL n 
1 277 LYS n 
1 278 ILE n 
1 279 ARG n 
1 280 LEU n 
1 281 LEU n 
1 282 VAL n 
1 283 CYS n 
1 284 ASN n 
1 285 TRP n 
1 286 ASP n 
1 287 LYS n 
1 288 ASN n 
1 289 ASP n 
1 290 VAL n 
1 291 TYR n 
1 292 SER n 
1 293 MET n 
1 294 ALA n 
1 295 THR n 
1 296 ALA n 
1 297 ARG n 
1 298 SER n 
1 299 LEU n 
1 300 ASP n 
1 301 ALA n 
1 302 LEU n 
1 303 CYS n 
1 304 VAL n 
1 305 GLN n 
1 306 ASN n 
1 307 ASP n 
1 308 LEU n 
1 309 SER n 
1 310 VAL n 
1 311 LYS n 
1 312 VAL n 
1 313 PHE n 
1 314 THR n 
1 315 ILE n 
1 316 GLN n 
1 317 ASN n 
1 318 ASN n 
1 319 THR n 
1 320 LYS n 
1 321 LEU n 
1 322 LEU n 
1 323 ILE n 
1 324 VAL n 
1 325 ASP n 
1 326 ASP n 
1 327 GLU n 
1 328 TYR n 
1 329 VAL n 
1 330 HIS n 
1 331 ILE n 
1 332 THR n 
1 333 SER n 
1 334 ALA n 
1 335 ASN n 
1 336 PHE n 
1 337 ASP n 
1 338 GLY n 
1 339 THR n 
1 340 HIS n 
1 341 TYR n 
1 342 GLN n 
1 343 ASN n 
1 344 HIS n 
1 345 GLY n 
1 346 PHE n 
1 347 VAL n 
1 348 SER n 
1 349 PHE n 
1 350 ASN n 
1 351 SER n 
1 352 ILE n 
1 353 ASP n 
1 354 LYS n 
1 355 GLN n 
1 356 LEU n 
1 357 VAL n 
1 358 SER n 
1 359 GLU n 
1 360 ALA n 
1 361 LYS n 
1 362 LYS n 
1 363 ILE n 
1 364 PHE n 
1 365 GLU n 
1 366 ARG n 
1 367 ASP n 
1 368 TRP n 
1 369 VAL n 
1 370 SER n 
1 371 SER n 
1 372 HIS n 
1 373 SER n 
1 374 LYS n 
1 375 SER n 
1 376 LEU n 
1 377 LYS n 
1 378 ILE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   378 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'OPG057, VACWR052, F13L' 
_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      'Vaccinia virus Western Reserve' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     696871 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
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   HIS 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   HIS 7   1   ?   ?   ?   A . n 
A 1 8   HIS 8   2   ?   ?   ?   A . n 
A 1 9   GLY 9   3   ?   ?   ?   A . n 
A 1 10  SER 10  4   ?   ?   ?   A . n 
A 1 11  GLY 11  5   ?   ?   ?   A . n 
A 1 12  SER 12  6   6   SER SER A . n 
A 1 13  VAL 13  7   7   VAL VAL A . n 
A 1 14  PRO 14  8   8   PRO PRO A . n 
A 1 15  ALA 15  9   9   ALA ALA A . n 
A 1 16  GLY 16  10  10  GLY GLY A . n 
A 1 17  ALA 17  11  11  ALA ALA A . n 
A 1 18  LYS 18  12  12  LYS LYS A . n 
A 1 19  CYS 19  13  13  CYS CYS A . n 
A 1 20  ARG 20  14  14  ARG ARG A . n 
A 1 21  LEU 21  15  15  LEU LEU A . n 
A 1 22  VAL 22  16  16  VAL VAL A . n 
A 1 23  GLU 23  17  17  GLU GLU A . n 
A 1 24  THR 24  18  18  THR THR A . n 
A 1 25  LEU 25  19  19  LEU LEU A . n 
A 1 26  PRO 26  20  20  PRO PRO A . n 
A 1 27  GLU 27  21  21  GLU GLU A . n 
A 1 28  ASN 28  22  22  ASN ASN A . n 
A 1 29  MET 29  23  23  MET MET A . n 
A 1 30  ASP 30  24  24  ASP ASP A . n 
A 1 31  PHE 31  25  25  PHE PHE A . n 
A 1 32  ARG 32  26  26  ARG ARG A . n 
A 1 33  SER 33  27  27  SER SER A . n 
A 1 34  ASP 34  28  28  ASP ASP A . n 
A 1 35  HIS 35  29  29  HIS HIS A . n 
A 1 36  LEU 36  30  30  LEU LEU A . n 
A 1 37  THR 37  31  31  THR THR A . n 
A 1 38  THR 38  32  32  THR THR A . n 
A 1 39  PHE 39  33  33  PHE PHE A . n 
A 1 40  GLU 40  34  34  GLU GLU A . n 
A 1 41  CYS 41  35  35  CYS CYS A . n 
A 1 42  PHE 42  36  36  PHE PHE A . n 
A 1 43  ASN 43  37  37  ASN ASN A . n 
A 1 44  GLU 44  38  38  GLU GLU A . n 
A 1 45  ILE 45  39  39  ILE ILE A . n 
A 1 46  ILE 46  40  40  ILE ILE A . n 
A 1 47  THR 47  41  41  THR THR A . n 
A 1 48  LEU 48  42  42  LEU LEU A . n 
A 1 49  ALA 49  43  43  ALA ALA A . n 
A 1 50  LYS 50  44  44  LYS LYS A . n 
A 1 51  LYS 51  45  45  LYS LYS A . n 
A 1 52  TYR 52  46  46  TYR TYR A . n 
A 1 53  ILE 53  47  47  ILE ILE A . n 
A 1 54  TYR 54  48  48  TYR TYR A . n 
A 1 55  ILE 55  49  49  ILE ILE A . n 
A 1 56  ALA 56  50  50  ALA ALA A . n 
A 1 57  SER 57  51  51  SER SER A . n 
A 1 58  PHE 58  52  52  PHE PHE A . n 
A 1 59  CYS 59  53  53  CYS CYS A . n 
A 1 60  CYS 60  54  54  CYS CYS A . n 
A 1 61  ASN 61  55  55  ASN ASN A . n 
A 1 62  PRO 62  56  56  PRO PRO A . n 
A 1 63  LEU 63  57  57  LEU LEU A . n 
A 1 64  SER 64  58  58  SER SER A . n 
A 1 65  THR 65  59  59  THR THR A . n 
A 1 66  THR 66  60  60  THR THR A . n 
A 1 67  ARG 67  61  61  ARG ARG A . n 
A 1 68  GLY 68  62  62  GLY GLY A . n 
A 1 69  ALA 69  63  63  ALA ALA A . n 
A 1 70  LEU 70  64  64  LEU LEU A . n 
A 1 71  ILE 71  65  65  ILE ILE A . n 
A 1 72  PHE 72  66  66  PHE PHE A . n 
A 1 73  ASP 73  67  67  ASP ASP A . n 
A 1 74  LYS 74  68  68  LYS LYS A . n 
A 1 75  LEU 75  69  69  LEU LEU A . n 
A 1 76  LYS 76  70  70  LYS LYS A . n 
A 1 77  GLU 77  71  71  GLU GLU A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  SER 79  73  73  SER SER A . n 
A 1 80  GLU 80  74  74  GLU GLU A . n 
A 1 81  LYS 81  75  75  LYS LYS A . n 
A 1 82  GLY 82  76  76  GLY GLY A . n 
A 1 83  ILE 83  77  77  ILE ILE A . n 
A 1 84  LYS 84  78  78  LYS LYS A . n 
A 1 85  ILE 85  79  79  ILE ILE A . n 
A 1 86  ILE 86  80  80  ILE ILE A . n 
A 1 87  VAL 87  81  81  VAL VAL A . n 
A 1 88  LEU 88  82  82  LEU LEU A . n 
A 1 89  LEU 89  83  83  LEU LEU A . n 
A 1 90  ASP 90  84  84  ASP ASP A . n 
A 1 91  GLU 91  85  85  GLU GLU A . n 
A 1 92  ARG 92  86  86  ARG ARG A . n 
A 1 93  GLY 93  87  87  GLY GLY A . n 
A 1 94  LYS 94  88  88  LYS LYS A . n 
A 1 95  ARG 95  89  89  ARG ARG A . n 
A 1 96  ASN 96  90  90  ASN ASN A . n 
A 1 97  LEU 97  91  91  LEU LEU A . n 
A 1 98  GLY 98  92  92  GLY GLY A . n 
A 1 99  GLU 99  93  93  GLU GLU A . n 
A 1 100 LEU 100 94  94  LEU LEU A . n 
A 1 101 GLN 101 95  95  GLN GLN A . n 
A 1 102 SER 102 96  96  SER SER A . n 
A 1 103 HIS 103 97  97  HIS HIS A . n 
A 1 104 CYS 104 98  98  CYS CYS A . n 
A 1 105 PRO 105 99  99  PRO PRO A . n 
A 1 106 ASP 106 100 100 ASP ASP A . n 
A 1 107 ILE 107 101 101 ILE ILE A . n 
A 1 108 ASN 108 102 102 ASN ASN A . n 
A 1 109 PHE 109 103 103 PHE PHE A . n 
A 1 110 ILE 110 104 104 ILE ILE A . n 
A 1 111 THR 111 105 105 THR THR A . n 
A 1 112 VAL 112 106 106 VAL VAL A . n 
A 1 113 ASN 113 107 107 ASN ASN A . n 
A 1 114 ILE 114 108 108 ILE ILE A . n 
A 1 115 ASP 115 109 109 ASP ASP A . n 
A 1 116 LYS 116 110 110 LYS LYS A . n 
A 1 117 LYS 117 111 111 LYS LYS A . n 
A 1 118 ASN 118 112 112 ASN ASN A . n 
A 1 119 ASN 119 113 113 ASN ASN A . n 
A 1 120 VAL 120 114 114 VAL VAL A . n 
A 1 121 GLY 121 115 115 GLY GLY A . n 
A 1 122 LEU 122 116 116 LEU LEU A . n 
A 1 123 LEU 123 117 117 LEU LEU A . n 
A 1 124 LEU 124 118 118 LEU LEU A . n 
A 1 125 GLY 125 119 119 GLY GLY A . n 
A 1 126 CYS 126 120 120 CYS CYS A . n 
A 1 127 PHE 127 121 121 PHE PHE A . n 
A 1 128 TRP 128 122 122 TRP TRP A . n 
A 1 129 VAL 129 123 123 VAL VAL A . n 
A 1 130 SER 130 124 124 SER SER A . n 
A 1 131 ASP 131 125 125 ASP ASP A . n 
A 1 132 ASP 132 126 126 ASP ASP A . n 
A 1 133 GLU 133 127 127 GLU GLU A . n 
A 1 134 ARG 134 128 128 ARG ARG A . n 
A 1 135 CYS 135 129 129 CYS CYS A . n 
A 1 136 TYR 136 130 130 TYR TYR A . n 
A 1 137 VAL 137 131 131 VAL VAL A . n 
A 1 138 GLY 138 132 132 GLY GLY A . n 
A 1 139 ASN 139 133 133 ASN ASN A . n 
A 1 140 ALA 140 134 134 ALA ALA A . n 
A 1 141 SER 141 135 135 SER SER A . n 
A 1 142 PHE 142 136 136 PHE PHE A . n 
A 1 143 THR 143 137 137 THR THR A . n 
A 1 144 GLY 144 138 138 GLY GLY A . n 
A 1 145 GLY 145 139 139 GLY GLY A . n 
A 1 146 SER 146 140 140 SER SER A . n 
A 1 147 ILE 147 141 141 ILE ILE A . n 
A 1 148 HIS 148 142 142 HIS HIS A . n 
A 1 149 THR 149 143 143 THR THR A . n 
A 1 150 ILE 150 144 144 ILE ILE A . n 
A 1 151 LYS 151 145 145 LYS LYS A . n 
A 1 152 THR 152 146 146 THR THR A . n 
A 1 153 LEU 153 147 147 LEU LEU A . n 
A 1 154 GLY 154 148 148 GLY GLY A . n 
A 1 155 VAL 155 149 149 VAL VAL A . n 
A 1 156 TYR 156 150 150 TYR TYR A . n 
A 1 157 SER 157 151 151 SER SER A . n 
A 1 158 ASP 158 152 152 ASP ASP A . n 
A 1 159 TYR 159 153 153 TYR TYR A . n 
A 1 160 PRO 160 154 154 PRO PRO A . n 
A 1 161 PRO 161 155 155 PRO PRO A . n 
A 1 162 LEU 162 156 156 LEU LEU A . n 
A 1 163 ALA 163 157 157 ALA ALA A . n 
A 1 164 THR 164 158 158 THR THR A . n 
A 1 165 ASP 165 159 159 ASP ASP A . n 
A 1 166 LEU 166 160 160 LEU LEU A . n 
A 1 167 ARG 167 161 161 ARG ARG A . n 
A 1 168 ARG 168 162 162 ARG ARG A . n 
A 1 169 ARG 169 163 163 ARG ARG A . n 
A 1 170 PHE 170 164 164 PHE PHE A . n 
A 1 171 ASP 171 165 165 ASP ASP A . n 
A 1 172 THR 172 166 166 THR THR A . n 
A 1 173 PHE 173 167 167 PHE PHE A . n 
A 1 174 LYS 174 168 168 LYS LYS A . n 
A 1 175 ALA 175 169 169 ALA ALA A . n 
A 1 176 PHE 176 170 170 PHE PHE A . n 
A 1 177 ASN 177 171 171 ASN ASN A . n 
A 1 178 SER 178 172 172 SER SER A . n 
A 1 179 ALA 179 173 173 ALA ALA A . n 
A 1 180 LYS 180 174 174 LYS LYS A . n 
A 1 181 ASN 181 175 175 ASN ASN A . n 
A 1 182 SER 182 176 176 SER SER A . n 
A 1 183 ALA 183 177 177 ALA ALA A . n 
A 1 184 ALA 184 178 178 ALA ALA A . n 
A 1 185 ASN 185 179 179 ASN ASN A . n 
A 1 186 LEU 186 180 180 LEU LEU A . n 
A 1 187 ALA 187 181 181 ALA ALA A . n 
A 1 188 SER 188 182 182 SER SER A . n 
A 1 189 ALA 189 183 183 ALA ALA A . n 
A 1 190 ALA 190 184 184 ALA ALA A . n 
A 1 191 ALA 191 185 185 ALA ALA A . n 
A 1 192 ALA 192 186 186 ALA ALA A . n 
A 1 193 LEU 193 187 187 LEU LEU A . n 
A 1 194 PRO 194 188 188 PRO PRO A . n 
A 1 195 VAL 195 189 189 VAL VAL A . n 
A 1 196 SER 196 190 190 SER SER A . n 
A 1 197 THR 197 191 191 THR THR A . n 
A 1 198 ALA 198 192 192 ALA ALA A . n 
A 1 199 TYR 199 193 193 TYR TYR A . n 
A 1 200 HIS 200 194 194 HIS HIS A . n 
A 1 201 ILE 201 195 195 ILE ILE A . n 
A 1 202 LYS 202 196 196 LYS LYS A . n 
A 1 203 ASN 203 197 197 ASN ASN A . n 
A 1 204 PRO 204 198 198 PRO PRO A . n 
A 1 205 ILE 205 199 199 ILE ILE A . n 
A 1 206 GLY 206 200 200 GLY GLY A . n 
A 1 207 GLY 207 201 201 GLY GLY A . n 
A 1 208 VAL 208 202 202 VAL VAL A . n 
A 1 209 PHE 209 203 203 PHE PHE A . n 
A 1 210 PHE 210 204 204 PHE PHE A . n 
A 1 211 THR 211 205 205 THR THR A . n 
A 1 212 ASP 212 206 206 ASP ASP A . n 
A 1 213 SER 213 207 207 SER SER A . n 
A 1 214 PRO 214 208 208 PRO PRO A . n 
A 1 215 GLU 215 209 209 GLU GLU A . n 
A 1 216 HIS 216 210 210 HIS HIS A . n 
A 1 217 LEU 217 211 211 LEU LEU A . n 
A 1 218 LEU 218 212 212 LEU LEU A . n 
A 1 219 GLY 219 213 213 GLY GLY A . n 
A 1 220 TYR 220 214 214 TYR TYR A . n 
A 1 221 SER 221 215 215 SER SER A . n 
A 1 222 ARG 222 216 216 ARG ARG A . n 
A 1 223 ASP 223 217 217 ASP ASP A . n 
A 1 224 LEU 224 218 218 LEU LEU A . n 
A 1 225 ASP 225 219 219 ASP ASP A . n 
A 1 226 THR 226 220 220 THR THR A . n 
A 1 227 ASP 227 221 221 ASP ASP A . n 
A 1 228 VAL 228 222 222 VAL VAL A . n 
A 1 229 VAL 229 223 223 VAL VAL A . n 
A 1 230 ILE 230 224 224 ILE ILE A . n 
A 1 231 ASP 231 225 225 ASP ASP A . n 
A 1 232 LYS 232 226 226 LYS LYS A . n 
A 1 233 LEU 233 227 227 LEU LEU A . n 
A 1 234 LYS 234 228 228 LYS LYS A . n 
A 1 235 SER 235 229 229 SER SER A . n 
A 1 236 ALA 236 230 230 ALA ALA A . n 
A 1 237 LYS 237 231 231 LYS LYS A . n 
A 1 238 THR 238 232 232 THR THR A . n 
A 1 239 SER 239 233 233 SER SER A . n 
A 1 240 ILE 240 234 234 ILE ILE A . n 
A 1 241 ASP 241 235 235 ASP ASP A . n 
A 1 242 ILE 242 236 236 ILE ILE A . n 
A 1 243 GLU 243 237 237 GLU GLU A . n 
A 1 244 HIS 244 238 238 HIS HIS A . n 
A 1 245 LEU 245 239 239 LEU LEU A . n 
A 1 246 ALA 246 240 240 ALA ALA A . n 
A 1 247 ILE 247 241 241 ILE ILE A . n 
A 1 248 VAL 248 242 242 VAL VAL A . n 
A 1 249 PRO 249 243 243 PRO PRO A . n 
A 1 250 THR 250 244 244 THR THR A . n 
A 1 251 THR 251 245 245 THR THR A . n 
A 1 252 ARG 252 246 246 ARG ARG A . n 
A 1 253 VAL 253 247 247 VAL VAL A . n 
A 1 254 ASP 254 248 248 ASP ASP A . n 
A 1 255 GLY 255 249 249 GLY GLY A . n 
A 1 256 ASN 256 250 250 ASN ASN A . n 
A 1 257 SER 257 251 251 SER SER A . n 
A 1 258 TYR 258 252 252 TYR TYR A . n 
A 1 259 TYR 259 253 253 TYR TYR A . n 
A 1 260 TRP 260 254 254 TRP TRP A . n 
A 1 261 PRO 261 255 255 PRO PRO A . n 
A 1 262 ASP 262 256 256 ASP ASP A . n 
A 1 263 ILE 263 257 257 ILE ILE A . n 
A 1 264 TYR 264 258 258 TYR TYR A . n 
A 1 265 ASN 265 259 259 ASN ASN A . n 
A 1 266 SER 266 260 260 SER SER A . n 
A 1 267 ILE 267 261 261 ILE ILE A . n 
A 1 268 ILE 268 262 262 ILE ILE A . n 
A 1 269 GLU 269 263 263 GLU GLU A . n 
A 1 270 ALA 270 264 264 ALA ALA A . n 
A 1 271 ALA 271 265 265 ALA ALA A . n 
A 1 272 ILE 272 266 266 ILE ILE A . n 
A 1 273 ASN 273 267 267 ASN ASN A . n 
A 1 274 ARG 274 268 268 ARG ARG A . n 
A 1 275 GLY 275 269 269 GLY GLY A . n 
A 1 276 VAL 276 270 270 VAL VAL A . n 
A 1 277 LYS 277 271 271 LYS LYS A . n 
A 1 278 ILE 278 272 272 ILE ILE A . n 
A 1 279 ARG 279 273 273 ARG ARG A . n 
A 1 280 LEU 280 274 274 LEU LEU A . n 
A 1 281 LEU 281 275 275 LEU LEU A . n 
A 1 282 VAL 282 276 276 VAL VAL A . n 
A 1 283 CYS 283 277 277 CYS CYS A . n 
A 1 284 ASN 284 278 278 ASN ASN A . n 
A 1 285 TRP 285 279 279 TRP TRP A . n 
A 1 286 ASP 286 280 280 ASP ASP A . n 
A 1 287 LYS 287 281 281 LYS LYS A . n 
A 1 288 ASN 288 282 282 ASN ASN A . n 
A 1 289 ASP 289 283 283 ASP ASP A . n 
A 1 290 VAL 290 284 284 VAL VAL A . n 
A 1 291 TYR 291 285 285 TYR TYR A . n 
A 1 292 SER 292 286 286 SER SER A . n 
A 1 293 MET 293 287 287 MET MET A . n 
A 1 294 ALA 294 288 288 ALA ALA A . n 
A 1 295 THR 295 289 289 THR THR A . n 
A 1 296 ALA 296 290 290 ALA ALA A . n 
A 1 297 ARG 297 291 291 ARG ARG A . n 
A 1 298 SER 298 292 292 SER SER A . n 
A 1 299 LEU 299 293 293 LEU LEU A . n 
A 1 300 ASP 300 294 294 ASP ASP A . n 
A 1 301 ALA 301 295 295 ALA ALA A . n 
A 1 302 LEU 302 296 296 LEU LEU A . n 
A 1 303 CYS 303 297 297 CYS CYS A . n 
A 1 304 VAL 304 298 298 VAL VAL A . n 
A 1 305 GLN 305 299 299 GLN GLN A . n 
A 1 306 ASN 306 300 300 ASN ASN A . n 
A 1 307 ASP 307 301 301 ASP ASP A . n 
A 1 308 LEU 308 302 302 LEU LEU A . n 
A 1 309 SER 309 303 303 SER SER A . n 
A 1 310 VAL 310 304 304 VAL VAL A . n 
A 1 311 LYS 311 305 305 LYS LYS A . n 
A 1 312 VAL 312 306 306 VAL VAL A . n 
A 1 313 PHE 313 307 307 PHE PHE A . n 
A 1 314 THR 314 308 308 THR THR A . n 
A 1 315 ILE 315 309 309 ILE ILE A . n 
A 1 316 GLN 316 310 310 GLN GLN A . n 
A 1 317 ASN 317 311 311 ASN ASN A . n 
A 1 318 ASN 318 312 312 ASN ASN A . n 
A 1 319 THR 319 313 313 THR THR A . n 
A 1 320 LYS 320 314 314 LYS LYS A . n 
A 1 321 LEU 321 315 315 LEU LEU A . n 
A 1 322 LEU 322 316 316 LEU LEU A . n 
A 1 323 ILE 323 317 317 ILE ILE A . n 
A 1 324 VAL 324 318 318 VAL VAL A . n 
A 1 325 ASP 325 319 319 ASP ASP A . n 
A 1 326 ASP 326 320 320 ASP ASP A . n 
A 1 327 GLU 327 321 321 GLU GLU A . n 
A 1 328 TYR 328 322 322 TYR TYR A . n 
A 1 329 VAL 329 323 323 VAL VAL A . n 
A 1 330 HIS 330 324 324 HIS HIS A . n 
A 1 331 ILE 331 325 325 ILE ILE A . n 
A 1 332 THR 332 326 326 THR THR A . n 
A 1 333 SER 333 327 327 SER SER A . n 
A 1 334 ALA 334 328 328 ALA ALA A . n 
A 1 335 ASN 335 329 329 ASN ASN A . n 
A 1 336 PHE 336 330 330 PHE PHE A . n 
A 1 337 ASP 337 331 331 ASP ASP A . n 
A 1 338 GLY 338 332 332 GLY GLY A . n 
A 1 339 THR 339 333 333 THR THR A . n 
A 1 340 HIS 340 334 334 HIS HIS A . n 
A 1 341 TYR 341 335 335 TYR TYR A . n 
A 1 342 GLN 342 336 336 GLN GLN A . n 
A 1 343 ASN 343 337 337 ASN ASN A . n 
A 1 344 HIS 344 338 338 HIS HIS A . n 
A 1 345 GLY 345 339 339 GLY GLY A . n 
A 1 346 PHE 346 340 340 PHE PHE A . n 
A 1 347 VAL 347 341 341 VAL VAL A . n 
A 1 348 SER 348 342 342 SER SER A . n 
A 1 349 PHE 349 343 343 PHE PHE A . n 
A 1 350 ASN 350 344 344 ASN ASN A . n 
A 1 351 SER 351 345 345 SER SER A . n 
A 1 352 ILE 352 346 346 ILE ILE A . n 
A 1 353 ASP 353 347 347 ASP ASP A . n 
A 1 354 LYS 354 348 348 LYS LYS A . n 
A 1 355 GLN 355 349 349 GLN GLN A . n 
A 1 356 LEU 356 350 350 LEU LEU A . n 
A 1 357 VAL 357 351 351 VAL VAL A . n 
A 1 358 SER 358 352 352 SER SER A . n 
A 1 359 GLU 359 353 353 GLU GLU A . n 
A 1 360 ALA 360 354 354 ALA ALA A . n 
A 1 361 LYS 361 355 355 LYS LYS A . n 
A 1 362 LYS 362 356 356 LYS LYS A . n 
A 1 363 ILE 363 357 357 ILE ILE A . n 
A 1 364 PHE 364 358 358 PHE PHE A . n 
A 1 365 GLU 365 359 359 GLU GLU A . n 
A 1 366 ARG 366 360 360 ARG ARG A . n 
A 1 367 ASP 367 361 361 ASP ASP A . n 
A 1 368 TRP 368 362 362 TRP TRP A . n 
A 1 369 VAL 369 363 363 VAL VAL A . n 
A 1 370 SER 370 364 364 SER SER A . n 
A 1 371 SER 371 365 365 SER SER A . n 
A 1 372 HIS 372 366 366 HIS HIS A . n 
A 1 373 SER 373 367 367 SER SER A . n 
A 1 374 LYS 374 368 368 LYS LYS A . n 
A 1 375 SER 375 369 369 SER SER A . n 
A 1 376 LEU 376 370 370 LEU LEU A . n 
A 1 377 LYS 377 371 371 LYS LYS A . n 
A 1 378 ILE 378 372 372 ILE ILE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          GOL 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     401 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      GOL 
_pdbx_nonpoly_scheme.auth_mon_id     GOL 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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  ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FJ0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     281.052 
_cell.length_a_esd                 ? 
_cell.length_b                     281.052 
_cell.length_b_esd                 ? 
_cell.length_c                     281.052 
_cell.length_c_esd                 ? 
_cell.volume                       22200361.196 
_cell.volume_esd                   ? 
_cell.Z_PDB                        96 
_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                         9FJ0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                209 
_symmetry.space_group_name_Hall            'F 4 2 3' 
_symmetry.space_group_name_H-M             'F 4 3 2' 
_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                   9FJ0 
_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             5.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          77.49 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '1 M Na3 citrate, 0.1 M Imidazole pH 8 (crystals cryoprotected in 33% glycerol)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978565 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978565 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          189.54 
_reflns.entry_id                                       9FJ0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              4.0 
_reflns.d_resolution_low                               49.84 
_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                                     8510 
_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                           93.31 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                77.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    4.00 
_reflns_shell.d_res_low                                     4.47 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2335 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.564 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               254.64 
_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                                 9FJ0 
_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                            4.00 
_refine.ls_d_res_low                             49.68 
_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                     7954 
_refine.ls_number_reflns_R_free                  401 
_refine.ls_number_reflns_R_work                  7553 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.44 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2415 
_refine.ls_R_factor_R_free                       0.2760 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2396 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 47.8581 
_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                            0.8824 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       4.00 
_refine_hist.d_res_low                        49.68 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2892 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2886 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0016 ? 2950 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.3890 ? 4000 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0401 ? 460  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0037 ? 510  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.5526 ? 1068 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 4.00 4.58  . . 102 2096 80.10 . . . . 0.5025 . . . . . . . . . . . 0.5658 
'X-RAY DIFFRACTION' 4.58 5.77  . . 138 2646 99.89 . . . . 0.3130 . . . . . . . . . . . 0.3039 
'X-RAY DIFFRACTION' 5.77 49.68 . . 161 2811 99.70 . . . . 0.1879 . . . . . . . . . . . 0.2377 
# 
_struct.entry_id                     9FJ0 
_struct.title                        'Structure of the F13 protein (mutant G277C) of Vaccinia virus' 
_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        9FJ0 
_struct_keywords.text            'poxvirus, phospholipase D, vaccinia virus, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PG057_VACCW 
_struct_ref.pdbx_db_accession          P04021 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDE
RGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFD
TFKAFNSAKNSWLNLCSAACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTT
RVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHI
TSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_struct_ref.pdbx_align_begin           6 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FJ0 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 12 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 378 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P04021 
_struct_ref_seq.db_align_beg                  6 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  372 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       6 
_struct_ref_seq.pdbx_auth_seq_align_end       372 
# 
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 9FJ0 HIS A 1   ? UNP P04021 ?   ?   'expression tag'      -5  1  
1 9FJ0 HIS A 2   ? UNP P04021 ?   ?   'expression tag'      -4  2  
1 9FJ0 HIS A 3   ? UNP P04021 ?   ?   'expression tag'      -3  3  
1 9FJ0 HIS A 4   ? UNP P04021 ?   ?   'expression tag'      -2  4  
1 9FJ0 HIS A 5   ? UNP P04021 ?   ?   'expression tag'      -1  5  
1 9FJ0 HIS A 6   ? UNP P04021 ?   ?   'expression tag'      0   6  
1 9FJ0 HIS A 7   ? UNP P04021 ?   ?   'expression tag'      1   7  
1 9FJ0 HIS A 8   ? UNP P04021 ?   ?   'expression tag'      2   8  
1 9FJ0 GLY A 9   ? UNP P04021 ?   ?   'expression tag'      3   9  
1 9FJ0 SER A 10  ? UNP P04021 ?   ?   'expression tag'      4   10 
1 9FJ0 GLY A 11  ? UNP P04021 ?   ?   'expression tag'      5   11 
1 9FJ0 ALA A 183 ? UNP P04021 TRP 177 conflict              177 12 
1 9FJ0 ALA A 184 ? UNP P04021 LEU 178 conflict              178 13 
1 9FJ0 ALA A 187 ? UNP P04021 CYS 181 conflict              181 14 
1 9FJ0 ALA A 191 ? UNP P04021 CYS 185 conflict              185 15 
1 9FJ0 ALA A 192 ? UNP P04021 CYS 186 conflict              186 16 
1 9FJ0 CYS A 283 ? UNP P04021 GLY 277 'engineered mutation' 277 17 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 2040  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  29190 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z           1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000    
2 'crystal symmetry operation' 51_554 -x+1/2,y,-z-1/2 -1.0000000000 0.0000000000 0.0000000000 140.5260000000 0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -140.5260000000 
# 
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 PRO A 14  ? ALA A 17  ? PRO A 8   ALA A 11  5 ? 4  
HELX_P HELX_P2  AA2 THR A 38  ? LEU A 48  ? THR A 32  LEU A 42  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 61  ? SER A 64  ? ASN A 55  SER A 58  5 ? 4  
HELX_P HELX_P4  AA4 THR A 65  ? GLU A 80  ? THR A 59  GLU A 74  1 ? 16 
HELX_P HELX_P5  AA5 ARG A 92  ? ARG A 95  ? ARG A 86  ARG A 89  5 ? 4  
HELX_P HELX_P6  AA6 ASN A 96  ? CYS A 104 ? ASN A 90  CYS A 98  1 ? 9  
HELX_P HELX_P7  AA7 THR A 143 ? HIS A 148 ? THR A 137 HIS A 142 1 ? 6  
HELX_P HELX_P8  AA8 TYR A 159 ? ALA A 175 ? TYR A 153 ALA A 169 1 ? 17 
HELX_P HELX_P9  AA9 PRO A 214 ? LEU A 218 ? PRO A 208 LEU A 212 5 ? 5  
HELX_P HELX_P10 AB1 LEU A 224 ? SER A 235 ? LEU A 218 SER A 229 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 261 ? ILE A 272 ? PRO A 255 ILE A 266 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 289 ? VAL A 304 ? ASP A 283 VAL A 298 1 ? 16 
HELX_P HELX_P13 AB4 ASP A 337 ? HIS A 344 ? ASP A 331 HIS A 338 1 ? 8  
HELX_P HELX_P14 AB5 ASP A 353 ? VAL A 369 ? ASP A 347 VAL A 363 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           213 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            207 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    214 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     208 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.31 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 36  ? THR A 37  ? LEU A 30  THR A 31  
AA1 2 CYS A 19  ? THR A 24  ? CYS A 13  THR A 18  
AA1 3 THR A 152 ? SER A 157 ? THR A 146 SER A 151 
AA1 4 ARG A 134 ? GLY A 138 ? ARG A 128 GLY A 132 
AA1 5 PHE A 127 ? SER A 130 ? PHE A 121 SER A 124 
AA1 6 TYR A 52  ? SER A 57  ? TYR A 46  SER A 51  
AA1 7 LYS A 84  ? ASP A 90  ? LYS A 78  ASP A 84  
AA1 8 ASN A 108 ? VAL A 112 ? ASN A 102 VAL A 106 
AA2 1 VAL A 208 ? SER A 213 ? VAL A 202 SER A 207 
AA2 2 PHE A 346 ? SER A 351 ? PHE A 340 SER A 345 
AA2 3 TYR A 328 ? THR A 332 ? TYR A 322 THR A 326 
AA2 4 LYS A 320 ? VAL A 324 ? LYS A 314 VAL A 318 
AA2 5 SER A 239 ? GLU A 243 ? SER A 233 GLU A 237 
AA2 6 LYS A 277 ? CYS A 283 ? LYS A 271 CYS A 277 
AA2 7 LEU A 308 ? PHE A 313 ? LEU A 302 PHE A 307 
AA2 8 LYS A 374 ? SER A 375 ? LYS A 368 SER A 369 
AA3 1 THR A 250 ? VAL A 253 ? THR A 244 VAL A 247 
AA3 2 ASN A 256 ? TYR A 259 ? ASN A 250 TYR A 253 
# 
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 LEU A 36  ? O LEU A 30  N GLU A 23  ? N GLU A 17  
AA1 2 3 N VAL A 22  ? N VAL A 16  O GLY A 154 ? O GLY A 148 
AA1 3 4 O VAL A 155 ? O VAL A 149 N VAL A 137 ? N VAL A 131 
AA1 4 5 O TYR A 136 ? O TYR A 130 N TRP A 128 ? N TRP A 122 
AA1 5 6 O VAL A 129 ? O VAL A 123 N TYR A 54  ? N TYR A 48  
AA1 6 7 N ILE A 55  ? N ILE A 49  O LEU A 88  ? O LEU A 82  
AA1 7 8 N ILE A 85  ? N ILE A 79  O ASN A 108 ? O ASN A 102 
AA2 1 2 N PHE A 209 ? N PHE A 203 O ASN A 350 ? O ASN A 344 
AA2 2 3 O PHE A 349 ? O PHE A 343 N ILE A 331 ? N ILE A 325 
AA2 3 4 O HIS A 330 ? O HIS A 324 N LEU A 322 ? N LEU A 316 
AA2 4 5 O ILE A 323 ? O ILE A 317 N ASP A 241 ? N ASP A 235 
AA2 5 6 N ILE A 240 ? N ILE A 234 O ARG A 279 ? O ARG A 273 
AA2 6 7 N LEU A 280 ? N LEU A 274 O SER A 309 ? O SER A 303 
AA2 7 8 N VAL A 312 ? N VAL A 306 O LYS A 374 ? O LYS A 368 
AA3 1 2 N THR A 251 ? N THR A 245 O TYR A 258 ? O TYR A 252 
# 
_pdbx_entry_details.entry_id                   9FJ0 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 55  ? ? -161.55 86.01   
2 1 ASP A 125 ? ? 59.51   15.03   
3 1 HIS A 142 ? ? -121.42 -53.56  
4 1 LYS A 174 ? ? 59.18   -147.02 
5 1 SER A 176 ? ? -159.90 -159.09 
6 1 ASN A 197 ? ? -161.79 84.53   
7 1 ASP A 248 ? ? 59.66   -125.24 
8 1 PHE A 330 ? ? -66.41  99.71   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z            
2  x,-z,y           
3  x,z,-y           
4  z,y,-x           
5  -z,y,x           
6  -y,x,z           
7  y,-x,z           
8  z,x,y            
9  y,z,x            
10 -y,-z,x          
11 z,-x,-y          
12 -y,z,-x          
13 -z,-x,y          
14 -z,x,-y          
15 y,-z,-x          
16 x,-y,-z          
17 -x,y,-z          
18 -x,-y,z          
19 y,x,-z           
20 -y,-x,-z         
21 z,-y,x           
22 -z,-y,-x         
23 -x,z,y           
24 -x,-z,-y         
25 x,y+1/2,z+1/2    
26 x,-z+1/2,y+1/2   
27 x,z+1/2,-y+1/2   
28 z,y+1/2,-x+1/2   
29 -z,y+1/2,x+1/2   
30 -y,x+1/2,z+1/2   
31 y,-x+1/2,z+1/2   
32 z,x+1/2,y+1/2    
33 y,z+1/2,x+1/2    
34 -y,-z+1/2,x+1/2  
35 z,-x+1/2,-y+1/2  
36 -y,z+1/2,-x+1/2  
37 -z,-x+1/2,y+1/2  
38 -z,x+1/2,-y+1/2  
39 y,-z+1/2,-x+1/2  
40 x,-y+1/2,-z+1/2  
41 -x,y+1/2,-z+1/2  
42 -x,-y+1/2,z+1/2  
43 y,x+1/2,-z+1/2   
44 -y,-x+1/2,-z+1/2 
45 z,-y+1/2,x+1/2   
46 -z,-y+1/2,-x+1/2 
47 -x,z+1/2,y+1/2   
48 -x,-z+1/2,-y+1/2 
49 x+1/2,y,z+1/2    
50 x+1/2,-z,y+1/2   
51 x+1/2,z,-y+1/2   
52 z+1/2,y,-x+1/2   
53 -z+1/2,y,x+1/2   
54 -y+1/2,x,z+1/2   
55 y+1/2,-x,z+1/2   
56 z+1/2,x,y+1/2    
57 y+1/2,z,x+1/2    
58 -y+1/2,-z,x+1/2  
59 z+1/2,-x,-y+1/2  
60 -y+1/2,z,-x+1/2  
61 -z+1/2,-x,y+1/2  
62 -z+1/2,x,-y+1/2  
63 y+1/2,-z,-x+1/2  
64 x+1/2,-y,-z+1/2  
65 -x+1/2,y,-z+1/2  
66 -x+1/2,-y,z+1/2  
67 y+1/2,x,-z+1/2   
68 -y+1/2,-x,-z+1/2 
69 z+1/2,-y,x+1/2   
70 -z+1/2,-y,-x+1/2 
71 -x+1/2,z,y+1/2   
72 -x+1/2,-z,-y+1/2 
73 x+1/2,y+1/2,z    
74 x+1/2,-z+1/2,y   
75 x+1/2,z+1/2,-y   
76 z+1/2,y+1/2,-x   
77 -z+1/2,y+1/2,x   
78 -y+1/2,x+1/2,z   
79 y+1/2,-x+1/2,z   
80 z+1/2,x+1/2,y    
81 y+1/2,z+1/2,x    
82 -y+1/2,-z+1/2,x  
83 z+1/2,-x+1/2,-y  
84 -y+1/2,z+1/2,-x  
85 -z+1/2,-x+1/2,y  
86 -z+1/2,x+1/2,-y  
87 y+1/2,-z+1/2,-x  
88 x+1/2,-y+1/2,-z  
89 -x+1/2,y+1/2,-z  
90 -x+1/2,-y+1/2,z  
91 y+1/2,x+1/2,-z   
92 -y+1/2,-x+1/2,-z 
93 z+1/2,-y+1/2,x   
94 -z+1/2,-y+1/2,-x 
95 -x+1/2,z+1/2,y   
96 -x+1/2,-z+1/2,-y 
# 
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 43.89212682   -22.6520949459 -95.6484106541 2.36957607872 ? 0.351793807968  ? -0.266927277825 ? 
2.30188210452 ? 0.110582931029   ? 2.19114851685 ? 2.34128335202 ? 2.58205149317   ? -0.386688247821 ? 2.73178337782 ? 
-0.634293515938 ? 0.98439654628 ? 0.106512665429  ? 0.153448104844  ? 0.186048079939  ? -0.196535084952 ? -0.134525256361 ? 
-0.0417167646424 ? -0.608740784545 ? 0.0599801399888 ? 0.0456585401237 ? 
2 'X-RAY DIFFRACTION' ? refined 49.5625798515 -12.2245040912 -90.2254055106 2.59042454804 ? 0.0276919740742 ? 0.215945620527  ? 
1.84145789993 ? -0.109599266366  ? 3.05573445994 ? 4.91193549496 ? -4.47439309647  ? 3.03557434097   ? 4.42905042918 ? 
-1.58705526747  ? 2.97053768576 ? 0.100026295726  ? 0.761065895869  ? 2.07501757393   ? 0.468809363876  ? 0.526484395012  ? 
-0.825324398069  ? -1.9695263342   ? 0.188222018194  ? -0.529076392215 ? 
3 'X-RAY DIFFRACTION' ? refined 56.3777108445 -27.2541129046 -75.3878091925 1.99314136372 ? 0.106383185036  ? 0.133182042922  ? 
2.09394230536 ? -0.0848415261251 ? 2.25804052469 ? 2.91498134815 ? -0.369099879876 ? 2.06538664371   ? 4.42256059023 ? 
-0.193934317687 ? 4.25132024148 ? -0.102979139477 ? -0.254958924668 ? 0.0143421304425 ? 0.437563917966  ? 0.243681879592  ? 
0.185542938599   ? -0.279735994011 ? -0.502800743553 ? -0.211794957236 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 6   ? A 132 A 137 ? ? 
;chain 'A' and (resid 6 through 137 )
;
2 'X-RAY DIFFRACTION' 2 A 133 A 138 ? A 196 A 201 ? ? 
;chain 'A' and (resid 138 through 201 )
;
3 'X-RAY DIFFRACTION' 3 A 197 A 202 ? A 367 A 372 ? ? 
;chain 'A' and (resid 202 through 372 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS -5 ? A HIS 1  
2  1 Y 1 A HIS -4 ? A HIS 2  
3  1 Y 1 A HIS -3 ? A HIS 3  
4  1 Y 1 A HIS -2 ? A HIS 4  
5  1 Y 1 A HIS -1 ? A HIS 5  
6  1 Y 1 A HIS 0  ? A HIS 6  
7  1 Y 1 A HIS 1  ? A HIS 7  
8  1 Y 1 A HIS 2  ? A HIS 8  
9  1 Y 1 A GLY 3  ? A GLY 9  
10 1 Y 1 A SER 4  ? A SER 10 
11 1 Y 1 A GLY 5  ? A GLY 11 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
ILE N    N N N 172 
ILE CA   C N S 173 
ILE C    C N N 174 
ILE O    O N N 175 
ILE CB   C N S 176 
ILE CG1  C N N 177 
ILE CG2  C N N 178 
ILE CD1  C N N 179 
ILE OXT  O N N 180 
ILE H    H N N 181 
ILE H2   H N N 182 
ILE HA   H N N 183 
ILE HB   H N N 184 
ILE HG12 H N N 185 
ILE HG13 H N N 186 
ILE HG21 H N N 187 
ILE HG22 H N N 188 
ILE HG23 H N N 189 
ILE HD11 H N N 190 
ILE HD12 H N N 191 
ILE HD13 H N N 192 
ILE HXT  H N N 193 
LEU N    N N N 194 
LEU CA   C N S 195 
LEU C    C N N 196 
LEU O    O N N 197 
LEU CB   C N N 198 
LEU CG   C N N 199 
LEU CD1  C N N 200 
LEU CD2  C N N 201 
LEU OXT  O N N 202 
LEU H    H N N 203 
LEU H2   H N N 204 
LEU HA   H N N 205 
LEU HB2  H N N 206 
LEU HB3  H N N 207 
LEU HG   H N N 208 
LEU HD11 H N N 209 
LEU HD12 H N N 210 
LEU HD13 H N N 211 
LEU HD21 H N N 212 
LEU HD22 H N N 213 
LEU HD23 H N N 214 
LEU HXT  H N N 215 
LYS N    N N N 216 
LYS CA   C N S 217 
LYS C    C N N 218 
LYS O    O N N 219 
LYS CB   C N N 220 
LYS CG   C N N 221 
LYS CD   C N N 222 
LYS CE   C N N 223 
LYS NZ   N N N 224 
LYS OXT  O N N 225 
LYS H    H N N 226 
LYS H2   H N N 227 
LYS HA   H N N 228 
LYS HB2  H N N 229 
LYS HB3  H N N 230 
LYS HG2  H N N 231 
LYS HG3  H N N 232 
LYS HD2  H N N 233 
LYS HD3  H N N 234 
LYS HE2  H N N 235 
LYS HE3  H N N 236 
LYS HZ1  H N N 237 
LYS HZ2  H N N 238 
LYS HZ3  H N N 239 
LYS HXT  H N N 240 
MET N    N N N 241 
MET CA   C N S 242 
MET C    C N N 243 
MET O    O N N 244 
MET CB   C N N 245 
MET CG   C N N 246 
MET SD   S N N 247 
MET CE   C N N 248 
MET OXT  O N N 249 
MET H    H N N 250 
MET H2   H N N 251 
MET HA   H N N 252 
MET HB2  H N N 253 
MET HB3  H N N 254 
MET HG2  H N N 255 
MET HG3  H N N 256 
MET HE1  H N N 257 
MET HE2  H N N 258 
MET HE3  H N N 259 
MET HXT  H N N 260 
PHE N    N N N 261 
PHE CA   C N S 262 
PHE C    C N N 263 
PHE O    O N N 264 
PHE CB   C N N 265 
PHE CG   C Y N 266 
PHE CD1  C Y N 267 
PHE CD2  C Y N 268 
PHE CE1  C Y N 269 
PHE CE2  C Y N 270 
PHE CZ   C Y N 271 
PHE OXT  O N N 272 
PHE H    H N N 273 
PHE H2   H N N 274 
PHE HA   H N N 275 
PHE HB2  H N N 276 
PHE HB3  H N N 277 
PHE HD1  H N N 278 
PHE HD2  H N N 279 
PHE HE1  H N N 280 
PHE HE2  H N N 281 
PHE HZ   H N N 282 
PHE HXT  H N N 283 
PRO N    N N N 284 
PRO CA   C N S 285 
PRO C    C N N 286 
PRO O    O N N 287 
PRO CB   C N N 288 
PRO CG   C N N 289 
PRO CD   C N N 290 
PRO OXT  O N N 291 
PRO H    H N N 292 
PRO HA   H N N 293 
PRO HB2  H N N 294 
PRO HB3  H N N 295 
PRO HG2  H N N 296 
PRO HG3  H N N 297 
PRO HD2  H N N 298 
PRO HD3  H N N 299 
PRO HXT  H N N 300 
SER N    N N N 301 
SER CA   C N S 302 
SER C    C N N 303 
SER O    O N N 304 
SER CB   C N N 305 
SER OG   O N N 306 
SER OXT  O N N 307 
SER H    H N N 308 
SER H2   H N N 309 
SER HA   H N N 310 
SER HB2  H N N 311 
SER HB3  H N N 312 
SER HG   H N N 313 
SER HXT  H N N 314 
THR N    N N N 315 
THR CA   C N S 316 
THR C    C N N 317 
THR O    O N N 318 
THR CB   C N R 319 
THR OG1  O N N 320 
THR CG2  C N N 321 
THR OXT  O N N 322 
THR H    H N N 323 
THR H2   H N N 324 
THR HA   H N N 325 
THR HB   H N N 326 
THR HG1  H N N 327 
THR HG21 H N N 328 
THR HG22 H N N 329 
THR HG23 H N N 330 
THR HXT  H N N 331 
TRP N    N N N 332 
TRP CA   C N S 333 
TRP C    C N N 334 
TRP O    O N N 335 
TRP CB   C N N 336 
TRP CG   C Y N 337 
TRP CD1  C Y N 338 
TRP CD2  C Y N 339 
TRP NE1  N Y N 340 
TRP CE2  C Y N 341 
TRP CE3  C Y N 342 
TRP CZ2  C Y N 343 
TRP CZ3  C Y N 344 
TRP CH2  C Y N 345 
TRP OXT  O N N 346 
TRP H    H N N 347 
TRP H2   H N N 348 
TRP HA   H N N 349 
TRP HB2  H N N 350 
TRP HB3  H N N 351 
TRP HD1  H N N 352 
TRP HE1  H N N 353 
TRP HE3  H N N 354 
TRP HZ2  H N N 355 
TRP HZ3  H N N 356 
TRP HH2  H N N 357 
TRP HXT  H N N 358 
TYR N    N N N 359 
TYR CA   C N S 360 
TYR C    C N N 361 
TYR O    O N N 362 
TYR CB   C N N 363 
TYR CG   C Y N 364 
TYR CD1  C Y N 365 
TYR CD2  C Y N 366 
TYR CE1  C Y N 367 
TYR CE2  C Y N 368 
TYR CZ   C Y N 369 
TYR OH   O N N 370 
TYR OXT  O N N 371 
TYR H    H N N 372 
TYR H2   H N N 373 
TYR HA   H N N 374 
TYR HB2  H N N 375 
TYR HB3  H N N 376 
TYR HD1  H N N 377 
TYR HD2  H N N 378 
TYR HE1  H N N 379 
TYR HE2  H N N 380 
TYR HH   H N N 381 
TYR HXT  H N N 382 
VAL N    N N N 383 
VAL CA   C N S 384 
VAL C    C N N 385 
VAL O    O N N 386 
VAL CB   C N N 387 
VAL CG1  C N N 388 
VAL CG2  C N N 389 
VAL OXT  O N N 390 
VAL H    H N N 391 
VAL H2   H N N 392 
VAL HA   H N N 393 
VAL HB   H N N 394 
VAL HG11 H N N 395 
VAL HG12 H N N 396 
VAL HG13 H N N 397 
VAL HG21 H N N 398 
VAL HG22 H N N 399 
VAL HG23 H N N 400 
VAL HXT  H N N 401 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
ILE N   CA   sing N N 163 
ILE N   H    sing N N 164 
ILE N   H2   sing N N 165 
ILE CA  C    sing N N 166 
ILE CA  CB   sing N N 167 
ILE CA  HA   sing N N 168 
ILE C   O    doub N N 169 
ILE C   OXT  sing N N 170 
ILE CB  CG1  sing N N 171 
ILE CB  CG2  sing N N 172 
ILE CB  HB   sing N N 173 
ILE CG1 CD1  sing N N 174 
ILE CG1 HG12 sing N N 175 
ILE CG1 HG13 sing N N 176 
ILE CG2 HG21 sing N N 177 
ILE CG2 HG22 sing N N 178 
ILE CG2 HG23 sing N N 179 
ILE CD1 HD11 sing N N 180 
ILE CD1 HD12 sing N N 181 
ILE CD1 HD13 sing N N 182 
ILE OXT HXT  sing N N 183 
LEU N   CA   sing N N 184 
LEU N   H    sing N N 185 
LEU N   H2   sing N N 186 
LEU CA  C    sing N N 187 
LEU CA  CB   sing N N 188 
LEU CA  HA   sing N N 189 
LEU C   O    doub N N 190 
LEU C   OXT  sing N N 191 
LEU CB  CG   sing N N 192 
LEU CB  HB2  sing N N 193 
LEU CB  HB3  sing N N 194 
LEU CG  CD1  sing N N 195 
LEU CG  CD2  sing N N 196 
LEU CG  HG   sing N N 197 
LEU CD1 HD11 sing N N 198 
LEU CD1 HD12 sing N N 199 
LEU CD1 HD13 sing N N 200 
LEU CD2 HD21 sing N N 201 
LEU CD2 HD22 sing N N 202 
LEU CD2 HD23 sing N N 203 
LEU OXT HXT  sing N N 204 
LYS N   CA   sing N N 205 
LYS N   H    sing N N 206 
LYS N   H2   sing N N 207 
LYS CA  C    sing N N 208 
LYS CA  CB   sing N N 209 
LYS CA  HA   sing N N 210 
LYS C   O    doub N N 211 
LYS C   OXT  sing N N 212 
LYS CB  CG   sing N N 213 
LYS CB  HB2  sing N N 214 
LYS CB  HB3  sing N N 215 
LYS CG  CD   sing N N 216 
LYS CG  HG2  sing N N 217 
LYS CG  HG3  sing N N 218 
LYS CD  CE   sing N N 219 
LYS CD  HD2  sing N N 220 
LYS CD  HD3  sing N N 221 
LYS CE  NZ   sing N N 222 
LYS CE  HE2  sing N N 223 
LYS CE  HE3  sing N N 224 
LYS NZ  HZ1  sing N N 225 
LYS NZ  HZ2  sing N N 226 
LYS NZ  HZ3  sing N N 227 
LYS OXT HXT  sing N N 228 
MET N   CA   sing N N 229 
MET N   H    sing N N 230 
MET N   H2   sing N N 231 
MET CA  C    sing N N 232 
MET CA  CB   sing N N 233 
MET CA  HA   sing N N 234 
MET C   O    doub N N 235 
MET C   OXT  sing N N 236 
MET CB  CG   sing N N 237 
MET CB  HB2  sing N N 238 
MET CB  HB3  sing N N 239 
MET CG  SD   sing N N 240 
MET CG  HG2  sing N N 241 
MET CG  HG3  sing N N 242 
MET SD  CE   sing N N 243 
MET CE  HE1  sing N N 244 
MET CE  HE2  sing N N 245 
MET CE  HE3  sing N N 246 
MET OXT HXT  sing N N 247 
PHE N   CA   sing N N 248 
PHE N   H    sing N N 249 
PHE N   H2   sing N N 250 
PHE CA  C    sing N N 251 
PHE CA  CB   sing N N 252 
PHE CA  HA   sing N N 253 
PHE C   O    doub N N 254 
PHE C   OXT  sing N N 255 
PHE CB  CG   sing N N 256 
PHE CB  HB2  sing N N 257 
PHE CB  HB3  sing N N 258 
PHE CG  CD1  doub Y N 259 
PHE CG  CD2  sing Y N 260 
PHE CD1 CE1  sing Y N 261 
PHE CD1 HD1  sing N N 262 
PHE CD2 CE2  doub Y N 263 
PHE CD2 HD2  sing N N 264 
PHE CE1 CZ   doub Y N 265 
PHE CE1 HE1  sing N N 266 
PHE CE2 CZ   sing Y N 267 
PHE CE2 HE2  sing N N 268 
PHE CZ  HZ   sing N N 269 
PHE OXT HXT  sing N N 270 
PRO N   CA   sing N N 271 
PRO N   CD   sing N N 272 
PRO N   H    sing N N 273 
PRO CA  C    sing N N 274 
PRO CA  CB   sing N N 275 
PRO CA  HA   sing N N 276 
PRO C   O    doub N N 277 
PRO C   OXT  sing N N 278 
PRO CB  CG   sing N N 279 
PRO CB  HB2  sing N N 280 
PRO CB  HB3  sing N N 281 
PRO CG  CD   sing N N 282 
PRO CG  HG2  sing N N 283 
PRO CG  HG3  sing N N 284 
PRO CD  HD2  sing N N 285 
PRO CD  HD3  sing N N 286 
PRO OXT HXT  sing N N 287 
SER N   CA   sing N N 288 
SER N   H    sing N N 289 
SER N   H2   sing N N 290 
SER CA  C    sing N N 291 
SER CA  CB   sing N N 292 
SER CA  HA   sing N N 293 
SER C   O    doub N N 294 
SER C   OXT  sing N N 295 
SER CB  OG   sing N N 296 
SER CB  HB2  sing N N 297 
SER CB  HB3  sing N N 298 
SER OG  HG   sing N N 299 
SER OXT HXT  sing N N 300 
THR N   CA   sing N N 301 
THR N   H    sing N N 302 
THR N   H2   sing N N 303 
THR CA  C    sing N N 304 
THR CA  CB   sing N N 305 
THR CA  HA   sing N N 306 
THR C   O    doub N N 307 
THR C   OXT  sing N N 308 
THR CB  OG1  sing N N 309 
THR CB  CG2  sing N N 310 
THR CB  HB   sing N N 311 
THR OG1 HG1  sing N N 312 
THR CG2 HG21 sing N N 313 
THR CG2 HG22 sing N N 314 
THR CG2 HG23 sing N N 315 
THR OXT HXT  sing N N 316 
TRP N   CA   sing N N 317 
TRP N   H    sing N N 318 
TRP N   H2   sing N N 319 
TRP CA  C    sing N N 320 
TRP CA  CB   sing N N 321 
TRP CA  HA   sing N N 322 
TRP C   O    doub N N 323 
TRP C   OXT  sing N N 324 
TRP CB  CG   sing N N 325 
TRP CB  HB2  sing N N 326 
TRP CB  HB3  sing N N 327 
TRP CG  CD1  doub Y N 328 
TRP CG  CD2  sing Y N 329 
TRP CD1 NE1  sing Y N 330 
TRP CD1 HD1  sing N N 331 
TRP CD2 CE2  doub Y N 332 
TRP CD2 CE3  sing Y N 333 
TRP NE1 CE2  sing Y N 334 
TRP NE1 HE1  sing N N 335 
TRP CE2 CZ2  sing Y N 336 
TRP CE3 CZ3  doub Y N 337 
TRP CE3 HE3  sing N N 338 
TRP CZ2 CH2  doub Y N 339 
TRP CZ2 HZ2  sing N N 340 
TRP CZ3 CH2  sing Y N 341 
TRP CZ3 HZ3  sing N N 342 
TRP CH2 HH2  sing N N 343 
TRP OXT HXT  sing N N 344 
TYR N   CA   sing N N 345 
TYR N   H    sing N N 346 
TYR N   H2   sing N N 347 
TYR CA  C    sing N N 348 
TYR CA  CB   sing N N 349 
TYR CA  HA   sing N N 350 
TYR C   O    doub N N 351 
TYR C   OXT  sing N N 352 
TYR CB  CG   sing N N 353 
TYR CB  HB2  sing N N 354 
TYR CB  HB3  sing N N 355 
TYR CG  CD1  doub Y N 356 
TYR CG  CD2  sing Y N 357 
TYR CD1 CE1  sing Y N 358 
TYR CD1 HD1  sing N N 359 
TYR CD2 CE2  doub Y N 360 
TYR CD2 HD2  sing N N 361 
TYR CE1 CZ   doub Y N 362 
TYR CE1 HE1  sing N N 363 
TYR CE2 CZ   sing Y N 364 
TYR CE2 HE2  sing N N 365 
TYR CZ  OH   sing N N 366 
TYR OH  HH   sing N N 367 
TYR OXT HXT  sing N N 368 
VAL N   CA   sing N N 369 
VAL N   H    sing N N 370 
VAL N   H2   sing N N 371 
VAL CA  C    sing N N 372 
VAL CA  CB   sing N N 373 
VAL CA  HA   sing N N 374 
VAL C   O    doub N N 375 
VAL C   OXT  sing N N 376 
VAL CB  CG1  sing N N 377 
VAL CB  CG2  sing N N 378 
VAL CB  HB   sing N N 379 
VAL CG1 HG11 sing N N 380 
VAL CG1 HG12 sing N N 381 
VAL CG1 HG13 sing N N 382 
VAL CG2 HG21 sing N N 383 
VAL CG2 HG22 sing N N 384 
VAL CG2 HG23 sing N N 385 
VAL OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-22-CE11-0003 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'F 4 3 2' 
_space_group.name_Hall        'F 4 2 3' 
_space_group.IT_number        209 
_space_group.crystal_system   cubic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FJ0 
_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]   0.003558 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.003558 
_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]   0.003558 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 12  ? 31.28081 -2.02959  -76.06012  1.000 238.43746 ? 6   SER A N   1 
ATOM   2    C CA  . SER A 1 12  ? 31.98012 -3.01013  -75.23756  1.000 259.66322 ? 6   SER A CA  1 
ATOM   3    C C   . SER A 1 12  ? 32.54487 -4.14159  -76.09271  1.000 285.23445 ? 6   SER A C   1 
ATOM   4    O O   . SER A 1 12  ? 32.02452 -4.43707  -77.16868  1.000 285.86446 ? 6   SER A O   1 
ATOM   5    C CB  . SER A 1 12  ? 31.04510 -3.57386  -74.16457  1.000 237.66603 ? 6   SER A CB  1 
ATOM   6    O OG  . SER A 1 12  ? 29.90968 -4.19037  -74.74676  1.000 264.40177 ? 6   SER A OG  1 
ATOM   7    N N   . VAL A 1 13  ? 33.61231 -4.76950  -75.60821  1.000 292.96766 ? 7   VAL A N   1 
ATOM   8    C CA  . VAL A 1 13  ? 34.25846 -5.87038  -76.31976  1.000 282.60731 ? 7   VAL A CA  1 
ATOM   9    C C   . VAL A 1 13  ? 33.86563 -7.18959  -75.66322  1.000 289.72668 ? 7   VAL A C   1 
ATOM   10   O O   . VAL A 1 13  ? 33.73244 -7.25411  -74.43222  1.000 299.43364 ? 7   VAL A O   1 
ATOM   11   C CB  . VAL A 1 13  ? 35.78578 -5.69439  -76.35262  1.000 267.32266 ? 7   VAL A CB  1 
ATOM   12   C CG1 . VAL A 1 13  ? 36.16205 -4.50028  -77.21604  1.000 268.90923 ? 7   VAL A CG1 1 
ATOM   13   C CG2 . VAL A 1 13  ? 36.33819 -5.52833  -74.94373  1.000 254.22929 ? 7   VAL A CG2 1 
ATOM   14   N N   . PRO A 1 14  ? 33.66127 -8.25551  -76.43220  1.000 290.71106 ? 8   PRO A N   1 
ATOM   15   C CA  . PRO A 1 14  ? 33.27229 -9.53519  -75.83421  1.000 298.90429 ? 8   PRO A CA  1 
ATOM   16   C C   . PRO A 1 14  ? 34.45578 -10.26552 -75.22020  1.000 295.61420 ? 8   PRO A C   1 
ATOM   17   O O   . PRO A 1 14  ? 35.60011 -10.13921 -75.66235  1.000 289.00877 ? 8   PRO A O   1 
ATOM   18   C CB  . PRO A 1 14  ? 32.70245 -10.31614 -77.02405  1.000 280.55415 ? 8   PRO A CB  1 
ATOM   19   C CG  . PRO A 1 14  ? 33.44834 -9.77791  -78.19672  1.000 273.61853 ? 8   PRO A CG  1 
ATOM   20   C CD  . PRO A 1 14  ? 33.68780 -8.31680  -77.90449  1.000 283.63262 ? 8   PRO A CD  1 
ATOM   21   N N   . ALA A 1 15  ? 34.15774 -11.04321 -74.18176  1.000 303.09631 ? 9   ALA A N   1 
ATOM   22   C CA  . ALA A 1 15  ? 35.18528 -11.83037 -73.51416  1.000 280.00531 ? 9   ALA A CA  1 
ATOM   23   C C   . ALA A 1 15  ? 35.61231 -12.99461 -74.39870  1.000 262.42382 ? 9   ALA A C   1 
ATOM   24   O O   . ALA A 1 15  ? 34.77176 -13.72254 -74.93590  1.000 260.39881 ? 9   ALA A O   1 
ATOM   25   C CB  . ALA A 1 15  ? 34.67276 -12.34367 -72.16989  1.000 265.46496 ? 9   ALA A CB  1 
ATOM   26   N N   . GLY A 1 16  ? 36.92446 -13.17069 -74.54838  1.000 261.91310 ? 10  GLY A N   1 
ATOM   27   C CA  . GLY A 1 16  ? 37.46450 -14.20166 -75.40556  1.000 248.17307 ? 10  GLY A CA  1 
ATOM   28   C C   . GLY A 1 16  ? 37.54614 -13.84101 -76.87126  1.000 254.53805 ? 10  GLY A C   1 
ATOM   29   O O   . GLY A 1 16  ? 38.09779 -14.62726 -77.65055  1.000 252.16468 ? 10  GLY A O   1 
ATOM   30   N N   . ALA A 1 17  ? 37.01280 -12.68379 -77.27231  1.000 260.60995 ? 11  ALA A N   1 
ATOM   31   C CA  . ALA A 1 17  ? 37.05838 -12.21267 -78.65935  1.000 256.87874 ? 11  ALA A CA  1 
ATOM   32   C C   . ALA A 1 17  ? 36.35697 -13.18258 -79.60924  1.000 265.13064 ? 11  ALA A C   1 
ATOM   33   O O   . ALA A 1 17  ? 36.82905 -13.44040 -80.71886  1.000 260.66886 ? 11  ALA A O   1 
ATOM   34   C CB  . ALA A 1 17  ? 38.49731 -11.95036 -79.11237  1.000 239.01354 ? 11  ALA A CB  1 
ATOM   35   N N   . LYS A 1 18  ? 35.21722 -13.72192 -79.16636  1.000 272.18965 ? 12  LYS A N   1 
ATOM   36   C CA  . LYS A 1 18  ? 34.37024 -14.58962 -79.99099  1.000 278.51049 ? 12  LYS A CA  1 
ATOM   37   C C   . LYS A 1 18  ? 35.13680 -15.81132 -80.49663  1.000 276.67234 ? 12  LYS A C   1 
ATOM   38   O O   . LYS A 1 18  ? 34.91494 -16.28804 -81.61137  1.000 275.15165 ? 12  LYS A O   1 
ATOM   39   C CB  . LYS A 1 18  ? 33.75872 -13.81152 -81.16035  1.000 278.47682 ? 12  LYS A CB  1 
ATOM   40   C CG  . LYS A 1 18  ? 32.85916 -12.65496 -80.74677  1.000 275.68212 ? 12  LYS A CG  1 
ATOM   41   C CD  . LYS A 1 18  ? 31.49874 -13.14323 -80.27336  1.000 269.08892 ? 12  LYS A CD  1 
ATOM   42   C CE  . LYS A 1 18  ? 30.70210 -13.75607 -81.41578  1.000 258.22809 ? 12  LYS A CE  1 
ATOM   43   N NZ  . LYS A 1 18  ? 30.45140 -12.77623 -82.51028  1.000 252.39557 ? 12  LYS A NZ  1 
ATOM   44   N N   . CYS A 1 19  ? 36.03859 -16.32915 -79.66779  1.000 277.65534 ? 13  CYS A N   1 
ATOM   45   C CA  . CYS A 1 19  ? 36.91121 -17.43159 -80.04681  1.000 272.49571 ? 13  CYS A CA  1 
ATOM   46   C C   . CYS A 1 19  ? 36.34420 -18.76213 -79.56737  1.000 268.47097 ? 13  CYS A C   1 
ATOM   47   O O   . CYS A 1 19  ? 35.88199 -18.88047 -78.42867  1.000 262.59285 ? 13  CYS A O   1 
ATOM   48   C CB  . CYS A 1 19  ? 38.31655 -17.23185 -79.47507  1.000 270.17573 ? 13  CYS A CB  1 
ATOM   49   S SG  . CYS A 1 19  ? 39.25854 -15.88832 -80.23757  1.000 269.22222 ? 13  CYS A SG  1 
ATOM   50   N N   . ARG A 1 20  ? 36.38644 -19.76261 -80.44617  1.000 263.05610 ? 14  ARG A N   1 
ATOM   51   C CA  . ARG A 1 20  ? 35.97607 -21.11866 -80.11402  1.000 252.06045 ? 14  ARG A CA  1 
ATOM   52   C C   . ARG A 1 20  ? 36.98387 -22.09459 -80.70273  1.000 235.02103 ? 14  ARG A C   1 
ATOM   53   O O   . ARG A 1 20  ? 37.63360 -21.80535 -81.71057  1.000 226.32053 ? 14  ARG A O   1 
ATOM   54   C CB  . ARG A 1 20  ? 34.56261 -21.42949 -80.62739  1.000 256.89182 ? 14  ARG A CB  1 
ATOM   55   C CG  . ARG A 1 20  ? 34.39259 -21.29182 -82.13016  1.000 250.50227 ? 14  ARG A CG  1 
ATOM   56   C CD  . ARG A 1 20  ? 32.93449 -21.45720 -82.52216  1.000 244.05717 ? 14  ARG A CD  1 
ATOM   57   N NE  . ARG A 1 20  ? 32.40070 -22.74557 -82.09707  1.000 232.48635 ? 14  ARG A NE  1 
ATOM   58   C CZ  . ARG A 1 20  ? 31.12611 -23.09768 -82.19482  1.000 247.12678 ? 14  ARG A CZ  1 
ATOM   59   N NH1 . ARG A 1 20  ? 30.21727 -22.27380 -82.69067  1.000 255.32006 ? 14  ARG A NH1 1 
ATOM   60   N NH2 . ARG A 1 20  ? 30.75356 -24.30617 -81.78299  1.000 249.40713 ? 14  ARG A NH2 1 
ATOM   61   N N   . LEU A 1 21  ? 37.10973 -23.25383 -80.06277  1.000 230.41106 ? 15  LEU A N   1 
ATOM   62   C CA  . LEU A 1 21  ? 38.14985 -24.20134 -80.43810  1.000 226.13979 ? 15  LEU A CA  1 
ATOM   63   C C   . LEU A 1 21  ? 37.79801 -24.92294 -81.73251  1.000 224.96802 ? 15  LEU A C   1 
ATOM   64   O O   . LEU A 1 21  ? 36.63229 -25.22478 -82.00223  1.000 212.57608 ? 15  LEU A O   1 
ATOM   65   C CB  . LEU A 1 21  ? 38.37601 -25.21403 -79.31756  1.000 235.58064 ? 15  LEU A CB  1 
ATOM   66   C CG  . LEU A 1 21  ? 38.90391 -24.63932 -78.00287  1.000 238.74985 ? 15  LEU A CG  1 
ATOM   67   C CD1 . LEU A 1 21  ? 39.21814 -25.75925 -77.02855  1.000 275.13636 ? 15  LEU A CD1 1 
ATOM   68   C CD2 . LEU A 1 21  ? 40.13020 -23.77020 -78.24389  1.000 212.76131 ? 15  LEU A CD2 1 
ATOM   69   N N   . VAL A 1 22  ? 38.82371 -25.19327 -82.53698  1.000 235.26831 ? 16  VAL A N   1 
ATOM   70   C CA  . VAL A 1 22  ? 38.68872 -25.92338 -83.79284  1.000 234.83053 ? 16  VAL A CA  1 
ATOM   71   C C   . VAL A 1 22  ? 39.81587 -26.94330 -83.86748  1.000 241.85375 ? 16  VAL A C   1 
ATOM   72   O O   . VAL A 1 22  ? 40.97243 -26.61726 -83.58168  1.000 249.59339 ? 16  VAL A O   1 
ATOM   73   C CB  . VAL A 1 22  ? 38.72326 -24.98248 -85.01397  1.000 228.26830 ? 16  VAL A CB  1 
ATOM   74   C CG1 . VAL A 1 22  ? 38.78432 -25.78290 -86.30355  1.000 224.45193 ? 16  VAL A CG1 1 
ATOM   75   C CG2 . VAL A 1 22  ? 37.50799 -24.07143 -85.01528  1.000 224.08683 ? 16  VAL A CG2 1 
ATOM   76   N N   . GLU A 1 23  ? 39.48390 -28.17658 -84.24353  1.000 224.59841 ? 17  GLU A N   1 
ATOM   77   C CA  . GLU A 1 23  ? 40.47823 -29.23721 -84.29001  1.000 219.96837 ? 17  GLU A CA  1 
ATOM   78   C C   . GLU A 1 23  ? 40.06272 -30.28357 -85.31300  1.000 221.24819 ? 17  GLU A C   1 
ATOM   79   O O   . GLU A 1 23  ? 38.90127 -30.35686 -85.72322  1.000 211.30482 ? 17  GLU A O   1 
ATOM   80   C CB  . GLU A 1 23  ? 40.66823 -29.88220 -82.91235  1.000 224.20360 ? 17  GLU A CB  1 
ATOM   81   C CG  . GLU A 1 23  ? 39.38232 -30.40113 -82.29445  1.000 240.69768 ? 17  GLU A CG  1 
ATOM   82   C CD  . GLU A 1 23  ? 39.59506 -30.98625 -80.91372  1.000 251.58292 ? 17  GLU A CD  1 
ATOM   83   O OE1 . GLU A 1 23  ? 40.76469 -31.11411 -80.49427  1.000 224.24207 ? 17  GLU A OE1 1 
ATOM   84   O OE2 . GLU A 1 23  ? 38.59194 -31.31696 -80.24733  1.000 275.66378 ? 17  GLU A OE2 1 
ATOM   85   N N   . THR A 1 24  ? 41.03534 -31.09433 -85.72217  1.000 235.06199 ? 18  THR A N   1 
ATOM   86   C CA  . THR A 1 24  ? 40.81509 -32.20588 -86.63898  1.000 232.70821 ? 18  THR A CA  1 
ATOM   87   C C   . THR A 1 24  ? 40.88116 -33.50451 -85.84845  1.000 237.92453 ? 18  THR A C   1 
ATOM   88   O O   . THR A 1 24  ? 41.90403 -33.80210 -85.22184  1.000 216.09981 ? 18  THR A O   1 
ATOM   89   C CB  . THR A 1 24  ? 41.85157 -32.21746 -87.76275  1.000 229.35846 ? 18  THR A CB  1 
ATOM   90   O OG1 . THR A 1 24  ? 41.88204 -30.93757 -88.40428  1.000 221.89630 ? 18  THR A OG1 1 
ATOM   91   C CG2 . THR A 1 24  ? 41.50711 -33.28440 -88.79099  1.000 231.19780 ? 18  THR A CG2 1 
ATOM   92   N N   . LEU A 1 25  ? 39.79458 -34.26982 -85.87640  1.000 250.93077 ? 19  LEU A N   1 
ATOM   93   C CA  . LEU A 1 25  ? 39.71707 -35.55126 -85.17537  1.000 235.77811 ? 19  LEU A CA  1 
ATOM   94   C C   . LEU A 1 25  ? 39.41633 -36.64733 -86.18640  1.000 239.27970 ? 19  LEU A C   1 
ATOM   95   O O   . LEU A 1 25  ? 38.24253 -36.86943 -86.53472  1.000 258.53048 ? 19  LEU A O   1 
ATOM   96   C CB  . LEU A 1 25  ? 38.64826 -35.51273 -84.08483  1.000 239.82478 ? 19  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 25  ? 38.67769 -34.30093 -83.14886  1.000 249.07525 ? 19  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 25  ? 37.61501 -34.43233 -82.06942  1.000 254.65385 ? 19  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 25  ? 40.05624 -34.10943 -82.53092  1.000 230.33836 ? 19  LEU A CD2 1 
ATOM   100  N N   . PRO A 1 26  ? 40.43088 -37.34687 -86.69335  1.000 230.82795 ? 20  PRO A N   1 
ATOM   101  C CA  . PRO A 1 26  ? 40.18629 -38.38293 -87.70261  1.000 234.21570 ? 20  PRO A CA  1 
ATOM   102  C C   . PRO A 1 26  ? 39.33281 -39.51877 -87.15694  1.000 233.35440 ? 20  PRO A C   1 
ATOM   103  O O   . PRO A 1 26  ? 39.24964 -39.75217 -85.94886  1.000 222.68696 ? 20  PRO A O   1 
ATOM   104  C CB  . PRO A 1 26  ? 41.59609 -38.86910 -88.06255  1.000 214.79222 ? 20  PRO A CB  1 
ATOM   105  C CG  . PRO A 1 26  ? 42.49635 -37.73636 -87.68084  1.000 209.80139 ? 20  PRO A CG  1 
ATOM   106  C CD  . PRO A 1 26  ? 41.86781 -37.12181 -86.46693  1.000 213.37479 ? 20  PRO A CD  1 
ATOM   107  N N   . GLU A 1 27  ? 38.68735 -40.23324 -88.08319  1.000 235.91640 ? 21  GLU A N   1 
ATOM   108  C CA  . GLU A 1 27  ? 37.80804 -41.33168 -87.69627  1.000 241.90822 ? 21  GLU A CA  1 
ATOM   109  C C   . GLU A 1 27  ? 38.58908 -42.50050 -87.11240  1.000 232.67725 ? 21  GLU A C   1 
ATOM   110  O O   . GLU A 1 27  ? 38.08969 -43.19223 -86.21752  1.000 239.99352 ? 21  GLU A O   1 
ATOM   111  C CB  . GLU A 1 27  ? 36.98222 -41.79934 -88.89618  1.000 244.28518 ? 21  GLU A CB  1 
ATOM   112  C CG  . GLU A 1 27  ? 36.01761 -40.75884 -89.44882  1.000 254.75095 ? 21  GLU A CG  1 
ATOM   113  C CD  . GLU A 1 27  ? 36.69886 -39.73245 -90.33467  1.000 242.90163 ? 21  GLU A CD  1 
ATOM   114  O OE1 . GLU A 1 27  ? 37.89105 -39.91928 -90.65834  1.000 225.58779 ? 21  GLU A OE1 1 
ATOM   115  O OE2 . GLU A 1 27  ? 36.04117 -38.73816 -90.70668  1.000 246.22706 ? 21  GLU A OE2 1 
ATOM   116  N N   . ASN A 1 28  ? 39.80700 -42.73694 -87.60011  1.000 225.64728 ? 22  ASN A N   1 
ATOM   117  C CA  . ASN A 1 28  ? 40.63941 -43.81495 -87.08081  1.000 242.86050 ? 22  ASN A CA  1 
ATOM   118  C C   . ASN A 1 28  ? 41.20366 -43.51531 -85.69866  1.000 240.30283 ? 22  ASN A C   1 
ATOM   119  O O   . ASN A 1 28  ? 41.91878 -44.35937 -85.14704  1.000 256.28647 ? 22  ASN A O   1 
ATOM   120  C CB  . ASN A 1 28  ? 41.78025 -44.10857 -88.05761  1.000 241.79511 ? 22  ASN A CB  1 
ATOM   121  C CG  . ASN A 1 28  ? 42.59755 -42.87484 -88.38751  1.000 238.49134 ? 22  ASN A CG  1 
ATOM   122  O OD1 . ASN A 1 28  ? 42.25644 -42.11385 -89.29335  1.000 230.40338 ? 22  ASN A OD1 1 
ATOM   123  N ND2 . ASN A 1 28  ? 43.68539 -42.67197 -87.65358  1.000 257.39146 ? 22  ASN A ND2 1 
ATOM   124  N N   . MET A 1 29  ? 40.90450 -42.35059 -85.13041  1.000 227.68838 ? 23  MET A N   1 
ATOM   125  C CA  . MET A 1 29  ? 41.36429 -41.97336 -83.80488  1.000 217.94209 ? 23  MET A CA  1 
ATOM   126  C C   . MET A 1 29  ? 40.16872 -41.81578 -82.87370  1.000 207.09779 ? 23  MET A C   1 
ATOM   127  O O   . MET A 1 29  ? 39.04031 -41.57322 -83.31081  1.000 206.08644 ? 23  MET A O   1 
ATOM   128  C CB  . MET A 1 29  ? 42.18120 -40.67602 -83.85266  1.000 227.67463 ? 23  MET A CB  1 
ATOM   129  C CG  . MET A 1 29  ? 43.35401 -40.72429 -84.82210  1.000 240.47951 ? 23  MET A CG  1 
ATOM   130  S SD  . MET A 1 29  ? 44.30383 -39.19221 -84.86970  1.000 236.65972 ? 23  MET A SD  1 
ATOM   131  C CE  . MET A 1 29  ? 45.48936 -39.56705 -86.15943  1.000 199.12137 ? 23  MET A CE  1 
ATOM   132  N N   . ASP A 1 30  ? 40.43011 -41.95675 -81.57624  1.000 205.55409 ? 24  ASP A N   1 
ATOM   133  C CA  . ASP A 1 30  ? 39.38510 -41.95470 -80.56143  1.000 214.52149 ? 24  ASP A CA  1 
ATOM   134  C C   . ASP A 1 30  ? 39.06954 -40.56305 -80.02582  1.000 227.43578 ? 24  ASP A C   1 
ATOM   135  O O   . ASP A 1 30  ? 38.36160 -40.44780 -79.02002  1.000 226.78582 ? 24  ASP A O   1 
ATOM   136  C CB  . ASP A 1 30  ? 39.77856 -42.87524 -79.40266  1.000 216.28306 ? 24  ASP A CB  1 
ATOM   137  C CG  . ASP A 1 30  ? 41.09257 -42.47396 -78.75832  1.000 226.69224 ? 24  ASP A CG  1 
ATOM   138  O OD1 . ASP A 1 30  ? 41.11314 -41.47338 -78.01037  1.000 221.19025 ? 24  ASP A OD1 1 
ATOM   139  O OD2 . ASP A 1 30  ? 42.10686 -43.16095 -79.00012  1.000 241.50724 ? 24  ASP A OD2 1 
ATOM   140  N N   . PHE A 1 31  ? 39.57068 -39.51056 -80.66562  1.000 221.67822 ? 25  PHE A N   1 
ATOM   141  C CA  . PHE A 1 31  ? 39.33746 -38.15281 -80.19026  1.000 226.73179 ? 25  PHE A CA  1 
ATOM   142  C C   . PHE A 1 31  ? 37.92911 -37.71079 -80.56858  1.000 242.49057 ? 25  PHE A C   1 
ATOM   143  O O   . PHE A 1 31  ? 37.55484 -37.74789 -81.74584  1.000 243.66371 ? 25  PHE A O   1 
ATOM   144  C CB  . PHE A 1 31  ? 40.37771 -37.19890 -80.77012  1.000 229.67980 ? 25  PHE A CB  1 
ATOM   145  C CG  . PHE A 1 31  ? 41.79313 -37.60150 -80.48222  1.000 241.73409 ? 25  PHE A CG  1 
ATOM   146  C CD1 . PHE A 1 31  ? 42.34975 -37.38261 -79.23365  1.000 240.65575 ? 25  PHE A CD1 1 
ATOM   147  C CD2 . PHE A 1 31  ? 42.56875 -38.19657 -81.46122  1.000 251.01342 ? 25  PHE A CD2 1 
ATOM   148  C CE1 . PHE A 1 31  ? 43.65349 -37.75362 -78.96678  1.000 241.81277 ? 25  PHE A CE1 1 
ATOM   149  C CE2 . PHE A 1 31  ? 43.87235 -38.56985 -81.20139  1.000 248.57002 ? 25  PHE A CE2 1 
ATOM   150  C CZ  . PHE A 1 31  ? 44.41585 -38.34786 -79.95258  1.000 235.19188 ? 25  PHE A CZ  1 
ATOM   151  N N   . ARG A 1 32  ? 37.15117 -37.29441 -79.57131  1.000 246.70025 ? 26  ARG A N   1 
ATOM   152  C CA  . ARG A 1 32  ? 35.78565 -36.83241 -79.77228  1.000 263.70661 ? 26  ARG A CA  1 
ATOM   153  C C   . ARG A 1 32  ? 35.57920 -35.52269 -79.02579  1.000 257.63413 ? 26  ARG A C   1 
ATOM   154  O O   . ARG A 1 32  ? 36.09546 -35.34253 -77.91846  1.000 229.38271 ? 26  ARG A O   1 
ATOM   155  C CB  . ARG A 1 32  ? 34.76448 -37.87356 -79.29026  1.000 271.79543 ? 26  ARG A CB  1 
ATOM   156  C CG  . ARG A 1 32  ? 34.85366 -39.22687 -79.98506  1.000 269.04996 ? 26  ARG A CG  1 
ATOM   157  C CD  . ARG A 1 32  ? 34.54848 -39.11940 -81.47197  1.000 286.28614 ? 26  ARG A CD  1 
ATOM   158  N NE  . ARG A 1 32  ? 34.34082 -40.42768 -82.08264  1.000 288.50815 ? 26  ARG A NE  1 
ATOM   159  C CZ  . ARG A 1 32  ? 35.30707 -41.18493 -82.58417  1.000 253.21043 ? 26  ARG A CZ  1 
ATOM   160  N NH1 . ARG A 1 32  ? 36.57128 -40.79545 -82.56487  1.000 245.05748 ? 26  ARG A NH1 1 
ATOM   161  N NH2 . ARG A 1 32  ? 34.99709 -42.36325 -83.11784  1.000 235.58531 ? 26  ARG A NH2 1 
ATOM   162  N N   . SER A 1 33  ? 34.82210 -34.61245 -79.63566  1.000 264.21912 ? 27  SER A N   1 
ATOM   163  C CA  . SER A 1 33  ? 34.52224 -33.32844 -79.01661  1.000 260.08653 ? 27  SER A CA  1 
ATOM   164  C C   . SER A 1 33  ? 33.33783 -32.69705 -79.73207  1.000 257.08605 ? 27  SER A C   1 
ATOM   165  O O   . SER A 1 33  ? 33.00308 -33.06179 -80.86227  1.000 240.58317 ? 27  SER A O   1 
ATOM   166  C CB  . SER A 1 33  ? 35.73086 -32.38634 -79.05114  1.000 247.68563 ? 27  SER A CB  1 
ATOM   167  O OG  . SER A 1 33  ? 36.06743 -32.03803 -80.38267  1.000 237.04786 ? 27  SER A OG  1 
ATOM   168  N N   . ASP A 1 34  ? 32.70957 -31.73990 -79.05338  1.000 264.58284 ? 28  ASP A N   1 
ATOM   169  C CA  . ASP A 1 34  ? 31.59137 -30.98922 -79.60750  1.000 281.00359 ? 28  ASP A CA  1 
ATOM   170  C C   . ASP A 1 34  ? 32.02560 -29.69412 -80.27848  1.000 274.03069 ? 28  ASP A C   1 
ATOM   171  O O   . ASP A 1 34  ? 31.17008 -28.94790 -80.76613  1.000 297.23434 ? 28  ASP A O   1 
ATOM   172  C CB  . ASP A 1 34  ? 30.56935 -30.67607 -78.50993  1.000 296.30985 ? 28  ASP A CB  1 
ATOM   173  C CG  . ASP A 1 34  ? 30.04447 -31.92305 -77.83039  1.000 304.13968 ? 28  ASP A CG  1 
ATOM   174  O OD1 . ASP A 1 34  ? 29.98849 -32.98162 -78.49061  1.000 316.92107 ? 28  ASP A OD1 1 
ATOM   175  O OD2 . ASP A 1 34  ? 29.68812 -31.84454 -76.63588  1.000 310.55015 ? 28  ASP A OD2 1 
ATOM   176  N N   . HIS A 1 35  ? 33.32440 -29.41090 -80.31413  1.000 248.49645 ? 29  HIS A N   1 
ATOM   177  C CA  . HIS A 1 35  ? 33.80941 -28.17290 -80.89758  1.000 241.57409 ? 29  HIS A CA  1 
ATOM   178  C C   . HIS A 1 35  ? 33.69958 -28.21522 -82.41973  1.000 243.83090 ? 29  HIS A C   1 
ATOM   179  O O   . HIS A 1 35  ? 33.37960 -29.24147 -83.02711  1.000 237.92754 ? 29  HIS A O   1 
ATOM   180  C CB  . HIS A 1 35  ? 35.25615 -27.91657 -80.48026  1.000 227.12940 ? 29  HIS A CB  1 
ATOM   181  C CG  . HIS A 1 35  ? 35.42991 -27.70363 -79.00990  1.000 240.99791 ? 29  HIS A CG  1 
ATOM   182  N ND1 . HIS A 1 35  ? 36.32827 -28.42550 -78.25422  1.000 239.02387 ? 29  HIS A ND1 1 
ATOM   183  C CD2 . HIS A 1 35  ? 34.82153 -26.84751 -78.15552  1.000 261.23283 ? 29  HIS A CD2 1 
ATOM   184  C CE1 . HIS A 1 35  ? 36.26435 -28.02487 -76.99707  1.000 252.23758 ? 29  HIS A CE1 1 
ATOM   185  N NE2 . HIS A 1 35  ? 35.35811 -27.06783 -76.91038  1.000 286.58297 ? 29  HIS A NE2 1 
ATOM   186  N N   . LEU A 1 36  ? 33.97052 -27.06875 -83.03455  1.000 236.80758 ? 30  LEU A N   1 
ATOM   187  C CA  . LEU A 1 36  ? 33.97124 -26.97723 -84.48578  1.000 229.45568 ? 30  LEU A CA  1 
ATOM   188  C C   . LEU A 1 36  ? 35.14412 -27.76229 -85.05942  1.000 223.66785 ? 30  LEU A C   1 
ATOM   189  O O   . LEU A 1 36  ? 36.23309 -27.79312 -84.48070  1.000 212.65027 ? 30  LEU A O   1 
ATOM   190  C CB  . LEU A 1 36  ? 34.05101 -25.51423 -84.91802  1.000 213.49174 ? 30  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 36  ? 33.76952 -25.20293 -86.38661  1.000 221.96353 ? 30  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 36  ? 32.30311 -25.44302 -86.70528  1.000 236.63776 ? 30  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 36  ? 34.16816 -23.77340 -86.71058  1.000 229.15042 ? 30  LEU A CD2 1 
ATOM   194  N N   . THR A 1 37  ? 34.91687 -28.40894 -86.19677  1.000 228.62072 ? 31  THR A N   1 
ATOM   195  C CA  . THR A 1 37  ? 35.97301 -29.15962 -86.85651  1.000 230.68252 ? 31  THR A CA  1 
ATOM   196  C C   . THR A 1 37  ? 36.69043 -28.27914 -87.87438  1.000 213.48162 ? 31  THR A C   1 
ATOM   197  O O   . THR A 1 37  ? 36.18466 -27.23810 -88.30019  1.000 211.49926 ? 31  THR A O   1 
ATOM   198  C CB  . THR A 1 37  ? 35.41461 -30.40679 -87.54549  1.000 232.31939 ? 31  THR A CB  1 
ATOM   199  O OG1 . THR A 1 37  ? 34.71971 -30.02779 -88.73946  1.000 210.21053 ? 31  THR A OG1 1 
ATOM   200  C CG2 . THR A 1 37  ? 34.45592 -31.14251 -86.62029  1.000 215.03007 ? 31  THR A CG2 1 
ATOM   201  N N   . THR A 1 38  ? 37.89301 -28.71275 -88.25845  1.000 209.11689 ? 32  THR A N   1 
ATOM   202  C CA  . THR A 1 38  ? 38.66842 -27.95734 -89.23689  1.000 202.84936 ? 32  THR A CA  1 
ATOM   203  C C   . THR A 1 38  ? 37.97736 -27.94566 -90.59405  1.000 209.27503 ? 32  THR A C   1 
ATOM   204  O O   . THR A 1 38  ? 38.02908 -26.94278 -91.31601  1.000 218.23427 ? 32  THR A O   1 
ATOM   205  C CB  . THR A 1 38  ? 40.07613 -28.53970 -89.35497  1.000 209.34499 ? 32  THR A CB  1 
ATOM   206  O OG1 . THR A 1 38  ? 40.66863 -28.62628 -88.05280  1.000 206.15938 ? 32  THR A OG1 1 
ATOM   207  C CG2 . THR A 1 38  ? 40.94708 -27.66142 -90.23861  1.000 216.44954 ? 32  THR A CG2 1 
ATOM   208  N N   . PHE A 1 39  ? 37.31928 -29.04865 -90.95553  1.000 198.79065 ? 33  PHE A N   1 
ATOM   209  C CA  . PHE A 1 39  ? 36.57873 -29.08036 -92.21115  1.000 214.99548 ? 33  PHE A CA  1 
ATOM   210  C C   . PHE A 1 39  ? 35.36481 -28.16049 -92.15752  1.000 218.20490 ? 33  PHE A C   1 
ATOM   211  O O   . PHE A 1 39  ? 35.07067 -27.45526 -93.12983  1.000 221.54074 ? 33  PHE A O   1 
ATOM   212  C CB  . PHE A 1 39  ? 36.15993 -30.51234 -92.53720  1.000 225.17440 ? 33  PHE A CB  1 
ATOM   213  C CG  . PHE A 1 39  ? 35.36194 -30.63315 -93.80044  1.000 235.70922 ? 33  PHE A CG  1 
ATOM   214  C CD1 . PHE A 1 39  ? 35.97906 -30.53579 -95.03597  1.000 220.95179 ? 33  PHE A CD1 1 
ATOM   215  C CD2 . PHE A 1 39  ? 33.99456 -30.84387 -93.75375  1.000 250.08949 ? 33  PHE A CD2 1 
ATOM   216  C CE1 . PHE A 1 39  ? 35.24732 -30.64579 -96.20194  1.000 237.68190 ? 33  PHE A CE1 1 
ATOM   217  C CE2 . PHE A 1 39  ? 33.25695 -30.95475 -94.91568  1.000 258.98314 ? 33  PHE A CE2 1 
ATOM   218  C CZ  . PHE A 1 39  ? 33.88419 -30.85585 -96.14172  1.000 254.21044 ? 33  PHE A CZ  1 
ATOM   219  N N   . GLU A 1 40  ? 34.64767 -28.15354 -91.03006  1.000 222.46564 ? 34  GLU A N   1 
ATOM   220  C CA  . GLU A 1 40  ? 33.53119 -27.22728 -90.86971  1.000 238.28467 ? 34  GLU A CA  1 
ATOM   221  C C   . GLU A 1 40  ? 34.00690 -25.78220 -90.80306  1.000 224.66163 ? 34  GLU A C   1 
ATOM   222  O O   . GLU A 1 40  ? 33.28188 -24.87177 -91.22091  1.000 210.26913 ? 34  GLU A O   1 
ATOM   223  C CB  . GLU A 1 40  ? 32.73272 -27.56963 -89.61067  1.000 248.86544 ? 34  GLU A CB  1 
ATOM   224  C CG  . GLU A 1 40  ? 31.91707 -28.85026 -89.69076  1.000 252.34791 ? 34  GLU A CG  1 
ATOM   225  C CD  . GLU A 1 40  ? 31.27493 -29.20969 -88.36131  1.000 252.97864 ? 34  GLU A CD  1 
ATOM   226  O OE1 . GLU A 1 40  ? 31.72535 -28.68518 -87.32076  1.000 230.96775 ? 34  GLU A OE1 1 
ATOM   227  O OE2 . GLU A 1 40  ? 30.31873 -30.01287 -88.35452  1.000 256.47672 ? 34  GLU A OE2 1 
ATOM   228  N N   . CYS A 1 41  ? 35.21515 -25.55383 -90.28298  1.000 218.81504 ? 35  CYS A N   1 
ATOM   229  C CA  . CYS A 1 41  ? 35.71597 -24.19137 -90.13573  1.000 222.86566 ? 35  CYS A CA  1 
ATOM   230  C C   . CYS A 1 41  ? 36.03509 -23.56558 -91.48748  1.000 222.54575 ? 35  CYS A C   1 
ATOM   231  O O   . CYS A 1 41  ? 35.71411 -22.39570 -91.72715  1.000 225.07989 ? 35  CYS A O   1 
ATOM   232  C CB  . CYS A 1 41  ? 36.95182 -24.18463 -89.23628  1.000 217.75692 ? 35  CYS A CB  1 
ATOM   233  S SG  . CYS A 1 41  ? 37.72393 -22.56353 -89.03478  1.000 253.72928 ? 35  CYS A SG  1 
ATOM   234  N N   . PHE A 1 42  ? 36.66476 -24.32700 -92.38451  1.000 215.02093 ? 36  PHE A N   1 
ATOM   235  C CA  . PHE A 1 42  ? 37.04921 -23.76995 -93.67655  1.000 222.83207 ? 36  PHE A CA  1 
ATOM   236  C C   . PHE A 1 42  ? 35.84225 -23.54600 -94.57851  1.000 222.66595 ? 36  PHE A C   1 
ATOM   237  O O   . PHE A 1 42  ? 35.87736 -22.66751 -95.44741  1.000 211.46456 ? 36  PHE A O   1 
ATOM   238  C CB  . PHE A 1 42  ? 38.06941 -24.68121 -94.35847  1.000 243.24559 ? 36  PHE A CB  1 
ATOM   239  C CG  . PHE A 1 42  ? 39.40044 -24.72762 -93.66152  1.000 239.22578 ? 36  PHE A CG  1 
ATOM   240  C CD1 . PHE A 1 42  ? 39.77204 -23.72396 -92.78101  1.000 238.55149 ? 36  PHE A CD1 1 
ATOM   241  C CD2 . PHE A 1 42  ? 40.28083 -25.77217 -93.88822  1.000 245.85780 ? 36  PHE A CD2 1 
ATOM   242  C CE1 . PHE A 1 42  ? 40.99467 -23.76246 -92.13829  1.000 243.01423 ? 36  PHE A CE1 1 
ATOM   243  C CE2 . PHE A 1 42  ? 41.50596 -25.81572 -93.24905  1.000 254.82578 ? 36  PHE A CE2 1 
ATOM   244  C CZ  . PHE A 1 42  ? 41.86278 -24.80953 -92.37276  1.000 250.43948 ? 36  PHE A CZ  1 
ATOM   245  N N   . ASN A 1 43  ? 34.77064 -24.32063 -94.39173  1.000 227.52116 ? 37  ASN A N   1 
ATOM   246  C CA  . ASN A 1 43  ? 33.56064 -24.09801 -95.17719  1.000 230.57544 ? 37  ASN A CA  1 
ATOM   247  C C   . ASN A 1 43  ? 32.87144 -22.80087 -94.77440  1.000 227.60083 ? 37  ASN A C   1 
ATOM   248  O O   . ASN A 1 43  ? 32.32731 -22.09032 -95.62735  1.000 226.45896 ? 37  ASN A O   1 
ATOM   249  C CB  . ASN A 1 43  ? 32.60238 -25.27923 -95.02507  1.000 226.93428 ? 37  ASN A CB  1 
ATOM   250  C CG  . ASN A 1 43  ? 33.00076 -26.46718 -95.87584  1.000 238.91493 ? 37  ASN A CG  1 
ATOM   251  O OD1 . ASN A 1 43  ? 32.79774 -26.47043 -97.09026  1.000 223.03205 ? 37  ASN A OD1 1 
ATOM   252  N ND2 . ASN A 1 43  ? 33.56078 -27.48960 -95.24045  1.000 259.51964 ? 37  ASN A ND2 1 
ATOM   253  N N   . GLU A 1 44  ? 32.88358 -22.47603 -93.47971  1.000 203.35705 ? 38  GLU A N   1 
ATOM   254  C CA  . GLU A 1 44  ? 32.23151 -21.25512 -93.01743  1.000 215.04029 ? 38  GLU A CA  1 
ATOM   255  C C   . GLU A 1 44  ? 32.97988 -20.01428 -93.48942  1.000 225.25666 ? 38  GLU A C   1 
ATOM   256  O O   . GLU A 1 44  ? 32.36122 -18.98789 -93.79498  1.000 229.52517 ? 38  GLU A O   1 
ATOM   257  C CB  . GLU A 1 44  ? 32.11754 -21.27082 -91.49225  1.000 225.39471 ? 38  GLU A CB  1 
ATOM   258  C CG  . GLU A 1 44  ? 31.42295 -20.05460 -90.88848  1.000 256.80037 ? 38  GLU A CG  1 
ATOM   259  C CD  . GLU A 1 44  ? 29.90630 -20.14572 -90.93648  1.000 246.29269 ? 38  GLU A CD  1 
ATOM   260  O OE1 . GLU A 1 44  ? 29.37296 -20.96974 -91.70918  1.000 261.40685 ? 38  GLU A OE1 1 
ATOM   261  O OE2 . GLU A 1 44  ? 29.24488 -19.39275 -90.19078  1.000 212.01111 ? 38  GLU A OE2 1 
ATOM   262  N N   . ILE A 1 45  ? 34.31023 -20.08933 -93.55957  1.000 222.12961 ? 39  ILE A N   1 
ATOM   263  C CA  . ILE A 1 45  ? 35.09439 -18.93993 -93.99966  1.000 230.21040 ? 39  ILE A CA  1 
ATOM   264  C C   . ILE A 1 45  ? 34.86845 -18.67432 -95.48306  1.000 231.23854 ? 39  ILE A C   1 
ATOM   265  O O   . ILE A 1 45  ? 34.74920 -17.51948 -95.91046  1.000 220.06080 ? 39  ILE A O   1 
ATOM   266  C CB  . ILE A 1 45  ? 36.58447 -19.16005 -93.68084  1.000 221.55067 ? 39  ILE A CB  1 
ATOM   267  C CG1 . ILE A 1 45  ? 36.78450 -19.35148 -92.17648  1.000 212.09464 ? 39  ILE A CG1 1 
ATOM   268  C CG2 . ILE A 1 45  ? 37.41878 -17.99177 -94.18116  1.000 232.82654 ? 39  ILE A CG2 1 
ATOM   269  C CD1 . ILE A 1 45  ? 38.22090 -19.60717 -91.78064  1.000 217.23172 ? 39  ILE A CD1 1 
ATOM   270  N N   . ILE A 1 46  ? 34.79618 -19.73457 -96.28880  1.000 231.30662 ? 40  ILE A N   1 
ATOM   271  C CA  . ILE A 1 46  ? 34.60292 -19.57133 -97.72588  1.000 232.73480 ? 40  ILE A CA  1 
ATOM   272  C C   . ILE A 1 46  ? 33.16535 -19.17036 -98.03950  1.000 239.62026 ? 40  ILE A C   1 
ATOM   273  O O   . ILE A 1 46  ? 32.91903 -18.35570 -98.93658  1.000 251.69421 ? 40  ILE A O   1 
ATOM   274  C CB  . ILE A 1 46  ? 35.01052 -20.86244 -98.46009  1.000 238.72794 ? 40  ILE A CB  1 
ATOM   275  C CG1 . ILE A 1 46  ? 36.49527 -21.15806 -98.23001  1.000 238.87365 ? 40  ILE A CG1 1 
ATOM   276  C CG2 . ILE A 1 46  ? 34.71366 -20.75628 -99.94785  1.000 231.88339 ? 40  ILE A CG2 1 
ATOM   277  C CD1 . ILE A 1 46  ? 36.98199 -22.41980 -98.91146  1.000 243.03182 ? 40  ILE A CD1 1 
ATOM   278  N N   . THR A 1 47  ? 32.19578 -19.72325 -97.30552  1.000 230.67688 ? 41  THR A N   1 
ATOM   279  C CA  . THR A 1 47  ? 30.79469 -19.40338 -97.56650  1.000 240.37591 ? 41  THR A CA  1 
ATOM   280  C C   . THR A 1 47  ? 30.49183 -17.94614 -97.23912  1.000 246.99087 ? 41  THR A C   1 
ATOM   281  O O   . THR A 1 47  ? 29.86282 -17.23795 -98.03424  1.000 244.54507 ? 41  THR A O   1 
ATOM   282  C CB  . THR A 1 47  ? 29.88152 -20.33211 -96.76461  1.000 230.40142 ? 41  THR A CB  1 
ATOM   283  O OG1 . THR A 1 47  ? 30.10216 -21.68979 -97.16741  1.000 228.06084 ? 41  THR A OG1 1 
ATOM   284  C CG2 . THR A 1 47  ? 28.41950 -19.97146 -96.99202  1.000 233.72859 ? 41  THR A CG2 1 
ATOM   285  N N   . LEU A 1 48  ? 30.93547 -17.47965 -96.07380  1.000 249.19253 ? 42  LEU A N   1 
ATOM   286  C CA  . LEU A 1 48  ? 30.68828 -16.11174 -95.63639  1.000 269.37260 ? 42  LEU A CA  1 
ATOM   287  C C   . LEU A 1 48  ? 31.67935 -15.10991 -96.21866  1.000 273.28995 ? 42  LEU A C   1 
ATOM   288  O O   . LEU A 1 48  ? 31.68228 -13.94860 -95.79532  1.000 271.34298 ? 42  LEU A O   1 
ATOM   289  C CB  . LEU A 1 48  ? 30.71654 -16.03713 -94.10733  1.000 260.82190 ? 42  LEU A CB  1 
ATOM   290  C CG  . LEU A 1 48  ? 29.72374 -16.93139 -93.36222  1.000 240.78379 ? 42  LEU A CG  1 
ATOM   291  C CD1 . LEU A 1 48  ? 29.79290 -16.67173 -91.86613  1.000 234.16343 ? 42  LEU A CD1 1 
ATOM   292  C CD2 . LEU A 1 48  ? 28.30994 -16.72199 -93.88325  1.000 257.67231 ? 42  LEU A CD2 1 
ATOM   293  N N   . ALA A 1 49  ? 32.51266 -15.52462 -97.16908  1.000 275.37979 ? 43  ALA A N   1 
ATOM   294  C CA  . ALA A 1 49  ? 33.48135 -14.62367 -97.77543  1.000 285.65842 ? 43  ALA A CA  1 
ATOM   295  C C   . ALA A 1 49  ? 32.80096 -13.70451 -98.78088  1.000 280.39251 ? 43  ALA A C   1 
ATOM   296  O O   . ALA A 1 49  ? 31.97131 -14.14133 -99.58363  1.000 272.75175 ? 43  ALA A O   1 
ATOM   297  C CB  . ALA A 1 49  ? 34.59338 -15.41624 -98.46107  1.000 276.24251 ? 43  ALA A CB  1 
ATOM   298  N N   . LYS A 1 50  ? 33.16047 -12.42225 -98.73331  1.000 287.84836 ? 44  LYS A N   1 
ATOM   299  C CA  . LYS A 1 50  ? 32.57143 -11.43081 -99.62494  1.000 284.76586 ? 44  LYS A CA  1 
ATOM   300  C C   . LYS A 1 50  ? 33.64399 -10.59850 -100.31487 1.000 284.13657 ? 44  LYS A C   1 
ATOM   301  O O   . LYS A 1 50  ? 33.41894 -10.06886 -101.40765 1.000 271.98423 ? 44  LYS A O   1 
ATOM   302  C CB  . LYS A 1 50  ? 31.61671 -10.51471 -98.85481  1.000 277.24566 ? 44  LYS A CB  1 
ATOM   303  C CG  . LYS A 1 50  ? 30.41679 -11.22081 -98.24625  1.000 262.53140 ? 44  LYS A CG  1 
ATOM   304  C CD  . LYS A 1 50  ? 29.50892 -10.23289 -97.53230  1.000 246.11997 ? 44  LYS A CD  1 
ATOM   305  C CE  . LYS A 1 50  ? 28.28667 -10.92103 -96.94842  1.000 206.68599 ? 44  LYS A CE  1 
ATOM   306  N NZ  . LYS A 1 50  ? 27.38334 -9.95123  -96.26939  1.000 223.62838 ? 44  LYS A NZ  1 
ATOM   307  N N   . LYS A 1 51  ? 34.81395 -10.47852 -99.68878  1.000 290.93429 ? 45  LYS A N   1 
ATOM   308  C CA  . LYS A 1 51  ? 35.86726 -9.60083  -100.18904 1.000 288.48298 ? 45  LYS A CA  1 
ATOM   309  C C   . LYS A 1 51  ? 37.11945 -10.36595 -100.59377 1.000 261.42575 ? 45  LYS A C   1 
ATOM   310  O O   . LYS A 1 51  ? 37.56236 -10.24445 -101.74042 1.000 251.61574 ? 45  LYS A O   1 
ATOM   311  C CB  . LYS A 1 51  ? 36.19814 -8.53823  -99.13122  1.000 294.43283 ? 45  LYS A CB  1 
ATOM   312  C CG  . LYS A 1 51  ? 34.99093 -7.72654  -98.67764  1.000 296.40049 ? 45  LYS A CG  1 
ATOM   313  C CD  . LYS A 1 51  ? 35.33985 -6.78430  -97.53391  1.000 277.70696 ? 45  LYS A CD  1 
ATOM   314  C CE  . LYS A 1 51  ? 34.11199 -6.02765  -97.04234  1.000 234.96202 ? 45  LYS A CE  1 
ATOM   315  N NZ  . LYS A 1 51  ? 34.43211 -5.13936  -95.88954  1.000 210.27392 ? 45  LYS A NZ  1 
ATOM   316  N N   . TYR A 1 52  ? 37.70521 -11.15026 -99.69347  1.000 257.96610 ? 46  TYR A N   1 
ATOM   317  C CA  . TYR A 1 52  ? 38.94979 -11.84588 -99.98977  1.000 251.52205 ? 46  TYR A CA  1 
ATOM   318  C C   . TYR A 1 52  ? 39.08044 -13.04684 -99.06384  1.000 257.01593 ? 46  TYR A C   1 
ATOM   319  O O   . TYR A 1 52  ? 38.35819 -13.17628 -98.07300  1.000 266.48625 ? 46  TYR A O   1 
ATOM   320  C CB  . TYR A 1 52  ? 40.15729 -10.91370 -99.84011  1.000 260.67561 ? 46  TYR A CB  1 
ATOM   321  C CG  . TYR A 1 52  ? 40.40552 -10.46372 -98.41639  1.000 270.89420 ? 46  TYR A CG  1 
ATOM   322  C CD1 . TYR A 1 52  ? 39.78679 -9.32949  -97.90612  1.000 264.86681 ? 46  TYR A CD1 1 
ATOM   323  C CD2 . TYR A 1 52  ? 41.25759 -11.17584 -97.58160  1.000 263.72109 ? 46  TYR A CD2 1 
ATOM   324  C CE1 . TYR A 1 52  ? 40.01159 -8.91822  -96.60445  1.000 253.52842 ? 46  TYR A CE1 1 
ATOM   325  C CE2 . TYR A 1 52  ? 41.48539 -10.77422 -96.28138  1.000 253.31316 ? 46  TYR A CE2 1 
ATOM   326  C CZ  . TYR A 1 52  ? 40.86231 -9.64571  -95.79824  1.000 256.36883 ? 46  TYR A CZ  1 
ATOM   327  O OH  . TYR A 1 52  ? 41.09339 -9.24754  -94.50318  1.000 258.41944 ? 46  TYR A OH  1 
ATOM   328  N N   . ILE A 1 53  ? 40.02137 -13.92735 -99.40436  1.000 244.74137 ? 47  ILE A N   1 
ATOM   329  C CA  . ILE A 1 53  ? 40.40269 -15.05952 -98.56390  1.000 241.68411 ? 47  ILE A CA  1 
ATOM   330  C C   . ILE A 1 53  ? 41.91744 -15.19124 -98.65992  1.000 250.79876 ? 47  ILE A C   1 
ATOM   331  O O   . ILE A 1 53  ? 42.44796 -15.49613 -99.73421  1.000 253.98617 ? 47  ILE A O   1 
ATOM   332  C CB  . ILE A 1 53  ? 39.72156 -16.37227 -98.98126  1.000 257.01877 ? 47  ILE A CB  1 
ATOM   333  C CG1 . ILE A 1 53  ? 38.20859 -16.29883 -98.76487  1.000 254.73497 ? 47  ILE A CG1 1 
ATOM   334  C CG2 . ILE A 1 53  ? 40.30893 -17.54632 -98.20959  1.000 269.15960 ? 47  ILE A CG2 1 
ATOM   335  C CD1 . ILE A 1 53  ? 37.47700 -17.56450 -99.15760  1.000 257.46545 ? 47  ILE A CD1 1 
ATOM   336  N N   . TYR A 1 54  ? 42.61323 -14.95925 -97.55008  1.000 249.71750 ? 48  TYR A N   1 
ATOM   337  C CA  . TYR A 1 54  ? 44.06797 -15.04702 -97.49751  1.000 249.34773 ? 48  TYR A CA  1 
ATOM   338  C C   . TYR A 1 54  ? 44.46140 -16.26741 -96.67563  1.000 244.73157 ? 48  TYR A C   1 
ATOM   339  O O   . TYR A 1 54  ? 44.07736 -16.38329 -95.50660  1.000 235.00293 ? 48  TYR A O   1 
ATOM   340  C CB  . TYR A 1 54  ? 44.67682 -13.77607 -96.90432  1.000 247.05124 ? 48  TYR A CB  1 
ATOM   341  C CG  . TYR A 1 54  ? 44.51512 -12.54569 -97.77037  1.000 271.66522 ? 48  TYR A CG  1 
ATOM   342  C CD1 . TYR A 1 54  ? 44.18117 -12.65516 -99.11452  1.000 278.44426 ? 48  TYR A CD1 1 
ATOM   343  C CD2 . TYR A 1 54  ? 44.70372 -11.27406 -97.24429  1.000 282.10276 ? 48  TYR A CD2 1 
ATOM   344  C CE1 . TYR A 1 54  ? 44.03363 -11.53292 -99.90852  1.000 284.71856 ? 48  TYR A CE1 1 
ATOM   345  C CE2 . TYR A 1 54  ? 44.55842 -10.14586 -98.03047  1.000 291.51761 ? 48  TYR A CE2 1 
ATOM   346  C CZ  . TYR A 1 54  ? 44.22366 -10.28132 -99.36156  1.000 289.86204 ? 48  TYR A CZ  1 
ATOM   347  O OH  . TYR A 1 54  ? 44.07879 -9.16149  -100.14831 1.000 283.64291 ? 48  TYR A OH  1 
ATOM   348  N N   . ILE A 1 55  ? 45.22731 -17.16868 -97.28719  1.000 246.43037 ? 49  ILE A N   1 
ATOM   349  C CA  . ILE A 1 55  ? 45.64462 -18.41994 -96.66709  1.000 240.86412 ? 49  ILE A CA  1 
ATOM   350  C C   . ILE A 1 55  ? 47.16546 -18.49408 -96.69684  1.000 234.69003 ? 49  ILE A C   1 
ATOM   351  O O   . ILE A 1 55  ? 47.79744 -18.06108 -97.66695  1.000 222.68546 ? 49  ILE A O   1 
ATOM   352  C CB  . ILE A 1 55  ? 45.01991 -19.63680 -97.38360  1.000 252.89196 ? 49  ILE A CB  1 
ATOM   353  C CG1 . ILE A 1 55  ? 43.49797 -19.49003 -97.45986  1.000 261.37396 ? 49  ILE A CG1 1 
ATOM   354  C CG2 . ILE A 1 55  ? 45.39097 -20.93206 -96.67875  1.000 256.89924 ? 49  ILE A CG2 1 
ATOM   355  C CD1 . ILE A 1 55  ? 42.81110 -20.60871 -98.21407  1.000 259.02486 ? 49  ILE A CD1 1 
ATOM   356  N N   . ALA A 1 56  ? 47.75177 -19.03914 -95.63050  1.000 230.53710 ? 50  ALA A N   1 
ATOM   357  C CA  . ALA A 1 56  ? 49.19559 -19.19710 -95.53268  1.000 234.13358 ? 50  ALA A CA  1 
ATOM   358  C C   . ALA A 1 56  ? 49.52279 -20.49004 -94.80062  1.000 246.48368 ? 50  ALA A C   1 
ATOM   359  O O   . ALA A 1 56  ? 48.85846 -20.84250 -93.82146  1.000 243.81458 ? 50  ALA A O   1 
ATOM   360  C CB  . ALA A 1 56  ? 49.84275 -18.01024 -94.80852  1.000 238.85353 ? 50  ALA A CB  1 
ATOM   361  N N   . SER A 1 57  ? 50.55157 -21.18677 -95.27946  1.000 253.37547 ? 51  SER A N   1 
ATOM   362  C CA  . SER A 1 57  ? 51.04015 -22.41513 -94.66197  1.000 232.53342 ? 51  SER A CA  1 
ATOM   363  C C   . SER A 1 57  ? 52.39191 -22.74493 -95.28054  1.000 227.52187 ? 51  SER A C   1 
ATOM   364  O O   . SER A 1 57  ? 52.84142 -22.08777 -96.22293  1.000 237.79352 ? 51  SER A O   1 
ATOM   365  C CB  . SER A 1 57  ? 50.05973 -23.57754 -94.84433  1.000 237.35211 ? 51  SER A CB  1 
ATOM   366  O OG  . SER A 1 57  ? 49.92035 -23.91804 -96.21258  1.000 235.33420 ? 51  SER A OG  1 
ATOM   367  N N   . PHE A 1 58  ? 53.03680 -23.77853 -94.73718  1.000 224.75290 ? 52  PHE A N   1 
ATOM   368  C CA  . PHE A 1 58  ? 54.32681 -24.20804 -95.26887  1.000 245.28823 ? 52  PHE A CA  1 
ATOM   369  C C   . PHE A 1 58  ? 54.16010 -24.90085 -96.61686  1.000 244.61574 ? 52  PHE A C   1 
ATOM   370  O O   . PHE A 1 58  ? 54.63935 -24.41143 -97.64639  1.000 231.15614 ? 52  PHE A O   1 
ATOM   371  C CB  . PHE A 1 58  ? 55.02791 -25.12755 -94.26646  1.000 255.97724 ? 52  PHE A CB  1 
ATOM   372  C CG  . PHE A 1 58  ? 56.22301 -25.83963 -94.83189  1.000 251.42538 ? 52  PHE A CG  1 
ATOM   373  C CD1 . PHE A 1 58  ? 57.41761 -25.16762 -95.03018  1.000 223.65048 ? 52  PHE A CD1 1 
ATOM   374  C CD2 . PHE A 1 58  ? 56.15186 -27.18301 -95.16333  1.000 259.18655 ? 52  PHE A CD2 1 
ATOM   375  C CE1 . PHE A 1 58  ? 58.51772 -25.82140 -95.55160  1.000 236.14736 ? 52  PHE A CE1 1 
ATOM   376  C CE2 . PHE A 1 58  ? 57.24756 -27.84185 -95.68511  1.000 253.74461 ? 52  PHE A CE2 1 
ATOM   377  C CZ  . PHE A 1 58  ? 58.43244 -27.16054 -95.87869  1.000 246.49353 ? 52  PHE A CZ  1 
ATOM   378  N N   . CYS A 1 59  ? 53.48398 -26.04565 -96.62839  1.000 255.56711 ? 53  CYS A N   1 
ATOM   379  C CA  . CYS A 1 59  ? 53.23112 -26.80698 -97.84264  1.000 263.49881 ? 53  CYS A CA  1 
ATOM   380  C C   . CYS A 1 59  ? 51.74760 -26.74841 -98.17946  1.000 253.68697 ? 53  CYS A C   1 
ATOM   381  O O   . CYS A 1 59  ? 50.89616 -26.82657 -97.28817  1.000 262.33210 ? 53  CYS A O   1 
ATOM   382  C CB  . CYS A 1 59  ? 53.67966 -28.26366 -97.68008  1.000 265.65157 ? 53  CYS A CB  1 
ATOM   383  S SG  . CYS A 1 59  ? 53.48406 -29.29550 -99.15465  1.000 243.09342 ? 53  CYS A SG  1 
ATOM   384  N N   . CYS A 1 60  ? 51.44142 -26.60430 -99.46560  1.000 238.42959 ? 54  CYS A N   1 
ATOM   385  C CA  . CYS A 1 60  ? 50.06679 -26.52042 -99.94260  1.000 231.68424 ? 54  CYS A CA  1 
ATOM   386  C C   . CYS A 1 60  ? 49.76266 -27.74352 -100.79660 1.000 254.11017 ? 54  CYS A C   1 
ATOM   387  O O   . CYS A 1 60  ? 50.36773 -27.93067 -101.85807 1.000 257.63570 ? 54  CYS A O   1 
ATOM   388  C CB  . CYS A 1 60  ? 49.83628 -25.23583 -100.73754 1.000 229.91108 ? 54  CYS A CB  1 
ATOM   389  S SG  . CYS A 1 60  ? 48.10943 -24.95609 -101.19475 1.000 242.00931 ? 54  CYS A SG  1 
ATOM   390  N N   . ASN A 1 61  ? 48.82717 -28.56892 -100.33121 1.000 256.12627 ? 55  ASN A N   1 
ATOM   391  C CA  . ASN A 1 61  ? 48.43166 -29.78419 -101.03042 1.000 250.61637 ? 55  ASN A CA  1 
ATOM   392  C C   . ASN A 1 61  ? 47.07547 -30.25265 -100.51737 1.000 239.61916 ? 55  ASN A C   1 
ATOM   393  O O   . ASN A 1 61  ? 47.00840 -31.08879 -99.60756  1.000 248.49398 ? 55  ASN A O   1 
ATOM   394  C CB  . ASN A 1 61  ? 49.48076 -30.88111 -100.84678 1.000 246.89797 ? 55  ASN A CB  1 
ATOM   395  C CG  . ASN A 1 61  ? 49.15394 -32.13254 -101.63221 1.000 247.65436 ? 55  ASN A CG  1 
ATOM   396  O OD1 . ASN A 1 61  ? 48.46459 -32.07631 -102.65067 1.000 250.12664 ? 55  ASN A OD1 1 
ATOM   397  N ND2 . ASN A 1 61  ? 49.64365 -33.27283 -101.16034 1.000 253.37769 ? 55  ASN A ND2 1 
ATOM   398  N N   . PRO A 1 62  ? 45.97826 -29.74186 -101.06921 1.000 222.61095 ? 56  PRO A N   1 
ATOM   399  C CA  . PRO A 1 62  ? 44.65463 -30.09177 -100.53901 1.000 233.39389 ? 56  PRO A CA  1 
ATOM   400  C C   . PRO A 1 62  ? 44.10353 -31.39308 -101.10130 1.000 243.69888 ? 56  PRO A C   1 
ATOM   401  O O   . PRO A 1 62  ? 43.24328 -32.02607 -100.48188 1.000 241.74021 ? 56  PRO A O   1 
ATOM   402  C CB  . PRO A 1 62  ? 43.79578 -28.89557 -100.96055 1.000 235.53845 ? 56  PRO A CB  1 
ATOM   403  C CG  . PRO A 1 62  ? 44.41944 -28.45275 -102.24217 1.000 229.31198 ? 56  PRO A CG  1 
ATOM   404  C CD  . PRO A 1 62  ? 45.90035 -28.70330 -102.11078 1.000 208.33971 ? 56  PRO A CD  1 
ATOM   405  N N   . LEU A 1 63  ? 44.59402 -31.80603 -102.26762 1.000 244.03293 ? 57  LEU A N   1 
ATOM   406  C CA  . LEU A 1 63  ? 44.04619 -32.95320 -102.98167 1.000 248.75410 ? 57  LEU A CA  1 
ATOM   407  C C   . LEU A 1 63  ? 44.51582 -34.29439 -102.42628 1.000 259.59889 ? 57  LEU A C   1 
ATOM   408  O O   . LEU A 1 63  ? 44.22989 -35.33022 -103.03727 1.000 256.53115 ? 57  LEU A O   1 
ATOM   409  C CB  . LEU A 1 63  ? 44.40216 -32.85752 -104.46762 1.000 235.88203 ? 57  LEU A CB  1 
ATOM   410  C CG  . LEU A 1 63  ? 44.01182 -31.54917 -105.15761 1.000 226.73873 ? 57  LEU A CG  1 
ATOM   411  C CD1 . LEU A 1 63  ? 44.42624 -31.56436 -106.61966 1.000 247.14972 ? 57  LEU A CD1 1 
ATOM   412  C CD2 . LEU A 1 63  ? 42.51858 -31.29790 -105.02224 1.000 244.97818 ? 57  LEU A CD2 1 
ATOM   413  N N   . SER A 1 64  ? 45.21609 -34.30800 -101.29042 1.000 260.17571 ? 58  SER A N   1 
ATOM   414  C CA  . SER A 1 64  ? 45.74011 -35.55751 -100.75258 1.000 258.89786 ? 58  SER A CA  1 
ATOM   415  C C   . SER A 1 64  ? 44.68546 -36.38202 -100.02458 1.000 258.66439 ? 58  SER A C   1 
ATOM   416  O O   . SER A 1 64  ? 44.89035 -37.58450 -99.82615  1.000 261.84192 ? 58  SER A O   1 
ATOM   417  C CB  . SER A 1 64  ? 46.91570 -35.27763 -99.81238  1.000 260.56022 ? 58  SER A CB  1 
ATOM   418  O OG  . SER A 1 64  ? 46.51844 -34.48007 -98.71227  1.000 268.12196 ? 58  SER A OG  1 
ATOM   419  N N   . THR A 1 65  ? 43.57319 -35.77271 -99.61497  1.000 260.96199 ? 59  THR A N   1 
ATOM   420  C CA  . THR A 1 65  ? 42.49103 -36.49121 -98.95522  1.000 261.79055 ? 59  THR A CA  1 
ATOM   421  C C   . THR A 1 65  ? 41.16485 -36.05071 -99.56033  1.000 256.93625 ? 59  THR A C   1 
ATOM   422  O O   . THR A 1 65  ? 41.11723 -35.22320 -100.47574 1.000 249.51429 ? 59  THR A O   1 
ATOM   423  C CB  . THR A 1 65  ? 42.49001 -36.25941 -97.43874  1.000 262.95755 ? 59  THR A CB  1 
ATOM   424  O OG1 . THR A 1 65  ? 42.31233 -34.86403 -97.16606  1.000 244.07521 ? 59  THR A OG1 1 
ATOM   425  C CG2 . THR A 1 65  ? 43.79160 -36.74272 -96.81119  1.000 267.29777 ? 59  THR A CG2 1 
ATOM   426  N N   . THR A 1 66  ? 40.07476 -36.60700 -99.02943  1.000 257.40137 ? 60  THR A N   1 
ATOM   427  C CA  . THR A 1 66  ? 38.74701 -36.29508 -99.54675  1.000 248.69912 ? 60  THR A CA  1 
ATOM   428  C C   . THR A 1 66  ? 38.26192 -34.93399 -99.05931  1.000 245.97310 ? 60  THR A C   1 
ATOM   429  O O   . THR A 1 66  ? 37.83878 -34.09508 -99.86239  1.000 242.33439 ? 60  THR A O   1 
ATOM   430  C CB  . THR A 1 66  ? 37.75578 -37.38881 -99.14559  1.000 245.02347 ? 60  THR A CB  1 
ATOM   431  O OG1 . THR A 1 66  ? 38.18002 -38.64507 -99.68994  1.000 252.10130 ? 60  THR A OG1 1 
ATOM   432  C CG2 . THR A 1 66  ? 36.36624 -37.05793 -99.66601  1.000 234.99491 ? 60  THR A CG2 1 
ATOM   433  N N   . ARG A 1 67  ? 38.31323 -34.69914 -97.74442  1.000 247.26042 ? 61  ARG A N   1 
ATOM   434  C CA  . ARG A 1 67  ? 37.84375 -33.42828 -97.20060  1.000 241.50288 ? 61  ARG A CA  1 
ATOM   435  C C   . ARG A 1 67  ? 38.69449 -32.25874 -97.67804  1.000 237.42013 ? 61  ARG A C   1 
ATOM   436  O O   . ARG A 1 67  ? 38.18022 -31.14420 -97.83125  1.000 242.06151 ? 61  ARG A O   1 
ATOM   437  C CB  . ARG A 1 67  ? 37.83200 -33.47440 -95.67238  1.000 234.25826 ? 61  ARG A CB  1 
ATOM   438  C CG  . ARG A 1 67  ? 36.90344 -34.52169 -95.08196  1.000 240.91366 ? 61  ARG A CG  1 
ATOM   439  C CD  . ARG A 1 67  ? 36.84525 -34.41274 -93.56528  1.000 227.73769 ? 61  ARG A CD  1 
ATOM   440  N NE  . ARG A 1 67  ? 36.32114 -35.62555 -92.94802  1.000 246.86189 ? 61  ARG A NE  1 
ATOM   441  C CZ  . ARG A 1 67  ? 35.03387 -35.87126 -92.74573  1.000 244.86511 ? 61  ARG A CZ  1 
ATOM   442  N NH1 . ARG A 1 67  ? 34.09970 -35.00857 -93.10956  1.000 243.55073 ? 61  ARG A NH1 1 
ATOM   443  N NH2 . ARG A 1 67  ? 34.67495 -37.01206 -92.16393  1.000 258.52170 ? 61  ARG A NH2 1 
ATOM   444  N N   . GLY A 1 68  ? 39.98947 -32.48435 -97.90901  1.000 232.60936 ? 62  GLY A N   1 
ATOM   445  C CA  . GLY A 1 68  ? 40.83511 -31.41003 -98.40189  1.000 240.36226 ? 62  GLY A CA  1 
ATOM   446  C C   . GLY A 1 68  ? 40.48156 -30.99154 -99.81551  1.000 253.15891 ? 62  GLY A C   1 
ATOM   447  O O   . GLY A 1 68  ? 40.57836 -29.81198 -100.16557 1.000 255.19521 ? 62  GLY A O   1 
ATOM   448  N N   . ALA A 1 69  ? 40.06605 -31.95108 -100.64629 1.000 245.43929 ? 63  ALA A N   1 
ATOM   449  C CA  . ALA A 1 69  ? 39.67264 -31.63372 -102.01403 1.000 223.31919 ? 63  ALA A CA  1 
ATOM   450  C C   . ALA A 1 69  ? 38.34663 -30.88618 -102.05926 1.000 238.72226 ? 63  ALA A C   1 
ATOM   451  O O   . ALA A 1 69  ? 38.14053 -30.04597 -102.94250 1.000 265.72922 ? 63  ALA A O   1 
ATOM   452  C CB  . ALA A 1 69  ? 39.59115 -32.91371 -102.84583 1.000 218.34319 ? 63  ALA A CB  1 
ATOM   453  N N   . LEU A 1 70  ? 37.43901 -31.17579 -101.12419 1.000 235.64595 ? 64  LEU A N   1 
ATOM   454  C CA  . LEU A 1 70  ? 36.17179 -30.45378 -101.07910 1.000 241.43642 ? 64  LEU A CA  1 
ATOM   455  C C   . LEU A 1 70  ? 36.37880 -29.00464 -100.65532 1.000 247.43262 ? 64  LEU A C   1 
ATOM   456  O O   . LEU A 1 70  ? 35.69164 -28.10319 -101.14995 1.000 244.43173 ? 64  LEU A O   1 
ATOM   457  C CB  . LEU A 1 70  ? 35.19905 -31.16178 -100.13683 1.000 252.99366 ? 64  LEU A CB  1 
ATOM   458  C CG  . LEU A 1 70  ? 34.79739 -32.58107 -100.54437 1.000 233.34894 ? 64  LEU A CG  1 
ATOM   459  C CD1 . LEU A 1 70  ? 33.90742 -33.21463 -99.48705  1.000 263.52829 ? 64  LEU A CD1 1 
ATOM   460  C CD2 . LEU A 1 70  ? 34.10459 -32.57440 -101.89907 1.000 235.93978 ? 64  LEU A CD2 1 
ATOM   461  N N   . ILE A 1 71  ? 37.31924 -28.76121 -99.73963  1.000 251.69672 ? 65  ILE A N   1 
ATOM   462  C CA  . ILE A 1 71  ? 37.66415 -27.38979 -99.37826  1.000 254.29038 ? 65  ILE A CA  1 
ATOM   463  C C   . ILE A 1 71  ? 38.31598 -26.68073 -100.55840 1.000 254.77145 ? 65  ILE A C   1 
ATOM   464  O O   . ILE A 1 71  ? 38.09595 -25.48412 -100.78326 1.000 255.42156 ? 65  ILE A O   1 
ATOM   465  C CB  . ILE A 1 71  ? 38.57276 -27.37809 -98.13461  1.000 257.05156 ? 65  ILE A CB  1 
ATOM   466  C CG1 . ILE A 1 71  ? 37.85119 -28.00286 -96.93948  1.000 256.01731 ? 65  ILE A CG1 1 
ATOM   467  C CG2 . ILE A 1 71  ? 39.01854 -25.96040 -97.80308  1.000 248.36296 ? 65  ILE A CG2 1 
ATOM   468  C CD1 . ILE A 1 71  ? 36.59527 -27.26727 -96.53716  1.000 246.75762 ? 65  ILE A CD1 1 
ATOM   469  N N   . PHE A 1 72  ? 39.11933 -27.40963 -101.33696 1.000 257.14355 ? 66  PHE A N   1 
ATOM   470  C CA  . PHE A 1 72  ? 39.75900 -26.81965 -102.50730 1.000 266.96015 ? 66  PHE A CA  1 
ATOM   471  C C   . PHE A 1 72  ? 38.74930 -26.52871 -103.61091 1.000 268.27752 ? 66  PHE A C   1 
ATOM   472  O O   . PHE A 1 72  ? 38.94773 -25.59748 -104.39943 1.000 270.60806 ? 66  PHE A O   1 
ATOM   473  C CB  . PHE A 1 72  ? 40.86367 -27.74711 -103.01504 1.000 273.33204 ? 66  PHE A CB  1 
ATOM   474  C CG  . PHE A 1 72  ? 41.82565 -27.09027 -103.96458 1.000 272.72094 ? 66  PHE A CG  1 
ATOM   475  C CD1 . PHE A 1 72  ? 42.47159 -25.91508 -103.61621 1.000 261.02698 ? 66  PHE A CD1 1 
ATOM   476  C CD2 . PHE A 1 72  ? 42.10533 -27.66326 -105.19436 1.000 278.07182 ? 66  PHE A CD2 1 
ATOM   477  C CE1 . PHE A 1 72  ? 43.36500 -25.31455 -104.48403 1.000 257.99874 ? 66  PHE A CE1 1 
ATOM   478  C CE2 . PHE A 1 72  ? 42.99811 -27.06790 -106.06617 1.000 276.86948 ? 66  PHE A CE2 1 
ATOM   479  C CZ  . PHE A 1 72  ? 43.62943 -25.89274 -105.70967 1.000 266.07282 ? 66  PHE A CZ  1 
ATOM   480  N N   . ASP A 1 73  ? 37.66604 -27.30710 -103.68379 1.000 270.87393 ? 67  ASP A N   1 
ATOM   481  C CA  . ASP A 1 73  ? 36.61301 -27.02901 -104.65540 1.000 267.02888 ? 67  ASP A CA  1 
ATOM   482  C C   . ASP A 1 73  ? 35.75796 -25.84178 -104.22814 1.000 274.13856 ? 67  ASP A C   1 
ATOM   483  O O   . ASP A 1 73  ? 35.36002 -25.02746 -105.06891 1.000 281.21256 ? 67  ASP A O   1 
ATOM   484  C CB  . ASP A 1 73  ? 35.73969 -28.26837 -104.86109 1.000 264.43690 ? 67  ASP A CB  1 
ATOM   485  C CG  . ASP A 1 73  ? 36.28021 -29.19316 -105.93609 1.000 281.08920 ? 67  ASP A CG  1 
ATOM   486  O OD1 . ASP A 1 73  ? 36.81253 -28.68626 -106.94621 1.000 297.71756 ? 67  ASP A OD1 1 
ATOM   487  O OD2 . ASP A 1 73  ? 36.16959 -30.42683 -105.77292 1.000 284.89806 ? 67  ASP A OD2 1 
ATOM   488  N N   . LYS A 1 74  ? 35.45972 -25.73072 -102.93058 1.000 270.55772 ? 68  LYS A N   1 
ATOM   489  C CA  . LYS A 1 74  ? 34.72845 -24.56640 -102.44064 1.000 259.95483 ? 68  LYS A CA  1 
ATOM   490  C C   . LYS A 1 74  ? 35.55076 -23.29559 -102.60766 1.000 255.12591 ? 68  LYS A C   1 
ATOM   491  O O   . LYS A 1 74  ? 35.00283 -22.22339 -102.89020 1.000 243.08789 ? 68  LYS A O   1 
ATOM   492  C CB  . LYS A 1 74  ? 34.33715 -24.76598 -100.97615 1.000 259.44138 ? 68  LYS A CB  1 
ATOM   493  C CG  . LYS A 1 74  ? 33.24600 -25.80187 -100.75603 1.000 261.46640 ? 68  LYS A CG  1 
ATOM   494  C CD  . LYS A 1 74  ? 31.94573 -25.38254 -101.42453 1.000 242.64872 ? 68  LYS A CD  1 
ATOM   495  C CE  . LYS A 1 74  ? 30.82981 -26.37486 -101.13926 1.000 246.20584 ? 68  LYS A CE  1 
ATOM   496  N NZ  . LYS A 1 74  ? 31.15607 -27.73889 -101.63802 1.000 299.87309 ? 68  LYS A NZ  1 
ATOM   497  N N   . LEU A 1 75  ? 36.87112 -23.39662 -102.43679 1.000 263.63947 ? 69  LEU A N   1 
ATOM   498  C CA  . LEU A 1 75  ? 37.73668 -22.24955 -102.68356 1.000 266.76614 ? 69  LEU A CA  1 
ATOM   499  C C   . LEU A 1 75  ? 37.86224 -21.95935 -104.17383 1.000 266.24046 ? 69  LEU A C   1 
ATOM   500  O O   . LEU A 1 75  ? 38.02992 -20.79888 -104.56632 1.000 263.13340 ? 69  LEU A O   1 
ATOM   501  C CB  . LEU A 1 75  ? 39.11428 -22.48968 -102.06541 1.000 265.94154 ? 69  LEU A CB  1 
ATOM   502  C CG  . LEU A 1 75  ? 40.05730 -21.28711 -102.00293 1.000 259.89232 ? 69  LEU A CG  1 
ATOM   503  C CD1 . LEU A 1 75  ? 39.46734 -20.19142 -101.12857 1.000 250.88891 ? 69  LEU A CD1 1 
ATOM   504  C CD2 . LEU A 1 75  ? 41.42780 -21.70520 -101.49460 1.000 271.69865 ? 69  LEU A CD2 1 
ATOM   505  N N   . LYS A 1 76  ? 37.78570 -22.99491 -105.01462 1.000 272.24652 ? 70  LYS A N   1 
ATOM   506  C CA  . LYS A 1 76  ? 37.78535 -22.77916 -106.45816 1.000 268.40163 ? 70  LYS A CA  1 
ATOM   507  C C   . LYS A 1 76  ? 36.51892 -22.06109 -106.90436 1.000 270.00152 ? 70  LYS A C   1 
ATOM   508  O O   . LYS A 1 76  ? 36.57735 -21.14000 -107.72733 1.000 278.05076 ? 70  LYS A O   1 
ATOM   509  C CB  . LYS A 1 76  ? 37.93053 -24.11383 -107.19032 1.000 282.79377 ? 70  LYS A CB  1 
ATOM   510  C CG  . LYS A 1 76  ? 37.81981 -24.01352 -108.70678 1.000 278.53518 ? 70  LYS A CG  1 
ATOM   511  C CD  . LYS A 1 76  ? 38.03588 -25.36741 -109.36806 1.000 280.85841 ? 70  LYS A CD  1 
ATOM   512  C CE  . LYS A 1 76  ? 37.82899 -25.29642 -110.87398 1.000 257.77617 ? 70  LYS A CE  1 
ATOM   513  N NZ  . LYS A 1 76  ? 36.42111 -24.96709 -111.22977 1.000 231.84217 ? 70  LYS A NZ  1 
ATOM   514  N N   . GLU A 1 77  ? 35.36446 -22.46984 -106.37154 1.000 268.61890 ? 71  GLU A N   1 
ATOM   515  C CA  . GLU A 1 77  ? 34.11417 -21.79683 -106.70435 1.000 274.29666 ? 71  GLU A CA  1 
ATOM   516  C C   . GLU A 1 77  ? 34.09311 -20.36658 -106.18095 1.000 267.97033 ? 71  GLU A C   1 
ATOM   517  O O   . GLU A 1 77  ? 33.49119 -19.48772 -106.80781 1.000 259.83039 ? 71  GLU A O   1 
ATOM   518  C CB  . GLU A 1 77  ? 32.92977 -22.58965 -106.14804 1.000 272.35750 ? 71  GLU A CB  1 
ATOM   519  C CG  . GLU A 1 77  ? 31.56457 -22.02699 -106.51537 1.000 287.59537 ? 71  GLU A CG  1 
ATOM   520  C CD  . GLU A 1 77  ? 30.42223 -22.86424 -105.97098 1.000 296.88372 ? 71  GLU A CD  1 
ATOM   521  O OE1 . GLU A 1 77  ? 30.69413 -23.91983 -105.36081 1.000 291.51192 ? 71  GLU A OE1 1 
ATOM   522  O OE2 . GLU A 1 77  ? 29.25202 -22.46660 -106.15300 1.000 302.89556 ? 71  GLU A OE2 1 
ATOM   523  N N   . ALA A 1 78  ? 34.74900 -20.11213 -105.04611 1.000 264.28107 ? 72  ALA A N   1 
ATOM   524  C CA  . ALA A 1 78  ? 34.78584 -18.75895 -104.50156 1.000 247.32935 ? 72  ALA A CA  1 
ATOM   525  C C   . ALA A 1 78  ? 35.64219 -17.83762 -105.36185 1.000 251.00064 ? 72  ALA A C   1 
ATOM   526  O O   . ALA A 1 78  ? 35.30628 -16.66181 -105.54492 1.000 245.99044 ? 72  ALA A O   1 
ATOM   527  C CB  . ALA A 1 78  ? 35.30167 -18.78563 -103.06328 1.000 236.56017 ? 72  ALA A CB  1 
ATOM   528  N N   . SER A 1 79  ? 36.75134 -18.35202 -105.89973 1.000 260.75661 ? 73  SER A N   1 
ATOM   529  C CA  . SER A 1 79  ? 37.61977 -17.53744 -106.74210 1.000 256.27158 ? 73  SER A CA  1 
ATOM   530  C C   . SER A 1 79  ? 36.96977 -17.17982 -108.07151 1.000 260.86244 ? 73  SER A C   1 
ATOM   531  O O   . SER A 1 79  ? 37.36639 -16.18863 -108.69372 1.000 249.06339 ? 73  SER A O   1 
ATOM   532  C CB  . SER A 1 79  ? 38.94366 -18.26183 -106.99376 1.000 248.99966 ? 73  SER A CB  1 
ATOM   533  O OG  . SER A 1 79  ? 38.73765 -19.48299 -107.68250 1.000 247.19922 ? 73  SER A OG  1 
ATOM   534  N N   . GLU A 1 80  ? 35.98729 -17.95838 -108.51759 1.000 264.59225 ? 74  GLU A N   1 
ATOM   535  C CA  . GLU A 1 80  ? 35.30308 -17.71296 -109.77923 1.000 264.27526 ? 74  GLU A CA  1 
ATOM   536  C C   . GLU A 1 80  ? 34.13481 -16.74473 -109.64500 1.000 272.06225 ? 74  GLU A C   1 
ATOM   537  O O   . GLU A 1 80  ? 33.51624 -16.40010 -110.65727 1.000 290.71563 ? 74  GLU A O   1 
ATOM   538  C CB  . GLU A 1 80  ? 34.81046 -19.03690 -110.37470 1.000 271.17237 ? 74  GLU A CB  1 
ATOM   539  C CG  . GLU A 1 80  ? 35.92507 -20.01843 -110.70725 1.000 277.48856 ? 74  GLU A CG  1 
ATOM   540  C CD  . GLU A 1 80  ? 35.40293 -21.36372 -111.17578 1.000 274.04143 ? 74  GLU A CD  1 
ATOM   541  O OE1 . GLU A 1 80  ? 34.16938 -21.55975 -111.17228 1.000 270.68965 ? 74  GLU A OE1 1 
ATOM   542  O OE2 . GLU A 1 80  ? 36.22726 -22.22610 -111.54694 1.000 276.17843 ? 74  GLU A OE2 1 
ATOM   543  N N   . LYS A 1 81  ? 33.81773 -16.29940 -108.43129 1.000 268.76975 ? 75  LYS A N   1 
ATOM   544  C CA  . LYS A 1 81  ? 32.73349 -15.35401 -108.20705 1.000 266.58416 ? 75  LYS A CA  1 
ATOM   545  C C   . LYS A 1 81  ? 33.22639 -13.93278 -107.96949 1.000 261.23988 ? 75  LYS A C   1 
ATOM   546  O O   . LYS A 1 81  ? 32.40414 -13.02750 -107.79750 1.000 261.95588 ? 75  LYS A O   1 
ATOM   547  C CB  . LYS A 1 81  ? 31.87390 -15.80701 -107.02124 1.000 271.50382 ? 75  LYS A CB  1 
ATOM   548  C CG  . LYS A 1 81  ? 31.30986 -17.21314 -107.16129 1.000 276.92990 ? 75  LYS A CG  1 
ATOM   549  C CD  . LYS A 1 81  ? 30.48605 -17.36228 -108.43113 1.000 285.15563 ? 75  LYS A CD  1 
ATOM   550  C CE  . LYS A 1 81  ? 30.03965 -18.80269 -108.63772 1.000 279.07275 ? 75  LYS A CE  1 
ATOM   551  N NZ  . LYS A 1 81  ? 29.23809 -19.31374 -107.49129 1.000 286.64988 ? 75  LYS A NZ  1 
ATOM   552  N N   . GLY A 1 82  ? 34.53870 -13.71534 -107.95787 1.000 262.29938 ? 76  GLY A N   1 
ATOM   553  C CA  . GLY A 1 82  ? 35.10834 -12.40025 -107.72060 1.000 262.34298 ? 76  GLY A CA  1 
ATOM   554  C C   . GLY A 1 82  ? 35.89109 -12.26414 -106.43007 1.000 251.80181 ? 76  GLY A C   1 
ATOM   555  O O   . GLY A 1 82  ? 36.40384 -11.17022 -106.15474 1.000 247.81745 ? 76  GLY A O   1 
ATOM   556  N N   . ILE A 1 83  ? 36.01714 -13.31028 -105.62061 1.000 250.82689 ? 77  ILE A N   1 
ATOM   557  C CA  . ILE A 1 83  ? 36.74424 -13.21651 -104.35938 1.000 250.63619 ? 77  ILE A CA  1 
ATOM   558  C C   . ILE A 1 83  ? 38.23874 -13.29658 -104.64091 1.000 254.13526 ? 77  ILE A C   1 
ATOM   559  O O   . ILE A 1 83  ? 38.70855 -14.22185 -105.31392 1.000 248.27543 ? 77  ILE A O   1 
ATOM   560  C CB  . ILE A 1 83  ? 36.29872 -14.32301 -103.38977 1.000 246.48571 ? 77  ILE A CB  1 
ATOM   561  C CG1 . ILE A 1 83  ? 34.77244 -14.35970 -103.28637 1.000 250.00718 ? 77  ILE A CG1 1 
ATOM   562  C CG2 . ILE A 1 83  ? 36.91192 -14.10701 -102.01662 1.000 239.42437 ? 77  ILE A CG2 1 
ATOM   563  C CD1 . ILE A 1 83  ? 34.16245 -13.07414 -102.77318 1.000 250.29079 ? 77  ILE A CD1 1 
ATOM   564  N N   . LYS A 1 84  ? 38.99005 -12.32284 -104.13064 1.000 248.44409 ? 78  LYS A N   1 
ATOM   565  C CA  . LYS A 1 84  ? 40.43578 -12.27950 -104.32800 1.000 255.15455 ? 78  LYS A CA  1 
ATOM   566  C C   . LYS A 1 84  ? 41.08496 -13.32834 -103.43282 1.000 259.37204 ? 78  LYS A C   1 
ATOM   567  O O   . LYS A 1 84  ? 41.13200 -13.16843 -102.20875 1.000 258.28963 ? 78  LYS A O   1 
ATOM   568  C CB  . LYS A 1 84  ? 40.97414 -10.88301 -104.02767 1.000 261.45995 ? 78  LYS A CB  1 
ATOM   569  C CG  . LYS A 1 84  ? 42.45300 -10.69716 -104.34407 1.000 284.16127 ? 78  LYS A CG  1 
ATOM   570  C CD  . LYS A 1 84  ? 42.90068 -9.26482  -104.07918 1.000 267.68007 ? 78  LYS A CD  1 
ATOM   571  C CE  . LYS A 1 84  ? 44.36091 -9.05750  -104.45454 1.000 220.62153 ? 78  LYS A CE  1 
ATOM   572  N NZ  . LYS A 1 84  ? 44.81593 -7.66242  -104.19702 1.000 201.45968 ? 78  LYS A NZ  1 
ATOM   573  N N   . ILE A 1 85  ? 41.58384 -14.40171 -104.03850 1.000 257.93501 ? 79  ILE A N   1 
ATOM   574  C CA  . ILE A 1 85  ? 42.19331 -15.50830 -103.31024 1.000 254.42503 ? 79  ILE A CA  1 
ATOM   575  C C   . ILE A 1 85  ? 43.70335 -15.42260 -103.48275 1.000 251.63506 ? 79  ILE A C   1 
ATOM   576  O O   . ILE A 1 85  ? 44.21227 -15.47354 -104.60922 1.000 255.31615 ? 79  ILE A O   1 
ATOM   577  C CB  . ILE A 1 85  ? 41.66090 -16.86439 -103.79857 1.000 262.94183 ? 79  ILE A CB  1 
ATOM   578  C CG1 . ILE A 1 85  ? 40.13563 -16.83571 -103.90630 1.000 251.05150 ? 79  ILE A CG1 1 
ATOM   579  C CG2 . ILE A 1 85  ? 42.10108 -17.97546 -102.85781 1.000 264.91617 ? 79  ILE A CG2 1 
ATOM   580  C CD1 . ILE A 1 85  ? 39.43170 -16.67633 -102.58326 1.000 238.81532 ? 79  ILE A CD1 1 
ATOM   581  N N   . ILE A 1 86  ? 44.42039 -15.29408 -102.36880 1.000 247.04190 ? 80  ILE A N   1 
ATOM   582  C CA  . ILE A 1 86  ? 45.87858 -15.26032 -102.36093 1.000 254.93094 ? 80  ILE A CA  1 
ATOM   583  C C   . ILE A 1 86  ? 46.36518 -16.30527 -101.36775 1.000 245.31000 ? 80  ILE A C   1 
ATOM   584  O O   . ILE A 1 86  ? 46.01991 -16.24654 -100.18139 1.000 248.93336 ? 80  ILE A O   1 
ATOM   585  C CB  . ILE A 1 86  ? 46.42722 -13.87050 -101.99683 1.000 257.67267 ? 80  ILE A CB  1 
ATOM   586  C CG1 . ILE A 1 86  ? 46.04587 -12.84682 -103.06857 1.000 245.42873 ? 80  ILE A CG1 1 
ATOM   587  C CG2 . ILE A 1 86  ? 47.93765 -13.92515 -101.81663 1.000 256.54512 ? 80  ILE A CG2 1 
ATOM   588  C CD1 . ILE A 1 86  ? 46.60304 -11.46233 -102.81696 1.000 256.24872 ? 80  ILE A CD1 1 
ATOM   589  N N   . VAL A 1 87  ? 47.16293 -17.25515 -101.84749 1.000 224.17638 ? 81  VAL A N   1 
ATOM   590  C CA  . VAL A 1 87  ? 47.68324 -18.34583 -101.03071 1.000 235.89949 ? 81  VAL A CA  1 
ATOM   591  C C   . VAL A 1 87  ? 49.19008 -18.16820 -100.90510 1.000 247.41925 ? 81  VAL A C   1 
ATOM   592  O O   . VAL A 1 87  ? 49.89948 -18.08494 -101.91568 1.000 242.78428 ? 81  VAL A O   1 
ATOM   593  C CB  . VAL A 1 87  ? 47.33647 -19.71714 -101.63057 1.000 237.60868 ? 81  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 87  ? 47.92715 -20.83347 -100.78300 1.000 251.67499 ? 81  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 87  ? 45.82847 -19.87551 -101.75419 1.000 235.95536 ? 81  VAL A CG2 1 
ATOM   596  N N   . LEU A 1 88  ? 49.67740 -18.10878 -99.66838  1.000 246.42078 ? 82  LEU A N   1 
ATOM   597  C CA  . LEU A 1 88  ? 51.10281 -17.99860 -99.38783  1.000 234.08107 ? 82  LEU A CA  1 
ATOM   598  C C   . LEU A 1 88  ? 51.64925 -19.35645 -98.96910  1.000 245.78304 ? 82  LEU A C   1 
ATOM   599  O O   . LEU A 1 88  ? 51.08973 -20.01030 -98.08273  1.000 257.11153 ? 82  LEU A O   1 
ATOM   600  C CB  . LEU A 1 88  ? 51.37334 -16.96828 -98.29017  1.000 224.28269 ? 82  LEU A CB  1 
ATOM   601  C CG  . LEU A 1 88  ? 51.10517 -15.49828 -98.61118  1.000 238.67159 ? 82  LEU A CG  1 
ATOM   602  C CD1 . LEU A 1 88  ? 51.58592 -14.61547 -97.47024  1.000 236.86834 ? 82  LEU A CD1 1 
ATOM   603  C CD2 . LEU A 1 88  ? 51.76755 -15.09949 -99.91803  1.000 244.47122 ? 82  LEU A CD2 1 
ATOM   604  N N   . LEU A 1 89  ? 52.74049 -19.77392 -99.60613  1.000 251.60219 ? 83  LEU A N   1 
ATOM   605  C CA  . LEU A 1 89  ? 53.41495 -21.01557 -99.26161  1.000 253.05953 ? 83  LEU A CA  1 
ATOM   606  C C   . LEU A 1 89  ? 54.91817 -20.79943 -99.33527  1.000 253.27128 ? 83  LEU A C   1 
ATOM   607  O O   . LEU A 1 89  ? 55.40341 -19.96703 -100.10600 1.000 260.38409 ? 83  LEU A O   1 
ATOM   608  C CB  . LEU A 1 89  ? 52.98957 -22.17285 -100.18471 1.000 252.49412 ? 83  LEU A CB  1 
ATOM   609  C CG  . LEU A 1 89  ? 53.09309 -22.00235 -101.70597 1.000 262.89991 ? 83  LEU A CG  1 
ATOM   610  C CD1 . LEU A 1 89  ? 54.46880 -22.38928 -102.23772 1.000 255.01344 ? 83  LEU A CD1 1 
ATOM   611  C CD2 . LEU A 1 89  ? 52.00742 -22.80431 -102.40829 1.000 265.08653 ? 83  LEU A CD2 1 
ATOM   612  N N   . ASP A 1 90  ? 55.65104 -21.55164 -98.52014  1.000 230.16149 ? 84  ASP A N   1 
ATOM   613  C CA  . ASP A 1 90  ? 57.10249 -21.47756 -98.55726  1.000 230.80423 ? 84  ASP A CA  1 
ATOM   614  C C   . ASP A 1 90  ? 57.62205 -22.04355 -99.87351  1.000 238.31275 ? 84  ASP A C   1 
ATOM   615  O O   . ASP A 1 90  ? 57.05517 -22.98158 -100.44030 1.000 242.18725 ? 84  ASP A O   1 
ATOM   616  C CB  . ASP A 1 90  ? 57.70960 -22.23206 -97.37369  1.000 217.86144 ? 84  ASP A CB  1 
ATOM   617  C CG  . ASP A 1 90  ? 59.20872 -22.02461 -97.25486  1.000 225.57754 ? 84  ASP A CG  1 
ATOM   618  O OD1 . ASP A 1 90  ? 59.95772 -22.51732 -98.12438  1.000 230.45519 ? 84  ASP A OD1 1 
ATOM   619  O OD2 . ASP A 1 90  ? 59.63845 -21.35328 -96.29530  1.000 207.38878 ? 84  ASP A OD2 1 
ATOM   620  N N   . GLU A 1 91  ? 58.72275 -21.46249 -100.35659 1.000 234.95223 ? 85  GLU A N   1 
ATOM   621  C CA  . GLU A 1 91  ? 59.27929 -21.84868 -101.64821 1.000 227.35193 ? 85  GLU A CA  1 
ATOM   622  C C   . GLU A 1 91  ? 59.74150 -23.30096 -101.68371 1.000 237.30582 ? 85  GLU A C   1 
ATOM   623  O O   . GLU A 1 91  ? 60.08250 -23.79801 -102.76290 1.000 234.52891 ? 85  GLU A O   1 
ATOM   624  C CB  . GLU A 1 91  ? 60.43820 -20.91532 -102.01014 1.000 237.11788 ? 85  GLU A CB  1 
ATOM   625  C CG  . GLU A 1 91  ? 60.70704 -20.79937 -103.50335 1.000 240.22803 ? 85  GLU A CG  1 
ATOM   626  C CD  . GLU A 1 91  ? 61.73900 -19.73803 -103.82999 1.000 246.18958 ? 85  GLU A CD  1 
ATOM   627  O OE1 . GLU A 1 91  ? 62.28023 -19.12245 -102.88764 1.000 278.97402 ? 85  GLU A OE1 1 
ATOM   628  O OE2 . GLU A 1 91  ? 62.00703 -19.51744 -105.02975 1.000 209.14726 ? 85  GLU A OE2 1 
ATOM   629  N N   . ARG A 1 92  ? 59.75865 -23.99123 -100.54391 1.000 235.49896 ? 86  ARG A N   1 
ATOM   630  C CA  . ARG A 1 92  ? 60.09075 -25.40795 -100.50367 1.000 232.83044 ? 86  ARG A CA  1 
ATOM   631  C C   . ARG A 1 92  ? 58.87305 -26.30728 -100.67533 1.000 233.00187 ? 86  ARG A C   1 
ATOM   632  O O   . ARG A 1 92  ? 59.03398 -27.52699 -100.79180 1.000 258.41639 ? 86  ARG A O   1 
ATOM   633  C CB  . ARG A 1 92  ? 60.80774 -25.74230 -99.19156  1.000 225.47799 ? 86  ARG A CB  1 
ATOM   634  C CG  . ARG A 1 92  ? 62.05329 -24.90052 -98.96127  1.000 238.43911 ? 86  ARG A CG  1 
ATOM   635  C CD  . ARG A 1 92  ? 62.91548 -25.44623 -97.83693  1.000 287.40608 ? 86  ARG A CD  1 
ATOM   636  N NE  . ARG A 1 92  ? 64.11394 -24.63801 -97.64446  1.000 289.60656 ? 86  ARG A NE  1 
ATOM   637  C CZ  . ARG A 1 92  ? 65.11124 -24.95471 -96.83003  1.000 280.33304 ? 86  ARG A CZ  1 
ATOM   638  N NH1 . ARG A 1 92  ? 65.09296 -26.06734 -96.11447  1.000 272.57324 ? 86  ARG A NH1 1 
ATOM   639  N NH2 . ARG A 1 92  ? 66.15467 -24.13559 -96.73324  1.000 272.44180 ? 86  ARG A NH2 1 
ATOM   640  N N   . GLY A 1 93  ? 57.66885 -25.74093 -100.68874 1.000 227.32045 ? 87  GLY A N   1 
ATOM   641  C CA  . GLY A 1 93  ? 56.47995 -26.48624 -101.05129 1.000 218.97539 ? 87  GLY A CA  1 
ATOM   642  C C   . GLY A 1 93  ? 56.10281 -26.21499 -102.49250 1.000 240.04389 ? 87  GLY A C   1 
ATOM   643  O O   . GLY A 1 93  ? 54.92602 -26.25887 -102.86391 1.000 228.82867 ? 87  GLY A O   1 
ATOM   644  N N   . LYS A 1 94  ? 57.11361 -25.93136 -103.31283 1.000 258.53011 ? 88  LYS A N   1 
ATOM   645  C CA  . LYS A 1 94  ? 56.93601 -25.53997 -104.70512 1.000 261.85551 ? 88  LYS A CA  1 
ATOM   646  C C   . LYS A 1 94  ? 56.67300 -26.72141 -105.63032 1.000 269.40910 ? 88  LYS A C   1 
ATOM   647  O O   . LYS A 1 94  ? 56.47946 -26.51253 -106.83305 1.000 268.62870 ? 88  LYS A O   1 
ATOM   648  C CB  . LYS A 1 94  ? 58.17584 -24.77580 -105.18099 1.000 231.29623 ? 88  LYS A CB  1 
ATOM   649  C CG  . LYS A 1 94  ? 57.91405 -23.70591 -106.22628 1.000 207.24360 ? 88  LYS A CG  1 
ATOM   650  C CD  . LYS A 1 94  ? 59.17956 -22.90650 -106.49729 1.000 214.28261 ? 88  LYS A CD  1 
ATOM   651  C CE  . LYS A 1 94  ? 58.91919 -21.74677 -107.44290 1.000 231.74854 ? 88  LYS A CE  1 
ATOM   652  N NZ  . LYS A 1 94  ? 60.14251 -20.92224 -107.64962 1.000 236.92798 ? 88  LYS A NZ  1 
ATOM   653  N N   . ARG A 1 95  ? 56.66140 -27.94885 -105.10651 1.000 269.47084 ? 89  ARG A N   1 
ATOM   654  C CA  . ARG A 1 95  ? 56.45189 -29.11645 -105.95694 1.000 278.40041 ? 89  ARG A CA  1 
ATOM   655  C C   . ARG A 1 95  ? 55.02392 -29.16314 -106.48665 1.000 283.12826 ? 89  ARG A C   1 
ATOM   656  O O   . ARG A 1 95  ? 54.80007 -29.40455 -107.67873 1.000 285.98166 ? 89  ARG A O   1 
ATOM   657  C CB  . ARG A 1 95  ? 56.78286 -30.39241 -105.18305 1.000 264.55863 ? 89  ARG A CB  1 
ATOM   658  C CG  . ARG A 1 95  ? 58.20189 -30.43640 -104.64684 1.000 257.43537 ? 89  ARG A CG  1 
ATOM   659  C CD  . ARG A 1 95  ? 58.45286 -31.70559 -103.85306 1.000 266.88780 ? 89  ARG A CD  1 
ATOM   660  N NE  . ARG A 1 95  ? 59.80253 -31.74166 -103.30359 1.000 293.63708 ? 89  ARG A NE  1 
ATOM   661  C CZ  . ARG A 1 95  ? 60.14290 -31.24747 -102.12120 1.000 311.92397 ? 89  ARG A CZ  1 
ATOM   662  N NH1 . ARG A 1 95  ? 59.25223 -30.67123 -101.33049 1.000 292.02527 ? 89  ARG A NH1 1 
ATOM   663  N NH2 . ARG A 1 95  ? 61.40866 -31.33361 -101.72199 1.000 342.63378 ? 89  ARG A NH2 1 
ATOM   664  N N   . ASN A 1 96  ? 54.04396 -28.93345 -105.61485 1.000 274.70807 ? 90  ASN A N   1 
ATOM   665  C CA  . ASN A 1 96  ? 52.64115 -28.95890 -106.00753 1.000 265.75369 ? 90  ASN A CA  1 
ATOM   666  C C   . ASN A 1 96  ? 52.19666 -27.68801 -106.71949 1.000 256.42051 ? 90  ASN A C   1 
ATOM   667  O O   . ASN A 1 96  ? 51.03073 -27.60391 -107.11826 1.000 263.82519 ? 90  ASN A O   1 
ATOM   668  C CB  . ASN A 1 96  ? 51.75502 -29.19068 -104.77909 1.000 259.22098 ? 90  ASN A CB  1 
ATOM   669  C CG  . ASN A 1 96  ? 52.01307 -30.53019 -104.11570 1.000 267.16459 ? 90  ASN A CG  1 
ATOM   670  O OD1 . ASN A 1 96  ? 52.43792 -30.59320 -102.96162 1.000 271.66530 ? 90  ASN A OD1 1 
ATOM   671  N ND2 . ASN A 1 96  ? 51.75161 -31.61064 -104.84236 1.000 262.19032 ? 90  ASN A ND2 1 
ATOM   672  N N   . LEU A 1 97  ? 53.09156 -26.71128 -106.89745 1.000 254.38392 ? 91  LEU A N   1 
ATOM   673  C CA  . LEU A 1 97  ? 52.69243 -25.42456 -107.46237 1.000 254.51277 ? 91  LEU A CA  1 
ATOM   674  C C   . LEU A 1 97  ? 52.11604 -25.58108 -108.86491 1.000 248.47715 ? 91  LEU A C   1 
ATOM   675  O O   . LEU A 1 97  ? 51.12943 -24.92218 -109.21470 1.000 212.40697 ? 91  LEU A O   1 
ATOM   676  C CB  . LEU A 1 97  ? 53.88427 -24.46788 -107.47539 1.000 260.77505 ? 91  LEU A CB  1 
ATOM   677  C CG  . LEU A 1 97  ? 53.59016 -23.03584 -107.92361 1.000 262.00494 ? 91  LEU A CG  1 
ATOM   678  C CD1 . LEU A 1 97  ? 52.54242 -22.40260 -107.02251 1.000 246.32195 ? 91  LEU A CD1 1 
ATOM   679  C CD2 . LEU A 1 97  ? 54.86407 -22.20551 -107.93780 1.000 253.65722 ? 91  LEU A CD2 1 
ATOM   680  N N   . GLY A 1 98  ? 52.71745 -26.44645 -109.68419 1.000 254.77619 ? 92  GLY A N   1 
ATOM   681  C CA  . GLY A 1 98  ? 52.17358 -26.69446 -111.00804 1.000 243.91703 ? 92  GLY A CA  1 
ATOM   682  C C   . GLY A 1 98  ? 50.83696 -27.40649 -110.97540 1.000 240.65644 ? 92  GLY A C   1 
ATOM   683  O O   . GLY A 1 98  ? 50.04101 -27.28429 -111.91117 1.000 231.23887 ? 92  GLY A O   1 
ATOM   684  N N   . GLU A 1 99  ? 50.57042 -28.15517 -109.90409 1.000 253.43373 ? 93  GLU A N   1 
ATOM   685  C CA  . GLU A 1 99  ? 49.29360 -28.84465 -109.75732 1.000 249.69638 ? 93  GLU A CA  1 
ATOM   686  C C   . GLU A 1 99  ? 48.20379 -27.90538 -109.25376 1.000 247.60534 ? 93  GLU A C   1 
ATOM   687  O O   . GLU A 1 99  ? 47.05966 -27.97129 -109.71789 1.000 217.95694 ? 93  GLU A O   1 
ATOM   688  C CB  . GLU A 1 99  ? 49.45869 -30.03504 -108.81064 1.000 254.66932 ? 93  GLU A CB  1 
ATOM   689  C CG  . GLU A 1 99  ? 48.16839 -30.55928 -108.20878 1.000 261.54203 ? 93  GLU A CG  1 
ATOM   690  C CD  . GLU A 1 99  ? 48.41348 -31.65342 -107.18846 1.000 245.40017 ? 93  GLU A CD  1 
ATOM   691  O OE1 . GLU A 1 99  ? 49.34262 -32.46294 -107.39436 1.000 229.28979 ? 93  GLU A OE1 1 
ATOM   692  O OE2 . GLU A 1 99  ? 47.68454 -31.69875 -106.17512 1.000 228.43254 ? 93  GLU A OE2 1 
ATOM   693  N N   . LEU A 1 100 ? 48.54350 -27.02169 -108.31257 1.000 256.64302 ? 94  LEU A N   1 
ATOM   694  C CA  . LEU A 1 100 ? 47.54660 -26.12284 -107.73983 1.000 234.19555 ? 94  LEU A CA  1 
ATOM   695  C C   . LEU A 1 100 ? 47.05877 -25.10610 -108.76364 1.000 227.01591 ? 94  LEU A C   1 
ATOM   696  O O   . LEU A 1 100 ? 45.85496 -24.83922 -108.85650 1.000 232.23383 ? 94  LEU A O   1 
ATOM   697  C CB  . LEU A 1 100 ? 48.12833 -25.41303 -106.51920 1.000 224.96855 ? 94  LEU A CB  1 
ATOM   698  C CG  . LEU A 1 100 ? 48.72610 -26.32239 -105.44681 1.000 232.62559 ? 94  LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 100 ? 49.46264 -25.50444 -104.40244 1.000 249.57615 ? 94  LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 100 ? 47.64809 -27.17831 -104.80912 1.000 232.45464 ? 94  LEU A CD2 1 
ATOM   701  N N   . GLN A 1 101 ? 47.97796 -24.52555 -109.53807 1.000 221.94916 ? 95  GLN A N   1 
ATOM   702  C CA  . GLN A 1 101 ? 47.58724 -23.52165 -110.52149 1.000 227.21090 ? 95  GLN A CA  1 
ATOM   703  C C   . GLN A 1 101 ? 46.80850 -24.13523 -111.67751 1.000 234.73671 ? 95  GLN A C   1 
ATOM   704  O O   . GLN A 1 101 ? 46.00900 -23.44389 -112.31898 1.000 227.49490 ? 95  GLN A O   1 
ATOM   705  C CB  . GLN A 1 101 ? 48.82397 -22.79088 -111.04259 1.000 246.02307 ? 95  GLN A CB  1 
ATOM   706  C CG  . GLN A 1 101 ? 49.57918 -22.01712 -109.97568 1.000 263.05933 ? 95  GLN A CG  1 
ATOM   707  C CD  . GLN A 1 101 ? 50.84172 -21.37165 -110.50928 1.000 270.77553 ? 95  GLN A CD  1 
ATOM   708  O OE1 . GLN A 1 101 ? 51.39908 -21.81014 -111.51540 1.000 266.91064 ? 95  GLN A OE1 1 
ATOM   709  N NE2 . GLN A 1 101 ? 51.29818 -20.32050 -109.83828 1.000 269.71764 ? 95  GLN A NE2 1 
ATOM   710  N N   . SER A 1 102 ? 47.02450 -25.42294 -111.95793 1.000 247.41229 ? 96  SER A N   1 
ATOM   711  C CA  . SER A 1 102 ? 46.30792 -26.07115 -113.05112 1.000 252.84085 ? 96  SER A CA  1 
ATOM   712  C C   . SER A 1 102 ? 44.83126 -26.25280 -112.72754 1.000 252.15020 ? 96  SER A C   1 
ATOM   713  O O   . SER A 1 102 ? 43.99114 -26.22459 -113.63423 1.000 241.76856 ? 96  SER A O   1 
ATOM   714  C CB  . SER A 1 102 ? 46.94766 -27.42201 -113.37224 1.000 237.18610 ? 96  SER A CB  1 
ATOM   715  O OG  . SER A 1 102 ? 48.30438 -27.26894 -113.75043 1.000 228.86689 ? 96  SER A OG  1 
ATOM   716  N N   . HIS A 1 103 ? 44.49605 -26.43963 -111.45220 1.000 255.28633 ? 97  HIS A N   1 
ATOM   717  C CA  . HIS A 1 103 ? 43.11072 -26.63081 -111.04915 1.000 261.27107 ? 97  HIS A CA  1 
ATOM   718  C C   . HIS A 1 103 ? 42.41363 -25.32800 -110.68393 1.000 257.73183 ? 97  HIS A C   1 
ATOM   719  O O   . HIS A 1 103 ? 41.18037 -25.26335 -110.74566 1.000 260.43411 ? 97  HIS A O   1 
ATOM   720  C CB  . HIS A 1 103 ? 43.03777 -27.59923 -109.86410 1.000 262.59412 ? 97  HIS A CB  1 
ATOM   721  C CG  . HIS A 1 103 ? 41.67911 -28.18833 -109.64814 1.000 281.66583 ? 97  HIS A CG  1 
ATOM   722  N ND1 . HIS A 1 103 ? 40.77189 -27.66176 -108.75425 1.000 302.30676 ? 97  HIS A ND1 1 
ATOM   723  C CD2 . HIS A 1 103 ? 41.07306 -29.25982 -110.21202 1.000 302.01431 ? 97  HIS A CD2 1 
ATOM   724  C CE1 . HIS A 1 103 ? 39.66589 -28.38401 -108.77599 1.000 322.58470 ? 97  HIS A CE1 1 
ATOM   725  N NE2 . HIS A 1 103 ? 39.82246 -29.35947 -109.65262 1.000 338.14923 ? 97  HIS A NE2 1 
ATOM   726  N N   . CYS A 1 104 ? 43.16757 -24.29402 -110.31182 1.000 244.91092 ? 98  CYS A N   1 
ATOM   727  C CA  . CYS A 1 104 ? 42.59796 -22.99941 -109.94171 1.000 237.86716 ? 98  CYS A CA  1 
ATOM   728  C C   . CYS A 1 104 ? 43.44350 -21.89265 -110.54987 1.000 239.43757 ? 98  CYS A C   1 
ATOM   729  O O   . CYS A 1 104 ? 44.38705 -21.39198 -109.92246 1.000 229.19966 ? 98  CYS A O   1 
ATOM   730  C CB  . CYS A 1 104 ? 42.50871 -22.84304 -108.42382 1.000 250.36534 ? 98  CYS A CB  1 
ATOM   731  S SG  . CYS A 1 104 ? 41.42984 -24.03987 -107.61518 1.000 311.46048 ? 98  CYS A SG  1 
ATOM   732  N N   . PRO A 1 105 ? 43.13503 -21.47962 -111.78175 1.000 246.78960 ? 99  PRO A N   1 
ATOM   733  C CA  . PRO A 1 105 ? 43.89672 -20.38320 -112.39746 1.000 256.37942 ? 99  PRO A CA  1 
ATOM   734  C C   . PRO A 1 105 ? 43.57515 -19.01909 -111.81406 1.000 255.61609 ? 99  PRO A C   1 
ATOM   735  O O   . PRO A 1 105 ? 44.39749 -18.10284 -111.93875 1.000 241.82424 ? 99  PRO A O   1 
ATOM   736  C CB  . PRO A 1 105 ? 43.49514 -20.46593 -113.87480 1.000 250.06915 ? 99  PRO A CB  1 
ATOM   737  C CG  . PRO A 1 105 ? 42.12247 -21.05538 -113.84457 1.000 229.72067 ? 99  PRO A CG  1 
ATOM   738  C CD  . PRO A 1 105 ? 42.10893 -22.02347 -112.68949 1.000 227.90202 ? 99  PRO A CD  1 
ATOM   739  N N   . ASP A 1 106 ? 42.41182 -18.85310 -111.18390 1.000 257.74624 ? 100 ASP A N   1 
ATOM   740  C CA  . ASP A 1 106 ? 42.02542 -17.57023 -110.61182 1.000 254.46303 ? 100 ASP A CA  1 
ATOM   741  C C   . ASP A 1 106 ? 42.60516 -17.33763 -109.22384 1.000 235.27125 ? 100 ASP A C   1 
ATOM   742  O O   . ASP A 1 106 ? 42.57346 -16.20023 -108.74149 1.000 221.98715 ? 100 ASP A O   1 
ATOM   743  C CB  . ASP A 1 106 ? 40.50019 -17.46097 -110.55424 1.000 251.87000 ? 100 ASP A CB  1 
ATOM   744  C CG  . ASP A 1 106 ? 39.85927 -17.55296 -111.92390 1.000 256.55793 ? 100 ASP A CG  1 
ATOM   745  O OD1 . ASP A 1 106 ? 40.46221 -17.05468 -112.89773 1.000 249.62730 ? 100 ASP A OD1 1 
ATOM   746  O OD2 . ASP A 1 106 ? 38.75491 -18.12646 -112.02775 1.000 281.57111 ? 100 ASP A OD2 1 
ATOM   747  N N   . ILE A 1 107 ? 43.12442 -18.37351 -108.57462 1.000 230.16450 ? 101 ILE A N   1 
ATOM   748  C CA  . ILE A 1 107 ? 43.74108 -18.23994 -107.26097 1.000 240.30417 ? 101 ILE A CA  1 
ATOM   749  C C   . ILE A 1 107 ? 45.19389 -17.82637 -107.44309 1.000 257.00113 ? 101 ILE A C   1 
ATOM   750  O O   . ILE A 1 107 ? 45.94170 -18.45933 -108.19831 1.000 263.38350 ? 101 ILE A O   1 
ATOM   751  C CB  . ILE A 1 107 ? 43.63410 -19.55056 -106.46508 1.000 239.87587 ? 101 ILE A CB  1 
ATOM   752  C CG1 . ILE A 1 107 ? 42.17132 -19.85308 -106.13610 1.000 245.73536 ? 101 ILE A CG1 1 
ATOM   753  C CG2 . ILE A 1 107 ? 44.46888 -19.47337 -105.19623 1.000 222.51942 ? 101 ILE A CG2 1 
ATOM   754  C CD1 . ILE A 1 107 ? 41.98209 -21.06989 -105.25972 1.000 267.94746 ? 101 ILE A CD1 1 
ATOM   755  N N   . ASN A 1 108 ? 45.59417 -16.76272 -106.75159 1.000 258.51370 ? 102 ASN A N   1 
ATOM   756  C CA  . ASN A 1 108 ? 46.94795 -16.22340 -106.85602 1.000 265.93877 ? 102 ASN A CA  1 
ATOM   757  C C   . ASN A 1 108 ? 47.84312 -16.96748 -105.87191 1.000 259.78313 ? 102 ASN A C   1 
ATOM   758  O O   . ASN A 1 108 ? 47.85000 -16.67358 -104.67411 1.000 253.99810 ? 102 ASN A O   1 
ATOM   759  C CB  . ASN A 1 108 ? 46.94606 -14.72225 -106.58986 1.000 266.30716 ? 102 ASN A CB  1 
ATOM   760  C CG  . ASN A 1 108 ? 48.31383 -14.09563 -106.76946 1.000 276.50244 ? 102 ASN A CG  1 
ATOM   761  O OD1 . ASN A 1 108 ? 49.17357 -14.63965 -107.46269 1.000 281.45326 ? 102 ASN A OD1 1 
ATOM   762  N ND2 . ASN A 1 108 ? 48.52200 -12.94254 -106.14418 1.000 285.25208 ? 102 ASN A ND2 1 
ATOM   763  N N   . PHE A 1 109 ? 48.59948 -17.93874 -106.37814 1.000 261.64855 ? 103 PHE A N   1 
ATOM   764  C CA  . PHE A 1 109 ? 49.56546 -18.67240 -105.57124 1.000 263.58069 ? 103 PHE A CA  1 
ATOM   765  C C   . PHE A 1 109 ? 50.89323 -17.92410 -105.56692 1.000 265.90699 ? 103 PHE A C   1 
ATOM   766  O O   . PHE A 1 109 ? 51.38841 -17.52144 -106.62468 1.000 256.12138 ? 103 PHE A O   1 
ATOM   767  C CB  . PHE A 1 109 ? 49.75351 -20.09252 -106.10801 1.000 265.34457 ? 103 PHE A CB  1 
ATOM   768  C CG  . PHE A 1 109 ? 48.51159 -20.93809 -106.04023 1.000 255.34742 ? 103 PHE A CG  1 
ATOM   769  C CD1 . PHE A 1 109 ? 48.20974 -21.65828 -104.89598 1.000 251.63267 ? 103 PHE A CD1 1 
ATOM   770  C CD2 . PHE A 1 109 ? 47.64863 -21.01582 -107.12135 1.000 248.36805 ? 103 PHE A CD2 1 
ATOM   771  C CE1 . PHE A 1 109 ? 47.06936 -22.43767 -104.82968 1.000 239.06841 ? 103 PHE A CE1 1 
ATOM   772  C CE2 . PHE A 1 109 ? 46.50682 -21.79431 -107.06159 1.000 242.13074 ? 103 PHE A CE2 1 
ATOM   773  C CZ  . PHE A 1 109 ? 46.21707 -22.50562 -105.91393 1.000 231.97442 ? 103 PHE A CZ  1 
ATOM   774  N N   . ILE A 1 110 ? 51.46535 -17.74003 -104.37810 1.000 266.60233 ? 104 ILE A N   1 
ATOM   775  C CA  . ILE A 1 110 ? 52.67585 -16.94471 -104.19598 1.000 261.49231 ? 104 ILE A CA  1 
ATOM   776  C C   . ILE A 1 110 ? 53.66268 -17.74198 -103.35358 1.000 264.34879 ? 104 ILE A C   1 
ATOM   777  O O   . ILE A 1 110 ? 53.32967 -18.17018 -102.24174 1.000 248.10795 ? 104 ILE A O   1 
ATOM   778  C CB  . ILE A 1 110 ? 52.37715 -15.58920 -103.53213 1.000 245.58930 ? 104 ILE A CB  1 
ATOM   779  C CG1 . ILE A 1 110 ? 51.52783 -14.71236 -104.45526 1.000 265.57684 ? 104 ILE A CG1 1 
ATOM   780  C CG2 . ILE A 1 110 ? 53.66920 -14.88259 -103.15032 1.000 234.14462 ? 104 ILE A CG2 1 
ATOM   781  C CD1 . ILE A 1 110 ? 51.16402 -13.36983 -103.85787 1.000 248.31424 ? 104 ILE A CD1 1 
ATOM   782  N N   . THR A 1 111 ? 54.87260 -17.93513 -103.87709 1.000 275.28732 ? 105 THR A N   1 
ATOM   783  C CA  . THR A 1 111 ? 55.94061 -18.56508 -103.11288 1.000 254.47796 ? 105 THR A CA  1 
ATOM   784  C C   . THR A 1 111 ? 56.62968 -17.53117 -102.23250 1.000 234.55541 ? 105 THR A C   1 
ATOM   785  O O   . THR A 1 111 ? 56.84888 -16.38875 -102.64512 1.000 232.71974 ? 105 THR A O   1 
ATOM   786  C CB  . THR A 1 111 ? 56.96324 -19.22200 -104.04152 1.000 234.15837 ? 105 THR A CB  1 
ATOM   787  O OG1 . THR A 1 111 ? 57.56147 -18.22644 -104.88119 1.000 212.59448 ? 105 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 111 ? 56.29671 -20.28029 -104.90868 1.000 236.86187 ? 105 THR A CG2 1 
ATOM   789  N N   . VAL A 1 112 ? 56.97569 -17.93963 -101.01481 1.000 232.56951 ? 106 VAL A N   1 
ATOM   790  C CA  . VAL A 1 112 ? 57.50791 -17.03634 -100.00279 1.000 236.33521 ? 106 VAL A CA  1 
ATOM   791  C C   . VAL A 1 112 ? 58.83867 -17.58044 -99.50572  1.000 237.09143 ? 106 VAL A C   1 
ATOM   792  O O   . VAL A 1 112 ? 58.95314 -18.77286 -99.20112  1.000 250.03272 ? 106 VAL A O   1 
ATOM   793  C CB  . VAL A 1 112 ? 56.52358 -16.85848 -98.83039  1.000 256.93179 ? 106 VAL A CB  1 
ATOM   794  C CG1 . VAL A 1 112 ? 57.16304 -16.06044 -97.70603  1.000 264.98776 ? 106 VAL A CG1 1 
ATOM   795  C CG2 . VAL A 1 112 ? 55.24883 -16.18244 -99.30916  1.000 253.83304 ? 106 VAL A CG2 1 
ATOM   796  N N   . ASN A 1 113 ? 59.84240 -16.70666 -99.42826  1.000 234.03097 ? 107 ASN A N   1 
ATOM   797  C CA  . ASN A 1 113 ? 61.14071 -17.02408 -98.83377  1.000 245.81540 ? 107 ASN A CA  1 
ATOM   798  C C   . ASN A 1 113 ? 61.48045 -15.87095 -97.89342  1.000 233.26549 ? 107 ASN A C   1 
ATOM   799  O O   . ASN A 1 113 ? 62.08557 -14.87782 -98.30625  1.000 221.14368 ? 107 ASN A O   1 
ATOM   800  C CB  . ASN A 1 113 ? 62.21036 -17.23233 -99.90144  1.000 250.38321 ? 107 ASN A CB  1 
ATOM   801  C CG  . ASN A 1 113 ? 63.50640 -17.77360 -99.32917  1.000 246.66887 ? 107 ASN A CG  1 
ATOM   802  O OD1 . ASN A 1 113 ? 63.58660 -18.10298 -98.14544  1.000 223.71330 ? 107 ASN A OD1 1 
ATOM   803  N ND2 . ASN A 1 113 ? 64.52695 -17.87865 -100.17194 1.000 256.83673 ? 107 ASN A ND2 1 
ATOM   804  N N   . ILE A 1 114 ? 61.07954 -16.00715 -96.62604  1.000 238.70656 ? 108 ILE A N   1 
ATOM   805  C CA  . ILE A 1 114 ? 61.27929 -14.93859 -95.65434  1.000 244.35440 ? 108 ILE A CA  1 
ATOM   806  C C   . ILE A 1 114 ? 62.74934 -14.73281 -95.32388  1.000 229.84900 ? 108 ILE A C   1 
ATOM   807  O O   . ILE A 1 114 ? 63.12470 -13.66314 -94.83008  1.000 239.47574 ? 108 ILE A O   1 
ATOM   808  C CB  . ILE A 1 114 ? 60.48563 -15.22081 -94.36449  1.000 233.44297 ? 108 ILE A CB  1 
ATOM   809  C CG1 . ILE A 1 114 ? 60.93514 -16.54223 -93.73681  1.000 227.09441 ? 108 ILE A CG1 1 
ATOM   810  C CG2 . ILE A 1 114 ? 58.99291 -15.23884 -94.64663  1.000 240.48297 ? 108 ILE A CG2 1 
ATOM   811  C CD1 . ILE A 1 114 ? 60.22657 -16.87435 -92.44210  1.000 222.75508 ? 108 ILE A CD1 1 
ATOM   812  N N   . ASP A 1 115 ? 63.59559 -15.72778 -95.57815  1.000 206.65487 ? 109 ASP A N   1 
ATOM   813  C CA  . ASP A 1 115 ? 65.01779 -15.65372 -95.25194  1.000 216.95716 ? 109 ASP A CA  1 
ATOM   814  C C   . ASP A 1 115 ? 65.81691 -16.01240 -96.50034  1.000 227.28433 ? 109 ASP A C   1 
ATOM   815  O O   . ASP A 1 115 ? 66.03691 -17.19269 -96.78676  1.000 220.85285 ? 109 ASP A O   1 
ATOM   816  C CB  . ASP A 1 115 ? 65.36264 -16.57815 -94.08791  1.000 228.75153 ? 109 ASP A CB  1 
ATOM   817  C CG  . ASP A 1 115 ? 66.79147 -16.40571 -93.60802  1.000 232.26636 ? 109 ASP A CG  1 
ATOM   818  O OD1 . ASP A 1 115 ? 67.45447 -15.43706 -94.03540  1.000 232.89497 ? 109 ASP A OD1 1 
ATOM   819  O OD2 . ASP A 1 115 ? 67.25290 -17.24170 -92.80307  1.000 218.39093 ? 109 ASP A OD2 1 
ATOM   820  N N   . LYS A 1 116 ? 66.24139 -14.99470 -97.24489  1.000 238.75515 ? 110 LYS A N   1 
ATOM   821  C CA  . LYS A 1 116 ? 67.17080 -15.17556 -98.34982  1.000 249.00034 ? 110 LYS A CA  1 
ATOM   822  C C   . LYS A 1 116 ? 68.60538 -14.85321 -97.95658  1.000 256.06231 ? 110 LYS A C   1 
ATOM   823  O O   . LYS A 1 116 ? 69.51305 -15.01687 -98.77782  1.000 270.34145 ? 110 LYS A O   1 
ATOM   824  C CB  . LYS A 1 116 ? 66.74938 -14.31814 -99.54890  1.000 267.42790 ? 110 LYS A CB  1 
ATOM   825  C CG  . LYS A 1 116 ? 65.42419 -14.73718 -100.16950 1.000 259.97003 ? 110 LYS A CG  1 
ATOM   826  C CD  . LYS A 1 116 ? 65.22751 -14.12129 -101.54566 1.000 264.58557 ? 110 LYS A CD  1 
ATOM   827  C CE  . LYS A 1 116 ? 63.93277 -14.59841 -102.18481 1.000 238.16947 ? 110 LYS A CE  1 
ATOM   828  N NZ  . LYS A 1 116 ? 63.72109 -13.99392 -103.52890 1.000 244.46463 ? 110 LYS A NZ  1 
ATOM   829  N N   . LYS A 1 117 ? 68.82778 -14.40094 -96.72024  1.000 246.61702 ? 111 LYS A N   1 
ATOM   830  C CA  . LYS A 1 117 ? 70.18060 -14.15348 -96.23471  1.000 252.85442 ? 111 LYS A CA  1 
ATOM   831  C C   . LYS A 1 117 ? 70.89877 -15.45545 -95.89969  1.000 260.95713 ? 111 LYS A C   1 
ATOM   832  O O   . LYS A 1 117 ? 72.07550 -15.62386 -96.23887  1.000 252.67952 ? 111 LYS A O   1 
ATOM   833  C CB  . LYS A 1 117 ? 70.13437 -13.23749 -95.00984  1.000 242.18105 ? 111 LYS A CB  1 
ATOM   834  C CG  . LYS A 1 117 ? 71.48519 -12.97791 -94.35861  1.000 254.04823 ? 111 LYS A CG  1 
ATOM   835  C CD  . LYS A 1 117 ? 71.32423 -12.20641 -93.05581  1.000 243.12346 ? 111 LYS A CD  1 
ATOM   836  C CE  . LYS A 1 117 ? 72.66785 -11.92286 -92.40170  1.000 237.27462 ? 111 LYS A CE  1 
ATOM   837  N NZ  . LYS A 1 117 ? 73.51881 -11.03016 -93.23630  1.000 270.75419 ? 111 LYS A NZ  1 
ATOM   838  N N   . ASN A 1 118 ? 70.20707 -16.38542 -95.23805  1.000 264.07279 ? 112 ASN A N   1 
ATOM   839  C CA  . ASN A 1 118 ? 70.78759 -17.66841 -94.87007  1.000 258.63376 ? 112 ASN A CA  1 
ATOM   840  C C   . ASN A 1 118 ? 69.97882 -18.86843 -95.34082  1.000 248.18596 ? 112 ASN A C   1 
ATOM   841  O O   . ASN A 1 118 ? 70.46103 -19.99866 -95.20288  1.000 234.77579 ? 112 ASN A O   1 
ATOM   842  C CB  . ASN A 1 118 ? 70.96741 -17.76028 -93.34590  1.000 255.02694 ? 112 ASN A CB  1 
ATOM   843  C CG  . ASN A 1 118 ? 71.81866 -16.63475 -92.79001  1.000 251.71537 ? 112 ASN A CG  1 
ATOM   844  O OD1 . ASN A 1 118 ? 71.36312 -15.84885 -91.95897  1.000 247.23175 ? 112 ASN A OD1 1 
ATOM   845  N ND2 . ASN A 1 118 ? 73.06255 -16.55150 -93.24762  1.000 255.58078 ? 112 ASN A ND2 1 
ATOM   846  N N   . ASN A 1 119 ? 68.77616 -18.66394 -95.88455  1.000 248.58686 ? 113 ASN A N   1 
ATOM   847  C CA  . ASN A 1 119 ? 67.92727 -19.74686 -96.38631  1.000 247.82893 ? 113 ASN A CA  1 
ATOM   848  C C   . ASN A 1 119 ? 67.62595 -20.77079 -95.29119  1.000 258.78599 ? 113 ASN A C   1 
ATOM   849  O O   . ASN A 1 119 ? 67.70456 -21.98351 -95.49950  1.000 272.56677 ? 113 ASN A O   1 
ATOM   850  C CB  . ASN A 1 119 ? 68.55447 -20.41533 -97.61281  1.000 254.47257 ? 113 ASN A CB  1 
ATOM   851  C CG  . ASN A 1 119 ? 68.65180 -19.47645 -98.80033  1.000 253.65615 ? 113 ASN A CG  1 
ATOM   852  O OD1 . ASN A 1 119 ? 69.63831 -18.75768 -98.95962  1.000 267.86986 ? 113 ASN A OD1 1 
ATOM   853  N ND2 . ASN A 1 119 ? 67.62437 -19.47886 -99.64226  1.000 246.08340 ? 113 ASN A ND2 1 
ATOM   854  N N   . VAL A 1 120 ? 67.27084 -20.26576 -94.10722  1.000 253.72723 ? 114 VAL A N   1 
ATOM   855  C CA  . VAL A 1 120 ? 66.92725 -21.09952 -92.96497  1.000 254.23045 ? 114 VAL A CA  1 
ATOM   856  C C   . VAL A 1 120 ? 65.49916 -20.85625 -92.49431  1.000 248.61867 ? 114 VAL A C   1 
ATOM   857  O O   . VAL A 1 120 ? 64.78043 -21.80566 -92.16064  1.000 252.37759 ? 114 VAL A O   1 
ATOM   858  C CB  . VAL A 1 120 ? 67.92290 -20.88793 -91.80239  1.000 238.81013 ? 114 VAL A CB  1 
ATOM   859  C CG1 . VAL A 1 120 ? 67.57802 -21.79316 -90.63001  1.000 220.91818 ? 114 VAL A CG1 1 
ATOM   860  C CG2 . VAL A 1 120 ? 69.34846 -21.13782 -92.27025  1.000 238.54596 ? 114 VAL A CG2 1 
ATOM   861  N N   . GLY A 1 121 ? 65.06467 -19.59908 -92.46515  1.000 239.99293 ? 115 GLY A N   1 
ATOM   862  C CA  . GLY A 1 121 ? 63.71884 -19.29376 -92.00661  1.000 239.30361 ? 115 GLY A CA  1 
ATOM   863  C C   . GLY A 1 121 ? 62.67565 -19.79537 -92.98949  1.000 232.13030 ? 115 GLY A C   1 
ATOM   864  O O   . GLY A 1 121 ? 62.73700 -19.50169 -94.18967  1.000 220.57460 ? 115 GLY A O   1 
ATOM   865  N N   . LEU A 1 122 ? 61.71154 -20.55800 -92.48316  1.000 227.25326 ? 116 LEU A N   1 
ATOM   866  C CA  . LEU A 1 122 ? 60.62874 -21.10042 -93.28742  1.000 226.71515 ? 116 LEU A CA  1 
ATOM   867  C C   . LEU A 1 122 ? 59.30976 -20.44018 -92.90889  1.000 230.15639 ? 116 LEU A C   1 
ATOM   868  O O   . LEU A 1 122 ? 59.11426 -20.01047 -91.76839  1.000 233.76963 ? 116 LEU A O   1 
ATOM   869  C CB  . LEU A 1 122 ? 60.51414 -22.61797 -93.11312  1.000 235.50817 ? 116 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 122 ? 61.71355 -23.45356 -93.56153  1.000 229.66807 ? 116 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 122 ? 61.44057 -24.93453 -93.34989  1.000 216.50756 ? 116 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 122 ? 62.05262 -23.16864 -95.01570  1.000 233.26353 ? 116 LEU A CD2 1 
ATOM   873  N N   . LEU A 1 123 ? 58.40372 -20.36540 -93.88030  1.000 224.33932 ? 117 LEU A N   1 
ATOM   874  C CA  . LEU A 1 123 ? 57.08103 -19.78514 -93.66159  1.000 217.32913 ? 117 LEU A CA  1 
ATOM   875  C C   . LEU A 1 123 ? 56.21316 -20.81367 -92.94960  1.000 221.16203 ? 117 LEU A C   1 
ATOM   876  O O   . LEU A 1 123 ? 55.70119 -21.74982 -93.56765  1.000 219.40235 ? 117 LEU A O   1 
ATOM   877  C CB  . LEU A 1 123 ? 56.45515 -19.35330 -94.98214  1.000 225.93252 ? 117 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 123 ? 55.02000 -18.83153 -94.88638  1.000 210.39222 ? 117 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 123 ? 54.95390 -17.60179 -93.99356  1.000 210.92592 ? 117 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 123 ? 54.46042 -18.53112 -96.26745  1.000 225.05265 ? 117 LEU A CD2 1 
ATOM   881  N N   . LEU A 1 124 ? 56.04872 -20.64456 -91.63888  1.000 233.49165 ? 118 LEU A N   1 
ATOM   882  C CA  . LEU A 1 124 ? 55.20250 -21.51971 -90.83970  1.000 248.11840 ? 118 LEU A CA  1 
ATOM   883  C C   . LEU A 1 124 ? 53.92394 -20.83382 -90.38107  1.000 244.51027 ? 118 LEU A C   1 
ATOM   884  O O   . LEU A 1 124 ? 53.19054 -21.39705 -89.56124  1.000 256.29466 ? 118 LEU A O   1 
ATOM   885  C CB  . LEU A 1 124 ? 55.97378 -22.05144 -89.63095  1.000 263.76644 ? 118 LEU A CB  1 
ATOM   886  C CG  . LEU A 1 124 ? 57.05906 -23.08294 -89.93616  1.000 265.26018 ? 118 LEU A CG  1 
ATOM   887  C CD1 . LEU A 1 124 ? 57.60382 -23.66290 -88.64598  1.000 257.33609 ? 118 LEU A CD1 1 
ATOM   888  C CD2 . LEU A 1 124 ? 56.51851 -24.18251 -90.83802  1.000 243.58270 ? 118 LEU A CD2 1 
ATOM   889  N N   . GLY A 1 125 ? 53.64604 -19.63053 -90.87689  1.000 226.56790 ? 119 GLY A N   1 
ATOM   890  C CA  . GLY A 1 125 ? 52.38477 -18.97917 -90.59262  1.000 216.72522 ? 119 GLY A CA  1 
ATOM   891  C C   . GLY A 1 125 ? 51.22668 -19.81953 -91.08368  1.000 236.48570 ? 119 GLY A C   1 
ATOM   892  O O   . GLY A 1 125 ? 51.07442 -20.03164 -92.28933  1.000 242.90547 ? 119 GLY A O   1 
ATOM   893  N N   . CYS A 1 126 ? 50.41601 -20.32108 -90.15757  1.000 234.55937 ? 120 CYS A N   1 
ATOM   894  C CA  . CYS A 1 126 ? 49.31495 -21.23030 -90.46480  1.000 246.09287 ? 120 CYS A CA  1 
ATOM   895  C C   . CYS A 1 126 ? 48.02202 -20.57916 -89.98428  1.000 253.66322 ? 120 CYS A C   1 
ATOM   896  O O   . CYS A 1 126 ? 47.64176 -20.71735 -88.81894  1.000 255.65199 ? 120 CYS A O   1 
ATOM   897  C CB  . CYS A 1 126 ? 49.54247 -22.59085 -89.81183  1.000 251.06646 ? 120 CYS A CB  1 
ATOM   898  S SG  . CYS A 1 126 ? 48.16971 -23.74227 -89.99032  1.000 302.44635 ? 120 CYS A SG  1 
ATOM   899  N N   . PHE A 1 127 ? 47.34392 -19.87398 -90.88761  1.000 246.05283 ? 121 PHE A N   1 
ATOM   900  C CA  . PHE A 1 127 ? 46.15161 -19.13027 -90.51049  1.000 240.96961 ? 121 PHE A CA  1 
ATOM   901  C C   . PHE A 1 127 ? 45.35682 -18.76017 -91.75425  1.000 239.58801 ? 121 PHE A C   1 
ATOM   902  O O   . PHE A 1 127 ? 45.90757 -18.65410 -92.85329  1.000 220.30768 ? 121 PHE A O   1 
ATOM   903  C CB  . PHE A 1 127 ? 46.51314 -17.86613 -89.72019  1.000 249.29680 ? 121 PHE A CB  1 
ATOM   904  C CG  . PHE A 1 127 ? 47.36755 -16.89479 -90.48581  1.000 259.26049 ? 121 PHE A CG  1 
ATOM   905  C CD1 . PHE A 1 127 ? 48.74433 -17.04200 -90.52242  1.000 263.08238 ? 121 PHE A CD1 1 
ATOM   906  C CD2 . PHE A 1 127 ? 46.79433 -15.83226 -91.16572  1.000 263.63749 ? 121 PHE A CD2 1 
ATOM   907  C CE1 . PHE A 1 127 ? 49.53281 -16.15066 -91.22395  1.000 284.59774 ? 121 PHE A CE1 1 
ATOM   908  C CE2 . PHE A 1 127 ? 47.57738 -14.93756 -91.86954  1.000 268.37560 ? 121 PHE A CE2 1 
ATOM   909  C CZ  . PHE A 1 127 ? 48.94844 -15.09702 -91.89843  1.000 288.41002 ? 121 PHE A CZ  1 
ATOM   910  N N   . TRP A 1 128 ? 44.05507 -18.56732 -91.56071  1.000 247.76220 ? 122 TRP A N   1 
ATOM   911  C CA  . TRP A 1 128 ? 43.15966 -18.02781 -92.57192  1.000 246.73139 ? 122 TRP A CA  1 
ATOM   912  C C   . TRP A 1 128 ? 42.62900 -16.67570 -92.11039  1.000 250.33020 ? 122 TRP A C   1 
ATOM   913  O O   . TRP A 1 128 ? 42.64910 -16.35110 -90.92020  1.000 252.26322 ? 122 TRP A O   1 
ATOM   914  C CB  . TRP A 1 128 ? 41.98507 -18.97716 -92.85051  1.000 251.88953 ? 122 TRP A CB  1 
ATOM   915  C CG  . TRP A 1 128 ? 42.35330 -20.25985 -93.54597  1.000 248.26138 ? 122 TRP A CG  1 
ATOM   916  C CD1 . TRP A 1 128 ? 43.51459 -20.96423 -93.41408  1.000 240.48535 ? 122 TRP A CD1 1 
ATOM   917  C CD2 . TRP A 1 128 ? 41.55053 -20.98479 -94.48877  1.000 261.80867 ? 122 TRP A CD2 1 
ATOM   918  N NE1 . TRP A 1 128 ? 43.48300 -22.08380 -94.21035  1.000 254.42113 ? 122 TRP A NE1 1 
ATOM   919  C CE2 . TRP A 1 128 ? 42.28927 -22.11852 -94.88187  1.000 257.79159 ? 122 TRP A CE2 1 
ATOM   920  C CE3 . TRP A 1 128 ? 40.27909 -20.78493 -95.03721  1.000 258.56648 ? 122 TRP A CE3 1 
ATOM   921  C CZ2 . TRP A 1 128 ? 41.79928 -23.04918 -95.79723  1.000 252.41129 ? 122 TRP A CZ2 1 
ATOM   922  C CZ3 . TRP A 1 128 ? 39.79464 -21.70993 -95.94656  1.000 247.81714 ? 122 TRP A CZ3 1 
ATOM   923  C CH2 . TRP A 1 128 ? 40.55355 -22.82719 -96.31721  1.000 250.19056 ? 122 TRP A CH2 1 
ATOM   924  N N   . VAL A 1 129 ? 42.15266 -15.88609 -93.06968  1.000 257.49938 ? 123 VAL A N   1 
ATOM   925  C CA  . VAL A 1 129 ? 41.54975 -14.58836 -92.77726  1.000 253.51770 ? 123 VAL A CA  1 
ATOM   926  C C   . VAL A 1 129 ? 40.72769 -14.16954 -93.98858  1.000 257.58491 ? 123 VAL A C   1 
ATOM   927  O O   . VAL A 1 129 ? 41.13250 -14.38270 -95.13483  1.000 249.29229 ? 123 VAL A O   1 
ATOM   928  C CB  . VAL A 1 129 ? 42.62359 -13.53553 -92.40547  1.000 225.76743 ? 123 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 129 ? 43.65465 -13.39664 -93.51179  1.000 222.64696 ? 123 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 129 ? 41.97911 -12.19205 -92.08804  1.000 228.33011 ? 123 VAL A CG2 1 
ATOM   931  N N   . SER A 1 130 ? 39.55986 -13.58371 -93.72705  1.000 254.94342 ? 124 SER A N   1 
ATOM   932  C CA  . SER A 1 130 ? 38.63321 -13.22647 -94.79344  1.000 250.73191 ? 124 SER A CA  1 
ATOM   933  C C   . SER A 1 130 ? 37.80717 -12.01879 -94.37841  1.000 261.19681 ? 124 SER A C   1 
ATOM   934  O O   . SER A 1 130 ? 37.26815 -11.98612 -93.26788  1.000 259.29943 ? 124 SER A O   1 
ATOM   935  C CB  . SER A 1 130 ? 37.71239 -14.40379 -95.13476  1.000 250.03266 ? 124 SER A CB  1 
ATOM   936  O OG  . SER A 1 130 ? 36.77557 -14.04655 -96.13571  1.000 269.49000 ? 124 SER A OG  1 
ATOM   937  N N   . ASP A 1 131 ? 37.72140 -11.03254 -95.27395  1.000 265.16085 ? 125 ASP A N   1 
ATOM   938  C CA  . ASP A 1 131 ? 36.88056 -9.84587  -95.11797  1.000 253.31271 ? 125 ASP A CA  1 
ATOM   939  C C   . ASP A 1 131 ? 37.22815 -9.03074  -93.87685  1.000 249.48928 ? 125 ASP A C   1 
ATOM   940  O O   . ASP A 1 131 ? 36.44223 -8.17175  -93.46376  1.000 242.75511 ? 125 ASP A O   1 
ATOM   941  C CB  . ASP A 1 131 ? 35.39295 -10.21841 -95.09367  1.000 260.68199 ? 125 ASP A CB  1 
ATOM   942  C CG  . ASP A 1 131 ? 34.95698 -10.95630 -96.34163  1.000 276.19081 ? 125 ASP A CG  1 
ATOM   943  O OD1 . ASP A 1 131 ? 35.80729 -11.17894 -97.22845  1.000 285.67210 ? 125 ASP A OD1 1 
ATOM   944  O OD2 . ASP A 1 131 ? 33.76486 -11.31523 -96.43578  1.000 272.73428 ? 125 ASP A OD2 1 
ATOM   945  N N   . ASP A 1 132 ? 38.39267 -9.28093  -93.27281  1.000 256.04747 ? 126 ASP A N   1 
ATOM   946  C CA  . ASP A 1 132 ? 38.79334 -8.62001  -92.02896  1.000 260.52667 ? 126 ASP A CA  1 
ATOM   947  C C   . ASP A 1 132 ? 37.76833 -8.84720  -90.91986  1.000 257.81511 ? 126 ASP A C   1 
ATOM   948  O O   . ASP A 1 132 ? 37.66424 -8.05479  -89.98162  1.000 250.31090 ? 126 ASP A O   1 
ATOM   949  C CB  . ASP A 1 132 ? 39.03029 -7.11919  -92.24128  1.000 263.92626 ? 126 ASP A CB  1 
ATOM   950  C CG  . ASP A 1 132 ? 40.40251 -6.81546  -92.80667  1.000 268.25015 ? 126 ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 132 ? 41.22570 -7.74803  -92.89866  1.000 268.03411 ? 126 ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 132 ? 40.66088 -5.64561  -93.15851  1.000 275.11205 ? 126 ASP A OD2 1 
ATOM   953  N N   . GLU A 1 133 ? 37.00138 -9.93179  -91.02469  1.000 259.32680 ? 127 GLU A N   1 
ATOM   954  C CA  . GLU A 1 133 ? 35.95785 -10.26140 -90.06167  1.000 258.02813 ? 127 GLU A CA  1 
ATOM   955  C C   . GLU A 1 133 ? 36.13650 -11.64551 -89.46083  1.000 262.73315 ? 127 GLU A C   1 
ATOM   956  O O   . GLU A 1 133 ? 36.08673 -11.79506 -88.23448  1.000 264.44007 ? 127 GLU A O   1 
ATOM   957  C CB  . GLU A 1 133 ? 34.57577 -10.15302 -90.72647  1.000 249.90631 ? 127 GLU A CB  1 
ATOM   958  C CG  . GLU A 1 133 ? 34.22208 -8.75187  -91.18984  1.000 258.11477 ? 127 GLU A CG  1 
ATOM   959  C CD  . GLU A 1 133 ? 32.89153 -8.70111  -91.90772  1.000 265.81276 ? 127 GLU A CD  1 
ATOM   960  O OE1 . GLU A 1 133 ? 32.24688 -9.76290  -92.03452  1.000 262.18785 ? 127 GLU A OE1 1 
ATOM   961  O OE2 . GLU A 1 133 ? 32.49088 -7.60246  -92.34556  1.000 268.27334 ? 127 GLU A OE2 1 
ATOM   962  N N   . ARG A 1 134 ? 36.34873 -12.66374 -90.28769  1.000 258.54705 ? 128 ARG A N   1 
ATOM   963  C CA  . ARG A 1 134 ? 36.52942 -14.03012 -89.82520  1.000 260.21842 ? 128 ARG A CA  1 
ATOM   964  C C   . ARG A 1 134 ? 37.96210 -14.48218 -90.07411  1.000 268.60407 ? 128 ARG A C   1 
ATOM   965  O O   . ARG A 1 134 ? 38.61291 -14.04401 -91.02739  1.000 262.38435 ? 128 ARG A O   1 
ATOM   966  C CB  . ARG A 1 134 ? 35.55062 -14.97634 -90.52460  1.000 247.26829 ? 128 ARG A CB  1 
ATOM   967  C CG  . ARG A 1 134 ? 34.10099 -14.75697 -90.13111  1.000 249.62683 ? 128 ARG A CG  1 
ATOM   968  C CD  . ARG A 1 134 ? 33.15683 -15.29354 -91.18969  1.000 231.63115 ? 128 ARG A CD  1 
ATOM   969  N NE  . ARG A 1 134 ? 33.26080 -14.53860 -92.43233  1.000 229.83324 ? 128 ARG A NE  1 
ATOM   970  C CZ  . ARG A 1 134 ? 32.61445 -13.40648 -92.67485  1.000 243.77277 ? 128 ARG A CZ  1 
ATOM   971  N NH1 . ARG A 1 134 ? 31.80771 -12.86516 -91.77673  1.000 244.06928 ? 128 ARG A NH1 1 
ATOM   972  N NH2 . ARG A 1 134 ? 32.78255 -12.80149 -93.84718  1.000 250.79105 ? 128 ARG A NH2 1 
ATOM   973  N N   . CYS A 1 135 ? 38.44851 -15.36642 -89.20597  1.000 276.34701 ? 129 CYS A N   1 
ATOM   974  C CA  . CYS A 1 135 ? 39.82240 -15.83541 -89.30625  1.000 270.32878 ? 129 CYS A CA  1 
ATOM   975  C C   . CYS A 1 135 ? 39.98000 -17.13042 -88.52284  1.000 262.03566 ? 129 CYS A C   1 
ATOM   976  O O   . CYS A 1 135 ? 39.33055 -17.33448 -87.49375  1.000 245.71948 ? 129 CYS A O   1 
ATOM   977  C CB  . CYS A 1 135 ? 40.81057 -14.78149 -88.79135  1.000 251.88699 ? 129 CYS A CB  1 
ATOM   978  S SG  . CYS A 1 135 ? 40.61952 -14.36657 -87.04129  1.000 230.65056 ? 129 CYS A SG  1 
ATOM   979  N N   . TYR A 1 136 ? 40.84881 -18.00135 -89.03121  1.000 258.25988 ? 130 TYR A N   1 
ATOM   980  C CA  . TYR A 1 136 ? 41.27119 -19.21055 -88.34161  1.000 253.09858 ? 130 TYR A CA  1 
ATOM   981  C C   . TYR A 1 136 ? 42.77380 -19.14692 -88.10686  1.000 246.14577 ? 130 TYR A C   1 
ATOM   982  O O   . TYR A 1 136 ? 43.51342 -18.55556 -88.89733  1.000 253.13217 ? 130 TYR A O   1 
ATOM   983  C CB  . TYR A 1 136 ? 40.91598 -20.47616 -89.14418  1.000 259.82107 ? 130 TYR A CB  1 
ATOM   984  C CG  . TYR A 1 136 ? 41.60947 -21.73481 -88.65786  1.000 267.53763 ? 130 TYR A CG  1 
ATOM   985  C CD1 . TYR A 1 136 ? 41.14488 -22.42240 -87.54354  1.000 273.41715 ? 130 TYR A CD1 1 
ATOM   986  C CD2 . TYR A 1 136 ? 42.72916 -22.23425 -89.31427  1.000 257.24994 ? 130 TYR A CD2 1 
ATOM   987  C CE1 . TYR A 1 136 ? 41.77629 -23.57008 -87.09514  1.000 265.20042 ? 130 TYR A CE1 1 
ATOM   988  C CE2 . TYR A 1 136 ? 43.36700 -23.38105 -88.87247  1.000 256.87178 ? 130 TYR A CE2 1 
ATOM   989  C CZ  . TYR A 1 136 ? 42.88596 -24.04452 -87.76298  1.000 247.71224 ? 130 TYR A CZ  1 
ATOM   990  O OH  . TYR A 1 136 ? 43.51524 -25.18539 -87.31871  1.000 209.54972 ? 130 TYR A OH  1 
ATOM   991  N N   . VAL A 1 137 ? 43.22007 -19.74941 -87.00818  1.000 239.39199 ? 131 VAL A N   1 
ATOM   992  C CA  . VAL A 1 137 ? 44.64168 -19.80880 -86.68339  1.000 242.33263 ? 131 VAL A CA  1 
ATOM   993  C C   . VAL A 1 137 ? 44.89197 -21.05883 -85.85132  1.000 253.63270 ? 131 VAL A C   1 
ATOM   994  O O   . VAL A 1 137 ? 44.11754 -21.38747 -84.94782  1.000 250.95223 ? 131 VAL A O   1 
ATOM   995  C CB  . VAL A 1 137 ? 45.11267 -18.52819 -85.95562  1.000 230.94742 ? 131 VAL A CB  1 
ATOM   996  C CG1 . VAL A 1 137 ? 44.28397 -18.27729 -84.70305  1.000 252.13739 ? 131 VAL A CG1 1 
ATOM   997  C CG2 . VAL A 1 137 ? 46.59774 -18.61065 -85.62084  1.000 211.87353 ? 131 VAL A CG2 1 
ATOM   998  N N   . GLY A 1 138 ? 45.97188 -21.76517 -86.17463  1.000 253.82339 ? 132 GLY A N   1 
ATOM   999  C CA  . GLY A 1 138 ? 46.32554 -22.98116 -85.47102  1.000 243.98193 ? 132 GLY A CA  1 
ATOM   1000 C C   . GLY A 1 138 ? 47.50686 -23.68791 -86.10023  1.000 247.30853 ? 132 GLY A C   1 
ATOM   1001 O O   . GLY A 1 138 ? 48.51569 -23.05469 -86.42509  1.000 260.44886 ? 132 GLY A O   1 
ATOM   1002 N N   . ASN A 1 139 ? 47.39320 -25.00489 -86.28140  1.000 244.19846 ? 133 ASN A N   1 
ATOM   1003 C CA  . ASN A 1 139 ? 48.44966 -25.79070 -86.90467  1.000 248.90355 ? 133 ASN A CA  1 
ATOM   1004 C C   . ASN A 1 139 ? 47.93632 -26.65769 -88.04869  1.000 242.90813 ? 133 ASN A C   1 
ATOM   1005 O O   . ASN A 1 139 ? 48.69084 -27.49121 -88.56446  1.000 238.67413 ? 133 ASN A O   1 
ATOM   1006 C CB  . ASN A 1 139 ? 49.15672 -26.66286 -85.86110  1.000 233.03765 ? 133 ASN A CB  1 
ATOM   1007 C CG  . ASN A 1 139 ? 48.18524 -27.43591 -84.99423  1.000 221.01350 ? 133 ASN A CG  1 
ATOM   1008 O OD1 . ASN A 1 139 ? 47.64762 -28.46004 -85.41038  1.000 225.60925 ? 133 ASN A OD1 1 
ATOM   1009 N ND2 . ASN A 1 139 ? 47.96228 -26.95336 -83.77683  1.000 204.39848 ? 133 ASN A ND2 1 
ATOM   1010 N N   . ALA A 1 140 ? 46.68122 -26.48516 -88.45874  1.000 230.66535 ? 134 ALA A N   1 
ATOM   1011 C CA  . ALA A 1 140 ? 46.12129 -27.21195 -89.59688  1.000 245.30373 ? 134 ALA A CA  1 
ATOM   1012 C C   . ALA A 1 140 ? 46.54362 -26.49612 -90.87257  1.000 245.74376 ? 134 ALA A C   1 
ATOM   1013 O O   . ALA A 1 140 ? 45.85346 -25.60528 -91.37074  1.000 248.52487 ? 134 ALA A O   1 
ATOM   1014 C CB  . ALA A 1 140 ? 44.60475 -27.30661 -89.48675  1.000 241.30874 ? 134 ALA A CB  1 
ATOM   1015 N N   . SER A 1 141 ? 47.70054 -26.88533 -91.40440  1.000 240.24967 ? 135 SER A N   1 
ATOM   1016 C CA  . SER A 1 141 ? 48.20612 -26.28565 -92.62948  1.000 243.26233 ? 135 SER A CA  1 
ATOM   1017 C C   . SER A 1 141 ? 47.27709 -26.60130 -93.80117  1.000 258.15570 ? 135 SER A C   1 
ATOM   1018 O O   . SER A 1 141 ? 46.39278 -27.45879 -93.71903  1.000 255.91905 ? 135 SER A O   1 
ATOM   1019 C CB  . SER A 1 141 ? 49.61991 -26.78466 -92.92794  1.000 249.60917 ? 135 SER A CB  1 
ATOM   1020 O OG  . SER A 1 141 ? 50.49863 -26.51693 -91.84999  1.000 239.44890 ? 135 SER A OG  1 
ATOM   1021 N N   . PHE A 1 142 ? 47.48883 -25.89466 -94.91267  1.000 258.39228 ? 136 PHE A N   1 
ATOM   1022 C CA  . PHE A 1 142 ? 46.68811 -26.13619 -96.10729  1.000 253.15222 ? 136 PHE A CA  1 
ATOM   1023 C C   . PHE A 1 142 ? 47.11870 -27.44106 -96.76731  1.000 267.16331 ? 136 PHE A C   1 
ATOM   1024 O O   . PHE A 1 142 ? 47.67172 -27.44359 -97.87287  1.000 258.30708 ? 136 PHE A O   1 
ATOM   1025 C CB  . PHE A 1 142 ? 46.79408 -24.96698 -97.09120  1.000 254.10586 ? 136 PHE A CB  1 
ATOM   1026 C CG  . PHE A 1 142 ? 45.63834 -24.87957 -98.05810  1.000 261.20471 ? 136 PHE A CG  1 
ATOM   1027 C CD1 . PHE A 1 142 ? 44.61045 -25.80924 -98.01730  1.000 258.56678 ? 136 PHE A CD1 1 
ATOM   1028 C CD2 . PHE A 1 142 ? 45.58020 -23.86969 -99.00569  1.000 258.89338 ? 136 PHE A CD2 1 
ATOM   1029 C CE1 . PHE A 1 142 ? 43.54879 -25.73535 -98.89882  1.000 245.70414 ? 136 PHE A CE1 1 
ATOM   1030 C CE2 . PHE A 1 142 ? 44.51901 -23.79126 -99.89179  1.000 245.55451 ? 136 PHE A CE2 1 
ATOM   1031 C CZ  . PHE A 1 142 ? 43.50275 -24.72568 -99.83695  1.000 231.27407 ? 136 PHE A CZ  1 
ATOM   1032 N N   . THR A 1 143 ? 46.87252 -28.55441 -96.08329  1.000 276.68481 ? 137 THR A N   1 
ATOM   1033 C CA  . THR A 1 143 ? 47.13030 -29.88357 -96.61035  1.000 266.75425 ? 137 THR A CA  1 
ATOM   1034 C C   . THR A 1 143 ? 45.90455 -30.75062 -96.37085  1.000 253.85218 ? 137 THR A C   1 
ATOM   1035 O O   . THR A 1 143 ? 45.19015 -30.58131 -95.37863  1.000 252.72249 ? 137 THR A O   1 
ATOM   1036 C CB  . THR A 1 143 ? 48.36433 -30.53979 -95.96131  1.000 262.85769 ? 137 THR A CB  1 
ATOM   1037 O OG1 . THR A 1 143 ? 48.22263 -30.53279 -94.53467  1.000 249.33425 ? 137 THR A OG1 1 
ATOM   1038 C CG2 . THR A 1 143 ? 49.63569 -29.80016 -96.34401  1.000 275.37367 ? 137 THR A CG2 1 
ATOM   1039 N N   . GLY A 1 144 ? 45.66026 -31.67864 -97.29704  1.000 255.20515 ? 138 GLY A N   1 
ATOM   1040 C CA  . GLY A 1 144 ? 44.54989 -32.59799 -97.12507  1.000 250.32008 ? 138 GLY A CA  1 
ATOM   1041 C C   . GLY A 1 144 ? 44.66304 -33.43079 -95.86427  1.000 264.76137 ? 138 GLY A C   1 
ATOM   1042 O O   . GLY A 1 144 ? 43.64874 -33.83634 -95.29029  1.000 258.69419 ? 138 GLY A O   1 
ATOM   1043 N N   . GLY A 1 145 ? 45.89085 -33.69442 -95.41368  1.000 291.86482 ? 139 GLY A N   1 
ATOM   1044 C CA  . GLY A 1 145 ? 46.06720 -34.45022 -94.18434  1.000 293.92632 ? 139 GLY A CA  1 
ATOM   1045 C C   . GLY A 1 145 ? 45.65042 -33.65973 -92.95817  1.000 289.17343 ? 139 GLY A C   1 
ATOM   1046 O O   . GLY A 1 145 ? 44.91849 -34.16008 -92.09934  1.000 293.58433 ? 139 GLY A O   1 
ATOM   1047 N N   . SER A 1 146 ? 46.10475 -32.40854 -92.86448  1.000 255.15325 ? 140 SER A N   1 
ATOM   1048 C CA  . SER A 1 146 ? 45.77425 -31.54399 -91.73865  1.000 247.75859 ? 140 SER A CA  1 
ATOM   1049 C C   . SER A 1 146 ? 44.28980 -31.19332 -91.68005  1.000 237.23237 ? 140 SER A C   1 
ATOM   1050 O O   . SER A 1 146 ? 43.83691 -30.63399 -90.67114  1.000 230.70973 ? 140 SER A O   1 
ATOM   1051 C CB  . SER A 1 146 ? 46.62911 -30.27394 -91.80527  1.000 233.11244 ? 140 SER A CB  1 
ATOM   1052 O OG  . SER A 1 146 ? 48.01303 -30.59365 -91.81161  1.000 228.54264 ? 140 SER A OG  1 
ATOM   1053 N N   . ILE A 1 147 ? 43.52379 -31.50534 -92.72522  1.000 233.87822 ? 141 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 147 ? 42.08390 -31.32507 -92.70306  1.000 219.15841 ? 141 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 147 ? 41.34855 -32.62936 -92.41065  1.000 230.79807 ? 141 ILE A C   1 
ATOM   1056 O O   . ILE A 1 147 ? 40.27933 -32.59697 -91.79090  1.000 222.16627 ? 141 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 147 ? 41.59154 -30.70712 -94.03090  1.000 202.51350 ? 141 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 147 ? 42.33419 -29.39388 -94.31094  1.000 228.63530 ? 141 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 147 ? 40.08177 -30.45009 -93.99703  1.000 187.54811 ? 141 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 147 ? 41.99505 -28.76567 -95.65115  1.000 253.23529 ? 141 ILE A CD1 1 
ATOM   1061 N N   . HIS A 1 148 ? 41.90526 -33.77825 -92.79897  1.000 239.89373 ? 142 HIS A N   1 
ATOM   1062 C CA  . HIS A 1 148 ? 41.17141 -35.03976 -92.76612  1.000 246.32711 ? 142 HIS A CA  1 
ATOM   1063 C C   . HIS A 1 148 ? 41.84091 -36.09128 -91.89757  1.000 243.83608 ? 142 HIS A C   1 
ATOM   1064 O O   . HIS A 1 148 ? 41.19195 -36.64616 -91.00400  1.000 244.17988 ? 142 HIS A O   1 
ATOM   1065 C CB  . HIS A 1 148 ? 40.99672 -35.57459 -94.19890  1.000 250.83886 ? 142 HIS A CB  1 
ATOM   1066 C CG  . HIS A 1 148 ? 39.96981 -36.66457 -94.34784  1.000 259.94667 ? 142 HIS A CG  1 
ATOM   1067 N ND1 . HIS A 1 148 ? 39.21919 -36.80326 -95.49466  1.000 269.65063 ? 142 HIS A ND1 1 
ATOM   1068 C CD2 . HIS A 1 148 ? 39.60085 -37.68767 -93.53684  1.000 261.14977 ? 142 HIS A CD2 1 
ATOM   1069 C CE1 . HIS A 1 148 ? 38.41521 -37.84442 -95.37699  1.000 276.22894 ? 142 HIS A CE1 1 
ATOM   1070 N NE2 . HIS A 1 148 ? 38.62705 -38.40097 -94.19828  1.000 275.73278 ? 142 HIS A NE2 1 
ATOM   1071 N N   . THR A 1 149 ? 43.12528 -36.38518 -92.13210  1.000 244.79490 ? 143 THR A N   1 
ATOM   1072 C CA  . THR A 1 149 ? 43.79152 -37.52195 -91.50754  1.000 236.02977 ? 143 THR A CA  1 
ATOM   1073 C C   . THR A 1 149 ? 44.78496 -37.14932 -90.41475  1.000 224.23734 ? 143 THR A C   1 
ATOM   1074 O O   . THR A 1 149 ? 45.13293 -38.01320 -89.60305  1.000 219.64935 ? 143 THR A O   1 
ATOM   1075 C CB  . THR A 1 149 ? 44.52303 -38.35577 -92.57127  1.000 242.46872 ? 143 THR A CB  1 
ATOM   1076 O OG1 . THR A 1 149 ? 45.51708 -37.54618 -93.20959  1.000 259.56076 ? 143 THR A OG1 1 
ATOM   1077 C CG2 . THR A 1 149 ? 43.54308 -38.85450 -93.62689  1.000 242.04697 ? 143 THR A CG2 1 
ATOM   1078 N N   . ILE A 1 150 ? 45.24265 -35.90241 -90.36252  1.000 236.82993 ? 144 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 150 ? 46.20561 -35.46462 -89.35797  1.000 238.32400 ? 144 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 150 ? 45.47051 -34.68349 -88.27843  1.000 242.94463 ? 144 ILE A C   1 
ATOM   1081 O O   . ILE A 1 150 ? 44.74356 -33.72690 -88.57681  1.000 264.34100 ? 144 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 150 ? 47.32685 -34.61724 -89.98401  1.000 248.54457 ? 144 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 150 ? 48.06900 -35.41841 -91.05680  1.000 247.72605 ? 144 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 150 ? 48.30011 -34.15001 -88.90744  1.000 232.70571 ? 144 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 150 ? 49.17368 -34.64532 -91.74724  1.000 248.52620 ? 144 ILE A CD1 1 
ATOM   1086 N N   . LYS A 1 151 ? 45.66037 -35.08784 -87.02403  1.000 221.63734 ? 145 LYS A N   1 
ATOM   1087 C CA  . LYS A 1 151 ? 45.05194 -34.37633 -85.90809  1.000 229.72946 ? 145 LYS A CA  1 
ATOM   1088 C C   . LYS A 1 151 ? 45.66221 -32.98679 -85.78113  1.000 235.65574 ? 145 LYS A C   1 
ATOM   1089 O O   . LYS A 1 151 ? 46.88669 -32.83036 -85.80683  1.000 234.04416 ? 145 LYS A O   1 
ATOM   1090 C CB  . LYS A 1 151 ? 45.24065 -35.15583 -84.60729  1.000 229.46191 ? 145 LYS A CB  1 
ATOM   1091 C CG  . LYS A 1 151 ? 44.63938 -34.46945 -83.38780  1.000 235.22201 ? 145 LYS A CG  1 
ATOM   1092 C CD  . LYS A 1 151 ? 44.99297 -35.19912 -82.10254  1.000 225.93571 ? 145 LYS A CD  1 
ATOM   1093 C CE  . LYS A 1 151 ? 44.35060 -34.53130 -80.89650  1.000 206.47861 ? 145 LYS A CE  1 
ATOM   1094 N NZ  . LYS A 1 151 ? 44.75574 -33.10409 -80.76582  1.000 173.16357 ? 145 LYS A NZ  1 
ATOM   1095 N N   . THR A 1 152 ? 44.80732 -31.97374 -85.65929  1.000 241.27341 ? 146 THR A N   1 
ATOM   1096 C CA  . THR A 1 152 ? 45.24506 -30.59141 -85.52530  1.000 240.41896 ? 146 THR A CA  1 
ATOM   1097 C C   . THR A 1 152 ? 44.50598 -29.93789 -84.36392  1.000 221.45211 ? 146 THR A C   1 
ATOM   1098 O O   . THR A 1 152 ? 43.72748 -30.57799 -83.65017  1.000 192.35883 ? 146 THR A O   1 
ATOM   1099 C CB  . THR A 1 152 ? 45.01749 -29.79553 -86.81854  1.000 245.09422 ? 146 THR A CB  1 
ATOM   1100 O OG1 . THR A 1 152 ? 43.61178 -29.64689 -87.05406  1.000 237.77628 ? 146 THR A OG1 1 
ATOM   1101 C CG2 . THR A 1 152 ? 45.66059 -30.49853 -88.00693  1.000 245.49282 ? 146 THR A CG2 1 
ATOM   1102 N N   . LEU A 1 153 ? 44.75971 -28.64403 -84.18082  1.000 224.09904 ? 147 LEU A N   1 
ATOM   1103 C CA  . LEU A 1 153 ? 44.11186 -27.87099 -83.12469  1.000 220.36793 ? 147 LEU A CA  1 
ATOM   1104 C C   . LEU A 1 153 ? 44.24683 -26.39654 -83.46341  1.000 219.13651 ? 147 LEU A C   1 
ATOM   1105 O O   . LEU A 1 153 ? 45.36519 -25.90410 -83.64436  1.000 213.21720 ? 147 LEU A O   1 
ATOM   1106 C CB  . LEU A 1 153 ? 44.73274 -28.17267 -81.76164  1.000 220.56841 ? 147 LEU A CB  1 
ATOM   1107 C CG  . LEU A 1 153 ? 44.13191 -27.40932 -80.58069  1.000 235.24709 ? 147 LEU A CG  1 
ATOM   1108 C CD1 . LEU A 1 153 ? 42.64300 -27.69691 -80.45923  1.000 224.44627 ? 147 LEU A CD1 1 
ATOM   1109 C CD2 . LEU A 1 153 ? 44.85683 -27.75946 -79.29169  1.000 235.06665 ? 147 LEU A CD2 1 
ATOM   1110 N N   . GLY A 1 154 ? 43.11877 -25.69741 -83.54948  1.000 227.66668 ? 148 GLY A N   1 
ATOM   1111 C CA  . GLY A 1 154 ? 43.12619 -24.28297 -83.86368  1.000 232.22060 ? 148 GLY A CA  1 
ATOM   1112 C C   . GLY A 1 154 ? 41.99853 -23.52458 -83.19551  1.000 237.25105 ? 148 GLY A C   1 
ATOM   1113 O O   . GLY A 1 154 ? 41.26020 -24.08633 -82.38076  1.000 229.80555 ? 148 GLY A O   1 
ATOM   1114 N N   . VAL A 1 155 ? 41.85878 -22.24277 -83.52698  1.000 245.08519 ? 149 VAL A N   1 
ATOM   1115 C CA  . VAL A 1 155 ? 40.83672 -21.37922 -82.94856  1.000 238.33822 ? 149 VAL A CA  1 
ATOM   1116 C C   . VAL A 1 155 ? 40.18789 -20.57500 -84.06708  1.000 250.72879 ? 149 VAL A C   1 
ATOM   1117 O O   . VAL A 1 155 ? 40.87878 -20.04999 -84.94735  1.000 255.89687 ? 149 VAL A O   1 
ATOM   1118 C CB  . VAL A 1 155 ? 41.42487 -20.43797 -81.87368  1.000 234.14714 ? 149 VAL A CB  1 
ATOM   1119 C CG1 . VAL A 1 155 ? 40.33849 -19.55787 -81.28546  1.000 246.52396 ? 149 VAL A CG1 1 
ATOM   1120 C CG2 . VAL A 1 155 ? 42.11729 -21.23402 -80.77492  1.000 232.85116 ? 149 VAL A CG2 1 
ATOM   1121 N N   . TYR A 1 156 ? 38.85959 -20.48232 -84.03421  1.000 250.16841 ? 150 TYR A N   1 
ATOM   1122 C CA  . TYR A 1 156 ? 38.09363 -19.69721 -84.99256  1.000 252.28228 ? 150 TYR A CA  1 
ATOM   1123 C C   . TYR A 1 156 ? 37.38551 -18.55856 -84.27216  1.000 256.71351 ? 150 TYR A C   1 
ATOM   1124 O O   . TYR A 1 156 ? 36.93088 -18.71871 -83.13484  1.000 253.10741 ? 150 TYR A O   1 
ATOM   1125 C CB  . TYR A 1 156 ? 37.06930 -20.56654 -85.73441  1.000 268.19429 ? 150 TYR A CB  1 
ATOM   1126 C CG  . TYR A 1 156 ? 36.06066 -19.78006 -86.54470  1.000 287.12942 ? 150 TYR A CG  1 
ATOM   1127 C CD1 . TYR A 1 156 ? 36.40195 -19.23376 -87.77568  1.000 276.89503 ? 150 TYR A CD1 1 
ATOM   1128 C CD2 . TYR A 1 156 ? 34.76487 -19.58843 -86.07988  1.000 296.13693 ? 150 TYR A CD2 1 
ATOM   1129 C CE1 . TYR A 1 156 ? 35.48242 -18.51455 -88.51896  1.000 272.59504 ? 150 TYR A CE1 1 
ATOM   1130 C CE2 . TYR A 1 156 ? 33.83919 -18.87122 -86.81569  1.000 290.53685 ? 150 TYR A CE2 1 
ATOM   1131 C CZ  . TYR A 1 156 ? 34.20307 -18.33709 -88.03405  1.000 272.40392 ? 150 TYR A CZ  1 
ATOM   1132 O OH  . TYR A 1 156 ? 33.28422 -17.62361 -88.76927  1.000 244.18271 ? 150 TYR A OH  1 
ATOM   1133 N N   . SER A 1 157 ? 37.29211 -17.40935 -84.94037  1.000 269.28285 ? 151 SER A N   1 
ATOM   1134 C CA  . SER A 1 157 ? 36.64058 -16.24138 -84.36063  1.000 272.99615 ? 151 SER A CA  1 
ATOM   1135 C C   . SER A 1 157 ? 36.13788 -15.34237 -85.47915  1.000 271.91742 ? 151 SER A C   1 
ATOM   1136 O O   . SER A 1 157 ? 36.88369 -15.04068 -86.41592  1.000 251.86280 ? 151 SER A O   1 
ATOM   1137 C CB  . SER A 1 157 ? 37.60064 -15.46969 -83.44837  1.000 253.64545 ? 151 SER A CB  1 
ATOM   1138 O OG  . SER A 1 157 ? 36.97641 -14.31699 -82.90991  1.000 254.33287 ? 151 SER A OG  1 
ATOM   1139 N N   . ASP A 1 158 ? 34.87742 -14.91709 -85.37632  1.000 277.51226 ? 152 ASP A N   1 
ATOM   1140 C CA  . ASP A 1 158 ? 34.27929 -13.98119 -86.32032  1.000 279.75564 ? 152 ASP A CA  1 
ATOM   1141 C C   . ASP A 1 158 ? 34.35272 -12.54038 -85.82469  1.000 279.88039 ? 152 ASP A C   1 
ATOM   1142 O O   . ASP A 1 158 ? 33.48404 -11.72388 -86.15114  1.000 260.31235 ? 152 ASP A O   1 
ATOM   1143 C CB  . ASP A 1 158 ? 32.83009 -14.37234 -86.61408  1.000 279.86648 ? 152 ASP A CB  1 
ATOM   1144 C CG  . ASP A 1 158 ? 31.98045 -14.46463 -85.35907  1.000 277.84852 ? 152 ASP A CG  1 
ATOM   1145 O OD1 . ASP A 1 158 ? 32.54233 -14.39087 -84.24603  1.000 278.67217 ? 152 ASP A OD1 1 
ATOM   1146 O OD2 . ASP A 1 158 ? 30.74629 -14.61049 -85.48728  1.000 272.94750 ? 152 ASP A OD2 1 
ATOM   1147 N N   . TYR A 1 159 ? 35.37818 -12.21397 -85.04002  1.000 280.84150 ? 153 TYR A N   1 
ATOM   1148 C CA  . TYR A 1 159 ? 35.53228 -10.87148 -84.49778  1.000 266.85087 ? 153 TYR A CA  1 
ATOM   1149 C C   . TYR A 1 159 ? 36.38547 -10.03805 -85.44423  1.000 259.88722 ? 153 TYR A C   1 
ATOM   1150 O O   . TYR A 1 159 ? 37.54918 -10.39024 -85.68084  1.000 267.56091 ? 153 TYR A O   1 
ATOM   1151 C CB  . TYR A 1 159 ? 36.16830 -10.92227 -83.11884  1.000 256.61641 ? 153 TYR A CB  1 
ATOM   1152 C CG  . TYR A 1 159 ? 35.96485 -9.66706  -82.30360  1.000 271.15377 ? 153 TYR A CG  1 
ATOM   1153 C CD1 . TYR A 1 159 ? 34.69457 -9.13900  -82.11423  1.000 297.41337 ? 153 TYR A CD1 1 
ATOM   1154 C CD2 . TYR A 1 159 ? 37.03817 -9.01888  -81.70975  1.000 277.50553 ? 153 TYR A CD2 1 
ATOM   1155 C CE1 . TYR A 1 159 ? 34.50063 -7.99253  -81.36745  1.000 312.26822 ? 153 TYR A CE1 1 
ATOM   1156 C CE2 . TYR A 1 159 ? 36.85255 -7.87349  -80.96008  1.000 297.58559 ? 153 TYR A CE2 1 
ATOM   1157 C CZ  . TYR A 1 159 ? 35.58364 -7.36434  -80.79186  1.000 300.99393 ? 153 TYR A CZ  1 
ATOM   1158 O OH  . TYR A 1 159 ? 35.39835 -6.22326  -80.04499  1.000 295.53968 ? 153 TYR A OH  1 
ATOM   1159 N N   . PRO A 1 160 ? 35.85808 -8.95512  -86.00927  1.000 262.42922 ? 154 PRO A N   1 
ATOM   1160 C CA  . PRO A 1 160 ? 36.60746 -8.18609  -87.01739  1.000 261.05542 ? 154 PRO A CA  1 
ATOM   1161 C C   . PRO A 1 160 ? 37.92212 -7.63095  -86.48794  1.000 263.21008 ? 154 PRO A C   1 
ATOM   1162 O O   . PRO A 1 160 ? 38.95027 -7.76200  -87.16980  1.000 244.67905 ? 154 PRO A O   1 
ATOM   1163 C CB  . PRO A 1 160 ? 35.62951 -7.06485  -87.40447  1.000 255.43608 ? 154 PRO A CB  1 
ATOM   1164 C CG  . PRO A 1 160 ? 34.28333 -7.65724  -87.15184  1.000 260.35061 ? 154 PRO A CG  1 
ATOM   1165 C CD  . PRO A 1 160 ? 34.44112 -8.55224  -85.94789  1.000 264.55540 ? 154 PRO A CD  1 
ATOM   1166 N N   . PRO A 1 161 ? 37.95741 -6.99434  -85.30426  1.000 279.34942 ? 155 PRO A N   1 
ATOM   1167 C CA  . PRO A 1 161 ? 39.24133 -6.42361  -84.85461  1.000 278.67050 ? 155 PRO A CA  1 
ATOM   1168 C C   . PRO A 1 161 ? 40.33552 -7.45794  -84.65701  1.000 252.37354 ? 155 PRO A C   1 
ATOM   1169 O O   . PRO A 1 161 ? 41.51529 -7.14334  -84.85887  1.000 248.04604 ? 155 PRO A O   1 
ATOM   1170 C CB  . PRO A 1 161 ? 38.87769 -5.73129  -83.53308  1.000 270.55497 ? 155 PRO A CB  1 
ATOM   1171 C CG  . PRO A 1 161 ? 37.42844 -5.47675  -83.62630  1.000 262.79718 ? 155 PRO A CG  1 
ATOM   1172 C CD  . PRO A 1 161 ? 36.88530 -6.66627  -84.34449  1.000 275.12895 ? 155 PRO A CD  1 
ATOM   1173 N N   . LEU A 1 162 ? 39.98560 -8.68395  -84.26725  1.000 228.82798 ? 156 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 162 ? 40.99744 -9.72128  -84.11325  1.000 234.80623 ? 156 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 162 ? 41.44711 -10.27777 -85.45801  1.000 234.86481 ? 156 LEU A C   1 
ATOM   1176 O O   . LEU A 1 162 ? 42.62196 -10.62762 -85.61773  1.000 223.97779 ? 156 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 162 ? 40.46494 -10.84711 -83.22600  1.000 265.91154 ? 156 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 162 ? 41.49091 -11.87138 -82.73986  1.000 272.53245 ? 156 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 162 ? 42.54152 -11.20110 -81.86748  1.000 270.33583 ? 156 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 162 ? 40.80282 -12.99768 -81.98712  1.000 254.14038 ? 156 LEU A CD2 1 
ATOM   1181 N N   . ALA A 1 163 ? 40.53636 -10.36233 -86.43119  1.000 237.48839 ? 157 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 163 ? 40.90909 -10.85362 -87.75304  1.000 234.04396 ? 157 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 163 ? 41.72565 -9.82691  -88.52490  1.000 227.54290 ? 157 ALA A C   1 
ATOM   1184 O O   . ALA A 1 163 ? 42.60528 -10.20028 -89.30962  1.000 213.69651 ? 157 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 163 ? 39.65912 -11.23864 -88.54378  1.000 246.37566 ? 157 ALA A CB  1 
ATOM   1186 N N   . THR A 1 164 ? 41.44880 -8.53671  -88.32132  1.000 238.48868 ? 158 THR A N   1 
ATOM   1187 C CA  . THR A 1 164 ? 42.21376 -7.49875  -89.00435  1.000 260.40589 ? 158 THR A CA  1 
ATOM   1188 C C   . THR A 1 164 ? 43.65953 -7.47598  -88.52437  1.000 262.44492 ? 158 THR A C   1 
ATOM   1189 O O   . THR A 1 164 ? 44.58188 -7.27067  -89.32248  1.000 271.99839 ? 158 THR A O   1 
ATOM   1190 C CB  . THR A 1 164 ? 41.55508 -6.13495  -88.79253  1.000 257.32312 ? 158 THR A CB  1 
ATOM   1191 O OG1 . THR A 1 164 ? 40.18394 -6.19573  -89.20501  1.000 236.89627 ? 158 THR A OG1 1 
ATOM   1192 C CG2 . THR A 1 164 ? 42.27168 -5.06238  -89.60096  1.000 259.17998 ? 158 THR A CG2 1 
ATOM   1193 N N   . ASP A 1 165 ? 43.87788 -7.68861  -87.22408  1.000 253.10320 ? 159 ASP A N   1 
ATOM   1194 C CA  . ASP A 1 165 ? 45.24113 -7.74634  -86.70951  1.000 263.04862 ? 159 ASP A CA  1 
ATOM   1195 C C   . ASP A 1 165 ? 45.98408 -8.96403  -87.24368  1.000 266.24712 ? 159 ASP A C   1 
ATOM   1196 O O   . ASP A 1 165 ? 47.20869 -8.91951  -87.40719  1.000 283.22907 ? 159 ASP A O   1 
ATOM   1197 C CB  . ASP A 1 165 ? 45.22761 -7.75414  -85.18076  1.000 270.12023 ? 159 ASP A CB  1 
ATOM   1198 C CG  . ASP A 1 165 ? 46.50636 -7.19805  -84.58347  1.000 283.73875 ? 159 ASP A CG  1 
ATOM   1199 O OD1 . ASP A 1 165 ? 47.30988 -6.60940  -85.33729  1.000 279.57476 ? 159 ASP A OD1 1 
ATOM   1200 O OD2 . ASP A 1 165 ? 46.70821 -7.34905  -83.36016  1.000 291.11253 ? 159 ASP A OD2 1 
ATOM   1201 N N   . LEU A 1 166 ? 45.26527 -10.05504 -87.52131  1.000 247.36653 ? 160 LEU A N   1 
ATOM   1202 C CA  . LEU A 1 166 ? 45.89108 -11.20760 -88.15902  1.000 243.16284 ? 160 LEU A CA  1 
ATOM   1203 C C   . LEU A 1 166 ? 46.15001 -10.95009 -89.63764  1.000 241.94208 ? 160 LEU A C   1 
ATOM   1204 O O   . LEU A 1 166 ? 47.09023 -11.51376 -90.20961  1.000 238.01855 ? 160 LEU A O   1 
ATOM   1205 C CB  . LEU A 1 166 ? 45.01689 -12.44820 -87.97668  1.000 231.76954 ? 160 LEU A CB  1 
ATOM   1206 C CG  . LEU A 1 166 ? 45.58760 -13.77026 -88.49238  1.000 231.86640 ? 160 LEU A CG  1 
ATOM   1207 C CD1 . LEU A 1 166 ? 46.89019 -14.10807 -87.78211  1.000 237.59008 ? 160 LEU A CD1 1 
ATOM   1208 C CD2 . LEU A 1 166 ? 44.57526 -14.89061 -88.32702  1.000 224.54684 ? 160 LEU A CD2 1 
ATOM   1209 N N   . ARG A 1 167 ? 45.33106 -10.10549 -90.27018  1.000 234.07080 ? 161 ARG A N   1 
ATOM   1210 C CA  . ARG A 1 167 ? 45.57998 -9.73237  -91.65807  1.000 238.03175 ? 161 ARG A CA  1 
ATOM   1211 C C   . ARG A 1 167 ? 46.85526 -8.90958  -91.79146  1.000 264.51344 ? 161 ARG A C   1 
ATOM   1212 O O   . ARG A 1 167 ? 47.55235 -9.01109  -92.80752  1.000 266.33209 ? 161 ARG A O   1 
ATOM   1213 C CB  . ARG A 1 167 ? 44.37750 -8.96647  -92.21668  1.000 253.01208 ? 161 ARG A CB  1 
ATOM   1214 C CG  . ARG A 1 167 ? 44.43667 -8.67098  -93.71335  1.000 267.38046 ? 161 ARG A CG  1 
ATOM   1215 C CD  . ARG A 1 167 ? 44.98989 -7.27926  -93.99803  1.000 274.71889 ? 161 ARG A CD  1 
ATOM   1216 N NE  . ARG A 1 167 ? 44.19242 -6.23187  -93.37082  1.000 270.25535 ? 161 ARG A NE  1 
ATOM   1217 C CZ  . ARG A 1 167 ? 44.50607 -4.94331  -93.38102  1.000 277.97554 ? 161 ARG A CZ  1 
ATOM   1218 N NH1 . ARG A 1 167 ? 45.60243 -4.50314  -93.97658  1.000 282.77130 ? 161 ARG A NH1 1 
ATOM   1219 N NH2 . ARG A 1 167 ? 43.70053 -4.07455  -92.77662  1.000 283.14374 ? 161 ARG A NH2 1 
ATOM   1220 N N   . ARG A 1 168 ? 47.17557 -8.09176  -90.78389  1.000 271.75784 ? 162 ARG A N   1 
ATOM   1221 C CA  . ARG A 1 168 ? 48.43469 -7.35442  -90.80551  1.000 272.59949 ? 162 ARG A CA  1 
ATOM   1222 C C   . ARG A 1 168 ? 49.63181 -8.29336  -90.73282  1.000 268.42300 ? 162 ARG A C   1 
ATOM   1223 O O   . ARG A 1 168 ? 50.70874 -7.96354  -91.24335  1.000 257.29170 ? 162 ARG A O   1 
ATOM   1224 C CB  . ARG A 1 168 ? 48.47582 -6.34041  -89.66067  1.000 271.70188 ? 162 ARG A CB  1 
ATOM   1225 C CG  . ARG A 1 168 ? 47.75994 -5.03065  -89.96703  1.000 290.94267 ? 162 ARG A CG  1 
ATOM   1226 C CD  . ARG A 1 168 ? 47.90453 -4.02991  -88.82842  1.000 293.15638 ? 162 ARG A CD  1 
ATOM   1227 N NE  . ARG A 1 168 ? 46.86404 -4.18504  -87.81895  1.000 286.96889 ? 162 ARG A NE  1 
ATOM   1228 C CZ  . ARG A 1 168 ? 45.74223 -3.47847  -87.78785  1.000 273.28081 ? 162 ARG A CZ  1 
ATOM   1229 N NH1 . ARG A 1 168 ? 45.48432 -2.55077  -88.69539  1.000 243.92418 ? 162 ARG A NH1 1 
ATOM   1230 N NH2 . ARG A 1 168 ? 44.85769 -3.70719  -86.82136  1.000 268.05731 ? 162 ARG A NH2 1 
ATOM   1231 N N   . ARG A 1 169 ? 49.46716 -9.46001  -90.10350  1.000 270.06546 ? 163 ARG A N   1 
ATOM   1232 C CA  . ARG A 1 169 ? 50.50975 -10.47783 -90.16036  1.000 260.24233 ? 163 ARG A CA  1 
ATOM   1233 C C   . ARG A 1 169 ? 50.65394 -11.03884 -91.56817  1.000 254.84608 ? 163 ARG A C   1 
ATOM   1234 O O   . ARG A 1 169 ? 51.76307 -11.39134 -91.98552  1.000 242.33362 ? 163 ARG A O   1 
ATOM   1235 C CB  . ARG A 1 169 ? 50.20550 -11.60599 -89.17424  1.000 255.31612 ? 163 ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 169 ? 49.86729 -11.14604 -87.76443  1.000 259.69937 ? 163 ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 169 ? 50.99414 -10.33119 -87.15402  1.000 273.38887 ? 163 ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 169 ? 50.82617 -10.16542 -85.71491  1.000 262.52322 ? 163 ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 169 ? 50.16495 -9.16720  -85.14525  1.000 250.85568 ? 163 ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 169 ? 49.59238 -8.21682  -85.86574  1.000 275.39230 ? 163 ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 169 ? 50.07565 -9.12167  -83.81899  1.000 219.71496 ? 163 ARG A NH2 1 
ATOM   1242 N N   . PHE A 1 170 ? 49.54635 -11.12906 -92.30906  1.000 258.92899 ? 164 PHE A N   1 
ATOM   1243 C CA  . PHE A 1 170 ? 49.60336 -11.60294 -93.68696  1.000 265.02347 ? 164 PHE A CA  1 
ATOM   1244 C C   . PHE A 1 170 ? 50.29147 -10.59384 -94.59702  1.000 262.11994 ? 164 PHE A C   1 
ATOM   1245 O O   . PHE A 1 170 ? 50.98807 -10.98683 -95.53978  1.000 256.21325 ? 164 PHE A O   1 
ATOM   1246 C CB  . PHE A 1 170 ? 48.18972 -11.90396 -94.19018  1.000 267.11319 ? 164 PHE A CB  1 
ATOM   1247 C CG  . PHE A 1 170 ? 48.14643 -12.54451 -95.54997  1.000 271.89123 ? 164 PHE A CG  1 
ATOM   1248 C CD1 . PHE A 1 170 ? 48.16084 -13.92328 -95.68075  1.000 264.32637 ? 164 PHE A CD1 1 
ATOM   1249 C CD2 . PHE A 1 170 ? 48.07742 -11.76892 -96.69630  1.000 279.66721 ? 164 PHE A CD2 1 
ATOM   1250 C CE1 . PHE A 1 170 ? 48.11524 -14.51608 -96.92856  1.000 260.53479 ? 164 PHE A CE1 1 
ATOM   1251 C CE2 . PHE A 1 170 ? 48.03359 -12.35553 -97.94674  1.000 280.11815 ? 164 PHE A CE2 1 
ATOM   1252 C CZ  . PHE A 1 170 ? 48.05223 -13.73057 -98.06312  1.000 270.17943 ? 164 PHE A CZ  1 
ATOM   1253 N N   . ASP A 1 171 ? 50.10984 -9.29681  -94.33410  1.000 279.18740 ? 165 ASP A N   1 
ATOM   1254 C CA  . ASP A 1 171 ? 50.74584 -8.27760  -95.16301  1.000 293.95909 ? 165 ASP A CA  1 
ATOM   1255 C C   . ASP A 1 171 ? 52.26014 -8.29252  -94.99402  1.000 284.34587 ? 165 ASP A C   1 
ATOM   1256 O O   . ASP A 1 171 ? 53.00018 -8.06728  -95.95884  1.000 296.28506 ? 165 ASP A O   1 
ATOM   1257 C CB  . ASP A 1 171 ? 50.18082 -6.89734  -94.82614  1.000 308.80040 ? 165 ASP A CB  1 
ATOM   1258 C CG  . ASP A 1 171 ? 48.69489 -6.78793  -95.11293  1.000 306.35714 ? 165 ASP A CG  1 
ATOM   1259 O OD1 . ASP A 1 171 ? 48.20952 -7.48755  -96.02665  1.000 325.75656 ? 165 ASP A OD1 1 
ATOM   1260 O OD2 . ASP A 1 171 ? 48.01230 -5.99945  -94.42536  1.000 313.41143 ? 165 ASP A OD2 1 
ATOM   1261 N N   . THR A 1 172 ? 52.74039 -8.55328  -93.77592  1.000 267.91513 ? 166 THR A N   1 
ATOM   1262 C CA  . THR A 1 172 ? 54.17996 -8.64065  -93.55795  1.000 264.83464 ? 166 THR A CA  1 
ATOM   1263 C C   . THR A 1 172 ? 54.77176 -9.87124  -94.23507  1.000 260.38927 ? 166 THR A C   1 
ATOM   1264 O O   . THR A 1 172 ? 55.90878 -9.82521  -94.71839  1.000 259.31009 ? 166 THR A O   1 
ATOM   1265 C CB  . THR A 1 172 ? 54.48493 -8.65347  -92.05819  1.000 257.47193 ? 166 THR A CB  1 
ATOM   1266 O OG1 . THR A 1 172 ? 53.83029 -7.54549  -91.42721  1.000 246.21249 ? 166 THR A OG1 1 
ATOM   1267 C CG2 . THR A 1 172 ? 55.98344 -8.54616  -91.81243  1.000 244.07587 ? 166 THR A CG2 1 
ATOM   1268 N N   . PHE A 1 173 ? 54.01448 -10.96934 -94.29558  1.000 252.41379 ? 167 PHE A N   1 
ATOM   1269 C CA  . PHE A 1 173 ? 54.50445 -12.18603 -94.93394  1.000 256.91651 ? 167 PHE A CA  1 
ATOM   1270 C C   . PHE A 1 173 ? 54.36171 -12.14345 -96.45112  1.000 253.32112 ? 167 PHE A C   1 
ATOM   1271 O O   . PHE A 1 173 ? 55.19442 -12.71961 -97.16037  1.000 241.63069 ? 167 PHE A O   1 
ATOM   1272 C CB  . PHE A 1 173 ? 53.76885 -13.40613 -94.37503  1.000 277.16227 ? 167 PHE A CB  1 
ATOM   1273 C CG  . PHE A 1 173 ? 54.18217 -13.77961 -92.97814  1.000 276.62865 ? 167 PHE A CG  1 
ATOM   1274 C CD1 . PHE A 1 173 ? 55.47884 -13.56151 -92.54222  1.000 268.59681 ? 167 PHE A CD1 1 
ATOM   1275 C CD2 . PHE A 1 173 ? 53.27335 -14.35023 -92.10145  1.000 284.97691 ? 167 PHE A CD2 1 
ATOM   1276 C CE1 . PHE A 1 173 ? 55.86166 -13.90591 -91.25839  1.000 258.07471 ? 167 PHE A CE1 1 
ATOM   1277 C CE2 . PHE A 1 173 ? 53.64983 -14.69613 -90.81625  1.000 261.58067 ? 167 PHE A CE2 1 
ATOM   1278 C CZ  . PHE A 1 173 ? 54.94556 -14.47345 -90.39467  1.000 251.59042 ? 167 PHE A CZ  1 
ATOM   1279 N N   . LYS A 1 174 ? 53.32276 -11.47783 -96.96584  1.000 261.12761 ? 168 LYS A N   1 
ATOM   1280 C CA  . LYS A 1 174 ? 53.12889 -11.41170 -98.41203  1.000 274.53255 ? 168 LYS A CA  1 
ATOM   1281 C C   . LYS A 1 174 ? 54.24446 -10.63193 -99.09606  1.000 262.08111 ? 168 LYS A C   1 
ATOM   1282 O O   . LYS A 1 174 ? 54.59390 -10.93108 -100.24400 1.000 273.56739 ? 168 LYS A O   1 
ATOM   1283 C CB  . LYS A 1 174 ? 51.77095 -10.78351 -98.73723  1.000 285.62819 ? 168 LYS A CB  1 
ATOM   1284 C CG  . LYS A 1 174 ? 51.46744 -10.68430 -100.23087 1.000 291.61410 ? 168 LYS A CG  1 
ATOM   1285 C CD  . LYS A 1 174 ? 50.28187 -9.76910  -100.51377 1.000 296.88800 ? 168 LYS A CD  1 
ATOM   1286 C CE  . LYS A 1 174 ? 50.08692 -9.56393  -102.01195 1.000 249.46905 ? 168 LYS A CE  1 
ATOM   1287 N NZ  . LYS A 1 174 ? 48.99294 -8.59845  -102.32051 1.000 223.46295 ? 168 LYS A NZ  1 
ATOM   1288 N N   . ALA A 1 175 ? 54.81868 -9.64098  -98.40912  1.000 246.17945 ? 169 ALA A N   1 
ATOM   1289 C CA  . ALA A 1 175 ? 55.86025 -8.82112  -99.01857  1.000 263.26399 ? 169 ALA A CA  1 
ATOM   1290 C C   . ALA A 1 175 ? 57.09048 -9.64308  -99.38004  1.000 275.53687 ? 169 ALA A C   1 
ATOM   1291 O O   . ALA A 1 175 ? 57.83521 -9.27447  -100.29555 1.000 295.93499 ? 169 ALA A O   1 
ATOM   1292 C CB  . ALA A 1 175 ? 56.24048 -7.67814  -98.07921  1.000 275.18784 ? 169 ALA A CB  1 
ATOM   1293 N N   . PHE A 1 176 ? 57.32064 -10.75490 -98.68094  1.000 262.91259 ? 170 PHE A N   1 
ATOM   1294 C CA  . PHE A 1 176 ? 58.44999 -11.63736 -98.97208  1.000 261.96191 ? 170 PHE A CA  1 
ATOM   1295 C C   . PHE A 1 176 ? 58.04290 -12.59503 -100.08707 1.000 255.87058 ? 170 PHE A C   1 
ATOM   1296 O O   . PHE A 1 176 ? 57.61822 -13.73073 -99.86222  1.000 261.19679 ? 170 PHE A O   1 
ATOM   1297 C CB  . PHE A 1 176 ? 58.88901 -12.38278 -97.71956  1.000 251.75206 ? 170 PHE A CB  1 
ATOM   1298 C CG  . PHE A 1 176 ? 59.48442 -11.49470 -96.67124  1.000 267.85227 ? 170 PHE A CG  1 
ATOM   1299 C CD1 . PHE A 1 176 ? 58.67996 -10.88080 -95.72719  1.000 269.93697 ? 170 PHE A CD1 1 
ATOM   1300 C CD2 . PHE A 1 176 ? 60.84868 -11.26465 -96.63556  1.000 263.65856 ? 170 PHE A CD2 1 
ATOM   1301 C CE1 . PHE A 1 176 ? 59.22519 -10.05796 -94.76357  1.000 274.80763 ? 170 PHE A CE1 1 
ATOM   1302 C CE2 . PHE A 1 176 ? 61.40028 -10.44352 -95.67423  1.000 264.77983 ? 170 PHE A CE2 1 
ATOM   1303 C CZ  . PHE A 1 176 ? 60.58723 -9.83847  -94.73811  1.000 271.55704 ? 170 PHE A CZ  1 
ATOM   1304 N N   . ASN A 1 177 ? 58.17585 -12.11537 -101.31883 1.000 252.66876 ? 171 ASN A N   1 
ATOM   1305 C CA  . ASN A 1 177 ? 57.86563 -12.89578 -102.50580 1.000 259.41443 ? 171 ASN A CA  1 
ATOM   1306 C C   . ASN A 1 177 ? 59.09855 -12.97660 -103.39226 1.000 262.32350 ? 171 ASN A C   1 
ATOM   1307 O O   . ASN A 1 177 ? 59.81637 -11.98671 -103.56685 1.000 267.00265 ? 171 ASN A O   1 
ATOM   1308 C CB  . ASN A 1 177 ? 56.69585 -12.28361 -103.28388 1.000 265.03501 ? 171 ASN A CB  1 
ATOM   1309 C CG  . ASN A 1 177 ? 56.32153 -13.09487 -104.50983 1.000 261.86111 ? 171 ASN A CG  1 
ATOM   1310 O OD1 . ASN A 1 177 ? 56.63215 -14.28285 -104.60324 1.000 251.30669 ? 171 ASN A OD1 1 
ATOM   1311 N ND2 . ASN A 1 177 ? 55.64695 -12.45502 -105.45775 1.000 284.28946 ? 171 ASN A ND2 1 
ATOM   1312 N N   . SER A 1 178 ? 59.34082 -14.16286 -103.94898 1.000 260.33125 ? 172 SER A N   1 
ATOM   1313 C CA  . SER A 1 178 ? 60.47881 -14.38647 -104.83821 1.000 267.05140 ? 172 SER A CA  1 
ATOM   1314 C C   . SER A 1 178 ? 60.15255 -13.89319 -106.25073 1.000 278.15067 ? 172 SER A C   1 
ATOM   1315 O O   . SER A 1 178 ? 60.08290 -14.65430 -107.21534 1.000 275.22156 ? 172 SER A O   1 
ATOM   1316 C CB  . SER A 1 178 ? 60.86241 -15.86041 -104.83517 1.000 251.78008 ? 172 SER A CB  1 
ATOM   1317 O OG  . SER A 1 178 ? 61.11102 -16.31784 -103.51702 1.000 223.84397 ? 172 SER A OG  1 
ATOM   1318 N N   . ALA A 1 179 ? 59.94983 -12.57831 -106.35713 1.000 284.76090 ? 173 ALA A N   1 
ATOM   1319 C CA  . ALA A 1 179 ? 59.57265 -11.96476 -107.63001 1.000 277.19730 ? 173 ALA A CA  1 
ATOM   1320 C C   . ALA A 1 179 ? 60.13751 -10.54709 -107.66147 1.000 298.43086 ? 173 ALA A C   1 
ATOM   1321 O O   . ALA A 1 179 ? 59.59198 -9.64622  -107.01626 1.000 301.02896 ? 173 ALA A O   1 
ATOM   1322 C CB  . ALA A 1 179 ? 58.06119 -11.96649 -107.81328 1.000 262.00627 ? 173 ALA A CB  1 
ATOM   1323 N N   . LYS A 1 180 ? 61.22043 -10.36540 -108.41017 1.000 313.36232 ? 174 LYS A N   1 
ATOM   1324 C CA  . LYS A 1 180 ? 61.82585 -9.05083  -108.66388 1.000 344.85150 ? 174 LYS A CA  1 
ATOM   1325 C C   . LYS A 1 180 ? 62.22675 -8.42052  -107.32592 1.000 367.89447 ? 174 LYS A C   1 
ATOM   1326 O O   . LYS A 1 180 ? 62.60742 -9.12557  -106.38209 1.000 361.26564 ? 174 LYS A O   1 
ATOM   1327 C CB  . LYS A 1 180 ? 60.87855 -8.21061  -109.50422 1.000 344.32958 ? 174 LYS A CB  1 
ATOM   1328 C CG  . LYS A 1 180 ? 60.59551 -8.78964  -110.88188 1.000 308.90702 ? 174 LYS A CG  1 
ATOM   1329 C CD  . LYS A 1 180 ? 59.51080 -8.00613  -111.60261 1.000 280.02947 ? 174 LYS A CD  1 
ATOM   1330 C CE  . LYS A 1 180 ? 58.18666 -8.09109  -110.86089 1.000 272.42606 ? 174 LYS A CE  1 
ATOM   1331 N NZ  . LYS A 1 180 ? 57.71902 -9.49819  -110.72277 1.000 264.48598 ? 174 LYS A NZ  1 
ATOM   1332 N N   . ASN A 1 181 ? 62.14703 -7.09504  -107.23448 1.000 391.61740 ? 175 ASN A N   1 
ATOM   1333 C CA  . ASN A 1 181 ? 62.52849 -6.37159  -106.02949 1.000 386.07325 ? 175 ASN A CA  1 
ATOM   1334 C C   . ASN A 1 181 ? 61.34581 -6.29064  -105.07193 1.000 387.30132 ? 175 ASN A C   1 
ATOM   1335 O O   . ASN A 1 181 ? 60.26337 -5.82839  -105.44720 1.000 391.83227 ? 175 ASN A O   1 
ATOM   1336 C CB  . ASN A 1 181 ? 63.03015 -4.96917  -106.38069 1.000 377.66900 ? 175 ASN A CB  1 
ATOM   1337 C CG  . ASN A 1 181 ? 62.03611 -4.18190  -107.21534 1.000 374.05446 ? 175 ASN A CG  1 
ATOM   1338 O OD1 . ASN A 1 181 ? 61.24726 -4.75470  -107.96702 1.000 400.46003 ? 175 ASN A OD1 1 
ATOM   1339 N ND2 . ASN A 1 181 ? 62.07137 -2.86012  -107.08700 1.000 347.80427 ? 175 ASN A ND2 1 
ATOM   1340 N N   . SER A 1 182 ? 61.55578 -6.74586  -103.84138 1.000 394.92389 ? 176 SER A N   1 
ATOM   1341 C CA  . SER A 1 182 ? 60.51993 -6.72494  -102.81477 1.000 396.20375 ? 176 SER A CA  1 
ATOM   1342 C C   . SER A 1 182 ? 61.20230 -6.82926  -101.45118 1.000 405.53384 ? 176 SER A C   1 
ATOM   1343 O O   . SER A 1 182 ? 62.39328 -6.53368  -101.31966 1.000 412.05748 ? 176 SER A O   1 
ATOM   1344 C CB  . SER A 1 182 ? 59.49795 -7.84933  -103.05387 1.000 374.53503 ? 176 SER A CB  1 
ATOM   1345 O OG  . SER A 1 182 ? 58.76030 -7.63192  -104.24398 1.000 374.82101 ? 176 SER A OG  1 
ATOM   1346 N N   . ALA A 1 183 ? 60.44268 -7.25386  -100.43775 1.000 408.89878 ? 177 ALA A N   1 
ATOM   1347 C CA  . ALA A 1 183 ? 61.00224 -7.40630  -99.10051  1.000 377.13864 ? 177 ALA A CA  1 
ATOM   1348 C C   . ALA A 1 183 ? 61.96683 -8.57939  -99.00429  1.000 380.03029 ? 177 ALA A C   1 
ATOM   1349 O O   . ALA A 1 183 ? 62.75869 -8.63771  -98.05764  1.000 391.53028 ? 177 ALA A O   1 
ATOM   1350 C CB  . ALA A 1 183 ? 59.88139 -7.57574  -98.07719  1.000 336.48250 ? 177 ALA A CB  1 
ATOM   1351 N N   . ALA A 1 184 ? 61.91648 -9.51294  -99.95325  1.000 353.65842 ? 178 ALA A N   1 
ATOM   1352 C CA  . ALA A 1 184 ? 62.82161 -10.65256 -99.95118  1.000 330.07161 ? 178 ALA A CA  1 
ATOM   1353 C C   . ALA A 1 184 ? 64.10090 -10.39924 -100.73595 1.000 372.81397 ? 178 ALA A C   1 
ATOM   1354 O O   . ALA A 1 184 ? 65.08794 -11.11381 -100.52891 1.000 365.45981 ? 178 ALA A O   1 
ATOM   1355 C CB  . ALA A 1 184 ? 62.11527 -11.88950 -100.51558 1.000 250.19238 ? 178 ALA A CB  1 
ATOM   1356 N N   . ASN A 1 185 ? 64.11320 -9.40249  -101.61866 1.000 406.18744 ? 179 ASN A N   1 
ATOM   1357 C CA  . ASN A 1 185 ? 65.27187 -9.10161  -102.45278 1.000 421.68445 ? 179 ASN A CA  1 
ATOM   1358 C C   . ASN A 1 185 ? 65.98216 -7.81285  -102.07119 1.000 430.83901 ? 179 ASN A C   1 
ATOM   1359 O O   . ASN A 1 185 ? 67.21450 -7.77634  -102.06364 1.000 448.26863 ? 179 ASN A O   1 
ATOM   1360 C CB  . ASN A 1 185 ? 64.85590 -9.02686  -103.92702 1.000 416.65189 ? 179 ASN A CB  1 
ATOM   1361 C CG  . ASN A 1 185 ? 66.00749 -8.64929  -104.83968 1.000 416.50390 ? 179 ASN A CG  1 
ATOM   1362 O OD1 . ASN A 1 185 ? 66.17208 -7.48386  -105.20124 1.000 402.84356 ? 179 ASN A OD1 1 
ATOM   1363 N ND2 . ASN A 1 185 ? 66.81353 -9.63601  -105.21495 1.000 428.71882 ? 179 ASN A ND2 1 
ATOM   1364 N N   . LEU A 1 186 ? 65.24457 -6.75232  -101.75726 1.000 417.37748 ? 180 LEU A N   1 
ATOM   1365 C CA  . LEU A 1 186 ? 65.83493 -5.46795  -101.41219 1.000 424.95726 ? 180 LEU A CA  1 
ATOM   1366 C C   . LEU A 1 186 ? 65.86956 -5.27206  -99.90180  1.000 437.48571 ? 180 LEU A C   1 
ATOM   1367 O O   . LEU A 1 186 ? 64.98339 -5.72789  -99.17448  1.000 435.97773 ? 180 LEU A O   1 
ATOM   1368 C CB  . LEU A 1 186 ? 65.06172 -4.31381  -102.05548 1.000 409.23876 ? 180 LEU A CB  1 
ATOM   1369 C CG  . LEU A 1 186 ? 65.23681 -4.07984  -103.55605 1.000 370.06594 ? 180 LEU A CG  1 
ATOM   1370 C CD1 . LEU A 1 186 ? 64.56004 -2.78072  -103.96778 1.000 335.09608 ? 180 LEU A CD1 1 
ATOM   1371 C CD2 . LEU A 1 186 ? 66.70937 -4.06312  -103.93079 1.000 352.53891 ? 180 LEU A CD2 1 
ATOM   1372 N N   . ALA A 1 187 ? 66.91140 -4.58166  -99.43769  1.000 439.10006 ? 181 ALA A N   1 
ATOM   1373 C CA  . ALA A 1 187 ? 67.00054 -4.17305  -98.04326  1.000 428.64646 ? 181 ALA A CA  1 
ATOM   1374 C C   . ALA A 1 187 ? 66.30009 -2.84924  -97.77515  1.000 441.16534 ? 181 ALA A C   1 
ATOM   1375 O O   . ALA A 1 187 ? 66.01451 -2.53813  -96.61303  1.000 448.14570 ? 181 ALA A O   1 
ATOM   1376 C CB  . ALA A 1 187 ? 68.46682 -4.07051  -97.61090  1.000 396.34607 ? 181 ALA A CB  1 
ATOM   1377 N N   . SER A 1 188 ? 66.02129 -2.06694  -98.81858  1.000 448.54979 ? 182 SER A N   1 
ATOM   1378 C CA  . SER A 1 188 ? 65.28519 -0.81629  -98.68194  1.000 430.83105 ? 182 SER A CA  1 
ATOM   1379 C C   . SER A 1 188 ? 63.77950 -1.02594  -98.77737  1.000 440.38915 ? 182 SER A C   1 
ATOM   1380 O O   . SER A 1 188 ? 63.01882 -0.39912  -98.03177  1.000 422.99742 ? 182 SER A O   1 
ATOM   1381 C CB  . SER A 1 188 ? 65.74058 0.18283   -99.74875  1.000 401.24549 ? 182 SER A CB  1 
ATOM   1382 O OG  . SER A 1 188 ? 65.52050 -0.32927  -101.05158 1.000 387.05467 ? 182 SER A OG  1 
ATOM   1383 N N   . ALA A 1 189 ? 63.33331 -1.89628  -99.68652  1.000 457.61867 ? 183 ALA A N   1 
ATOM   1384 C CA  . ALA A 1 189 ? 61.91658 -2.22797  -99.76600  1.000 447.89951 ? 183 ALA A CA  1 
ATOM   1385 C C   . ALA A 1 189 ? 61.45222 -3.05632  -98.57718  1.000 432.83491 ? 183 ALA A C   1 
ATOM   1386 O O   . ALA A 1 189 ? 60.24739 -3.11335  -98.31060  1.000 411.15229 ? 183 ALA A O   1 
ATOM   1387 C CB  . ALA A 1 189 ? 61.61715 -2.97592  -101.06608 1.000 435.32351 ? 183 ALA A CB  1 
ATOM   1388 N N   . ALA A 1 190 ? 62.37326 -3.70670  -97.86497  1.000 430.90779 ? 184 ALA A N   1 
ATOM   1389 C CA  . ALA A 1 190 ? 61.98799 -4.45539  -96.67566  1.000 404.31149 ? 184 ALA A CA  1 
ATOM   1390 C C   . ALA A 1 190 ? 61.92077 -3.56397  -95.44319  1.000 424.55153 ? 184 ALA A C   1 
ATOM   1391 O O   . ALA A 1 190 ? 61.19639 -3.88120  -94.49346  1.000 410.10372 ? 184 ALA A O   1 
ATOM   1392 C CB  . ALA A 1 190 ? 62.95994 -5.61325  -96.44079  1.000 397.56418 ? 184 ALA A CB  1 
ATOM   1393 N N   . ALA A 1 191 ? 62.66275 -2.45470  -95.43803  1.000 507.15126 ? 185 ALA A N   1 
ATOM   1394 C CA  . ALA A 1 191 ? 62.58935 -1.50011  -94.34008  1.000 494.18125 ? 185 ALA A CA  1 
ATOM   1395 C C   . ALA A 1 191 ? 61.38275 -0.57810  -94.44921  1.000 478.24760 ? 185 ALA A C   1 
ATOM   1396 O O   . ALA A 1 191 ? 60.93804 -0.03705  -93.43085  1.000 495.22334 ? 185 ALA A O   1 
ATOM   1397 C CB  . ALA A 1 191 ? 63.87282 -0.66917  -94.27664  1.000 458.92193 ? 185 ALA A CB  1 
ATOM   1398 N N   . ALA A 1 192 ? 60.84767 -0.38712  -95.65352  1.000 419.81317 ? 186 ALA A N   1 
ATOM   1399 C CA  . ALA A 1 192 ? 59.63448 0.39268   -95.85795  1.000 388.11189 ? 186 ALA A CA  1 
ATOM   1400 C C   . ALA A 1 192 ? 58.36766 -0.39853  -95.55690  1.000 374.56897 ? 186 ALA A C   1 
ATOM   1401 O O   . ALA A 1 192 ? 57.27050 0.07128   -95.87665  1.000 348.84070 ? 186 ALA A O   1 
ATOM   1402 C CB  . ALA A 1 192 ? 59.58484 0.92334   -97.29348  1.000 374.25138 ? 186 ALA A CB  1 
ATOM   1403 N N   . LEU A 1 193 ? 58.49287 -1.57613  -94.95536  1.000 380.01629 ? 187 LEU A N   1 
ATOM   1404 C CA  . LEU A 1 193 ? 57.33127 -2.40205  -94.65317  1.000 349.78999 ? 187 LEU A CA  1 
ATOM   1405 C C   . LEU A 1 193 ? 56.62821 -1.88964  -93.40379  1.000 358.56959 ? 187 LEU A C   1 
ATOM   1406 O O   . LEU A 1 193 ? 57.26666 -1.77384  -92.35139  1.000 374.62085 ? 187 LEU A O   1 
ATOM   1407 C CB  . LEU A 1 193 ? 57.74101 -3.85172  -94.43860  1.000 313.57987 ? 187 LEU A CB  1 
ATOM   1408 C CG  . LEU A 1 193 ? 58.27251 -4.65312  -95.62143  1.000 301.07159 ? 187 LEU A CG  1 
ATOM   1409 C CD1 . LEU A 1 193 ? 58.40516 -6.10903  -95.21295  1.000 256.63161 ? 187 LEU A CD1 1 
ATOM   1410 C CD2 . LEU A 1 193 ? 57.35904 -4.50006  -96.82221  1.000 287.43510 ? 187 LEU A CD2 1 
ATOM   1411 N N   . PRO A 1 194 ? 55.33679 -1.57234  -93.46779  1.000 360.61080 ? 188 PRO A N   1 
ATOM   1412 C CA  . PRO A 1 194 ? 54.58171 -1.34638  -92.22982  1.000 354.52946 ? 188 PRO A CA  1 
ATOM   1413 C C   . PRO A 1 194 ? 54.41868 -2.63876  -91.44556  1.000 342.21942 ? 188 PRO A C   1 
ATOM   1414 O O   . PRO A 1 194 ? 53.65368 -3.52291  -91.84432  1.000 318.06549 ? 188 PRO A O   1 
ATOM   1415 C CB  . PRO A 1 194 ? 53.23214 -0.80983  -92.72731  1.000 323.30321 ? 188 PRO A CB  1 
ATOM   1416 C CG  . PRO A 1 194 ? 53.50034 -0.31112  -94.11312  1.000 317.96935 ? 188 PRO A CG  1 
ATOM   1417 C CD  . PRO A 1 194 ? 54.55239 -1.22461  -94.66364  1.000 351.26496 ? 188 PRO A CD  1 
ATOM   1418 N N   . VAL A 1 195 ? 55.14835 -2.76970  -90.34364  1.000 352.10837 ? 189 VAL A N   1 
ATOM   1419 C CA  . VAL A 1 195 ? 55.05103 -3.93880  -89.47132  1.000 302.70190 ? 189 VAL A CA  1 
ATOM   1420 C C   . VAL A 1 195 ? 54.22921 -3.49459  -88.26634  1.000 309.22608 ? 189 VAL A C   1 
ATOM   1421 O O   . VAL A 1 195 ? 54.76373 -3.07332  -87.23853  1.000 318.39273 ? 189 VAL A O   1 
ATOM   1422 C CB  . VAL A 1 195 ? 56.42492 -4.47336  -89.07359  1.000 282.61731 ? 189 VAL A CB  1 
ATOM   1423 C CG1 . VAL A 1 195 ? 56.28317 -5.77570  -88.30533  1.000 273.58016 ? 189 VAL A CG1 1 
ATOM   1424 C CG2 . VAL A 1 195 ? 57.29382 -4.67221  -90.30715  1.000 262.16714 ? 189 VAL A CG2 1 
ATOM   1425 N N   . SER A 1 196 ? 52.90904 -3.58758  -88.39681  1.000 303.57512 ? 190 SER A N   1 
ATOM   1426 C CA  . SER A 1 196 ? 51.97963 -3.05475  -87.41243  1.000 313.14412 ? 190 SER A CA  1 
ATOM   1427 C C   . SER A 1 196 ? 51.24650 -4.18105  -86.69779  1.000 291.45928 ? 190 SER A C   1 
ATOM   1428 O O   . SER A 1 196 ? 50.87356 -5.18503  -87.31296  1.000 271.57652 ? 190 SER A O   1 
ATOM   1429 C CB  . SER A 1 196 ? 50.96207 -2.11994  -88.07372  1.000 313.45082 ? 190 SER A CB  1 
ATOM   1430 O OG  . SER A 1 196 ? 51.60870 -1.09654  -88.80816  1.000 303.88295 ? 190 SER A OG  1 
ATOM   1431 N N   . THR A 1 197 ? 51.04338 -4.00444  -85.39594  1.000 297.73258 ? 191 THR A N   1 
ATOM   1432 C CA  . THR A 1 197 ? 50.20533 -4.88687  -84.60061  1.000 292.97325 ? 191 THR A CA  1 
ATOM   1433 C C   . THR A 1 197 ? 49.29770 -4.03358  -83.72856  1.000 312.40025 ? 191 THR A C   1 
ATOM   1434 O O   . THR A 1 197 ? 49.73754 -3.03733  -83.14659  1.000 321.67283 ? 191 THR A O   1 
ATOM   1435 C CB  . THR A 1 197 ? 51.04123 -5.84580  -83.73377  1.000 284.81422 ? 191 THR A CB  1 
ATOM   1436 O OG1 . THR A 1 197 ? 50.17246 -6.61504  -82.89249  1.000 295.83985 ? 191 THR A OG1 1 
ATOM   1437 C CG2 . THR A 1 197 ? 52.03796 -5.07917  -82.87100  1.000 271.15675 ? 191 THR A CG2 1 
ATOM   1438 N N   . ALA A 1 198 ? 48.02291 -4.40903  -83.66413  1.000 339.42852 ? 192 ALA A N   1 
ATOM   1439 C CA  . ALA A 1 198 ? 47.06557 -3.66546  -82.85981  1.000 346.12931 ? 192 ALA A CA  1 
ATOM   1440 C C   . ALA A 1 198 ? 47.01326 -4.13719  -81.41537  1.000 346.59345 ? 192 ALA A C   1 
ATOM   1441 O O   . ALA A 1 198 ? 46.57967 -3.37336  -80.54550  1.000 375.76391 ? 192 ALA A O   1 
ATOM   1442 C CB  . ALA A 1 198 ? 45.66697 -3.75836  -83.47802  1.000 345.98642 ? 192 ALA A CB  1 
ATOM   1443 N N   . TYR A 1 199 ? 47.44888 -5.36529  -81.13809  1.000 308.56877 ? 193 TYR A N   1 
ATOM   1444 C CA  . TYR A 1 199 ? 47.36838 -5.93499  -79.80177  1.000 303.52182 ? 193 TYR A CA  1 
ATOM   1445 C C   . TYR A 1 199 ? 48.59380 -6.79591  -79.53727  1.000 296.86582 ? 193 TYR A C   1 
ATOM   1446 O O   . TYR A 1 199 ? 49.10220 -7.46253  -80.44318  1.000 298.58303 ? 193 TYR A O   1 
ATOM   1447 C CB  . TYR A 1 199 ? 46.08981 -6.76600  -79.63357  1.000 301.02135 ? 193 TYR A CB  1 
ATOM   1448 C CG  . TYR A 1 199 ? 44.85588 -6.07429  -80.16506  1.000 304.90221 ? 193 TYR A CG  1 
ATOM   1449 C CD1 . TYR A 1 199 ? 44.22122 -5.08275  -79.42895  1.000 309.70415 ? 193 TYR A CD1 1 
ATOM   1450 C CD2 . TYR A 1 199 ? 44.33436 -6.40244  -81.40989  1.000 296.15911 ? 193 TYR A CD2 1 
ATOM   1451 C CE1 . TYR A 1 199 ? 43.09776 -4.44259  -79.91356  1.000 312.84959 ? 193 TYR A CE1 1 
ATOM   1452 C CE2 . TYR A 1 199 ? 43.20965 -5.77001  -81.90135  1.000 294.48170 ? 193 TYR A CE2 1 
ATOM   1453 C CZ  . TYR A 1 199 ? 42.59721 -4.78959  -81.15010  1.000 310.61277 ? 193 TYR A CZ  1 
ATOM   1454 O OH  . TYR A 1 199 ? 41.47683 -4.15649  -81.63595  1.000 318.06287 ? 193 TYR A OH  1 
ATOM   1455 N N   . HIS A 1 200 ? 49.06122 -6.77594  -78.29238  1.000 294.89801 ? 194 HIS A N   1 
ATOM   1456 C CA  . HIS A 1 200 ? 50.22706 -7.54858  -77.88210  1.000 301.33858 ? 194 HIS A CA  1 
ATOM   1457 C C   . HIS A 1 200 ? 50.08334 -7.88327  -76.39978  1.000 296.84948 ? 194 HIS A C   1 
ATOM   1458 O O   . HIS A 1 200 ? 49.01648 -7.69728  -75.80659  1.000 289.59883 ? 194 HIS A O   1 
ATOM   1459 C CB  . HIS A 1 200 ? 51.51831 -6.78364  -78.20365  1.000 310.85447 ? 194 HIS A CB  1 
ATOM   1460 C CG  . HIS A 1 200 ? 51.46723 -5.32729  -77.85736  1.000 294.95470 ? 194 HIS A CG  1 
ATOM   1461 N ND1 . HIS A 1 200 ? 51.84429 -4.84006  -76.62442  1.000 289.87040 ? 194 HIS A ND1 1 
ATOM   1462 C CD2 . HIS A 1 200 ? 51.09054 -4.25070  -78.58745  1.000 286.97121 ? 194 HIS A CD2 1 
ATOM   1463 C CE1 . HIS A 1 200 ? 51.69923 -3.52692  -76.60893  1.000 290.81588 ? 194 HIS A CE1 1 
ATOM   1464 N NE2 . HIS A 1 200 ? 51.24268 -3.14426  -77.78761  1.000 287.86242 ? 194 HIS A NE2 1 
ATOM   1465 N N   . ILE A 1 201 ? 51.16585 -8.38517  -75.79608  1.000 297.93781 ? 195 ILE A N   1 
ATOM   1466 C CA  . ILE A 1 201 ? 51.10279 -8.82183  -74.40418  1.000 289.78009 ? 195 ILE A CA  1 
ATOM   1467 C C   . ILE A 1 201 ? 50.87392 -7.65266  -73.45452  1.000 280.80661 ? 195 ILE A C   1 
ATOM   1468 O O   . ILE A 1 201 ? 50.40408 -7.85627  -72.32893  1.000 266.69067 ? 195 ILE A O   1 
ATOM   1469 C CB  . ILE A 1 201 ? 52.37737 -9.59871  -74.01523  1.000 280.49656 ? 195 ILE A CB  1 
ATOM   1470 C CG1 . ILE A 1 201 ? 52.10159 -10.51261 -72.81826  1.000 260.36353 ? 195 ILE A CG1 1 
ATOM   1471 C CG2 . ILE A 1 201 ? 53.51822 -8.64541  -73.68679  1.000 273.34927 ? 195 ILE A CG2 1 
ATOM   1472 C CD1 . ILE A 1 201 ? 53.30890 -11.29921 -72.35267  1.000 226.50545 ? 195 ILE A CD1 1 
ATOM   1473 N N   . LYS A 1 202 ? 51.18529 -6.43011  -73.87805  1.000 289.66844 ? 196 LYS A N   1 
ATOM   1474 C CA  . LYS A 1 202 ? 50.93458 -5.24064  -73.07702  1.000 315.28550 ? 196 LYS A CA  1 
ATOM   1475 C C   . LYS A 1 202 ? 49.59383 -4.58983  -73.39396  1.000 319.26511 ? 196 LYS A C   1 
ATOM   1476 O O   . LYS A 1 202 ? 49.27245 -3.55035  -72.80852  1.000 328.35386 ? 196 LYS A O   1 
ATOM   1477 C CB  . LYS A 1 202 ? 52.06694 -4.22520  -73.27352  1.000 324.99443 ? 196 LYS A CB  1 
ATOM   1478 C CG  . LYS A 1 202 ? 53.42235 -4.69829  -72.76366  1.000 304.64361 ? 196 LYS A CG  1 
ATOM   1479 C CD  . LYS A 1 202 ? 54.53789 -3.74496  -73.16748  1.000 266.75121 ? 196 LYS A CD  1 
ATOM   1480 C CE  . LYS A 1 202 ? 54.75473 -3.75465  -74.67226  1.000 258.00682 ? 196 LYS A CE  1 
ATOM   1481 N NZ  . LYS A 1 202 ? 55.13504 -5.10713  -75.16626  1.000 254.46312 ? 196 LYS A NZ  1 
ATOM   1482 N N   . ASN A 1 203 ? 48.80744 -5.17531  -74.29942  1.000 309.71855 ? 197 ASN A N   1 
ATOM   1483 C CA  . ASN A 1 203 ? 47.49297 -4.65678  -74.65899  1.000 306.43742 ? 197 ASN A CA  1 
ATOM   1484 C C   . ASN A 1 203 ? 46.67242 -5.74191  -75.34778  1.000 299.83491 ? 197 ASN A C   1 
ATOM   1485 O O   . ASN A 1 203 ? 46.65170 -5.81517  -76.58297  1.000 292.50981 ? 197 ASN A O   1 
ATOM   1486 C CB  . ASN A 1 203 ? 47.62430 -3.42932  -75.56420  1.000 310.38992 ? 197 ASN A CB  1 
ATOM   1487 C CG  . ASN A 1 203 ? 46.27966 -2.88701  -76.01243  1.000 313.68883 ? 197 ASN A CG  1 
ATOM   1488 O OD1 . ASN A 1 203 ? 45.60449 -2.17590  -75.26870  1.000 287.08521 ? 197 ASN A OD1 1 
ATOM   1489 N ND2 . ASN A 1 203 ? 45.88614 -3.21932  -77.23672  1.000 331.31383 ? 197 ASN A ND2 1 
ATOM   1490 N N   . PRO A 1 204 ? 45.99893 -6.60556  -74.59465  1.000 298.02933 ? 198 PRO A N   1 
ATOM   1491 C CA  . PRO A 1 204 ? 45.17069 -7.64291  -75.21480  1.000 288.15237 ? 198 PRO A CA  1 
ATOM   1492 C C   . PRO A 1 204 ? 43.79920 -7.11016  -75.60478  1.000 297.71428 ? 198 PRO A C   1 
ATOM   1493 O O   . PRO A 1 204 ? 43.36427 -6.04185  -75.17104  1.000 298.88943 ? 198 PRO A O   1 
ATOM   1494 C CB  . PRO A 1 204 ? 45.04790 -8.71078  -74.11722  1.000 279.57382 ? 198 PRO A CB  1 
ATOM   1495 C CG  . PRO A 1 204 ? 45.98971 -8.27670  -73.00903  1.000 294.01982 ? 198 PRO A CG  1 
ATOM   1496 C CD  . PRO A 1 204 ? 46.10981 -6.79557  -73.14156  1.000 302.04467 ? 198 PRO A CD  1 
ATOM   1497 N N   . ILE A 1 205 ? 43.11595 -7.88673  -76.44192  1.000 295.37753 ? 199 ILE A N   1 
ATOM   1498 C CA  . ILE A 1 205 ? 41.75054 -7.59068  -76.86316  1.000 290.19569 ? 199 ILE A CA  1 
ATOM   1499 C C   . ILE A 1 205 ? 40.88267 -8.77840  -76.46755  1.000 274.12903 ? 199 ILE A C   1 
ATOM   1500 O O   . ILE A 1 205 ? 41.04862 -9.88626  -76.99573  1.000 242.89401 ? 199 ILE A O   1 
ATOM   1501 C CB  . ILE A 1 205 ? 41.65445 -7.29640  -78.36773  1.000 288.44935 ? 199 ILE A CB  1 
ATOM   1502 C CG1 . ILE A 1 205 ? 40.19271 -7.22684  -78.80916  1.000 290.99854 ? 199 ILE A CG1 1 
ATOM   1503 C CG2 . ILE A 1 205 ? 42.43036 -8.32169  -79.18981  1.000 282.17538 ? 199 ILE A CG2 1 
ATOM   1504 C CD1 . ILE A 1 205 ? 40.02621 -6.83673  -80.25322  1.000 281.63201 ? 199 ILE A CD1 1 
ATOM   1505 N N   . GLY A 1 206 ? 39.96489 -8.55356  -75.53019  1.000 274.75316 ? 200 GLY A N   1 
ATOM   1506 C CA  . GLY A 1 206 ? 39.16204 -9.64270  -75.00188  1.000 265.46997 ? 200 GLY A CA  1 
ATOM   1507 C C   . GLY A 1 206 ? 39.97921 -10.74532 -74.36955  1.000 265.24483 ? 200 GLY A C   1 
ATOM   1508 O O   . GLY A 1 206 ? 39.53334 -11.89701 -74.32964  1.000 273.45183 ? 200 GLY A O   1 
ATOM   1509 N N   . GLY A 1 207 ? 41.17152 -10.42306 -73.87304  1.000 274.01193 ? 201 GLY A N   1 
ATOM   1510 C CA  . GLY A 1 207 ? 42.05745 -11.43262 -73.33345  1.000 283.32671 ? 201 GLY A CA  1 
ATOM   1511 C C   . GLY A 1 207 ? 42.77892 -12.25824 -74.37086  1.000 257.45894 ? 201 GLY A C   1 
ATOM   1512 O O   . GLY A 1 207 ? 43.21022 -13.37314 -74.06570  1.000 235.14773 ? 201 GLY A O   1 
ATOM   1513 N N   . VAL A 1 208 ? 42.92172 -11.74795 -75.59264  1.000 258.39132 ? 202 VAL A N   1 
ATOM   1514 C CA  . VAL A 1 208 ? 43.55780 -12.46689 -76.68963  1.000 246.43993 ? 202 VAL A CA  1 
ATOM   1515 C C   . VAL A 1 208 ? 44.54664 -11.53276 -77.37397  1.000 245.21728 ? 202 VAL A C   1 
ATOM   1516 O O   . VAL A 1 208 ? 44.25016 -10.35285 -77.59043  1.000 232.96442 ? 202 VAL A O   1 
ATOM   1517 C CB  . VAL A 1 208 ? 42.51546 -12.99562 -77.70047  1.000 239.72024 ? 202 VAL A CB  1 
ATOM   1518 C CG1 . VAL A 1 208 ? 43.20040 -13.65047 -78.88821  1.000 253.23554 ? 202 VAL A CG1 1 
ATOM   1519 C CG2 . VAL A 1 208 ? 41.56244 -13.97512 -77.02765  1.000 227.33366 ? 202 VAL A CG2 1 
ATOM   1520 N N   . PHE A 1 209 ? 45.72552 -12.05747 -77.70628  1.000 246.10214 ? 203 PHE A N   1 
ATOM   1521 C CA  . PHE A 1 209 ? 46.73026 -11.28500 -78.42332  1.000 250.83352 ? 203 PHE A CA  1 
ATOM   1522 C C   . PHE A 1 209 ? 47.61369 -12.23293 -79.22176  1.000 239.49138 ? 203 PHE A C   1 
ATOM   1523 O O   . PHE A 1 209 ? 47.72244 -13.42219 -78.91210  1.000 224.08156 ? 203 PHE A O   1 
ATOM   1524 C CB  . PHE A 1 209 ? 47.57589 -10.42723 -77.47077  1.000 266.28106 ? 203 PHE A CB  1 
ATOM   1525 C CG  . PHE A 1 209 ? 48.36802 -11.22297 -76.46958  1.000 261.50858 ? 203 PHE A CG  1 
ATOM   1526 C CD1 . PHE A 1 209 ? 47.78807 -11.64430 -75.28418  1.000 256.76396 ? 203 PHE A CD1 1 
ATOM   1527 C CD2 . PHE A 1 209 ? 49.69722 -11.53613 -76.70722  1.000 253.95943 ? 203 PHE A CD2 1 
ATOM   1528 C CE1 . PHE A 1 209 ? 48.51466 -12.37157 -74.35988  1.000 259.56277 ? 203 PHE A CE1 1 
ATOM   1529 C CE2 . PHE A 1 209 ? 50.42922 -12.26280 -75.78640  1.000 239.09206 ? 203 PHE A CE2 1 
ATOM   1530 C CZ  . PHE A 1 209 ? 49.83699 -12.68023 -74.61105  1.000 244.78433 ? 203 PHE A CZ  1 
ATOM   1531 N N   . PHE A 1 210 ? 48.24557 -11.68884 -80.25863  1.000 242.21191 ? 204 PHE A N   1 
ATOM   1532 C CA  . PHE A 1 210 ? 49.11127 -12.45713 -81.14203  1.000 224.90290 ? 204 PHE A CA  1 
ATOM   1533 C C   . PHE A 1 210 ? 50.57612 -12.18657 -80.82804  1.000 230.51208 ? 204 PHE A C   1 
ATOM   1534 O O   . PHE A 1 210 ? 50.98277 -11.03540 -80.64526  1.000 245.86243 ? 204 PHE A O   1 
ATOM   1535 C CB  . PHE A 1 210 ? 48.84254 -12.12223 -82.61126  1.000 222.35859 ? 204 PHE A CB  1 
ATOM   1536 C CG  . PHE A 1 210 ? 47.51064 -12.59600 -83.11239  1.000 242.00340 ? 204 PHE A CG  1 
ATOM   1537 C CD1 . PHE A 1 210 ? 47.24631 -13.94898 -83.24367  1.000 241.42287 ? 204 PHE A CD1 1 
ATOM   1538 C CD2 . PHE A 1 210 ? 46.52953 -11.68772 -83.47251  1.000 251.12121 ? 204 PHE A CD2 1 
ATOM   1539 C CE1 . PHE A 1 210 ? 46.02277 -14.38760 -83.71130  1.000 256.35095 ? 204 PHE A CE1 1 
ATOM   1540 C CE2 . PHE A 1 210 ? 45.30474 -12.11955 -83.94218  1.000 242.33068 ? 204 PHE A CE2 1 
ATOM   1541 C CZ  . PHE A 1 210 ? 45.05072 -13.47122 -84.06144  1.000 264.81177 ? 204 PHE A CZ  1 
ATOM   1542 N N   . THR A 1 211 ? 51.36353 -13.25503 -80.77092  1.000 223.96275 ? 205 THR A N   1 
ATOM   1543 C CA  . THR A 1 211 ? 52.81309 -13.16693 -80.70823  1.000 231.44293 ? 205 THR A CA  1 
ATOM   1544 C C   . THR A 1 211 ? 53.39323 -13.60488 -82.04650  1.000 231.64957 ? 205 THR A C   1 
ATOM   1545 O O   . THR A 1 211 ? 52.81444 -14.43999 -82.74737  1.000 228.48431 ? 205 THR A O   1 
ATOM   1546 C CB  . THR A 1 211 ? 53.37894 -14.02799 -79.57506  1.000 240.82697 ? 205 THR A CB  1 
ATOM   1547 O OG1 . THR A 1 211 ? 52.86346 -15.36068 -79.67955  1.000 253.08237 ? 205 THR A OG1 1 
ATOM   1548 C CG2 . THR A 1 211 ? 52.99486 -13.44374 -78.22423  1.000 215.94613 ? 205 THR A CG2 1 
ATOM   1549 N N   . ASP A 1 212 ? 54.53854 -13.03101 -82.40307  1.000 237.74155 ? 206 ASP A N   1 
ATOM   1550 C CA  . ASP A 1 212 ? 55.08925 -13.19261 -83.73933  1.000 236.90047 ? 206 ASP A CA  1 
ATOM   1551 C C   . ASP A 1 212 ? 56.52543 -13.69508 -83.66947  1.000 237.49748 ? 206 ASP A C   1 
ATOM   1552 O O   . ASP A 1 212 ? 57.13946 -13.76620 -82.60133  1.000 238.76128 ? 206 ASP A O   1 
ATOM   1553 C CB  . ASP A 1 212 ? 55.01069 -11.87680 -84.52347  1.000 231.83164 ? 206 ASP A CB  1 
ATOM   1554 C CG  . ASP A 1 212 ? 53.58151 -11.44395 -84.77979  1.000 231.80736 ? 206 ASP A CG  1 
ATOM   1555 O OD1 . ASP A 1 212 ? 52.80425 -12.25903 -85.31952  1.000 222.85065 ? 206 ASP A OD1 1 
ATOM   1556 O OD2 . ASP A 1 212 ? 53.22820 -10.30027 -84.42498  1.000 241.01134 ? 206 ASP A OD2 1 
ATOM   1557 N N   . SER A 1 213 ? 57.05202 -14.04520 -84.84244  1.000 230.09646 ? 207 SER A N   1 
ATOM   1558 C CA  . SER A 1 213 ? 58.37285 -14.63570 -85.01367  1.000 233.90421 ? 207 SER A CA  1 
ATOM   1559 C C   . SER A 1 213 ? 58.73547 -14.57737 -86.49393  1.000 238.55031 ? 207 SER A C   1 
ATOM   1560 O O   . SER A 1 213 ? 57.83945 -14.63551 -87.34580  1.000 227.95205 ? 207 SER A O   1 
ATOM   1561 C CB  . SER A 1 213 ? 58.38309 -16.07649 -84.49455  1.000 223.61687 ? 207 SER A CB  1 
ATOM   1562 O OG  . SER A 1 213 ? 59.66112 -16.67502 -84.61470  1.000 227.23590 ? 207 SER A OG  1 
ATOM   1563 N N   . PRO A 1 214 ? 60.02328 -14.45163 -86.85290  1.000 235.15785 ? 208 PRO A N   1 
ATOM   1564 C CA  . PRO A 1 214 ? 61.21484 -14.36125 -85.99576  1.000 244.02233 ? 208 PRO A CA  1 
ATOM   1565 C C   . PRO A 1 214 ? 61.44195 -12.96175 -85.43645  1.000 262.95575 ? 208 PRO A C   1 
ATOM   1566 O O   . PRO A 1 214 ? 60.53101 -12.14020 -85.40938  1.000 283.56311 ? 208 PRO A O   1 
ATOM   1567 C CB  . PRO A 1 214 ? 62.33990 -14.78219 -86.94666  1.000 249.07205 ? 208 PRO A CB  1 
ATOM   1568 C CG  . PRO A 1 214 ? 61.88687 -14.25683 -88.27524  1.000 248.13167 ? 208 PRO A CG  1 
ATOM   1569 C CD  . PRO A 1 214 ? 60.38633 -14.43749 -88.28224  1.000 218.59085 ? 208 PRO A CD  1 
ATOM   1570 N N   . GLU A 1 215 ? 62.66424 -12.66539 -84.98946  1.000 266.82798 ? 209 GLU A N   1 
ATOM   1571 C CA  . GLU A 1 215 ? 62.93291 -11.38101 -84.35209  1.000 281.20601 ? 209 GLU A CA  1 
ATOM   1572 C C   . GLU A 1 215 ? 63.17857 -10.27813 -85.37605  1.000 284.79286 ? 209 GLU A C   1 
ATOM   1573 O O   . GLU A 1 215 ? 62.78632 -9.12688  -85.15446  1.000 295.01502 ? 209 GLU A O   1 
ATOM   1574 C CB  . GLU A 1 215 ? 64.12660 -11.50698 -83.40385  1.000 275.14939 ? 209 GLU A CB  1 
ATOM   1575 C CG  . GLU A 1 215 ? 64.38831 -10.26650 -82.56367  1.000 293.40710 ? 209 GLU A CG  1 
ATOM   1576 C CD  . GLU A 1 215 ? 65.50776 -10.46646 -81.56109  1.000 284.92273 ? 209 GLU A CD  1 
ATOM   1577 O OE1 . GLU A 1 215 ? 66.13483 -11.54648 -81.57570  1.000 281.79908 ? 209 GLU A OE1 1 
ATOM   1578 O OE2 . GLU A 1 215 ? 65.75920 -9.54451  -80.75668  1.000 305.55171 ? 209 GLU A OE2 1 
ATOM   1579 N N   . HIS A 1 216 ? 63.81760 -10.60352 -86.49965  1.000 276.97832 ? 210 HIS A N   1 
ATOM   1580 C CA  . HIS A 1 216 ? 64.10945 -9.60198  -87.51847  1.000 271.24571 ? 210 HIS A CA  1 
ATOM   1581 C C   . HIS A 1 216 ? 62.88903 -9.22280  -88.34867  1.000 256.82837 ? 210 HIS A C   1 
ATOM   1582 O O   . HIS A 1 216 ? 63.02187 -8.42760  -89.28548  1.000 243.84109 ? 210 HIS A O   1 
ATOM   1583 C CB  . HIS A 1 216 ? 65.23601 -10.09080 -88.43631  1.000 274.35534 ? 210 HIS A CB  1 
ATOM   1584 C CG  . HIS A 1 216 ? 64.89333 -11.31764 -89.22311  1.000 271.20708 ? 210 HIS A CG  1 
ATOM   1585 N ND1 . HIS A 1 216 ? 64.38042 -11.26294 -90.50118  1.000 262.37665 ? 210 HIS A ND1 1 
ATOM   1586 C CD2 . HIS A 1 216 ? 64.99827 -12.63231 -88.91626  1.000 269.88463 ? 210 HIS A CD2 1 
ATOM   1587 C CE1 . HIS A 1 216 ? 64.18026 -12.49053 -90.94636  1.000 261.48267 ? 210 HIS A CE1 1 
ATOM   1588 N NE2 . HIS A 1 216 ? 64.54764 -13.34008 -90.00415  1.000 270.93291 ? 210 HIS A NE2 1 
ATOM   1589 N N   . LEU A 1 217 ? 61.71198 -9.76399  -88.03010  1.000 256.42053 ? 211 LEU A N   1 
ATOM   1590 C CA  . LEU A 1 217 ? 60.46854 -9.38940  -88.69284  1.000 263.30812 ? 211 LEU A CA  1 
ATOM   1591 C C   . LEU A 1 217 ? 59.46662 -8.76249  -87.73054  1.000 272.14706 ? 211 LEU A C   1 
ATOM   1592 O O   . LEU A 1 217 ? 58.31875 -8.51586  -88.12012  1.000 278.30101 ? 211 LEU A O   1 
ATOM   1593 C CB  . LEU A 1 217 ? 59.84016 -10.60537 -89.38241  1.000 244.63718 ? 211 LEU A CB  1 
ATOM   1594 C CG  . LEU A 1 217 ? 60.69342 -11.31654 -90.43502  1.000 229.51608 ? 211 LEU A CG  1 
ATOM   1595 C CD1 . LEU A 1 217 ? 59.86681 -12.33646 -91.20536  1.000 198.28864 ? 211 LEU A CD1 1 
ATOM   1596 C CD2 . LEU A 1 217 ? 61.32608 -10.31029 -91.37953  1.000 251.88973 ? 211 LEU A CD2 1 
ATOM   1597 N N   . LEU A 1 218 ? 59.86913 -8.49803  -86.48508  1.000 269.70643 ? 212 LEU A N   1 
ATOM   1598 C CA  . LEU A 1 218 ? 58.95983 -7.91525  -85.50443  1.000 272.53092 ? 212 LEU A CA  1 
ATOM   1599 C C   . LEU A 1 218 ? 58.80330 -6.41227  -85.67994  1.000 273.12259 ? 212 LEU A C   1 
ATOM   1600 O O   . LEU A 1 218 ? 57.73223 -5.86744  -85.38993  1.000 267.49966 ? 212 LEU A O   1 
ATOM   1601 C CB  . LEU A 1 218 ? 59.45573 -8.19917  -84.08644  1.000 271.30957 ? 212 LEU A CB  1 
ATOM   1602 C CG  . LEU A 1 218 ? 59.55877 -9.64624  -83.61430  1.000 284.80519 ? 212 LEU A CG  1 
ATOM   1603 C CD1 . LEU A 1 218 ? 60.34038 -9.69626  -82.31678  1.000 288.49545 ? 212 LEU A CD1 1 
ATOM   1604 C CD2 . LEU A 1 218 ? 58.17734 -10.25145 -83.43415  1.000 274.49724 ? 212 LEU A CD2 1 
ATOM   1605 N N   . GLY A 1 219 ? 59.84549 -5.73277  -86.13799  1.000 278.56523 ? 213 GLY A N   1 
ATOM   1606 C CA  . GLY A 1 219 ? 59.83388 -4.27993  -86.13149  1.000 275.09775 ? 213 GLY A CA  1 
ATOM   1607 C C   . GLY A 1 219 ? 60.14104 -3.77418  -84.74205  1.000 285.83053 ? 213 GLY A C   1 
ATOM   1608 O O   . GLY A 1 219 ? 61.08508 -4.23613  -84.09549  1.000 290.77240 ? 213 GLY A O   1 
ATOM   1609 N N   . TYR A 1 220 ? 59.33618 -2.82453  -84.26631  1.000 291.55063 ? 214 TYR A N   1 
ATOM   1610 C CA  . TYR A 1 220 ? 59.48486 -2.29596  -82.91982  1.000 305.16619 ? 214 TYR A CA  1 
ATOM   1611 C C   . TYR A 1 220 ? 58.26130 -2.49996  -82.03852  1.000 286.41243 ? 214 TYR A C   1 
ATOM   1612 O O   . TYR A 1 220 ? 58.38922 -2.41519  -80.81210  1.000 282.87669 ? 214 TYR A O   1 
ATOM   1613 C CB  . TYR A 1 220 ? 59.81369 -0.79380  -82.96196  1.000 334.65743 ? 214 TYR A CB  1 
ATOM   1614 C CG  . TYR A 1 220 ? 61.08961 -0.44288  -83.70015  1.000 324.58364 ? 214 TYR A CG  1 
ATOM   1615 C CD1 . TYR A 1 220 ? 62.33422 -0.67329  -83.12697  1.000 327.72167 ? 214 TYR A CD1 1 
ATOM   1616 C CD2 . TYR A 1 220 ? 61.04807 0.13811   -84.96194  1.000 303.10751 ? 214 TYR A CD2 1 
ATOM   1617 C CE1 . TYR A 1 220 ? 63.50193 -0.34732  -83.79528  1.000 319.86051 ? 214 TYR A CE1 1 
ATOM   1618 C CE2 . TYR A 1 220 ? 62.21036 0.46835   -85.63729  1.000 298.64817 ? 214 TYR A CE2 1 
ATOM   1619 C CZ  . TYR A 1 220 ? 63.43391 0.22339   -85.04930  1.000 308.40306 ? 214 TYR A CZ  1 
ATOM   1620 O OH  . TYR A 1 220 ? 64.59288 0.54988   -85.71676  1.000 289.94126 ? 214 TYR A OH  1 
ATOM   1621 N N   . SER A 1 221 ? 57.09232 -2.77256  -82.61637  1.000 277.03758 ? 215 SER A N   1 
ATOM   1622 C CA  . SER A 1 221 ? 55.85142 -2.90108  -81.86174  1.000 268.48481 ? 215 SER A CA  1 
ATOM   1623 C C   . SER A 1 221 ? 55.50265 -4.34220  -81.51870  1.000 256.37437 ? 215 SER A C   1 
ATOM   1624 O O   . SER A 1 221 ? 55.04968 -4.61318  -80.40233  1.000 254.09099 ? 215 SER A O   1 
ATOM   1625 C CB  . SER A 1 221 ? 54.69292 -2.27472  -82.64450  1.000 270.17216 ? 215 SER A CB  1 
ATOM   1626 O OG  . SER A 1 221 ? 54.51901 -2.91646  -83.89622  1.000 263.05151 ? 215 SER A OG  1 
ATOM   1627 N N   . ARG A 1 222 ? 55.69819 -5.27068  -82.45114  1.000 248.48518 ? 216 ARG A N   1 
ATOM   1628 C CA  . ARG A 1 222 ? 55.33413 -6.65986  -82.21602  1.000 244.91579 ? 216 ARG A CA  1 
ATOM   1629 C C   . ARG A 1 222 ? 56.21344 -7.27756  -81.13454  1.000 255.91832 ? 216 ARG A C   1 
ATOM   1630 O O   . ARG A 1 222 ? 57.36567 -6.88361  -80.93482  1.000 261.30067 ? 216 ARG A O   1 
ATOM   1631 C CB  . ARG A 1 222 ? 55.44999 -7.46873  -83.50822  1.000 238.11867 ? 216 ARG A CB  1 
ATOM   1632 C CG  . ARG A 1 222 ? 54.52555 -6.99856  -84.61887  1.000 245.01630 ? 216 ARG A CG  1 
ATOM   1633 C CD  . ARG A 1 222 ? 54.65660 -7.86758  -85.85724  1.000 252.62882 ? 216 ARG A CD  1 
ATOM   1634 N NE  . ARG A 1 222 ? 53.70707 -7.48469  -86.89542  1.000 258.85340 ? 216 ARG A NE  1 
ATOM   1635 C CZ  . ARG A 1 222 ? 53.58879 -8.09769  -88.06526  1.000 254.22552 ? 216 ARG A CZ  1 
ATOM   1636 N NH1 . ARG A 1 222 ? 54.34822 -9.13339  -88.38278  1.000 258.46451 ? 216 ARG A NH1 1 
ATOM   1637 N NH2 . ARG A 1 222 ? 52.68548 -7.66102  -88.93828  1.000 243.91539 ? 216 ARG A NH2 1 
ATOM   1638 N N   . ASP A 1 223 ? 55.65193 -8.25527  -80.43020  1.000 249.25526 ? 217 ASP A N   1 
ATOM   1639 C CA  . ASP A 1 223 ? 56.35826 -8.97023  -79.37805  1.000 252.60575 ? 217 ASP A CA  1 
ATOM   1640 C C   . ASP A 1 223 ? 56.87616 -10.29988 -79.90700  1.000 256.24849 ? 217 ASP A C   1 
ATOM   1641 O O   . ASP A 1 223 ? 56.19720 -10.97990 -80.68222  1.000 245.87279 ? 217 ASP A O   1 
ATOM   1642 C CB  . ASP A 1 223 ? 55.45035 -9.21222  -78.17113  1.000 243.90698 ? 217 ASP A CB  1 
ATOM   1643 C CG  . ASP A 1 223 ? 55.03235 -7.92709  -77.48979  1.000 256.16923 ? 217 ASP A CG  1 
ATOM   1644 O OD1 . ASP A 1 223 ? 55.70321 -6.89417  -77.69662  1.000 260.54779 ? 217 ASP A OD1 1 
ATOM   1645 O OD2 . ASP A 1 223 ? 54.03582 -7.95235  -76.74028  1.000 263.50348 ? 217 ASP A OD2 1 
ATOM   1646 N N   . LEU A 1 224 ? 58.08255 -10.66471 -79.48172  1.000 268.64708 ? 218 LEU A N   1 
ATOM   1647 C CA  . LEU A 1 224 ? 58.66661 -11.93454 -79.88852  1.000 258.02230 ? 218 LEU A CA  1 
ATOM   1648 C C   . LEU A 1 224 ? 57.96854 -13.08254 -79.17319  1.000 242.25652 ? 218 LEU A C   1 
ATOM   1649 O O   . LEU A 1 224 ? 57.79132 -13.05101 -77.95151  1.000 245.24558 ? 218 LEU A O   1 
ATOM   1650 C CB  . LEU A 1 224 ? 60.16379 -11.95345 -79.58424  1.000 251.35684 ? 218 LEU A CB  1 
ATOM   1651 C CG  . LEU A 1 224 ? 60.94726 -13.17287 -80.07444  1.000 228.52708 ? 218 LEU A CG  1 
ATOM   1652 C CD1 . LEU A 1 224 ? 60.76254 -13.36787 -81.57131  1.000 224.64390 ? 218 LEU A CD1 1 
ATOM   1653 C CD2 . LEU A 1 224 ? 62.42205 -13.03424 -79.72921  1.000 247.32502 ? 218 LEU A CD2 1 
ATOM   1654 N N   . ASP A 1 225 ? 57.56756 -14.09927 -79.93933  1.000 230.41151 ? 219 ASP A N   1 
ATOM   1655 C CA  . ASP A 1 225 ? 56.93667 -15.26580 -79.33378  1.000 234.68263 ? 219 ASP A CA  1 
ATOM   1656 C C   . ASP A 1 225 ? 57.90453 -16.01289 -78.42590  1.000 226.86298 ? 219 ASP A C   1 
ATOM   1657 O O   . ASP A 1 225 ? 57.47331 -16.70019 -77.49351  1.000 220.18047 ? 219 ASP A O   1 
ATOM   1658 C CB  . ASP A 1 225 ? 56.39838 -16.19677 -80.41951  1.000 240.21485 ? 219 ASP A CB  1 
ATOM   1659 C CG  . ASP A 1 225 ? 55.42385 -17.22233 -79.87587  1.000 247.68585 ? 219 ASP A CG  1 
ATOM   1660 O OD1 . ASP A 1 225 ? 54.94088 -17.04086 -78.73832  1.000 240.62702 ? 219 ASP A OD1 1 
ATOM   1661 O OD2 . ASP A 1 225 ? 55.14267 -18.21120 -80.58481  1.000 249.46904 ? 219 ASP A OD2 1 
ATOM   1662 N N   . THR A 1 226 ? 59.20970 -15.88774 -78.67742  1.000 226.00788 ? 220 THR A N   1 
ATOM   1663 C CA  . THR A 1 226 ? 60.19407 -16.53827 -77.81950  1.000 233.81804 ? 220 THR A CA  1 
ATOM   1664 C C   . THR A 1 226 ? 60.20480 -15.92148 -76.42610  1.000 222.90141 ? 220 THR A C   1 
ATOM   1665 O O   . THR A 1 226 ? 60.23258 -16.64250 -75.42226  1.000 209.68212 ? 220 THR A O   1 
ATOM   1666 C CB  . THR A 1 226 ? 61.58278 -16.45113 -78.45350  1.000 238.47881 ? 220 THR A CB  1 
ATOM   1667 O OG1 . THR A 1 226 ? 61.54312 -17.00324 -79.77544  1.000 230.58269 ? 220 THR A OG1 1 
ATOM   1668 C CG2 . THR A 1 226 ? 62.60043 -17.21696 -77.62056  1.000 242.91080 ? 220 THR A CG2 1 
ATOM   1669 N N   . ASP A 1 227 ? 60.17588 -14.58903 -76.34383  1.000 240.09849 ? 221 ASP A N   1 
ATOM   1670 C CA  . ASP A 1 227 ? 60.20207 -13.92932 -75.04280  1.000 256.91291 ? 221 ASP A CA  1 
ATOM   1671 C C   . ASP A 1 227 ? 58.89550 -14.12158 -74.28181  1.000 253.12465 ? 221 ASP A C   1 
ATOM   1672 O O   . ASP A 1 227 ? 58.90806 -14.21053 -73.04916  1.000 264.61257 ? 221 ASP A O   1 
ATOM   1673 C CB  . ASP A 1 227 ? 60.50083 -12.43858 -75.21337  1.000 280.21163 ? 221 ASP A CB  1 
ATOM   1674 C CG  . ASP A 1 227 ? 61.88031 -12.17991 -75.79267  1.000 270.36456 ? 221 ASP A CG  1 
ATOM   1675 O OD1 . ASP A 1 227 ? 62.78594 -13.01269 -75.57644  1.000 270.37138 ? 221 ASP A OD1 1 
ATOM   1676 O OD2 . ASP A 1 227 ? 62.05975 -11.14006 -76.46171  1.000 268.45807 ? 221 ASP A OD2 1 
ATOM   1677 N N   . VAL A 1 228 ? 57.76527 -14.19193 -74.98853  1.000 242.02214 ? 222 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 228 ? 56.47767 -14.31840 -74.31145  1.000 242.68448 ? 222 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 228 ? 56.30890 -15.71729 -73.73076  1.000 229.57804 ? 222 VAL A C   1 
ATOM   1680 O O   . VAL A 1 228 ? 55.83140 -15.88067 -72.60155  1.000 235.65899 ? 222 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 228 ? 55.33071 -13.95852 -75.27350  1.000 225.29925 ? 222 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 228 ? 53.98192 -14.20434 -74.61310  1.000 204.65227 ? 222 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 228 ? 55.45115 -12.50912 -75.71552  1.000 231.18639 ? 222 VAL A CG2 1 
ATOM   1684 N N   . VAL A 1 229 ? 56.70063 -16.74640 -74.48484  1.000 214.05623 ? 223 VAL A N   1 
ATOM   1685 C CA  . VAL A 1 229 ? 56.55098 -18.11658 -74.00304  1.000 231.55629 ? 223 VAL A CA  1 
ATOM   1686 C C   . VAL A 1 229 ? 57.48314 -18.37908 -72.82541  1.000 243.00859 ? 223 VAL A C   1 
ATOM   1687 O O   . VAL A 1 229 ? 57.09102 -19.01017 -71.83621  1.000 244.62038 ? 223 VAL A O   1 
ATOM   1688 C CB  . VAL A 1 229 ? 56.78694 -19.11421 -75.15200  1.000 227.31181 ? 223 VAL A CB  1 
ATOM   1689 C CG1 . VAL A 1 229 ? 56.87815 -20.53481 -74.61729  1.000 220.34481 ? 223 VAL A CG1 1 
ATOM   1690 C CG2 . VAL A 1 229 ? 55.67140 -19.00707 -76.17930  1.000 237.84703 ? 223 VAL A CG2 1 
ATOM   1691 N N   . ILE A 1 230 ? 58.72566 -17.89607 -72.90549  1.000 244.86472 ? 224 ILE A N   1 
ATOM   1692 C CA  . ILE A 1 230 ? 59.67584 -18.10669 -71.81530  1.000 244.78451 ? 224 ILE A CA  1 
ATOM   1693 C C   . ILE A 1 230 ? 59.20807 -17.39280 -70.55265  1.000 242.41564 ? 224 ILE A C   1 
ATOM   1694 O O   . ILE A 1 230 ? 59.32824 -17.92310 -69.44083  1.000 236.66958 ? 224 ILE A O   1 
ATOM   1695 C CB  . ILE A 1 230 ? 61.08608 -17.65331 -72.23910  1.000 247.79947 ? 224 ILE A CB  1 
ATOM   1696 C CG1 . ILE A 1 230 ? 61.64003 -18.57935 -73.32390  1.000 239.63622 ? 224 ILE A CG1 1 
ATOM   1697 C CG2 . ILE A 1 230 ? 62.02638 -17.61854 -71.04270  1.000 246.44710 ? 224 ILE A CG2 1 
ATOM   1698 C CD1 . ILE A 1 230 ? 63.01809 -18.18998 -73.81397  1.000 243.44661 ? 224 ILE A CD1 1 
ATOM   1699 N N   . ASP A 1 231 ? 58.65771 -16.18490 -70.70221  1.000 241.05544 ? 225 ASP A N   1 
ATOM   1700 C CA  . ASP A 1 231 ? 58.15456 -15.45580 -69.54180  1.000 241.55210 ? 225 ASP A CA  1 
ATOM   1701 C C   . ASP A 1 231 ? 56.96187 -16.16697 -68.91410  1.000 239.94725 ? 225 ASP A C   1 
ATOM   1702 O O   . ASP A 1 231 ? 56.82894 -16.19873 -67.68528  1.000 245.06524 ? 225 ASP A O   1 
ATOM   1703 C CB  . ASP A 1 231 ? 57.78134 -14.02660 -69.93638  1.000 251.15175 ? 225 ASP A CB  1 
ATOM   1704 C CG  . ASP A 1 231 ? 58.99647 -13.15678 -70.19786  1.000 276.08026 ? 225 ASP A CG  1 
ATOM   1705 O OD1 . ASP A 1 231 ? 60.13164 -13.65592 -70.04683  1.000 284.86495 ? 225 ASP A OD1 1 
ATOM   1706 O OD2 . ASP A 1 231 ? 58.81612 -11.97305 -70.55432  1.000 292.72394 ? 225 ASP A OD2 1 
ATOM   1707 N N   . LYS A 1 232 ? 56.08410 -16.74448 -69.73857  1.000 240.04678 ? 226 LYS A N   1 
ATOM   1708 C CA  . LYS A 1 232 ? 54.94412 -17.47722 -69.19771  1.000 246.58266 ? 226 LYS A CA  1 
ATOM   1709 C C   . LYS A 1 232 ? 55.37313 -18.79254 -68.55924  1.000 236.40356 ? 226 LYS A C   1 
ATOM   1710 O O   . LYS A 1 232 ? 54.71199 -19.27322 -67.63167  1.000 234.24096 ? 226 LYS A O   1 
ATOM   1711 C CB  . LYS A 1 232 ? 53.90743 -17.72668 -70.29378  1.000 242.73848 ? 226 LYS A CB  1 
ATOM   1712 C CG  . LYS A 1 232 ? 53.24397 -16.46178 -70.82002  1.000 234.43910 ? 226 LYS A CG  1 
ATOM   1713 C CD  . LYS A 1 232 ? 52.56319 -15.68754 -69.70197  1.000 244.38046 ? 226 LYS A CD  1 
ATOM   1714 C CE  . LYS A 1 232 ? 51.93139 -14.40474 -70.21920  1.000 237.97069 ? 226 LYS A CE  1 
ATOM   1715 N NZ  . LYS A 1 232 ? 51.27006 -13.63407 -69.12919  1.000 218.50983 ? 226 LYS A NZ  1 
ATOM   1716 N N   . LEU A 1 233 ? 56.46923 -19.38722 -69.03580  1.000 237.24137 ? 227 LEU A N   1 
ATOM   1717 C CA  . LEU A 1 233 ? 56.98282 -20.60235 -68.41252  1.000 246.82689 ? 227 LEU A CA  1 
ATOM   1718 C C   . LEU A 1 233 ? 57.74545 -20.29125 -67.13068  1.000 250.03517 ? 227 LEU A C   1 
ATOM   1719 O O   . LEU A 1 233 ? 57.67673 -21.05780 -66.16337  1.000 256.36711 ? 227 LEU A O   1 
ATOM   1720 C CB  . LEU A 1 233 ? 57.87605 -21.36352 -69.39279  1.000 240.75855 ? 227 LEU A CB  1 
ATOM   1721 C CG  . LEU A 1 233 ? 57.17338 -22.03011 -70.57670  1.000 247.90474 ? 227 LEU A CG  1 
ATOM   1722 C CD1 . LEU A 1 233 ? 58.18359 -22.71804 -71.48104  1.000 233.47406 ? 227 LEU A CD1 1 
ATOM   1723 C CD2 . LEU A 1 233 ? 56.12356 -23.01793 -70.08992  1.000 246.13656 ? 227 LEU A CD2 1 
ATOM   1724 N N   . LYS A 1 234 ? 58.47825 -19.17521 -67.10570  1.000 253.12084 ? 228 LYS A N   1 
ATOM   1725 C CA  . LYS A 1 234 ? 59.17590 -18.76942 -65.89169  1.000 263.82144 ? 228 LYS A CA  1 
ATOM   1726 C C   . LYS A 1 234 ? 58.22334 -18.24263 -64.82637  1.000 258.40525 ? 228 LYS A C   1 
ATOM   1727 O O   . LYS A 1 234 ? 58.58562 -18.22238 -63.64517  1.000 248.34511 ? 228 LYS A O   1 
ATOM   1728 C CB  . LYS A 1 234 ? 60.23112 -17.70966 -66.21581  1.000 259.60891 ? 228 LYS A CB  1 
ATOM   1729 C CG  . LYS A 1 234 ? 61.47147 -18.24984 -66.91283  1.000 249.31394 ? 228 LYS A CG  1 
ATOM   1730 C CD  . LYS A 1 234 ? 62.46928 -17.13634 -67.19665  1.000 249.56856 ? 228 LYS A CD  1 
ATOM   1731 C CE  . LYS A 1 234 ? 63.78786 -17.68745 -67.71497  1.000 240.90564 ? 228 LYS A CE  1 
ATOM   1732 N NZ  . LYS A 1 234 ? 64.47150 -18.53413 -66.69874  1.000 236.60616 ? 228 LYS A NZ  1 
ATOM   1733 N N   . SER A 1 235 ? 57.02052 -17.81611 -65.21326  1.000 253.52364 ? 229 SER A N   1 
ATOM   1734 C CA  . SER A 1 235 ? 56.01542 -17.33656 -64.27490  1.000 252.48569 ? 229 SER A CA  1 
ATOM   1735 C C   . SER A 1 235 ? 54.95374 -18.38874 -63.97329  1.000 245.08127 ? 229 SER A C   1 
ATOM   1736 O O   . SER A 1 235 ? 53.83840 -18.03890 -63.57286  1.000 235.56235 ? 229 SER A O   1 
ATOM   1737 C CB  . SER A 1 235 ? 55.35848 -16.06193 -64.80725  1.000 259.47052 ? 229 SER A CB  1 
ATOM   1738 O OG  . SER A 1 235 ? 54.68534 -16.30636 -66.03009  1.000 265.86247 ? 229 SER A OG  1 
ATOM   1739 N N   . ALA A 1 236 ? 55.27533 -19.66606 -64.16143  1.000 243.62994 ? 230 ALA A N   1 
ATOM   1740 C CA  . ALA A 1 236 ? 54.33463 -20.74001 -63.87626  1.000 244.62028 ? 230 ALA A CA  1 
ATOM   1741 C C   . ALA A 1 236 ? 54.37300 -21.08678 -62.39376  1.000 249.51508 ? 230 ALA A C   1 
ATOM   1742 O O   . ALA A 1 236 ? 55.45011 -21.25477 -61.81440  1.000 239.63115 ? 230 ALA A O   1 
ATOM   1743 C CB  . ALA A 1 236 ? 54.66247 -21.97165 -64.71742  1.000 233.33960 ? 230 ALA A CB  1 
ATOM   1744 N N   . LYS A 1 237 ? 53.19555 -21.19875 -61.78137  1.000 254.92817 ? 231 LYS A N   1 
ATOM   1745 C CA  . LYS A 1 237 ? 53.08976 -21.46544 -60.35320  1.000 258.28304 ? 231 LYS A CA  1 
ATOM   1746 C C   . LYS A 1 237 ? 52.50347 -22.82583 -60.01708  1.000 255.76709 ? 231 LYS A C   1 
ATOM   1747 O O   . LYS A 1 237 ? 52.86222 -23.39582 -58.98488  1.000 257.48927 ? 231 LYS A O   1 
ATOM   1748 C CB  . LYS A 1 237 ? 52.23940 -20.38633 -59.66693  1.000 255.93801 ? 231 LYS A CB  1 
ATOM   1749 C CG  . LYS A 1 237 ? 53.00928 -19.14737 -59.22160  1.000 255.62018 ? 231 LYS A CG  1 
ATOM   1750 C CD  . LYS A 1 237 ? 53.34438 -18.22758 -60.38669  1.000 263.79008 ? 231 LYS A CD  1 
ATOM   1751 C CE  . LYS A 1 237 ? 54.02247 -16.95076 -59.90754  1.000 276.08395 ? 231 LYS A CE  1 
ATOM   1752 N NZ  . LYS A 1 237 ? 54.31410 -16.01582 -61.03072  1.000 243.45213 ? 231 LYS A NZ  1 
ATOM   1753 N N   . THR A 1 238 ? 51.61659 -23.36249 -60.85263  1.000 254.03632 ? 232 THR A N   1 
ATOM   1754 C CA  . THR A 1 238 ? 50.88551 -24.56471 -60.47257  1.000 263.69242 ? 232 THR A CA  1 
ATOM   1755 C C   . THR A 1 238 ? 51.03936 -25.70402 -61.47445  1.000 263.34484 ? 232 THR A C   1 
ATOM   1756 O O   . THR A 1 238 ? 51.32165 -26.83706 -61.07619  1.000 266.18137 ? 232 THR A O   1 
ATOM   1757 C CB  . THR A 1 238 ? 49.39786 -24.23640 -60.27870  1.000 273.38308 ? 232 THR A CB  1 
ATOM   1758 O OG1 . THR A 1 238 ? 48.87443 -23.65517 -61.47917  1.000 292.85970 ? 232 THR A OG1 1 
ATOM   1759 C CG2 . THR A 1 238 ? 49.20902 -23.25973 -59.12642  1.000 243.72992 ? 232 THR A CG2 1 
ATOM   1760 N N   . SER A 1 239 ? 50.85693 -25.43296 -62.76576  1.000 265.96364 ? 233 SER A N   1 
ATOM   1761 C CA  . SER A 1 239 ? 50.86232 -26.50803 -63.74862  1.000 242.78572 ? 233 SER A CA  1 
ATOM   1762 C C   . SER A 1 239 ? 51.37671 -26.00331 -65.08838  1.000 235.69132 ? 233 SER A C   1 
ATOM   1763 O O   . SER A 1 239 ? 51.18971 -24.83738 -65.44650  1.000 251.24971 ? 233 SER A O   1 
ATOM   1764 C CB  . SER A 1 239 ? 49.46445 -27.11327 -63.92701  1.000 242.97635 ? 233 SER A CB  1 
ATOM   1765 O OG  . SER A 1 239 ? 48.56253 -26.15782 -64.45662  1.000 252.58635 ? 233 SER A OG  1 
ATOM   1766 N N   . ILE A 1 240 ? 52.02695 -26.90403 -65.82342  1.000 206.87156 ? 234 ILE A N   1 
ATOM   1767 C CA  . ILE A 1 240 ? 52.48104 -26.65627 -67.18684  1.000 228.16742 ? 234 ILE A CA  1 
ATOM   1768 C C   . ILE A 1 240 ? 52.07613 -27.85456 -68.03216  1.000 226.08007 ? 234 ILE A C   1 
ATOM   1769 O O   . ILE A 1 240 ? 52.55680 -28.97065 -67.80185  1.000 216.25281 ? 234 ILE A O   1 
ATOM   1770 C CB  . ILE A 1 240 ? 54.00015 -26.43175 -67.26619  1.000 237.97475 ? 234 ILE A CB  1 
ATOM   1771 C CG1 . ILE A 1 240 ? 54.39322 -25.13650 -66.55624  1.000 234.46644 ? 234 ILE A CG1 1 
ATOM   1772 C CG2 . ILE A 1 240 ? 54.45781 -26.40575 -68.71611  1.000 231.66356 ? 234 ILE A CG2 1 
ATOM   1773 C CD1 . ILE A 1 240 ? 55.86867 -24.81837 -66.65118  1.000 238.19488 ? 234 ILE A CD1 1 
ATOM   1774 N N   . ASP A 1 241 ? 51.19525 -27.62821 -69.00286  1.000 245.06946 ? 235 ASP A N   1 
ATOM   1775 C CA  . ASP A 1 241 ? 50.71184 -28.67620 -69.89361  1.000 254.00964 ? 235 ASP A CA  1 
ATOM   1776 C C   . ASP A 1 241 ? 51.10201 -28.32162 -71.32056  1.000 243.03388 ? 235 ASP A C   1 
ATOM   1777 O O   . ASP A 1 241 ? 50.69670 -27.27384 -71.83546  1.000 241.66912 ? 235 ASP A O   1 
ATOM   1778 C CB  . ASP A 1 241 ? 49.19649 -28.84569 -69.76945  1.000 260.34450 ? 235 ASP A CB  1 
ATOM   1779 C CG  . ASP A 1 241 ? 48.77408 -29.30865 -68.38859  1.000 241.94161 ? 235 ASP A CG  1 
ATOM   1780 O OD1 . ASP A 1 241 ? 49.53767 -30.06577 -67.75248  1.000 244.30991 ? 235 ASP A OD1 1 
ATOM   1781 O OD2 . ASP A 1 241 ? 47.67878 -28.91446 -67.93905  1.000 226.72000 ? 235 ASP A OD2 1 
ATOM   1782 N N   . ILE A 1 242 ? 51.88752 -29.19045 -71.95434  1.000 225.51263 ? 236 ILE A N   1 
ATOM   1783 C CA  . ILE A 1 242 ? 52.40591 -28.95454 -73.29629  1.000 227.20493 ? 236 ILE A CA  1 
ATOM   1784 C C   . ILE A 1 242 ? 52.11501 -30.17568 -74.15659  1.000 223.34732 ? 236 ILE A C   1 
ATOM   1785 O O   . ILE A 1 242 ? 52.37536 -31.31056 -73.74147  1.000 208.58938 ? 236 ILE A O   1 
ATOM   1786 C CB  . ILE A 1 242 ? 53.91745 -28.65427 -73.28114  1.000 229.86702 ? 236 ILE A CB  1 
ATOM   1787 C CG1 . ILE A 1 242 ? 54.21354 -27.45669 -72.37730  1.000 230.59883 ? 236 ILE A CG1 1 
ATOM   1788 C CG2 . ILE A 1 242 ? 54.42751 -28.39800 -74.69187  1.000 243.40620 ? 236 ILE A CG2 1 
ATOM   1789 C CD1 . ILE A 1 242 ? 55.66298 -27.04027 -72.36605  1.000 247.84067 ? 236 ILE A CD1 1 
ATOM   1790 N N   . GLU A 1 243 ? 51.57360 -29.94034 -75.35219  1.000 232.89247 ? 237 GLU A N   1 
ATOM   1791 C CA  . GLU A 1 243 ? 51.34318 -30.97932 -76.35697  1.000 218.20768 ? 237 GLU A CA  1 
ATOM   1792 C C   . GLU A 1 243 ? 51.94594 -30.46711 -77.66195  1.000 225.84920 ? 237 GLU A C   1 
ATOM   1793 O O   . GLU A 1 243 ? 51.28068 -29.77005 -78.43268  1.000 223.84346 ? 237 GLU A O   1 
ATOM   1794 C CB  . GLU A 1 243 ? 49.85781 -31.30078 -76.50205  1.000 213.77310 ? 237 GLU A CB  1 
ATOM   1795 C CG  . GLU A 1 243 ? 49.54979 -32.33551 -77.57521  1.000 212.46457 ? 237 GLU A CG  1 
ATOM   1796 C CD  . GLU A 1 243 ? 48.06341 -32.58686 -77.73513  1.000 220.82144 ? 237 GLU A CD  1 
ATOM   1797 O OE1 . GLU A 1 243 ? 47.29656 -32.22489 -76.81819  1.000 241.90016 ? 237 GLU A OE1 1 
ATOM   1798 O OE2 . GLU A 1 243 ? 47.66153 -33.14283 -78.77945  1.000 188.15098 ? 237 GLU A OE2 1 
ATOM   1799 N N   . HIS A 1 244 ? 53.21000 -30.80633 -77.90108  1.000 232.31789 ? 238 HIS A N   1 
ATOM   1800 C CA  . HIS A 1 244 ? 53.94226 -30.35909 -79.07708  1.000 243.25517 ? 238 HIS A CA  1 
ATOM   1801 C C   . HIS A 1 244 ? 54.58827 -31.55948 -79.75890  1.000 245.57534 ? 238 HIS A C   1 
ATOM   1802 O O   . HIS A 1 244 ? 54.40260 -32.71105 -79.35349  1.000 247.89496 ? 238 HIS A O   1 
ATOM   1803 C CB  . HIS A 1 244 ? 54.99818 -29.30871 -78.70691  1.000 233.17219 ? 238 HIS A CB  1 
ATOM   1804 C CG  . HIS A 1 244 ? 54.47692 -27.90528 -78.68829  1.000 242.33686 ? 238 HIS A CG  1 
ATOM   1805 N ND1 . HIS A 1 244 ? 54.97632 -26.91639 -79.50831  1.000 234.37898 ? 238 HIS A ND1 1 
ATOM   1806 C CD2 . HIS A 1 244 ? 53.49913 -27.32534 -77.95272  1.000 249.76431 ? 238 HIS A CD2 1 
ATOM   1807 C CE1 . HIS A 1 244 ? 54.33118 -25.78721 -79.27656  1.000 227.92725 ? 238 HIS A CE1 1 
ATOM   1808 N NE2 . HIS A 1 244 ? 53.42836 -26.00849 -78.33817  1.000 234.68659 ? 238 HIS A NE2 1 
ATOM   1809 N N   . LEU A 1 245 ? 55.35815 -31.27617 -80.81085  1.000 244.00179 ? 239 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 245 ? 56.03612 -32.33506 -81.55129  1.000 244.54261 ? 239 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 245 ? 57.15255 -32.95288 -80.71624  1.000 243.21257 ? 239 LEU A C   1 
ATOM   1812 O O   . LEU A 1 245 ? 57.17292 -34.16693 -80.48099  1.000 236.19330 ? 239 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 245 ? 56.58175 -31.77614 -82.86792  1.000 250.49558 ? 239 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 245 ? 56.92191 -32.75997 -83.98789  1.000 263.05554 ? 239 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 245 ? 55.65805 -33.40245 -84.53526  1.000 234.59378 ? 239 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 245 ? 57.69238 -32.05873 -85.09593  1.000 285.80905 ? 239 LEU A CD2 1 
ATOM   1817 N N   . ALA A 1 246 ? 58.08933 -32.12637 -80.25503  1.000 242.11233 ? 240 ALA A N   1 
ATOM   1818 C CA  . ALA A 1 246 ? 59.18969 -32.58324 -79.41802  1.000 228.59046 ? 240 ALA A CA  1 
ATOM   1819 C C   . ALA A 1 246 ? 59.80480 -31.37996 -78.71989  1.000 227.53285 ? 240 ALA A C   1 
ATOM   1820 O O   . ALA A 1 246 ? 59.74906 -30.25703 -79.22791  1.000 249.60903 ? 240 ALA A O   1 
ATOM   1821 C CB  . ALA A 1 246 ? 60.25321 -33.32816 -80.23306  1.000 233.96327 ? 240 ALA A CB  1 
ATOM   1822 N N   . ILE A 1 247 ? 60.38961 -31.62746 -77.54821  1.000 227.63790 ? 241 ILE A N   1 
ATOM   1823 C CA  . ILE A 1 247 ? 61.03466 -30.57288 -76.77260  1.000 232.54111 ? 241 ILE A CA  1 
ATOM   1824 C C   . ILE A 1 247 ? 62.51548 -30.90734 -76.62515  1.000 229.44721 ? 241 ILE A C   1 
ATOM   1825 O O   . ILE A 1 247 ? 63.15527 -30.54269 -75.63165  1.000 215.87844 ? 241 ILE A O   1 
ATOM   1826 C CB  . ILE A 1 247 ? 60.35516 -30.39056 -75.40094  1.000 240.29757 ? 241 ILE A CB  1 
ATOM   1827 C CG1 . ILE A 1 247 ? 58.83956 -30.56081 -75.52554  1.000 258.88388 ? 241 ILE A CG1 1 
ATOM   1828 C CG2 . ILE A 1 247 ? 60.64663 -29.00668 -74.82975  1.000 223.63712 ? 241 ILE A CG2 1 
ATOM   1829 C CD1 . ILE A 1 247 ? 58.15624 -29.44814 -76.29855  1.000 263.35224 ? 241 ILE A CD1 1 
ATOM   1830 N N   . VAL A 1 248 ? 63.06779 -31.60550 -77.60901  1.000 233.76396 ? 242 VAL A N   1 
ATOM   1831 C CA  . VAL A 1 248 ? 64.50390 -31.90785 -77.59381  1.000 232.99346 ? 242 VAL A CA  1 
ATOM   1832 C C   . VAL A 1 248 ? 65.28601 -30.61186 -77.78576  1.000 232.61614 ? 242 VAL A C   1 
ATOM   1833 O O   . VAL A 1 248 ? 65.03000 -29.87517 -78.75538  1.000 245.25875 ? 242 VAL A O   1 
ATOM   1834 C CB  . VAL A 1 248 ? 64.84714 -32.92820 -78.68173  1.000 254.96930 ? 242 VAL A CB  1 
ATOM   1835 C CG1 . VAL A 1 248 ? 66.34335 -33.21375 -78.69290  1.000 241.50715 ? 242 VAL A CG1 1 
ATOM   1836 C CG2 . VAL A 1 248 ? 64.05813 -34.21394 -78.47168  1.000 226.04093 ? 242 VAL A CG2 1 
ATOM   1837 N N   . PRO A 1 249 ? 66.23525 -30.28698 -76.90320  1.000 229.89427 ? 243 PRO A N   1 
ATOM   1838 C CA  . PRO A 1 249 ? 66.93316 -28.99636 -77.00252  1.000 231.85771 ? 243 PRO A CA  1 
ATOM   1839 C C   . PRO A 1 249 ? 67.90506 -28.89744 -78.16580  1.000 221.99090 ? 243 PRO A C   1 
ATOM   1840 O O   . PRO A 1 249 ? 68.49308 -27.82794 -78.36420  1.000 224.02321 ? 243 PRO A O   1 
ATOM   1841 C CB  . PRO A 1 249 ? 67.67638 -28.90483 -75.66305  1.000 241.15918 ? 243 PRO A CB  1 
ATOM   1842 C CG  . PRO A 1 249 ? 67.91243 -30.32642 -75.28064  1.000 243.53050 ? 243 PRO A CG  1 
ATOM   1843 C CD  . PRO A 1 249 ? 66.69995 -31.08217 -75.75316  1.000 243.77153 ? 243 PRO A CD  1 
ATOM   1844 N N   . THR A 1 250 ? 68.09790 -29.96182 -78.93899  1.000 228.49981 ? 244 THR A N   1 
ATOM   1845 C CA  . THR A 1 250 ? 69.05203 -29.97024 -80.03815  1.000 245.20089 ? 244 THR A CA  1 
ATOM   1846 C C   . THR A 1 250 ? 68.32803 -30.27543 -81.34101  1.000 254.28049 ? 244 THR A C   1 
ATOM   1847 O O   . THR A 1 250 ? 67.61343 -31.27857 -81.43936  1.000 264.48693 ? 244 THR A O   1 
ATOM   1848 C CB  . THR A 1 250 ? 70.16197 -30.99746 -79.79813  1.000 242.83243 ? 244 THR A CB  1 
ATOM   1849 O OG1 . THR A 1 250 ? 70.75347 -30.77180 -78.51250  1.000 235.36366 ? 244 THR A OG1 1 
ATOM   1850 C CG2 . THR A 1 250 ? 71.23500 -30.87518 -80.86743  1.000 251.46053 ? 244 THR A CG2 1 
ATOM   1851 N N   . THR A 1 251 ? 68.51244 -29.40828 -82.33282  1.000 248.68961 ? 245 THR A N   1 
ATOM   1852 C CA  . THR A 1 251 ? 67.97476 -29.60455 -83.66907  1.000 244.70005 ? 245 THR A CA  1 
ATOM   1853 C C   . THR A 1 251 ? 69.12186 -29.74111 -84.66178  1.000 264.35788 ? 245 THR A C   1 
ATOM   1854 O O   . THR A 1 251 ? 70.27281 -29.41170 -84.36205  1.000 278.84647 ? 245 THR A O   1 
ATOM   1855 C CB  . THR A 1 251 ? 67.05694 -28.44656 -84.08435  1.000 228.56409 ? 245 THR A CB  1 
ATOM   1856 O OG1 . THR A 1 251 ? 67.79137 -27.21635 -84.05556  1.000 244.47837 ? 245 THR A OG1 1 
ATOM   1857 C CG2 . THR A 1 251 ? 65.86751 -28.34417 -83.14211  1.000 215.39251 ? 245 THR A CG2 1 
ATOM   1858 N N   . ARG A 1 252 ? 68.79727 -30.23249 -85.85475  1.000 258.69331 ? 246 ARG A N   1 
ATOM   1859 C CA  . ARG A 1 252 ? 69.78780 -30.48359 -86.89997  1.000 265.11839 ? 246 ARG A CA  1 
ATOM   1860 C C   . ARG A 1 252 ? 69.43631 -29.64057 -88.12235  1.000 276.82019 ? 246 ARG A C   1 
ATOM   1861 O O   . ARG A 1 252 ? 68.55921 -30.00942 -88.90987  1.000 272.17160 ? 246 ARG A O   1 
ATOM   1862 C CB  . ARG A 1 252 ? 69.85154 -31.96951 -87.24582  1.000 235.66362 ? 246 ARG A CB  1 
ATOM   1863 C CG  . ARG A 1 252 ? 70.89395 -32.31608 -88.29709  1.000 257.68297 ? 246 ARG A CG  1 
ATOM   1864 C CD  . ARG A 1 252 ? 71.03321 -33.81998 -88.46744  1.000 252.14385 ? 246 ARG A CD  1 
ATOM   1865 N NE  . ARG A 1 252 ? 72.00700 -34.16404 -89.49675  1.000 258.83575 ? 246 ARG A NE  1 
ATOM   1866 C CZ  . ARG A 1 252 ? 73.31234 -34.26970 -89.28836  1.000 268.77834 ? 246 ARG A CZ  1 
ATOM   1867 N NH1 . ARG A 1 252 ? 73.84136 -34.05672 -88.09450  1.000 259.65466 ? 246 ARG A NH1 1 
ATOM   1868 N NH2 . ARG A 1 252 ? 74.10722 -34.59581 -90.30369  1.000 275.63011 ? 246 ARG A NH2 1 
ATOM   1869 N N   . VAL A 1 253 ? 70.12134 -28.51103 -88.27659  1.000 286.82466 ? 247 VAL A N   1 
ATOM   1870 C CA  . VAL A 1 253 ? 69.97321 -27.65814 -89.45016  1.000 277.40453 ? 247 VAL A CA  1 
ATOM   1871 C C   . VAL A 1 253 ? 71.04935 -28.03450 -90.45843  1.000 299.88462 ? 247 VAL A C   1 
ATOM   1872 O O   . VAL A 1 253 ? 72.24360 -28.02923 -90.13475  1.000 300.86570 ? 247 VAL A O   1 
ATOM   1873 C CB  . VAL A 1 253 ? 70.06893 -26.17164 -89.06882  1.000 237.22406 ? 247 VAL A CB  1 
ATOM   1874 C CG1 . VAL A 1 253 ? 69.97476 -25.29779 -90.31115  1.000 213.61231 ? 247 VAL A CG1 1 
ATOM   1875 C CG2 . VAL A 1 253 ? 68.98059 -25.80857 -88.07142  1.000 222.96700 ? 247 VAL A CG2 1 
ATOM   1876 N N   . ASP A 1 254 ? 70.62684 -28.35829 -91.67907  1.000 309.69429 ? 248 ASP A N   1 
ATOM   1877 C CA  . ASP A 1 254 ? 71.51714 -28.83736 -92.74719  1.000 325.11689 ? 248 ASP A CA  1 
ATOM   1878 C C   . ASP A 1 254 ? 72.17825 -30.11551 -92.23220  1.000 316.87011 ? 248 ASP A C   1 
ATOM   1879 O O   . ASP A 1 254 ? 71.46228 -31.04433 -91.82514  1.000 308.46157 ? 248 ASP A O   1 
ATOM   1880 C CB  . ASP A 1 254 ? 72.46885 -27.72256 -93.17192  1.000 325.99559 ? 248 ASP A CB  1 
ATOM   1881 C CG  . ASP A 1 254 ? 71.73957 -26.49514 -93.68434  1.000 311.97384 ? 248 ASP A CG  1 
ATOM   1882 O OD1 . ASP A 1 254 ? 70.67315 -26.65372 -94.31503  1.000 314.47634 ? 248 ASP A OD1 1 
ATOM   1883 O OD2 . ASP A 1 254 ? 72.23328 -25.37070 -93.45532  1.000 295.42360 ? 248 ASP A OD2 1 
ATOM   1884 N N   . GLY A 1 255 ? 73.50504 -30.21323 -92.22412  1.000 312.98476 ? 249 GLY A N   1 
ATOM   1885 C CA  . GLY A 1 255 ? 74.17033 -31.39408 -91.71037  1.000 301.45562 ? 249 GLY A CA  1 
ATOM   1886 C C   . GLY A 1 255 ? 74.90750 -31.13507 -90.41314  1.000 302.96388 ? 249 GLY A C   1 
ATOM   1887 O O   . GLY A 1 255 ? 75.81039 -31.89053 -90.04035  1.000 310.78715 ? 249 GLY A O   1 
ATOM   1888 N N   . ASN A 1 256 ? 74.52820 -30.06686 -89.71498  1.000 300.07888 ? 250 ASN A N   1 
ATOM   1889 C CA  . ASN A 1 256 ? 75.16641 -29.67317 -88.46796  1.000 290.19958 ? 250 ASN A CA  1 
ATOM   1890 C C   . ASN A 1 256 ? 74.11428 -29.52781 -87.37978  1.000 273.23199 ? 250 ASN A C   1 
ATOM   1891 O O   . ASN A 1 256 ? 73.03530 -28.97647 -87.61571  1.000 270.93607 ? 250 ASN A O   1 
ATOM   1892 C CB  . ASN A 1 256 ? 75.93750 -28.35893 -88.63003  1.000 273.00359 ? 250 ASN A CB  1 
ATOM   1893 C CG  . ASN A 1 256 ? 76.93422 -28.40738 -89.76953  1.000 275.15292 ? 250 ASN A CG  1 
ATOM   1894 O OD1 . ASN A 1 256 ? 78.08569 -28.80160 -89.58604  1.000 274.98060 ? 250 ASN A OD1 1 
ATOM   1895 N ND2 . ASN A 1 256 ? 76.49459 -28.00755 -90.95735  1.000 276.88631 ? 250 ASN A ND2 1 
ATOM   1896 N N   . SER A 1 257 ? 74.43584 -30.02078 -86.18786  1.000 268.74230 ? 251 SER A N   1 
ATOM   1897 C CA  . SER A 1 257 ? 73.50602 -29.96691 -85.07018  1.000 263.24276 ? 251 SER A CA  1 
ATOM   1898 C C   . SER A 1 257 ? 73.52469 -28.58804 -84.42254  1.000 261.55398 ? 251 SER A C   1 
ATOM   1899 O O   . SER A 1 257 ? 74.57541 -27.94920 -84.31455  1.000 264.97777 ? 251 SER A O   1 
ATOM   1900 C CB  . SER A 1 257 ? 73.85475 -31.03899 -84.03830  1.000 267.41970 ? 251 SER A CB  1 
ATOM   1901 O OG  . SER A 1 257 ? 73.83433 -32.32972 -84.62355  1.000 244.41553 ? 251 SER A OG  1 
ATOM   1902 N N   . TYR A 1 258 ? 72.35008 -28.13145 -83.99335  1.000 258.73961 ? 252 TYR A N   1 
ATOM   1903 C CA  . TYR A 1 258 ? 72.18746 -26.83491 -83.34899  1.000 265.14821 ? 252 TYR A CA  1 
ATOM   1904 C C   . TYR A 1 258 ? 71.60866 -27.03727 -81.95639  1.000 262.17607 ? 252 TYR A C   1 
ATOM   1905 O O   . TYR A 1 258 ? 70.60704 -27.74114 -81.79169  1.000 253.67080 ? 252 TYR A O   1 
ATOM   1906 C CB  . TYR A 1 258 ? 71.28425 -25.91564 -84.17777  1.000 266.00477 ? 252 TYR A CB  1 
ATOM   1907 C CG  . TYR A 1 258 ? 71.02935 -24.56322 -83.54700  1.000 282.55217 ? 252 TYR A CG  1 
ATOM   1908 C CD1 . TYR A 1 258 ? 72.01706 -23.58608 -83.52615  1.000 279.47662 ? 252 TYR A CD1 1 
ATOM   1909 C CD2 . TYR A 1 258 ? 69.79704 -24.26018 -82.98184  1.000 272.51412 ? 252 TYR A CD2 1 
ATOM   1910 C CE1 . TYR A 1 258 ? 71.78654 -22.34753 -82.95284  1.000 276.96961 ? 252 TYR A CE1 1 
ATOM   1911 C CE2 . TYR A 1 258 ? 69.55713 -23.02484 -82.40794  1.000 266.56343 ? 252 TYR A CE2 1 
ATOM   1912 C CZ  . TYR A 1 258 ? 70.55466 -22.07289 -82.39577  1.000 273.78367 ? 252 TYR A CZ  1 
ATOM   1913 O OH  . TYR A 1 258 ? 70.31819 -20.84288 -81.82494  1.000 255.88237 ? 252 TYR A OH  1 
ATOM   1914 N N   . TYR A 1 259 ? 72.23698 -26.41551 -80.96354  1.000 260.18387 ? 253 TYR A N   1 
ATOM   1915 C CA  . TYR A 1 259 ? 71.87193 -26.56792 -79.56220  1.000 247.46905 ? 253 TYR A CA  1 
ATOM   1916 C C   . TYR A 1 259 ? 71.15426 -25.31332 -79.08307  1.000 247.71503 ? 253 TYR A C   1 
ATOM   1917 O O   . TYR A 1 259 ? 71.64489 -24.19730 -79.28501  1.000 244.47841 ? 253 TYR A O   1 
ATOM   1918 C CB  . TYR A 1 259 ? 73.11555 -26.83532 -78.71087  1.000 243.90201 ? 253 TYR A CB  1 
ATOM   1919 C CG  . TYR A 1 259 ? 72.83359 -27.02400 -77.24013  1.000 243.40969 ? 253 TYR A CG  1 
ATOM   1920 C CD1 . TYR A 1 259 ? 72.14888 -28.14194 -76.78331  1.000 238.71940 ? 253 TYR A CD1 1 
ATOM   1921 C CD2 . TYR A 1 259 ? 73.26461 -26.09144 -76.30631  1.000 236.65893 ? 253 TYR A CD2 1 
ATOM   1922 C CE1 . TYR A 1 259 ? 71.89133 -28.32086 -75.43838  1.000 242.48015 ? 253 TYR A CE1 1 
ATOM   1923 C CE2 . TYR A 1 259 ? 73.01438 -26.26239 -74.95948  1.000 230.23780 ? 253 TYR A CE2 1 
ATOM   1924 C CZ  . TYR A 1 259 ? 72.32715 -27.37852 -74.53074  1.000 235.48825 ? 253 TYR A CZ  1 
ATOM   1925 O OH  . TYR A 1 259 ? 72.07430 -27.55183 -73.18940  1.000 244.01625 ? 253 TYR A OH  1 
ATOM   1926 N N   . TRP A 1 260 ? 69.99652 -25.50015 -78.44820  1.000 243.33954 ? 254 TRP A N   1 
ATOM   1927 C CA  . TRP A 1 260 ? 69.17677 -24.38665 -77.98582  1.000 236.97336 ? 254 TRP A CA  1 
ATOM   1928 C C   . TRP A 1 260 ? 68.23835 -24.85948 -76.88156  1.000 225.10151 ? 254 TRP A C   1 
ATOM   1929 O O   . TRP A 1 260 ? 67.15068 -25.37699 -77.16731  1.000 216.64461 ? 254 TRP A O   1 
ATOM   1930 C CB  . TRP A 1 260 ? 68.38560 -23.79057 -79.15025  1.000 238.28996 ? 254 TRP A CB  1 
ATOM   1931 C CG  . TRP A 1 260 ? 67.78161 -22.45318 -78.86142  1.000 238.85056 ? 254 TRP A CG  1 
ATOM   1932 C CD1 . TRP A 1 260 ? 68.40126 -21.24040 -78.94225  1.000 239.26264 ? 254 TRP A CD1 1 
ATOM   1933 C CD2 . TRP A 1 260 ? 66.43238 -22.18852 -78.46005  1.000 242.19445 ? 254 TRP A CD2 1 
ATOM   1934 N NE1 . TRP A 1 260 ? 67.52388 -20.23729 -78.60991  1.000 233.47153 ? 254 TRP A NE1 1 
ATOM   1935 C CE2 . TRP A 1 260 ? 66.30801 -20.79302 -78.30997  1.000 243.56940 ? 254 TRP A CE2 1 
ATOM   1936 C CE3 . TRP A 1 260 ? 65.31877 -22.99593 -78.20912  1.000 248.03122 ? 254 TRP A CE3 1 
ATOM   1937 C CZ2 . TRP A 1 260 ? 65.11476 -20.18750 -77.92267  1.000 252.21877 ? 254 TRP A CZ2 1 
ATOM   1938 C CZ3 . TRP A 1 260 ? 64.13581 -22.39319 -77.82456  1.000 251.57722 ? 254 TRP A CZ3 1 
ATOM   1939 C CH2 . TRP A 1 260 ? 64.04306 -21.00290 -77.68377  1.000 247.91040 ? 254 TRP A CH2 1 
ATOM   1940 N N   . PRO A 1 261 ? 68.62260 -24.70797 -75.61361  1.000 228.34326 ? 255 PRO A N   1 
ATOM   1941 C CA  . PRO A 1 261 ? 67.81314 -25.26935 -74.52699  1.000 236.70006 ? 255 PRO A CA  1 
ATOM   1942 C C   . PRO A 1 261 ? 66.99173 -24.23596 -73.77121  1.000 239.16716 ? 255 PRO A C   1 
ATOM   1943 O O   . PRO A 1 261 ? 66.61049 -24.48102 -72.62257  1.000 254.40759 ? 255 PRO A O   1 
ATOM   1944 C CB  . PRO A 1 261 ? 68.87592 -25.89067 -73.61819  1.000 252.01835 ? 255 PRO A CB  1 
ATOM   1945 C CG  . PRO A 1 261 ? 70.02384 -24.91222 -73.73527  1.000 241.28481 ? 255 PRO A CG  1 
ATOM   1946 C CD  . PRO A 1 261 ? 69.96073 -24.31456 -75.13845  1.000 232.48381 ? 255 PRO A CD  1 
ATOM   1947 N N   . ASP A 1 262 ? 66.71424 -23.08527 -74.39079  1.000 236.10198 ? 256 ASP A N   1 
ATOM   1948 C CA  . ASP A 1 262 ? 66.01941 -22.01144 -73.68267  1.000 243.46596 ? 256 ASP A CA  1 
ATOM   1949 C C   . ASP A 1 262 ? 64.65600 -22.47116 -73.17849  1.000 228.41905 ? 256 ASP A C   1 
ATOM   1950 O O   . ASP A 1 262 ? 64.32712 -22.30060 -71.99860  1.000 226.18667 ? 256 ASP A O   1 
ATOM   1951 C CB  . ASP A 1 262 ? 65.87772 -20.78837 -74.58847  1.000 234.64700 ? 256 ASP A CB  1 
ATOM   1952 C CG  . ASP A 1 262 ? 67.20287 -20.09731 -74.84733  1.000 237.81914 ? 256 ASP A CG  1 
ATOM   1953 O OD1 . ASP A 1 262 ? 68.21362 -20.49198 -74.22822  1.000 243.54056 ? 256 ASP A OD1 1 
ATOM   1954 O OD2 . ASP A 1 262 ? 67.23370 -19.15891 -75.67103  1.000 239.76662 ? 256 ASP A OD2 1 
ATOM   1955 N N   . ILE A 1 263 ? 63.84586 -23.05846 -74.06093  1.000 217.52414 ? 257 ILE A N   1 
ATOM   1956 C CA  . ILE A 1 263 ? 62.57751 -23.62649 -73.61875  1.000 215.09030 ? 257 ILE A CA  1 
ATOM   1957 C C   . ILE A 1 263 ? 62.81735 -24.88885 -72.80186  1.000 207.58554 ? 257 ILE A C   1 
ATOM   1958 O O   . ILE A 1 263 ? 62.07527 -25.17689 -71.85474  1.000 190.87841 ? 257 ILE A O   1 
ATOM   1959 C CB  . ILE A 1 263 ? 61.66526 -23.89474 -74.82984  1.000 219.76601 ? 257 ILE A CB  1 
ATOM   1960 C CG1 . ILE A 1 263 ? 61.41410 -22.59709 -75.59907  1.000 232.00591 ? 257 ILE A CG1 1 
ATOM   1961 C CG2 . ILE A 1 263 ? 60.34670 -24.51187 -74.38853  1.000 223.40805 ? 257 ILE A CG2 1 
ATOM   1962 C CD1 . ILE A 1 263 ? 60.54080 -22.77060 -76.82016  1.000 258.52960 ? 257 ILE A CD1 1 
ATOM   1963 N N   . TYR A 1 264 ? 63.86330 -25.64864 -73.13571  1.000 207.81565 ? 258 TYR A N   1 
ATOM   1964 C CA  . TYR A 1 264 ? 64.15372 -26.88200 -72.41253  1.000 222.74985 ? 258 TYR A CA  1 
ATOM   1965 C C   . TYR A 1 264 ? 64.56937 -26.61142 -70.97051  1.000 222.27989 ? 258 TYR A C   1 
ATOM   1966 O O   . TYR A 1 264 ? 64.38907 -27.47527 -70.10526  1.000 209.09591 ? 258 TYR A O   1 
ATOM   1967 C CB  . TYR A 1 264 ? 65.24063 -27.66790 -73.14982  1.000 238.28912 ? 258 TYR A CB  1 
ATOM   1968 C CG  . TYR A 1 264 ? 65.59058 -29.00501 -72.53034  1.000 260.63025 ? 258 TYR A CG  1 
ATOM   1969 C CD1 . TYR A 1 264 ? 64.79268 -30.12257 -72.74234  1.000 240.41615 ? 258 TYR A CD1 1 
ATOM   1970 C CD2 . TYR A 1 264 ? 66.72935 -29.15341 -71.74819  1.000 287.01639 ? 258 TYR A CD2 1 
ATOM   1971 C CE1 . TYR A 1 264 ? 65.11295 -31.34790 -72.18244  1.000 241.75356 ? 258 TYR A CE1 1 
ATOM   1972 C CE2 . TYR A 1 264 ? 67.05790 -30.37438 -71.18535  1.000 290.74787 ? 258 TYR A CE2 1 
ATOM   1973 C CZ  . TYR A 1 264 ? 66.24617 -31.46758 -71.40537  1.000 262.95006 ? 258 TYR A CZ  1 
ATOM   1974 O OH  . TYR A 1 264 ? 66.56897 -32.68390 -70.84728  1.000 232.58733 ? 258 TYR A OH  1 
ATOM   1975 N N   . ASN A 1 265 ? 65.11425 -25.42707 -70.68810  1.000 225.73915 ? 259 ASN A N   1 
ATOM   1976 C CA  . ASN A 1 265 ? 65.56180 -25.10001 -69.33843  1.000 226.33205 ? 259 ASN A CA  1 
ATOM   1977 C C   . ASN A 1 265 ? 64.48426 -24.40488 -68.51439  1.000 209.80894 ? 259 ASN A C   1 
ATOM   1978 O O   . ASN A 1 265 ? 64.38007 -24.64808 -67.30713  1.000 218.90634 ? 259 ASN A O   1 
ATOM   1979 C CB  . ASN A 1 265 ? 66.81396 -24.21998 -69.39269  1.000 250.36967 ? 259 ASN A CB  1 
ATOM   1980 C CG  . ASN A 1 265 ? 68.01704 -24.94851 -69.95961  1.000 251.03781 ? 259 ASN A CG  1 
ATOM   1981 O OD1 . ASN A 1 265 ? 68.19298 -26.14784 -69.74354  1.000 247.34645 ? 259 ASN A OD1 1 
ATOM   1982 N ND2 . ASN A 1 265 ? 68.85316 -24.22333 -70.69198  1.000 247.26104 ? 259 ASN A ND2 1 
ATOM   1983 N N   . SER A 1 266 ? 63.68217 -23.53802 -69.13971  1.000 206.45667 ? 260 SER A N   1 
ATOM   1984 C CA  . SER A 1 266 ? 62.63745 -22.83467 -68.40130  1.000 218.58095 ? 260 SER A CA  1 
ATOM   1985 C C   . SER A 1 266 ? 61.58071 -23.79500 -67.87245  1.000 229.79641 ? 260 SER A C   1 
ATOM   1986 O O   . SER A 1 266 ? 60.91132 -23.49518 -66.87690  1.000 226.27617 ? 260 SER A O   1 
ATOM   1987 C CB  . SER A 1 266 ? 61.99219 -21.76927 -69.28806  1.000 198.99347 ? 260 SER A CB  1 
ATOM   1988 O OG  . SER A 1 266 ? 61.40650 -22.35090 -70.43966  1.000 207.95014 ? 260 SER A OG  1 
ATOM   1989 N N   . ILE A 1 267 ? 61.41659 -24.94842 -68.52033  1.000 225.40527 ? 261 ILE A N   1 
ATOM   1990 C CA  . ILE A 1 267 ? 60.47171 -25.94838 -68.03646  1.000 230.66063 ? 261 ILE A CA  1 
ATOM   1991 C C   . ILE A 1 267 ? 61.06605 -26.73136 -66.87155  1.000 221.08039 ? 261 ILE A C   1 
ATOM   1992 O O   . ILE A 1 267 ? 60.38758 -26.98443 -65.86943  1.000 219.98203 ? 261 ILE A O   1 
ATOM   1993 C CB  . ILE A 1 267 ? 60.04837 -26.87267 -69.19236  1.000 218.09702 ? 261 ILE A CB  1 
ATOM   1994 C CG1 . ILE A 1 267 ? 59.42128 -26.05522 -70.32283  1.000 205.29685 ? 261 ILE A CG1 1 
ATOM   1995 C CG2 . ILE A 1 267 ? 59.07336 -27.93121 -68.70411  1.000 215.81357 ? 261 ILE A CG2 1 
ATOM   1996 C CD1 . ILE A 1 267 ? 59.19435 -26.84488 -71.59092  1.000 217.19179 ? 261 ILE A CD1 1 
ATOM   1997 N N   . ILE A 1 268 ? 62.33876 -27.12293 -66.98030  1.000 205.07559 ? 262 ILE A N   1 
ATOM   1998 C CA  . ILE A 1 268 ? 62.99981 -27.82063 -65.88113  1.000 219.28359 ? 262 ILE A CA  1 
ATOM   1999 C C   . ILE A 1 268 ? 63.13050 -26.90748 -64.66983  1.000 218.29691 ? 262 ILE A C   1 
ATOM   2000 O O   . ILE A 1 268 ? 63.02990 -27.36235 -63.52258  1.000 200.72044 ? 262 ILE A O   1 
ATOM   2001 C CB  . ILE A 1 268 ? 64.36962 -28.35616 -66.33886  1.000 221.31433 ? 262 ILE A CB  1 
ATOM   2002 C CG1 . ILE A 1 268 ? 64.19399 -29.34045 -67.49573  1.000 211.04239 ? 262 ILE A CG1 1 
ATOM   2003 C CG2 . ILE A 1 268 ? 65.10357 -29.02128 -65.18616  1.000 225.51841 ? 262 ILE A CG2 1 
ATOM   2004 C CD1 . ILE A 1 268 ? 65.49266 -29.93189 -67.99504  1.000 238.34658 ? 262 ILE A CD1 1 
ATOM   2005 N N   . GLU A 1 269 ? 63.34562 -25.61014 -64.89854  1.000 219.88639 ? 263 GLU A N   1 
ATOM   2006 C CA  . GLU A 1 269 ? 63.38491 -24.65099 -63.80201  1.000 221.16411 ? 263 GLU A CA  1 
ATOM   2007 C C   . GLU A 1 269 ? 62.06169 -24.59066 -63.05058  1.000 217.91892 ? 263 GLU A C   1 
ATOM   2008 O O   . GLU A 1 269 ? 62.04286 -24.21028 -61.87504  1.000 224.39792 ? 263 GLU A O   1 
ATOM   2009 C CB  . GLU A 1 269 ? 63.75183 -23.26561 -64.33896  1.000 233.03319 ? 263 GLU A CB  1 
ATOM   2010 C CG  . GLU A 1 269 ? 64.09155 -22.23846 -63.27213  1.000 256.17989 ? 263 GLU A CG  1 
ATOM   2011 C CD  . GLU A 1 269 ? 64.39889 -20.87377 -63.85837  1.000 259.99459 ? 263 GLU A CD  1 
ATOM   2012 O OE1 . GLU A 1 269 ? 64.06889 -20.64650 -65.04148  1.000 235.68103 ? 263 GLU A OE1 1 
ATOM   2013 O OE2 . GLU A 1 269 ? 64.97271 -20.02952 -63.13823  1.000 287.73830 ? 263 GLU A OE2 1 
ATOM   2014 N N   . ALA A 1 270 ? 60.95773 -24.96689 -63.69829  1.000 204.24233 ? 264 ALA A N   1 
ATOM   2015 C CA  . ALA A 1 270 ? 59.66049 -24.95305 -63.03348  1.000 213.36340 ? 264 ALA A CA  1 
ATOM   2016 C C   . ALA A 1 270 ? 59.42091 -26.22954 -62.23610  1.000 229.22927 ? 264 ALA A C   1 
ATOM   2017 O O   . ALA A 1 270 ? 58.81646 -26.18586 -61.15908  1.000 256.59929 ? 264 ALA A O   1 
ATOM   2018 C CB  . ALA A 1 270 ? 58.54697 -24.75307 -64.06176  1.000 220.59498 ? 264 ALA A CB  1 
ATOM   2019 N N   . ALA A 1 271 ? 59.88900 -27.37179 -62.74253  1.000 206.30418 ? 265 ALA A N   1 
ATOM   2020 C CA  . ALA A 1 271 ? 59.60525 -28.64375 -62.08666  1.000 225.19763 ? 265 ALA A CA  1 
ATOM   2021 C C   . ALA A 1 271 ? 60.51076 -28.88063 -60.88400  1.000 238.34180 ? 265 ALA A C   1 
ATOM   2022 O O   . ALA A 1 271 ? 60.06814 -29.43779 -59.87330  1.000 253.70308 ? 265 ALA A O   1 
ATOM   2023 C CB  . ALA A 1 271 ? 59.74174 -29.79219 -63.08639  1.000 211.11928 ? 265 ALA A CB  1 
ATOM   2024 N N   . ILE A 1 272 ? 61.77450 -28.47006 -60.97051  1.000 229.37688 ? 266 ILE A N   1 
ATOM   2025 C CA  . ILE A 1 272 ? 62.73794 -28.73312 -59.90725  1.000 242.18440 ? 266 ILE A CA  1 
ATOM   2026 C C   . ILE A 1 272 ? 62.71289 -27.60605 -58.88419  1.000 246.04061 ? 266 ILE A C   1 
ATOM   2027 O O   . ILE A 1 272 ? 62.51967 -27.84366 -57.68636  1.000 240.40082 ? 266 ILE A O   1 
ATOM   2028 C CB  . ILE A 1 272 ? 64.15599 -28.92201 -60.47565  1.000 234.30841 ? 266 ILE A CB  1 
ATOM   2029 C CG1 . ILE A 1 272 ? 64.21933 -30.17890 -61.34471  1.000 241.69904 ? 266 ILE A CG1 1 
ATOM   2030 C CG2 . ILE A 1 272 ? 65.17585 -28.99385 -59.34924  1.000 247.45231 ? 266 ILE A CG2 1 
ATOM   2031 C CD1 . ILE A 1 272 ? 65.60713 -30.49659 -61.85409  1.000 232.75257 ? 266 ILE A CD1 1 
ATOM   2032 N N   . ASN A 1 273 ? 62.90865 -26.37119 -59.34845  1.000 239.81981 ? 267 ASN A N   1 
ATOM   2033 C CA  . ASN A 1 273 ? 63.02631 -25.24659 -58.42704  1.000 254.79613 ? 267 ASN A CA  1 
ATOM   2034 C C   . ASN A 1 273 ? 61.67407 -24.82287 -57.86765  1.000 260.46542 ? 267 ASN A C   1 
ATOM   2035 O O   . ASN A 1 273 ? 61.56830 -24.49636 -56.68018  1.000 263.72322 ? 267 ASN A O   1 
ATOM   2036 C CB  . ASN A 1 273 ? 63.70717 -24.06794 -59.12266  1.000 262.84238 ? 267 ASN A CB  1 
ATOM   2037 C CG  . ASN A 1 273 ? 65.09888 -24.40837 -59.60542  1.000 257.79976 ? 267 ASN A CG  1 
ATOM   2038 O OD1 . ASN A 1 273 ? 65.55756 -23.90684 -60.63207  1.000 248.59442 ? 267 ASN A OD1 1 
ATOM   2039 N ND2 . ASN A 1 273 ? 65.77666 -25.27806 -58.86937  1.000 265.45800 ? 267 ASN A ND2 1 
ATOM   2040 N N   . ARG A 1 274 ? 60.63335 -24.82143 -58.69830  1.000 258.85431 ? 268 ARG A N   1 
ATOM   2041 C CA  . ARG A 1 274 ? 59.31880 -24.34792 -58.28965  1.000 269.61777 ? 268 ARG A CA  1 
ATOM   2042 C C   . ARG A 1 274 ? 58.31080 -25.47014 -58.07940  1.000 279.82752 ? 268 ARG A C   1 
ATOM   2043 O O   . ARG A 1 274 ? 57.17034 -25.19181 -57.69270  1.000 284.26612 ? 268 ARG A O   1 
ATOM   2044 C CB  . ARG A 1 274 ? 58.78382 -23.33957 -59.31576  1.000 262.30017 ? 268 ARG A CB  1 
ATOM   2045 C CG  . ARG A 1 274 ? 59.54592 -22.01829 -59.30744  1.000 263.73426 ? 268 ARG A CG  1 
ATOM   2046 C CD  . ARG A 1 274 ? 58.97422 -20.99589 -60.28168  1.000 243.90968 ? 268 ARG A CD  1 
ATOM   2047 N NE  . ARG A 1 274 ? 59.57688 -21.09041 -61.60624  1.000 235.77415 ? 268 ARG A NE  1 
ATOM   2048 C CZ  . ARG A 1 274 ? 58.94349 -21.51408 -62.69106  1.000 242.75380 ? 268 ARG A CZ  1 
ATOM   2049 N NH1 . ARG A 1 274 ? 57.67240 -21.87863 -62.65100  1.000 245.09694 ? 268 ARG A NH1 1 
ATOM   2050 N NH2 . ARG A 1 274 ? 59.60043 -21.56749 -63.84651  1.000 244.41919 ? 268 ARG A NH2 1 
ATOM   2051 N N   . GLY A 1 275 ? 58.69758 -26.72137 -58.31129  1.000 284.95180 ? 269 GLY A N   1 
ATOM   2052 C CA  . GLY A 1 275 ? 57.81496 -27.84871 -58.04260  1.000 270.81799 ? 269 GLY A CA  1 
ATOM   2053 C C   . GLY A 1 275 ? 56.52108 -27.83041 -58.82632  1.000 267.89057 ? 269 GLY A C   1 
ATOM   2054 O O   . GLY A 1 275 ? 55.47024 -28.21306 -58.29634  1.000 271.10623 ? 269 GLY A O   1 
ATOM   2055 N N   . VAL A 1 276 ? 56.57261 -27.39560 -60.08011  1.000 267.54351 ? 270 VAL A N   1 
ATOM   2056 C CA  . VAL A 1 276 ? 55.37524 -27.29158 -60.90587  1.000 264.94917 ? 270 VAL A CA  1 
ATOM   2057 C C   . VAL A 1 276 ? 55.03045 -28.66544 -61.46505  1.000 253.44135 ? 270 VAL A C   1 
ATOM   2058 O O   . VAL A 1 276 ? 55.88975 -29.35528 -62.02705  1.000 238.05992 ? 270 VAL A O   1 
ATOM   2059 C CB  . VAL A 1 276 ? 55.58236 -26.26597 -62.03209  1.000 251.12441 ? 270 VAL A CB  1 
ATOM   2060 C CG1 . VAL A 1 276 ? 54.40171 -26.27357 -62.98628  1.000 237.56697 ? 270 VAL A CG1 1 
ATOM   2061 C CG2 . VAL A 1 276 ? 55.79022 -24.87542 -61.44937  1.000 238.34834 ? 270 VAL A CG2 1 
ATOM   2062 N N   . LYS A 1 277 ? 53.77186 -29.07120 -61.30227  1.000 262.44661 ? 271 LYS A N   1 
ATOM   2063 C CA  . LYS A 1 277 ? 53.28840 -30.31730 -61.88891  1.000 254.13661 ? 271 LYS A CA  1 
ATOM   2064 C C   . LYS A 1 277 ? 53.19633 -30.14958 -63.39996  1.000 243.58719 ? 271 LYS A C   1 
ATOM   2065 O O   . LYS A 1 277 ? 52.29999 -29.46520 -63.90395  1.000 214.54775 ? 271 LYS A O   1 
ATOM   2066 C CB  . LYS A 1 277 ? 51.93406 -30.69760 -61.29780  1.000 251.89163 ? 271 LYS A CB  1 
ATOM   2067 C CG  . LYS A 1 277 ? 51.95759 -30.99942 -59.80736  1.000 265.11991 ? 271 LYS A CG  1 
ATOM   2068 C CD  . LYS A 1 277 ? 50.62251 -31.56508 -59.34276  1.000 291.35001 ? 271 LYS A CD  1 
ATOM   2069 C CE  . LYS A 1 277 ? 50.63611 -31.88422 -57.85530  1.000 284.31181 ? 271 LYS A CE  1 
ATOM   2070 N NZ  . LYS A 1 277 ? 49.37153 -32.53737 -57.41433  1.000 261.03913 ? 271 LYS A NZ  1 
ATOM   2071 N N   . ILE A 1 278 ? 54.12080 -30.77125 -64.12561  1.000 245.13050 ? 272 ILE A N   1 
ATOM   2072 C CA  . ILE A 1 278 ? 54.23843 -30.60991 -65.56926  1.000 235.01543 ? 272 ILE A CA  1 
ATOM   2073 C C   . ILE A 1 278 ? 53.90788 -31.93656 -66.23696  1.000 227.01262 ? 272 ILE A C   1 
ATOM   2074 O O   . ILE A 1 278 ? 54.37877 -32.99418 -65.80108  1.000 234.36322 ? 272 ILE A O   1 
ATOM   2075 C CB  . ILE A 1 278 ? 55.64417 -30.12515 -65.96352  1.000 227.00187 ? 272 ILE A CB  1 
ATOM   2076 C CG1 . ILE A 1 278 ? 55.97707 -28.82577 -65.22856  1.000 241.07072 ? 272 ILE A CG1 1 
ATOM   2077 C CG2 . ILE A 1 278 ? 55.74243 -29.92701 -67.46727  1.000 218.22166 ? 272 ILE A CG2 1 
ATOM   2078 C CD1 . ILE A 1 278 ? 57.36283 -28.30074 -65.50915  1.000 230.63165 ? 272 ILE A CD1 1 
ATOM   2079 N N   . ARG A 1 279 ? 53.09208 -31.87930 -67.28798  1.000 224.43962 ? 273 ARG A N   1 
ATOM   2080 C CA  . ARG A 1 279 ? 52.74385 -33.04774 -68.08736  1.000 236.06056 ? 273 ARG A CA  1 
ATOM   2081 C C   . ARG A 1 279 ? 53.06750 -32.74552 -69.54141  1.000 229.99835 ? 273 ARG A C   1 
ATOM   2082 O O   . ARG A 1 279 ? 52.55921 -31.76892 -70.10191  1.000 214.48985 ? 273 ARG A O   1 
ATOM   2083 C CB  . ARG A 1 279 ? 51.26569 -33.41267 -67.92710  1.000 231.99040 ? 273 ARG A CB  1 
ATOM   2084 C CG  . ARG A 1 279 ? 50.88049 -33.83713 -66.52128  1.000 230.59853 ? 273 ARG A CG  1 
ATOM   2085 C CD  . ARG A 1 279 ? 49.40187 -34.16801 -66.43969  1.000 228.62303 ? 273 ARG A CD  1 
ATOM   2086 N NE  . ARG A 1 279 ? 48.57282 -33.02703 -66.80795  1.000 231.07438 ? 273 ARG A NE  1 
ATOM   2087 C CZ  . ARG A 1 279 ? 47.24853 -33.05060 -66.86514  1.000 252.67159 ? 273 ARG A CZ  1 
ATOM   2088 N NH1 . ARG A 1 279 ? 46.56409 -34.14813 -66.58688  1.000 263.03827 ? 273 ARG A NH1 1 
ATOM   2089 N NH2 . ARG A 1 279 ? 46.59441 -31.94532 -67.21072  1.000 258.72204 ? 273 ARG A NH2 1 
ATOM   2090 N N   . LEU A 1 280 ? 53.90814 -33.57864 -70.14763  1.000 233.50021 ? 274 LEU A N   1 
ATOM   2091 C CA  . LEU A 1 280 ? 54.37211 -33.37605 -71.51165  1.000 228.42191 ? 274 LEU A CA  1 
ATOM   2092 C C   . LEU A 1 280 ? 53.88150 -34.50718 -72.40304  1.000 231.68357 ? 274 LEU A C   1 
ATOM   2093 O O   . LEU A 1 280 ? 53.96021 -35.68289 -72.03259  1.000 233.36123 ? 274 LEU A O   1 
ATOM   2094 C CB  . LEU A 1 280 ? 55.89907 -33.29403 -71.56388  1.000 216.27068 ? 274 LEU A CB  1 
ATOM   2095 C CG  . LEU A 1 280 ? 56.52674 -32.21631 -70.67940  1.000 221.42191 ? 274 LEU A CG  1 
ATOM   2096 C CD1 . LEU A 1 280 ? 58.04046 -32.25108 -70.79038  1.000 263.07783 ? 274 LEU A CD1 1 
ATOM   2097 C CD2 . LEU A 1 280 ? 55.98841 -30.84108 -71.04530  1.000 238.53953 ? 274 LEU A CD2 1 
ATOM   2098 N N   . LEU A 1 281 ? 53.37957 -34.14350 -73.58327  1.000 229.81117 ? 275 LEU A N   1 
ATOM   2099 C CA  . LEU A 1 281 ? 52.86433 -35.09776 -74.56580  1.000 223.46129 ? 275 LEU A CA  1 
ATOM   2100 C C   . LEU A 1 281 ? 53.52944 -34.79178 -75.90529  1.000 218.92890 ? 275 LEU A C   1 
ATOM   2101 O O   . LEU A 1 281 ? 53.05238 -33.94684 -76.66779  1.000 207.54913 ? 275 LEU A O   1 
ATOM   2102 C CB  . LEU A 1 281 ? 51.34301 -35.02315 -74.65659  1.000 217.27915 ? 275 LEU A CB  1 
ATOM   2103 C CG  . LEU A 1 281 ? 50.66745 -36.00055 -75.61971  1.000 214.97468 ? 275 LEU A CG  1 
ATOM   2104 C CD1 . LEU A 1 281 ? 50.94427 -37.43867 -75.20960  1.000 211.01412 ? 275 LEU A CD1 1 
ATOM   2105 C CD2 . LEU A 1 281 ? 49.17210 -35.73591 -75.68609  1.000 229.59886 ? 275 LEU A CD2 1 
ATOM   2106 N N   . VAL A 1 282 ? 54.63433 -35.48144 -76.18659  1.000 225.56499 ? 276 VAL A N   1 
ATOM   2107 C CA  . VAL A 1 282 ? 55.36238 -35.30339 -77.43823  1.000 231.23851 ? 276 VAL A CA  1 
ATOM   2108 C C   . VAL A 1 282 ? 55.27748 -36.58593 -78.25300  1.000 223.47481 ? 276 VAL A C   1 
ATOM   2109 O O   . VAL A 1 282 ? 54.73579 -37.59511 -77.78955  1.000 222.16902 ? 276 VAL A O   1 
ATOM   2110 C CB  . VAL A 1 282 ? 56.82985 -34.91239 -77.18556  1.000 225.45926 ? 276 VAL A CB  1 
ATOM   2111 C CG1 . VAL A 1 282 ? 56.90614 -33.65089 -76.34141  1.000 241.23751 ? 276 VAL A CG1 1 
ATOM   2112 C CG2 . VAL A 1 282 ? 57.57800 -36.05908 -76.52066  1.000 202.77911 ? 276 VAL A CG2 1 
ATOM   2113 N N   . CYS A 1 283 ? 55.81164 -36.55645 -79.46956  1.000 217.60580 ? 277 CYS A N   1 
ATOM   2114 C CA  . CYS A 1 283 ? 55.81524 -37.73791 -80.31370  1.000 216.02419 ? 277 CYS A CA  1 
ATOM   2115 C C   . CYS A 1 283 ? 56.90822 -38.70615 -79.87114  1.000 227.12225 ? 277 CYS A C   1 
ATOM   2116 O O   . CYS A 1 283 ? 57.77649 -38.38221 -79.05595  1.000 228.71097 ? 277 CYS A O   1 
ATOM   2117 C CB  . CYS A 1 283 ? 56.02107 -37.35365 -81.77781  1.000 216.97585 ? 277 CYS A CB  1 
ATOM   2118 S SG  . CYS A 1 283 ? 54.80332 -36.19795 -82.43299  1.000 307.81365 ? 277 CYS A SG  1 
ATOM   2119 N N   . ASN A 1 284 ? 56.85564 -39.91596 -80.42099  1.000 238.74710 ? 278 ASN A N   1 
ATOM   2120 C CA  . ASN A 1 284 ? 57.95130 -40.84915 -80.23381  1.000 251.78456 ? 278 ASN A CA  1 
ATOM   2121 C C   . ASN A 1 284 ? 59.16906 -40.37604 -81.02481  1.000 272.61495 ? 278 ASN A C   1 
ATOM   2122 O O   . ASN A 1 284 ? 59.08275 -39.50483 -81.89528  1.000 278.46290 ? 278 ASN A O   1 
ATOM   2123 C CB  . ASN A 1 284 ? 57.54207 -42.25842 -80.65987  1.000 254.11387 ? 278 ASN A CB  1 
ATOM   2124 C CG  . ASN A 1 284 ? 57.31195 -42.37251 -82.15242  1.000 282.98445 ? 278 ASN A CG  1 
ATOM   2125 O OD1 . ASN A 1 284 ? 56.82219 -41.44064 -82.79060  1.000 285.69247 ? 278 ASN A OD1 1 
ATOM   2126 N ND2 . ASN A 1 284 ? 57.66871 -43.51944 -82.71910  1.000 311.18144 ? 278 ASN A ND2 1 
ATOM   2127 N N   . TRP A 1 285 ? 60.31939 -40.96219 -80.71401  1.000 271.09665 ? 279 TRP A N   1 
ATOM   2128 C CA  . TRP A 1 285 ? 61.58262 -40.51570 -81.27572  1.000 282.24593 ? 279 TRP A CA  1 
ATOM   2129 C C   . TRP A 1 285 ? 62.30617 -41.68399 -81.92912  1.000 283.91377 ? 279 TRP A C   1 
ATOM   2130 O O   . TRP A 1 285 ? 62.06507 -42.85170 -81.61170  1.000 275.21295 ? 279 TRP A O   1 
ATOM   2131 C CB  . TRP A 1 285 ? 62.46960 -39.87962 -80.20014  1.000 275.61269 ? 279 TRP A CB  1 
ATOM   2132 C CG  . TRP A 1 285 ? 62.83109 -40.82666 -79.10433  1.000 286.48700 ? 279 TRP A CG  1 
ATOM   2133 C CD1 . TRP A 1 285 ? 64.00117 -41.51222 -78.96926  1.000 295.53399 ? 279 TRP A CD1 1 
ATOM   2134 C CD2 . TRP A 1 285 ? 62.01155 -41.20692 -77.99213  1.000 290.10022 ? 279 TRP A CD2 1 
ATOM   2135 N NE1 . TRP A 1 285 ? 63.96535 -42.29183 -77.83891  1.000 311.62060 ? 279 TRP A NE1 1 
ATOM   2136 C CE2 . TRP A 1 285 ? 62.75423 -42.12269 -77.22136  1.000 309.42888 ? 279 TRP A CE2 1 
ATOM   2137 C CE3 . TRP A 1 285 ? 60.72390 -40.85941 -77.57156  1.000 266.40310 ? 279 TRP A CE3 1 
ATOM   2138 C CZ2 . TRP A 1 285 ? 62.25292 -42.69577 -76.05520  1.000 301.53261 ? 279 TRP A CZ2 1 
ATOM   2139 C CZ3 . TRP A 1 285 ? 60.22803 -41.42991 -76.41434  1.000 278.23331 ? 279 TRP A CZ3 1 
ATOM   2140 C CH2 . TRP A 1 285 ? 60.99099 -42.33794 -75.66987  1.000 289.78390 ? 279 TRP A CH2 1 
ATOM   2141 N N   . ASP A 1 286 ? 63.20181 -41.34769 -82.85402  1.000 282.77343 ? 280 ASP A N   1 
ATOM   2142 C CA  . ASP A 1 286 ? 63.99702 -42.35912 -83.53513  1.000 290.70502 ? 280 ASP A CA  1 
ATOM   2143 C C   . ASP A 1 286 ? 65.02310 -42.94915 -82.57689  1.000 285.55197 ? 280 ASP A C   1 
ATOM   2144 O O   . ASP A 1 286 ? 65.73398 -42.21649 -81.88176  1.000 273.59094 ? 280 ASP A O   1 
ATOM   2145 C CB  . ASP A 1 286 ? 64.69501 -41.75275 -84.75250  1.000 292.65226 ? 280 ASP A CB  1 
ATOM   2146 C CG  . ASP A 1 286 ? 65.47691 -42.78001 -85.55356  1.000 310.11230 ? 280 ASP A CG  1 
ATOM   2147 O OD1 . ASP A 1 286 ? 65.24492 -43.99333 -85.36660  1.000 320.20411 ? 280 ASP A OD1 1 
ATOM   2148 O OD2 . ASP A 1 286 ? 66.32900 -42.37170 -86.37082  1.000 301.94930 ? 280 ASP A OD2 1 
ATOM   2149 N N   . LYS A 1 287 ? 65.09747 -44.28133 -82.54030  1.000 288.05265 ? 281 LYS A N   1 
ATOM   2150 C CA  . LYS A 1 287 ? 66.08944 -44.94709 -81.70604  1.000 280.11382 ? 281 LYS A CA  1 
ATOM   2151 C C   . LYS A 1 287 ? 67.51095 -44.69023 -82.18742  1.000 292.07533 ? 281 LYS A C   1 
ATOM   2152 O O   . LYS A 1 287 ? 68.45235 -44.82112 -81.39801  1.000 282.00273 ? 281 LYS A O   1 
ATOM   2153 C CB  . LYS A 1 287 ? 65.81502 -46.45105 -81.66192  1.000 265.77361 ? 281 LYS A CB  1 
ATOM   2154 C CG  . LYS A 1 287 ? 64.44787 -46.81641 -81.10459  1.000 246.64396 ? 281 LYS A CG  1 
ATOM   2155 C CD  . LYS A 1 287 ? 64.23979 -48.32244 -81.09689  1.000 255.50944 ? 281 LYS A CD  1 
ATOM   2156 C CE  . LYS A 1 287 ? 62.87240 -48.69026 -80.54397  1.000 266.00548 ? 281 LYS A CE  1 
ATOM   2157 N NZ  . LYS A 1 287 ? 62.65348 -50.16359 -80.53916  1.000 295.98222 ? 281 LYS A NZ  1 
ATOM   2158 N N   . ASN A 1 288 ? 67.68637 -44.32691 -83.45875  1.000 301.57083 ? 282 ASN A N   1 
ATOM   2159 C CA  . ASN A 1 288 ? 69.00423 -44.01482 -83.99476  1.000 310.43003 ? 282 ASN A CA  1 
ATOM   2160 C C   . ASN A 1 288 ? 69.45756 -42.59852 -83.66596  1.000 308.22084 ? 282 ASN A C   1 
ATOM   2161 O O   . ASN A 1 288 ? 70.62516 -42.26990 -83.90218  1.000 322.96888 ? 282 ASN A O   1 
ATOM   2162 C CB  . ASN A 1 288 ? 69.01519 -44.21393 -85.51337  1.000 307.97374 ? 282 ASN A CB  1 
ATOM   2163 C CG  . ASN A 1 288 ? 68.50677 -45.58205 -85.92719  1.000 310.39489 ? 282 ASN A CG  1 
ATOM   2164 O OD1 . ASN A 1 288 ? 67.56438 -45.69515 -86.71134  1.000 319.02615 ? 282 ASN A OD1 1 
ATOM   2165 N ND2 . ASN A 1 288 ? 69.12951 -46.63002 -85.40058  1.000 312.14754 ? 282 ASN A ND2 1 
ATOM   2166 N N   . ASP A 1 289 ? 68.57288 -41.75902 -83.13274  1.000 282.76572 ? 283 ASP A N   1 
ATOM   2167 C CA  . ASP A 1 289 ? 68.90806 -40.38136 -82.78807  1.000 264.19425 ? 283 ASP A CA  1 
ATOM   2168 C C   . ASP A 1 289 ? 69.42308 -40.34846 -81.35303  1.000 270.10236 ? 283 ASP A C   1 
ATOM   2169 O O   . ASP A 1 289 ? 68.65905 -40.56435 -80.40642  1.000 249.34901 ? 283 ASP A O   1 
ATOM   2170 C CB  . ASP A 1 289 ? 67.69205 -39.47463 -82.95980  1.000 228.21644 ? 283 ASP A CB  1 
ATOM   2171 C CG  . ASP A 1 289 ? 68.02576 -38.00774 -82.77132  1.000 247.31380 ? 283 ASP A CG  1 
ATOM   2172 O OD1 . ASP A 1 289 ? 69.22656 -37.66898 -82.71281  1.000 254.65938 ? 283 ASP A OD1 1 
ATOM   2173 O OD2 . ASP A 1 289 ? 67.08501 -37.19190 -82.67953  1.000 269.51735 ? 283 ASP A OD2 1 
ATOM   2174 N N   . VAL A 1 290 ? 70.72098 -40.07466 -81.19188  1.000 283.35990 ? 284 VAL A N   1 
ATOM   2175 C CA  . VAL A 1 290 ? 71.31221 -40.02771 -79.85973  1.000 277.93406 ? 284 VAL A CA  1 
ATOM   2176 C C   . VAL A 1 290 ? 70.87942 -38.78607 -79.09191  1.000 263.65091 ? 284 VAL A C   1 
ATOM   2177 O O   . VAL A 1 290 ? 70.88688 -38.79358 -77.85533  1.000 268.93762 ? 284 VAL A O   1 
ATOM   2178 C CB  . VAL A 1 290 ? 72.84936 -40.10278 -79.94515  1.000 257.84145 ? 284 VAL A CB  1 
ATOM   2179 C CG1 . VAL A 1 290 ? 73.28287 -41.42340 -80.56327  1.000 265.05653 ? 284 VAL A CG1 1 
ATOM   2180 C CG2 . VAL A 1 290 ? 73.40251 -38.92870 -80.74112  1.000 243.59560 ? 284 VAL A CG2 1 
ATOM   2181 N N   . TYR A 1 291 ? 70.49927 -37.71427 -79.79181  1.000 254.16652 ? 285 TYR A N   1 
ATOM   2182 C CA  . TYR A 1 291 ? 70.03994 -36.51115 -79.10667  1.000 251.26197 ? 285 TYR A CA  1 
ATOM   2183 C C   . TYR A 1 291 ? 68.65284 -36.69976 -78.50905  1.000 238.47279 ? 285 TYR A C   1 
ATOM   2184 O O   . TYR A 1 291 ? 68.33426 -36.09110 -77.48142  1.000 225.80714 ? 285 TYR A O   1 
ATOM   2185 C CB  . TYR A 1 291 ? 70.04636 -35.32413 -80.06860  1.000 252.24694 ? 285 TYR A CB  1 
ATOM   2186 C CG  . TYR A 1 291 ? 71.42994 -34.82107 -80.40730  1.000 267.80030 ? 285 TYR A CG  1 
ATOM   2187 C CD1 . TYR A 1 291 ? 72.45880 -34.88405 -79.47716  1.000 272.95292 ? 285 TYR A CD1 1 
ATOM   2188 C CD2 . TYR A 1 291 ? 71.70885 -34.28634 -81.65747  1.000 276.59107 ? 285 TYR A CD2 1 
ATOM   2189 C CE1 . TYR A 1 291 ? 73.72544 -34.42513 -79.78126  1.000 269.27071 ? 285 TYR A CE1 1 
ATOM   2190 C CE2 . TYR A 1 291 ? 72.97290 -33.82492 -81.97056  1.000 282.16423 ? 285 TYR A CE2 1 
ATOM   2191 C CZ  . TYR A 1 291 ? 73.97701 -33.89605 -81.02864  1.000 279.18132 ? 285 TYR A CZ  1 
ATOM   2192 O OH  . TYR A 1 291 ? 75.23771 -33.43757 -81.33538  1.000 284.58500 ? 285 TYR A OH  1 
ATOM   2193 N N   . SER A 1 292 ? 67.81818 -37.53162 -79.13343  1.000 241.52352 ? 286 SER A N   1 
ATOM   2194 C CA  . SER A 1 292 ? 66.48642 -37.78848 -78.60080  1.000 239.37593 ? 286 SER A CA  1 
ATOM   2195 C C   . SER A 1 292 ? 66.50483 -38.84536 -77.50471  1.000 248.08770 ? 286 SER A C   1 
ATOM   2196 O O   . SER A 1 292 ? 65.70295 -38.77140 -76.56696  1.000 252.44968 ? 286 SER A O   1 
ATOM   2197 C CB  . SER A 1 292 ? 65.54539 -38.21457 -79.72713  1.000 239.25159 ? 286 SER A CB  1 
ATOM   2198 O OG  . SER A 1 292 ? 65.42772 -37.19742 -80.70605  1.000 244.83284 ? 286 SER A OG  1 
ATOM   2199 N N   . MET A 1 293 ? 67.40241 -39.82950 -77.60398  1.000 245.67177 ? 287 MET A N   1 
ATOM   2200 C CA  . MET A 1 293 ? 67.50961 -40.84100 -76.55714  1.000 256.07830 ? 287 MET A CA  1 
ATOM   2201 C C   . MET A 1 293 ? 68.06850 -40.24648 -75.27105  1.000 246.47270 ? 287 MET A C   1 
ATOM   2202 O O   . MET A 1 293 ? 67.58194 -40.55258 -74.17597  1.000 246.05805 ? 287 MET A O   1 
ATOM   2203 C CB  . MET A 1 293 ? 68.38345 -42.00151 -77.03276  1.000 254.24249 ? 287 MET A CB  1 
ATOM   2204 C CG  . MET A 1 293 ? 67.77648 -42.82421 -78.15629  1.000 255.64983 ? 287 MET A CG  1 
ATOM   2205 S SD  . MET A 1 293 ? 66.27200 -43.68195 -77.65597  1.000 307.74991 ? 287 MET A SD  1 
ATOM   2206 C CE  . MET A 1 293 ? 66.87796 -44.66960 -76.29085  1.000 260.70827 ? 287 MET A CE  1 
ATOM   2207 N N   . ALA A 1 294 ? 69.09452 -39.39954 -75.38273  1.000 237.69437 ? 288 ALA A N   1 
ATOM   2208 C CA  . ALA A 1 294 ? 69.64807 -38.75253 -74.19834  1.000 245.32117 ? 288 ALA A CA  1 
ATOM   2209 C C   . ALA A 1 294 ? 68.65299 -37.77200 -73.59248  1.000 253.49969 ? 288 ALA A C   1 
ATOM   2210 O O   . ALA A 1 294 ? 68.58480 -37.62565 -72.36656  1.000 262.87452 ? 288 ALA A O   1 
ATOM   2211 C CB  . ALA A 1 294 ? 70.95668 -38.04533 -74.54772  1.000 250.62388 ? 288 ALA A CB  1 
ATOM   2212 N N   . THR A 1 295 ? 67.87356 -37.09081 -74.43544  1.000 256.80733 ? 289 THR A N   1 
ATOM   2213 C CA  . THR A 1 295 ? 66.84559 -36.19085 -73.92423  1.000 251.93807 ? 289 THR A CA  1 
ATOM   2214 C C   . THR A 1 295 ? 65.73250 -36.96822 -73.23265  1.000 248.62275 ? 289 THR A C   1 
ATOM   2215 O O   . THR A 1 295 ? 65.21905 -36.53709 -72.19372  1.000 238.18534 ? 289 THR A O   1 
ATOM   2216 C CB  . THR A 1 295 ? 66.28093 -35.33712 -75.06087  1.000 235.34543 ? 289 THR A CB  1 
ATOM   2217 O OG1 . THR A 1 295 ? 67.34901 -34.63463 -75.70909  1.000 215.56919 ? 289 THR A OG1 1 
ATOM   2218 C CG2 . THR A 1 295 ? 65.27429 -34.32952 -74.52611  1.000 236.04592 ? 289 THR A CG2 1 
ATOM   2219 N N   . ALA A 1 296 ? 65.35582 -38.12328 -73.78724  1.000 254.56610 ? 290 ALA A N   1 
ATOM   2220 C CA  . ALA A 1 296 ? 64.30447 -38.92982 -73.17596  1.000 267.12367 ? 290 ALA A CA  1 
ATOM   2221 C C   . ALA A 1 296 ? 64.75603 -39.51363 -71.84293  1.000 254.69288 ? 290 ALA A C   1 
ATOM   2222 O O   . ALA A 1 296 ? 64.00225 -39.49059 -70.86285  1.000 258.68269 ? 290 ALA A O   1 
ATOM   2223 C CB  . ALA A 1 296 ? 63.87212 -40.04180 -74.13100  1.000 283.85600 ? 290 ALA A CB  1 
ATOM   2224 N N   . ARG A 1 297 ? 65.97919 -40.04700 -71.78532  1.000 232.17610 ? 291 ARG A N   1 
ATOM   2225 C CA  . ARG A 1 297 ? 66.47987 -40.59046 -70.52732  1.000 234.63506 ? 291 ARG A CA  1 
ATOM   2226 C C   . ARG A 1 297 ? 66.70400 -39.49620 -69.49220  1.000 245.82967 ? 291 ARG A C   1 
ATOM   2227 O O   . ARG A 1 297 ? 66.62377 -39.76081 -68.28714  1.000 232.64937 ? 291 ARG A O   1 
ATOM   2228 C CB  . ARG A 1 297 ? 67.76898 -41.37672 -70.76438  1.000 231.08925 ? 291 ARG A CB  1 
ATOM   2229 C CG  . ARG A 1 297 ? 67.54548 -42.74857 -71.37858  1.000 223.30847 ? 291 ARG A CG  1 
ATOM   2230 C CD  . ARG A 1 297 ? 68.81938 -43.57485 -71.37051  1.000 231.00366 ? 291 ARG A CD  1 
ATOM   2231 N NE  . ARG A 1 297 ? 69.78744 -43.09986 -72.35099  1.000 259.14288 ? 291 ARG A NE  1 
ATOM   2232 C CZ  . ARG A 1 297 ? 69.95927 -43.63718 -73.55077  1.000 259.24670 ? 291 ARG A CZ  1 
ATOM   2233 N NH1 . ARG A 1 297 ? 69.25120 -44.68192 -73.94755  1.000 224.01110 ? 291 ARG A NH1 1 
ATOM   2234 N NH2 . ARG A 1 297 ? 70.86634 -43.11551 -74.37165  1.000 268.12877 ? 291 ARG A NH2 1 
ATOM   2235 N N   . SER A 1 298 ? 66.98401 -38.26839 -69.93597  1.000 257.26153 ? 292 SER A N   1 
ATOM   2236 C CA  . SER A 1 298 ? 67.08630 -37.15539 -68.99795  1.000 250.89014 ? 292 SER A CA  1 
ATOM   2237 C C   . SER A 1 298 ? 65.72729 -36.82628 -68.39246  1.000 235.78936 ? 292 SER A C   1 
ATOM   2238 O O   . SER A 1 298 ? 65.62768 -36.53557 -67.19491  1.000 230.31909 ? 292 SER A O   1 
ATOM   2239 C CB  . SER A 1 298 ? 67.67912 -35.93083 -69.69581  1.000 243.83101 ? 292 SER A CB  1 
ATOM   2240 O OG  . SER A 1 298 ? 68.99487 -36.19069 -70.15558  1.000 261.14761 ? 292 SER A OG  1 
ATOM   2241 N N   . LEU A 1 299 ? 64.66877 -36.87284 -69.20558  1.000 242.79684 ? 293 LEU A N   1 
ATOM   2242 C CA  . LEU A 1 299 ? 63.31602 -36.66729 -68.70254  1.000 254.62499 ? 293 LEU A CA  1 
ATOM   2243 C C   . LEU A 1 299 ? 62.81616 -37.85510 -67.89297  1.000 259.19488 ? 293 LEU A C   1 
ATOM   2244 O O   . LEU A 1 299 ? 61.93605 -37.68478 -67.04194  1.000 263.51713 ? 293 LEU A O   1 
ATOM   2245 C CB  . LEU A 1 299 ? 62.35842 -36.40169 -69.86262  1.000 266.44630 ? 293 LEU A CB  1 
ATOM   2246 C CG  . LEU A 1 299 ? 62.66936 -35.19140 -70.74204  1.000 274.39423 ? 293 LEU A CG  1 
ATOM   2247 C CD1 . LEU A 1 299 ? 61.65304 -35.07761 -71.86923  1.000 334.73770 ? 293 LEU A CD1 1 
ATOM   2248 C CD2 . LEU A 1 299 ? 62.69595 -33.92445 -69.90529  1.000 285.02967 ? 293 LEU A CD2 1 
ATOM   2249 N N   . ASP A 1 300 ? 63.35124 -39.05233 -68.14345  1.000 251.85610 ? 294 ASP A N   1 
ATOM   2250 C CA  . ASP A 1 300 ? 62.91382 -40.22783 -67.39867  1.000 260.53906 ? 294 ASP A CA  1 
ATOM   2251 C C   . ASP A 1 300 ? 63.35158 -40.14948 -65.94167  1.000 256.68107 ? 294 ASP A C   1 
ATOM   2252 O O   . ASP A 1 300 ? 62.61953 -40.58203 -65.04414  1.000 267.18870 ? 294 ASP A O   1 
ATOM   2253 C CB  . ASP A 1 300 ? 63.45340 -41.49638 -68.06106  1.000 252.71601 ? 294 ASP A CB  1 
ATOM   2254 C CG  . ASP A 1 300 ? 62.83695 -42.76461 -67.49320  1.000 260.49896 ? 294 ASP A CG  1 
ATOM   2255 O OD1 . ASP A 1 300 ? 61.63386 -43.00311 -67.72913  1.000 263.70674 ? 294 ASP A OD1 1 
ATOM   2256 O OD2 . ASP A 1 300 ? 63.55894 -43.52992 -66.82136  1.000 280.93333 ? 294 ASP A OD2 1 
ATOM   2257 N N   . ALA A 1 301 ? 64.53862 -39.59507 -65.68435  1.000 230.59258 ? 295 ALA A N   1 
ATOM   2258 C CA  . ALA A 1 301 ? 65.01146 -39.46853 -64.31129  1.000 220.19940 ? 295 ALA A CA  1 
ATOM   2259 C C   . ALA A 1 301 ? 64.33322 -38.32321 -63.56998  1.000 222.33851 ? 295 ALA A C   1 
ATOM   2260 O O   . ALA A 1 301 ? 64.37729 -38.28832 -62.33524  1.000 204.64418 ? 295 ALA A O   1 
ATOM   2261 C CB  . ALA A 1 301 ? 66.52943 -39.28460 -64.29210  1.000 237.98415 ? 295 ALA A CB  1 
ATOM   2262 N N   . LEU A 1 302 ? 63.70649 -37.39374 -64.29305  1.000 228.06483 ? 296 LEU A N   1 
ATOM   2263 C CA  . LEU A 1 302 ? 62.98553 -36.28442 -63.68129  1.000 237.83060 ? 296 LEU A CA  1 
ATOM   2264 C C   . LEU A 1 302 ? 61.55905 -36.64929 -63.29461  1.000 259.24240 ? 296 LEU A C   1 
ATOM   2265 O O   . LEU A 1 302 ? 61.02833 -36.09719 -62.32326  1.000 251.16306 ? 296 LEU A O   1 
ATOM   2266 C CB  . LEU A 1 302 ? 62.96017 -35.08581 -64.63276  1.000 237.92565 ? 296 LEU A CB  1 
ATOM   2267 C CG  . LEU A 1 302 ? 64.31685 -34.47451 -64.98282  1.000 237.66795 ? 296 LEU A CG  1 
ATOM   2268 C CD1 . LEU A 1 302 ? 64.16031 -33.38771 -66.03529  1.000 241.68075 ? 296 LEU A CD1 1 
ATOM   2269 C CD2 . LEU A 1 302 ? 64.97976 -33.92322 -63.73388  1.000 243.24048 ? 296 LEU A CD2 1 
ATOM   2270 N N   . CYS A 1 303 ? 60.92207 -37.56126 -64.03415  1.000 273.23193 ? 297 CYS A N   1 
ATOM   2271 C CA  . CYS A 1 303 ? 59.56793 -37.97631 -63.68337  1.000 277.17639 ? 297 CYS A CA  1 
ATOM   2272 C C   . CYS A 1 303 ? 59.53928 -38.75323 -62.37436  1.000 276.41274 ? 297 CYS A C   1 
ATOM   2273 O O   . CYS A 1 303 ? 58.54747 -38.69003 -61.63884  1.000 275.17747 ? 297 CYS A O   1 
ATOM   2274 C CB  . CYS A 1 303 ? 58.96432 -38.81882 -64.80608  1.000 275.01629 ? 297 CYS A CB  1 
ATOM   2275 S SG  . CYS A 1 303 ? 58.75495 -37.94552 -66.37294  1.000 269.42314 ? 297 CYS A SG  1 
ATOM   2276 N N   . VAL A 1 304 ? 60.60646 -39.49026 -62.06744  1.000 267.82028 ? 298 VAL A N   1 
ATOM   2277 C CA  . VAL A 1 304 ? 60.64703 -40.26357 -60.83297  1.000 255.72539 ? 298 VAL A CA  1 
ATOM   2278 C C   . VAL A 1 304 ? 61.15567 -39.44830 -59.65194  1.000 253.11657 ? 298 VAL A C   1 
ATOM   2279 O O   . VAL A 1 304 ? 60.97465 -39.86521 -58.49911  1.000 261.85350 ? 298 VAL A O   1 
ATOM   2280 C CB  . VAL A 1 304 ? 61.51504 -41.52147 -61.00604  1.000 243.07072 ? 298 VAL A CB  1 
ATOM   2281 C CG1 . VAL A 1 304 ? 60.98537 -42.36965 -62.14791  1.000 245.14753 ? 298 VAL A CG1 1 
ATOM   2282 C CG2 . VAL A 1 304 ? 62.96607 -41.13529 -61.24823  1.000 212.19318 ? 298 VAL A CG2 1 
ATOM   2283 N N   . GLN A 1 305 ? 61.77599 -38.29816 -59.90111  1.000 244.73396 ? 299 GLN A N   1 
ATOM   2284 C CA  . GLN A 1 305 ? 62.33263 -37.47325 -58.84002  1.000 250.92363 ? 299 GLN A CA  1 
ATOM   2285 C C   . GLN A 1 305 ? 61.50880 -36.22999 -58.54332  1.000 263.96069 ? 299 GLN A C   1 
ATOM   2286 O O   . GLN A 1 305 ? 61.52929 -35.74667 -57.40893  1.000 264.00334 ? 299 GLN A O   1 
ATOM   2287 C CB  . GLN A 1 305 ? 63.76856 -37.06400 -59.19525  1.000 238.22863 ? 299 GLN A CB  1 
ATOM   2288 C CG  . GLN A 1 305 ? 64.51771 -36.33625 -58.09314  1.000 277.35298 ? 299 GLN A CG  1 
ATOM   2289 C CD  . GLN A 1 305 ? 64.54855 -37.10587 -56.78755  1.000 290.56589 ? 299 GLN A CD  1 
ATOM   2290 O OE1 . GLN A 1 305 ? 64.64224 -38.33336 -56.77452  1.000 283.22261 ? 299 GLN A OE1 1 
ATOM   2291 N NE2 . GLN A 1 305 ? 64.46736 -36.38241 -55.67678  1.000 305.10887 ? 299 GLN A NE2 1 
ATOM   2292 N N   . ASN A 1 306 ? 60.77577 -35.71099 -59.52418  1.000 259.98005 ? 300 ASN A N   1 
ATOM   2293 C CA  . ASN A 1 306 ? 59.89506 -34.57041 -59.32938  1.000 252.77305 ? 300 ASN A CA  1 
ATOM   2294 C C   . ASN A 1 306 ? 58.50740 -34.92621 -59.84480  1.000 253.92381 ? 300 ASN A C   1 
ATOM   2295 O O   . ASN A 1 306 ? 58.25899 -36.04337 -60.30877  1.000 251.91149 ? 300 ASN A O   1 
ATOM   2296 C CB  . ASN A 1 306 ? 60.44593 -33.32076 -60.02553  1.000 223.80393 ? 300 ASN A CB  1 
ATOM   2297 C CG  . ASN A 1 306 ? 61.75957 -32.86282 -59.43121  1.000 237.62488 ? 300 ASN A CG  1 
ATOM   2298 O OD1 . ASN A 1 306 ? 62.83161 -33.27082 -59.87688  1.000 250.41132 ? 300 ASN A OD1 1 
ATOM   2299 N ND2 . ASN A 1 306 ? 61.68341 -32.01958 -58.40861  1.000 231.38453 ? 300 ASN A ND2 1 
ATOM   2300 N N   . ASP A 1 307 ? 57.59100 -33.96277 -59.75426  1.000 266.42769 ? 301 ASP A N   1 
ATOM   2301 C CA  . ASP A 1 307 ? 56.21745 -34.16154 -60.21175  1.000 272.48998 ? 301 ASP A CA  1 
ATOM   2302 C C   . ASP A 1 307 ? 56.16544 -33.84566 -61.70326  1.000 252.14766 ? 301 ASP A C   1 
ATOM   2303 O O   . ASP A 1 307 ? 55.72871 -32.77865 -62.13981  1.000 246.22752 ? 301 ASP A O   1 
ATOM   2304 C CB  . ASP A 1 307 ? 55.25138 -33.30222 -59.40754  1.000 282.86018 ? 301 ASP A CB  1 
ATOM   2305 C CG  . ASP A 1 307 ? 53.85958 -33.89497 -59.34965  1.000 284.84300 ? 301 ASP A CG  1 
ATOM   2306 O OD1 . ASP A 1 307 ? 53.42431 -34.49297 -60.35574  1.000 298.85391 ? 301 ASP A OD1 1 
ATOM   2307 O OD2 . ASP A 1 307 ? 53.20472 -33.77180 -58.29390  1.000 285.63318 ? 301 ASP A OD2 1 
ATOM   2308 N N   . LEU A 1 308 ? 56.63703 -34.80387 -62.49514  1.000 255.43900 ? 302 LEU A N   1 
ATOM   2309 C CA  . LEU A 1 308 ? 56.66727 -34.69278 -63.94475  1.000 258.78447 ? 302 LEU A CA  1 
ATOM   2310 C C   . LEU A 1 308 ? 56.15323 -35.98902 -64.55176  1.000 277.15387 ? 302 LEU A C   1 
ATOM   2311 O O   . LEU A 1 308 ? 56.39935 -37.07388 -64.01673  1.000 291.78388 ? 302 LEU A O   1 
ATOM   2312 C CB  . LEU A 1 308 ? 58.08640 -34.39243 -64.44648  1.000 221.55271 ? 302 LEU A CB  1 
ATOM   2313 C CG  . LEU A 1 308 ? 58.31404 -34.33974 -65.95844  1.000 215.83861 ? 302 LEU A CG  1 
ATOM   2314 C CD1 . LEU A 1 308 ? 57.49364 -33.23282 -66.59688  1.000 202.65044 ? 302 LEU A CD1 1 
ATOM   2315 C CD2 . LEU A 1 308 ? 59.79020 -34.16068 -66.26559  1.000 225.51331 ? 302 LEU A CD2 1 
ATOM   2316 N N   . SER A 1 309 ? 55.42878 -35.87176 -65.66245  1.000 273.74680 ? 303 SER A N   1 
ATOM   2317 C CA  . SER A 1 309 ? 54.88640 -37.02762 -66.36079  1.000 281.81015 ? 303 SER A CA  1 
ATOM   2318 C C   . SER A 1 309 ? 55.00482 -36.80756 -67.86099  1.000 272.92577 ? 303 SER A C   1 
ATOM   2319 O O   . SER A 1 309 ? 54.71922 -35.71536 -68.35970  1.000 274.55048 ? 303 SER A O   1 
ATOM   2320 C CB  . SER A 1 309 ? 53.42304 -37.28028 -65.97461  1.000 298.45797 ? 303 SER A CB  1 
ATOM   2321 O OG  . SER A 1 309 ? 53.29605 -37.54504 -64.58790  1.000 279.20459 ? 303 SER A OG  1 
ATOM   2322 N N   . VAL A 1 310 ? 55.42863 -37.84889 -68.57517  1.000 254.12095 ? 304 VAL A N   1 
ATOM   2323 C CA  . VAL A 1 310 ? 55.66704 -37.78090 -70.01231  1.000 233.07280 ? 304 VAL A CA  1 
ATOM   2324 C C   . VAL A 1 310 ? 54.97146 -38.95826 -70.68075  1.000 227.20494 ? 304 VAL A C   1 
ATOM   2325 O O   . VAL A 1 310 ? 55.08651 -40.09809 -70.21687  1.000 228.01097 ? 304 VAL A O   1 
ATOM   2326 C CB  . VAL A 1 310 ? 57.17274 -37.78811 -70.34339  1.000 221.35030 ? 304 VAL A CB  1 
ATOM   2327 C CG1 . VAL A 1 310 ? 57.38960 -37.81482 -71.84972  1.000 229.45203 ? 304 VAL A CG1 1 
ATOM   2328 C CG2 . VAL A 1 310 ? 57.86314 -36.58188 -69.72420  1.000 224.75447 ? 304 VAL A CG2 1 
ATOM   2329 N N   . LYS A 1 311 ? 54.24980 -38.68109 -71.76527  1.000 226.46148 ? 305 LYS A N   1 
ATOM   2330 C CA  . LYS A 1 311 ? 53.63559 -39.70953 -72.59062  1.000 226.48812 ? 305 LYS A CA  1 
ATOM   2331 C C   . LYS A 1 311 ? 53.92146 -39.41157 -74.05538  1.000 224.31308 ? 305 LYS A C   1 
ATOM   2332 O O   . LYS A 1 311 ? 54.06746 -38.25213 -74.45194  1.000 220.45784 ? 305 LYS A O   1 
ATOM   2333 C CB  . LYS A 1 311 ? 52.12032 -39.80291 -72.35302  1.000 221.06119 ? 305 LYS A CB  1 
ATOM   2334 C CG  . LYS A 1 311 ? 51.74284 -40.37090 -70.99284  1.000 224.86145 ? 305 LYS A CG  1 
ATOM   2335 C CD  . LYS A 1 311 ? 50.25272 -40.66018 -70.90188  1.000 223.08321 ? 305 LYS A CD  1 
ATOM   2336 C CE  . LYS A 1 311 ? 49.90193 -41.33289 -69.58317  1.000 218.19832 ? 305 LYS A CE  1 
ATOM   2337 N NZ  . LYS A 1 311 ? 48.45973 -41.69600 -69.50669  1.000 192.17647 ? 305 LYS A NZ  1 
ATOM   2338 N N   . VAL A 1 312 ? 54.00531 -40.47164 -74.85776  1.000 228.68716 ? 306 VAL A N   1 
ATOM   2339 C CA  . VAL A 1 312 ? 54.36518 -40.35354 -76.26329  1.000 226.63441 ? 306 VAL A CA  1 
ATOM   2340 C C   . VAL A 1 312 ? 53.23358 -40.90082 -77.12396  1.000 224.26696 ? 306 VAL A C   1 
ATOM   2341 O O   . VAL A 1 312 ? 52.37772 -41.66221 -76.66627  1.000 221.94888 ? 306 VAL A O   1 
ATOM   2342 C CB  . VAL A 1 312 ? 55.68982 -41.07564 -76.58675  1.000 226.38881 ? 306 VAL A CB  1 
ATOM   2343 C CG1 . VAL A 1 312 ? 56.82715 -40.49063 -75.76357  1.000 232.56548 ? 306 VAL A CG1 1 
ATOM   2344 C CG2 . VAL A 1 312 ? 55.55583 -42.56999 -76.33847  1.000 227.36813 ? 306 VAL A CG2 1 
ATOM   2345 N N   . PHE A 1 313 ? 53.24052 -40.49426 -78.39256  1.000 231.21764 ? 307 PHE A N   1 
ATOM   2346 C CA  . PHE A 1 313 ? 52.26317 -40.96505 -79.36301  1.000 231.68365 ? 307 PHE A CA  1 
ATOM   2347 C C   . PHE A 1 313 ? 52.93415 -41.07638 -80.72424  1.000 226.38678 ? 307 PHE A C   1 
ATOM   2348 O O   . PHE A 1 313 ? 53.92875 -40.40282 -81.00599  1.000 224.84684 ? 307 PHE A O   1 
ATOM   2349 C CB  . PHE A 1 313 ? 51.03849 -40.04189 -79.43378  1.000 225.86348 ? 307 PHE A CB  1 
ATOM   2350 C CG  . PHE A 1 313 ? 51.36156 -38.62407 -79.81431  1.000 241.37702 ? 307 PHE A CG  1 
ATOM   2351 C CD1 . PHE A 1 313 ? 51.72135 -37.69829 -78.84857  1.000 247.46053 ? 307 PHE A CD1 1 
ATOM   2352 C CD2 . PHE A 1 313 ? 51.29060 -38.21297 -81.13533  1.000 223.94269 ? 307 PHE A CD2 1 
ATOM   2353 C CE1 . PHE A 1 313 ? 52.01383 -36.39264 -79.19390  1.000 227.68406 ? 307 PHE A CE1 1 
ATOM   2354 C CE2 . PHE A 1 313 ? 51.58143 -36.90958 -81.48589  1.000 209.65837 ? 307 PHE A CE2 1 
ATOM   2355 C CZ  . PHE A 1 313 ? 51.94290 -35.99787 -80.51376  1.000 210.76362 ? 307 PHE A CZ  1 
ATOM   2356 N N   . THR A 1 314 ? 52.37305 -41.93892 -81.57062  1.000 213.86383 ? 308 THR A N   1 
ATOM   2357 C CA  . THR A 1 314 ? 52.93865 -42.22710 -82.88131  1.000 222.46908 ? 308 THR A CA  1 
ATOM   2358 C C   . THR A 1 314 ? 52.06166 -41.75600 -84.03264  1.000 222.65711 ? 308 THR A C   1 
ATOM   2359 O O   . THR A 1 314 ? 52.46263 -41.89259 -85.19351  1.000 225.44027 ? 308 THR A O   1 
ATOM   2360 C CB  . THR A 1 314 ? 53.20000 -43.73155 -83.02436  1.000 250.26961 ? 308 THR A CB  1 
ATOM   2361 O OG1 . THR A 1 314 ? 51.96323 -44.44653 -82.90823  1.000 247.78920 ? 308 THR A OG1 1 
ATOM   2362 C CG2 . THR A 1 314 ? 54.15893 -44.21033 -81.94471  1.000 271.17322 ? 308 THR A CG2 1 
ATOM   2363 N N   . ILE A 1 315 ? 50.88277 -41.20763 -83.74919  1.000 230.18145 ? 309 ILE A N   1 
ATOM   2364 C CA  . ILE A 1 315 ? 49.98086 -40.78085 -84.81038  1.000 231.04956 ? 309 ILE A CA  1 
ATOM   2365 C C   . ILE A 1 315 ? 50.45719 -39.45690 -85.40019  1.000 225.07452 ? 309 ILE A C   1 
ATOM   2366 O O   . ILE A 1 315 ? 51.24565 -38.72028 -84.80149  1.000 222.55578 ? 309 ILE A O   1 
ATOM   2367 C CB  . ILE A 1 315 ? 48.53685 -40.67218 -84.29118  1.000 205.92060 ? 309 ILE A CB  1 
ATOM   2368 C CG1 . ILE A 1 315 ? 48.46208 -39.66292 -83.14410  1.000 189.19315 ? 309 ILE A CG1 1 
ATOM   2369 C CG2 . ILE A 1 315 ? 48.02990 -42.03278 -83.84083  1.000 218.96206 ? 309 ILE A CG2 1 
ATOM   2370 C CD1 . ILE A 1 315 ? 47.08306 -39.51889 -82.54622  1.000 188.78277 ? 309 ILE A CD1 1 
ATOM   2371 N N   . GLN A 1 316 ? 49.96789 -39.15615 -86.60130  1.000 210.61368 ? 310 GLN A N   1 
ATOM   2372 C CA  . GLN A 1 316 ? 50.25844 -37.87941 -87.24537  1.000 217.59249 ? 310 GLN A CA  1 
ATOM   2373 C C   . GLN A 1 316 ? 49.45486 -36.78126 -86.56110  1.000 223.13172 ? 310 GLN A C   1 
ATOM   2374 O O   . GLN A 1 316 ? 48.23377 -36.69764 -86.72804  1.000 221.24815 ? 310 GLN A O   1 
ATOM   2375 C CB  . GLN A 1 316 ? 49.93555 -37.94818 -88.73467  1.000 223.92071 ? 310 GLN A CB  1 
ATOM   2376 C CG  . GLN A 1 316 ? 50.92324 -38.76549 -89.54951  1.000 225.42956 ? 310 GLN A CG  1 
ATOM   2377 C CD  . GLN A 1 316 ? 50.59947 -38.75765 -91.03036  1.000 250.94222 ? 310 GLN A CD  1 
ATOM   2378 O OE1 . GLN A 1 316 ? 49.44385 -38.91161 -91.42562  1.000 266.87147 ? 310 GLN A OE1 1 
ATOM   2379 N NE2 . GLN A 1 316 ? 51.62044 -38.56911 -91.85853  1.000 259.08361 ? 310 GLN A NE2 1 
ATOM   2380 N N   . ASN A 1 317 ? 50.13681 -35.93868 -85.78825  1.000 217.06125 ? 311 ASN A N   1 
ATOM   2381 C CA  . ASN A 1 317 ? 49.48623 -34.88449 -85.01905  1.000 210.83102 ? 311 ASN A CA  1 
ATOM   2382 C C   . ASN A 1 317 ? 50.35207 -33.63639 -85.07025  1.000 215.57672 ? 311 ASN A C   1 
ATOM   2383 O O   . ASN A 1 317 ? 51.51540 -33.66958 -84.65778  1.000 205.08472 ? 311 ASN A O   1 
ATOM   2384 C CB  . ASN A 1 317 ? 49.25728 -35.32497 -83.56964  1.000 200.04428 ? 311 ASN A CB  1 
ATOM   2385 C CG  . ASN A 1 317 ? 48.56046 -34.26625 -82.73965  1.000 207.59659 ? 311 ASN A CG  1 
ATOM   2386 O OD1 . ASN A 1 317 ? 47.79751 -33.45512 -83.26080  1.000 220.73227 ? 311 ASN A OD1 1 
ATOM   2387 N ND2 . ASN A 1 317 ? 48.82131 -34.26910 -81.43785  1.000 210.60354 ? 311 ASN A ND2 1 
ATOM   2388 N N   . ASN A 1 318 ? 49.78659 -32.54199 -85.57663  1.000 228.23574 ? 312 ASN A N   1 
ATOM   2389 C CA  . ASN A 1 318 ? 50.47827 -31.26339 -85.65740  1.000 227.42958 ? 312 ASN A CA  1 
ATOM   2390 C C   . ASN A 1 318 ? 50.16479 -30.35216 -84.47683  1.000 220.14889 ? 312 ASN A C   1 
ATOM   2391 O O   . ASN A 1 318 ? 50.56847 -29.18515 -84.48704  1.000 209.24151 ? 312 ASN A O   1 
ATOM   2392 C CB  . ASN A 1 318 ? 50.12534 -30.55217 -86.96729  1.000 240.90639 ? 312 ASN A CB  1 
ATOM   2393 C CG  . ASN A 1 318 ? 50.51406 -31.35547 -88.19506  1.000 242.25314 ? 312 ASN A CG  1 
ATOM   2394 O OD1 . ASN A 1 318 ? 51.45318 -32.15058 -88.16089  1.000 244.37591 ? 312 ASN A OD1 1 
ATOM   2395 N ND2 . ASN A 1 318 ? 49.79273 -31.14589 -89.29120  1.000 232.98372 ? 312 ASN A ND2 1 
ATOM   2396 N N   . THR A 1 319 ? 49.46508 -30.85980 -83.46191  1.000 227.43625 ? 313 THR A N   1 
ATOM   2397 C CA  . THR A 1 319 ? 49.01770 -30.02445 -82.35294  1.000 224.47420 ? 313 THR A CA  1 
ATOM   2398 C C   . THR A 1 319 ? 50.20165 -29.40689 -81.61908  1.000 217.48465 ? 313 THR A C   1 
ATOM   2399 O O   . THR A 1 319 ? 51.14725 -30.10318 -81.23879  1.000 227.43413 ? 313 THR A O   1 
ATOM   2400 C CB  . THR A 1 319 ? 48.17097 -30.84688 -81.37917  1.000 216.33793 ? 313 THR A CB  1 
ATOM   2401 O OG1 . THR A 1 319 ? 47.03521 -31.38779 -82.06582  1.000 226.61808 ? 313 THR A OG1 1 
ATOM   2402 C CG2 . THR A 1 319 ? 47.69084 -29.98043 -80.22343  1.000 202.83296 ? 313 THR A CG2 1 
ATOM   2403 N N   . LYS A 1 320 ? 50.14419 -28.08868 -81.42576  1.000 211.92347 ? 314 LYS A N   1 
ATOM   2404 C CA  . LYS A 1 320 ? 51.15681 -27.33264 -80.68750  1.000 220.09700 ? 314 LYS A CA  1 
ATOM   2405 C C   . LYS A 1 320 ? 50.41588 -26.53297 -79.61814  1.000 214.71174 ? 314 LYS A C   1 
ATOM   2406 O O   . LYS A 1 320 ? 49.96704 -25.41159 -79.86968  1.000 209.09263 ? 314 LYS A O   1 
ATOM   2407 C CB  . LYS A 1 320 ? 51.96424 -26.43116 -81.61860  1.000 213.17382 ? 314 LYS A CB  1 
ATOM   2408 C CG  . LYS A 1 320 ? 52.57304 -27.14174 -82.82045  1.000 216.23112 ? 314 LYS A CG  1 
ATOM   2409 C CD  . LYS A 1 320 ? 53.57365 -28.20515 -82.39808  1.000 230.86484 ? 314 LYS A CD  1 
ATOM   2410 C CE  . LYS A 1 320 ? 54.24877 -28.83955 -83.60518  1.000 217.63166 ? 314 LYS A CE  1 
ATOM   2411 N NZ  . LYS A 1 320 ? 53.26861 -29.47929 -84.52521  1.000 193.79588 ? 314 LYS A NZ  1 
ATOM   2412 N N   . LEU A 1 321 ? 50.29059 -27.11168 -78.42600  1.000 208.89534 ? 315 LEU A N   1 
ATOM   2413 C CA  . LEU A 1 321 ? 49.49155 -26.54412 -77.34913  1.000 204.08649 ? 315 LEU A CA  1 
ATOM   2414 C C   . LEU A 1 321 ? 50.35550 -26.29868 -76.11911  1.000 218.12171 ? 315 LEU A C   1 
ATOM   2415 O O   . LEU A 1 321 ? 51.26358 -27.08008 -75.81934  1.000 229.76810 ? 315 LEU A O   1 
ATOM   2416 C CB  . LEU A 1 321 ? 48.32317 -27.47417 -76.99414  1.000 200.97217 ? 315 LEU A CB  1 
ATOM   2417 C CG  . LEU A 1 321 ? 47.43667 -27.09954 -75.80432  1.000 217.31148 ? 315 LEU A CG  1 
ATOM   2418 C CD1 . LEU A 1 321 ? 46.79551 -25.73862 -76.01431  1.000 208.54793 ? 315 LEU A CD1 1 
ATOM   2419 C CD2 . LEU A 1 321 ? 46.37655 -28.16460 -75.57123  1.000 234.70879 ? 315 LEU A CD2 1 
ATOM   2420 N N   . LEU A 1 322 ? 50.06516 -25.20810 -75.40982  1.000 225.88738 ? 316 LEU A N   1 
ATOM   2421 C CA  . LEU A 1 322 ? 50.74749 -24.86910 -74.16478  1.000 225.56294 ? 316 LEU A CA  1 
ATOM   2422 C C   . LEU A 1 322 ? 49.74127 -24.23712 -73.21564  1.000 229.13569 ? 316 LEU A C   1 
ATOM   2423 O O   . LEU A 1 322 ? 49.11469 -23.22925 -73.55605  1.000 230.83145 ? 316 LEU A O   1 
ATOM   2424 C CB  . LEU A 1 322 ? 51.92350 -23.91904 -74.41537  1.000 222.46908 ? 316 LEU A CB  1 
ATOM   2425 C CG  . LEU A 1 322 ? 52.46802 -23.14574 -73.21014  1.000 215.21566 ? 316 LEU A CG  1 
ATOM   2426 C CD1 . LEU A 1 322 ? 53.00921 -24.08544 -72.14413  1.000 202.92775 ? 316 LEU A CD1 1 
ATOM   2427 C CD2 . LEU A 1 322 ? 53.53804 -22.15712 -73.64811  1.000 229.08923 ? 316 LEU A CD2 1 
ATOM   2428 N N   . ILE A 1 323 ? 49.58812 -24.82755 -72.03154  1.000 231.37958 ? 317 ILE A N   1 
ATOM   2429 C CA  . ILE A 1 323 ? 48.67141 -24.33825 -71.00790  1.000 242.70433 ? 317 ILE A CA  1 
ATOM   2430 C C   . ILE A 1 323 ? 49.45031 -24.17130 -69.71136  1.000 241.63433 ? 317 ILE A C   1 
ATOM   2431 O O   . ILE A 1 323 ? 50.17301 -25.08373 -69.29515  1.000 239.79028 ? 317 ILE A O   1 
ATOM   2432 C CB  . ILE A 1 323 ? 47.47669 -25.28990 -70.80362  1.000 241.08633 ? 317 ILE A CB  1 
ATOM   2433 C CG1 . ILE A 1 323 ? 46.70468 -25.46620 -72.11279  1.000 227.91091 ? 317 ILE A CG1 1 
ATOM   2434 C CG2 . ILE A 1 323 ? 46.55854 -24.77004 -69.70601  1.000 204.88452 ? 317 ILE A CG2 1 
ATOM   2435 C CD1 . ILE A 1 323 ? 45.55484 -26.44162 -72.01605  1.000 210.64237 ? 317 ILE A CD1 1 
ATOM   2436 N N   . VAL A 1 324 ? 49.30257 -23.01150 -69.07473  1.000 239.52228 ? 318 VAL A N   1 
ATOM   2437 C CA  . VAL A 1 324 ? 50.04622 -22.67323 -67.86647  1.000 243.23510 ? 318 VAL A CA  1 
ATOM   2438 C C   . VAL A 1 324 ? 49.05677 -22.24793 -66.79079  1.000 253.84097 ? 318 VAL A C   1 
ATOM   2439 O O   . VAL A 1 324 ? 48.32805 -21.26397 -66.96818  1.000 259.81370 ? 318 VAL A O   1 
ATOM   2440 C CB  . VAL A 1 324 ? 51.07847 -21.56099 -68.11824  1.000 243.16226 ? 318 VAL A CB  1 
ATOM   2441 C CG1 . VAL A 1 324 ? 51.73755 -21.14546 -66.81275  1.000 257.19798 ? 318 VAL A CG1 1 
ATOM   2442 C CG2 . VAL A 1 324 ? 52.12244 -22.02221 -69.12446  1.000 217.39697 ? 318 VAL A CG2 1 
ATOM   2443 N N   . ASP A 1 325 ? 49.02851 -22.99214 -65.68346  1.000 260.65032 ? 319 ASP A N   1 
ATOM   2444 C CA  . ASP A 1 325 ? 48.26028 -22.65407 -64.48519  1.000 276.50669 ? 319 ASP A CA  1 
ATOM   2445 C C   . ASP A 1 325 ? 46.76482 -22.51525 -64.75474  1.000 261.15666 ? 319 ASP A C   1 
ATOM   2446 O O   . ASP A 1 325 ? 46.05624 -21.85710 -63.98410  1.000 224.14512 ? 319 ASP A O   1 
ATOM   2447 C CB  . ASP A 1 325 ? 48.79173 -21.37203 -63.83089  1.000 277.05863 ? 319 ASP A CB  1 
ATOM   2448 C CG  . ASP A 1 325 ? 50.22252 -21.51229 -63.34738  1.000 268.32113 ? 319 ASP A CG  1 
ATOM   2449 O OD1 . ASP A 1 325 ? 50.78419 -22.62263 -63.45664  1.000 270.87613 ? 319 ASP A OD1 1 
ATOM   2450 O OD2 . ASP A 1 325 ? 50.78630 -20.51096 -62.85806  1.000 247.65670 ? 319 ASP A OD2 1 
ATOM   2451 N N   . ASP A 1 326 ? 46.26783 -23.12180 -65.83510  1.000 263.80338 ? 320 ASP A N   1 
ATOM   2452 C CA  . ASP A 1 326 ? 44.85935 -23.02950 -66.22647  1.000 270.51055 ? 320 ASP A CA  1 
ATOM   2453 C C   . ASP A 1 326 ? 44.40794 -21.57977 -66.38913  1.000 250.87511 ? 320 ASP A C   1 
ATOM   2454 O O   . ASP A 1 326 ? 43.21422 -21.27440 -66.29255  1.000 236.84606 ? 320 ASP A O   1 
ATOM   2455 C CB  . ASP A 1 326 ? 43.95413 -23.76300 -65.22912  1.000 266.10432 ? 320 ASP A CB  1 
ATOM   2456 C CG  . ASP A 1 326 ? 44.26416 -25.24337 -65.14024  1.000 273.74745 ? 320 ASP A CG  1 
ATOM   2457 O OD1 . ASP A 1 326 ? 45.15786 -25.71023 -65.87696  1.000 266.56281 ? 320 ASP A OD1 1 
ATOM   2458 O OD2 . ASP A 1 326 ? 43.61572 -25.94123 -64.33363  1.000 273.23457 ? 320 ASP A OD2 1 
ATOM   2459 N N   . GLU A 1 327 ? 45.35516 -20.68114 -66.63526  1.000 249.35446 ? 321 GLU A N   1 
ATOM   2460 C CA  . GLU A 1 327 ? 45.08685 -19.26010 -66.78531  1.000 241.47364 ? 321 GLU A CA  1 
ATOM   2461 C C   . GLU A 1 327 ? 45.56781 -18.69493 -68.11136  1.000 237.39379 ? 321 GLU A C   1 
ATOM   2462 O O   . GLU A 1 327 ? 45.00075 -17.70977 -68.58908  1.000 228.94565 ? 321 GLU A O   1 
ATOM   2463 C CB  . GLU A 1 327 ? 45.74186 -18.47795 -65.63446  1.000 246.39066 ? 321 GLU A CB  1 
ATOM   2464 C CG  . GLU A 1 327 ? 45.31640 -17.02635 -65.52737  1.000 260.50038 ? 321 GLU A CG  1 
ATOM   2465 C CD  . GLU A 1 327 ? 45.88898 -16.34847 -64.30013  1.000 275.38311 ? 321 GLU A CD  1 
ATOM   2466 O OE1 . GLU A 1 327 ? 46.55065 -17.03727 -63.49473  1.000 256.30722 ? 321 GLU A OE1 1 
ATOM   2467 O OE2 . GLU A 1 327 ? 45.67746 -15.12835 -64.14021  1.000 297.88660 ? 321 GLU A OE2 1 
ATOM   2468 N N   . TYR A 1 328 ? 46.58416 -19.29869 -68.72223  1.000 226.86059 ? 322 TYR A N   1 
ATOM   2469 C CA  . TYR A 1 328 ? 47.12026 -18.86005 -70.00117  1.000 231.98565 ? 322 TYR A CA  1 
ATOM   2470 C C   . TYR A 1 328 ? 47.21755 -20.04998 -70.94351  1.000 231.36858 ? 322 TYR A C   1 
ATOM   2471 O O   . TYR A 1 328 ? 47.66856 -21.12985 -70.54972  1.000 217.38810 ? 322 TYR A O   1 
ATOM   2472 C CB  . TYR A 1 328 ? 48.49836 -18.20638 -69.82757  1.000 247.63108 ? 322 TYR A CB  1 
ATOM   2473 C CG  . TYR A 1 328 ? 49.25910 -18.00001 -71.11896  1.000 254.93973 ? 322 TYR A CG  1 
ATOM   2474 C CD1 . TYR A 1 328 ? 48.96555 -16.93349 -71.95902  1.000 255.29285 ? 322 TYR A CD1 1 
ATOM   2475 C CD2 . TYR A 1 328 ? 50.28004 -18.86624 -71.49198  1.000 243.11475 ? 322 TYR A CD2 1 
ATOM   2476 C CE1 . TYR A 1 328 ? 49.66172 -16.74004 -73.13846  1.000 256.27418 ? 322 TYR A CE1 1 
ATOM   2477 C CE2 . TYR A 1 328 ? 50.98094 -18.68098 -72.66883  1.000 243.41905 ? 322 TYR A CE2 1 
ATOM   2478 C CZ  . TYR A 1 328 ? 50.66807 -17.61636 -73.48764  1.000 250.95908 ? 322 TYR A CZ  1 
ATOM   2479 O OH  . TYR A 1 328 ? 51.36378 -17.42721 -74.65961  1.000 253.17337 ? 322 TYR A OH  1 
ATOM   2480 N N   . VAL A 1 329 ? 46.79226 -19.84642 -72.18784  1.000 244.38550 ? 323 VAL A N   1 
ATOM   2481 C CA  . VAL A 1 329 ? 46.83976 -20.87857 -73.21453  1.000 231.45991 ? 323 VAL A CA  1 
ATOM   2482 C C   . VAL A 1 329 ? 47.66759 -20.36247 -74.38446  1.000 227.37596 ? 323 VAL A C   1 
ATOM   2483 O O   . VAL A 1 329 ? 47.68317 -19.16257 -74.67898  1.000 230.97180 ? 323 VAL A O   1 
ATOM   2484 C CB  . VAL A 1 329 ? 45.42205 -21.29757 -73.67073  1.000 212.22013 ? 323 VAL A CB  1 
ATOM   2485 C CG1 . VAL A 1 329 ? 44.71335 -20.14645 -74.37190  1.000 202.28536 ? 323 VAL A CG1 1 
ATOM   2486 C CG2 . VAL A 1 329 ? 45.48104 -22.52975 -74.56280  1.000 212.74498 ? 323 VAL A CG2 1 
ATOM   2487 N N   . HIS A 1 330 ? 48.37545 -21.27944 -75.04408  1.000 227.57261 ? 324 HIS A N   1 
ATOM   2488 C CA  . HIS A 1 330 ? 49.25030 -20.93571 -76.16322  1.000 235.57000 ? 324 HIS A CA  1 
ATOM   2489 C C   . HIS A 1 330 ? 49.12492 -22.01210 -77.23268  1.000 225.91736 ? 324 HIS A C   1 
ATOM   2490 O O   . HIS A 1 330 ? 49.64395 -23.12027 -77.06519  1.000 211.03372 ? 324 HIS A O   1 
ATOM   2491 C CB  . HIS A 1 330 ? 50.70213 -20.79230 -75.70514  1.000 241.28827 ? 324 HIS A CB  1 
ATOM   2492 C CG  . HIS A 1 330 ? 51.66764 -20.54307 -76.82213  1.000 228.13458 ? 324 HIS A CG  1 
ATOM   2493 N ND1 . HIS A 1 330 ? 51.90658 -19.28545 -77.33288  1.000 238.99360 ? 324 HIS A ND1 1 
ATOM   2494 C CD2 . HIS A 1 330 ? 52.45375 -21.39080 -77.52729  1.000 199.08608 ? 324 HIS A CD2 1 
ATOM   2495 C CE1 . HIS A 1 330 ? 52.79937 -19.36871 -78.30300  1.000 218.38726 ? 324 HIS A CE1 1 
ATOM   2496 N NE2 . HIS A 1 330 ? 53.14703 -20.63539 -78.44159  1.000 217.24203 ? 324 HIS A NE2 1 
ATOM   2497 N N   . ILE A 1 331 ? 48.44318 -21.68549 -78.32782  1.000 224.20942 ? 325 ILE A N   1 
ATOM   2498 C CA  . ILE A 1 331 ? 48.31560 -22.56443 -79.48473  1.000 216.73698 ? 325 ILE A CA  1 
ATOM   2499 C C   . ILE A 1 331 ? 49.07616 -21.93132 -80.64056  1.000 224.48160 ? 325 ILE A C   1 
ATOM   2500 O O   . ILE A 1 331 ? 48.94954 -20.72576 -80.88753  1.000 237.53372 ? 325 ILE A O   1 
ATOM   2501 C CB  . ILE A 1 331 ? 46.84167 -22.80073 -79.85870  1.000 215.92154 ? 325 ILE A CB  1 
ATOM   2502 C CG1 . ILE A 1 331 ? 46.07190 -23.37318 -78.66814  1.000 212.69487 ? 325 ILE A CG1 1 
ATOM   2503 C CG2 . ILE A 1 331 ? 46.73404 -23.73358 -81.05643  1.000 218.53504 ? 325 ILE A CG2 1 
ATOM   2504 C CD1 . ILE A 1 331 ? 44.62351 -23.68714 -78.97373  1.000 211.97027 ? 325 ILE A CD1 1 
ATOM   2505 N N   . THR A 1 332 ? 49.86636 -22.73700 -81.34339  1.000 223.64086 ? 326 THR A N   1 
ATOM   2506 C CA  . THR A 1 332 ? 50.66445 -22.24309 -82.45767  1.000 236.10517 ? 326 THR A CA  1 
ATOM   2507 C C   . THR A 1 332 ? 50.82054 -23.36322 -83.47964  1.000 231.38499 ? 326 THR A C   1 
ATOM   2508 O O   . THR A 1 332 ? 50.22451 -24.43653 -83.34920  1.000 226.59793 ? 326 THR A O   1 
ATOM   2509 C CB  . THR A 1 332 ? 52.02312 -21.72482 -81.96819  1.000 224.32622 ? 326 THR A CB  1 
ATOM   2510 O OG1 . THR A 1 332 ? 52.81671 -21.32181 -83.09162  1.000 202.40519 ? 326 THR A OG1 1 
ATOM   2511 C CG2 . THR A 1 332 ? 52.75958 -22.80947 -81.19627  1.000 223.83048 ? 326 THR A CG2 1 
ATOM   2512 N N   . SER A 1 333 ? 51.62337 -23.10108 -84.51266  1.000 221.61731 ? 327 SER A N   1 
ATOM   2513 C CA  . SER A 1 333 ? 51.96179 -24.10033 -85.51400  1.000 227.93879 ? 327 SER A CA  1 
ATOM   2514 C C   . SER A 1 333 ? 53.40914 -24.55673 -85.44065  1.000 231.15991 ? 327 SER A C   1 
ATOM   2515 O O   . SER A 1 333 ? 53.70938 -25.67539 -85.86877  1.000 237.52148 ? 327 SER A O   1 
ATOM   2516 C CB  . SER A 1 333 ? 51.68369 -23.56072 -86.92486  1.000 250.05447 ? 327 SER A CB  1 
ATOM   2517 O OG  . SER A 1 333 ? 52.44463 -22.39279 -87.18068  1.000 243.73448 ? 327 SER A OG  1 
ATOM   2518 N N   . ALA A 1 334 ? 54.30220 -23.72786 -84.91171  1.000 224.08452 ? 328 ALA A N   1 
ATOM   2519 C CA  . ALA A 1 334 ? 55.69599 -24.10651 -84.76037  1.000 228.62517 ? 328 ALA A CA  1 
ATOM   2520 C C   . ALA A 1 334 ? 55.90015 -24.89637 -83.47400  1.000 230.92115 ? 328 ALA A C   1 
ATOM   2521 O O   . ALA A 1 334 ? 55.13927 -24.76783 -82.51073  1.000 228.78598 ? 328 ALA A O   1 
ATOM   2522 C CB  . ALA A 1 334 ? 56.59093 -22.86822 -84.76168  1.000 233.39913 ? 328 ALA A CB  1 
ATOM   2523 N N   . ASN A 1 335 ? 56.94356 -25.71814 -83.46714  1.000 244.71974 ? 329 ASN A N   1 
ATOM   2524 C CA  . ASN A 1 335 ? 57.27715 -26.55474 -82.32549  1.000 254.67623 ? 329 ASN A CA  1 
ATOM   2525 C C   . ASN A 1 335 ? 58.32290 -25.87339 -81.44996  1.000 252.53998 ? 329 ASN A C   1 
ATOM   2526 O O   . ASN A 1 335 ? 59.18032 -25.12970 -81.93478  1.000 246.42127 ? 329 ASN A O   1 
ATOM   2527 C CB  . ASN A 1 335 ? 57.79152 -27.92050 -82.78828  1.000 265.17359 ? 329 ASN A CB  1 
ATOM   2528 C CG  . ASN A 1 335 ? 58.25357 -28.79344 -81.63706  1.000 275.57393 ? 329 ASN A CG  1 
ATOM   2529 O OD1 . ASN A 1 335 ? 57.44108 -29.37990 -80.92177  1.000 270.71885 ? 329 ASN A OD1 1 
ATOM   2530 N ND2 . ASN A 1 335 ? 59.56584 -28.88616 -81.45483  1.000 292.05977 ? 329 ASN A ND2 1 
ATOM   2531 N N   . PHE A 1 336 ? 58.23767 -26.13473 -80.14752  1.000 245.61936 ? 330 PHE A N   1 
ATOM   2532 C CA  . PHE A 1 336 ? 59.18712 -25.59870 -79.17415  1.000 243.13635 ? 330 PHE A CA  1 
ATOM   2533 C C   . PHE A 1 336 ? 60.56121 -26.20697 -79.42691  1.000 251.66198 ? 330 PHE A C   1 
ATOM   2534 O O   . PHE A 1 336 ? 60.84076 -27.33455 -79.01312  1.000 261.84504 ? 330 PHE A O   1 
ATOM   2535 C CB  . PHE A 1 336 ? 58.71762 -25.89482 -77.75400  1.000 237.01913 ? 330 PHE A CB  1 
ATOM   2536 C CG  . PHE A 1 336 ? 57.45625 -25.17635 -77.36206  1.000 239.17207 ? 330 PHE A CG  1 
ATOM   2537 C CD1 . PHE A 1 336 ? 57.08464 -23.99789 -77.98767  1.000 242.13927 ? 330 PHE A CD1 1 
ATOM   2538 C CD2 . PHE A 1 336 ? 56.64491 -25.67960 -76.35813  1.000 253.73643 ? 330 PHE A CD2 1 
ATOM   2539 C CE1 . PHE A 1 336 ? 55.92495 -23.33748 -77.62053  1.000 245.58691 ? 330 PHE A CE1 1 
ATOM   2540 C CE2 . PHE A 1 336 ? 55.48516 -25.02457 -75.98734  1.000 250.97376 ? 330 PHE A CE2 1 
ATOM   2541 C CZ  . PHE A 1 336 ? 55.12487 -23.85175 -76.61926  1.000 241.69652 ? 330 PHE A CZ  1 
ATOM   2542 N N   . ASP A 1 337 ? 61.42600 -25.46210 -80.10331  1.000 244.59467 ? 331 ASP A N   1 
ATOM   2543 C CA  . ASP A 1 337 ? 62.80322 -25.88172 -80.35878  1.000 235.61797 ? 331 ASP A CA  1 
ATOM   2544 C C   . ASP A 1 337 ? 63.59014 -24.65541 -80.80951  1.000 238.66710 ? 331 ASP A C   1 
ATOM   2545 O O   . ASP A 1 337 ? 63.07758 -23.52940 -80.79930  1.000 242.00919 ? 331 ASP A O   1 
ATOM   2546 C CB  . ASP A 1 337 ? 62.86426 -27.01165 -81.38819  1.000 231.53949 ? 331 ASP A CB  1 
ATOM   2547 C CG  . ASP A 1 337 ? 62.23383 -26.62976 -82.70965  1.000 233.78066 ? 331 ASP A CG  1 
ATOM   2548 O OD1 . ASP A 1 337 ? 62.87558 -25.89156 -83.48632  1.000 217.86845 ? 331 ASP A OD1 1 
ATOM   2549 O OD2 . ASP A 1 337 ? 61.09417 -27.06752 -82.96994  1.000 248.95107 ? 331 ASP A OD2 1 
ATOM   2550 N N   . GLY A 1 338 ? 64.83822 -24.87584 -81.21326  1.000 221.54644 ? 332 GLY A N   1 
ATOM   2551 C CA  . GLY A 1 338 ? 65.70839 -23.78738 -81.60786  1.000 228.08630 ? 332 GLY A CA  1 
ATOM   2552 C C   . GLY A 1 338 ? 65.49233 -23.30997 -83.02785  1.000 229.58998 ? 332 GLY A C   1 
ATOM   2553 O O   . GLY A 1 338 ? 65.46874 -22.10374 -83.28403  1.000 218.81729 ? 332 GLY A O   1 
ATOM   2554 N N   . THR A 1 339 ? 65.32822 -24.24875 -83.96182  1.000 223.88226 ? 333 THR A N   1 
ATOM   2555 C CA  . THR A 1 339 ? 65.18984 -23.87716 -85.36668  1.000 226.51636 ? 333 THR A CA  1 
ATOM   2556 C C   . THR A 1 339 ? 63.91763 -23.07167 -85.60827  1.000 229.73026 ? 333 THR A C   1 
ATOM   2557 O O   . THR A 1 339 ? 63.90460 -22.14918 -86.43220  1.000 237.45470 ? 333 THR A O   1 
ATOM   2558 C CB  . THR A 1 339 ? 65.20731 -25.13198 -86.24146  1.000 228.74892 ? 333 THR A CB  1 
ATOM   2559 O OG1 . THR A 1 339 ? 66.39815 -25.88349 -85.97578  1.000 219.16441 ? 333 THR A OG1 1 
ATOM   2560 C CG2 . THR A 1 339 ? 65.17485 -24.76072 -87.71643  1.000 267.03607 ? 333 THR A CG2 1 
ATOM   2561 N N   . HIS A 1 340 ? 62.84176 -23.39303 -84.88855  1.000 225.20939 ? 334 HIS A N   1 
ATOM   2562 C CA  . HIS A 1 340 ? 61.56009 -22.74095 -85.13701  1.000 239.24278 ? 334 HIS A CA  1 
ATOM   2563 C C   . HIS A 1 340 ? 61.52806 -21.32043 -84.58212  1.000 232.89636 ? 334 HIS A C   1 
ATOM   2564 O O   . HIS A 1 340 ? 61.22904 -20.36892 -85.31194  1.000 243.90978 ? 334 HIS A O   1 
ATOM   2565 C CB  . HIS A 1 340 ? 60.42385 -23.57614 -84.54258  1.000 234.20338 ? 334 HIS A CB  1 
ATOM   2566 C CG  . HIS A 1 340 ? 60.08623 -24.79528 -85.34419  1.000 237.33678 ? 334 HIS A CG  1 
ATOM   2567 N ND1 . HIS A 1 340 ? 58.82574 -25.02657 -85.85120  1.000 248.47394 ? 334 HIS A ND1 1 
ATOM   2568 C CD2 . HIS A 1 340 ? 60.84587 -25.84658 -85.73307  1.000 235.18216 ? 334 HIS A CD2 1 
ATOM   2569 C CE1 . HIS A 1 340 ? 58.82171 -26.16990 -86.51285  1.000 251.33524 ? 334 HIS A CE1 1 
ATOM   2570 N NE2 . HIS A 1 340 ? 60.03538 -26.68771 -86.45624  1.000 246.03613 ? 334 HIS A NE2 1 
ATOM   2571 N N   . TYR A 1 341 ? 61.83264 -21.15542 -83.29680  1.000 213.25220 ? 335 TYR A N   1 
ATOM   2572 C CA  . TYR A 1 341 ? 61.68053 -19.86147 -82.64225  1.000 232.38230 ? 335 TYR A CA  1 
ATOM   2573 C C   . TYR A 1 341 ? 62.83498 -18.90247 -82.90663  1.000 237.27004 ? 335 TYR A C   1 
ATOM   2574 O O   . TYR A 1 341 ? 62.78448 -17.76065 -82.43596  1.000 233.20791 ? 335 TYR A O   1 
ATOM   2575 C CB  . TYR A 1 341 ? 61.50148 -20.05764 -81.13518  1.000 226.27442 ? 335 TYR A CB  1 
ATOM   2576 C CG  . TYR A 1 341 ? 60.06719 -20.31492 -80.73777  1.000 228.46829 ? 335 TYR A CG  1 
ATOM   2577 C CD1 . TYR A 1 341 ? 59.51214 -21.58341 -80.84315  1.000 226.47433 ? 335 TYR A CD1 1 
ATOM   2578 C CD2 . TYR A 1 341 ? 59.26415 -19.28485 -80.26733  1.000 241.54676 ? 335 TYR A CD2 1 
ATOM   2579 C CE1 . TYR A 1 341 ? 58.19789 -21.81886 -80.48531  1.000 252.61769 ? 335 TYR A CE1 1 
ATOM   2580 C CE2 . TYR A 1 341 ? 57.95171 -19.51037 -79.90660  1.000 244.32271 ? 335 TYR A CE2 1 
ATOM   2581 C CZ  . TYR A 1 341 ? 57.42279 -20.77787 -80.01730  1.000 257.08596 ? 335 TYR A CZ  1 
ATOM   2582 O OH  . TYR A 1 341 ? 56.11354 -21.00123 -79.65836  1.000 268.57635 ? 335 TYR A OH  1 
ATOM   2583 N N   . GLN A 1 342 ? 63.86254 -19.32227 -83.64231  1.000 228.44400 ? 336 GLN A N   1 
ATOM   2584 C CA  . GLN A 1 342 ? 64.96080 -18.43266 -83.99909  1.000 232.58790 ? 336 GLN A CA  1 
ATOM   2585 C C   . GLN A 1 342 ? 64.88670 -17.93300 -85.43380  1.000 236.83698 ? 336 GLN A C   1 
ATOM   2586 O O   . GLN A 1 342 ? 65.29061 -16.79691 -85.70218  1.000 237.79681 ? 336 GLN A O   1 
ATOM   2587 C CB  . GLN A 1 342 ? 66.30929 -19.13251 -83.78745  1.000 219.22697 ? 336 GLN A CB  1 
ATOM   2588 C CG  . GLN A 1 342 ? 66.69372 -19.34521 -82.32990  1.000 221.37856 ? 336 GLN A CG  1 
ATOM   2589 C CD  . GLN A 1 342 ? 67.19372 -18.07872 -81.66321  1.000 235.84931 ? 336 GLN A CD  1 
ATOM   2590 O OE1 . GLN A 1 342 ? 66.40654 -17.24827 -81.20943  1.000 239.03389 ? 336 GLN A OE1 1 
ATOM   2591 N NE2 . GLN A 1 342 ? 68.51168 -17.92494 -81.60088  1.000 221.21761 ? 336 GLN A NE2 1 
ATOM   2592 N N   . ASN A 1 343 ? 64.37664 -18.74083 -86.35372  1.000 239.37854 ? 337 ASN A N   1 
ATOM   2593 C CA  . ASN A 1 343 ? 64.39166 -18.39163 -87.77051  1.000 249.35184 ? 337 ASN A CA  1 
ATOM   2594 C C   . ASN A 1 343 ? 63.01818 -18.44189 -88.42396  1.000 243.93029 ? 337 ASN A C   1 
ATOM   2595 O O   . ASN A 1 343 ? 62.69876 -17.56527 -89.23142  1.000 240.69888 ? 337 ASN A O   1 
ATOM   2596 C CB  . ASN A 1 343 ? 65.35598 -19.32777 -88.52182  1.000 240.74075 ? 337 ASN A CB  1 
ATOM   2597 C CG  . ASN A 1 343 ? 66.72073 -19.41048 -87.86416  1.000 235.13654 ? 337 ASN A CG  1 
ATOM   2598 O OD1 . ASN A 1 343 ? 66.93055 -20.19686 -86.94018  1.000 221.04299 ? 337 ASN A OD1 1 
ATOM   2599 N ND2 . ASN A 1 343 ? 67.65803 -18.60010 -88.34086  1.000 240.17750 ? 337 ASN A ND2 1 
ATOM   2600 N N   . HIS A 1 344 ? 62.20012 -19.43895 -88.09770  1.000 242.60395 ? 338 HIS A N   1 
ATOM   2601 C CA  . HIS A 1 344 ? 60.92995 -19.62740 -88.78443  1.000 234.68331 ? 338 HIS A CA  1 
ATOM   2602 C C   . HIS A 1 344 ? 59.95389 -18.49535 -88.47481  1.000 230.83750 ? 338 HIS A C   1 
ATOM   2603 O O   . HIS A 1 344 ? 59.92609 -17.95141 -87.36582  1.000 227.50177 ? 338 HIS A O   1 
ATOM   2604 C CB  . HIS A 1 344 ? 60.31121 -20.97098 -88.39835  1.000 249.96662 ? 338 HIS A CB  1 
ATOM   2605 C CG  . HIS A 1 344 ? 61.08351 -22.15434 -88.89270  1.000 249.80032 ? 338 HIS A CG  1 
ATOM   2606 N ND1 . HIS A 1 344 ? 62.04639 -22.05687 -89.87399  1.000 240.24765 ? 338 HIS A ND1 1 
ATOM   2607 C CD2 . HIS A 1 344 ? 61.03697 -23.46088 -88.54036  1.000 271.20743 ? 338 HIS A CD2 1 
ATOM   2608 C CE1 . HIS A 1 344 ? 62.55813 -23.25240 -90.10637  1.000 259.71210 ? 338 HIS A CE1 1 
ATOM   2609 N NE2 . HIS A 1 344 ? 61.96286 -24.12205 -89.31022  1.000 283.13159 ? 338 HIS A NE2 1 
ATOM   2610 N N   . GLY A 1 345 ? 59.15045 -18.14723 -89.47270  1.000 237.37460 ? 339 GLY A N   1 
ATOM   2611 C CA  . GLY A 1 345 ? 58.15957 -17.09220 -89.34279  1.000 242.84680 ? 339 GLY A CA  1 
ATOM   2612 C C   . GLY A 1 345 ? 56.76860 -17.67108 -89.20227  1.000 244.07959 ? 339 GLY A C   1 
ATOM   2613 O O   . GLY A 1 345 ? 56.33798 -18.49712 -90.01243  1.000 243.49768 ? 339 GLY A O   1 
ATOM   2614 N N   . PHE A 1 346 ? 56.06256 -17.22552 -88.16509  1.000 244.11701 ? 340 PHE A N   1 
ATOM   2615 C CA  . PHE A 1 346 ? 54.73659 -17.74127 -87.85795  1.000 238.48022 ? 340 PHE A CA  1 
ATOM   2616 C C   . PHE A 1 346 ? 54.04866 -16.77806 -86.90238  1.000 223.07940 ? 340 PHE A C   1 
ATOM   2617 O O   . PHE A 1 346 ? 54.66843 -15.86211 -86.35671  1.000 232.15586 ? 340 PHE A O   1 
ATOM   2618 C CB  . PHE A 1 346 ? 54.81180 -19.15033 -87.25759  1.000 238.76496 ? 340 PHE A CB  1 
ATOM   2619 C CG  . PHE A 1 346 ? 55.73103 -19.25694 -86.07091  1.000 231.37534 ? 340 PHE A CG  1 
ATOM   2620 C CD1 . PHE A 1 346 ? 57.08161 -19.51566 -86.24439  1.000 214.34369 ? 340 PHE A CD1 1 
ATOM   2621 C CD2 . PHE A 1 346 ? 55.24476 -19.10188 -84.78290  1.000 235.69774 ? 340 PHE A CD2 1 
ATOM   2622 C CE1 . PHE A 1 346 ? 57.92990 -19.61287 -85.15737  1.000 212.99053 ? 340 PHE A CE1 1 
ATOM   2623 C CE2 . PHE A 1 346 ? 56.08837 -19.19950 -83.69122  1.000 237.47295 ? 340 PHE A CE2 1 
ATOM   2624 C CZ  . PHE A 1 346 ? 57.43225 -19.45605 -83.87915  1.000 225.35252 ? 340 PHE A CZ  1 
ATOM   2625 N N   . VAL A 1 347 ? 52.75137 -16.99852 -86.70904  1.000 194.44371 ? 341 VAL A N   1 
ATOM   2626 C CA  . VAL A 1 347 ? 51.95301 -16.24851 -85.74899  1.000 222.38488 ? 341 VAL A CA  1 
ATOM   2627 C C   . VAL A 1 347 ? 51.34660 -17.23689 -84.76266  1.000 223.62305 ? 341 VAL A C   1 
ATOM   2628 O O   . VAL A 1 347 ? 50.88401 -18.31498 -85.15284  1.000 198.15291 ? 341 VAL A O   1 
ATOM   2629 C CB  . VAL A 1 347 ? 50.86135 -15.40498 -86.44373  1.000 228.35441 ? 341 VAL A CB  1 
ATOM   2630 C CG1 . VAL A 1 347 ? 49.96774 -16.28014 -87.30996  1.000 225.77921 ? 341 VAL A CG1 1 
ATOM   2631 C CG2 . VAL A 1 347 ? 50.04165 -14.63478 -85.41797  1.000 227.15532 ? 341 VAL A CG2 1 
ATOM   2632 N N   . SER A 1 348 ? 51.37156 -16.87865 -83.48275  1.000 238.59795 ? 342 SER A N   1 
ATOM   2633 C CA  . SER A 1 348 ? 50.90943 -17.75166 -82.41613  1.000 239.74202 ? 342 SER A CA  1 
ATOM   2634 C C   . SER A 1 348 ? 49.68508 -17.15771 -81.73274  1.000 215.93848 ? 342 SER A C   1 
ATOM   2635 O O   . SER A 1 348 ? 49.52983 -15.93611 -81.64478  1.000 208.53309 ? 342 SER A O   1 
ATOM   2636 C CB  . SER A 1 348 ? 52.01383 -17.98932 -81.38210  1.000 239.43175 ? 342 SER A CB  1 
ATOM   2637 O OG  . SER A 1 348 ? 53.15271 -18.58625 -81.97779  1.000 248.54495 ? 342 SER A OG  1 
ATOM   2638 N N   . PHE A 1 349 ? 48.81773 -18.04182 -81.24740  1.000 212.77015 ? 343 PHE A N   1 
ATOM   2639 C CA  . PHE A 1 349 ? 47.60795 -17.64469 -80.54186  1.000 217.37531 ? 343 PHE A CA  1 
ATOM   2640 C C   . PHE A 1 349 ? 47.86754 -17.63902 -79.04114  1.000 222.40984 ? 343 PHE A C   1 
ATOM   2641 O O   . PHE A 1 349 ? 48.31065 -18.64439 -78.47647  1.000 221.96104 ? 343 PHE A O   1 
ATOM   2642 C CB  . PHE A 1 349 ? 46.45457 -18.59094 -80.87990  1.000 232.04528 ? 343 PHE A CB  1 
ATOM   2643 C CG  . PHE A 1 349 ? 45.19727 -18.32159 -80.10201  1.000 234.12192 ? 343 PHE A CG  1 
ATOM   2644 C CD1 . PHE A 1 349 ? 44.32435 -17.32187 -80.49623  1.000 236.37718 ? 343 PHE A CD1 1 
ATOM   2645 C CD2 . PHE A 1 349 ? 44.88307 -19.07518 -78.98217  1.000 245.64193 ? 343 PHE A CD2 1 
ATOM   2646 C CE1 . PHE A 1 349 ? 43.16539 -17.07384 -79.78493  1.000 246.15923 ? 343 PHE A CE1 1 
ATOM   2647 C CE2 . PHE A 1 349 ? 43.72620 -18.83086 -78.26669  1.000 255.51524 ? 343 PHE A CE2 1 
ATOM   2648 C CZ  . PHE A 1 349 ? 42.86644 -17.82881 -78.66926  1.000 247.46504 ? 343 PHE A CZ  1 
ATOM   2649 N N   . ASN A 1 350 ? 47.58940 -16.50633 -78.40106  1.000 226.92869 ? 344 ASN A N   1 
ATOM   2650 C CA  . ASN A 1 350 ? 47.77321 -16.34747 -76.96543  1.000 237.08642 ? 344 ASN A CA  1 
ATOM   2651 C C   . ASN A 1 350 ? 46.48848 -15.79833 -76.36676  1.000 238.19482 ? 344 ASN A C   1 
ATOM   2652 O O   . ASN A 1 350 ? 45.94922 -14.80147 -76.85781  1.000 226.52604 ? 344 ASN A O   1 
ATOM   2653 C CB  . ASN A 1 350 ? 48.94876 -15.41432 -76.65649  1.000 235.92161 ? 344 ASN A CB  1 
ATOM   2654 C CG  . ASN A 1 350 ? 50.22726 -15.83559 -77.35495  1.000 229.58376 ? 344 ASN A CG  1 
ATOM   2655 O OD1 . ASN A 1 350 ? 51.07110 -16.51747 -76.77356  1.000 246.12738 ? 344 ASN A OD1 1 
ATOM   2656 N ND2 . ASN A 1 350 ? 50.37544 -15.43113 -78.61118  1.000 218.98164 ? 344 ASN A ND2 1 
ATOM   2657 N N   . SER A 1 351 ? 45.99941 -16.44742 -75.31276  1.000 238.85354 ? 345 SER A N   1 
ATOM   2658 C CA  . SER A 1 351 ? 44.75488 -16.03442 -74.68303  1.000 231.22823 ? 345 SER A CA  1 
ATOM   2659 C C   . SER A 1 351 ? 44.81509 -16.32491 -73.19165  1.000 232.16170 ? 345 SER A C   1 
ATOM   2660 O O   . SER A 1 351 ? 45.39365 -17.32917 -72.76847  1.000 217.83568 ? 345 SER A O   1 
ATOM   2661 C CB  . SER A 1 351 ? 43.54781 -16.74275 -75.30891  1.000 239.04680 ? 345 SER A CB  1 
ATOM   2662 O OG  . SER A 1 351 ? 42.33757 -16.31523 -74.70759  1.000 245.71842 ? 345 SER A OG  1 
ATOM   2663 N N   . ILE A 1 352 ? 44.21245 -15.43555 -72.40257  1.000 245.56710 ? 346 ILE A N   1 
ATOM   2664 C CA  . ILE A 1 352 ? 44.10051 -15.59775 -70.96096  1.000 254.48574 ? 346 ILE A CA  1 
ATOM   2665 C C   . ILE A 1 352 ? 42.64890 -15.70299 -70.51221  1.000 258.69439 ? 346 ILE A C   1 
ATOM   2666 O O   . ILE A 1 352 ? 42.36862 -15.64702 -69.31432  1.000 256.11413 ? 346 ILE A O   1 
ATOM   2667 C CB  . ILE A 1 352 ? 44.82131 -14.45900 -70.21249  1.000 263.57909 ? 346 ILE A CB  1 
ATOM   2668 C CG1 . ILE A 1 352 ? 44.21657 -13.10514 -70.59035  1.000 285.06486 ? 346 ILE A CG1 1 
ATOM   2669 C CG2 . ILE A 1 352 ? 46.31300 -14.48690 -70.51034  1.000 237.73678 ? 346 ILE A CG2 1 
ATOM   2670 C CD1 . ILE A 1 352 ? 44.84892 -11.93131 -69.87380  1.000 295.20107 ? 346 ILE A CD1 1 
ATOM   2671 N N   . ASP A 1 353 ? 41.71837 -15.85039 -71.45323  1.000 254.25373 ? 347 ASP A N   1 
ATOM   2672 C CA  . ASP A 1 353 ? 40.30713 -15.99001 -71.11662  1.000 257.91993 ? 347 ASP A CA  1 
ATOM   2673 C C   . ASP A 1 353 ? 40.08238 -17.30518 -70.37975  1.000 265.03798 ? 347 ASP A C   1 
ATOM   2674 O O   . ASP A 1 353 ? 40.36445 -18.38080 -70.91778  1.000 264.72083 ? 347 ASP A O   1 
ATOM   2675 C CB  . ASP A 1 353 ? 39.45734 -15.92535 -72.38370  1.000 239.08302 ? 347 ASP A CB  1 
ATOM   2676 C CG  . ASP A 1 353 ? 37.97223 -16.02625 -72.09772  1.000 249.40971 ? 347 ASP A CG  1 
ATOM   2677 O OD1 . ASP A 1 353 ? 37.41230 -15.07800 -71.50879  1.000 244.76874 ? 347 ASP A OD1 1 
ATOM   2678 O OD2 . ASP A 1 353 ? 37.36338 -17.05239 -72.46637  1.000 252.28165 ? 347 ASP A OD2 1 
ATOM   2679 N N   . LYS A 1 354 ? 39.57379 -17.21594 -69.14718  1.000 267.87738 ? 348 LYS A N   1 
ATOM   2680 C CA  . LYS A 1 354 ? 39.40870 -18.40729 -68.31829  1.000 270.00320 ? 348 LYS A CA  1 
ATOM   2681 C C   . LYS A 1 354 ? 38.48068 -19.42399 -68.97259  1.000 280.51337 ? 348 LYS A C   1 
ATOM   2682 O O   . LYS A 1 354 ? 38.72899 -20.63357 -68.90460  1.000 268.32351 ? 348 LYS A O   1 
ATOM   2683 C CB  . LYS A 1 354 ? 38.88417 -18.01522 -66.93671  1.000 286.87046 ? 348 LYS A CB  1 
ATOM   2684 C CG  . LYS A 1 354 ? 39.94131 -17.44789 -66.00247  1.000 267.92799 ? 348 LYS A CG  1 
ATOM   2685 C CD  . LYS A 1 354 ? 40.94876 -18.51427 -65.60297  1.000 248.61776 ? 348 LYS A CD  1 
ATOM   2686 C CE  . LYS A 1 354 ? 41.91077 -17.99916 -64.54545  1.000 248.78378 ? 348 LYS A CE  1 
ATOM   2687 N NZ  . LYS A 1 354 ? 42.84070 -19.06428 -64.07731  1.000 233.19665 ? 348 LYS A NZ  1 
ATOM   2688 N N   . GLN A 1 355 ? 37.40575 -18.95533 -69.61087  1.000 289.43666 ? 349 GLN A N   1 
ATOM   2689 C CA  . GLN A 1 355 ? 36.47795 -19.87714 -70.25930  1.000 277.83567 ? 349 GLN A CA  1 
ATOM   2690 C C   . GLN A 1 355 ? 37.11132 -20.53690 -71.47774  1.000 273.27437 ? 349 GLN A C   1 
ATOM   2691 O O   . GLN A 1 355 ? 36.84071 -21.70850 -71.76656  1.000 273.79609 ? 349 GLN A O   1 
ATOM   2692 C CB  . GLN A 1 355 ? 35.19504 -19.14534 -70.65055  1.000 263.05433 ? 349 GLN A CB  1 
ATOM   2693 C CG  . GLN A 1 355 ? 34.34707 -18.71272 -69.46789  1.000 277.43953 ? 349 GLN A CG  1 
ATOM   2694 C CD  . GLN A 1 355 ? 33.07649 -18.00397 -69.89074  1.000 324.92106 ? 349 GLN A CD  1 
ATOM   2695 O OE1 . GLN A 1 355 ? 32.96550 -17.52382 -71.01890  1.000 351.15428 ? 349 GLN A OE1 1 
ATOM   2696 N NE2 . GLN A 1 355 ? 32.10678 -17.93814 -68.98566  1.000 344.70403 ? 349 GLN A NE2 1 
ATOM   2697 N N   . LEU A 1 356 ? 37.95503 -19.80322 -72.20559  1.000 272.74817 ? 350 LEU A N   1 
ATOM   2698 C CA  . LEU A 1 356 ? 38.62342 -20.38038 -73.36544  1.000 261.30779 ? 350 LEU A CA  1 
ATOM   2699 C C   . LEU A 1 356 ? 39.76853 -21.29976 -72.95999  1.000 259.18121 ? 350 LEU A C   1 
ATOM   2700 O O   . LEU A 1 356 ? 40.01038 -22.31199 -73.62722  1.000 256.84758 ? 350 LEU A O   1 
ATOM   2701 C CB  . LEU A 1 356 ? 39.13176 -19.26925 -74.28609  1.000 258.68233 ? 350 LEU A CB  1 
ATOM   2702 C CG  . LEU A 1 356 ? 39.68003 -19.70417 -75.64654  1.000 266.44195 ? 350 LEU A CG  1 
ATOM   2703 C CD1 . LEU A 1 356 ? 38.64096 -20.50862 -76.41466  1.000 250.04933 ? 350 LEU A CD1 1 
ATOM   2704 C CD2 . LEU A 1 356 ? 40.12564 -18.49479 -76.45181  1.000 258.91419 ? 350 LEU A CD2 1 
ATOM   2705 N N   . VAL A 1 357 ? 40.47697 -20.97137 -71.87659  1.000 257.66725 ? 351 VAL A N   1 
ATOM   2706 C CA  . VAL A 1 357 ? 41.52489 -21.85921 -71.38343  1.000 251.58684 ? 351 VAL A CA  1 
ATOM   2707 C C   . VAL A 1 357 ? 40.91785 -23.12399 -70.78801  1.000 254.01345 ? 351 VAL A C   1 
ATOM   2708 O O   . VAL A 1 357 ? 41.49831 -24.21158 -70.89940  1.000 254.09233 ? 351 VAL A O   1 
ATOM   2709 C CB  . VAL A 1 357 ? 42.41777 -21.11970 -70.36745  1.000 246.27775 ? 351 VAL A CB  1 
ATOM   2710 C CG1 . VAL A 1 357 ? 43.45101 -22.06198 -69.76823  1.000 255.76998 ? 351 VAL A CG1 1 
ATOM   2711 C CG2 . VAL A 1 357 ? 43.10846 -19.93854 -71.03131  1.000 232.60240 ? 351 VAL A CG2 1 
ATOM   2712 N N   . SER A 1 358 ? 39.74158 -23.01287 -70.16304  1.000 250.87981 ? 352 SER A N   1 
ATOM   2713 C CA  . SER A 1 358 ? 39.08551 -24.19177 -69.60449  1.000 250.48929 ? 352 SER A CA  1 
ATOM   2714 C C   . SER A 1 358 ? 38.72628 -25.19232 -70.69608  1.000 253.64097 ? 352 SER A C   1 
ATOM   2715 O O   . SER A 1 358 ? 38.87004 -26.40619 -70.50772  1.000 240.35711 ? 352 SER A O   1 
ATOM   2716 C CB  . SER A 1 358 ? 37.83838 -23.78025 -68.82132  1.000 264.09783 ? 352 SER A CB  1 
ATOM   2717 O OG  . SER A 1 358 ? 36.88683 -23.15455 -69.66456  1.000 269.04356 ? 352 SER A OG  1 
ATOM   2718 N N   . GLU A 1 359 ? 38.25424 -24.70272 -71.84565  1.000 258.82790 ? 353 GLU A N   1 
ATOM   2719 C CA  . GLU A 1 359 ? 37.99558 -25.59357 -72.97153  1.000 260.77980 ? 353 GLU A CA  1 
ATOM   2720 C C   . GLU A 1 359 ? 39.28725 -26.17970 -73.52602  1.000 255.80781 ? 353 GLU A C   1 
ATOM   2721 O O   . GLU A 1 359 ? 39.28994 -27.31272 -74.02088  1.000 248.86979 ? 353 GLU A O   1 
ATOM   2722 C CB  . GLU A 1 359 ? 37.23263 -24.85092 -74.06977  1.000 263.90784 ? 353 GLU A CB  1 
ATOM   2723 C CG  . GLU A 1 359 ? 35.78754 -24.51909 -73.72165  1.000 267.58394 ? 353 GLU A CG  1 
ATOM   2724 C CD  . GLU A 1 359 ? 34.87297 -25.73023 -73.78140  1.000 273.25455 ? 353 GLU A CD  1 
ATOM   2725 O OE1 . GLU A 1 359 ? 35.31048 -26.78879 -74.28063  1.000 268.44798 ? 353 GLU A OE1 1 
ATOM   2726 O OE2 . GLU A 1 359 ? 33.71286 -25.62220 -73.33059  1.000 285.28798 ? 353 GLU A OE2 1 
ATOM   2727 N N   . ALA A 1 360 ? 40.38900 -25.42821 -73.45278  1.000 253.75219 ? 354 ALA A N   1 
ATOM   2728 C CA  . ALA A 1 360 ? 41.67650 -25.95581 -73.89211  1.000 250.01172 ? 354 ALA A CA  1 
ATOM   2729 C C   . ALA A 1 360 ? 42.21077 -26.98992 -72.90990  1.000 244.34345 ? 354 ALA A C   1 
ATOM   2730 O O   . ALA A 1 360 ? 42.81572 -27.98853 -73.31795  1.000 227.57078 ? 354 ALA A O   1 
ATOM   2731 C CB  . ALA A 1 360 ? 42.67774 -24.81600 -74.07081  1.000 241.20540 ? 354 ALA A CB  1 
ATOM   2732 N N   . LYS A 1 361 ? 42.00693 -26.76151 -71.60982  1.000 245.80248 ? 355 LYS A N   1 
ATOM   2733 C CA  . LYS A 1 361 ? 42.37164 -27.76510 -70.61632  1.000 241.06436 ? 355 LYS A CA  1 
ATOM   2734 C C   . LYS A 1 361 ? 41.56421 -29.04226 -70.80188  1.000 249.10140 ? 355 LYS A C   1 
ATOM   2735 O O   . LYS A 1 361 ? 42.07782 -30.14248 -70.56875  1.000 249.84715 ? 355 LYS A O   1 
ATOM   2736 C CB  . LYS A 1 361 ? 42.16835 -27.20351 -69.20865  1.000 244.74196 ? 355 LYS A CB  1 
ATOM   2737 C CG  . LYS A 1 361 ? 42.64239 -28.11428 -68.08770  1.000 243.48913 ? 355 LYS A CG  1 
ATOM   2738 C CD  . LYS A 1 361 ? 44.15519 -28.08831 -67.94897  1.000 246.35902 ? 355 LYS A CD  1 
ATOM   2739 C CE  . LYS A 1 361 ? 44.60211 -28.86350 -66.72013  1.000 250.51276 ? 355 LYS A CE  1 
ATOM   2740 N NZ  . LYS A 1 361 ? 46.04102 -28.64208 -66.41145  1.000 240.07417 ? 355 LYS A NZ  1 
ATOM   2741 N N   . LYS A 1 362 ? 40.30299 -28.91496 -71.22437  1.000 252.42414 ? 356 LYS A N   1 
ATOM   2742 C CA  . LYS A 1 362 ? 39.48639 -30.08920 -71.51229  1.000 248.33385 ? 356 LYS A CA  1 
ATOM   2743 C C   . LYS A 1 362 ? 40.06154 -30.90011 -72.66604  1.000 244.27482 ? 356 LYS A C   1 
ATOM   2744 O O   . LYS A 1 362 ? 39.94487 -32.13109 -72.68007  1.000 238.97812 ? 356 LYS A O   1 
ATOM   2745 C CB  . LYS A 1 362 ? 38.05147 -29.65761 -71.82337  1.000 243.26318 ? 356 LYS A CB  1 
ATOM   2746 C CG  . LYS A 1 362 ? 37.10523 -30.79290 -72.18262  1.000 242.88807 ? 356 LYS A CG  1 
ATOM   2747 C CD  . LYS A 1 362 ? 35.72673 -30.26078 -72.54480  1.000 232.34341 ? 356 LYS A CD  1 
ATOM   2748 C CE  . LYS A 1 362 ? 34.77844 -31.38463 -72.92931  1.000 238.56358 ? 356 LYS A CE  1 
ATOM   2749 N NZ  . LYS A 1 362 ? 33.42669 -30.86949 -73.28416  1.000 254.76764 ? 356 LYS A NZ  1 
ATOM   2750 N N   . ILE A 1 363 ? 40.69085 -30.23283 -73.63512  1.000 243.12348 ? 357 ILE A N   1 
ATOM   2751 C CA  . ILE A 1 363 ? 41.27034 -30.94271 -74.77053  1.000 249.01369 ? 357 ILE A CA  1 
ATOM   2752 C C   . ILE A 1 363 ? 42.55456 -31.65424 -74.36025  1.000 236.84784 ? 357 ILE A C   1 
ATOM   2753 O O   . ILE A 1 363 ? 42.82025 -32.78180 -74.79479  1.000 236.29088 ? 357 ILE A O   1 
ATOM   2754 C CB  . ILE A 1 363 ? 41.50419 -29.96978 -75.94125  1.000 255.57474 ? 357 ILE A CB  1 
ATOM   2755 C CG1 . ILE A 1 363 ? 40.17442 -29.37955 -76.41755  1.000 269.66960 ? 357 ILE A CG1 1 
ATOM   2756 C CG2 . ILE A 1 363 ? 42.22215 -30.66555 -77.08887  1.000 242.85109 ? 357 ILE A CG2 1 
ATOM   2757 C CD1 . ILE A 1 363 ? 39.18144 -30.41525 -76.90272  1.000 267.63675 ? 357 ILE A CD1 1 
ATOM   2758 N N   . PHE A 1 364 ? 43.36798 -31.01636 -73.51321  1.000 223.54878 ? 358 PHE A N   1 
ATOM   2759 C CA  . PHE A 1 364 ? 44.62260 -31.63570 -73.09543  1.000 227.51004 ? 358 PHE A CA  1 
ATOM   2760 C C   . PHE A 1 364 ? 44.37364 -32.86597 -72.23224  1.000 217.21799 ? 358 PHE A C   1 
ATOM   2761 O O   . PHE A 1 364 ? 45.08214 -33.87155 -72.35811  1.000 212.07367 ? 358 PHE A O   1 
ATOM   2762 C CB  . PHE A 1 364 ? 45.49326 -30.62662 -72.34674  1.000 233.27856 ? 358 PHE A CB  1 
ATOM   2763 C CG  . PHE A 1 364 ? 46.84634 -31.16293 -71.96515  1.000 245.99354 ? 358 PHE A CG  1 
ATOM   2764 C CD1 . PHE A 1 364 ? 47.90026 -31.12006 -72.86334  1.000 243.52139 ? 358 PHE A CD1 1 
ATOM   2765 C CD2 . PHE A 1 364 ? 47.06349 -31.71392 -70.71174  1.000 233.82841 ? 358 PHE A CD2 1 
ATOM   2766 C CE1 . PHE A 1 364 ? 49.14510 -31.61428 -72.51928  1.000 215.11777 ? 358 PHE A CE1 1 
ATOM   2767 C CE2 . PHE A 1 364 ? 48.30605 -32.21111 -70.36244  1.000 232.01190 ? 358 PHE A CE2 1 
ATOM   2768 C CZ  . PHE A 1 364 ? 49.34807 -32.15988 -71.26736  1.000 217.05361 ? 358 PHE A CZ  1 
ATOM   2769 N N   . GLU A 1 365 ? 43.37915 -32.80377 -71.34334  1.000 218.61597 ? 359 GLU A N   1 
ATOM   2770 C CA  . GLU A 1 365 ? 43.04629 -33.97092 -70.53413  1.000 221.31680 ? 359 GLU A CA  1 
ATOM   2771 C C   . GLU A 1 365 ? 42.53483 -35.11712 -71.39608  1.000 220.57873 ? 359 GLU A C   1 
ATOM   2772 O O   . GLU A 1 365 ? 42.74432 -36.28827 -71.05980  1.000 201.40402 ? 359 GLU A O   1 
ATOM   2773 C CB  . GLU A 1 365 ? 42.01113 -33.59834 -69.47147  1.000 233.99512 ? 359 GLU A CB  1 
ATOM   2774 C CG  . GLU A 1 365 ? 42.48730 -32.55700 -68.46793  1.000 229.76878 ? 359 GLU A CG  1 
ATOM   2775 C CD  . GLU A 1 365 ? 43.54403 -33.09065 -67.51855  1.000 246.75118 ? 359 GLU A CD  1 
ATOM   2776 O OE1 . GLU A 1 365 ? 43.69544 -34.32697 -67.42190  1.000 256.37899 ? 359 GLU A OE1 1 
ATOM   2777 O OE2 . GLU A 1 365 ? 44.22327 -32.27092 -66.86549  1.000 260.00409 ? 359 GLU A OE2 1 
ATOM   2778 N N   . ARG A 1 366 ? 41.86818 -34.80150 -72.50880  1.000 225.30069 ? 360 ARG A N   1 
ATOM   2779 C CA  . ARG A 1 366 ? 41.40353 -35.84113 -73.42168  1.000 238.42994 ? 360 ARG A CA  1 
ATOM   2780 C C   . ARG A 1 366 ? 42.57673 -36.53577 -74.10177  1.000 228.58679 ? 360 ARG A C   1 
ATOM   2781 O O   . ARG A 1 366 ? 42.61632 -37.76856 -74.19218  1.000 225.73901 ? 360 ARG A O   1 
ATOM   2782 C CB  . ARG A 1 366 ? 40.45980 -35.23708 -74.46277  1.000 245.72057 ? 360 ARG A CB  1 
ATOM   2783 C CG  . ARG A 1 366 ? 39.95597 -36.22543 -75.50391  1.000 240.40611 ? 360 ARG A CG  1 
ATOM   2784 C CD  . ARG A 1 366 ? 39.37935 -35.50120 -76.71112  1.000 220.86613 ? 360 ARG A CD  1 
ATOM   2785 N NE  . ARG A 1 366 ? 40.39375 -34.71054 -77.39872  1.000 243.58992 ? 360 ARG A NE  1 
ATOM   2786 C CZ  . ARG A 1 366 ? 40.15930 -33.93665 -78.44976  1.000 255.00868 ? 360 ARG A CZ  1 
ATOM   2787 N NH1 . ARG A 1 366 ? 38.94587 -33.81644 -78.96298  1.000 260.18029 ? 360 ARG A NH1 1 
ATOM   2788 N NH2 . ARG A 1 366 ? 41.16798 -33.26584 -78.99943  1.000 244.68530 ? 360 ARG A NH2 1 
ATOM   2789 N N   . ASP A 1 367 ? 43.54464 -35.75669 -74.58684  1.000 228.50996 ? 361 ASP A N   1 
ATOM   2790 C CA  . ASP A 1 367 ? 44.70060 -36.31940 -75.27147  1.000 235.62803 ? 361 ASP A CA  1 
ATOM   2791 C C   . ASP A 1 367 ? 45.69907 -36.95823 -74.31529  1.000 238.31391 ? 361 ASP A C   1 
ATOM   2792 O O   . ASP A 1 367 ? 46.49914 -37.79587 -74.74628  1.000 230.93957 ? 361 ASP A O   1 
ATOM   2793 C CB  . ASP A 1 367 ? 45.39904 -35.23486 -76.09600  1.000 232.04401 ? 361 ASP A CB  1 
ATOM   2794 C CG  . ASP A 1 367 ? 44.46630 -34.56381 -77.08747  1.000 225.28624 ? 361 ASP A CG  1 
ATOM   2795 O OD1 . ASP A 1 367 ? 43.29125 -34.97791 -77.17597  1.000 233.07703 ? 361 ASP A OD1 1 
ATOM   2796 O OD2 . ASP A 1 367 ? 44.90765 -33.62037 -77.77715  1.000 225.51236 ? 361 ASP A OD2 1 
ATOM   2797 N N   . TRP A 1 368 ? 45.67077 -36.58743 -73.03302  1.000 241.12630 ? 362 TRP A N   1 
ATOM   2798 C CA  . TRP A 1 368 ? 46.62741 -37.14680 -72.08338  1.000 243.65333 ? 362 TRP A CA  1 
ATOM   2799 C C   . TRP A 1 368 ? 46.28903 -38.59149 -71.73936  1.000 233.65587 ? 362 TRP A C   1 
ATOM   2800 O O   . TRP A 1 368 ? 47.18574 -39.43587 -71.62736  1.000 227.51602 ? 362 TRP A O   1 
ATOM   2801 C CB  . TRP A 1 368 ? 46.67226 -36.29237 -70.81727  1.000 243.78157 ? 362 TRP A CB  1 
ATOM   2802 C CG  . TRP A 1 368 ? 47.61697 -36.81769 -69.78387  1.000 253.23179 ? 362 TRP A CG  1 
ATOM   2803 C CD1 . TRP A 1 368 ? 47.29424 -37.50036 -68.64681  1.000 246.62856 ? 362 TRP A CD1 1 
ATOM   2804 C CD2 . TRP A 1 368 ? 49.04483 -36.71369 -69.79818  1.000 242.05064 ? 362 TRP A CD2 1 
ATOM   2805 N NE1 . TRP A 1 368 ? 48.43329 -37.82239 -67.94916  1.000 247.98077 ? 362 TRP A NE1 1 
ATOM   2806 C CE2 . TRP A 1 368 ? 49.52140 -37.35089 -68.63566  1.000 246.60219 ? 362 TRP A CE2 1 
ATOM   2807 C CE3 . TRP A 1 368 ? 49.96656 -36.14113 -70.68021  1.000 211.18658 ? 362 TRP A CE3 1 
ATOM   2808 C CZ2 . TRP A 1 368 ? 50.87757 -37.43174 -68.33303  1.000 247.39788 ? 362 TRP A CZ2 1 
ATOM   2809 C CZ3 . TRP A 1 368 ? 51.31205 -36.22210 -70.37759  1.000 211.26802 ? 362 TRP A CZ3 1 
ATOM   2810 C CH2 . TRP A 1 368 ? 51.75523 -36.86223 -69.21405  1.000 237.93281 ? 362 TRP A CH2 1 
ATOM   2811 N N   . VAL A 1 369 ? 45.00298 -38.89452 -71.56581  1.000 227.38950 ? 363 VAL A N   1 
ATOM   2812 C CA  . VAL A 1 369 ? 44.56146 -40.23739 -71.21338  1.000 238.26458 ? 363 VAL A CA  1 
ATOM   2813 C C   . VAL A 1 369 ? 44.07446 -41.01473 -72.43149  1.000 234.51746 ? 363 VAL A C   1 
ATOM   2814 O O   . VAL A 1 369 ? 43.47527 -42.08382 -72.28048  1.000 249.33188 ? 363 VAL A O   1 
ATOM   2815 C CB  . VAL A 1 369 ? 43.47671 -40.19080 -70.12635  1.000 244.98395 ? 363 VAL A CB  1 
ATOM   2816 C CG1 . VAL A 1 369 ? 44.00148 -39.48059 -68.88748  1.000 246.12828 ? 363 VAL A CG1 1 
ATOM   2817 C CG2 . VAL A 1 369 ? 42.22907 -39.50063 -70.65456  1.000 251.02007 ? 363 VAL A CG2 1 
ATOM   2818 N N   . SER A 1 370 ? 44.31765 -40.50411 -73.63551  1.000 209.28665 ? 364 SER A N   1 
ATOM   2819 C CA  . SER A 1 370 ? 43.88516 -41.19211 -74.84042  1.000 208.01254 ? 364 SER A CA  1 
ATOM   2820 C C   . SER A 1 370 ? 44.68032 -42.47964 -75.03961  1.000 221.11582 ? 364 SER A C   1 
ATOM   2821 O O   . SER A 1 370 ? 45.77508 -42.66010 -74.49821  1.000 224.37739 ? 364 SER A O   1 
ATOM   2822 C CB  . SER A 1 370 ? 44.03927 -40.28626 -76.06199  1.000 208.06853 ? 364 SER A CB  1 
ATOM   2823 O OG  . SER A 1 370 ? 43.63255 -40.95331 -77.24418  1.000 215.70433 ? 364 SER A OG  1 
ATOM   2824 N N   . SER A 1 371 ? 44.10583 -43.38685 -75.83358  1.000 221.23787 ? 365 SER A N   1 
ATOM   2825 C CA  . SER A 1 371 ? 44.76613 -44.66025 -76.09954  1.000 228.67103 ? 365 SER A CA  1 
ATOM   2826 C C   . SER A 1 371 ? 46.04097 -44.47474 -76.91135  1.000 226.89600 ? 365 SER A C   1 
ATOM   2827 O O   . SER A 1 371 ? 46.96790 -45.28538 -76.80045  1.000 242.33944 ? 365 SER A O   1 
ATOM   2828 C CB  . SER A 1 371 ? 43.80976 -45.60715 -76.82397  1.000 228.89620 ? 365 SER A CB  1 
ATOM   2829 O OG  . SER A 1 371 ? 43.41559 -45.07287 -78.07573  1.000 221.21383 ? 365 SER A OG  1 
ATOM   2830 N N   . HIS A 1 372 ? 46.10861 -43.42122 -77.72717  1.000 215.70792 ? 366 HIS A N   1 
ATOM   2831 C CA  . HIS A 1 372 ? 47.30577 -43.15217 -78.51238  1.000 219.26049 ? 366 HIS A CA  1 
ATOM   2832 C C   . HIS A 1 372 ? 48.45652 -42.62450 -77.66758  1.000 219.54249 ? 366 HIS A C   1 
ATOM   2833 O O   . HIS A 1 372 ? 49.59213 -42.59226 -78.15282  1.000 210.97485 ? 366 HIS A O   1 
ATOM   2834 C CB  . HIS A 1 372 ? 46.98835 -42.15378 -79.62706  1.000 211.72206 ? 366 HIS A CB  1 
ATOM   2835 C CG  . HIS A 1 372 ? 45.77476 -42.50863 -80.42804  1.000 229.48600 ? 366 HIS A CG  1 
ATOM   2836 N ND1 . HIS A 1 372 ? 45.74974 -43.56381 -81.31431  1.000 247.87075 ? 366 HIS A ND1 1 
ATOM   2837 C CD2 . HIS A 1 372 ? 44.54396 -41.94639 -80.47789  1.000 213.70887 ? 366 HIS A CD2 1 
ATOM   2838 C CE1 . HIS A 1 372 ? 44.55545 -43.63753 -81.87430  1.000 226.95891 ? 366 HIS A CE1 1 
ATOM   2839 N NE2 . HIS A 1 372 ? 43.80502 -42.66730 -81.38424  1.000 213.61007 ? 366 HIS A NE2 1 
ATOM   2840 N N   . SER A 1 373 ? 48.19610 -42.21838 -76.42647  1.000 228.14227 ? 367 SER A N   1 
ATOM   2841 C CA  . SER A 1 373 ? 49.21572 -41.64544 -75.54867  1.000 234.39312 ? 367 SER A CA  1 
ATOM   2842 C C   . SER A 1 373 ? 49.69783 -42.73485 -74.59570  1.000 249.96768 ? 367 SER A C   1 
ATOM   2843 O O   . SER A 1 373 ? 49.17433 -42.89975 -73.49293  1.000 236.09048 ? 367 SER A O   1 
ATOM   2844 C CB  . SER A 1 373 ? 48.66390 -40.44227 -74.79243  1.000 215.73080 ? 367 SER A CB  1 
ATOM   2845 O OG  . SER A 1 373 ? 48.20020 -39.44602 -75.68620  1.000 202.08679 ? 367 SER A OG  1 
ATOM   2846 N N   . LYS A 1 374 ? 50.70671 -43.48482 -75.02993  1.000 253.87681 ? 368 LYS A N   1 
ATOM   2847 C CA  . LYS A 1 374 ? 51.33170 -44.47616 -74.16910  1.000 262.83780 ? 368 LYS A CA  1 
ATOM   2848 C C   . LYS A 1 374 ? 52.33787 -43.81087 -73.23866  1.000 254.86278 ? 368 LYS A C   1 
ATOM   2849 O O   . LYS A 1 374 ? 52.94181 -42.78628 -73.56959  1.000 240.06916 ? 368 LYS A O   1 
ATOM   2850 C CB  . LYS A 1 374 ? 52.02434 -45.56041 -74.99649  1.000 252.78495 ? 368 LYS A CB  1 
ATOM   2851 C CG  . LYS A 1 374 ? 51.07787 -46.57940 -75.61303  1.000 265.69376 ? 368 LYS A CG  1 
ATOM   2852 C CD  . LYS A 1 374 ? 51.84327 -47.75632 -76.20171  1.000 264.86495 ? 368 LYS A CD  1 
ATOM   2853 C CE  . LYS A 1 374 ? 50.90023 -48.84735 -76.68622  1.000 250.59397 ? 368 LYS A CE  1 
ATOM   2854 N NZ  . LYS A 1 374 ? 51.63955 -50.03594 -77.19619  1.000 250.83843 ? 368 LYS A NZ  1 
ATOM   2855 N N   . SER A 1 375 ? 52.51077 -44.40604 -72.06206  1.000 261.44753 ? 369 SER A N   1 
ATOM   2856 C CA  . SER A 1 375 ? 53.42082 -43.85586 -71.07123  1.000 244.74666 ? 369 SER A CA  1 
ATOM   2857 C C   . SER A 1 375 ? 54.86607 -43.95400 -71.55290  1.000 254.83789 ? 369 SER A C   1 
ATOM   2858 O O   . SER A 1 375 ? 55.22062 -44.79770 -72.38099  1.000 242.73811 ? 369 SER A O   1 
ATOM   2859 C CB  . SER A 1 375 ? 53.25979 -44.58154 -69.73488  1.000 254.22542 ? 369 SER A CB  1 
ATOM   2860 O OG  . SER A 1 375 ? 54.10238 -44.02027 -68.74338  1.000 286.59374 ? 369 SER A OG  1 
ATOM   2861 N N   . LEU A 1 376 ? 55.70401 -43.06785 -71.01912  1.000 263.42506 ? 370 LEU A N   1 
ATOM   2862 C CA  . LEU A 1 376 ? 57.11372 -43.03585 -71.38806  1.000 259.19118 ? 370 LEU A CA  1 
ATOM   2863 C C   . LEU A 1 376 ? 57.82046 -44.27643 -70.85535  1.000 263.32150 ? 370 LEU A C   1 
ATOM   2864 O O   . LEU A 1 376 ? 57.90270 -44.47958 -69.63935  1.000 272.63546 ? 370 LEU A O   1 
ATOM   2865 C CB  . LEU A 1 376 ? 57.77179 -41.77022 -70.84498  1.000 251.48026 ? 370 LEU A CB  1 
ATOM   2866 C CG  . LEU A 1 376 ? 59.26639 -41.60888 -71.12583  1.000 245.94910 ? 370 LEU A CG  1 
ATOM   2867 C CD1 . LEU A 1 376 ? 59.51247 -41.46453 -72.61683  1.000 235.91486 ? 370 LEU A CD1 1 
ATOM   2868 C CD2 . LEU A 1 376 ? 59.83337 -40.42047 -70.36538  1.000 243.81851 ? 370 LEU A CD2 1 
ATOM   2869 N N   . LYS A 1 377 ? 58.32960 -45.10471 -71.76342  1.000 248.02874 ? 371 LYS A N   1 
ATOM   2870 C CA  . LYS A 1 377 ? 59.05706 -46.31571 -71.41021  1.000 265.52545 ? 371 LYS A CA  1 
ATOM   2871 C C   . LYS A 1 377 ? 60.42539 -46.28836 -72.07453  1.000 272.14547 ? 371 LYS A C   1 
ATOM   2872 O O   . LYS A 1 377 ? 60.52913 -46.04542 -73.28165  1.000 259.63466 ? 371 LYS A O   1 
ATOM   2873 C CB  . LYS A 1 377 ? 58.28426 -47.57052 -71.82991  1.000 261.72390 ? 371 LYS A CB  1 
ATOM   2874 C CG  . LYS A 1 377 ? 56.99677 -47.80198 -71.05181  1.000 253.40915 ? 371 LYS A CG  1 
ATOM   2875 C CD  . LYS A 1 377 ? 56.35796 -49.13232 -71.42442  1.000 254.05042 ? 371 LYS A CD  1 
ATOM   2876 C CE  . LYS A 1 377 ? 55.11646 -49.40806 -70.58937  1.000 269.00292 ? 371 LYS A CE  1 
ATOM   2877 N NZ  . LYS A 1 377 ? 54.50167 -50.72400 -70.92227  1.000 249.97945 ? 371 LYS A NZ  1 
ATOM   2878 N N   . ILE A 1 378 ? 61.46836 -46.52745 -71.28470  1.000 285.02005 ? 372 ILE A N   1 
ATOM   2879 C CA  . ILE A 1 378 ? 62.83490 -46.55154 -71.79418  1.000 277.85064 ? 372 ILE A CA  1 
ATOM   2880 C C   . ILE A 1 378 ? 63.54955 -47.81087 -71.31585  1.000 296.16123 ? 372 ILE A C   1 
ATOM   2881 O O   . ILE A 1 378 ? 63.45346 -48.18820 -70.14787  1.000 300.83100 ? 372 ILE A O   1 
ATOM   2882 C CB  . ILE A 1 378 ? 63.61106 -45.29030 -71.37212  1.000 252.31180 ? 372 ILE A CB  1 
ATOM   2883 C CG1 . ILE A 1 378 ? 62.95737 -44.03854 -71.95924  1.000 235.57472 ? 372 ILE A CG1 1 
ATOM   2884 C CG2 . ILE A 1 378 ? 65.06674 -45.38629 -71.80569  1.000 214.59213 ? 372 ILE A CG2 1 
ATOM   2885 C CD1 . ILE A 1 378 ? 63.63045 -42.75535 -71.54910  1.000 236.60680 ? 372 ILE A CD1 1 
ATOM   2886 O OXT . ILE A 1 378 ? 64.24273 -48.48123 -72.08186  1.000 316.70053 ? 372 ILE A OXT 1 
HETATM 2887 C C1  . GOL B 2 .   ? 56.43922 -28.33305 -90.77978  1.000 216.55120 ? 401 GOL A C1  1 
HETATM 2888 O O1  . GOL B 2 .   ? 55.54638 -29.05143 -91.59831  1.000 236.70250 ? 401 GOL A O1  1 
HETATM 2889 C C2  . GOL B 2 .   ? 57.83723 -28.88922 -90.95117  1.000 218.08494 ? 401 GOL A C2  1 
HETATM 2890 O O2  . GOL B 2 .   ? 58.70950 -28.18052 -90.09958  1.000 187.63795 ? 401 GOL A O2  1 
HETATM 2891 C C3  . GOL B 2 .   ? 58.27109 -28.77796 -92.40405  1.000 229.50539 ? 401 GOL A C3  1 
HETATM 2892 O O3  . GOL B 2 .   ? 59.56837 -29.32222 -92.51583  1.000 224.60482 ? 401 GOL A O3  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   . SER A 12  ? 3.34233 2.49971 3.21750 0.15813  0.32745  -0.35461 6   SER A N   
2    C CA  . SER A 12  ? 3.62726 2.81305 3.42571 0.11417  0.31257  -0.35907 6   SER A CA  
3    C C   . SER A 12  ? 3.93587 3.17871 3.72303 0.13314  0.25559  -0.31862 6   SER A C   
4    O O   . SER A 12  ? 3.91684 3.18542 3.75928 0.18001  0.23197  -0.29419 6   SER A O   
5    C CB  . SER A 12  ? 3.34541 2.53977 3.14504 0.09345  0.34179  -0.39318 6   SER A CB  
6    O OG  . SER A 12  ? 3.64941 2.87807 3.51859 0.13789  0.33192  -0.38441 6   SER A OG  
7    N N   . VAL A 13  ? 4.05089 3.31282 3.76773 0.09482  0.23421  -0.31131 7   VAL A N   
8    C CA  . VAL A 13  ? 3.90640 3.22074 3.61065 0.10767  0.18344  -0.27539 7   VAL A CA  
9    C C   . VAL A 13  ? 3.98689 3.34401 3.67740 0.09271  0.17324  -0.28166 7   VAL A C   
10   O O   . VAL A 13  ? 4.12592 3.47096 3.78023 0.05040  0.19835  -0.31005 7   VAL A O   
11   C CB  . VAL A 13  ? 3.73390 3.04381 3.37934 0.07904  0.16241  -0.25716 7   VAL A CB  
12   C CG1 . VAL A 13  ? 3.75993 3.03391 3.42349 0.10034  0.16566  -0.24520 7   VAL A CG1 
13   C CG2 . VAL A 13  ? 3.59769 2.88579 3.17607 0.01709  0.18409  -0.28183 7   VAL A CG2 
14   N N   . PRO A 14  ? 3.97446 3.38042 3.69082 0.12371  0.13778  -0.25664 8   PRO A N   
15   C CA  . PRO A 14  ? 4.06829 3.51496 3.77375 0.11055  0.12690  -0.26142 8   PRO A CA  
16   C C   . PRO A 14  ? 4.04084 3.50877 3.68239 0.06740  0.10289  -0.25046 8   PRO A C   
17   O O   . PRO A 14  ? 3.96444 3.43403 3.58254 0.06221  0.08032  -0.22753 8   PRO A O   
18   C CB  . PRO A 14  ? 3.80480 3.29234 3.56264 0.16119  0.09675  -0.23592 8   PRO A CB  
19   C CG  . PRO A 14  ? 3.71649 3.19663 3.48314 0.18538  0.07607  -0.20791 8   PRO A CG  
20   C CD  . PRO A 14  ? 3.86473 3.28895 3.62307 0.17180  0.10800  -0.22407 8   PRO A CD  
21   N N   . ALA A 15  ? 4.13838 3.62358 3.75432 0.03521  0.10756  -0.26612 9   ALA A N   
22   C CA  . ALA A 15  ? 3.85654 3.36533 3.41706 -0.00821 0.08269  -0.25367 9   ALA A CA  
23   C C   . ALA A 15  ? 3.61065 3.17049 3.18977 0.01890  0.03669  -0.21812 9   ALA A C   
24   O O   . ALA A 15  ? 3.56162 3.15027 3.18208 0.05391  0.02674  -0.21346 9   ALA A O   
25   C CB  . ALA A 15  ? 3.68154 3.19434 3.21057 -0.05158 0.09984  -0.27945 9   ALA A CB  
26   N N   . GLY A 16  ? 3.61028 3.18096 3.16026 0.00161  0.00985  -0.19346 10  GLY A N   
27   C CA  . GLY A 16  ? 3.41520 3.03040 2.98384 0.02505  -0.03041 -0.16071 10  GLY A CA  
28   C C   . GLY A 16  ? 3.48301 3.09789 3.09038 0.07398  -0.04106 -0.14215 10  GLY A C   
29   O O   . GLY A 16  ? 3.43733 3.08590 3.05787 0.09154  -0.07196 -0.11587 10  GLY A O   
30   N N   . ALA A 17  ? 3.56584 3.14322 3.19292 0.09495  -0.01602 -0.15476 11  ALA A N   
31   C CA  . ALA A 17  ? 3.50861 3.08144 3.17017 0.13792  -0.02570 -0.13639 11  ALA A CA  
32   C C   . ALA A 17  ? 3.58575 3.19755 3.29045 0.17898  -0.04710 -0.12152 11  ALA A C   
33   O O   . ALA A 17  ? 3.51896 3.14821 3.23706 0.20276  -0.07092 -0.09698 11  ALA A O   
34   C CB  . ALA A 17  ? 3.29159 2.86253 2.92730 0.12698  -0.04474 -0.11371 11  ALA A CB  
35   N N   . LYS A 18  ? 3.66408 3.28904 3.38885 0.18512  -0.03734 -0.13740 12  LYS A N   
36   C CA  . LYS A 18  ? 3.71882 3.37804 3.48527 0.22278  -0.05410 -0.12641 12  LYS A CA  
37   C C   . LYS A 18  ? 3.68415 3.38589 3.44224 0.22472  -0.08962 -0.10153 12  LYS A C   
38   O O   . LYS A 18  ? 3.64822 3.37199 3.43431 0.25744  -0.10829 -0.08394 12  LYS A O   
39   C CB  . LYS A 18  ? 3.70908 3.35241 3.51936 0.26430  -0.05069 -0.11796 12  LYS A CB  
40   C CG  . LYS A 18  ? 3.67922 3.28223 3.51321 0.26849  -0.01485 -0.14138 12  LYS A CG  
41   C CD  . LYS A 18  ? 3.58041 3.19727 3.44647 0.27783  -0.00063 -0.15962 12  LYS A CD  
42   C CE  . LYS A 18  ? 3.41664 3.06489 3.32996 0.31996  -0.02255 -0.13974 12  LYS A CE  
43   N NZ  . LYS A 18  ? 3.33702 2.96375 3.28911 0.35186  -0.02293 -0.12465 12  LYS A NZ  
44   N N   . CYS A 19  ? 3.70523 3.41829 3.42611 0.18776  -0.09862 -0.09967 13  CYS A N   
45   C CA  . CYS A 19  ? 3.62883 3.37941 3.34536 0.18579  -0.13013 -0.07594 13  CYS A CA  
46   C C   . CYS A 19  ? 3.56321 3.35026 3.28720 0.18175  -0.14153 -0.07825 13  CYS A C   
47   O O   . CYS A 19  ? 3.49553 3.27893 3.20287 0.15534  -0.12840 -0.09681 13  CYS A O   
48   C CB  . CYS A 19  ? 3.61432 3.35838 3.29276 0.14774  -0.13711 -0.06712 13  CYS A CB  
49   S SG  . CYS A 19  ? 3.61696 3.32638 3.28588 0.15323  -0.13192 -0.05715 13  CYS A SG  
50   N N   . ARG A 20  ? 3.47546 3.29656 3.22292 0.20616  -0.16511 -0.05997 14  ARG A N   
51   C CA  . ARG A 20  ? 3.32108 3.17880 3.07727 0.20373  -0.17960 -0.05838 14  ARG A CA  
52   C C   . ARG A 20  ? 3.09284 2.98142 2.85546 0.20616  -0.20749 -0.03353 14  ARG A C   
53   O O   . ARG A 20  ? 2.98102 2.86651 2.75162 0.22302  -0.21440 -0.01900 14  ARG A O   
54   C CB  . ARG A 20  ? 3.36783 3.23592 3.15697 0.23731  -0.17475 -0.06655 14  ARG A CB  
55   C CG  . ARG A 20  ? 3.27642 3.14768 3.09384 0.27721  -0.18345 -0.05178 14  ARG A CG  
56   C CD  . ARG A 20  ? 3.18150 3.06035 3.03120 0.30609  -0.17771 -0.05950 14  ARG A CD  
57   N NE  . ARG A 20  ? 3.02206 2.93423 2.87713 0.30245  -0.18796 -0.06246 14  ARG A NE  
58   C CZ  . ARG A 20  ? 3.19499 3.11941 3.07529 0.32112  -0.18399 -0.07050 14  ARG A CZ  
59   N NH1 . ARG A 20  ? 3.29543 3.20297 3.20260 0.34532  -0.17043 -0.07540 14  ARG A NH1 
60   N NH2 . ARG A 20  ? 3.21336 3.16818 3.09480 0.31496  -0.19468 -0.07228 14  ARG A NH2 
61   N N   . LEU A 21  ? 3.02524 2.94309 2.78624 0.18816  -0.22252 -0.02893 15  LEU A N   
62   C CA  . LEU A 21  ? 2.95819 2.90445 2.72963 0.18545  -0.24711 -0.00581 15  LEU A CA  
63   C C   . LEU A 21  ? 2.92541 2.89293 2.72942 0.22402  -0.25743 0.00341  15  LEU A C   
64   O O   . LEU A 21  ? 2.76144 2.73564 2.57984 0.24542  -0.25329 -0.00611 15  LEU A O   
65   C CB  . LEU A 21  ? 3.07248 3.04262 2.83590 0.15271  -0.26115 -0.00176 15  LEU A CB  
66   C CG  . LEU A 21  ? 3.13095 3.08363 2.85683 0.10590  -0.25539 -0.00677 15  LEU A CG  
67   C CD1 . LEU A 21  ? 3.58386 3.56468 3.30539 0.07296  -0.27553 0.00386  15  LEU A CD1 
68   C CD2 . LEU A 21  ? 2.81218 2.74648 2.52530 0.09514  -0.25552 0.00502  15  LEU A CD2 
69   N N   . VAL A 22  ? 3.04864 3.02659 2.86389 0.23083  -0.26998 0.02176  16  VAL A N   
70   C CA  . VAL A 22  ? 3.02776 3.02516 2.86956 0.26146  -0.27909 0.03093  16  VAL A CA  
71   C C   . VAL A 22  ? 3.10259 3.12643 2.96032 0.25086  -0.29638 0.04871  16  VAL A C   
72   O O   . VAL A 22  ? 3.20426 3.22357 3.05558 0.23065  -0.29986 0.05920  16  VAL A O   
73   C CB  . VAL A 22  ? 2.95141 2.92796 2.79379 0.28539  -0.27103 0.03333  16  VAL A CB  
74   C CG1 . VAL A 22  ? 2.88924 2.88599 2.75292 0.30921  -0.28077 0.04384  16  VAL A CG1 
75   C CG2 . VAL A 22  ? 2.90759 2.86069 2.74600 0.29962  -0.25541 0.01832  16  VAL A CG2 
76   N N   . GLU A 23  ? 2.86697 2.91829 2.74846 0.26396  -0.30675 0.05253  17  GLU A N   
77   C CA  . GLU A 23  ? 2.79174 2.86882 2.69723 0.25526  -0.32173 0.06883  17  GLU A CA  
78   C C   . GLU A 23  ? 2.79255 2.88993 2.72394 0.28114  -0.32593 0.07023  17  GLU A C   
79   O O   . GLU A 23  ? 2.66795 2.76429 2.59638 0.30070  -0.32119 0.05942  17  GLU A O   
80   C CB  . GLU A 23  ? 2.84040 2.93280 2.74552 0.22424  -0.33377 0.07336  17  GLU A CB  
81   C CG  . GLU A 23  ? 3.04860 3.14889 2.94792 0.22473  -0.33369 0.05992  17  GLU A CG  
82   C CD  . GLU A 23  ? 3.18371 3.29769 3.07760 0.18938  -0.34645 0.06536  17  GLU A CD  
83   O OE1 . GLU A 23  ? 2.83296 2.95386 2.73336 0.16583  -0.35838 0.08279  17  GLU A OE1 
84   O OE2 . GLU A 23  ? 3.49058 3.60910 3.37429 0.18354  -0.34526 0.05332  17  GLU A OE2 
85   N N   . THR A 24  ? 2.95227 3.06797 2.91104 0.27984  -0.33410 0.08383  18  THR A N   
86   C CA  . THR A 24  ? 2.90731 3.04228 2.89226 0.29942  -0.33669 0.08496  18  THR A CA  
87   C C   . THR A 24  ? 2.95601 3.11748 2.96656 0.28681  -0.35080 0.09170  18  THR A C   
88   O O   . THR A 24  ? 2.67002 2.84179 2.69901 0.26627  -0.36044 0.10599  18  THR A O   
89   C CB  . THR A 24  ? 2.85928 2.99420 2.86110 0.30754  -0.33171 0.09322  18  THR A CB  
90   O OG1 . THR A 24  ? 2.78206 2.89126 2.75772 0.31496  -0.32067 0.08934  18  THR A OG1 
91   C CG2 . THR A 24  ? 2.87058 3.02067 2.89321 0.32657  -0.32999 0.09032  18  THR A CG2 
92   N N   . LEU A 25  ? 3.11598 3.28891 3.12933 0.29811  -0.35329 0.08322  19  LEU A N   
93   C CA  . LEU A 25  ? 2.90791 3.10551 2.94507 0.28754  -0.36722 0.08917  19  LEU A CA  
94   C C   . LEU A 25  ? 2.93898 3.15135 3.00121 0.30877  -0.36629 0.08731  19  LEU A C   
95   O O   . LEU A 25  ? 3.18644 3.39975 3.23679 0.32416  -0.36320 0.07550  19  LEU A O   
96   C CB  . LEU A 25  ? 2.96665 3.16457 2.98103 0.27616  -0.37101 0.07945  19  LEU A CB  
97   C CG  . LEU A 25  ? 3.10173 3.27924 3.08275 0.25545  -0.36591 0.07468  19  LEU A CG  
98   C CD1 . LEU A 25  ? 3.17806 3.35797 3.13966 0.24180  -0.36731 0.06308  19  LEU A CD1 
99   C CD2 . LEU A 25  ? 2.86209 3.04035 2.84937 0.22827  -0.37470 0.09170  19  LEU A CD2 
100  N N   . PRO A 26  ? 2.81622 3.03985 2.91434 0.30944  -0.36755 0.09813  20  PRO A N   
101  C CA  . PRO A 26  ? 2.84801 3.08254 2.96857 0.32748  -0.36290 0.09391  20  PRO A CA  
102  C C   . PRO A 26  ? 2.82753 3.08004 2.95884 0.32675  -0.37364 0.09156  20  PRO A C   
103  O O   . PRO A 26  ? 2.68870 2.95031 2.82208 0.30865  -0.38722 0.09781  20  PRO A O   
104  C CB  . PRO A 26  ? 2.58486 2.82768 2.74858 0.32268  -0.36103 0.10668  20  PRO A CB  
105  C CG  . PRO A 26  ? 2.52935 2.75987 2.68228 0.30896  -0.36072 0.11522  20  PRO A CG  
106  C CD  . PRO A 26  ? 2.58746 2.81218 2.70763 0.29398  -0.37041 0.11375  20  PRO A CD  
107  N N   . GLU A 27  ? 2.85707 3.11419 2.99249 0.34449  -0.36750 0.08251  21  GLU A N   
108  C CA  . GLU A 27  ? 2.92470 3.19810 3.06861 0.34556  -0.37661 0.07913  21  GLU A CA  
109  C C   . GLU A 27  ? 2.78589 3.07813 2.97666 0.33283  -0.38805 0.09293  21  GLU A C   
110  O O   . GLU A 27  ? 2.87208 3.17785 3.06873 0.32297  -0.40200 0.09607  21  GLU A O   
111  C CB  . GLU A 27  ? 2.95781 3.23059 3.09332 0.36556  -0.36702 0.06693  21  GLU A CB  
112  C CG  . GLU A 27  ? 3.10929 3.36678 3.20331 0.37800  -0.35986 0.05647  21  GLU A CG  
113  C CD  . GLU A 27  ? 2.96957 3.20850 3.05109 0.38277  -0.34783 0.05737  21  GLU A CD  
114  O OE1 . GLU A 27  ? 2.74262 2.98145 2.84724 0.37791  -0.34256 0.06376  21  GLU A OE1 
115  O OE2 . GLU A 27  ? 3.02649 3.25117 3.07785 0.39104  -0.34366 0.05240  21  GLU A OE2 
116  N N   . ASN A 28  ? 2.68419 2.97789 2.91149 0.33221  -0.38244 0.10206  22  ASN A N   
117  C CA  . ASN A 28  ? 2.87780 3.18951 3.16028 0.32083  -0.39328 0.11819  22  ASN A CA  
118  C C   . ASN A 28  ? 2.84080 3.15954 3.13007 0.29528  -0.41256 0.13657  22  ASN A C   
119  O O   . ASN A 28  ? 3.02152 3.35671 3.35949 0.28258  -0.42591 0.15473  22  ASN A O   
120  C CB  . ASN A 28  ? 2.85047 3.16130 3.17534 0.32813  -0.37839 0.12155  22  ASN A CB  
121  C CG  . ASN A 28  ? 2.81841 3.11477 3.12841 0.32597  -0.36892 0.12374  22  ASN A CG  
122  O OD1 . ASN A 28  ? 2.73390 3.01365 3.00673 0.33808  -0.35399 0.10998  22  ASN A OD1 
123  N ND2 . ASN A 28  ? 3.04579 3.34877 3.38514 0.30897  -0.37899 0.14279  22  ASN A ND2 
124  N N   . MET A 29  ? 2.70053 3.00680 2.94380 0.28572  -0.41430 0.13304  23  MET A N   
125  C CA  . MET A 29  ? 2.57735 2.88740 2.81606 0.25682  -0.43123 0.14834  23  MET A CA  
126  C C   . MET A 29  ? 2.45446 2.76341 2.65090 0.24595  -0.43876 0.13867  23  MET A C   
127  O O   . MET A 29  ? 2.45495 2.75542 2.61997 0.26306  -0.42784 0.11923  23  MET A O   
128  C CB  . MET A 29  ? 2.71210 3.00588 2.93262 0.24947  -0.42420 0.15184  23  MET A CB  
129  C CG  . MET A 29  ? 2.86116 3.15508 3.12088 0.25995  -0.41387 0.15937  23  MET A CG  
130  S SD  . MET A 29  ? 2.82690 3.10188 3.06321 0.25019  -0.40640 0.16393  23  MET A SD  
131  C CE  . MET A 29  ? 2.33265 2.61185 2.62120 0.26587  -0.39147 0.16907  23  MET A CE  
132  N N   . ASP A 30  ? 2.43164 2.74986 2.62862 0.21520  -0.45764 0.15324  24  ASP A N   
133  C CA  . ASP A 30  ? 2.55694 2.87647 2.71743 0.19874  -0.46521 0.14500  24  ASP A CA  
134  C C   . ASP A 30  ? 2.74533 3.04375 2.85244 0.18571  -0.45568 0.13283  24  ASP A C   
135  O O   . ASP A 30  ? 2.74766 3.04555 2.82362 0.16486  -0.46032 0.12627  24  ASP A O   
136  C CB  . ASP A 30  ? 2.56422 2.90432 2.74923 0.16740  -0.49127 0.16722  24  ASP A CB  
137  C CG  . ASP A 30  ? 2.69065 3.03253 2.89010 0.13879  -0.50441 0.19127  24  ASP A CG  
138  O OD1 . ASP A 30  ? 2.63975 2.96852 2.79595 0.11502  -0.50379 0.18856  24  ASP A OD1 
139  O OD2 . ASP A 30  ? 2.85466 3.21086 3.11066 0.13917  -0.51462 0.21297  24  ASP A OD2 
140  N N   . PHE A 31  ? 2.68223 2.96228 2.77825 0.19618  -0.44115 0.12877  25  PHE A N   
141  C CA  . PHE A 31  ? 2.76955 3.02670 2.81852 0.18409  -0.43026 0.11716  25  PHE A CA  
142  C C   . PHE A 31  ? 2.98325 3.22792 3.00237 0.20581  -0.41341 0.09189  25  PHE A C   
143  O O   . PHE A 31  ? 2.99616 3.23794 3.02400 0.23747  -0.40287 0.08390  25  PHE A O   
144  C CB  . PHE A 31  ? 2.81174 3.05340 2.86165 0.18793  -0.42142 0.12294  25  PHE A CB  
145  C CG  . PHE A 31  ? 2.94778 3.20322 3.03380 0.16848  -0.43723 0.14916  25  PHE A CG  
146  C CD1 . PHE A 31  ? 2.93718 3.19503 3.01161 0.12918  -0.45230 0.16377  25  PHE A CD1 
147  C CD2 . PHE A 31  ? 3.04608 3.31218 3.17911 0.18757  -0.43644 0.15956  25  PHE A CD2 
148  C CE1 . PHE A 31  ? 2.93405 3.20678 3.04696 0.11045  -0.46925 0.19142  25  PHE A CE1 
149  C CE2 . PHE A 31  ? 2.99646 3.27668 3.17139 0.17078  -0.45018 0.18473  25  PHE A CE2 
150  C CZ  . PHE A 31  ? 2.82829 3.11286 2.99507 0.13275  -0.46807 0.20225  25  PHE A CZ  
151  N N   . ARG A 32  ? 3.05027 3.28781 3.03541 0.18688  -0.41061 0.07984  26  ARG A N   
152  C CA  . ARG A 32  ? 3.27696 3.50359 3.23909 0.20464  -0.39422 0.05655  26  ARG A CA  
153  C C   . ARG A 32  ? 3.22114 3.42283 3.14496 0.18615  -0.37962 0.04320  26  ARG A C   
154  O O   . ARG A 32  ? 2.87010 3.06933 2.77606 0.14962  -0.38605 0.04874  26  ARG A O   
155  C CB  . ARG A 32  ? 3.37195 3.61791 3.33713 0.20194  -0.40215 0.05068  26  ARG A CB  
156  C CG  . ARG A 32  ? 3.31706 3.58610 3.31952 0.21932  -0.41502 0.06163  26  ARG A CG  
157  C CD  . ARG A 32  ? 3.53325 3.79720 3.54711 0.25755  -0.40304 0.05500  26  ARG A CD  
158  N NE  . ARG A 32  ? 3.54524 3.82904 3.58772 0.27259  -0.41135 0.05953  26  ARG A NE  
159  C CZ  . ARG A 32  ? 3.08347 3.37720 3.16017 0.27569  -0.41867 0.07413  26  ARG A CZ  
160  N NH1 . ARG A 32  ? 2.97778 3.26613 3.06715 0.26553  -0.42031 0.08741  26  ARG A NH1 
161  N NH2 . ARG A 32  ? 2.84708 3.15618 2.94791 0.28877  -0.42320 0.07499  26  ARG A NH2 
162  N N   . SER A 33  ? 3.31475 3.49736 3.22701 0.20973  -0.35997 0.02630  27  SER A N   
163  C CA  . SER A 33  ? 3.28187 3.43758 3.16266 0.19601  -0.34169 0.01065  27  SER A CA  
164  C C   . SER A 33  ? 3.24769 3.39050 3.12990 0.22773  -0.32304 -0.00701 27  SER A C   
165  O O   . SER A 33  ? 3.02869 3.18024 2.93213 0.25947  -0.32553 -0.00350 27  SER A O   
166  C CB  . SER A 33  ? 3.13486 3.27120 3.00486 0.18358  -0.33889 0.01966  27  SER A CB  
167  O OG  . SER A 33  ? 2.99676 3.12654 2.88343 0.21517  -0.33485 0.02509  27  SER A OG  
168  N N   . ASP A 34  ? 3.35693 3.47842 3.21759 0.21684  -0.30392 -0.02558 28  ASP A N   
169  C CA  . ASP A 34  ? 3.56744 3.67439 3.43503 0.24447  -0.28484 -0.04139 28  ASP A CA  
170  C C   . ASP A 34  ? 3.48950 3.56782 3.35460 0.25771  -0.27213 -0.04075 28  ASP A C   
171  O O   . ASP A 34  ? 3.78493 3.84867 3.65994 0.28034  -0.25698 -0.05095 28  ASP A O   
172  C CB  . ASP A 34  ? 3.76880 3.86782 3.62181 0.22687  -0.26733 -0.06416 28  ASP A CB  
173  C CG  . ASP A 34  ? 3.85864 3.98542 3.71186 0.21259  -0.27939 -0.06571 28  ASP A CG  
174  O OD1 . ASP A 34  ? 4.00527 4.15701 3.87927 0.23050  -0.29733 -0.05304 28  ASP A OD1 
175  O OD2 . ASP A 34  ? 3.94860 4.07117 3.77971 0.18164  -0.27010 -0.08023 28  ASP A OD2 
176  N N   . HIS A 35  ? 3.17208 3.24263 3.02702 0.24379  -0.27869 -0.02767 29  HIS A N   
177  C CA  . HIS A 35  ? 3.09552 3.13810 2.94510 0.25314  -0.26727 -0.02652 29  HIS A CA  
178  C C   . HIS A 35  ? 3.11508 3.16188 2.98750 0.29033  -0.27214 -0.01636 29  HIS A C   
179  O O   . HIS A 35  ? 3.02607 3.09742 2.91667 0.30665  -0.28448 -0.00972 29  HIS A O   
180  C CB  . HIS A 35  ? 2.92072 2.95631 2.75285 0.22537  -0.27413 -0.01429 29  HIS A CB  
181  C CG  . HIS A 35  ? 3.10891 3.13607 2.91184 0.18353  -0.26919 -0.02298 29  HIS A CG  
182  N ND1 . HIS A 35  ? 3.08091 3.12520 2.87571 0.15121  -0.28746 -0.00877 29  HIS A ND1 
183  C CD2 . HIS A 35  ? 3.38101 3.38376 3.16089 0.16618  -0.24749 -0.04423 29  HIS A CD2 
184  C CE1 . HIS A 35  ? 3.26330 3.29447 3.02611 0.11338  -0.27898 -0.02002 29  HIS A CE1 
185  N NE2 . HIS A 35  ? 3.71061 3.71559 3.46264 0.12144  -0.25289 -0.04343 29  HIS A NE2 
186  N N   . LEU A 36  ? 3.03582 3.05696 2.90482 0.30122  -0.26204 -0.01519 30  LEU A N   
187  C CA  . LEU A 36  ? 2.93726 2.95913 2.82188 0.33098  -0.26692 -0.00410 30  LEU A CA  
188  C C   . LEU A 36  ? 2.85678 2.89615 2.74542 0.32822  -0.28268 0.01295  30  LEU A C   
189  O O   . LEU A 36  ? 2.72049 2.75967 2.59958 0.30495  -0.28685 0.01919  30  LEU A O   
190  C CB  . LEU A 36  ? 2.74812 2.73666 2.62693 0.33922  -0.25318 -0.00560 30  LEU A CB  
191  C CG  . LEU A 36  ? 2.85188 2.83674 2.74498 0.36873  -0.25668 0.00483  30  LEU A CG  
192  C CD1 . LEU A 36  ? 3.02743 3.02188 2.94185 0.39058  -0.25573 -0.00038 30  LEU A CD1 
193  C CD2 . LEU A 36  ? 2.95695 2.90804 2.84168 0.37055  -0.24584 0.00675  30  LEU A CD2 
194  N N   . THR A 37  ? 2.90914 2.96383 2.81357 0.35046  -0.29077 0.02057  31  THR A N   
195  C CA  . THR A 37  ? 2.92742 2.99727 2.84020 0.34970  -0.30144 0.03423  31  THR A CA  
196  C C   . THR A 37  ? 2.71790 2.76897 2.62446 0.35778  -0.29692 0.04225  31  THR A C   
197  O O   . THR A 37  ? 2.70251 2.73194 2.60155 0.36941  -0.28873 0.03938  31  THR A O   
198  C CB  . THR A 37  ? 2.93387 3.02920 2.86400 0.36521  -0.31041 0.03638  31  THR A CB  
199  O OG1 . THR A 37  ? 2.65611 2.74433 2.58660 0.38832  -0.30754 0.03716  31  THR A OG1 
200  C CG2 . THR A 37  ? 2.70799 2.81948 2.64269 0.36031  -0.31389 0.02719  31  THR A CG2 
201  N N   . THR A 38  ? 2.65765 2.71744 2.57040 0.35077  -0.30222 0.05308  32  THR A N   
202  C CA  . THR A 38  ? 2.58586 2.62971 2.49177 0.35571  -0.29771 0.06066  32  THR A CA  
203  C C   . THR A 38  ? 2.66763 2.70998 2.57389 0.37836  -0.29706 0.06185  32  THR A C   
204  O O   . THR A 38  ? 2.79205 2.81353 2.68633 0.38514  -0.29225 0.06535  32  THR A O   
205  C CB  . THR A 38  ? 2.65961 2.71642 2.57813 0.34314  -0.30208 0.07126  32  THR A CB  
206  O OG1 . THR A 38  ? 2.61737 2.67861 2.53713 0.31927  -0.30653 0.07362  32  THR A OG1 
207  C CG2 . THR A 38  ? 2.75875 2.79778 2.66756 0.34440  -0.29578 0.07798  32  THR A CG2 
208  N N   . PHE A 39  ? 2.52355 2.58747 2.44212 0.38815  -0.30290 0.06011  33  PHE A N   
209  C CA  . PHE A 39  ? 2.72985 2.79346 2.64554 0.40583  -0.30400 0.06224  33  PHE A CA  
210  C C   . PHE A 39  ? 2.77718 2.82560 2.68801 0.41782  -0.30212 0.05912  33  PHE A C   
211  O O   . PHE A 39  ? 2.82628 2.86107 2.73019 0.42797  -0.30210 0.06571  33  PHE A O   
212  C CB  . PHE A 39  ? 2.84568 2.93553 2.77439 0.41078  -0.31017 0.06041  33  PHE A CB  
213  C CG  . PHE A 39  ? 2.98084 3.07196 2.90307 0.42469  -0.31260 0.06317  33  PHE A CG  
214  C CD1 . PHE A 39  ? 2.79946 2.88446 2.71125 0.42405  -0.30982 0.06941  33  PHE A CD1 
215  C CD2 . PHE A 39  ? 3.15920 3.25811 3.08495 0.43587  -0.31784 0.06011  33  PHE A CD2 
216  C CE1 . PHE A 39  ? 3.01464 3.10050 2.91570 0.43193  -0.31346 0.07336  33  PHE A CE1 
217  C CE2 . PHE A 39  ? 3.27323 3.37449 3.19246 0.44572  -0.32256 0.06546  33  PHE A CE2 
218  C CZ  . PHE A 39  ? 3.21986 3.31422 3.12476 0.44255  -0.32100 0.07250  33  PHE A CZ  
219  N N   . GLU A 40  ? 2.82848 2.87906 2.74514 0.41556  -0.30026 0.04969  34  GLU A N   
220  C CA  . GLU A 40  ? 3.03303 3.06803 2.95267 0.42653  -0.29490 0.04523  34  GLU A CA  
221  C C   . GLU A 40  ? 2.87431 2.87787 2.78393 0.42301  -0.28555 0.04680  34  GLU A C   
222  O O   . GLU A 40  ? 2.69576 2.68235 2.61116 0.43597  -0.28220 0.04920  34  GLU A O   
223  C CB  . GLU A 40  ? 3.16138 3.20525 3.08912 0.42149  -0.29138 0.03193  34  GLU A CB  
224  C CG  . GLU A 40  ? 3.19194 3.26456 3.13158 0.42841  -0.30033 0.02985  34  GLU A CG  
225  C CD  . GLU A 40  ? 3.19540 3.27692 3.13972 0.41887  -0.29649 0.01634  34  GLU A CD  
226  O OE1 . GLU A 40  ? 2.92431 2.99264 2.85878 0.40128  -0.28809 0.00896  34  GLU A OE1 
227  O OE2 . GLU A 40  ? 3.22937 3.33073 3.18484 0.42667  -0.30165 0.01293  34  GLU A OE2 
228  N N   . CYS A 41  ? 2.80709 2.80264 2.70424 0.40508  -0.28195 0.04684  35  CYS A N   
229  C CA  . CYS A 41  ? 2.87277 2.83734 2.75777 0.39911  -0.27242 0.04740  35  CYS A CA  
230  C C   . CYS A 41  ? 2.87486 2.82636 2.75450 0.40972  -0.27523 0.06042  35  CYS A C   
231  O O   . CYS A 41  ? 2.91585 2.84174 2.79442 0.41653  -0.26959 0.06257  35  CYS A O   
232  C CB  . CYS A 41  ? 2.81322 2.77536 2.68519 0.37439  -0.26998 0.04603  35  CYS A CB  
233  S SG  . CYS A 41  ? 3.28806 3.21188 3.14061 0.36299  -0.25827 0.04676  35  CYS A SG  
234  N N   . PHE A 42  ? 2.77502 2.74280 2.65200 0.40980  -0.28307 0.06901  36  PHE A N   
235  C CA  . PHE A 42  ? 2.88144 2.83702 2.74814 0.41489  -0.28520 0.08088  36  PHE A CA  
236  C C   . PHE A 42  ? 2.87804 2.83149 2.75077 0.43247  -0.29143 0.08746  36  PHE A C   
237  O O   . PHE A 42  ? 2.74497 2.68001 2.60971 0.43636  -0.29327 0.09828  36  PHE A O   
238  C CB  . PHE A 42  ? 3.13541 3.10856 2.99825 0.40726  -0.28823 0.08556  36  PHE A CB  
239  C CG  . PHE A 42  ? 3.08474 3.05851 2.94624 0.38964  -0.28374 0.08455  36  PHE A CG  
240  C CD1 . PHE A 42  ? 3.08596 3.03890 2.93902 0.37948  -0.27792 0.08237  36  PHE A CD1 
241  C CD2 . PHE A 42  ? 3.15847 3.15341 3.02959 0.38208  -0.28493 0.08638  36  PHE A CD2 
242  C CE1 . PHE A 42  ? 3.14234 3.09725 2.99385 0.36074  -0.27602 0.08402  36  PHE A CE1 
243  C CE2 . PHE A 42  ? 3.26936 3.26711 3.14574 0.36557  -0.28268 0.08867  36  PHE A CE2 
244  C CZ  . PHE A 42  ? 3.22394 3.20249 3.08913 0.35420  -0.27955 0.08850  36  PHE A CZ  
245  N N   . ASN A 43  ? 2.92824 2.90083 2.81571 0.44182  -0.29614 0.08292  37  ASN A N   
246  C CA  . ASN A 43  ? 2.96363 2.93620 2.86099 0.45746  -0.30382 0.09139  37  ASN A CA  
247  C C   . ASN A 43  ? 2.92945 2.87726 2.84108 0.46615  -0.29797 0.09187  37  ASN A C   
248  O O   . ASN A 43  ? 2.91668 2.85282 2.83491 0.47598  -0.30434 0.10562  37  ASN A O   
249  C CB  . ASN A 43  ? 2.90374 2.90425 2.81448 0.46422  -0.31006 0.08626  37  ASN A CB  
250  C CG  . ASN A 43  ? 3.05219 3.07387 2.95162 0.45938  -0.31704 0.08956  37  ASN A CG  
251  O OD1 . ASN A 43  ? 2.85414 2.87611 2.74395 0.46165  -0.32461 0.10101  37  ASN A OD1 
252  N ND2 . ASN A 43  ? 3.30685 3.34567 3.20805 0.45084  -0.31424 0.07982  37  ASN A ND2 
253  N N   . GLU A 44  ? 2.62340 2.56218 2.54107 0.46090  -0.28548 0.07738  38  GLU A N   
254  C CA  . GLU A 44  ? 2.77441 2.68730 2.70884 0.46809  -0.27513 0.07414  38  GLU A CA  
255  C C   . GLU A 44  ? 2.91801 2.79998 2.84075 0.46473  -0.27185 0.08349  38  GLU A C   
256  O O   . GLU A 44  ? 2.97315 2.83401 2.91375 0.47597  -0.26994 0.09068  38  GLU A O   
257  C CB  . GLU A 44  ? 2.90550 2.81526 2.84321 0.45803  -0.25984 0.05350  38  GLU A CB  
258  C CG  . GLU A 44  ? 3.30623 3.18754 3.26347 0.46343  -0.24344 0.04507  38  GLU A CG  
259  C CD  . GLU A 44  ? 3.15770 3.04859 3.15172 0.48233  -0.24326 0.04399  38  GLU A CD  
260  O OE1 . GLU A 44  ? 3.33784 3.25441 3.34002 0.49311  -0.25943 0.05501  38  GLU A OE1 
261  O OE2 . GLU A 44  ? 2.72234 2.59483 2.73829 0.48528  -0.22569 0.03155  38  GLU A OE2 
262  N N   . ILE A 45  ? 2.88818 2.76737 2.78436 0.44929  -0.27142 0.08455  39  ILE A N   
263  C CA  . ILE A 45  ? 3.00478 2.85524 2.88693 0.44418  -0.26840 0.09324  39  ILE A CA  
264  C C   . ILE A 45  ? 3.01882 2.86702 2.90018 0.45376  -0.28199 0.11342  39  ILE A C   
265  O O   . ILE A 45  ? 2.88463 2.70658 2.77010 0.45838  -0.28195 0.12377  39  ILE A O   
266  C CB  . ILE A 45  ? 2.90322 2.75483 2.75987 0.42408  -0.26491 0.08993  39  ILE A CB  
267  C CG1 . ILE A 45  ? 2.78353 2.63625 2.63886 0.41022  -0.25395 0.07293  39  ILE A CG1 
268  C CG2 . ILE A 45  ? 3.06106 2.88391 2.90138 0.41790  -0.26215 0.09924  39  ILE A CG2 
269  C CD1 . ILE A 45  ? 2.85374 2.71065 2.68942 0.38885  -0.25308 0.07269  39  ILE A CD1 
270  N N   . ILE A 46  ? 3.01287 2.88748 2.88825 0.45480  -0.29385 0.11970  40  ILE A N   
271  C CA  . ILE A 46  ? 3.03370 2.90750 2.90166 0.45821  -0.30750 0.13901  40  ILE A CA  
272  C C   . ILE A 46  ? 3.11221 2.98392 3.00835 0.47490  -0.31646 0.14998  40  ILE A C   
273  O O   . ILE A 46  ? 3.26960 3.12594 3.16770 0.47804  -0.32614 0.16891  40  ILE A O   
274  C CB  . ILE A 46  ? 3.10642 3.00745 2.95670 0.45043  -0.31418 0.13965  40  ILE A CB  
275  C CG1 . ILE A 46  ? 3.11439 3.01651 2.94521 0.43452  -0.30490 0.13163  40  ILE A CG1 
276  C CG2 . ILE A 46  ? 3.02409 2.92486 2.86156 0.44943  -0.32815 0.15876  40  ILE A CG2 
277  C CD1 . ILE A 46  ? 3.16268 3.08932 2.98210 0.42653  -0.30698 0.12989  40  ILE A CD1 
278  N N   . THR A 47  ? 2.98540 2.87305 2.90622 0.48491  -0.31415 0.13980  41  THR A N   
279  C CA  . THR A 47  ? 3.09642 2.98555 3.05122 0.50136  -0.32235 0.15072  41  THR A CA  
280  C C   . THR A 47  ? 3.18252 3.03920 3.16280 0.50961  -0.31412 0.15457  41  THR A C   
281  O O   . THR A 47  ? 3.14811 2.99484 3.14864 0.51857  -0.32578 0.17555  41  THR A O   
282  C CB  . THR A 47  ? 2.95482 2.86861 2.93078 0.50897  -0.31913 0.13658  41  THR A CB  
283  O OG1 . THR A 47  ? 2.92253 2.86520 2.87755 0.50198  -0.32771 0.13480  41  THR A OG1 
284  C CG2 . THR A 47  ? 2.98213 2.89877 2.99972 0.52645  -0.32662 0.14829  41  THR A CG2 
285  N N   . LEU A 48  ? 3.21625 3.05533 3.19660 0.50498  -0.29419 0.13530  42  LEU A N   
286  C CA  . LEU A 48  ? 3.47511 3.28020 3.47962 0.51110  -0.28135 0.13428  42  LEU A CA  
287  C C   . LEU A 48  ? 3.54157 3.31812 3.52408 0.50258  -0.28275 0.14620  42  LEU A C   
288  O O   . LEU A 48  ? 3.52265 3.26713 3.52002 0.50468  -0.26982 0.14338  42  LEU A O   
289  C CB  . LEU A 48  ? 3.36818 3.16459 3.37727 0.50536  -0.25727 0.10649  42  LEU A CB  
290  C CG  . LEU A 48  ? 3.09873 2.92033 3.12962 0.51163  -0.25260 0.09182  42  LEU A CG  
291  C CD1 . LEU A 48  ? 3.01964 2.82692 3.05059 0.50109  -0.22718 0.06459  42  LEU A CD1 
292  C CD2 . LEU A 48  ? 3.29463 3.12232 3.37343 0.53305  -0.26042 0.10523  42  LEU A CD2 
293  N N   . ALA A 49  ? 3.57628 3.36261 3.52429 0.49207  -0.29636 0.15824  43  ALA A N   
294  C CA  . ALA A 49  ? 3.72268 3.48384 3.64719 0.48218  -0.29821 0.16984  43  ALA A CA  
295  C C   . ALA A 49  ? 3.65417 3.39915 3.60032 0.49207  -0.31278 0.19603  43  ALA A C   
296  O O   . ALA A 49  ? 3.54674 3.31036 3.50622 0.49922  -0.33054 0.21253  43  ALA A O   
297  C CB  . ALA A 49  ? 3.61170 3.38986 3.49439 0.46614  -0.30547 0.17243  43  ALA A CB  
298  N N   . LYS A 50  ? 3.75906 3.46890 3.70897 0.49084  -0.30631 0.20128  44  LYS A N   
299  C CA  . LYS A 50  ? 3.71805 3.40887 3.69289 0.49927  -0.32067 0.22839  44  LYS A CA  
300  C C   . LYS A 50  ? 3.72923 3.39527 3.67140 0.48499  -0.32522 0.24152  44  LYS A C   
301  O O   . LYS A 50  ? 3.57685 3.23487 3.52244 0.48443  -0.34450 0.26912  44  LYS A O   
302  C CB  . LYS A 50  ? 3.61211 3.28009 3.64187 0.51657  -0.30729 0.22406  44  LYS A CB  
303  C CG  . LYS A 50  ? 3.40492 3.09639 3.47368 0.53154  -0.30293 0.21335  44  LYS A CG  
304  C CD  . LYS A 50  ? 3.18591 2.85216 3.31336 0.54783  -0.28615 0.20817  44  LYS A CD  
305  C CE  . LYS A 50  ? 2.66455 2.35518 2.83339 0.56223  -0.28073 0.19740  44  LYS A CE  
306  N NZ  . LYS A 50  ? 2.86642 2.53212 3.09833 0.57803  -0.26092 0.19083  44  LYS A NZ  
307  N N   . LYS A 51  ? 3.82984 3.48437 3.73996 0.47150  -0.30885 0.22342  45  LYS A N   
308  C CA  . LYS A 51  ? 3.81725 3.44587 3.69792 0.45762  -0.30990 0.23322  45  LYS A CA  
309  C C   . LYS A 51  ? 3.48511 3.13168 3.31620 0.43809  -0.31153 0.22867  45  LYS A C   
310  O O   . LYS A 51  ? 3.36932 3.01529 3.17565 0.42750  -0.32544 0.24687  45  LYS A O   
311  C CB  . LYS A 51  ? 3.90154 3.49448 3.79109 0.45705  -0.28796 0.21823  45  LYS A CB  
312  C CG  . LYS A 51  ? 3.91526 3.48691 3.85970 0.47622  -0.28089 0.21955  45  LYS A CG  
313  C CD  . LYS A 51  ? 3.68892 3.22468 3.63800 0.47228  -0.25422 0.19908  45  LYS A CD  
314  C CE  . LYS A 51  ? 3.13462 2.64884 3.14403 0.49149  -0.24228 0.19677  45  LYS A CE  
315  N NZ  . LYS A 51  ? 2.83374 2.31078 2.84492 0.48467  -0.21229 0.17304  45  LYS A NZ  
316  N N   . TYR A 52  ? 3.44033 3.10293 3.25827 0.43162  -0.29753 0.20561  46  TYR A N   
317  C CA  . TYR A 52  ? 3.36581 3.04487 3.14601 0.41383  -0.29659 0.20095  46  TYR A CA  
318  C C   . TYR A 52  ? 3.42517 3.13260 3.20766 0.41260  -0.28747 0.17999  46  TYR A C   
319  O O   . TYR A 52  ? 3.53660 3.24592 3.34274 0.42208  -0.27969 0.16717  46  TYR A O   
320  C CB  . TYR A 52  ? 3.49872 3.15095 3.25482 0.39892  -0.28763 0.20030  46  TYR A CB  
321  C CG  . TYR A 52  ? 3.63157 3.26691 3.39426 0.39655  -0.26903 0.18133  46  TYR A CG  
322  C CD1 . TYR A 52  ? 3.55905 3.16130 3.34339 0.40511  -0.26101 0.18039  46  TYR A CD1 
323  C CD2 . TYR A 52  ? 3.53996 3.19190 3.28834 0.38366  -0.25917 0.16485  46  TYR A CD2 
324  C CE1 . TYR A 52  ? 3.42095 3.00566 3.20632 0.39876  -0.24162 0.16093  46  TYR A CE1 
325  C CE2 . TYR A 52  ? 3.41301 3.04958 3.16216 0.37644  -0.24349 0.14867  46  TYR A CE2 
326  C CZ  . TYR A 52  ? 3.45803 3.06028 3.22254 0.38294  -0.23376 0.14547  46  TYR A CZ  
327  O OH  . TYR A 52  ? 3.49115 3.07611 3.25150 0.37171  -0.21584 0.12729  46  TYR A OH  
328  N N   . ILE A 53  ? 3.27013 2.99937 3.02955 0.39967  -0.28790 0.17684  47  ILE A N   
329  C CA  . ILE A 53  ? 3.22191 2.97749 2.98349 0.39509  -0.28034 0.15975  47  ILE A CA  
330  C C   . ILE A 53  ? 3.34403 3.10262 3.08255 0.37641  -0.27450 0.15793  47  ILE A C   
331  O O   . ILE A 53  ? 3.38695 3.15400 3.10937 0.36911  -0.27898 0.16603  47  ILE A O   
332  C CB  . ILE A 53  ? 3.40206 3.19062 3.17286 0.40245  -0.28853 0.15870  47  ILE A CB  
333  C CG1 . ILE A 53  ? 3.36390 3.15287 3.16201 0.42074  -0.29403 0.16014  47  ILE A CG1 
334  C CG2 . ILE A 53  ? 3.54621 3.36114 3.31949 0.39539  -0.28167 0.14359  47  ILE A CG2 
335  C CD1 . ILE A 53  ? 3.38523 3.20603 3.19125 0.42724  -0.30283 0.15964  47  ILE A CD1 
336  N N   . TYR A 54  ? 3.33306 3.08490 3.07016 0.36669  -0.26405 0.14755  48  TYR A N   
337  C CA  . TYR A 54  ? 3.33227 3.08818 3.05362 0.34837  -0.25879 0.14708  48  TYR A CA  
338  C C   . TYR A 54  ? 3.25935 3.04578 2.99356 0.34235  -0.25605 0.13648  48  TYR A C   
339  O O   . TYR A 54  ? 3.13235 2.91994 2.87675 0.34219  -0.25272 0.12669  48  TYR A O   
340  C CB  . TYR A 54  ? 3.31822 3.04212 3.02647 0.33762  -0.25117 0.14713  48  TYR A CB  
341  C CG  . TYR A 54  ? 3.64449 3.33708 3.34047 0.34087  -0.25435 0.15990  48  TYR A CG  
342  C CD1 . TYR A 54  ? 3.73054 3.42760 3.42148 0.34680  -0.26492 0.17303  48  TYR A CD1 
343  C CD2 . TYR A 54  ? 3.79088 3.44850 3.47924 0.33559  -0.24713 0.15951  48  TYR A CD2 
344  C CE1 . TYR A 54  ? 3.82294 3.49180 3.50328 0.34752  -0.27060 0.18772  48  TYR A CE1 
345  C CE2 . TYR A 54  ? 3.92263 3.55070 3.60301 0.33850  -0.25107 0.17280  48  TYR A CE2 
346  C CZ  . TYR A 54  ? 3.90057 3.53508 3.57779 0.34452  -0.26401 0.18804  48  TYR A CZ  
347  O OH  . TYR A 54  ? 3.83392 3.43947 3.50374 0.34525  -0.27063 0.20420  48  TYR A OH  
348  N N   . ILE A 55  ? 3.27265 3.08293 3.00765 0.33594  -0.25676 0.13855  49  ILE A N   
349  C CA  . ILE A 55  ? 3.18559 3.02678 2.93937 0.33084  -0.25560 0.13159  49  ILE A CA  
350  C C   . ILE A 55  ? 3.10531 2.95331 2.85853 0.31330  -0.25041 0.13529  49  ILE A C   
351  O O   . ILE A 55  ? 2.96086 2.80025 2.69992 0.30802  -0.24748 0.14176  49  ILE A O   
352  C CB  . ILE A 55  ? 3.32537 3.19221 3.09117 0.34156  -0.25974 0.12953  49  ILE A CB  
353  C CG1 . ILE A 55  ? 3.43426 3.29487 3.20189 0.35862  -0.26631 0.12864  49  ILE A CG1 
354  C CG2 . ILE A 55  ? 3.35784 3.25517 3.14799 0.33730  -0.25894 0.12297  49  ILE A CG2 
355  C CD1 . ILE A 55  ? 3.39435 3.27810 3.16931 0.36750  -0.27148 0.12773  49  ILE A CD1 
356  N N   . ALA A 56  ? 3.04178 2.90596 2.81162 0.30273  -0.24991 0.13239  50  ALA A N   
357  C CA  . ALA A 56  ? 3.08085 2.95586 2.85931 0.28567  -0.24642 0.13798  50  ALA A CA  
358  C C   . ALA A 56  ? 3.21528 3.12315 3.02683 0.28079  -0.24960 0.13673  50  ALA A C   
359  O O   . ALA A 56  ? 3.17721 3.09109 2.99554 0.28199  -0.25504 0.13207  50  ALA A O   
360  C CB  . ALA A 56  ? 3.15462 3.00576 2.91496 0.26992  -0.24466 0.14191  50  ALA A CB  
361  N N   . SER A 57  ? 3.28805 3.21672 3.12235 0.27438  -0.24560 0.14117  51  SER A N   
362  C CA  . SER A 57  ? 3.00017 2.96065 2.87440 0.26879  -0.24881 0.14334  51  SER A CA  
363  C C   . SER A 57  ? 2.92355 2.89858 2.82266 0.25957  -0.24064 0.14979  51  SER A C   
364  O O   . SER A 57  ? 3.06436 3.02534 2.94538 0.25780  -0.23195 0.15041  51  SER A O   
365  C CB  . SER A 57  ? 3.04974 3.02836 2.94020 0.28418  -0.25113 0.13544  51  SER A CB  
366  O OG  . SER A 57  ? 3.02461 3.00489 2.91213 0.29406  -0.24252 0.13086  51  SER A OG  
367  N N   . PHE A 58  ? 2.86403 2.86774 2.80781 0.25293  -0.24337 0.15521  52  PHE A N   
368  C CA  . PHE A 58  ? 3.10647 3.12732 3.08605 0.24502  -0.23388 0.16127  52  PHE A CA  
369  C C   . PHE A 58  ? 3.09325 3.12019 3.08084 0.25698  -0.21904 0.15055  52  PHE A C   
370  O O   . PHE A 58  ? 2.93165 2.94765 2.90358 0.25412  -0.20637 0.14800  52  PHE A O   
371  C CB  . PHE A 58  ? 3.21433 3.26470 3.24694 0.23445  -0.24258 0.17281  52  PHE A CB  
372  C CG  . PHE A 58  ? 3.13164 3.20457 3.21681 0.23031  -0.23123 0.17816  52  PHE A CG  
373  C CD1 . PHE A 58  ? 2.77864 2.84913 2.86992 0.21659  -0.22529 0.18725  52  PHE A CD1 
374  C CD2 . PHE A 58  ? 3.20686 3.30298 3.33806 0.23982  -0.22496 0.17348  52  PHE A CD2 
375  C CE1 . PHE A 58  ? 2.91168 3.00368 3.05716 0.21297  -0.21245 0.19139  52  PHE A CE1 
376  C CE2 . PHE A 58  ? 3.11319 3.22890 3.29905 0.23634  -0.21108 0.17680  52  PHE A CE2 
377  C CZ  . PHE A 58  ? 3.01887 3.13318 3.21357 0.22314  -0.20440 0.18570  52  PHE A CZ  
378  N N   . CYS A 59  ? 3.21917 3.26272 3.22850 0.26799  -0.21988 0.14373  53  CYS A N   
379  C CA  . CYS A 59  ? 3.31607 3.36497 3.33072 0.27689  -0.20523 0.13188  53  CYS A CA  
380  C C   . CYS A 59  ? 3.20909 3.24510 3.18475 0.29050  -0.21086 0.12280  53  CYS A C   
381  O O   . CYS A 59  ? 3.31972 3.35674 3.29097 0.29671  -0.22478 0.12360  53  CYS A O   
382  C CB  . CYS A 59  ? 3.31296 3.39165 3.38894 0.27795  -0.19973 0.13112  53  CYS A CB  
383  S SG  . CYS A 59  ? 3.02229 3.10654 3.10761 0.28478  -0.17676 0.11360  53  CYS A SG  
384  N N   . CYS A 60  ? 3.02909 3.05350 2.97665 0.29306  -0.20022 0.11491  54  CYS A N   
385  C CA  . CYS A 60  ? 2.95933 2.97239 2.87123 0.30413  -0.20641 0.10916  54  CYS A CA  
386  C C   . CYS A 60  ? 3.23456 3.26176 3.15871 0.30728  -0.19542 0.09803  54  CYS A C   
387  O O   . CYS A 60  ? 3.28036 3.30654 3.20208 0.29847  -0.17830 0.09210  54  CYS A O   
388  C CB  . CYS A 60  ? 2.96238 2.94769 2.82551 0.30128  -0.20710 0.11252  54  CYS A CB  
389  S SG  . CYS A 60  ? 3.13282 3.10421 2.95822 0.31446  -0.21956 0.11146  54  CYS A SG  
390  N N   . ASN A 61  ? 3.25220 3.29157 3.18785 0.31797  -0.20391 0.09415  55  ASN A N   
391  C CA  . ASN A 61  ? 3.17449 3.22665 3.12115 0.32080  -0.19444 0.08304  55  ASN A CA  
392  C C   . ASN A 61  ? 3.03502 3.09311 2.97631 0.33366  -0.20939 0.08129  55  ASN A C   
393  O O   . ASN A 61  ? 3.12975 3.20579 3.10609 0.33818  -0.21491 0.08113  55  ASN A O   
394  C CB  . ASN A 61  ? 3.10157 3.17509 3.10434 0.31601  -0.18056 0.07937  55  ASN A CB  
395  C CG  . ASN A 61  ? 3.10373 3.18726 3.11874 0.31718  -0.16646 0.06555  55  ASN A CG  
396  O OD1 . ASN A 61  ? 3.15216 3.22452 3.12699 0.31531  -0.16172 0.05792  55  ASN A OD1 
397  N ND2 . ASN A 61  ? 3.15063 3.25476 3.22181 0.31864  -0.16022 0.06325  55  ASN A ND2 
398  N N   . PRO A 62  ? 2.83781 2.88220 2.73820 0.33884  -0.21712 0.08139  56  PRO A N   
399  C CA  . PRO A 62  ? 2.97342 3.02384 2.87064 0.35138  -0.23161 0.08060  56  PRO A CA  
400  C C   . PRO A 62  ? 3.09649 3.16165 3.00130 0.35341  -0.22640 0.07081  56  PRO A C   
401  O O   . PRO A 62  ? 3.06400 3.14109 2.97993 0.36269  -0.23627 0.06885  56  PRO A O   
402  C CB  . PRO A 62  ? 3.02145 3.05050 2.87744 0.35532  -0.24181 0.08752  56  PRO A CB  
403  C CG  . PRO A 62  ? 2.95538 2.97136 2.78607 0.34289  -0.23073 0.08836  56  PRO A CG  
404  C CD  . PRO A 62  ? 2.67877 2.70123 2.53596 0.33268  -0.21541 0.08517  56  PRO A CD  
405  N N   . LEU A 63  ? 3.10366 3.16729 3.00119 0.34299  -0.20961 0.06354  57  LEU A N   
406  C CA  . LEU A 63  ? 3.16093 3.23375 3.05684 0.34129  -0.20201 0.05267  57  LEU A CA  
407  C C   . LEU A 63  ? 3.27448 3.36780 3.22129 0.34344  -0.19285 0.04451  57  LEU A C   
408  O O   . LEU A 63  ? 3.23236 3.33222 3.18244 0.34035  -0.18224 0.03333  57  LEU A O   
409  C CB  . LEU A 63  ? 3.01246 3.07318 2.87680 0.32481  -0.18493 0.04627  57  LEU A CB  
410  C CG  . LEU A 63  ? 2.92031 2.96017 2.73456 0.31929  -0.19476 0.05687  57  LEU A CG  
411  C CD1 . LEU A 63  ? 3.19343 3.22251 2.97462 0.29797  -0.17726 0.05013  57  LEU A CD1 
412  C CD2 . LEU A 63  ? 3.15914 3.19760 2.95132 0.33017  -0.21712 0.06526  57  LEU A CD2 
413  N N   . SER A 64  ? 3.26521 3.36831 3.25197 0.34695  -0.19732 0.05082  58  SER A N   
414  C CA  . SER A 64  ? 3.22406 3.34709 3.26579 0.34787  -0.19067 0.04691  58  SER A CA  
415  C C   . SER A 64  ? 3.21329 3.34977 3.26500 0.35795  -0.20537 0.04609  58  SER A C   
416  O O   . SER A 64  ? 3.23487 3.38656 3.32737 0.35859  -0.19924 0.04117  58  SER A O   
417  C CB  . SER A 64  ? 3.22912 3.35937 3.31161 0.34445  -0.19284 0.05773  58  SER A CB  
418  O OG  . SER A 64  ? 3.33009 3.45772 3.39960 0.34838  -0.21421 0.06912  58  SER A OG  
419  N N   . THR A 65  ? 3.25508 3.38627 3.27402 0.36560  -0.22376 0.05082  59  THR A N   
420  C CA  . THR A 65  ? 3.25952 3.40325 3.28407 0.37438  -0.23733 0.04938  59  THR A CA  
421  C C   . THR A 65  ? 3.21659 3.35085 3.19497 0.38002  -0.24536 0.04781  59  THR A C   
422  O O   . THR A 65  ? 3.13943 3.25764 3.08334 0.37622  -0.24170 0.04935  59  THR A O   
423  C CB  . THR A 65  ? 3.26514 3.41682 3.30923 0.37687  -0.25388 0.05871  59  THR A CB  
424  O OG1 . THR A 65  ? 3.04168 3.17705 3.05502 0.37750  -0.26155 0.06520  59  THR A OG1 
425  C CG2 . THR A 65  ? 3.29953 3.46329 3.39327 0.36906  -0.24983 0.06458  59  THR A CG2 
426  N N   . THR A 66  ? 3.21837 3.36355 3.19816 0.38817  -0.25766 0.04640  60  THR A N   
427  C CA  . THR A 66  ? 3.12180 3.26186 3.06578 0.39400  -0.26693 0.04680  60  THR A CA  
428  C C   . THR A 66  ? 3.09767 3.22526 3.02294 0.40029  -0.27921 0.05600  60  THR A C   
429  O O   . THR A 66  ? 3.06641 3.17985 2.96134 0.40047  -0.28156 0.06104  60  THR A O   
430  C CB  . THR A 66  ? 3.06592 3.22311 3.02075 0.40018  -0.27483 0.04181  60  THR A CB  
431  O OG1 . THR A 66  ? 3.14697 3.31267 3.11906 0.39391  -0.26138 0.03227  60  THR A OG1 
432  C CG2 . THR A 66  ? 2.95079 3.10499 2.87296 0.40587  -0.28570 0.04437  60  THR A CG2 
433  N N   . ARG A 67  ? 3.10648 3.23823 3.05005 0.40365  -0.28680 0.05858  61  ARG A N   
434  C CA  . ARG A 67  ? 3.04318 3.16108 2.97174 0.40864  -0.29488 0.06445  61  ARG A CA  
435  C C   . ARG A 67  ? 3.00352 3.10091 2.91646 0.40306  -0.28866 0.07043  61  ARG A C   
436  O O   . ARG A 67  ? 3.07442 3.15530 2.96752 0.40767  -0.29324 0.07590  61  ARG A O   
437  C CB  . ARG A 67  ? 2.94247 3.06784 2.89043 0.40788  -0.30132 0.06379  61  ARG A CB  
438  C CG  . ARG A 67  ? 3.01591 3.16068 2.97704 0.41252  -0.30900 0.05848  61  ARG A CG  
439  C CD  . ARG A 67  ? 2.84346 2.99296 2.81657 0.40767  -0.31550 0.05809  61  ARG A CD  
440  N NE  . ARG A 67  ? 3.07272 3.24348 3.06343 0.40734  -0.32233 0.05400  61  ARG A NE  
441  C CZ  . ARG A 67  ? 3.04702 3.22494 3.03179 0.41528  -0.32836 0.04914  61  ARG A CZ  
442  N NH1 . ARG A 67  ? 3.04026 3.20692 3.00663 0.42523  -0.32868 0.04856  61  ARG A NH1 
443  N NH2 . ARG A 67  ? 3.20814 3.40549 3.20902 0.41296  -0.33467 0.04591  61  ARG A NH2 
444  N N   . GLY A 68  ? 2.93836 3.03649 2.86325 0.39321  -0.27803 0.07003  62  GLY A N   
445  C CA  . GLY A 68  ? 3.04802 3.12745 2.95721 0.38657  -0.27158 0.07547  62  GLY A CA  
446  C C   . GLY A 68  ? 3.22514 3.29173 3.10201 0.38526  -0.26881 0.07740  62  GLY A C   
447  O O   . GLY A 68  ? 3.26470 3.31193 3.11962 0.38363  -0.27038 0.08471  62  GLY A O   
448  N N   . ALA A 69  ? 3.12568 3.20209 2.99781 0.38372  -0.26520 0.07159  63  ALA A N   
449  C CA  . ALA A 69  ? 2.86093 2.92624 2.69794 0.37765  -0.26427 0.07455  63  ALA A CA  
450  C C   . ALA A 69  ? 3.06472 3.12272 2.88292 0.38720  -0.28146 0.08449  63  ALA A C   
451  O O   . ALA A 69  ? 3.42116 3.46381 3.21153 0.38227  -0.28574 0.09407  63  ALA A O   
452  C CB  . ALA A 69  ? 2.79459 2.87168 2.62977 0.36985  -0.25429 0.06432  63  ALA A CB  
453  N N   . LEU A 70  ? 3.01628 3.08538 2.85182 0.39991  -0.29152 0.08330  64  LEU A N   
454  C CA  . LEU A 70  ? 3.09428 3.15765 2.92156 0.41048  -0.30618 0.09260  64  LEU A CA  
455  C C   . LEU A 70  ? 3.17781 3.22026 3.00324 0.41429  -0.30851 0.10070  64  LEU A C   
456  O O   . LEU A 70  ? 3.14815 3.17753 2.96161 0.41831  -0.31761 0.11241  64  LEU A O   
457  C CB  . LEU A 70  ? 3.22761 3.30877 3.07622 0.42188  -0.31333 0.08704  64  LEU A CB  
458  C CG  . LEU A 70  ? 2.97173 3.07270 2.82176 0.41915  -0.31282 0.07979  64  LEU A CG  
459  C CD1 . LEU A 70  ? 3.34099 3.45911 3.21278 0.42969  -0.32009 0.07450  64  LEU A CD1 
460  C CD2 . LEU A 70  ? 3.01479 3.11305 2.83679 0.41349  -0.31884 0.08750  64  LEU A CD2 
461  N N   . ILE A 71  ? 3.22866 3.26731 3.06736 0.41189  -0.30095 0.09580  65  ILE A N   
462  C CA  . ILE A 71  ? 3.27070 3.28692 3.10425 0.41225  -0.30055 0.10203  65  ILE A CA  
463  C C   . ILE A 71  ? 3.29072 3.28997 3.09947 0.40259  -0.29765 0.11071  65  ILE A C   
464  O O   . ILE A 71  ? 3.30957 3.28813 3.10716 0.40482  -0.30251 0.12082  65  ILE A O   
465  C CB  . ILE A 71  ? 3.29975 3.31723 3.14980 0.40738  -0.29383 0.09544  65  ILE A CB  
466  C CG1 . ILE A 71  ? 3.27486 3.30760 3.14503 0.41368  -0.29797 0.08776  65  ILE A CG1 
467  C CG2 . ILE A 71  ? 3.20123 3.19339 3.04204 0.40475  -0.29157 0.10076  65  ILE A CG2 
468  C CD1 . ILE A 71  ? 3.16055 3.18373 3.03138 0.42543  -0.30380 0.08891  65  ILE A CD1 
469  N N   . PHE A 72  ? 3.32077 3.32775 3.12177 0.39072  -0.28870 0.10655  66  PHE A N   
470  C CA  . PHE A 72  ? 3.45911 3.45095 3.23320 0.37791  -0.28421 0.11315  66  PHE A CA  
471  C C   . PHE A 72  ? 3.48632 3.47186 3.23515 0.37660  -0.29596 0.12442  66  PHE A C   
472  O O   . PHE A 72  ? 3.52984 3.49707 3.25497 0.36823  -0.29908 0.13574  66  PHE A O   
473  C CB  . PHE A 72  ? 3.53558 3.53799 3.31180 0.36425  -0.26790 0.10300  66  PHE A CB  
474  C CG  . PHE A 72  ? 3.54100 3.52771 3.29345 0.34857  -0.25876 0.10678  66  PHE A CG  
475  C CD1 . PHE A 72  ? 3.39992 3.36909 3.14882 0.34725  -0.25908 0.11389  66  PHE A CD1 
476  C CD2 . PHE A 72  ? 3.61487 3.60368 3.34692 0.33289  -0.24831 0.10195  66  PHE A CD2 
477  C CE1 . PHE A 72  ? 3.37375 3.32891 3.10012 0.33186  -0.25076 0.11742  66  PHE A CE1 
478  C CE2 . PHE A 72  ? 3.61230 3.58680 3.32068 0.31598  -0.23849 0.10425  66  PHE A CE2 
479  C CZ  . PHE A 72  ? 3.48167 3.44001 3.18787 0.31608  -0.24042 0.11257  66  PHE A CZ  
480  N N   . ASP A 73  ? 3.51253 3.51341 3.26603 0.38307  -0.30407 0.12329  67  ASP A N   
481  C CA  . ASP A 73  ? 3.47191 3.46914 3.20482 0.38093  -0.31878 0.13739  67  ASP A CA  
482  C C   . ASP A 73  ? 3.56247 3.54652 3.30702 0.39526  -0.33332 0.15193  67  ASP A C   
483  O O   . ASP A 73  ? 3.66203 3.63264 3.39013 0.39052  -0.34513 0.16955  67  ASP A O   
484  C CB  . ASP A 73  ? 3.43118 3.44998 3.16624 0.38195  -0.32281 0.13195  67  ASP A CB  
485  C CG  . ASP A 73  ? 3.64863 3.67292 3.35856 0.36156  -0.31133 0.12381  67  ASP A CG  
486  O OD1 . ASP A 73  ? 3.87400 3.88413 3.55378 0.34417  -0.30816 0.12997  67  ASP A OD1 
487  O OD2 . ASP A 73  ? 3.68771 3.72939 3.40773 0.36157  -0.30433 0.11054  67  ASP A OD2 
488  N N   . LYS A 74  ? 3.50622 3.49331 3.28043 0.41124  -0.33213 0.14505  68  LYS A N   
489  C CA  . LYS A 74  ? 3.37168 3.34349 3.16193 0.42463  -0.34056 0.15536  68  LYS A CA  
490  C C   . LYS A 74  ? 3.32329 3.26827 3.10206 0.41892  -0.33713 0.16307  68  LYS A C   
491  O O   . LYS A 74  ? 3.17559 3.10305 2.95760 0.42408  -0.34681 0.17859  68  LYS A O   
492  C CB  . LYS A 74  ? 3.35257 3.33208 3.17294 0.43839  -0.33560 0.14238  68  LYS A CB  
493  C CG  . LYS A 74  ? 3.36517 3.36894 3.20042 0.44671  -0.34195 0.13778  68  LYS A CG  
494  C CD  . LYS A 74  ? 3.12489 3.12826 2.96640 0.45466  -0.35788 0.15490  68  LYS A CD  
495  C CE  . LYS A 74  ? 3.15615 3.18437 3.01419 0.46301  -0.36421 0.15046  68  LYS A CE  
496  N NZ  . LYS A 74  ? 3.83572 3.88325 3.67484 0.45166  -0.36221 0.14226  68  LYS A NZ  
497  N N   . LEU A 75  ? 3.43566 3.37729 3.20415 0.40811  -0.32372 0.15351  69  LEU A N   
498  C CA  . LEU A 75  ? 3.48836 3.40537 3.24217 0.40015  -0.32013 0.16074  69  LEU A CA  
499  C C   . LEU A 75  ? 3.49479 3.40344 3.21770 0.38585  -0.32701 0.17518  69  LEU A C   
500  O O   . LEU A 75  ? 3.46676 3.35252 3.17859 0.38220  -0.33200 0.18870  69  LEU A O   
501  C CB  . LEU A 75  ? 3.47708 3.39585 3.23164 0.39143  -0.30460 0.14766  69  LEU A CB  
502  C CG  . LEU A 75  ? 3.41254 3.30640 3.15579 0.38396  -0.29945 0.15280  69  LEU A CG  
503  C CD1 . LEU A 75  ? 3.30045 3.17437 3.05782 0.39583  -0.30271 0.15617  69  LEU A CD1 
504  C CD2 . LEU A 75  ? 3.55845 3.45971 3.30515 0.37327  -0.28561 0.14184  69  LEU A CD2 
505  N N   . LYS A 76  ? 3.57048 3.49614 3.27751 0.37538  -0.32698 0.17241  70  LYS A N   
506  C CA  . LYS A 76  ? 3.53578 3.45404 3.20822 0.35723  -0.33418 0.18608  70  LYS A CA  
507  C C   . LYS A 76  ? 3.55797 3.46860 3.23225 0.36327  -0.35662 0.20884  70  LYS A C   
508  O O   . LYS A 76  ? 3.67261 3.56518 3.32687 0.35238  -0.36664 0.22727  70  LYS A O   
509  C CB  . LYS A 76  ? 3.71761 3.65500 3.37226 0.34254  -0.32640 0.17516  70  LYS A CB  
510  C CG  . LYS A 76  ? 3.67975 3.61066 3.29266 0.31865  -0.33349 0.18795  70  LYS A CG  
511  C CD  . LYS A 76  ? 3.70983 3.65715 3.30436 0.30184  -0.32051 0.17263  70  LYS A CD  
512  C CE  . LYS A 76  ? 3.43559 3.37603 2.98269 0.27331  -0.32769 0.18485  70  LYS A CE  
513  N NZ  . LYS A 76  ? 3.10778 3.04994 2.65123 0.27626  -0.35559 0.20837  70  LYS A NZ  
514  N N   . GLU A 77  ? 3.52683 3.45169 3.22777 0.37990  -0.36545 0.20925  71  GLU A N   
515  C CA  . GLU A 77  ? 3.59605 3.51611 3.30987 0.38789  -0.38694 0.23227  71  GLU A CA  
516  C C   . GLU A 77  ? 3.51701 3.41204 3.25261 0.40018  -0.38962 0.24264  71  GLU A C   
517  O O   . GLU A 77  ? 3.41704 3.29916 3.15617 0.39959  -0.40697 0.26704  71  GLU A O   
518  C CB  . GLU A 77  ? 3.55452 3.49705 3.29677 0.40370  -0.39296 0.22804  71  GLU A CB  
519  C CG  . GLU A 77  ? 3.74064 3.68309 3.50358 0.41217  -0.41573 0.25306  71  GLU A CG  
520  C CD  . GLU A 77  ? 3.84075 3.80747 3.63201 0.42676  -0.42044 0.24784  71  GLU A CD  
521  O OE1 . GLU A 77  ? 3.76756 3.75054 3.55803 0.42877  -0.40689 0.22501  71  GLU A OE1 
522  O OE2 . GLU A 77  ? 3.90720 3.87723 3.72422 0.43587  -0.43822 0.26774  71  GLU A OE2 
523  N N   . ALA A 78  ? 3.46784 3.35499 3.21865 0.40952  -0.37300 0.22546  72  ALA A N   
524  C CA  . ALA A 78  ? 3.25587 3.11638 3.02514 0.41918  -0.37194 0.23211  72  ALA A CA  
525  C C   . ALA A 78  ? 3.31981 3.15712 3.05995 0.40299  -0.37462 0.24583  72  ALA A C   
526  O O   . ALA A 78  ? 3.26015 3.07493 3.01143 0.40733  -0.38414 0.26382  72  ALA A O   
527  C CB  . ALA A 78  ? 3.11457 2.97277 2.90088 0.42799  -0.35307 0.20936  72  ALA A CB  
528  N N   . SER A 79  ? 3.45337 3.29546 3.15873 0.38389  -0.36554 0.23761  73  SER A N   
529  C CA  . SER A 79  ? 3.41377 3.23521 3.08817 0.36581  -0.36661 0.24909  73  SER A CA  
530  C C   . SER A 79  ? 3.47999 3.29640 3.13520 0.35324  -0.38832 0.27579  73  SER A C   
531  O O   . SER A 79  ? 3.34391 3.13823 2.98114 0.34152  -0.39505 0.29203  73  SER A O   
532  C CB  . SER A 79  ? 3.32804 3.15836 2.97445 0.34780  -0.34905 0.23211  73  SER A CB  
533  O OG  . SER A 79  ? 3.30279 3.15594 2.93372 0.33737  -0.34878 0.22657  73  SER A OG  
534  N N   . GLU A 80  ? 3.51979 3.35620 3.17731 0.35333  -0.40064 0.28205  74  GLU A N   
535  C CA  . GLU A 80  ? 3.52275 3.35749 3.16101 0.33776  -0.42416 0.30982  74  GLU A CA  
536  C C   . GLU A 80  ? 3.61183 3.43604 3.28926 0.35471  -0.44554 0.33574  74  GLU A C   
537  O O   . GLU A 80  ? 3.85205 3.67392 3.51990 0.34186  -0.46928 0.36448  74  GLU A O   
538  C CB  . GLU A 80  ? 3.60737 3.46879 3.22715 0.32615  -0.42769 0.30528  74  GLU A CB  
539  C CG  . GLU A 80  ? 3.69653 3.56712 3.27965 0.30645  -0.40584 0.28132  74  GLU A CG  
540  C CD  . GLU A 80  ? 3.64956 3.54457 3.21819 0.29649  -0.40609 0.27353  74  GLU A CD  
541  O OE1 . GLU A 80  ? 3.59716 3.50398 3.18383 0.30573  -0.42422 0.28666  74  GLU A OE1 
542  O OE2 . GLU A 80  ? 3.68332 3.58544 3.22476 0.27909  -0.38714 0.25402  74  GLU A OE2 
543  N N   . LYS A 81  ? 3.55724 3.37485 3.27993 0.38131  -0.43739 0.32688  75  LYS A N   
544  C CA  . LYS A 81  ? 3.51786 3.32387 3.28725 0.39963  -0.45276 0.34849  75  LYS A CA  
545  C C   . LYS A 81  ? 3.45787 3.22976 3.23830 0.40356  -0.44953 0.35660  75  LYS A C   
546  O O   . LYS A 81  ? 3.45716 3.21493 3.28104 0.41875  -0.46014 0.37491  75  LYS A O   
547  C CB  . LYS A 81  ? 3.55956 3.38031 3.37604 0.42586  -0.44405 0.33237  75  LYS A CB  
548  C CG  . LYS A 81  ? 3.61943 3.47367 3.42897 0.42387  -0.44734 0.32408  75  LYS A CG  
549  C CD  . LYS A 81  ? 3.72343 3.58861 3.52258 0.41007  -0.47515 0.35432  75  LYS A CD  
550  C CE  . LYS A 81  ? 3.64089 3.53760 3.42500 0.40399  -0.47672 0.34432  75  LYS A CE  
551  N NZ  . LYS A 81  ? 3.71648 3.62988 3.54503 0.42929  -0.46874 0.32836  75  LYS A NZ  
552  N N   . GLY A 82  ? 3.48753 3.24574 3.23291 0.39020  -0.43458 0.34372  76  GLY A N   
553  C CA  . GLY A 82  ? 3.49743 3.22243 3.24798 0.39164  -0.43003 0.34951  76  GLY A CA  
554  C C   . GLY A 82  ? 3.36475 3.07997 3.12260 0.40130  -0.40340 0.32060  76  GLY A C   
555  O O   . GLY A 82  ? 3.32315 3.00930 3.08349 0.40150  -0.39744 0.32308  76  GLY A O   
556  N N   . ILE A 83  ? 3.34412 3.08153 3.10463 0.40728  -0.38801 0.29450  77  ILE A N   
557  C CA  . ILE A 83  ? 3.34235 3.07212 3.10856 0.41270  -0.36512 0.26927  77  ILE A CA  
558  C C   . ILE A 83  ? 3.40161 3.12796 3.12641 0.39224  -0.35490 0.26119  77  ILE A C   
559  O O   . ILE A 83  ? 3.32969 3.07640 3.02724 0.37824  -0.35509 0.25770  77  ILE A O   
560  C CB  . ILE A 83  ? 3.27457 3.03048 3.06028 0.42438  -0.35517 0.24730  77  ILE A CB  
561  C CG1 . ILE A 83  ? 3.30310 3.06688 3.12916 0.44293  -0.36636 0.25666  77  ILE A CG1 
562  C CG2 . ILE A 83  ? 3.18588 2.93181 2.97935 0.42761  -0.33419 0.22456  77  ILE A CG2 
563  C CD1 . ILE A 83  ? 3.30335 3.03859 3.16797 0.45778  -0.36454 0.26423  77  ILE A CD1 
564  N N   . LYS A 84  ? 3.33936 3.03946 3.06093 0.38963  -0.34458 0.25768  78  LYS A N   
565  C CA  . LYS A 84  ? 3.43734 3.13317 3.12420 0.37048  -0.33443 0.25108  78  LYS A CA  
566  C C   . LYS A 84  ? 3.48276 3.20164 3.17055 0.36912  -0.31809 0.22642  78  LYS A C   
567  O O   . LYS A 84  ? 3.46488 3.17853 3.17042 0.37662  -0.30698 0.21262  78  LYS A O   
568  C CB  . LYS A 84  ? 3.53000 3.19005 3.21423 0.36769  -0.32967 0.25629  78  LYS A CB  
569  C CG  . LYS A 84  ? 3.83141 3.48548 3.47995 0.34666  -0.32117 0.25316  78  LYS A CG  
570  C CD  . LYS A 84  ? 3.63628 3.25305 3.28129 0.34353  -0.31790 0.25982  78  LYS A CD  
571  C CE  . LYS A 84  ? 3.05373 2.66561 2.66327 0.32162  -0.31047 0.25834  78  LYS A CE  
572  N NZ  . LYS A 84  ? 2.82541 2.40012 2.42902 0.31724  -0.30742 0.26482  78  LYS A NZ  
573  N N   . ILE A 85  ? 3.46236 3.20602 3.13198 0.35773  -0.31630 0.22125  79  ILE A N   
574  C CA  . ILE A 85  ? 3.40758 3.17581 3.08360 0.35600  -0.30291 0.20104  79  ILE A CA  
575  C C   . ILE A 85  ? 3.37991 3.14569 3.03538 0.33771  -0.29132 0.19657  79  ILE A C   
576  O O   . ILE A 85  ? 3.43474 3.20091 3.06520 0.32286  -0.29205 0.20318  79  ILE A O   
577  C CB  . ILE A 85  ? 3.50462 3.30308 3.18289 0.35740  -0.30651 0.19665  79  ILE A CB  
578  C CG1 . ILE A 85  ? 3.34767 3.14794 3.04321 0.37294  -0.32122 0.20627  79  ILE A CG1 
579  C CG2 . ILE A 85  ? 3.51594 3.33857 3.21110 0.35936  -0.29448 0.17725  79  ILE A CG2 
580  C CD1 . ILE A 85  ? 3.18231 2.98071 2.91088 0.39117  -0.31797 0.19732  79  ILE A CD1 
581  N N   . ILE A 86  ? 3.31902 3.08273 2.98472 0.33657  -0.28045 0.18568  80  ILE A N   
582  C CA  . ILE A 86  ? 3.42255 3.18732 3.07635 0.31977  -0.26943 0.18174  80  ILE A CA  
583  C C   . ILE A 86  ? 3.28465 3.07522 2.96079 0.31951  -0.26065 0.16726  80  ILE A C   
584  O O   . ILE A 86  ? 3.32549 3.11488 3.01796 0.32659  -0.26016 0.16089  80  ILE A O   
585  C CB  . ILE A 86  ? 3.47160 3.20483 3.11395 0.31368  -0.26725 0.18763  80  ILE A CB  
586  C CG1 . ILE A 86  ? 3.33190 3.03957 2.95371 0.31188  -0.27739 0.20478  80  ILE A CG1 
587  C CG2 . ILE A 86  ? 3.45798 3.19650 3.09306 0.29628  -0.25603 0.18323  80  ILE A CG2 
588  C CD1 . ILE A 86  ? 3.48409 3.15848 3.09371 0.30512  -0.27511 0.21129  80  ILE A CD1 
589  N N   . VAL A 87  ? 3.00873 2.82193 2.68703 0.30981  -0.25322 0.16235  81  VAL A N   
590  C CA  . VAL A 87  ? 3.13919 2.97929 2.84462 0.30864  -0.24632 0.15168  81  VAL A CA  
591  C C   . VAL A 87  ? 3.28382 3.12568 2.99130 0.29223  -0.23637 0.15222  81  VAL A C   
592  O O   . VAL A 87  ? 3.23013 3.07063 2.92394 0.28108  -0.22953 0.15475  81  VAL A O   
593  C CB  . VAL A 87  ? 3.14815 3.01496 2.86493 0.31216  -0.24434 0.14506  81  VAL A CB  
594  C CG1 . VAL A 87  ? 3.30607 3.19994 3.05650 0.31079  -0.23799 0.13622  81  VAL A CG1 
595  C CG2 . VAL A 87  ? 3.12800 2.99432 2.84291 0.32735  -0.25566 0.14622  81  VAL A CG2 
596  N N   . LEU A 88  ? 3.26450 3.10984 2.98853 0.28854  -0.23559 0.15032  82  LEU A N   
597  C CA  . LEU A 88  ? 3.10368 2.95438 2.83596 0.27224  -0.22828 0.15294  82  LEU A CA  
598  C C   . LEU A 88  ? 3.22754 3.11270 2.99840 0.26982  -0.22422 0.14836  82  LEU A C   
599  O O   . LEU A 88  ? 3.36013 3.25880 3.15014 0.27658  -0.23018 0.14456  82  LEU A O   
600  C CB  . LEU A 88  ? 2.98919 2.81982 2.71270 0.26482  -0.23133 0.15658  82  LEU A CB  
601  C CG  . LEU A 88  ? 3.19492 2.98823 2.88528 0.26438  -0.23306 0.16211  82  LEU A CG  
602  C CD1 . LEU A 88  ? 3.18046 2.95571 2.86375 0.25258  -0.23239 0.16342  82  LEU A CD1 
603  C CD2 . LEU A 88  ? 3.27727 3.06302 2.94850 0.25630  -0.22861 0.16854  82  LEU A CD2 
604  N N   . LEU A 89  ? 3.29200 3.19101 3.07673 0.25957  -0.21351 0.14895  83  LEU A N   
605  C CA  . LEU A 89  ? 3.28469 3.21574 3.11467 0.25651  -0.20810 0.14655  83  LEU A CA  
606  C C   . LEU A 89  ? 3.27967 3.21703 3.12645 0.24006  -0.19897 0.15278  83  LEU A C   
607  O O   . LEU A 89  ? 3.38405 3.30445 3.20491 0.23186  -0.19235 0.15504  83  LEU A O   
608  C CB  . LEU A 89  ? 3.26780 3.21557 3.11025 0.26446  -0.19995 0.13697  83  LEU A CB  
609  C CG  . LEU A 89  ? 3.41168 3.34961 3.22771 0.25942  -0.18789 0.13272  83  LEU A CG  
610  C CD1 . LEU A 89  ? 3.29887 3.25043 3.14004 0.24555  -0.16939 0.13039  83  LEU A CD1 
611  C CD2 . LEU A 89  ? 3.44038 3.38373 3.24797 0.26908  -0.18768 0.12414  83  LEU A CD2 
612  N N   . ASP A 90  ? 2.96339 2.92599 2.85571 0.23432  -0.19974 0.15710  84  ASP A N   
613  C CA  . ASP A 90  ? 2.95884 2.93265 2.87802 0.21897  -0.19143 0.16475  84  ASP A CA  
614  C C   . ASP A 90  ? 3.04593 3.02932 2.97955 0.21802  -0.17124 0.15653  84  ASP A C   
615  O O   . ASP A 90  ? 3.08819 3.08157 3.03225 0.22769  -0.16416 0.14585  84  ASP A O   
616  C CB  . ASP A 90  ? 2.76841 2.76964 2.73969 0.21242  -0.19953 0.17448  84  ASP A CB  
617  C CG  . ASP A 90  ? 2.85189 2.86503 2.85400 0.19512  -0.19449 0.18649  84  ASP A CG  
618  O OD1 . ASP A 90  ? 2.89902 2.92580 2.93143 0.19363  -0.17741 0.18312  84  ASP A OD1 
619  O OD2 . ASP A 90  ? 2.62523 2.63365 2.62096 0.18146  -0.20660 0.19892  84  ASP A OD2 
620  N N   . GLU A 91  ? 3.00487 2.98448 2.93777 0.20421  -0.16054 0.16062  85  GLU A N   
621  C CA  . GLU A 91  ? 2.90419 2.88925 2.84490 0.19910  -0.13796 0.15098  85  GLU A CA  
622  C C   . GLU A 91  ? 2.99771 3.01473 3.00410 0.20193  -0.12434 0.14512  85  GLU A C   
623  O O   . GLU A 91  ? 2.95781 2.97957 2.97365 0.19796  -0.10178 0.13297  85  GLU A O   
624  C CB  . GLU A 91  ? 3.03408 3.01040 2.96493 0.18213  -0.12945 0.15743  85  GLU A CB  
625  C CG  . GLU A 91  ? 3.08450 3.05176 2.99131 0.17361  -0.10814 0.14621  85  GLU A CG  
626  C CD  . GLU A 91  ? 3.17004 3.12530 3.05874 0.15632  -0.10205 0.15316  85  GLU A CD  
627  O OE1 . GLU A 91  ? 3.58253 3.53738 3.47982 0.15124  -0.11414 0.16692  85  GLU A OE1 
628  O OE2 . GLU A 91  ? 2.71251 2.65834 2.57579 0.14557  -0.08519 0.14485  85  GLU A OE2 
629  N N   . ARG A 92  ? 2.95266 2.99054 3.00469 0.20697  -0.13666 0.15328  86  ARG A N   
630  C CA  . ARG A 92  ? 2.88656 2.95394 3.00600 0.21147  -0.12611 0.14948  86  ARG A CA  
631  C C   . ARG A 92  ? 2.89022 2.95945 3.00334 0.22653  -0.12761 0.13709  86  ARG A C   
632  O O   . ARG A 92  ? 3.18768 3.27799 3.35298 0.23108  -0.11633 0.13104  86  ARG A O   
633  C CB  . ARG A 92  ? 2.76629 2.85745 2.94339 0.20631  -0.14085 0.16829  86  ARG A CB  
634  C CG  . ARG A 92  ? 2.92673 3.01889 3.11398 0.18949  -0.14089 0.18274  86  ARG A CG  
635  C CD  . ARG A 92  ? 3.51378 3.63543 3.77091 0.18131  -0.15326 0.20325  86  ARG A CD  
636  N NE  . ARG A 92  ? 3.53770 3.66146 3.80457 0.16366  -0.15390 0.21828  86  ARG A NE  
637  C CZ  . ARG A 92  ? 3.39045 3.54063 3.72030 0.15181  -0.16337 0.23954  86  ARG A CZ  
638  N NH1 . ARG A 92  ? 3.26269 3.43957 3.65428 0.15534  -0.17371 0.24956  86  ARG A NH1 
639  N NH2 . ARG A 92  ? 3.28970 3.44002 3.62183 0.13484  -0.16380 0.25280  86  ARG A NH2 
640  N N   . GLY A 93  ? 2.84499 2.89285 2.89929 0.23422  -0.14086 0.13372  87  GLY A N   
641  C CA  . GLY A 93  ? 2.74383 2.79144 2.78480 0.24701  -0.14112 0.12160  87  GLY A CA  
642  C C   . GLY A 93  ? 3.03225 3.06175 3.02657 0.24406  -0.12632 0.10871  87  GLY A C   
643  O O   . GLY A 93  ? 2.90613 2.92492 2.86339 0.25200  -0.13282 0.10268  87  GLY A O   
644  N N   . LYS A 94  ? 3.26669 3.29345 3.26283 0.23041  -0.10675 0.10545  88  LYS A N   
645  C CA  . LYS A 94  ? 3.33139 3.33957 3.27836 0.22086  -0.09241 0.09500  88  LYS A CA  
646  C C   . LYS A 94  ? 3.42055 3.43749 3.37828 0.21935  -0.07128 0.07673  88  LYS A C   
647  O O   . LYS A 94  ? 3.43023 3.43241 3.34402 0.20745  -0.05864 0.06708  88  LYS A O   
648  C CB  . LYS A 94  ? 2.94728 2.94940 2.89152 0.20391  -0.07828 0.09783  88  LYS A CB  
649  C CG  . LYS A 94  ? 2.67508 2.64929 2.54995 0.19219  -0.07739 0.09701  88  LYS A CG  
650  C CD  . LYS A 94  ? 2.76589 2.73521 2.64066 0.17559  -0.06600 0.10169  88  LYS A CD  
651  C CE  . LYS A 94  ? 3.02030 2.96039 2.82470 0.16282  -0.06900 0.10418  88  LYS A CE  
652  N NZ  . LYS A 94  ? 3.08837 3.02313 2.89069 0.14623  -0.05920 0.10941  88  LYS A NZ  
653  N N   . ARG A 95  ? 3.39532 3.43471 3.40863 0.22882  -0.06722 0.07208  89  ARG A N   
654  C CA  . ARG A 95  ? 3.50167 3.54801 3.52827 0.22642  -0.04443 0.05306  89  ARG A CA  
655  C C   . ARG A 95  ? 3.58534 3.61778 3.55447 0.23028  -0.05487 0.04717  89  ARG A C   
656  O O   . ARG A 95  ? 3.63551 3.65853 3.57196 0.21762  -0.03731 0.03302  89  ARG A O   
657  C CB  . ARG A 95  ? 3.29135 3.36435 3.39632 0.23652  -0.03971 0.05194  89  ARG A CB  
658  C CG  . ARG A 95  ? 3.17309 3.26343 3.34485 0.23211  -0.03105 0.06100  89  ARG A CG  
659  C CD  . ARG A 95  ? 3.25684 3.37381 3.50987 0.24200  -0.03045 0.06384  89  ARG A CD  
660  N NE  . ARG A 95  ? 3.56602 3.70185 3.88900 0.23708  -0.02547 0.07675  89  ARG A NE  
661  C CZ  . ARG A 95  ? 3.78845 3.93347 4.12977 0.23807  -0.05126 0.09975  89  ARG A CZ  
662  N NH1 . ARG A 95  ? 3.55479 3.69057 3.85027 0.24394  -0.08125 0.11008  89  ARG A NH1 
663  N NH2 . ARG A 95  ? 4.14883 4.31273 4.55696 0.23126  -0.04605 0.11266  89  ARG A NH2 
664  N N   . ASN A 96  ? 3.48340 3.51467 3.43959 0.24561  -0.08305 0.05812  90  ASN A N   
665  C CA  . ASN A 96  ? 3.38934 3.41006 3.29803 0.25098  -0.09586 0.05556  90  ASN A CA  
666  C C   . ASN A 96  ? 3.30178 3.29712 3.14391 0.24274  -0.10585 0.06278  90  ASN A C   
667  O O   . ASN A 96  ? 3.41161 3.39787 3.21468 0.24564  -0.11835 0.06392  90  ASN A O   
668  C CB  . ASN A 96  ? 3.29834 3.32813 3.22274 0.27019  -0.12060 0.06398  90  ASN A CB  
669  C CG  . ASN A 96  ? 3.36971 3.42434 3.35699 0.27760  -0.11434 0.05864  90  ASN A CG  
670  O OD1 . ASN A 96  ? 3.40899 3.47640 3.43665 0.28360  -0.12494 0.06883  90  ASN A OD1 
671  N ND2 . ASN A 96  ? 3.30197 3.36281 3.29726 0.27524  -0.09758 0.04339  90  ASN A ND2 
672  N N   . LEU A 97  ? 3.28348 3.26774 3.11420 0.23191  -0.10156 0.06913  91  LEU A N   
673  C CA  . LEU A 97  ? 3.31328 3.27232 3.08473 0.22467  -0.11404 0.07919  91  LEU A CA  
674  C C   . LEU A 97  ? 3.25642 3.20467 2.97991 0.20936  -0.10655 0.07179  91  LEU A C   
675  O O   . LEU A 97  ? 2.81964 2.75217 2.49869 0.20986  -0.12563 0.08195  91  LEU A O   
676  C CB  . LEU A 97  ? 3.39600 3.34620 3.16607 0.21301  -0.10740 0.08563  91  LEU A CB  
677  C CG  . LEU A 97  ? 3.43940 3.36207 3.15352 0.20585  -0.12174 0.09854  91  LEU A CG  
678  C CD1 . LEU A 97  ? 3.24712 3.16008 2.95192 0.22442  -0.14940 0.11156  91  LEU A CD1 
679  C CD2 . LEU A 97  ? 3.33548 3.25121 3.05112 0.19289  -0.11277 0.10335  91  LEU A CD2 
680  N N   . GLY A 98  ? 3.33038 3.28653 3.06343 0.19380  -0.07850 0.05462  92  GLY A N   
681  C CA  . GLY A 98  ? 3.21253 3.15861 2.89660 0.17440  -0.06980 0.04599  92  GLY A CA  
682  C C   . GLY A 98  ? 3.17269 3.12401 2.84715 0.18458  -0.08353 0.04484  92  GLY A C   
683  O O   . GLY A 98  ? 3.07428 3.01421 2.69753 0.17070  -0.08985 0.04671  92  GLY A O   
684  N N   . GLU A 99  ? 3.31249 3.28164 3.03520 0.20690  -0.08958 0.04320  93  GLU A N   
685  C CA  . GLU A 99  ? 3.26471 3.24055 2.98206 0.21814  -0.10349 0.04246  93  GLU A CA  
686  C C   . GLU A 99  ? 3.24955 3.21589 2.94243 0.23284  -0.13677 0.06207  93  GLU A C   
687  O O   . GLU A 99  ? 2.88599 2.84835 2.54704 0.23205  -0.15057 0.06651  93  GLU A O   
688  C CB  . GLU A 99  ? 3.29938 3.29795 3.07894 0.23452  -0.09660 0.03324  93  GLU A CB  
689  C CG  . GLU A 99  ? 3.38240 3.38972 3.16529 0.25221  -0.11724 0.03676  93  GLU A CG  
690  C CD  . GLU A 99  ? 3.14983 3.17907 2.99519 0.26703  -0.11282 0.03040  93  GLU A CD  
691  O OE1 . GLU A 99  ? 2.93015 2.96869 2.81312 0.25988  -0.08754 0.01741  93  GLU A OE1 
692  O OE2 . GLU A 99  ? 2.92775 2.96478 2.78686 0.28488  -0.13426 0.03880  93  GLU A OE2 
693  N N   . LEU A 100 ? 3.36001 3.32228 3.06897 0.24504  -0.14902 0.07397  94  LEU A N   
694  C CA  . LEU A 100 ? 3.08438 3.03628 2.77770 0.25987  -0.17669 0.09031  94  LEU A CA  
695  C C   . LEU A 100 ? 3.01860 2.94847 2.65850 0.24717  -0.18779 0.10281  94  LEU A C   
696  O O   . LEU A 100 ? 3.09247 3.01719 2.71416 0.25447  -0.20789 0.11344  94  LEU A O   
697  C CB  . LEU A 100 ? 2.95908 2.90917 2.67953 0.27133  -0.18318 0.09772  94  LEU A CB  
698  C CG  . LEU A 100 ? 3.03062 3.00279 2.80530 0.28022  -0.17552 0.08998  94  LEU A CG  
699  C CD1 . LEU A 100 ? 3.24075 3.20878 3.03323 0.28339  -0.18111 0.09888  94  LEU A CD1 
700  C CD2 . LEU A 100 ? 3.01787 3.00441 2.80994 0.29602  -0.18663 0.08696  94  LEU A CD2 
701  N N   . GLN A 101 ? 2.96634 2.88370 2.58301 0.22723  -0.17578 0.10319  95  GLN A N   
702  C CA  . GLN A 101 ? 3.05727 2.95303 2.62267 0.21208  -0.18800 0.11760  95  GLN A CA  
703  C C   . GLN A 101 ? 3.16415 3.06110 2.69368 0.19524  -0.18859 0.11536  95  GLN A C   
704  O O   . GLN A 101 ? 3.08945 2.97263 2.58169 0.18744  -0.20847 0.13249  95  GLN A O   
705  C CB  . GLN A 101 ? 3.30548 3.18830 2.85397 0.19253  -0.17400 0.11773  95  GLN A CB  
706  C CG  . GLN A 101 ? 3.51337 3.39202 3.08966 0.20526  -0.17612 0.12316  95  GLN A CG  
707  C CD  . GLN A 101 ? 3.61963 3.48767 3.18093 0.18496  -0.16107 0.12261  95  GLN A CD  
708  O OE1 . GLN A 101 ? 3.57572 3.44582 3.11985 0.16258  -0.14100 0.11164  95  GLN A OE1 
709  N NE2 . GLN A 101 ? 3.60855 3.46437 3.17512 0.19102  -0.16926 0.13342  95  GLN A NE2 
710  N N   . SER A 102 ? 3.31551 3.22822 2.85681 0.18796  -0.16747 0.09551  96  SER A N   
711  C CA  . SER A 102 ? 3.39661 3.30977 2.90042 0.16830  -0.16590 0.09139  96  SER A CA  
712  C C   . SER A 102 ? 3.38584 3.30507 2.88965 0.18487  -0.19231 0.10316  96  SER A C   
713  O O   . SER A 102 ? 3.26981 3.18363 2.73267 0.16859  -0.20479 0.11252  96  SER A O   
714  C CB  . SER A 102 ? 3.18819 3.11478 2.70902 0.15668  -0.13302 0.06466  96  SER A CB  
715  O OG  . SER A 102 ? 3.08337 3.00515 2.60738 0.13986  -0.10629 0.05325  96  SER A OG  
716  N N   . HIS A 103 ? 3.40665 3.33765 2.95542 0.21486  -0.20138 0.10361  97  HIS A N   
717  C CA  . HIS A 103 ? 3.47803 3.41646 3.03262 0.23202  -0.22440 0.11324  97  HIS A CA  
718  C C   . HIS A 103 ? 3.43908 3.36384 2.98972 0.24553  -0.25149 0.13679  97  HIS A C   
719  O O   . HIS A 103 ? 3.47432 3.40119 3.01980 0.25290  -0.27244 0.14959  97  HIS A O   
720  C CB  . HIS A 103 ? 3.47136 3.43014 3.07588 0.25501  -0.21901 0.10011  97  HIS A CB  
721  C CG  . HIS A 103 ? 3.70768 3.67825 3.31610 0.26705  -0.23549 0.10353  97  HIS A CG  
722  N ND1 . HIS A 103 ? 3.96264 3.93438 3.58926 0.28990  -0.25740 0.11625  97  HIS A ND1 
723  C CD2 . HIS A 103 ? 3.96566 3.94712 3.56239 0.25825  -0.23198 0.09518  97  HIS A CD2 
724  C CE1 . HIS A 103 ? 4.21482 4.19933 3.84260 0.29553  -0.26751 0.11644  97  HIS A CE1 
725  N NE2 . HIS A 103 ? 4.41638 4.40690 4.02485 0.27645  -0.25340 0.10437  97  HIS A NE2 
726  N N   . CYS A 104 ? 3.27977 3.19036 2.83537 0.24853  -0.25080 0.14289  98  CYS A N   
727  C CA  . CYS A 104 ? 3.19607 3.09016 2.75164 0.26106  -0.27300 0.16367  98  CYS A CA  
728  C C   . CYS A 104 ? 3.23243 3.10467 2.76044 0.24394  -0.27091 0.17314  98  CYS A C   
729  O O   . CYS A 104 ? 3.09991 2.96566 2.64297 0.24831  -0.26131 0.16896  98  CYS A O   
730  C CB  . CYS A 104 ? 3.33832 3.23694 2.93748 0.28828  -0.27547 0.16013  98  CYS A CB  
731  S SG  . CYS A 104 ? 4.09315 4.01652 3.72440 0.30844  -0.28045 0.15084  98  CYS A SG  
732  N N   . PRO A 105 ? 3.34357 3.20410 2.82921 0.22189  -0.28088 0.18728  99  PRO A N   
733  C CA  . PRO A 105 ? 3.48201 3.32068 2.93856 0.20367  -0.28083 0.19810  99  PRO A CA  
734  C C   . PRO A 105 ? 3.47468 3.29370 2.94387 0.22009  -0.29995 0.21798  99  PRO A C   
735  O O   . PRO A 105 ? 3.31021 3.11141 2.76660 0.21110  -0.29655 0.22325  99  PRO A O   
736  C CB  . PRO A 105 ? 3.42052 3.25433 2.82664 0.17267  -0.28865 0.20874  99  PRO A CB  
737  C CG  . PRO A 105 ? 3.15567 3.00258 2.57008 0.18310  -0.30636 0.21591  99  PRO A CG  
738  C CD  . PRO A 105 ? 3.11074 2.97791 2.57059 0.20909  -0.29322 0.19483  99  PRO A CD  
739  N N   . ASP A 106 ? 3.49228 3.31324 2.98767 0.24326  -0.31826 0.22827  100 ASP A N   
740  C CA  . ASP A 106 ? 3.45171 3.25225 2.96448 0.25955  -0.33365 0.24548  100 ASP A CA  
741  C C   . ASP A 106 ? 3.19813 2.99650 2.74461 0.27923  -0.32081 0.23157  100 ASP A C   
742  O O   . ASP A 106 ? 3.03358 2.81069 2.59023 0.28846  -0.32734 0.24180  100 ASP A O   
743  C CB  . ASP A 106 ? 3.41183 3.21506 2.94303 0.27497  -0.35695 0.26251  100 ASP A CB  
744  C CG  . ASP A 106 ? 3.48227 3.28641 2.97935 0.25269  -0.37478 0.28203  100 ASP A CG  
745  O OD1 . ASP A 106 ? 3.41205 3.20228 2.87036 0.22661  -0.37624 0.29178  100 ASP A OD1 
746  O OD2 . ASP A 106 ? 3.79067 3.60974 3.29801 0.25897  -0.38784 0.28820  100 ASP A OD2 
747  N N   . ILE A 107 ? 3.12071 2.93958 2.68491 0.28401  -0.30325 0.20959  101 ILE A N   
748  C CA  . ILE A 107 ? 3.23936 3.05847 2.83264 0.29746  -0.29228 0.19768  101 ILE A CA  
749  C C   . ILE A 107 ? 3.45868 3.26878 3.03741 0.28090  -0.27772 0.19360  101 ILE A C   
750  O O   . ILE A 107 ? 3.54137 3.36153 3.10448 0.26314  -0.26459 0.18547  101 ILE A O   
751  C CB  . ILE A 107 ? 3.21521 3.06164 2.83733 0.30842  -0.28311 0.17951  101 ILE A CB  
752  C CG1 . ILE A 107 ? 3.28114 3.13564 2.92005 0.32617  -0.29761 0.18352  101 ILE A CG1 
753  C CG2 . ILE A 107 ? 2.98634 2.83460 2.63378 0.31489  -0.27209 0.16890  101 ILE A CG2 
754  C CD1 . ILE A 107 ? 3.54455 3.42434 3.21189 0.33736  -0.29067 0.16696  101 ILE A CD1 
755  N N   . ASN A 108 ? 3.48235 3.27300 3.06699 0.28564  -0.27849 0.19839  102 ASN A N   
756  C CA  . ASN A 108 ? 3.58414 3.36463 3.15569 0.27016  -0.26658 0.19680  102 ASN A CA  
757  C C   . ASN A 108 ? 3.49028 3.29019 3.09010 0.27258  -0.25077 0.18026  102 ASN A C   
758  O O   . ASN A 108 ? 3.41107 3.20778 3.03192 0.28354  -0.25167 0.17776  102 ASN A O   
759  C CB  . ASN A 108 ? 3.60195 3.35105 3.16547 0.27233  -0.27533 0.21056  102 ASN A CB  
760  C CG  . ASN A 108 ? 3.74070 3.47810 3.28703 0.25473  -0.26455 0.21066  102 ASN A CG  
761  O OD1 . ASN A 108 ? 3.80354 3.55327 3.33714 0.23773  -0.25238 0.20423  102 ASN A OD1 
762  N ND2 . ASN A 108 ? 3.85952 3.57240 3.40636 0.25786  -0.26740 0.21711  102 ASN A ND2 
763  N N   . PHE A 109 ? 3.50664 3.32644 3.10837 0.26050  -0.23593 0.16941  103 PHE A N   
764  C CA  . PHE A 109 ? 3.51360 3.35348 3.14778 0.26041  -0.22150 0.15700  103 PHE A CA  
765  C C   . PHE A 109 ? 3.54848 3.37812 3.17666 0.24583  -0.21208 0.15971  103 PHE A C   
766  O O   . PHE A 109 ? 3.43728 3.25675 3.03741 0.22919  -0.20635 0.16300  103 PHE A O   
767  C CB  . PHE A 109 ? 3.52287 3.38856 3.17046 0.25529  -0.20787 0.14377  103 PHE A CB  
768  C CG  . PHE A 109 ? 3.38954 3.26771 3.04479 0.26870  -0.21641 0.14016  103 PHE A CG  
769  C CD1 . PHE A 109 ? 3.32467 3.22025 3.01598 0.28403  -0.21874 0.13377  103 PHE A CD1 
770  C CD2 . PHE A 109 ? 3.31291 3.18593 2.93801 0.26360  -0.22322 0.14437  103 PHE A CD2 
771  C CE1 . PHE A 109 ? 3.15934 3.06681 2.85735 0.29580  -0.22645 0.13031  103 PHE A CE1 
772  C CE2 . PHE A 109 ? 3.22737 3.11285 2.85965 0.27492  -0.23169 0.14193  103 PHE A CE2 
773  C CZ  . PHE A 109 ? 3.08069 2.98335 2.74992 0.29193  -0.23266 0.13421  103 PHE A CZ  
774  N N   . ILE A 110 ? 3.54818 3.38073 3.20076 0.24964  -0.21092 0.15885  104 ILE A N   
775  C CA  . ILE A 110 ? 3.48825 3.31065 3.13662 0.23621  -0.20450 0.16328  104 ILE A CA  
776  C C   . ILE A 110 ? 3.50212 3.35017 3.19176 0.23318  -0.19461 0.15703  104 ILE A C   
777  O O   . ILE A 110 ? 3.28424 3.14342 2.99931 0.24320  -0.20088 0.15513  104 ILE A O   
778  C CB  . ILE A 110 ? 3.30215 3.09528 2.93384 0.24004  -0.21624 0.17312  104 ILE A CB  
779  C CG1 . ILE A 110 ? 3.57568 3.34255 3.17249 0.24145  -0.22677 0.18321  104 ILE A CG1 
780  C CG2 . ILE A 110 ? 3.16017 2.94568 2.79057 0.22534  -0.20966 0.17689  104 ILE A CG2 
781  C CD1 . ILE A 110 ? 3.37126 3.10660 2.95695 0.24661  -0.23644 0.19239  104 ILE A CD1 
782  N N   . THR A 111 ? 3.63454 3.49237 3.33276 0.21805  -0.17954 0.15490  105 THR A N   
783  C CA  . THR A 111 ? 3.34793 3.22988 3.09120 0.21329  -0.17127 0.15321  105 THR A CA  
784  C C   . THR A 111 ? 3.10110 2.97026 2.84069 0.20532  -0.17767 0.16356  105 THR A C   
785  O O   . THR A 111 ? 3.09789 2.94204 2.80236 0.19685  -0.17890 0.16966  105 THR A O   
786  C CB  . THR A 111 ? 3.07892 2.97769 2.84035 0.20037  -0.14991 0.14608  105 THR A CB  
787  O OG1 . THR A 111 ? 2.82415 2.70322 2.55026 0.18478  -0.14375 0.15005  105 THR A OG1 
788  C CG2 . THR A 111 ? 3.10924 3.01887 2.87157 0.20499  -0.14109 0.13377  105 THR A CG2 
789  N N   . VAL A 112 ? 3.05863 2.94460 2.83335 0.20584  -0.18245 0.16637  106 VAL A N   
790  C CA  . VAL A 112 ? 3.11200 2.98630 2.88136 0.19607  -0.19031 0.17601  106 VAL A CA  
791  C C   . VAL A 112 ? 3.09746 2.99897 2.91197 0.18292  -0.18493 0.18193  106 VAL A C   
792  O O   . VAL A 112 ? 3.23651 3.16730 3.09630 0.18718  -0.18319 0.17992  106 VAL A O   
793  C CB  . VAL A 112 ? 3.37809 3.24318 3.14097 0.20494  -0.20458 0.17601  106 VAL A CB  
794  C CG1 . VAL A 112 ? 3.48505 3.34007 3.24320 0.18986  -0.21061 0.18449  106 VAL A CG1 
795  C CG2 . VAL A 112 ? 3.36097 3.19797 3.08556 0.21801  -0.20974 0.17247  106 VAL A CG2 
796  N N   . ASN A 113 ? 3.06496 2.95711 2.87004 0.16663  -0.18298 0.19062  107 ASN A N   
797  C CA  . ASN A 113 ? 3.19170 3.10823 3.03994 0.15168  -0.18114 0.20055  107 ASN A CA  
798  C C   . ASN A 113 ? 3.04806 2.94468 2.87029 0.13697  -0.19241 0.21145  107 ASN A C   
799  O O   . ASN A 113 ? 2.90974 2.78782 2.70489 0.12535  -0.18816 0.21564  107 ASN A O   
800  C CB  . ASN A 113 ? 3.23865 3.16796 3.10681 0.14316  -0.16259 0.19918  107 ASN A CB  
801  C CG  . ASN A 113 ? 3.16118 3.12190 3.08921 0.13049  -0.16001 0.21033  107 ASN A CG  
802  O OD1 . ASN A 113 ? 2.85640 2.83169 2.81199 0.12736  -0.17421 0.22056  107 ASN A OD1 
803  N ND2 . ASN A 113 ? 3.27877 3.25081 3.22904 0.12154  -0.14197 0.20924  107 ASN A ND2 
804  N N   . ILE A 114 ? 3.11413 3.01353 2.94211 0.13535  -0.20615 0.21535  108 ILE A N   
805  C CA  . ILE A 114 ? 3.20284 3.08044 3.00108 0.11882  -0.21557 0.22315  108 ILE A CA  
806  C C   . ILE A 114 ? 3.00690 2.89916 2.82715 0.09544  -0.21617 0.23833  108 ILE A C   
807  O O   . ILE A 114 ? 3.14677 3.01704 2.93518 0.07833  -0.22043 0.24480  108 ILE A O   
808  C CB  . ILE A 114 ? 3.06458 2.94279 2.86239 0.11880  -0.22831 0.22202  108 ILE A CB  
809  C CG1 . ILE A 114 ? 2.95125 2.87092 2.80638 0.11451  -0.23513 0.23024  108 ILE A CG1 
810  C CG2 . ILE A 114 ? 3.16772 3.02810 2.94144 0.14122  -0.22761 0.20750  108 ILE A CG2 
811  C CD1 . ILE A 114 ? 2.89580 2.81831 2.74956 0.11002  -0.24863 0.23040  108 ILE A CD1 
812  N N   . ASP A 115 ? 2.68220 2.61090 2.55884 0.09367  -0.21139 0.24448  109 ASP A N   
813  C CA  . ASP A 115 ? 2.79510 2.74354 2.70474 0.07195  -0.21275 0.26139  109 ASP A CA  
814  C C   . ASP A 115 ? 2.91027 2.87473 2.85077 0.07554  -0.19384 0.25840  109 ASP A C   
815  O O   . ASP A 115 ? 2.79968 2.79505 2.79667 0.08392  -0.18642 0.25684  109 ASP A O   
816  C CB  . ASP A 115 ? 2.91597 2.89762 2.87792 0.06215  -0.22737 0.27599  109 ASP A CB  
817  C CG  . ASP A 115 ? 2.94250 2.94422 2.93834 0.03668  -0.23320 0.29778  109 ASP A CG  
818  O OD1 . ASP A 115 ? 2.96442 2.95019 2.93434 0.02538  -0.22658 0.30035  109 ASP A OD1 
819  O OD2 . ASP A 115 ? 2.73791 2.77205 2.78790 0.02704  -0.24563 0.31396  109 ASP A OD2 
820  N N   . LYS A 116 ? 3.07532 3.01751 2.97878 0.06805  -0.18470 0.25668  110 LYS A N   
821  C CA  . LYS A 116 ? 3.19210 3.14807 3.12071 0.06461  -0.16547 0.25456  110 LYS A CA  
822  C C   . LYS A 116 ? 3.26573 3.23838 3.22509 0.04193  -0.16656 0.27235  110 LYS A C   
823  O O   . LYS A 116 ? 3.43192 3.41945 3.42037 0.03670  -0.14931 0.27164  110 LYS A O   
824  C CB  . LYS A 116 ? 3.45647 3.37926 3.32531 0.06860  -0.15427 0.24198  110 LYS A CB  
825  C CG  . LYS A 116 ? 3.37367 3.28478 3.21923 0.08960  -0.15162 0.22600  110 LYS A CG  
826  C CD  . LYS A 116 ? 3.45550 3.34267 3.25487 0.08930  -0.13922 0.21653  110 LYS A CD  
827  C CE  . LYS A 116 ? 3.13056 3.00924 2.90956 0.10745  -0.13833 0.20333  110 LYS A CE  
828  N NZ  . LYS A 116 ? 3.23384 3.08943 2.96527 0.10311  -0.12928 0.19711  110 LYS A NZ  
829  N N   . LYS A 117 ? 3.14886 3.11945 3.10201 0.02634  -0.18576 0.28809  111 LYS A N   
830  C CA  . LYS A 117 ? 3.21068 3.20039 3.19625 0.00236  -0.19044 0.30847  111 LYS A CA  
831  C C   . LYS A 117 ? 3.26704 3.30486 3.34328 0.00158  -0.19147 0.32127  111 LYS A C   
832  O O   . LYS A 117 ? 3.13753 3.19963 3.26351 -0.00848 -0.18206 0.33129  111 LYS A O   
833  C CB  . LYS A 117 ? 3.09616 3.06582 3.03980 -0.01791 -0.21099 0.32102  111 LYS A CB  
834  C CG  . LYS A 117 ? 3.22954 3.21960 3.20354 -0.04662 -0.22032 0.34534  111 LYS A CG  
835  C CD  . LYS A 117 ? 3.11260 3.08271 3.04227 -0.06965 -0.24080 0.35623  111 LYS A CD  
836  C CE  . LYS A 117 ? 3.02289 3.01341 2.97906 -0.10185 -0.25233 0.38267  111 LYS A CE  
837  N NZ  . LYS A 117 ? 3.45657 3.43559 3.39527 -0.11023 -0.23917 0.38317  111 LYS A NZ  
838  N N   . ASN A 118 ? 3.29304 3.34530 3.39522 0.01195  -0.20258 0.32172  112 ASN A N   
839  C CA  . ASN A 118 ? 3.17943 3.27614 3.37133 0.01238  -0.20575 0.33538  112 ASN A CA  
840  C C   . ASN A 118 ? 3.03317 3.14135 3.25542 0.03802  -0.19563 0.31906  112 ASN A C   
841  O O   . ASN A 118 ? 2.82445 2.96854 3.12742 0.04114  -0.19419 0.32817  112 ASN A O   
842  C CB  . ASN A 118 ? 3.12386 3.23472 3.33128 -0.00793 -0.23482 0.36006  112 ASN A CB  
843  C CG  . ASN A 118 ? 3.09447 3.19587 3.27369 -0.03750 -0.24607 0.37805  112 ASN A CG  
844  O OD1 . ASN A 118 ? 3.06643 3.14221 3.18503 -0.05200 -0.26132 0.38037  112 ASN A OD1 
845  N ND2 . ASN A 118 ? 3.12194 3.24345 3.34552 -0.04777 -0.23701 0.38996  112 ASN A ND2 
846  N N   . ASN A 119 ? 3.06753 3.14672 3.23093 0.05567  -0.18909 0.29663  113 ASN A N   
847  C CA  . ASN A 119 ? 3.04864 3.13571 3.23202 0.07881  -0.17939 0.27992  113 ASN A CA  
848  C C   . ASN A 119 ? 3.16338 3.27551 3.39380 0.08095  -0.19794 0.29156  113 ASN A C   
849  O O   . ASN A 119 ? 3.30769 3.44657 3.60204 0.09198  -0.19033 0.28984  113 ASN A O   
850  C CB  . ASN A 119 ? 3.11124 3.21541 3.34216 0.08599  -0.15105 0.26897  113 ASN A CB  
851  C CG  . ASN A 119 ? 3.12846 3.20549 3.30383 0.08354  -0.13229 0.25451  113 ASN A CG  
852  O OD1 . ASN A 119 ? 3.30888 3.38518 3.48377 0.06741  -0.12765 0.26321  113 ASN A OD1 
853  N ND2 . ASN A 119 ? 3.05568 3.11078 3.18359 0.09781  -0.12272 0.23382  113 ASN A ND2 
854  N N   . VAL A 120 ? 3.11388 3.21572 3.31088 0.06843  -0.22179 0.30304  114 VAL A N   
855  C CA  . VAL A 120 ? 3.10274 3.22481 3.33205 0.06532  -0.24253 0.31533  114 VAL A CA  
856  C C   . VAL A 120 ? 3.06134 3.15718 3.22785 0.07378  -0.25202 0.30164  114 VAL A C   
857  O O   . VAL A 120 ? 3.09766 3.20615 3.28539 0.08501  -0.25829 0.29820  114 VAL A O   
858  C CB  . VAL A 120 ? 2.89201 3.03255 3.14914 0.03545  -0.26428 0.34543  114 VAL A CB  
859  C CG1 . VAL A 120 ? 2.64700 2.80954 2.93735 0.02875  -0.28752 0.36020  114 VAL A CG1 
860  C CG2 . VAL A 120 ? 2.85568 3.02474 3.18324 0.02778  -0.25471 0.36054  114 VAL A CG2 
861  N N   . GLY A 121 ? 2.98911 3.04820 3.08132 0.06874  -0.25227 0.29357  115 GLY A N   
862  C CA  . GLY A 121 ? 3.00739 3.04052 3.04454 0.07652  -0.25897 0.28018  115 GLY A CA  
863  C C   . GLY A 121 ? 2.92162 2.94789 2.95038 0.10586  -0.24551 0.25860  115 GLY A C   
864  O O   . GLY A 121 ? 2.78354 2.79852 2.79877 0.11681  -0.22859 0.24771  115 GLY A O   
865  N N   . LEU A 122 ? 2.85550 2.88881 2.89028 0.11621  -0.25365 0.25306  116 LEU A N   
866  C CA  . LEU A 122 ? 2.85309 2.88152 2.87952 0.14218  -0.24385 0.23408  116 LEU A CA  
867  C C   . LEU A 122 ? 2.92630 2.92453 2.89407 0.14914  -0.24940 0.22216  116 LEU A C   
868  O O   . LEU A 122 ? 2.98180 2.97124 2.92914 0.13446  -0.26195 0.22742  116 LEU A O   
869  C CB  . LEU A 122 ? 2.93325 2.99543 3.01956 0.15111  -0.24682 0.23600  116 LEU A CB  
870  C CG  . LEU A 122 ? 2.82497 2.91869 2.98268 0.14838  -0.23784 0.24571  116 LEU A CG  
871  C CD1 . LEU A 122 ? 2.62933 2.75202 2.84495 0.15875  -0.24087 0.24647  116 LEU A CD1 
872  C CD2 . LEU A 122 ? 2.87667 2.96053 3.02575 0.15704  -0.21378 0.23276  116 LEU A CD2 
873  N N   . LEU A 123 ? 2.86643 2.84888 2.80856 0.16994  -0.23927 0.20621  117 LEU A N   
874  C CA  . LEU A 123 ? 2.80235 2.75753 2.69763 0.18013  -0.24287 0.19493  117 LEU A CA  
875  C C   . LEU A 123 ? 2.83849 2.81115 2.75351 0.18808  -0.25186 0.19097  117 LEU A C   
876  O O   . LEU A 123 ? 2.80472 2.79183 2.73974 0.20506  -0.24763 0.18342  117 LEU A O   
877  C CB  . LEU A 123 ? 2.92819 2.86284 2.79338 0.19741  -0.23176 0.18352  117 LEU A CB  
878  C CG  . LEU A 123 ? 2.75253 2.66166 2.57976 0.21117  -0.23534 0.17342  117 LEU A CG  
879  C CD1 . LEU A 123 ? 2.78010 2.66054 2.57359 0.19859  -0.23972 0.17561  117 LEU A CD1 
880  C CD2 . LEU A 123 ? 2.95107 2.84480 2.75510 0.22600  -0.22756 0.16673  117 LEU A CD2 
881  N N   . LEU A 124 ? 2.99800 2.96870 2.90492 0.17334  -0.26387 0.19570  118 LEU A N   
882  C CA  . LEU A 124 ? 3.17416 3.15925 3.09397 0.17703  -0.27338 0.19219  118 LEU A CA  
883  C C   . LEU A 124 ? 3.15264 3.10987 3.02776 0.18252  -0.27343 0.17883  118 LEU A C   
884  O O   . LEU A 124 ? 3.29784 3.26353 3.17665 0.18160  -0.28091 0.17496  118 LEU A O   
885  C CB  . LEU A 124 ? 3.35423 3.36320 3.30449 0.15236  -0.28806 0.20888  118 LEU A CB  
886  C CG  . LEU A 124 ? 3.34033 3.38467 3.35368 0.15012  -0.28992 0.22331  118 LEU A CG  
887  C CD1 . LEU A 124 ? 3.22129 3.28991 3.26639 0.12558  -0.30904 0.24256  118 LEU A CD1 
888  C CD2 . LEU A 124 ? 3.05062 3.11062 3.09378 0.17574  -0.28154 0.21279  118 LEU A CD2 
889  N N   . GLY A 125 ? 2.94946 2.87363 2.78545 0.18749  -0.26481 0.17209  119 GLY A N   
890  C CA  . GLY A 125 ? 2.84498 2.74210 2.64749 0.19651  -0.26201 0.15888  119 GLY A CA  
891  C C   . GLY A 125 ? 3.08735 2.99583 2.90219 0.22109  -0.26197 0.14921  119 GLY A C   
892  O O   . GLY A 125 ? 3.16615 3.07722 2.98593 0.23839  -0.25713 0.14752  119 GLY A O   
893  N N   . CYS A 126 ? 3.05947 2.97520 2.87752 0.22024  -0.26739 0.14298  120 CYS A N   
894  C CA  . CYS A 126 ? 3.19612 3.12615 3.02814 0.24114  -0.26900 0.13457  120 CYS A CA  
895  C C   . CYS A 126 ? 3.30817 3.21458 3.11530 0.24821  -0.26542 0.12177  120 CYS A C   
896  O O   . CYS A 126 ? 3.33419 3.24198 3.13744 0.23583  -0.26826 0.11681  120 CYS A O   
897  C CB  . CYS A 126 ? 3.23605 3.20081 3.10252 0.23383  -0.27894 0.13964  120 CYS A CB  
898  S SG  . CYS A 126 ? 3.87591 3.85826 3.75741 0.25595  -0.28182 0.12895  120 CYS A SG  
899  N N   . PHE A 127 ? 3.22386 3.10885 3.01618 0.26675  -0.25896 0.11702  121 PHE A N   
900  C CA  . PHE A 127 ? 3.17312 3.03346 2.94916 0.27496  -0.25360 0.10602  121 PHE A CA  
901  C C   . PHE A 127 ? 3.16045 3.00876 2.93405 0.29925  -0.25155 0.10594  121 PHE A C   
902  O O   . PHE A 127 ? 2.91707 2.76535 2.68826 0.30347  -0.25214 0.11423  121 PHE A O   
903  C CB  . PHE A 127 ? 3.29758 3.12630 3.04826 0.25625  -0.24604 0.10342  121 PHE A CB  
904  C CG  . PHE A 127 ? 3.43558 3.24384 3.17129 0.25319  -0.24239 0.11199  121 PHE A CG  
905  C CD1 . PHE A 127 ? 3.47930 3.29951 3.21713 0.23578  -0.24596 0.12312  121 PHE A CD1 
906  C CD2 . PHE A 127 ? 3.50563 3.28328 3.22812 0.26711  -0.23602 0.11025  121 PHE A CD2 
907  C CE1 . PHE A 127 ? 3.76281 3.56473 3.48588 0.23184  -0.24214 0.13057  121 PHE A CE1 
908  C CE2 . PHE A 127 ? 3.57722 3.33554 3.28429 0.26279  -0.23361 0.11887  121 PHE A CE2 
909  C CZ  . PHE A 127 ? 3.82752 3.59791 3.53283 0.24487  -0.23611 0.12813  121 PHE A CZ  
910  N N   . TRP A 128 ? 3.26667 3.10539 3.04177 0.31315  -0.24933 0.09725  122 TRP A N   
911  C CA  . TRP A 128 ? 3.25877 3.08250 3.03339 0.33412  -0.24911 0.09948  122 TRP A CA  
912  C C   . TRP A 128 ? 3.31972 3.10676 3.08492 0.33486  -0.23963 0.09412  122 TRP A C   
913  O O   . TRP A 128 ? 3.34993 3.12586 3.10906 0.32090  -0.23149 0.08393  122 TRP A O   
914  C CB  . TRP A 128 ? 3.31081 3.15612 3.10372 0.35220  -0.25500 0.09593  122 TRP A CB  
915  C CG  . TRP A 128 ? 3.25089 3.12806 3.05385 0.35445  -0.26243 0.10056  122 TRP A CG  
916  C CD1 . TRP A 128 ? 3.14442 3.04037 2.95256 0.34062  -0.26341 0.10353  122 TRP A CD1 
917  C CD2 . TRP A 128 ? 3.41435 3.30733 3.22585 0.37046  -0.26866 0.10264  122 TRP A CD2 
918  N NE1 . TRP A 128 ? 3.30833 3.22912 3.12939 0.34796  -0.26738 0.10529  122 TRP A NE1 
919  C CE2 . TRP A 128 ? 3.35213 3.27106 3.17171 0.36502  -0.27071 0.10431  122 TRP A CE2 
920  C CE3 . TRP A 128 ? 3.37379 3.26164 3.18891 0.38768  -0.27276 0.10412  122 TRP A CE3 
921  C CZ2 . TRP A 128 ? 3.27577 3.21322 3.10149 0.37474  -0.27490 0.10502  122 TRP A CZ2 
922  C CZ3 . TRP A 128 ? 3.22914 3.13755 3.04924 0.39648  -0.27986 0.10731  122 TRP A CZ3 
923  C CH2 . TRP A 128 ? 3.25055 3.18234 3.07321 0.38929  -0.28001 0.10657  122 TRP A CH2 
924  N N   . VAL A 129 ? 3.41729 3.18465 3.18187 0.34945  -0.24038 0.10139  123 VAL A N   
925  C CA  . VAL A 129 ? 3.37909 3.11010 3.14332 0.35391  -0.23089 0.09769  123 VAL A CA  
926  C C   . VAL A 129 ? 3.42965 3.15200 3.20541 0.37479  -0.23826 0.10986  123 VAL A C   
927  O O   . VAL A 129 ? 3.32430 3.05566 3.09201 0.37671  -0.24845 0.12325  123 VAL A O   
928  C CB  . VAL A 129 ? 3.04475 2.74747 2.78592 0.33459  -0.22245 0.09822  123 VAL A CB  
929  C CG1 . VAL A 129 ? 3.00947 2.71384 2.73626 0.33048  -0.23013 0.11353  123 VAL A CG1 
930  C CG2 . VAL A 129 ? 3.08988 2.75206 2.83357 0.33915  -0.21004 0.09276  123 VAL A CG2 
931  N N   . SER A 130 ? 3.39506 3.10032 3.19131 0.38868  -0.23285 0.10562  124 SER A N   
932  C CA  . SER A 130 ? 3.33743 3.03712 3.15212 0.40841  -0.24255 0.12003  124 SER A CA  
933  C C   . SER A 130 ? 3.47383 3.13933 3.31113 0.41801  -0.23128 0.11674  124 SER A C   
934  O O   . SER A 130 ? 3.44698 3.10720 3.29801 0.41777  -0.21662 0.09892  124 SER A O   
935  C CB  . SER A 130 ? 3.31132 3.04483 3.14395 0.42185  -0.25336 0.12134  124 SER A CB  
936  O OG  . SER A 130 ? 3.55293 3.28213 3.40434 0.43845  -0.26482 0.13774  124 SER A OG  
937  N N   . ASP A 131 ? 3.53032 3.17206 3.37252 0.42494  -0.23734 0.13386  125 ASP A N   
938  C CA  . ASP A 131 ? 3.38109 2.98942 3.25422 0.43727  -0.22871 0.13557  125 ASP A CA  
939  C C   . ASP A 131 ? 3.34505 2.92182 3.21259 0.42507  -0.20422 0.11518  125 ASP A C   
940  O O   . ASP A 131 ? 3.25858 2.80802 3.15699 0.43461  -0.19027 0.10920  125 ASP A O   
941  C CB  . ASP A 131 ? 3.45507 3.07771 3.37195 0.45829  -0.23147 0.13575  125 ASP A CB  
942  C CG  . ASP A 131 ? 3.64039 3.29188 3.56173 0.46812  -0.25627 0.15720  125 ASP A CG  
943  O OD1 . ASP A 131 ? 3.76862 3.42768 3.65794 0.45785  -0.26925 0.17004  125 ASP A OD1 
944  O OD2 . ASP A 131 ? 3.58000 3.24649 3.53616 0.48429  -0.26189 0.16075  125 ASP A OD2 
945  N N   . ASP A 132 ? 3.43954 3.01921 3.26988 0.40263  -0.19808 0.10465  126 ASP A N   
946  C CA  . ASP A 132 ? 3.50991 3.06203 3.32689 0.38478  -0.17551 0.08466  126 ASP A CA  
947  C C   . ASP A 132 ? 3.46754 3.02019 3.30808 0.38818  -0.15824 0.06270  126 ASP A C   
948  O O   . ASP A 132 ? 3.38292 2.90417 3.22359 0.37792  -0.13532 0.04506  126 ASP A O   
949  C CB  . ASP A 132 ? 3.56835 3.07454 3.38511 0.38334  -0.16638 0.09002  126 ASP A CB  
950  C CG  . ASP A 132 ? 3.63761 3.13813 3.41655 0.36717  -0.17540 0.10284  126 ASP A CG  
951  O OD1 . ASP A 132 ? 3.63270 3.16392 3.38746 0.35551  -0.18548 0.10507  126 ASP A OD1 
952  O OD2 . ASP A 132 ? 3.73717 3.20249 3.51335 0.36601  -0.17184 0.11084  126 ASP A OD2 
953  N N   . GLU A 133 ? 3.46881 3.05629 3.32814 0.40093  -0.16773 0.06258  127 GLU A N   
954  C CA  . GLU A 133 ? 3.44262 3.03536 3.32592 0.40496  -0.15282 0.04263  127 GLU A CA  
955  C C   . GLU A 133 ? 3.49503 3.12605 3.36158 0.39337  -0.15869 0.03333  127 GLU A C   
956  O O   . GLU A 133 ? 3.52090 3.14896 3.37766 0.37605  -0.14250 0.01227  127 GLU A O   
957  C CB  . GLU A 133 ? 3.32186 2.91819 3.25525 0.43446  -0.15790 0.05219  127 GLU A CB  
958  C CG  . GLU A 133 ? 3.42951 2.98654 3.39113 0.44693  -0.15094 0.06169  127 GLU A CG  
959  C CD  . GLU A 133 ? 3.50623 3.07108 3.52236 0.47515  -0.16040 0.07647  127 GLU A CD  
960  O OE1 . GLU A 133 ? 3.44436 3.04522 3.47236 0.48420  -0.17162 0.07789  127 GLU A OE1 
961  O OE2 . GLU A 133 ? 3.53629 3.07159 3.58528 0.48757  -0.15756 0.08808  127 GLU A OE2 
962  N N   . ARG A 134 ? 3.43176 3.09760 3.29425 0.40043  -0.18095 0.04840  128 ARG A N   
963  C CA  . ARG A 134 ? 3.44419 3.14706 3.29586 0.39123  -0.18842 0.04230  128 ARG A CA  
964  C C   . ARG A 134 ? 3.55646 3.27258 3.37670 0.37390  -0.19958 0.05156  128 ARG A C   
965  O O   . ARG A 134 ? 3.48363 3.19140 3.29438 0.37629  -0.20751 0.06684  128 ARG A O   
966  C CB  . ARG A 134 ? 3.26119 2.99544 3.13844 0.41300  -0.20294 0.05016  128 ARG A CB  
967  C CG  . ARG A 134 ? 3.28060 3.00982 3.19426 0.42889  -0.19222 0.04011  128 ARG A CG  
968  C CD  . ARG A 134 ? 3.03582 2.78800 2.97711 0.45283  -0.20964 0.05588  128 ARG A CD  
969  N NE  . ARG A 134 ? 3.01622 2.75348 2.96292 0.46399  -0.22122 0.07821  128 ARG A NE  
970  C CZ  . ARG A 134 ? 3.19209 2.90173 3.16844 0.47698  -0.21536 0.08457  128 ARG A CZ  
971  N NH1 . ARG A 134 ? 3.19162 2.88411 3.19780 0.48190  -0.19492 0.06826  128 ARG A NH1 
972  N NH2 . ARG A 134 ? 3.28424 2.98263 3.26205 0.48398  -0.22967 0.10794  128 ARG A NH2 
973  N N   . CYS A 135 ? 3.65195 3.38937 3.45861 0.35539  -0.20029 0.04307  129 CYS A N   
974  C CA  . CYS A 135 ? 3.57810 3.33004 3.36313 0.33779  -0.20985 0.05203  129 CYS A CA  
975  C C   . CYS A 135 ? 3.46196 3.24709 3.24711 0.32489  -0.21606 0.04665  129 CYS A C   
976  O O   . CYS A 135 ? 3.25413 3.04048 3.04161 0.31744  -0.20815 0.03210  129 CYS A O   
977  C CB  . CYS A 135 ? 3.36304 3.08481 3.12271 0.31546  -0.19969 0.05024  129 CYS A CB  
978  S SG  . CYS A 135 ? 3.10579 2.80775 2.85013 0.28859  -0.18021 0.02779  129 CYS A SG  
979  N N   . TYR A 136 ? 3.40556 3.21707 3.19006 0.32149  -0.22957 0.05859  130 TYR A N   
980  C CA  . TYR A 136 ? 3.32874 3.17135 3.11650 0.30675  -0.23767 0.05803  130 TYR A CA  
981  C C   . TYR A 136 ? 3.24439 3.08894 3.01909 0.28324  -0.24144 0.06753  130 TYR A C   
982  O O   . TYR A 136 ? 3.33906 3.17198 3.10683 0.28498  -0.24137 0.07703  130 TYR A O   
983  C CB  . TYR A 136 ? 3.39588 3.27167 3.20447 0.32451  -0.24984 0.06400  130 TYR A CB  
984  C CG  . TYR A 136 ? 3.47997 3.38777 3.29747 0.31020  -0.25976 0.06799  130 TYR A CG  
985  C CD1 . TYR A 136 ? 3.54819 3.47052 3.36989 0.29925  -0.26182 0.05978  130 TYR A CD1 
986  C CD2 . TYR A 136 ? 3.34209 3.26543 3.16681 0.30677  -0.26663 0.08047  130 TYR A CD2 
987  C CE1 . TYR A 136 ? 3.43037 3.38178 3.26426 0.28555  -0.27306 0.06635  130 TYR A CE1 
988  C CE2 . TYR A 136 ? 3.32198 3.27440 3.16358 0.29467  -0.27560 0.08587  130 TYR A CE2 
989  C CZ  . TYR A 136 ? 3.19963 3.16598 3.04632 0.28427  -0.28010 0.08002  130 TYR A CZ  
990  O OH  . TYR A 136 ? 2.69985 2.69500 2.56708 0.27164  -0.29117 0.08818  130 TYR A OH  
991  N N   . VAL A 137 ? 3.15459 3.01447 2.92674 0.25958  -0.24562 0.06626  131 VAL A N   
992  C CA  . VAL A 137 ? 3.19158 3.05844 2.95752 0.23498  -0.25199 0.07818  131 VAL A CA  
993  C C   . VAL A 137 ? 3.31900 3.21868 3.09921 0.21858  -0.26433 0.08245  131 VAL A C   
994  O O   . VAL A 137 ? 3.28513 3.18839 3.06153 0.21085  -0.26344 0.07209  131 VAL A O   
995  C CB  . VAL A 137 ? 3.06863 2.90196 2.80436 0.21133  -0.24152 0.07411  131 VAL A CB  
996  C CG1 . VAL A 137 ? 3.34702 3.16621 3.06685 0.19579  -0.23154 0.05692  131 VAL A CG1 
997  C CG2 . VAL A 137 ? 2.82533 2.66858 2.55632 0.18425  -0.25030 0.08908  131 VAL A CG2 
998  N N   . GLY A 138 ? 3.30690 3.23074 3.10649 0.21297  -0.27553 0.09822  132 GLY A N   
999  C CA  . GLY A 138 ? 3.16428 3.12053 2.98540 0.19785  -0.28952 0.10666  132 GLY A CA  
1000 C C   . GLY A 138 ? 3.18762 3.16857 3.04041 0.19822  -0.29855 0.12422  132 GLY A C   
1001 O O   . GLY A 138 ? 3.35826 3.33040 3.20721 0.19014  -0.29636 0.13321  132 GLY A O   
1002 N N   . ASN A 139 ? 3.12676 3.13830 3.01336 0.20737  -0.30734 0.12865  133 ASN A N   
1003 C CA  . ASN A 139 ? 3.16533 3.20119 3.09068 0.20956  -0.31278 0.14333  133 ASN A CA  
1004 C C   . ASN A 139 ? 3.07724 3.12679 3.02537 0.23813  -0.30858 0.13760  133 ASN A C   
1005 O O   . ASN A 139 ? 3.00404 3.07504 2.98945 0.24104  -0.31026 0.14660  133 ASN A O   
1006 C CB  . ASN A 139 ? 2.94592 3.00859 2.89986 0.18454  -0.32927 0.15936  133 ASN A CB  
1007 C CG  . ASN A 139 ? 2.78969 2.86429 2.74353 0.18041  -0.33800 0.15366  133 ASN A CG  
1008 O OD1 . ASN A 139 ? 2.83358 2.92624 2.81230 0.19858  -0.34003 0.15038  133 ASN A OD1 
1009 N ND2 . ASN A 139 ? 2.59284 2.65669 2.51668 0.15419  -0.34231 0.15175  133 ASN A ND2 
1010 N N   . ALA A 140 ? 2.93272 2.97028 2.86123 0.25785  -0.30241 0.12307  134 ALA A N   
1011 C CA  . ALA A 140 ? 3.11006 3.15777 3.05259 0.28231  -0.29845 0.11749  134 ALA A CA  
1012 C C   . ALA A 140 ? 3.12479 3.15655 3.05581 0.29239  -0.28784 0.11791  134 ALA A C   
1013 O O   . ALA A 140 ? 3.17702 3.18584 3.07995 0.30326  -0.28213 0.11138  134 ALA A O   
1014 C CB  . ALA A 140 ? 3.06592 3.10915 2.99356 0.29684  -0.29836 0.10453  134 ALA A CB  
1015 N N   . SER A 141 ? 3.04290 3.08710 2.99839 0.28757  -0.28511 0.12650  135 SER A N   
1016 C CA  . SER A 141 ? 3.08916 3.12010 3.03360 0.29337  -0.27419 0.12680  135 SER A CA  
1017 C C   . SER A 141 ? 3.28186 3.31059 3.21629 0.31317  -0.26859 0.11752  135 SER A C   
1018 O O   . SER A 141 ? 3.24614 3.28795 3.18966 0.32298  -0.27261 0.11157  135 SER A O   
1019 C CB  . SER A 141 ? 3.15221 3.20026 3.13154 0.28341  -0.27015 0.13633  135 SER A CB  
1020 O OG  . SER A 141 ? 3.01830 3.07076 3.00891 0.26286  -0.27806 0.14829  135 SER A OG  
1021 N N   . PHE A 142 ? 3.29735 3.30940 3.21098 0.31672  -0.26015 0.11737  136 PHE A N   
1022 C CA  . PHE A 142 ? 3.23647 3.24573 3.13643 0.33048  -0.25614 0.11118  136 PHE A CA  
1023 C C   . PHE A 142 ? 3.39669 3.42901 3.32529 0.33095  -0.24870 0.10771  136 PHE A C   
1024 O O   . PHE A 142 ? 3.28698 3.31638 3.21113 0.32792  -0.23732 0.10637  136 PHE A O   
1025 C CB  . PHE A 142 ? 3.26808 3.25188 3.13491 0.33025  -0.25105 0.11404  136 PHE A CB  
1026 C CG  . PHE A 142 ? 3.36833 3.34367 3.21258 0.34249  -0.25318 0.11131  136 PHE A CG  
1027 C CD1 . PHE A 142 ? 3.32677 3.31731 3.18028 0.35315  -0.25815 0.10555  136 PHE A CD1 
1028 C CD2 . PHE A 142 ? 3.35658 3.30939 3.17080 0.34162  -0.25186 0.11643  136 PHE A CD2 
1029 C CE1 . PHE A 142 ? 3.17238 3.15691 3.00634 0.36232  -0.26209 0.10553  136 PHE A CE1 
1030 C CE2 . PHE A 142 ? 3.19603 3.14257 2.99135 0.35017  -0.25694 0.11771  136 PHE A CE2 
1031 C CZ  . PHE A 142 ? 3.00629 2.96924 2.81183 0.36034  -0.26223 0.11255  136 PHE A CZ  
1032 N N   . THR A 143 ? 3.50007 3.55428 3.45840 0.33321  -0.25387 0.10558  137 THR A N   
1033 C CA  . THR A 143 ? 3.35670 3.43193 3.34681 0.33508  -0.24628 0.10090  137 THR A CA  
1034 C C   . THR A 143 ? 3.18879 3.27519 3.18125 0.34600  -0.25391 0.09433  137 THR A C   
1035 O O   . THR A 143 ? 3.17639 3.26286 3.16305 0.34838  -0.26611 0.09549  137 THR A O   
1036 C CB  . THR A 143 ? 3.28447 3.37932 3.32360 0.32433  -0.24492 0.10832  137 THR A CB  
1037 O OG1 . THR A 143 ? 3.10752 3.20941 3.15664 0.31871  -0.26069 0.11584  137 THR A OG1 
1038 C CG2 . THR A 143 ? 3.44489 3.53171 3.48635 0.31330  -0.23533 0.11451  137 THR A CG2 
1039 N N   . GLY A 144 ? 2.89592 3.25699 3.54372 0.28644  -0.50835 -0.19927 138 GLY A N   
1040 C CA  . GLY A 144 ? 2.80846 3.17770 3.52486 0.30131  -0.57344 -0.18036 138 GLY A CA  
1041 C C   . GLY A 144 ? 2.97558 3.34718 3.73697 0.27034  -0.59797 -0.19737 138 GLY A C   
1042 O O   . GLY A 144 ? 2.87755 3.24451 3.70714 0.27033  -0.62005 -0.16375 138 GLY A O   
1043 N N   . GLY A 145 ? 3.32690 3.70870 4.05393 0.24497  -0.59340 -0.24622 139 GLY A N   
1044 C CA  . GLY A 145 ? 3.34147 3.72320 4.10319 0.21713  -0.61320 -0.26388 139 GLY A CA  
1045 C C   . GLY A 145 ? 3.29185 3.63093 4.06449 0.19554  -0.54416 -0.23391 139 GLY A C   
1046 O O   . GLY A 145 ? 3.32959 3.66741 4.15787 0.19185  -0.55916 -0.20839 139 GLY A O   
1047 N N   . SER A 146 ? 2.88987 3.19395 3.61084 0.18440  -0.46906 -0.23437 140 SER A N   
1048 C CA  . SER A 146 ? 2.81321 3.06924 3.53125 0.17127  -0.40434 -0.21213 140 SER A CA  
1049 C C   . SER A 146 ? 2.67034 2.91229 3.43111 0.19462  -0.38952 -0.14859 140 SER A C   
1050 O O   . SER A 146 ? 2.59790 2.80646 3.36155 0.19291  -0.34320 -0.12521 140 SER A O   
1051 C CB  . SER A 146 ? 2.66055 2.87825 3.31841 0.15568  -0.33813 -0.22897 140 SER A CB  
1052 O OG  . SER A 146 ? 2.60649 2.84280 3.23429 0.13292  -0.35026 -0.28444 140 SER A OG  
1053 N N   . ILE A 147 ? 2.60881 2.87604 3.40146 0.22044  -0.42923 -0.12105 141 ILE A N   
1054 C CA  . ILE A 147 ? 2.40587 2.66865 3.25251 0.24299  -0.42529 -0.06002 141 ILE A CA  
1055 C C   . ILE A 147 ? 2.51100 2.81340 3.44488 0.24821  -0.49513 -0.03978 141 ILE A C   
1056 O O   . ILE A 147 ? 2.38227 2.68519 3.37385 0.25675  -0.48217 0.01231  141 ILE A O   
1057 C CB  . ILE A 147 ? 2.20126 2.46037 3.03295 0.27089  -0.42228 -0.03652 141 ILE A CB  
1058 C CG1 . ILE A 147 ? 2.57125 2.79112 3.32474 0.26319  -0.35181 -0.04943 141 ILE A CG1 
1059 C CG2 . ILE A 147 ? 1.99406 2.24798 2.88393 0.29470  -0.41589 0.02733  141 ILE A CG2 
1060 C CD1 . ILE A 147 ? 2.89184 3.10913 3.62081 0.29177  -0.34497 -0.02735 141 ILE A CD1 
1061 N N   . HIS A 148 ? 2.60988 2.94648 3.55851 0.24401  -0.56920 -0.07750 142 HIS A N   
1062 C CA  . HIS A 148 ? 2.64885 3.02053 3.68993 0.25103  -0.64976 -0.05651 142 HIS A CA  
1063 C C   . HIS A 148 ? 2.60521 2.99459 3.66486 0.22679  -0.68706 -0.08875 142 HIS A C   
1064 O O   . HIS A 148 ? 2.58122 2.98302 3.71348 0.22014  -0.69906 -0.05178 142 HIS A O   
1065 C CB  . HIS A 148 ? 2.69472 3.08806 3.74795 0.27914  -0.72606 -0.06828 142 HIS A CB  
1066 C CG  . HIS A 148 ? 2.76476 3.18471 3.92732 0.29211  -0.81244 -0.03527 142 HIS A CG  
1067 N ND1 . HIS A 148 ? 2.87441 3.30170 4.06939 0.32597  -0.86677 -0.01837 142 HIS A ND1 
1068 C CD2 . HIS A 148 ? 2.74360 3.18410 3.99480 0.27656  -0.85933 -0.01603 142 HIS A CD2 
1069 C CE1 . HIS A 148 ? 2.91383 3.36273 4.21888 0.32872  -0.94589 0.00939  142 HIS A CE1 
1070 N NE2 . HIS A 148 ? 2.89124 3.35020 4.23515 0.29767  -0.94163 0.01433  142 HIS A NE2 
1071 N N   . THR A 149 ? 2.63638 3.03059 3.63412 0.21503  -0.70460 -0.15374 143 THR A N   
1072 C CA  . THR A 149 ? 2.51327 2.92686 3.52793 0.19618  -0.75568 -0.19058 143 THR A CA  
1073 C C   . THR A 149 ? 2.38974 2.78335 3.34691 0.16861  -0.69797 -0.22482 143 THR A C   
1074 O O   . THR A 149 ? 2.32072 2.72552 3.29944 0.15296  -0.72839 -0.24266 143 THR A O   
1075 C CB  . THR A 149 ? 2.59338 3.03329 3.58604 0.20861  -0.83497 -0.24412 143 THR A CB  
1076 O OG1 . THR A 149 ? 2.84280 3.27675 3.74258 0.21121  -0.79076 -0.28335 143 THR A OG1 
1077 C CG2 . THR A 149 ? 2.56316 3.01881 3.61470 0.24135  -0.90781 -0.21670 143 THR A CG2 
1078 N N   . ILE A 150 ? 2.58281 2.94453 3.47112 0.16314  -0.62007 -0.23428 144 ILE A N   
1079 C CA  . ILE A 150 ? 2.62823 2.96417 3.46282 0.13909  -0.56952 -0.27044 144 ILE A CA  
1080 C C   . ILE A 150 ? 2.69615 2.99705 3.53759 0.14205  -0.50391 -0.22672 144 ILE A C   
1081 O O   . ILE A 150 ? 2.97557 3.25446 3.81373 0.15725  -0.45962 -0.18703 144 ILE A O   
1082 C CB  . ILE A 150 ? 2.78723 3.10971 3.54662 0.12994  -0.53297 -0.31326 144 ILE A CB  
1083 C CG1 . ILE A 150 ? 2.76670 3.13258 3.51318 0.13587  -0.59612 -0.35495 144 ILE A CG1 
1084 C CG2 . ILE A 150 ? 2.61213 2.90337 3.32626 0.10433  -0.48701 -0.35129 144 ILE A CG2 
1085 C CD1 . ILE A 150 ? 2.79818 3.16492 3.47977 0.12992  -0.55961 -0.38820 144 ILE A CD1 
1086 N N   . LYS A 151 ? 2.42637 2.72232 3.27251 0.13236  -0.49804 -0.23431 145 LYS A N   
1087 C CA  . LYS A 151 ? 2.54120 2.80579 3.38168 0.14362  -0.43566 -0.19756 145 LYS A CA  
1088 C C   . LYS A 151 ? 2.66047 2.87036 3.42301 0.13975  -0.36804 -0.22392 145 LYS A C   
1089 O O   . LYS A 151 ? 2.66146 2.85690 3.37425 0.11850  -0.36633 -0.28269 145 LYS A O   
1090 C CB  . LYS A 151 ? 2.53087 2.80402 3.38361 0.13935  -0.44620 -0.20416 145 LYS A CB  
1091 C CG  . LYS A 151 ? 2.61833 2.86317 3.45587 0.16115  -0.38213 -0.16719 145 LYS A CG  
1092 C CD  . LYS A 151 ? 2.49954 2.75138 3.33361 0.16102  -0.38940 -0.18000 145 LYS A CD  
1093 C CE  . LYS A 151 ? 2.26838 2.49650 3.08037 0.19406  -0.32574 -0.14059 145 LYS A CE  
1094 N NZ  . LYS A 151 ? 1.89600 2.05945 2.62397 0.20242  -0.26684 -0.17132 145 LYS A NZ  
1095 N N   . THR A 152 ? 2.74358 2.92303 3.50068 0.16057  -0.31520 -0.17931 146 THR A N   
1096 C CA  . THR A 152 ? 2.77484 2.89430 3.46569 0.15976  -0.25457 -0.19774 146 THR A CA  
1097 C C   . THR A 152 ? 2.55133 2.63477 3.22807 0.18743  -0.20366 -0.16448 146 THR A C   
1098 O O   . THR A 152 ? 2.15970 2.27191 2.87715 0.20648  -0.21077 -0.12575 146 THR A O   
1099 C CB  . THR A 152 ? 2.83924 2.94969 3.52353 0.16269  -0.24036 -0.18041 146 THR A CB  
1100 O OG1 . THR A 152 ? 2.72870 2.84944 3.45627 0.19101  -0.23200 -0.11474 146 THR A OG1 
1101 C CG2 . THR A 152 ? 2.82644 2.98046 3.52070 0.14725  -0.29213 -0.20840 146 THR A CG2 
1102 N N   . LEU A 153 ? 2.62474 2.64550 3.24450 0.19242  -0.15301 -0.17782 147 LEU A N   
1103 C CA  . LEU A 153 ? 2.60131 2.57915 3.19251 0.22684  -0.10410 -0.15269 147 LEU A CA  
1104 C C   . LEU A 153 ? 2.62461 2.53442 3.16716 0.23022  -0.06070 -0.16006 147 LEU A C   
1105 O O   . LEU A 153 ? 2.57430 2.44680 3.08018 0.20308  -0.05880 -0.21121 147 LEU A O   
1106 C CB  . LEU A 153 ? 2.62199 2.58197 3.17664 0.23199  -0.10198 -0.19058 147 LEU A CB  
1107 C CG  . LEU A 153 ? 2.83691 2.75235 3.34906 0.27810  -0.05390 -0.17028 147 LEU A CG  
1108 C CD1 . LEU A 153 ? 2.66716 2.62900 3.23178 0.31513  -0.04031 -0.08922 147 LEU A CD1 
1109 C CD2 . LEU A 153 ? 2.85522 2.75259 3.32365 0.28647  -0.05761 -0.21465 147 LEU A CD2 
1110 N N   . GLY A 154 ? 2.73596 2.63071 3.28363 0.26296  -0.02753 -0.10710 148 GLY A N   
1111 C CA  . GLY A 154 ? 2.83084 2.65725 3.33524 0.26970  0.01189  -0.10826 148 GLY A CA  
1112 C C   . GLY A 154 ? 2.91094 2.70600 3.39752 0.31942  0.05390  -0.06404 148 GLY A C   
1113 O O   . GLY A 154 ? 2.79872 2.62845 3.30440 0.35064  0.05745  -0.03180 148 GLY A O   
1114 N N   . VAL A 155 ? 3.04323 2.77463 3.49425 0.32949  0.08642  -0.05943 149 VAL A N   
1115 C CA  . VAL A 155 ? 2.97941 2.67279 3.40356 0.38086  0.12679  -0.02225 149 VAL A CA  
1116 C C   . VAL A 155 ? 3.13781 2.81546 3.57328 0.38443  0.14371  0.01561  149 VAL A C   
1117 O O   . VAL A 155 ? 3.21681 2.86381 3.64230 0.35163  0.14039  -0.00638 149 VAL A O   
1118 C CB  . VAL A 155 ? 2.98136 2.58620 3.32897 0.40058  0.14857  -0.06831 149 VAL A CB  
1119 C CG1 . VAL A 155 ? 3.16240 2.72917 3.47522 0.46237  0.18784  -0.03098 149 VAL A CG1 
1120 C CG2 . VAL A 155 ? 2.96624 2.58434 3.29670 0.39988  0.12998  -0.10958 149 VAL A CG2 
1121 N N   . TYR A 156 ? 3.11476 2.81697 3.57353 0.42584  0.16293  0.07580  150 TYR A N   
1122 C CA  . TYR A 156 ? 3.14425 2.83035 3.61098 0.43806  0.18085  0.11557  150 TYR A CA  
1123 C C   . TYR A 156 ? 3.23766 2.86219 3.65409 0.49008  0.22432  0.13394  150 TYR A C   
1124 O O   . TYR A 156 ? 3.19369 2.82758 3.59566 0.53103  0.23976  0.14551  150 TYR A O   
1125 C CB  . TYR A 156 ? 3.29109 3.06197 3.83711 0.44364  0.15972  0.17271  150 TYR A CB  
1126 C CG  . TYR A 156 ? 3.53236 3.29020 4.08705 0.46850  0.18044  0.22026  150 TYR A CG  
1127 C CD1 . TYR A 156 ? 3.41571 3.14637 3.95867 0.44576  0.17634  0.21208  150 TYR A CD1 
1128 C CD2 . TYR A 156 ? 3.63342 3.41009 4.20834 0.51765  0.20548  0.27614  150 TYR A CD2 
1129 C CE1 . TYR A 156 ? 3.36450 3.08104 3.91183 0.47058  0.19446  0.25494  150 TYR A CE1 
1130 C CE2 . TYR A 156 ? 3.56381 3.32862 4.14665 0.54163  0.22305  0.31818  150 TYR A CE2 
1131 C CZ  . TYR A 156 ? 3.35034 3.08219 3.91757 0.51754  0.21627  0.30572  150 TYR A CZ  
1132 O OH  . TYR A 156 ? 2.99607 2.71398 3.56778 0.54338  0.23295  0.34697  150 TYR A OH  
1133 N N   . SER A 157 ? 3.42720 2.98963 3.81470 0.49237  0.24370  0.13806  151 SER A N   
1134 C CA  . SER A 157 ? 3.51422 3.00922 3.84918 0.54350  0.28060  0.15195  151 SER A CA  
1135 C C   . SER A 157 ? 3.51071 2.97388 3.84703 0.54468  0.29480  0.18207  151 SER A C   
1136 O O   . SER A 157 ? 3.26490 2.70281 3.60193 0.50203  0.28429  0.16279  151 SER A O   
1137 C CB  . SER A 157 ? 3.32421 2.72671 3.58645 0.54631  0.28589  0.09104  151 SER A CB  
1138 O OG  . SER A 157 ? 3.37567 2.70615 3.58167 0.60113  0.31532  0.10028  151 SER A OG  
1139 N N   . ASP A 158 ? 3.57982 3.04766 3.91672 0.59605  0.32016  0.23195  152 ASP A N   
1140 C CA  . ASP A 158 ? 3.62235 3.05391 3.95319 0.60689  0.33651  0.26255  152 ASP A CA  
1141 C C   . ASP A 158 ? 3.68621 3.00733 3.94064 0.63744  0.36279  0.24250  152 ASP A C   
1142 O O   . ASP A 158 ? 3.45313 2.74452 3.69303 0.67253  0.38443  0.27683  152 ASP A O   
1143 C CB  . ASP A 158 ? 3.58167 3.08573 3.96625 0.64410  0.34406  0.33035  152 ASP A CB  
1144 C CG  . ASP A 158 ? 3.55068 3.07873 3.92757 0.70357  0.36792  0.35702  152 ASP A CG  
1145 O OD1 . ASP A 158 ? 3.58846 3.08379 3.91602 0.71697  0.37440  0.31982  152 ASP A OD1 
1146 O OD2 . ASP A 158 ? 3.45581 3.03817 3.87678 0.74022  0.38012  0.41687  152 ASP A OD2 
1147 N N   . TYR A 159 ? 3.73588 2.99237 3.94244 0.62623  0.35668  0.18549  153 TYR A N   
1148 C CA  . TYR A 159 ? 3.62041 2.76277 3.75594 0.65607  0.37074  0.15883  153 TYR A CA  
1149 C C   . TYR A 159 ? 3.55666 2.62811 3.68976 0.60641  0.36288  0.13899  153 TYR A C   
1150 O O   . TYR A 159 ? 3.64646 2.72086 3.79877 0.55064  0.34188  0.10327  153 TYR A O   
1151 C CB  . TYR A 159 ? 3.52006 2.62379 3.60641 0.67593  0.36236  0.10636  153 TYR A CB  
1152 C CG  . TYR A 159 ? 3.76632 2.76235 3.77394 0.73348  0.37401  0.08485  153 TYR A CG  
1153 C CD1 . TYR A 159 ? 4.10866 3.10158 4.09011 0.80164  0.40186  0.12820  153 TYR A CD1 
1154 C CD2 . TYR A 159 ? 3.89535 2.79228 3.85632 0.72304  0.35300  0.01985  153 TYR A CD2 
1155 C CE1 . TYR A 159 ? 4.35666 3.24863 4.25948 0.86126  0.40842  0.10541  153 TYR A CE1 
1156 C CE2 . TYR A 159 ? 4.20955 3.00066 4.09669 0.78052  0.35482  -0.00444 153 TYR A CE2 
1157 C CZ  . TYR A 159 ? 4.26471 3.05286 4.11883 0.85138  0.38250  0.03740  153 TYR A CZ  
1158 O OH  . TYR A 159 ? 4.25830 2.93844 4.03241 0.91503  0.38036  0.00997  153 TYR A OH  
1159 N N   . PRO A 160 ? 3.61522 2.62687 3.72903 0.62487  0.37975  0.16442  154 PRO A N   
1160 C CA  . PRO A 160 ? 3.61463 2.56815 3.73614 0.57707  0.37557  0.15859  154 PRO A CA  
1161 C C   . PRO A 160 ? 3.67775 2.54548 3.77755 0.54489  0.35724  0.09998  154 PRO A C   
1162 O O   . PRO A 160 ? 3.42882 2.30420 3.56367 0.48443  0.34499  0.08702  154 PRO A O   
1163 C CB  . PRO A 160 ? 3.57225 2.46728 3.66588 0.61904  0.39807  0.19633  154 PRO A CB  
1164 C CG  . PRO A 160 ? 3.60600 2.57774 3.70840 0.67249  0.41328  0.23857  154 PRO A CG  
1165 C CD  . PRO A 160 ? 3.64536 2.66277 3.74378 0.68824  0.40486  0.21242  154 PRO A CD  
1166 N N   . PRO A 161 ? 3.92803 2.71338 3.97259 0.58540  0.35236  0.06350  155 PRO A N   
1167 C CA  . PRO A 161 ? 3.95299 2.64942 3.98580 0.55250  0.32674  0.00572  155 PRO A CA  
1168 C C   . PRO A 161 ? 3.58939 2.34344 3.65621 0.50210  0.30507  -0.03146 155 PRO A C   
1169 O O   . PRO A 161 ? 3.54096 2.25238 3.63128 0.44991  0.28591  -0.06296 155 PRO A O   
1170 C CB  . PRO A 161 ? 3.90383 2.51292 3.86311 0.62204  0.32111  -0.02722 155 PRO A CB  
1171 C CG  . PRO A 161 ? 3.80812 2.43569 3.74128 0.68508  0.35056  0.02320  155 PRO A CG  
1172 C CD  . PRO A 161 ? 3.90087 2.66284 3.88994 0.66615  0.36697  0.07161  155 PRO A CD  
1173 N N   . LEU A 162 ? 3.25604 2.10696 3.33142 0.51577  0.30641  -0.02643 156 LEU A N   
1174 C CA  . LEU A 162 ? 3.30209 2.21059 3.40888 0.46916  0.28407  -0.06124 156 LEU A CA  
1175 C C   . LEU A 162 ? 3.25781 2.23911 3.42687 0.40831  0.28204  -0.03701 156 LEU A C   
1176 O O   . LEU A 162 ? 3.10650 2.10077 3.30286 0.35655  0.26273  -0.06997 156 LEU A O   
1177 C CB  . LEU A 162 ? 3.67386 2.65876 3.77081 0.50581  0.28410  -0.06092 156 LEU A CB  
1178 C CG  . LEU A 162 ? 3.73758 2.76621 3.85120 0.47031  0.25782  -0.10631 156 LEU A CG  
1179 C CD1 . LEU A 162 ? 3.75552 2.68544 3.83057 0.46588  0.23600  -0.17304 156 LEU A CD1 
1180 C CD2 . LEU A 162 ? 3.47750 2.58896 3.58972 0.50804  0.26136  -0.09070 156 LEU A CD2 
1181 N N   . ALA A 163 ? 3.26784 2.29786 3.45777 0.41801  0.30025  0.01932  157 ALA A N   
1182 C CA  . ALA A 163 ? 3.18556 2.28260 3.42444 0.37159  0.29676  0.04253  157 ALA A CA  
1183 C C   . ALA A 163 ? 3.12155 2.15476 3.36928 0.33302  0.30217  0.04275  157 ALA A C   
1184 O O   . ALA A 163 ? 2.91956 1.99661 3.20332 0.28569  0.29444  0.04042  157 ALA A O   
1185 C CB  . ALA A 163 ? 3.31357 2.47704 3.57054 0.39967  0.30929  0.10049  157 ALA A CB  
1186 N N   . THR A 164 ? 3.30395 2.23598 3.52155 0.35464  0.31483  0.04841  158 THR A N   
1187 C CA  . THR A 164 ? 3.59803 2.46336 3.83285 0.31700  0.31879  0.05443  158 THR A CA  
1188 C C   . THR A 164 ? 3.62650 2.46158 3.88362 0.26930  0.29520  0.00319  158 THR A C   
1189 O O   . THR A 164 ? 3.73026 2.57359 4.03085 0.21910  0.29572  0.01235  158 THR A O   
1190 C CB  . THR A 164 ? 3.60780 2.36360 3.80570 0.35415  0.33091  0.06903  158 THR A CB  
1191 O OG1 . THR A 164 ? 3.34398 2.13372 3.52328 0.40077  0.35269  0.11634  158 THR A OG1 
1192 C CG2 . THR A 164 ? 3.64387 2.33364 3.87015 0.31355  0.33528  0.08657  158 THR A CG2 
1193 N N   . ASP A 165 ? 3.52805 2.33138 3.75734 0.28699  0.27465  -0.04898 159 ASP A N   
1194 C CA  . ASP A 165 ? 3.65507 2.43234 3.90724 0.24396  0.24730  -0.10220 159 ASP A CA  
1195 C C   . ASP A 165 ? 3.64381 2.53277 3.93960 0.19901  0.24058  -0.10686 159 ASP A C   
1196 O O   . ASP A 165 ? 3.84598 2.73290 4.18253 0.14841  0.22643  -0.12980 159 ASP A O   
1197 C CB  . ASP A 165 ? 3.78028 2.50023 3.98282 0.28321  0.22509  -0.15845 159 ASP A CB  
1198 C CG  . ASP A 165 ? 3.97471 2.61262 4.19345 0.25008  0.19210  -0.21428 159 ASP A CG  
1199 O OD1 . ASP A 165 ? 3.91183 2.52558 4.18516 0.19778  0.18957  -0.20201 159 ASP A OD1 
1200 O OD2 . ASP A 165 ? 4.09402 2.69306 4.27387 0.27815  0.16780  -0.26833 159 ASP A OD2 
1201 N N   . LEU A 166 ? 3.37330 2.36021 3.66529 0.21786  0.24750  -0.08487 160 LEU A N   
1202 C CA  . LEU A 166 ? 3.27220 2.36438 3.60250 0.18075  0.23734  -0.08678 160 LEU A CA  
1203 C C   . LEU A 166 ? 3.23304 2.36091 3.59874 0.15125  0.25385  -0.04206 160 LEU A C   
1204 O O   . LEU A 166 ? 3.15102 2.34140 3.55120 0.11208  0.24538  -0.04961 160 LEU A O   
1205 C CB  . LEU A 166 ? 3.10211 2.28090 3.42318 0.21187  0.23185  -0.07692 160 LEU A CB  
1206 C CG  . LEU A 166 ? 3.05680 2.34150 3.41156 0.18169  0.21167  -0.08619 160 LEU A CG  
1207 C CD1 . LEU A 166 ? 3.12845 2.40718 3.49170 0.14641  0.18810  -0.14543 160 LEU A CD1 
1208 C CD2 . LEU A 166 ? 2.93930 2.29837 3.29409 0.21480  0.20227  -0.06860 160 LEU A CD2 
1209 N N   . ARG A 167 ? 3.14929 2.24064 3.50369 0.17379  0.27814  0.00557  161 ARG A N   
1210 C CA  . ARG A 167 ? 3.18175 2.29872 3.56365 0.15146  0.29699  0.05159  161 ARG A CA  
1211 C C   . ARG A 167 ? 3.52157 2.58838 3.94035 0.10282  0.29822  0.04286  161 ARG A C   
1212 O O   . ARG A 167 ? 3.51449 2.63596 3.96895 0.07177  0.30822  0.06837  161 ARG A O   
1213 C CB  . ARG A 167 ? 3.39147 2.47242 3.74941 0.19010  0.32163  0.10315  161 ARG A CB  
1214 C CG  . ARG A 167 ? 3.55558 2.67143 3.93222 0.17922  0.34309  0.15711  161 ARG A CG  
1215 C CD  . ARG A 167 ? 3.67223 2.70022 4.06562 0.15482  0.36088  0.17834  161 ARG A CD  
1216 N NE  . ARG A 167 ? 3.66207 2.58290 4.02350 0.18620  0.36644  0.18135  161 ARG A NE  
1217 C CZ  . ARG A 167 ? 3.78914 2.61118 4.16149 0.17203  0.37367  0.19410  161 ARG A CZ  
1218 N NH1 . ARG A 167 ? 3.83428 2.65234 4.25740 0.12342  0.37938  0.21091  161 ARG A NH1 
1219 N NH2 . ARG A 167 ? 3.89904 2.62517 4.23396 0.20908  0.37384  0.19218  161 ARG A NH2 
1220 N N   . ARG A 168 ? 3.64908 2.61379 4.06269 0.09858  0.28625  0.00883  162 ARG A N   
1221 C CA  . ARG A 168 ? 3.65976 2.57473 4.12305 0.04865  0.27898  -0.00233 162 ARG A CA  
1222 C C   . ARG A 168 ? 3.56875 2.55981 4.07030 0.00690  0.26088  -0.03711 162 ARG A C   
1223 O O   . ARG A 168 ? 3.40534 2.40593 3.96464 -0.03973 0.26360  -0.02597 162 ARG A O   
1224 C CB  . ARG A 168 ? 3.69773 2.48056 4.14515 0.05951  0.25869  -0.03950 162 ARG A CB  
1225 C CG  . ARG A 168 ? 3.97747 2.66617 4.41086 0.08172  0.27471  0.00031  162 ARG A CG  
1226 C CD  . ARG A 168 ? 4.05635 2.60837 4.47389 0.09482  0.24530  -0.04318 162 ARG A CD  
1227 N NE  . ARG A 168 ? 4.01460 2.53414 4.35478 0.16051  0.23842  -0.07230 162 ARG A NE  
1228 C CZ  . ARG A 168 ? 3.87639 2.33786 4.16917 0.21098  0.25192  -0.04787 162 ARG A CZ  
1229 N NH1 . ARG A 168 ? 3.51180 1.93323 3.82297 0.20308  0.27073  0.00347  162 ARG A NH1 
1230 N NH2 . ARG A 168 ? 3.83786 2.28396 4.06314 0.27338  0.24779  -0.07297 162 ARG A NH2 
1231 N N   . ARG A 169 ? 3.57971 2.62762 4.05393 0.02337  0.24264  -0.07610 163 ARG A N   
1232 C CA  . ARG A 169 ? 3.41681 2.54902 3.92219 -0.01154 0.22555  -0.10610 163 ARG A CA  
1233 C C   . ARG A 169 ? 3.30539 2.54405 3.83355 -0.02319 0.24361  -0.06103 163 ARG A C   
1234 O O   . ARG A 169 ? 3.11375 2.41032 3.68351 -0.06071 0.23956  -0.06756 163 ARG A O   
1235 C CB  . ARG A 169 ? 3.35542 2.52134 3.82408 0.01280  0.20104  -0.15372 163 ARG A CB  
1236 C CG  . ARG A 169 ? 3.45647 2.52568 3.88523 0.04204  0.18581  -0.19518 163 ARG A CG  
1237 C CD  . ARG A 169 ? 3.64856 2.63322 4.10575 0.00878  0.16552  -0.23569 163 ARG A CD  
1238 N NE  . ARG A 169 ? 3.55289 2.45810 3.96370 0.04227  0.14122  -0.28951 163 ARG A NE  
1239 C CZ  . ARG A 169 ? 3.45256 2.25426 3.82455 0.08115  0.14178  -0.29062 163 ARG A CZ  
1240 N NH1 . ARG A 169 ? 3.77570 2.53537 4.15258 0.08784  0.16482  -0.24106 163 ARG A NH1 
1241 N NH2 . ARG A 169 ? 3.09579 1.83411 3.41827 0.11884  0.11761  -0.34335 163 ARG A NH2 
1242 N N   . PHE A 170 ? 3.35712 2.62389 3.85711 0.01295  0.26195  -0.01591 164 PHE A N   
1243 C CA  . PHE A 170 ? 3.39904 2.75997 3.91067 0.01287  0.27611  0.02664  164 PHE A CA  
1244 C C   . PHE A 170 ? 3.35460 2.69967 3.90509 -0.01534 0.30461  0.07208  164 PHE A C   
1245 O O   . PHE A 170 ? 3.24396 2.67240 3.81858 -0.03045 0.31344  0.09340  164 PHE A O   
1246 C CB  . PHE A 170 ? 3.43019 2.81546 3.90343 0.06234  0.28286  0.06086  164 PHE A CB  
1247 C CG  . PHE A 170 ? 3.45781 2.94043 3.93238 0.07395  0.28736  0.09604  164 PHE A CG  
1248 C CD1 . PHE A 170 ? 3.33342 2.90668 3.80310 0.08413  0.25769  0.07248  164 PHE A CD1 
1249 C CD2 . PHE A 170 ? 3.55586 3.03666 4.03356 0.07940  0.31827  0.15244  164 PHE A CD2 
1250 C CE1 . PHE A 170 ? 3.25899 2.91679 3.72336 0.10283  0.25480  0.09972  164 PHE A CE1 
1251 C CE2 . PHE A 170 ? 3.53475 3.10428 4.00418 0.09952  0.32060  0.18277  164 PHE A CE2 
1252 C CZ  . PHE A 170 ? 3.38262 3.03950 3.84346 0.11308  0.28685  0.15405  164 PHE A CZ  
1253 N N   . ASP A 171 ? 3.60318 2.84371 4.16097 -0.01980 0.31850  0.08977  165 ASP A N   
1254 C CA  . ASP A 171 ? 3.78158 3.00142 4.38610 -0.04889 0.34522  0.13995  165 ASP A CA  
1255 C C   . ASP A 171 ? 3.63066 2.87167 4.30152 -0.10317 0.33591  0.11996  165 ASP A C   
1256 O O   . ASP A 171 ? 3.74895 3.04229 4.46624 -0.12745 0.35931  0.16554  165 ASP A O   
1257 C CB  . ASP A 171 ? 4.01349 3.10659 4.61293 -0.04072 0.35412  0.15912  165 ASP A CB  
1258 C CG  . ASP A 171 ? 4.00802 3.08472 4.54744 0.01349  0.36783  0.18706  165 ASP A CG  
1259 O OD1 . ASP A 171 ? 4.23175 3.39563 4.74989 0.03793  0.37986  0.21603  165 ASP A OD1 
1260 O OD2 . ASP A 171 ? 4.13948 3.11561 4.65312 0.03472  0.36375  0.17887  165 ASP A OD2 
1261 N N   . THR A 172 ? 3.43262 2.63683 4.11010 -0.12000 0.30253  0.05435  166 THR A N   
1262 C CA  . THR A 172 ? 3.36368 2.59104 4.10778 -0.17105 0.28878  0.03023  166 THR A CA  
1263 C C   . THR A 172 ? 3.25931 2.62458 4.00971 -0.17675 0.29091  0.02909  166 THR A C   
1264 O O   . THR A 172 ? 3.20721 2.62524 4.02015 -0.21423 0.29964  0.04582  166 THR A O   
1265 C CB  . THR A 172 ? 3.29737 2.44781 4.03758 -0.17990 0.24815  -0.04479 166 THR A CB  
1266 O OG1 . THR A 172 ? 3.20452 2.22531 3.92512 -0.16215 0.24236  -0.04713 166 THR A OG1 
1267 C CG2 . THR A 172 ? 3.09844 2.25683 3.91850 -0.23533 0.23069  -0.06808 166 THR A CG2 
1268 N N   . PHE A 173 ? 3.15805 2.58418 3.84834 -0.13820 0.28132  0.01198  167 PHE A N   
1269 C CA  . PHE A 173 ? 3.17383 2.72539 3.86244 -0.13623 0.27537  0.00596  167 PHE A CA  
1270 C C   . PHE A 173 ? 3.10414 2.73069 3.79022 -0.11743 0.30819  0.07334  167 PHE A C   
1271 O O   . PHE A 173 ? 2.91675 2.64101 3.62310 -0.12576 0.31262  0.08250  167 PHE A O   
1272 C CB  . PHE A 173 ? 3.43827 3.02114 4.07149 -0.10296 0.24430  -0.03925 167 PHE A CB  
1273 C CG  . PHE A 173 ? 3.44418 2.98827 4.07818 -0.11955 0.21064  -0.10892 167 PHE A CG  
1274 C CD1 . PHE A 173 ? 3.32858 2.86307 4.01381 -0.16457 0.20040  -0.13886 167 PHE A CD1 
1275 C CD2 . PHE A 173 ? 3.57386 3.09387 4.16009 -0.08786 0.18924  -0.14168 167 PHE A CD2 
1276 C CE1 . PHE A 173 ? 3.20958 2.70580 3.89029 -0.17521 0.16688  -0.20562 167 PHE A CE1 
1277 C CE2 . PHE A 173 ? 3.29088 2.77675 3.87124 -0.09695 0.16017  -0.20344 167 PHE A CE2 
1278 C CZ  . PHE A 173 ? 3.15483 2.62607 3.77839 -0.13943 0.14771  -0.23818 167 PHE A CZ  
1279 N N   . LYS A 174 ? 3.22662 2.81111 3.88394 -0.08720 0.33092  0.12027  168 LYS A N   
1280 C CA  . LYS A 174 ? 3.37776 3.02900 4.02423 -0.06182 0.36144  0.18450  168 LYS A CA  
1281 C C   . LYS A 174 ? 3.19169 2.86440 3.90180 -0.09698 0.39495  0.23383  168 LYS A C   
1282 O O   . LYS A 174 ? 3.30606 3.07324 4.01502 -0.08077 0.41647  0.27551  168 LYS A O   
1283 C CB  . LYS A 174 ? 3.55225 3.14395 4.15637 -0.02269 0.37738  0.22264  168 LYS A CB  
1284 C CG  . LYS A 174 ? 3.61436 3.26757 4.19808 0.01144  0.40712  0.28839  168 LYS A CG  
1285 C CD  . LYS A 174 ? 3.71631 3.29364 4.27044 0.04121  0.42738  0.33091  168 LYS A CD  
1286 C CE  . LYS A 174 ? 3.10358 2.73718 3.63793 0.07528  0.45903  0.39882  168 LYS A CE  
1287 N NZ  . LYS A 174 ? 2.80865 2.36548 3.31645 0.10271  0.48013  0.44254  168 LYS A NZ  
1288 N N   . ALA A 175 ? 2.99904 2.58713 3.76753 -0.14214 0.39770  0.23150  169 ALA A N   
1289 C CA  . ALA A 175 ? 3.18407 2.78812 4.03064 -0.18033 0.42866  0.28658  169 ALA A CA  
1290 C C   . ALA A 175 ? 3.28686 3.01077 4.17151 -0.19959 0.42858  0.27940  169 ALA A C   
1291 O O   . ALA A 175 ? 3.50744 3.29409 4.44265 -0.21238 0.46376  0.34146  169 ALA A O   
1292 C CB  . ALA A 175 ? 3.35490 2.83666 4.26432 -0.22631 0.41772  0.27538  169 ALA A CB  
1293 N N   . PHE A 176 ? 3.12248 2.88281 3.98419 -0.19940 0.39083  0.20767  170 PHE A N   
1294 C CA  . PHE A 176 ? 3.06276 2.93846 3.95215 -0.21246 0.38570  0.19277  170 PHE A CA  
1295 C C   . PHE A 176 ? 2.97083 2.95681 3.79427 -0.15680 0.39316  0.21235  170 PHE A C   
1296 O O   . PHE A 176 ? 3.04572 3.06681 3.81175 -0.12749 0.35847  0.16153  170 PHE A O   
1297 C CB  . PHE A 176 ? 2.93766 2.79764 3.83014 -0.23539 0.33895  0.10620  170 PHE A CB  
1298 C CG  . PHE A 176 ? 3.15206 2.91236 4.11274 -0.28710 0.32557  0.08237  170 PHE A CG  
1299 C CD1 . PHE A 176 ? 3.22926 2.86197 4.16514 -0.28349 0.30780  0.05497  170 PHE A CD1 
1300 C CD2 . PHE A 176 ? 3.05730 2.85190 4.10862 -0.33564 0.32801  0.08759  170 PHE A CD2 
1301 C CE1 . PHE A 176 ? 3.30457 2.83884 4.29803 -0.32412 0.28783  0.02806  170 PHE A CE1 
1302 C CE2 . PHE A 176 ? 3.08112 2.77838 4.20093 -0.38203 0.30728  0.06285  170 PHE A CE2 
1303 C CZ  . PHE A 176 ? 3.22233 2.78573 4.30987 -0.37466 0.28482  0.03067  170 PHE A CZ  
1304 N N   . ASN A 177 ? 2.90920 2.94867 3.74239 -0.13936 0.43675  0.28906  171 ASN A N   
1305 C CA  . ASN A 177 ? 2.98107 3.12477 3.75073 -0.07941 0.44500  0.31396  171 ASN A CA  
1306 C C   . ASN A 177 ? 2.96460 3.22516 3.77733 -0.08299 0.47689  0.35901  171 ASN A C   
1307 O O   . ASN A 177 ? 3.00046 3.25260 3.89183 -0.12126 0.51490  0.41468  171 ASN A O   
1308 C CB  . ASN A 177 ? 3.08131 3.18653 3.80229 -0.03597 0.46976  0.36901  171 ASN A CB  
1309 C CG  . ASN A 177 ? 3.03150 3.23722 3.68082 0.03350  0.47082  0.38978  171 ASN A CG  
1310 O OD1 . ASN A 177 ? 2.88055 3.16796 3.49999 0.05585  0.43902  0.34647  171 ASN A OD1 
1311 N ND2 . ASN A 177 ? 3.32886 3.52524 3.94760 0.07149  0.50354  0.45422  171 ASN A ND2 
1312 N N   . SER A 178 ? 2.91874 3.28972 3.68294 -0.04089 0.45952  0.33669  172 SER A N   
1313 C CA  . SER A 178 ? 2.95234 3.45053 3.74387 -0.03048 0.48895  0.37716  172 SER A CA  
1314 C C   . SER A 178 ? 3.08716 3.63520 3.84610 0.02266  0.53746  0.46467  172 SER A C   
1315 O O   . SER A 178 ? 3.04047 3.68497 3.73172 0.08873  0.53557  0.47344  172 SER A O   
1316 C CB  . SER A 178 ? 2.74327 3.33465 3.48857 -0.00051 0.44580  0.31309  172 SER A CB  
1317 O OG  . SER A 178 ? 2.39762 2.93934 3.16809 -0.04668 0.40131  0.23357  172 SER A OG  
1318 N N   . ALA A 179 ? 3.17901 3.65533 3.98527 -0.00397 0.57879  0.52951  173 ALA A N   
1319 C CA  . ALA A 179 ? 3.08230 3.59017 3.85976 0.04377  0.62794  0.61781  173 ALA A CA  
1320 C C   . ALA A 179 ? 3.33072 3.79710 4.21120 -0.01070 0.67930  0.69688  173 ALA A C   
1321 O O   . ALA A 179 ? 3.39577 3.73606 4.30590 -0.04826 0.67600  0.69776  173 ALA A O   
1322 C CB  . ALA A 179 ? 2.94327 3.37908 3.63269 0.09149  0.60975  0.60723  173 ALA A CB  
1323 N N   . LYS A 180 ? 3.46533 4.03907 4.40194 -0.01217 0.72450  0.76435  174 LYS A N   
1324 C CA  . LYS A 180 ? 3.83373 4.39046 4.87860 -0.05815 0.77814  0.85798  174 LYS A CA  
1325 C C   . LYS A 180 ? 4.12813 4.57343 5.27675 -0.14789 0.75106  0.81998  174 LYS A C   
1326 O O   . LYS A 180 ? 4.04288 4.48207 5.20150 -0.17635 0.70541  0.73601  174 LYS A O   
1327 C CB  . LYS A 180 ? 3.85686 4.36818 4.85792 -0.01858 0.81490  0.93124  174 LYS A CB  
1328 C CG  . LYS A 180 ? 3.40310 4.02959 4.30438 0.07525  0.84173  0.97277  174 LYS A CG  
1329 C CD  . LYS A 180 ? 3.07607 3.64135 3.92242 0.11707  0.86906  1.03187  174 LYS A CD  
1330 C CE  . LYS A 180 ? 3.04440 3.47989 3.82666 0.11937  0.81837  0.95819  174 LYS A CE  
1331 N NZ  . LYS A 180 ? 2.96196 3.43762 3.64968 0.16747  0.76314  0.86902  174 LYS A NZ  
1332 N N   . ASN A 181 ? 4.43394 4.78749 5.65825 -0.18963 0.77520  0.87983  175 ASN A N   
1333 C CA  . ASN A 181 ? 4.36834 4.60692 5.69376 -0.26958 0.74590  0.84873  175 ASN A CA  
1334 C C   . ASN A 181 ? 4.45559 4.54838 5.71172 -0.26708 0.69837  0.77181  175 ASN A C   
1335 O O   . ASN A 181 ? 4.55456 4.58570 5.74758 -0.23186 0.71030  0.79763  175 ASN A O   
1336 C CB  . ASN A 181 ? 4.23235 4.43721 5.68014 -0.31522 0.78785  0.95080  175 ASN A CB  
1337 C CG  . ASN A 181 ? 4.21918 4.37740 5.61579 -0.27520 0.82445  1.02281  175 ASN A CG  
1338 O OD1 . ASN A 181 ? 4.57683 4.78363 5.85520 -0.20284 0.83715  1.02457  175 ASN A OD1 
1339 N ND2 . ASN A 181 ? 3.88914 3.94924 5.37660 -0.32108 0.83728  1.08142  175 ASN A ND2 
1340 N N   . SER A 182 ? 4.56548 4.60760 5.83222 -0.30071 0.64589  0.67943  176 SER A N   
1341 C CA  . SER A 182 ? 4.64579 4.55784 5.85030 -0.29657 0.60075  0.60427  176 SER A CA  
1342 C C   . SER A 182 ? 4.76366 4.61718 6.02760 -0.35160 0.55239  0.52667  176 SER A C   
1343 O O   . SER A 182 ? 4.80037 4.68281 6.17312 -0.40251 0.55579  0.54517  176 SER A O   
1344 C CB  . SER A 182 ? 4.40179 4.35423 5.47460 -0.22900 0.58466  0.55879  176 SER A CB  
1345 O OG  . SER A 182 ? 4.41379 4.39843 5.42927 -0.17547 0.62264  0.62604  176 SER A OG  
1346 N N   . ALA A 183 ? 4.85604 4.62992 6.05034 -0.33866 0.50716  0.44196  177 ALA A N   
1347 C CA  . ALA A 183 ? 4.46067 4.17474 5.69414 -0.38041 0.45843  0.36221  177 ALA A CA  
1348 C C   . ALA A 183 ? 4.45477 4.28446 5.70019 -0.38883 0.44352  0.31963  177 ALA A C   
1349 O O   . ALA A 183 ? 4.59096 4.39161 5.89379 -0.43123 0.40923  0.26700  177 ALA A O   
1350 C CB  . ALA A 183 ? 4.00999 3.61730 5.15751 -0.35469 0.41945  0.28974  177 ALA A CB  
1351 N N   . ALA A 184 ? 4.09703 4.05356 5.28682 -0.34591 0.46447  0.33814  178 ALA A N   
1352 C CA  . ALA A 184 ? 3.75824 3.82987 4.95310 -0.34737 0.44994  0.29959  178 ALA A CA  
1353 C C   . ALA A 184 ? 4.23182 4.40975 5.52366 -0.37359 0.48793  0.36643  178 ALA A C   
1354 O O   . ALA A 184 ? 4.10041 4.35894 5.42646 -0.39048 0.47336  0.33351  178 ALA A O   
1355 C CB  . ALA A 184 ? 2.75750 2.91001 3.83866 -0.28172 0.44254  0.27619  178 ALA A CB  
1356 N N   . ASN A 185 ? 4.63693 4.81982 5.97652 -0.37637 0.53706  0.46208  179 ASN A N   
1357 C CA  . ASN A 185 ? 4.76395 5.05706 6.20108 -0.39664 0.58160  0.54219  179 ASN A CA  
1358 C C   . ASN A 185 ? 4.85539 5.07678 6.43775 -0.46797 0.58880  0.58820  179 ASN A C   
1359 O O   . ASN A 185 ? 5.01626 5.30772 6.70818 -0.50952 0.59589  0.60985  179 ASN A O   
1360 C CB  . ASN A 185 ? 4.68840 5.06819 6.07428 -0.33808 0.63805  0.63078  179 ASN A CB  
1361 C CG  . ASN A 185 ? 4.61286 5.11308 6.09931 -0.35235 0.69245  0.72708  179 ASN A CG  
1362 O OD1 . ASN A 185 ? 4.42185 4.88997 5.99439 -0.38126 0.72939  0.81293  179 ASN A OD1 
1363 N ND2 . ASN A 185 ? 4.72291 5.36485 6.20160 -0.33041 0.69751  0.71615  179 ASN A ND2 
1364 N N   . LEU A 186 ? 4.72802 4.81141 6.31901 -0.48250 0.58395  0.60429  180 LEU A N   
1365 C CA  . LEU A 186 ? 4.80536 4.80549 6.53560 -0.54793 0.58287  0.64871  180 LEU A CA  
1366 C C   . LEU A 186 ? 5.00172 4.86485 6.75589 -0.58861 0.51514  0.55416  180 LEU A C   
1367 O O   . LEU A 186 ? 5.04269 4.83279 6.68968 -0.55889 0.47903  0.47316  180 LEU A O   
1368 C CB  . LEU A 186 ? 4.62995 4.55775 6.36151 -0.53722 0.61764  0.73146  180 LEU A CB  
1369 C CG  . LEU A 186 ? 4.08856 4.13476 5.83750 -0.50977 0.68983  0.85001  180 LEU A CG  
1370 C CD1 . LEU A 186 ? 3.67153 3.61906 5.44154 -0.51228 0.71495  0.92653  180 LEU A CD1 
1371 C CD2 . LEU A 186 ? 3.78061 3.94776 5.66651 -0.55098 0.71683  0.90932  180 LEU A CD2 
1372 N N   . ALA A 187 ? 4.98448 4.81518 6.88414 -0.65450 0.49708  0.56773  181 ALA A N   
1373 C CA  . ALA A 187 ? 4.88848 4.57465 6.82348 -0.69241 0.42987  0.48639  181 ALA A CA  
1374 C C   . ALA A 187 ? 5.09414 4.61919 7.04895 -0.70331 0.41645  0.51021  181 ALA A C   
1375 O O   . ALA A 187 ? 5.23352 4.62113 7.17284 -0.71220 0.35848  0.43335  181 ALA A O   
1376 C CB  . ALA A 187 ? 4.41761 4.13700 6.50473 -0.75722 0.40549  0.48147  181 ALA A CB  
1377 N N   . SER A 188 ? 5.17334 4.71168 7.15783 -0.69837 0.46742  0.61425  182 SER A N   
1378 C CA  . SER A 188 ? 4.99535 4.38403 6.99024 -0.70295 0.45759  0.64274  182 SER A CA  
1379 C C   . SER A 188 ? 5.18754 4.52685 7.01839 -0.63561 0.46644  0.61672  182 SER A C   
1380 O O   . SER A 188 ? 5.02951 4.22089 6.82158 -0.62732 0.42955  0.57538  182 SER A O   
1381 C CB  . SER A 188 ? 4.56872 3.99194 6.68484 -0.73286 0.50761  0.77347  182 SER A CB  
1382 O OG  . SER A 188 ? 4.36090 3.92742 6.41800 -0.68809 0.57816  0.84616  182 SER A OG  
1383 N N   . ALA A 189 ? 5.39696 4.85825 7.13221 -0.58409 0.51209  0.64010  183 ALA A N   
1384 C CA  . ALA A 189 ? 5.33571 4.76150 6.92093 -0.51972 0.51595  0.61143  183 ALA A CA  
1385 C C   . ALA A 189 ? 5.19093 4.56811 6.68671 -0.49966 0.46313  0.49444  183 ALA A C   
1386 O O   . ALA A 189 ? 4.97355 4.28430 6.36407 -0.45505 0.45365  0.46240  183 ALA A O   
1387 C CB  . ALA A 189 ? 5.15251 4.72230 6.66550 -0.46799 0.57071  0.66475  183 ALA A CB  
1388 N N   . ALA A 190 ? 5.14096 4.55389 6.67768 -0.52957 0.43007  0.43342  184 ALA A N   
1389 C CA  . ALA A 190 ? 4.84725 4.21059 6.30415 -0.51120 0.37966  0.32528  184 ALA A CA  
1390 C C   . ALA A 190 ? 5.14839 4.34649 6.63614 -0.53476 0.32730  0.27402  184 ALA A C   
1391 O O   . ALA A 190 ? 5.01910 4.14462 6.41835 -0.50332 0.29226  0.19783  184 ALA A O   
1392 C CB  . ALA A 190 ? 4.71919 4.19284 6.19360 -0.52605 0.36480  0.27737  184 ALA A CB  
1393 N N   . ALA A 191 ? 6.17278 5.31044 7.78622 -0.58637 0.31913  0.31592  185 ALA A N   
1394 C CA  . ALA A 191 ? 6.05395 5.02369 7.69900 -0.60419 0.26319  0.27003  185 ALA A CA  
1395 C C   . ALA A 191 ? 5.91012 4.76567 7.49544 -0.56992 0.27018  0.29670  185 ALA A C   
1396 O O   . ALA A 191 ? 6.18223 4.89714 7.73685 -0.55717 0.22165  0.23837  185 ALA A O   
1397 C CB  . ALA A 191 ? 5.55915 4.50308 7.37471 -0.67485 0.24235  0.30361  185 ALA A CB  
1398 N N   . ALA A 192 ? 5.15811 4.07070 6.72217 -0.55004 0.32797  0.38185  186 ALA A N   
1399 C CA  . ALA A 192 ? 4.81047 3.62810 6.30791 -0.51194 0.33942  0.40951  186 ALA A CA  
1400 C C   . ALA A 192 ? 4.68936 3.50966 6.03290 -0.44460 0.34027  0.35547  186 ALA A C   
1401 O O   . ALA A 192 ? 4.40295 3.17131 5.68010 -0.40515 0.35806  0.38298  186 ALA A O   
1402 C CB  . ALA A 192 ? 4.60108 3.48017 6.13860 -0.51545 0.40116  0.52534  186 ALA A CB  
1403 N N   . LEU A 193 ? 4.75565 3.63601 6.04723 -0.43118 0.32085  0.28285  187 LEU A N   
1404 C CA  . LEU A 193 ? 4.41262 3.30535 5.57246 -0.37049 0.32030  0.23659  187 LEU A CA  
1405 C C   . LEU A 193 ? 4.59023 3.33692 5.69687 -0.34462 0.27597  0.17202  187 LEU A C   
1406 O O   . LEU A 193 ? 4.80402 3.48578 5.94408 -0.36661 0.22852  0.10989  187 LEU A O   
1407 C CB  . LEU A 193 ? 3.92594 2.93350 5.05517 -0.36603 0.31253  0.18502  187 LEU A CB  
1408 C CG  . LEU A 193 ? 3.70794 2.87481 4.85660 -0.37179 0.35262  0.23396  187 LEU A CG  
1409 C CD1 . LEU A 193 ? 3.13375 2.38819 4.22890 -0.35539 0.33333  0.16787  187 LEU A CD1 
1410 C CD2 . LEU A 193 ? 3.53889 2.74510 4.63723 -0.33222 0.39968  0.30644  187 LEU A CD2 
1411 N N   . PRO A 194 ? 4.66192 3.35482 5.68483 -0.29414 0.28815  0.18331  188 PRO A N   
1412 C CA  . PRO A 194 ? 4.64703 3.22522 5.59826 -0.25472 0.24916  0.11549  188 PRO A CA  
1413 C C   . PRO A 194 ? 4.49432 3.13131 5.37715 -0.22785 0.23180  0.04422  188 PRO A C   
1414 O O   . PRO A 194 ? 4.18226 2.90433 4.99845 -0.19204 0.25704  0.05340  188 PRO A O   
1415 C CB  . PRO A 194 ? 4.28796 2.82556 5.17053 -0.20591 0.27728  0.15927  188 PRO A CB  
1416 C CG  . PRO A 194 ? 4.18411 2.76980 5.12748 -0.23302 0.32066  0.25124  188 PRO A CG  
1417 C CD  . PRO A 194 ? 4.54222 3.26444 5.53981 -0.27026 0.33653  0.26286  188 PRO A CD  
1418 N N   . VAL A 195 ? 4.62770 3.22014 5.53067 -0.24474 0.18606  -0.02564 189 VAL A N   
1419 C CA  . VAL A 195 ? 4.00823 2.64484 4.84823 -0.21918 0.16567  -0.09567 189 VAL A CA  
1420 C C   . VAL A 195 ? 4.15676 2.67204 4.92039 -0.16706 0.13443  -0.14835 189 VAL A C   
1421 O O   . VAL A 195 ? 4.29917 2.72186 5.07644 -0.17207 0.08774  -0.20586 189 VAL A O   
1422 C CB  . VAL A 195 ? 3.71762 2.39659 4.62396 -0.26698 0.13739  -0.13863 189 VAL A CB  
1423 C CG1 . VAL A 195 ? 3.60649 2.34384 4.44447 -0.23920 0.12138  -0.20292 189 VAL A CG1 
1424 C CG2 . VAL A 195 ? 3.39316 2.18352 4.38447 -0.31658 0.17036  -0.07723 189 VAL A CG2 
1425 N N   . SER A 196 ? 4.11179 2.62906 4.79362 -0.11205 0.15901  -0.12827 190 SER A N   
1426 C CA  . SER A 196 ? 4.29479 2.70338 4.89988 -0.05329 0.13913  -0.16285 190 SER A CA  
1427 C C   . SER A 196 ? 4.02951 2.49461 4.55001 -0.00229 0.14029  -0.20106 190 SER A C   
1428 O O   . SER A 196 ? 3.74336 2.32509 4.25022 0.00150  0.16915  -0.17447 190 SER A O   
1429 C CB  . SER A 196 ? 4.32371 2.68035 4.90564 -0.02543 0.16669  -0.10408 190 SER A CB  
1430 O OG  . SER A 196 ? 4.19037 2.50039 4.85541 -0.07333 0.16898  -0.05876 190 SER A OG  
1431 N N   . THR A 197 ? 4.15535 2.53632 4.62081 0.03976  0.10637  -0.26194 191 THR A N   
1432 C CA  . THR A 197 ? 4.11038 2.52942 4.49185 0.09863  0.10951  -0.29090 191 THR A CA  
1433 C C   . THR A 197 ? 4.41942 2.72397 4.72640 0.16778  0.09719  -0.31001 191 THR A C   
1434 O O   . THR A 197 ? 4.57580 2.75832 4.88799 0.17057  0.05991  -0.34495 191 THR A O   
1435 C CB  . THR A 197 ? 3.99452 2.45161 4.37551 0.08678  0.07965  -0.35499 191 THR A CB  
1436 O OG1 . THR A 197 ? 4.15153 2.63785 4.45119 0.14895  0.08361  -0.37723 191 THR A OG1 
1437 C CG2 . THR A 197 ? 3.85136 2.19452 4.25684 0.07137  0.02841  -0.41497 191 THR A CG2 
1438 N N   . ALA A 198 ? 4.77043 3.11466 5.01164 0.22565  0.12621  -0.28536 192 ALA A N   
1439 C CA  . ALA A 198 ? 4.91243 3.16280 5.07611 0.30070  0.12029  -0.29842 192 ALA A CA  
1440 C C   . ALA A 198 ? 4.94768 3.17850 5.04279 0.35552  0.09513  -0.36185 192 ALA A C   
1441 O O   . ALA A 198 ? 5.37260 3.50146 5.40326 0.41799  0.07565  -0.39152 192 ALA A O   
1442 C CB  . ALA A 198 ? 4.90436 3.20704 5.03450 0.34144  0.16525  -0.23592 192 ALA A CB  
1443 N N   . TYR A 199 ? 4.43209 2.75641 4.53570 0.33805  0.09378  -0.38339 193 TYR A N   
1444 C CA  . TYR A 199 ? 4.39177 2.71194 4.42874 0.39230  0.07510  -0.43676 193 TYR A CA  
1445 C C   . TYR A 199 ? 4.27876 2.64540 4.35538 0.34183  0.04893  -0.48219 193 TYR A C   
1446 O O   . TYR A 199 ? 4.24800 2.70571 4.39108 0.27835  0.06186  -0.45684 193 TYR A O   
1447 C CB  . TYR A 199 ? 4.34655 2.75736 4.33354 0.44928  0.11344  -0.39887 193 TYR A CB  
1448 C CG  . TYR A 199 ? 4.40878 2.80262 4.37349 0.48841  0.14610  -0.34163 193 TYR A CG  
1449 C CD1 . TYR A 199 ? 4.52770 2.81805 4.42160 0.56077  0.13868  -0.35650 193 TYR A CD1 
1450 C CD2 . TYR A 199 ? 4.25410 2.73316 4.26544 0.45711  0.18117  -0.27522 193 TYR A CD2 
1451 C CE1 . TYR A 199 ? 4.57955 2.85477 4.45253 0.59799  0.16787  -0.30511 193 TYR A CE1 
1452 C CE2 . TYR A 199 ? 4.24473 2.70779 4.23644 0.49362  0.20929  -0.22420 193 TYR A CE2 
1453 C CZ  . TYR A 199 ? 4.50519 2.86736 4.42932 0.56232  0.20373  -0.23858 193 TYR A CZ  
1454 O OH  . TYR A 199 ? 4.61136 2.95839 4.51519 0.60031  0.23128  -0.18854 193 TYR A OH  
1455 N N   . HIS A 200 ? 4.29010 2.59347 4.32122 0.37542  0.01057  -0.55084 194 HIS A N   
1456 C CA  . HIS A 200 ? 4.35103 2.68711 4.41135 0.33561  -0.01945 -0.60234 194 HIS A CA  
1457 C C   . HIS A 200 ? 4.33490 2.63732 4.30670 0.40894  -0.04246 -0.66052 194 HIS A C   
1458 O O   . HIS A 200 ? 4.27668 2.55762 4.16914 0.48868  -0.02598 -0.64975 194 HIS A O   
1459 C CB  . HIS A 200 ? 4.46924 2.73417 4.60764 0.26854  -0.05762 -0.63029 194 HIS A CB  
1460 C CG  . HIS A 200 ? 4.32290 2.43798 4.44605 0.29572  -0.08873 -0.65008 194 HIS A CG  
1461 N ND1 . HIS A 200 ? 4.31235 2.31487 4.38653 0.34099  -0.14233 -0.72448 194 HIS A ND1 
1462 C CD2 . HIS A 200 ? 4.23290 2.28805 4.38265 0.28639  -0.07824 -0.60660 194 HIS A CD2 
1463 C CE1 . HIS A 200 ? 4.36651 2.24370 4.43947 0.35836  -0.16699 -0.72766 194 HIS A CE1 
1464 N NE2 . HIS A 200 ? 4.30364 2.21034 4.42349 0.32406  -0.12756 -0.65524 194 HIS A NE2 
1465 N N   . ILE A 201 ? 4.34495 2.64637 4.32896 0.38562  -0.07966 -0.72092 195 ILE A N   
1466 C CA  . ILE A 201 ? 4.27769 2.55707 4.17557 0.45575  -0.10090 -0.77615 195 ILE A CA  
1467 C C   . ILE A 201 ? 4.23731 2.37186 4.06020 0.53062  -0.13479 -0.82096 195 ILE A C   
1468 O O   . ILE A 201 ? 4.09691 2.21189 3.82423 0.61584  -0.13963 -0.85040 195 ILE A O   
1469 C CB  . ILE A 201 ? 4.14014 2.44727 4.07018 0.41172  -0.13681 -0.83364 195 ILE A CB  
1470 C CG1 . ILE A 201 ? 3.90271 2.24264 3.74727 0.47960  -0.13892 -0.86606 195 ILE A CG1 
1471 C CG2 . ILE A 201 ? 4.07923 2.26476 4.04204 0.38617  -0.19690 -0.89770 195 ILE A CG2 
1472 C CD1 . ILE A 201 ? 3.45875 1.82258 3.32484 0.44407  -0.17577 -0.92599 195 ILE A CD1 
1473 N N   . LYS A 202 ? 4.37037 2.40256 4.23315 0.50505  -0.15982 -0.82524 196 LYS A N   
1474 C CA  . LYS A 202 ? 4.76643 2.65166 4.56132 0.57673  -0.19845 -0.86698 196 LYS A CA  
1475 C C   . LYS A 202 ? 4.83853 2.70601 4.58608 0.63130  -0.15982 -0.81115 196 LYS A C   
1476 O O   . LYS A 202 ? 5.01491 2.75985 4.70119 0.69668  -0.19003 -0.84076 196 LYS A O   
1477 C CB  . LYS A 202 ? 4.90217 2.67237 4.77377 0.51991  -0.25825 -0.90687 196 LYS A CB  
1478 C CG  . LYS A 202 ? 4.63253 2.39721 4.54533 0.47850  -0.30821 -0.97413 196 LYS A CG  
1479 C CD  . LYS A 202 ? 4.14811 1.81989 4.16733 0.40691  -0.36148 -0.99597 196 LYS A CD  
1480 C CE  . LYS A 202 ? 3.97103 1.72452 4.10753 0.30984  -0.31927 -0.91832 196 LYS A CE  
1481 N NZ  . LYS A 202 ? 3.86127 1.76990 4.03727 0.25659  -0.28164 -0.89564 196 LYS A NZ  
1482 N N   . ASN A 203 ? 4.66994 2.65422 4.44373 0.60917  -0.09806 -0.73377 197 ASN A N   
1483 C CA  . ASN A 203 ? 4.64201 2.62426 4.37695 0.65878  -0.05787 -0.67594 197 ASN A CA  
1484 C C   . ASN A 203 ? 4.50024 2.63626 4.25586 0.64509  0.00425  -0.60312 197 ASN A C   
1485 O O   . ASN A 203 ? 4.36355 2.55591 4.19457 0.57885  0.02996  -0.54982 197 ASN A O   
1486 C CB  . ASN A 203 ? 4.70156 2.59868 4.49316 0.61593  -0.06856 -0.65289 197 ASN A CB  
1487 C CG  . ASN A 203 ? 4.75622 2.65211 4.51042 0.66400  -0.02726 -0.59235 197 ASN A CG  
1488 O OD1 . ASN A 203 ? 4.47571 2.28768 4.14454 0.75055  -0.03881 -0.61154 197 ASN A OD1 
1489 N ND2 . ASN A 203 ? 4.92804 2.91709 4.74328 0.61230  0.01914  -0.52040 197 ASN A ND2 
1490 N N   . PRO A 204 ? 4.47410 2.68134 4.16832 0.70734  0.02713  -0.59720 198 PRO A N   
1491 C CA  . PRO A 204 ? 4.29185 2.64166 4.01496 0.69611  0.07928  -0.52631 198 PRO A CA  
1492 C C   . PRO A 204 ? 4.41949 2.77474 4.11756 0.74573  0.11918  -0.46341 198 PRO A C   
1493 O O   . PRO A 204 ? 4.48801 2.74306 4.12537 0.80725  0.11042  -0.47690 198 PRO A O   
1494 C CB  . PRO A 204 ? 4.17924 2.59271 3.85058 0.74674  0.08263  -0.54583 198 PRO A CB  
1495 C CG  . PRO A 204 ? 4.41591 2.72204 4.03346 0.77502  0.03000  -0.63350 198 PRO A CG  
1496 C CD  . PRO A 204 ? 4.56764 2.73580 4.17288 0.78474  0.00193  -0.65666 198 PRO A CD  
1497 N N   . ILE A 205 ? 4.33413 2.80790 4.08097 0.72013  0.15966  -0.39555 199 ILE A N   
1498 C CA  . ILE A 205 ? 4.26305 2.76577 3.99729 0.76430  0.20023  -0.32911 199 ILE A CA  
1499 C C   . ILE A 205 ? 4.02007 2.64680 3.74879 0.80376  0.23246  -0.28682 199 ILE A C   
1500 O O   . ILE A 205 ? 3.56828 2.29945 3.36114 0.75077  0.23906  -0.26246 199 ILE A O   
1501 C CB  . ILE A 205 ? 4.20948 2.73291 4.01737 0.69787  0.21559  -0.27986 199 ILE A CB  
1502 C CG1 . ILE A 205 ? 4.22688 2.80133 4.02840 0.74282  0.25764  -0.20854 199 ILE A CG1 
1503 C CG2 . ILE A 205 ? 4.07193 2.68810 3.96135 0.61123  0.21169  -0.27221 199 ILE A CG2 
1504 C CD1 . ILE A 205 ? 4.08513 2.66956 3.94604 0.68972  0.27172  -0.16160 199 ILE A CD1 
1505 N N   . GLY A 206 ? 4.05617 2.67249 3.71071 0.89921  0.25068  -0.27643 200 GLY A N   
1506 C CA  . GLY A 206 ? 3.90073 2.63313 3.55279 0.94310  0.28136  -0.23288 200 GLY A CA  
1507 C C   . GLY A 206 ? 3.87870 2.66082 3.53858 0.92091  0.26259  -0.26803 200 GLY A C   
1508 O O   . GLY A 206 ? 3.93116 2.82926 3.62950 0.91893  0.28267  -0.22401 200 GLY A O   
1509 N N   . GLY A 207 ? 4.02891 2.72433 3.65797 0.90364  0.22118  -0.34602 201 GLY A N   
1510 C CA  . GLY A 207 ? 4.13043 2.86642 3.76827 0.87675  0.19918  -0.38529 201 GLY A CA  
1511 C C   . GLY A 207 ? 3.74723 2.55340 3.48163 0.77290  0.18837  -0.37787 201 GLY A C   
1512 O O   . GLY A 207 ? 3.43471 2.31075 3.18908 0.75189  0.17963  -0.38832 201 GLY A O   
1513 N N   . VAL A 208 ? 3.13329 3.24014 3.44427 0.57497  0.10319  -0.18158 202 VAL A N   
1514 C CA  . VAL A 208 ? 2.98105 3.08092 3.30163 0.52346  0.08992  -0.15865 202 VAL A CA  
1515 C C   . VAL A 208 ? 3.01511 3.01620 3.28583 0.51038  0.05479  -0.15860 202 VAL A C   
1516 O O   . VAL A 208 ? 2.88189 2.83365 3.13604 0.54157  0.03038  -0.16835 202 VAL A O   
1517 C CB  . VAL A 208 ? 2.85191 3.01819 3.23818 0.51913  0.08523  -0.14204 202 VAL A CB  
1518 C CG1 . VAL A 208 ? 3.02933 3.17805 3.41442 0.46976  0.06881  -0.12152 202 VAL A CG1 
1519 C CG2 . VAL A 208 ? 2.64262 2.91089 3.08413 0.52526  0.12016  -0.13833 202 VAL A CG2 
1520 N N   . PHE A 209 ? 3.04341 3.01605 3.29130 0.46434  0.05199  -0.14706 203 PHE A N   
1521 C CA  . PHE A 209 ? 3.14533 3.03381 3.35139 0.44358  0.02220  -0.14210 203 PHE A CA  
1522 C C   . PHE A 209 ? 2.99736 2.89478 3.20745 0.39171  0.02461  -0.12286 203 PHE A C   
1523 O O   . PHE A 209 ? 2.77708 2.72812 3.00888 0.37266  0.04806  -0.11848 203 PHE A O   
1524 C CB  . PHE A 209 ? 3.38285 3.19983 3.53479 0.45357  0.01458  -0.15969 203 PHE A CB  
1525 C CG  . PHE A 209 ? 3.32178 3.15439 3.45997 0.43462  0.03758  -0.16474 203 PHE A CG  
1526 C CD1 . PHE A 209 ? 3.24409 3.12349 3.38828 0.46064  0.06503  -0.17804 203 PHE A CD1 
1527 C CD2 . PHE A 209 ? 3.24305 3.04444 3.36181 0.39156  0.03150  -0.15564 203 PHE A CD2 
1528 C CE1 . PHE A 209 ? 3.28277 3.17082 3.40861 0.44336  0.08309  -0.18122 203 PHE A CE1 
1529 C CE2 . PHE A 209 ? 3.05445 2.86824 3.16171 0.37617  0.04854  -0.16052 203 PHE A CE2 
1530 C CZ  . PHE A 209 ? 3.11309 2.96654 3.22106 0.40185  0.07282  -0.17293 203 PHE A CZ  
1531 N N   . PHE A 210 ? 3.05783 2.90052 3.24460 0.36976  -0.00003 -0.11119 204 PHE A N   
1532 C CA  . PHE A 210 ? 2.83721 2.68481 3.02326 0.32382  0.00163  -0.09412 204 PHE A CA  
1533 C C   . PHE A 210 ? 2.93774 2.73387 3.08680 0.29712  -0.00118 -0.09538 204 PHE A C   
1534 O O   . PHE A 210 ? 3.16570 2.89506 3.28089 0.30434  -0.02092 -0.10031 204 PHE A O   
1535 C CB  . PHE A 210 ? 2.81190 2.64070 2.99601 0.31380  -0.02106 -0.07726 204 PHE A CB  
1536 C CG  . PHE A 210 ? 3.02746 2.91336 3.25421 0.33132  -0.02151 -0.07294 204 PHE A CG  
1537 C CD1 . PHE A 210 ? 2.98545 2.93914 3.24838 0.31447  -0.00285 -0.06759 204 PHE A CD1 
1538 C CD2 . PHE A 210 ? 3.14650 3.01614 3.37882 0.36415  -0.04405 -0.07394 204 PHE A CD2 
1539 C CE1 . PHE A 210 ? 3.14234 3.14916 3.44867 0.32735  -0.00658 -0.06263 204 PHE A CE1 
1540 C CE2 . PHE A 210 ? 3.00096 2.92750 3.27900 0.37971  -0.04725 -0.06964 204 PHE A CE2 
1541 C CZ  . PHE A 210 ? 3.24967 3.24606 3.56591 0.35978  -0.02854 -0.06355 204 PHE A CZ  
1542 N N   . THR A 211 ? 2.84155 2.66837 2.99964 0.26630  0.01622  -0.09095 205 THR A N   
1543 C CA  . THR A 211 ? 2.95603 2.74720 3.09054 0.23516  0.01344  -0.08870 205 THR A CA  
1544 C C   . THR A 211 ? 2.95538 2.75337 3.09288 0.19983  0.01204  -0.07052 205 THR A C   
1545 O O   . THR A 211 ? 2.89311 2.73530 3.05295 0.19604  0.01966  -0.06330 205 THR A O   
1546 C CB  . THR A 211 ? 3.06363 2.88240 3.20429 0.22951  0.03283  -0.09919 205 THR A CB  
1547 O OG1 . THR A 211 ? 3.18566 3.07076 3.35956 0.22514  0.05285  -0.09505 205 THR A OG1 
1548 C CG2 . THR A 211 ? 2.76054 2.56063 2.88380 0.26313  0.03317  -0.11790 205 THR A CG2 
1549 N N   . ASP A 212 ? 3.05494 2.80921 3.16895 0.17360  0.00198  -0.06315 206 ASP A N   
1550 C CA  . ASP A 212 ? 3.04643 2.80016 3.15455 0.14233  0.00061  -0.04491 206 ASP A CA  
1551 C C   . ASP A 212 ? 3.04955 2.81339 3.16088 0.10908  0.01265  -0.04299 206 ASP A C   
1552 O O   . ASP A 212 ? 3.06495 2.82632 3.18057 0.10904  0.01616  -0.05466 206 ASP A O   
1553 C CB  . ASP A 212 ? 3.01346 2.70509 3.08999 0.14021  -0.02440 -0.03159 206 ASP A CB  
1554 C CG  . ASP A 212 ? 3.01477 2.70054 3.09231 0.17415  -0.03881 -0.03254 206 ASP A CG  
1555 O OD1 . ASP A 212 ? 2.87825 2.61164 2.97741 0.18002  -0.03119 -0.02982 206 ASP A OD1 
1556 O OD2 . ASP A 212 ? 3.15504 2.78856 3.21373 0.19612  -0.05967 -0.03705 206 ASP A OD2 
1557 N N   . SER A 213 ? 2.95250 2.72912 3.06100 0.08212  0.01844  -0.02854 207 SER A N   
1558 C CA  . SER A 213 ? 2.99020 2.78905 3.10804 0.05167  0.03295  -0.02588 207 SER A CA  
1559 C C   . SER A 213 ? 3.05476 2.85322 3.15584 0.02705  0.03579  -0.00720 207 SER A C   
1560 O O   . SER A 213 ? 2.92457 2.72343 3.01314 0.03592  0.03085  -0.00012 207 SER A O   
1561 C CB  . SER A 213 ? 2.83141 2.68625 2.97877 0.05692  0.05185  -0.03897 207 SER A CB  
1562 O OG  . SER A 213 ? 2.86516 2.74343 3.02534 0.03233  0.06452  -0.03906 207 SER A OG  
1563 N N   . PRO A 214 ? 3.01193 2.81133 3.11167 -0.00398 0.04358  0.00179  208 PRO A N   
1564 C CA  . PRO A 214 ? 3.11714 2.91885 3.23574 -0.01940 0.04662  -0.00418 208 PRO A CA  
1565 C C   . PRO A 214 ? 3.38321 3.12292 3.48499 -0.02345 0.02329  0.00040  208 PRO A C   
1566 O O   . PRO A 214 ? 3.66707 3.36194 3.74509 -0.00473 0.00464  0.00223  208 PRO A O   
1567 C CB  . PRO A 214 ? 3.16765 3.00269 3.29327 -0.05112 0.06522  0.00720  208 PRO A CB  
1568 C CG  . PRO A 214 ? 3.17507 2.98781 3.26499 -0.05968 0.06190  0.02715  208 PRO A CG  
1569 C CD  . PRO A 214 ? 2.80755 2.61133 2.88657 -0.02749 0.05108  0.02029  208 PRO A CD  
1570 N N   . GLU A 215 ? 3.42935 3.16429 3.54461 -0.04735 0.02143  0.00167  209 GLU A N   
1571 C CA  . GLU A 215 ? 3.63795 3.30905 3.73754 -0.05233 -0.00496 0.00375  209 GLU A CA  
1572 C C   . GLU A 215 ? 3.70746 3.33318 3.78019 -0.07924 -0.01748 0.03006  209 GLU A C   
1573 O O   . GLU A 215 ? 3.86913 3.42622 3.91387 -0.07233 -0.04483 0.03370  209 GLU A O   
1574 C CB  . GLU A 215 ? 3.54836 3.23069 3.67537 -0.06831 -0.00693 -0.00551 209 GLU A CB  
1575 C CG  . GLU A 215 ? 3.80858 3.42112 3.91844 -0.07081 -0.03850 -0.00827 209 GLU A CG  
1576 C CD  . GLU A 215 ? 3.68789 3.31251 3.82537 -0.08430 -0.04426 -0.01953 209 GLU A CD  
1577 O OE1 . GLU A 215 ? 3.61498 3.30424 3.78787 -0.09261 -0.02305 -0.02350 209 GLU A OE1 
1578 O OE2 . GLU A 215 ? 3.97340 3.54003 4.09614 -0.08526 -0.07278 -0.02542 209 GLU A OE2 
1579 N N   . HIS A 216 ? 3.59545 3.25574 3.67272 -0.10912 0.00177  0.04873  210 HIS A N   
1580 C CA  . HIS A 216 ? 3.54613 3.16582 3.59415 -0.13924 -0.00720 0.07786  210 HIS A CA  
1581 C C   . HIS A 216 ? 3.38954 2.97312 3.39566 -0.12080 -0.01817 0.08786  210 HIS A C   
1582 O O   . HIS A 216 ? 3.24853 2.79404 3.22229 -0.14436 -0.02674 0.11430  210 HIS A O   
1583 C CB  . HIS A 216 ? 3.56153 3.23629 3.62643 -0.17702 0.02116  0.09477  210 HIS A CB  
1584 C CG  . HIS A 216 ? 3.50096 3.23628 3.56739 -0.16503 0.04954  0.08927  210 HIS A CG  
1585 N ND1 . HIS A 216 ? 3.40447 3.13262 3.43203 -0.16875 0.05532  0.10659  210 HIS A ND1 
1586 C CD2 . HIS A 216 ? 3.45250 3.25090 3.55099 -0.14946 0.07056  0.06810  210 HIS A CD2 
1587 C CE1 . HIS A 216 ? 3.37184 3.15601 3.40730 -0.15559 0.07836  0.09469  210 HIS A CE1 
1588 N NE2 . HIS A 216 ? 3.46279 3.28940 3.54202 -0.14393 0.08784  0.07157  210 HIS A NE2 
1589 N N   . LEU A 217 ? 3.38018 2.97544 3.38719 -0.08065 -0.01924 0.06901  211 LEU A N   
1590 C CA  . LEU A 217 ? 3.48890 3.05191 3.46369 -0.05838 -0.03444 0.07569  211 LEU A CA  
1591 C C   . LEU A 217 ? 3.61693 3.13614 3.58727 -0.01929 -0.05969 0.05869  211 LEU A C   
1592 O O   . LEU A 217 ? 3.70697 3.20690 3.66030 0.00679  -0.07347 0.05967  211 LEU A O   
1593 C CB  . LEU A 217 ? 3.23045 2.85224 3.21240 -0.04545 -0.01394 0.07066  211 LEU A CB  
1594 C CG  . LEU A 217 ? 3.02479 2.69138 3.00439 -0.07653 0.01257  0.08367  211 LEU A CG  
1595 C CD1 . LEU A 217 ? 2.61844 2.32316 2.59247 -0.05991 0.02293  0.07852  211 LEU A CD1 
1596 C CD2 . LEU A 217 ? 3.33452 2.95902 3.27712 -0.11147 0.00625  0.11426  211 LEU A CD2 
1597 N N   . LEU A 218 ? 3.58628 3.09039 3.57094 -0.01283 -0.06667 0.04215  212 LEU A N   
1598 C CA  . LEU A 218 ? 3.63792 3.10234 3.61467 0.02757  -0.08762 0.02278  212 LEU A CA  
1599 C C   . LEU A 218 ? 3.68849 3.06201 3.62691 0.02813  -0.12348 0.03415  212 LEU A C   
1600 O O   . LEU A 218 ? 3.63378 2.97215 3.55784 0.06688  -0.14265 0.02321  212 LEU A O   
1601 C CB  . LEU A 218 ? 3.61156 3.08831 3.60866 0.03579  -0.08315 -0.00045 212 LEU A CB  
1602 C CG  . LEU A 218 ? 3.74416 3.30019 3.77695 0.04108  -0.05299 -0.01508 212 LEU A CG  
1603 C CD1 . LEU A 218 ? 3.78871 3.34067 3.83213 0.03957  -0.05535 -0.03201 212 LEU A CD1 
1604 C CD2 . LEU A 218 ? 3.59985 3.18880 3.64099 0.08056  -0.04422 -0.02801 212 LEU A CD2 
1605 N N   . GLY A 219 ? 3.77521 3.11045 3.69855 -0.01374 -0.13352 0.05611  213 GLY A N   
1606 C CA  . GLY A 219 ? 3.77561 3.01471 3.66214 -0.01683 -0.17187 0.06644  213 GLY A CA  
1607 C C   . GLY A 219 ? 3.92408 3.12363 3.81256 -0.00324 -0.19035 0.04319  213 GLY A C   
1608 O O   . GLY A 219 ? 3.96729 3.19921 3.88153 -0.02277 -0.17780 0.03540  213 GLY A O   
1609 N N   . TYR A 220 ? 4.03006 3.15792 3.88962 0.03296  -0.22206 0.03036  214 TYR A N   
1610 C CA  . TYR A 220 ? 4.22056 3.30255 4.07182 0.05372  -0.24233 0.00405  214 TYR A CA  
1611 C C   . TYR A 220 ? 3.97912 3.07348 3.82976 0.11593  -0.23933 -0.02883 214 TYR A C   
1612 O O   . TYR A 220 ? 3.94056 3.02047 3.78699 0.13620  -0.24466 -0.05497 214 TYR A O   
1613 C CB  . TYR A 220 ? 4.64515 3.61421 4.45609 0.04014  -0.28844 0.01504  214 TYR A CB  
1614 C CG  . TYR A 220 ? 4.52326 3.47426 4.33517 -0.02537 -0.29397 0.04941  214 TYR A CG  
1615 C CD1 . TYR A 220 ? 4.54748 3.51928 4.38517 -0.06127 -0.28851 0.04841  214 TYR A CD1 
1616 C CD2 . TYR A 220 ? 4.27176 3.18585 4.05910 -0.05169 -0.30536 0.08401  214 TYR A CD2 
1617 C CE1 . TYR A 220 ? 4.44755 3.41196 4.29373 -0.12223 -0.29142 0.08094  214 TYR A CE1 
1618 C CE2 . TYR A 220 ? 4.21888 3.12128 4.00712 -0.11365 -0.30689 0.11800  214 TYR A CE2 
1619 C CZ  . TYR A 220 ? 4.32184 3.25307 4.14300 -0.14898 -0.29868 0.11629  214 TYR A CZ  
1620 O OH  . TYR A 220 ? 4.08595 3.01488 3.91562 -0.21170 -0.29796 0.15115  214 TYR A OH  
1621 N N   . SER A 221 ? 3.84931 2.97250 3.70435 0.14618  -0.23082 -0.02801 215 SER A N   
1622 C CA  . SER A 221 ? 3.73349 2.87440 3.59331 0.20541  -0.22697 -0.05649 215 SER A CA  
1623 C C   . SER A 221 ? 3.53169 2.77694 3.43243 0.21612  -0.18543 -0.06783 215 SER A C   
1624 O O   . SER A 221 ? 3.49352 2.76044 3.40035 0.25116  -0.17495 -0.09418 215 SER A O   
1625 C CB  . SER A 221 ? 3.76969 2.87987 3.61576 0.23557  -0.24718 -0.04960 215 SER A CB  
1626 O OG  . SER A 221 ? 3.65810 2.81683 3.51983 0.21306  -0.23216 -0.02470 215 SER A OG  
1627 N N   . ARG A 222 ? 3.40296 2.71019 3.32816 0.18686  -0.16220 -0.04837 216 ARG A N   
1628 C CA  . ARG A 222 ? 3.31426 2.71420 3.27722 0.19507  -0.12676 -0.05717 216 ARG A CA  
1629 C C   . ARG A 222 ? 3.44114 2.86684 3.41574 0.18340  -0.11026 -0.07143 216 ARG A C   
1630 O O   . ARG A 222 ? 3.52500 2.91491 3.48833 0.15339  -0.12109 -0.06706 216 ARG A O   
1631 C CB  . ARG A 222 ? 3.20631 2.65534 3.18578 0.16506  -0.11029 -0.03431 216 ARG A CB  
1632 C CG  . ARG A 222 ? 3.30463 2.73354 3.27133 0.17684  -0.12716 -0.01953 216 ARG A CG  
1633 C CD  . ARG A 222 ? 3.38202 2.85854 3.35819 0.14834  -0.11076 0.00044  216 ARG A CD  
1634 N NE  . ARG A 222 ? 3.47161 2.93009 3.43355 0.16160  -0.12927 0.01374  216 ARG A NE  
1635 C CZ  . ARG A 222 ? 3.40343 2.89217 3.36382 0.14378  -0.12201 0.03031  216 ARG A CZ  
1636 N NH1 . ARG A 222 ? 3.43613 2.97562 3.40872 0.11359  -0.09494 0.03463  216 ARG A NH1 
1637 N NH2 . ARG A 222 ? 3.28611 2.75136 3.23021 0.15870  -0.14440 0.04155  216 ARG A NH2 
1638 N N   . ASP A 223 ? 3.32793 2.81636 3.32628 0.20637  -0.08554 -0.08724 217 ASP A N   
1639 C CA  . ASP A 223 ? 3.35798 2.87431 3.36558 0.19913  -0.06976 -0.10052 217 ASP A CA  
1640 C C   . ASP A 223 ? 3.37000 2.95588 3.41039 0.16867  -0.04379 -0.08888 217 ASP A C   
1641 O O   . ASP A 223 ? 3.21664 2.84861 3.27680 0.17074  -0.02993 -0.08017 217 ASP A O   
1642 C CB  . ASP A 223 ? 3.24112 2.77846 3.24778 0.24319  -0.05851 -0.12438 217 ASP A CB  
1643 C CG  . ASP A 223 ? 3.43210 2.89901 3.40216 0.27828  -0.08334 -0.14179 217 ASP A CG  
1644 O OD1 . ASP A 223 ? 3.52103 2.91449 3.46410 0.26309  -0.11254 -0.13739 217 ASP A OD1 
1645 O OD2 . ASP A 223 ? 3.51963 3.00457 3.48773 0.32115  -0.07366 -0.15997 217 ASP A OD2 
1646 N N   . LEU A 224 ? 3.52317 3.11463 3.56957 0.14181  -0.03995 -0.09002 218 LEU A N   
1647 C CA  . LEU A 224 ? 3.35737 3.01176 3.43454 0.11651  -0.01688 -0.08249 218 LEU A CA  
1648 C C   . LEU A 224 ? 3.13353 2.84269 3.22842 0.13910  0.00456  -0.09498 218 LEU A C   
1649 O O   . LEU A 224 ? 3.17784 2.87867 3.26170 0.16065  0.00431  -0.11140 218 LEU A O   
1650 C CB  . LEU A 224 ? 3.27341 2.91998 3.35703 0.08428  -0.02134 -0.08118 218 LEU A CB  
1651 C CG  . LEU A 224 ? 2.95285 2.66075 3.06938 0.05817  0.00010  -0.07426 218 LEU A CG  
1652 C CD1 . LEU A 224 ? 2.89462 2.62417 3.01666 0.04245  0.01008  -0.05577 218 LEU A CD1 
1653 C CD2 . LEU A 224 ? 3.18937 2.89002 3.31784 0.02891  -0.00768 -0.07358 218 LEU A CD2 
1654 N N   . ASP A 225 ? 2.95767 2.72025 3.07666 0.13319  0.02225  -0.08652 219 ASP A N   
1655 C CA  . ASP A 225 ? 2.98792 2.80250 3.12645 0.14842  0.04150  -0.09446 219 ASP A CA  
1656 C C   . ASP A 225 ? 2.88224 2.71085 3.02667 0.13679  0.04866  -0.10256 219 ASP A C   
1657 O O   . ASP A 225 ? 2.78846 2.64120 2.93619 0.15259  0.05979  -0.11129 219 ASP A O   
1658 C CB  . ASP A 225 ? 3.03462 2.89590 3.19655 0.14043  0.05347  -0.08337 219 ASP A CB  
1659 C CG  . ASP A 225 ? 3.10607 3.01580 3.28906 0.15800  0.06908  -0.08843 219 ASP A CG  
1660 O OD1 . ASP A 225 ? 3.01932 2.92739 3.19602 0.18121  0.07263  -0.09908 219 ASP A OD1 
1661 O OD2 . ASP A 225 ? 3.10877 3.05722 3.31270 0.14788  0.07759  -0.08142 219 ASP A OD2 
1662 N N   . THR A 226 ? 2.87505 2.69037 3.02185 0.10896  0.04196  -0.09862 220 THR A N   
1663 C CA  . THR A 226 ? 2.96730 2.79418 3.12254 0.09893  0.04399  -0.10675 220 THR A CA  
1664 C C   . THR A 226 ? 2.85099 2.63913 2.97912 0.11765  0.03137  -0.12164 220 THR A C   
1665 O O   . THR A 226 ? 2.67934 2.48271 2.80491 0.12728  0.03757  -0.13096 220 THR A O   
1666 C CB  . THR A 226 ? 3.02105 2.84818 3.19187 0.06557  0.03909  -0.09889 220 THR A CB  
1667 O OG1 . THR A 226 ? 2.90389 2.76536 3.09184 0.05121  0.05262  -0.08664 220 THR A OG1 
1668 C CG2 . THR A 226 ? 3.06578 2.91110 3.25262 0.05697  0.03920  -0.10765 220 THR A CG2 
1669 N N   . ASP A 227 ? 3.09561 2.82871 3.19834 0.12360  0.01191  -0.12416 221 ASP A N   
1670 C CA  . ASP A 227 ? 3.33460 3.02272 3.40420 0.14357  -0.00314 -0.14118 221 ASP A CA  
1671 C C   . ASP A 227 ? 3.28824 2.98865 3.34069 0.18232  0.01034  -0.15248 221 ASP A C   
1672 O O   . ASP A 227 ? 3.44593 3.13445 3.47370 0.19936  0.00963  -0.16705 221 ASP A O   
1673 C CB  . ASP A 227 ? 3.66079 3.27997 3.70601 0.13980  -0.03095 -0.14141 221 ASP A CB  
1674 C CG  . ASP A 227 ? 3.53379 3.14179 3.59703 0.09824  -0.04440 -0.12909 221 ASP A CG  
1675 O OD1 . ASP A 227 ? 3.51406 3.15687 3.60195 0.07913  -0.03806 -0.12879 221 ASP A OD1 
1676 O OD2 . ASP A 227 ? 3.52693 3.09223 3.58102 0.08458  -0.06169 -0.11883 221 ASP A OD2 
1677 N N   . VAL A 228 ? 3.13468 2.86119 3.19987 0.19645  0.02273  -0.14555 222 VAL A N   
1678 C CA  . VAL A 228 ? 3.13902 2.88590 3.19598 0.23313  0.03736  -0.15491 222 VAL A CA  
1679 C C   . VAL A 228 ? 2.94900 2.75206 3.02185 0.23136  0.06098  -0.15359 222 VAL A C   
1680 O O   . VAL A 228 ? 3.03075 2.83980 3.08342 0.25466  0.07134  -0.16434 222 VAL A O   
1681 C CB  . VAL A 228 ? 2.90877 2.66985 2.98172 0.24785  0.03990  -0.14704 222 VAL A CB  
1682 C CG1 . VAL A 228 ? 2.63351 2.43176 2.71058 0.28431  0.05865  -0.15513 222 VAL A CG1 
1683 C CG2 . VAL A 228 ? 3.01328 2.70815 3.06260 0.25297  0.01306  -0.14845 222 VAL A CG2 
1684 N N   . VAL A 229 ? 2.72856 2.57062 2.83397 0.20413  0.06943  -0.14031 223 VAL A N   
1685 C CA  . VAL A 229 ? 2.92961 2.81855 3.04992 0.20021  0.08799  -0.13728 223 VAL A CA  
1686 C C   . VAL A 229 ? 3.08929 2.95800 3.18593 0.19655  0.08237  -0.14666 223 VAL A C   
1687 O O   . VAL A 229 ? 3.10852 2.99387 3.19207 0.20881  0.09485  -0.14975 223 VAL A O   
1688 C CB  . VAL A 229 ? 2.85107 2.77774 3.00801 0.17414  0.09395  -0.12348 223 VAL A CB  
1689 C CG1 . VAL A 229 ? 2.74706 2.70904 2.91600 0.16651  0.10657  -0.12080 223 VAL A CG1 
1690 C CG2 . VAL A 229 ? 2.97009 2.92015 3.14686 0.18089  0.09898  -0.11451 223 VAL A CG2 
1691 N N   . ILE A 230 ? 3.12659 2.95980 3.21735 0.17857  0.06259  -0.14999 224 ILE A N   
1692 C CA  . ILE A 230 ? 3.13938 2.95138 3.20993 0.17440  0.05161  -0.15929 224 ILE A CA  
1693 C C   . ILE A 230 ? 3.13804 2.91290 3.15975 0.20403  0.04709  -0.17477 224 ILE A C   
1694 O O   . ILE A 230 ? 3.07398 2.84762 3.07077 0.21204  0.04977  -0.18106 224 ILE A O   
1695 C CB  . ILE A 230 ? 3.18180 2.96870 3.26475 0.14742  0.02971  -0.15870 224 ILE A CB  
1696 C CG1 . ILE A 230 ? 3.04861 2.87986 3.17662 0.12129  0.03870  -0.14603 224 ILE A CG1 
1697 C CG2 . ILE A 230 ? 3.18256 2.93902 3.24229 0.14618  0.01106  -0.17051 224 ILE A CG2 
1698 C CD1 . ILE A 230 ? 3.09369 2.91413 3.24204 0.09372  0.02261  -0.14349 224 ILE A CD1 
1699 N N   . ASP A 231 ? 3.13822 2.87945 3.14134 0.22252  0.03943  -0.18164 225 ASP A N   
1700 C CA  . ASP A 231 ? 3.17364 2.87769 3.12655 0.25609  0.03575  -0.19976 225 ASP A CA  
1701 C C   . ASP A 231 ? 3.14022 2.89001 3.08668 0.28125  0.06610  -0.19978 225 ASP A C   
1702 O O   . ASP A 231 ? 3.22389 2.96002 3.12745 0.30138  0.07051  -0.21185 225 ASP A O   
1703 C CB  . ASP A 231 ? 3.31638 2.97281 3.25343 0.27280  0.01923  -0.20758 225 ASP A CB  
1704 C CG  . ASP A 231 ? 3.65417 3.25167 3.58395 0.24916  -0.01448 -0.20930 225 ASP A CG  
1705 O OD1 . ASP A 231 ? 3.76080 3.36076 3.70201 0.22131  -0.02377 -0.20567 225 ASP A OD1 
1706 O OD2 . ASP A 231 ? 3.88611 3.43510 3.80096 0.25797  -0.03302 -0.21352 225 ASP A OD2 
1707 N N   . LYS A 232 ? 3.10942 2.91423 3.09703 0.27926  0.08689  -0.18552 226 LYS A N   
1708 C CA  . LYS A 232 ? 3.17390 3.03023 3.16490 0.29769  0.11645  -0.18172 226 LYS A CA  
1709 C C   . LYS A 232 ? 3.03721 2.91847 3.02658 0.27987  0.12674  -0.17329 226 LYS A C   
1710 O O   . LYS A 232 ? 3.00842 2.91351 2.97817 0.29517  0.14743  -0.17283 226 LYS A O   
1711 C CB  . LYS A 232 ? 3.09188 2.99907 3.13200 0.29755  0.13059  -0.16807 226 LYS A CB  
1712 C CG  . LYS A 232 ? 2.99403 2.87982 3.03376 0.32203  0.12147  -0.17585 226 LYS A CG  
1713 C CD  . LYS A 232 ? 3.13900 3.00783 3.13851 0.36434  0.12860  -0.19500 226 LYS A CD  
1714 C CE  . LYS A 232 ? 3.06745 2.90846 3.06590 0.39226  0.11533  -0.20465 226 LYS A CE  
1715 N NZ  . LYS A 232 ? 2.84058 2.66385 2.79794 0.43872  0.12230  -0.22707 226 LYS A NZ  
1716 N N   . LEU A 233 ? 3.04279 2.91938 3.05192 0.24841  0.11285  -0.16604 227 LEU A N   
1717 C CA  . LEU A 233 ? 3.16077 3.05158 3.16595 0.23320  0.11655  -0.15937 227 LEU A CA  
1718 C C   . LEU A 233 ? 3.23500 3.07850 3.18670 0.24160  0.10132  -0.17329 227 LEU A C   
1719 O O   . LEU A 233 ? 3.32176 3.17201 3.24701 0.24462  0.11001  -0.17037 227 LEU A O   
1720 C CB  . LEU A 233 ? 3.06521 2.96997 3.11256 0.20133  0.10661  -0.14929 227 LEU A CB  
1721 C CG  . LEU A 233 ? 3.12421 3.07643 3.21860 0.19026  0.12073  -0.13473 227 LEU A CG  
1722 C CD1 . LEU A 233 ? 2.92824 2.88775 3.05496 0.16285  0.11010  -0.12930 227 LEU A CD1 
1723 C CD2 . LEU A 233 ? 3.08683 3.07995 3.18529 0.19560  0.14313  -0.12376 227 LEU A CD2 
1724 N N   . LYS A 234 ? 3.29749 3.08964 3.23032 0.24394  0.07625  -0.18739 228 LYS A N   
1725 C CA  . LYS A 234 ? 3.46815 3.20900 3.34686 0.25315  0.05660  -0.20288 228 LYS A CA  
1726 C C   . LYS A 234 ? 3.42366 3.14900 3.24556 0.29008  0.07019  -0.21600 228 LYS A C   
1727 O O   . LYS A 234 ? 3.32588 3.01709 3.09301 0.30078  0.06094  -0.22704 228 LYS A O   
1728 C CB  . LYS A 234 ? 3.43190 3.12121 3.31084 0.24164  0.02280  -0.21315 228 LYS A CB  
1729 C CG  . LYS A 234 ? 3.28184 2.98358 3.20737 0.20595  0.00720  -0.20343 228 LYS A CG  
1730 C CD  . LYS A 234 ? 3.29963 2.95460 3.22823 0.19191  -0.02474 -0.21101 228 LYS A CD  
1731 C CE  . LYS A 234 ? 3.16793 2.84169 3.14369 0.15822  -0.03888 -0.20277 228 LYS A CE  
1732 N NZ  . LYS A 234 ? 3.11867 2.79113 3.08016 0.15657  -0.05002 -0.20703 228 LYS A NZ  
1733 N N   . SER A 235 ? 3.34981 3.10038 3.18256 0.31144  0.09143  -0.21586 229 SER A N   
1734 C CA  . SER A 235 ? 3.35338 3.10098 3.13894 0.35054  0.10983  -0.22899 229 SER A CA  
1735 C C   . SER A 235 ? 3.23264 3.04862 3.03071 0.35582  0.14867  -0.21345 229 SER A C   
1736 O O   . SER A 235 ? 3.10920 2.94844 2.89265 0.38741  0.17303  -0.21942 229 SER A O   
1737 C CB  . SER A 235 ? 3.44673 3.17599 3.23598 0.37609  0.10568  -0.24151 229 SER A CB  
1738 O OG  . SER A 235 ? 3.48972 3.26978 3.34206 0.36656  0.11912  -0.22522 229 SER A OG  
1739 N N   . ALA A 236 ? 3.19365 3.04279 3.02039 0.32561  0.15431  -0.19346 230 ALA A N   
1740 C CA  . ALA A 236 ? 3.18151 3.09151 3.02144 0.32387  0.18769  -0.17507 230 ALA A CA  
1741 C C   . ALA A 236 ? 3.27110 3.16575 3.04359 0.33587  0.19751  -0.17786 230 ALA A C   
1742 O O   . ALA A 236 ? 3.17378 3.02188 2.90923 0.32558  0.17366  -0.18305 230 ALA A O   
1743 C CB  . ALA A 236 ? 3.00939 2.95245 2.90400 0.28675  0.18561  -0.15303 230 ALA A CB  
1744 N N   . LYS A 237 ? 3.33104 3.26719 3.08787 0.35755  0.23267  -0.17366 231 LYS A N   
1745 C CA  . LYS A 237 ? 3.40131 3.32618 3.08609 0.37194  0.24764  -0.17536 231 LYS A CA  
1746 C C   . LYS A 237 ? 3.34724 3.32726 3.04349 0.35228  0.27671  -0.14605 231 LYS A C   
1747 O O   . LYS A 237 ? 3.39531 3.35383 3.03429 0.34769  0.27769  -0.14005 231 LYS A O   
1748 C CB  . LYS A 237 ? 3.38729 3.31016 3.02702 0.41834  0.26773  -0.19700 231 LYS A CB  
1749 C CG  . LYS A 237 ? 3.43085 3.27117 3.01037 0.44220  0.23549  -0.22912 231 LYS A CG  
1750 C CD  . LYS A 237 ? 3.52751 3.34210 3.15321 0.43981  0.20730  -0.24022 231 LYS A CD  
1751 C CE  . LYS A 237 ? 3.73167 3.46121 3.29705 0.46283  0.17391  -0.27123 231 LYS A CE  
1752 N NZ  . LYS A 237 ? 3.31386 3.01514 2.92108 0.45842  0.14652  -0.27888 231 LYS A NZ  
1753 N N   . THR A 238 ? 3.27961 3.32644 3.04618 0.33915  0.29761  -0.12662 232 THR A N   
1754 C CA  . THR A 238 ? 3.37990 3.48164 3.15757 0.32126  0.32737  -0.09762 232 THR A CA  
1755 C C   . THR A 238 ? 3.34487 3.47135 3.18969 0.28067  0.31664  -0.07373 232 THR A C   
1756 O O   . THR A 238 ? 3.38594 3.50935 3.21839 0.25511  0.31524  -0.05334 232 THR A O   
1757 C CB  . THR A 238 ? 3.47346 3.64476 3.26909 0.34622  0.36986  -0.09423 232 THR A CB  
1758 O OG1 . THR A 238 ? 3.68675 3.88814 3.55244 0.35313  0.36631  -0.10038 232 THR A OG1 
1759 C CG2 . THR A 238 ? 3.13162 3.27905 2.84996 0.38939  0.38461  -0.11814 232 THR A CG2 
1760 N N   . SER A 239 ? 3.34929 3.49573 3.26039 0.27520  0.30722  -0.07617 233 SER A N   
1761 C CA  . SER A 239 ? 3.02673 3.19907 2.99896 0.24010  0.29888  -0.05536 233 SER A CA  
1762 C C   . SER A 239 ? 2.92798 3.08363 2.94359 0.23527  0.27288  -0.06754 233 SER A C   
1763 O O   . SER A 239 ? 3.12605 3.27490 3.14540 0.25858  0.27043  -0.08511 233 SER A O   
1764 C CB  . SER A 239 ? 2.98763 3.23639 3.00797 0.23244  0.32979  -0.03227 233 SER A CB  
1765 O OG  . SER A 239 ? 3.08498 3.37131 3.14085 0.25741  0.34248  -0.04284 233 SER A OG  
1766 N N   . ILE A 240 ? 2.55595 2.70304 2.60118 0.20539  0.25331  -0.05774 234 ILE A N   
1767 C CA  . ILE A 240 ? 2.81412 2.95315 2.90206 0.19582  0.23230  -0.06474 234 ILE A CA  
1768 C C   . ILE A 240 ? 2.75893 2.93319 2.89789 0.16845  0.23220  -0.04496 234 ILE A C   
1769 O O   . ILE A 240 ? 2.64001 2.80296 2.77365 0.14737  0.22407  -0.03366 234 ILE A O   
1770 C CB  . ILE A 240 ? 2.96456 3.04695 3.03044 0.18964  0.20313  -0.07924 234 ILE A CB  
1771 C CG1 . ILE A 240 ? 2.94940 2.99137 2.96789 0.21510  0.19727  -0.10021 234 ILE A CG1 
1772 C CG2 . ILE A 240 ? 2.86946 2.95200 2.98070 0.17500  0.18627  -0.08180 234 ILE A CG2 
1773 C CD1 . ILE A 240 ? 3.01829 3.00924 3.02279 0.20694  0.16690  -0.11361 234 ILE A CD1 
1774 N N   . ASP A 241 ? 2.97089 3.18341 3.15722 0.16956  0.23783  -0.04136 235 ASP A N   
1775 C CA  . ASP A 241 ? 3.05719 3.30148 3.29253 0.14469  0.23437  -0.02447 235 ASP A CA  
1776 C C   . ASP A 241 ? 2.91281 3.14519 3.17617 0.14048  0.21429  -0.03426 235 ASP A C   
1777 O O   . ASP A 241 ? 2.88958 3.12904 3.16371 0.15786  0.21525  -0.04322 235 ASP A O   
1778 C CB  . ASP A 241 ? 3.10487 3.41227 3.37476 0.14698  0.25826  -0.00827 235 ASP A CB  
1779 C CG  . ASP A 241 ? 2.87525 3.20052 3.11691 0.14720  0.28230  0.00556  235 ASP A CG  
1780 O OD1 . ASP A 241 ? 2.92814 3.21961 3.13491 0.13253  0.27496  0.01145  235 ASP A OD1 
1781 O OD2 . ASP A 241 ? 2.66218 3.03633 2.91581 0.16293  0.30874  0.01087  235 ASP A OD2 
1782 N N   . ILE A 242 ? 2.69461 2.90726 2.96658 0.11888  0.19596  -0.03266 236 ILE A N   
1783 C CA  . ILE A 242 ? 2.71429 2.91362 3.00484 0.11351  0.17854  -0.04188 236 ILE A CA  
1784 C C   . ILE A 242 ? 2.64937 2.86448 2.97233 0.09110  0.16917  -0.03086 236 ILE A C   
1785 O O   . ILE A 242 ? 2.46636 2.67380 2.78529 0.07575  0.16472  -0.02252 236 ILE A O   
1786 C CB  . ILE A 242 ? 2.77180 2.92616 3.03593 0.11334  0.16375  -0.05691 236 ILE A CB  
1787 C CG1 . ILE A 242 ? 2.80032 2.93201 3.02938 0.13384  0.16812  -0.06835 236 ILE A CG1 
1788 C CG2 . ILE A 242 ? 2.93991 3.08648 3.22194 0.10682  0.15054  -0.06435 236 ILE A CG2 
1789 C CD1 . ILE A 242 ? 3.03871 3.12975 3.24836 0.13179  0.15138  -0.08215 236 ILE A CD1 
1790 N N   . GLU A 243 ? 2.75518 2.98707 3.10660 0.08972  0.16316  -0.03108 237 GLU A N   
1791 C CA  . GLU A 243 ? 2.55783 2.79740 2.93567 0.07021  0.14922  -0.02470 237 GLU A CA  
1792 C C   . GLU A 243 ? 2.66164 2.88224 3.03737 0.07221  0.13581  -0.03775 237 GLU A C   
1793 O O   . GLU A 243 ? 2.62680 2.86179 3.01644 0.07911  0.13408  -0.03763 237 GLU A O   
1794 C CB  . GLU A 243 ? 2.47366 2.75911 2.88963 0.06434  0.15455  -0.00852 237 GLU A CB  
1795 C CG  . GLU A 243 ? 2.44730 2.73613 2.88925 0.04361  0.13523  -0.00284 237 GLU A CG  
1796 C CD  . GLU A 243 ? 2.52190 2.85979 3.00852 0.03590  0.13735  0.01392  237 GLU A CD  
1797 O OE1 . GLU A 243 ? 2.77246 3.14698 3.27167 0.04392  0.15812  0.02406  237 GLU A OE1 
1798 O OE2 . GLU A 243 ? 2.09924 2.44078 2.60886 0.02238  0.11797  0.01641  237 GLU A OE2 
1799 N N   . HIS A 244 ? 2.75973 2.94951 3.11778 0.06675  0.12656  -0.04830 238 HIS A N   
1800 C CA  . HIS A 244 ? 2.90569 3.07935 3.25755 0.06712  0.11789  -0.05984 238 HIS A CA  
1801 C C   . HIS A 244 ? 2.93855 3.09996 3.29223 0.05444  0.10509  -0.06514 238 HIS A C   
1802 O O   . HIS A 244 ? 2.96579 3.12667 3.32642 0.04511  0.09947  -0.05940 238 HIS A O   
1803 C CB  . HIS A 244 ? 2.79283 2.94443 3.12223 0.07659  0.12186  -0.07029 238 HIS A CB  
1804 C CG  . HIS A 244 ? 2.91049 3.06302 3.23418 0.09058  0.12755  -0.06999 238 HIS A CG  
1805 N ND1 . HIS A 244 ? 2.81864 2.95450 3.13220 0.09256  0.12310  -0.07551 238 HIS A ND1 
1806 C CD2 . HIS A 244 ? 2.99915 3.16591 3.32485 0.10445  0.13683  -0.06494 238 HIS A CD2 
1807 C CE1 . HIS A 244 ? 2.73944 2.87297 3.04779 0.10725  0.12593  -0.07414 238 HIS A CE1 
1808 N NE2 . HIS A 244 ? 2.81553 2.96948 3.13202 0.11677  0.13490  -0.06937 238 HIS A NE2 
1809 N N   . LEU A 245 ? 2.92531 3.07520 3.27044 0.05465  0.10044  -0.07609 239 LEU A N   
1810 C CA  . LEU A 245 ? 2.93647 3.07509 3.27995 0.04777  0.08978  -0.08534 239 LEU A CA  
1811 C C   . LEU A 245 ? 2.92602 3.05012 3.26484 0.04861  0.08823  -0.09259 239 LEU A C   
1812 O O   . LEU A 245 ? 2.83895 2.95372 3.18159 0.04345  0.07782  -0.09237 239 LEU A O   
1813 C CB  . LEU A 245 ? 3.01699 3.15184 3.34886 0.04930  0.08987  -0.09466 239 LEU A CB  
1814 C CG  . LEU A 245 ? 3.18058 3.30786 3.50647 0.04564  0.07964  -0.10523 239 LEU A CG  
1815 C CD1 . LEU A 245 ? 2.81673 2.94687 3.14990 0.03927  0.06577  -0.09823 239 LEU A CD1 
1816 C CD2 . LEU A 245 ? 3.47503 3.60117 3.78324 0.04794  0.08634  -0.11371 239 LEU A CD2 
1817 N N   . ALA A 246 ? 2.91632 3.03554 3.24731 0.05470  0.09526  -0.09862 240 ALA A N   
1818 C CA  . ALA A 246 ? 2.74986 2.85676 3.07878 0.05692  0.09102  -0.10574 240 ALA A CA  
1819 C C   . ALA A 246 ? 2.74042 2.84341 3.06137 0.06217  0.09747  -0.10777 240 ALA A C   
1820 O O   . ALA A 246 ? 3.01990 3.12653 3.33757 0.06313  0.10409  -0.10762 240 ALA A O   
1821 C CB  . ALA A 246 ? 2.81688 2.92089 3.15177 0.05759  0.08406  -0.12054 240 ALA A CB  
1822 N N   . ILE A 247 ? 2.74788 2.83847 3.06286 0.06505  0.09229  -0.10926 241 ILE A N   
1823 C CA  . ILE A 247 ? 2.81664 2.89745 3.12141 0.06965  0.09310  -0.11277 241 ILE A CA  
1824 C C   . ILE A 247 ? 2.77531 2.85177 3.09088 0.06937  0.08255  -0.12449 241 ILE A C   
1825 O O   . ILE A 247 ? 2.61065 2.67361 2.91814 0.07243  0.07512  -0.12745 241 ILE A O   
1826 C CB  . ILE A 247 ? 2.92594 2.99545 3.20883 0.07555  0.09531  -0.10451 241 ILE A CB  
1827 C CG1 . ILE A 247 ? 3.15603 3.24085 3.43953 0.07536  0.10577  -0.09174 241 ILE A CG1 
1828 C CG2 . ILE A 247 ? 2.72496 2.78099 2.99124 0.08251  0.09664  -0.10885 241 ILE A CG2 
1829 C CD1 . ILE A 247 ? 3.20747 3.30357 3.49515 0.07944  0.11437  -0.09064 241 ILE A CD1 
1830 N N   . VAL A 248 ? 2.81971 2.90848 3.15378 0.06731  0.08077  -0.13239 242 VAL A N   
1831 C CA  . VAL A 248 ? 2.80183 2.89609 3.15477 0.06956  0.07252  -0.14509 242 VAL A CA  
1832 C C   . VAL A 248 ? 2.79085 2.89483 3.15268 0.06463  0.07772  -0.14794 242 VAL A C   
1833 O O   . VAL A 248 ? 2.94768 3.06214 3.30889 0.05868  0.08975  -0.14479 242 VAL A O   
1834 C CB  . VAL A 248 ? 3.07039 3.17806 3.43921 0.07217  0.07216  -0.15504 242 VAL A CB  
1835 C CG1 . VAL A 248 ? 2.88644 3.00831 3.28142 0.07791  0.06577  -0.16964 242 VAL A CG1 
1836 C CG2 . VAL A 248 ? 2.71308 2.80326 3.07219 0.07435  0.06214  -0.15117 242 VAL A CG2 
1837 N N   . PRO A 249 ? 2.75588 2.85407 3.12498 0.06522  0.06658  -0.15257 243 PRO A N   
1838 C CA  . PRO A 249 ? 2.77606 2.87919 3.15429 0.05668  0.06802  -0.15307 243 PRO A CA  
1839 C C   . PRO A 249 ? 2.62900 2.76603 3.03961 0.04904  0.07712  -0.15869 243 PRO A C   
1840 O O   . PRO A 249 ? 2.64908 2.79258 3.07020 0.03739  0.07923  -0.15599 243 PRO A O   
1841 C CB  . PRO A 249 ? 2.89974 2.98573 3.27748 0.05970  0.04844  -0.15747 243 PRO A CB  
1842 C CG  . PRO A 249 ? 2.92745 3.01368 3.31192 0.06937  0.03794  -0.16286 243 PRO A CG  
1843 C CD  . PRO A 249 ? 2.93730 3.02017 3.30474 0.07247  0.04869  -0.15635 243 PRO A CD  
1844 N N   . THR A 250 ? 2.69961 2.85762 3.12473 0.05494  0.08264  -0.16624 244 THR A N   
1845 C CA  . THR A 250 ? 2.88891 3.08465 3.34296 0.05097  0.09492  -0.17338 244 THR A CA  
1846 C C   . THR A 250 ? 3.00722 3.20996 3.44432 0.05177  0.11086  -0.17233 244 THR A C   
1847 O O   . THR A 250 ? 3.14550 3.33535 3.56844 0.06161  0.10647  -0.17577 244 THR A O   
1848 C CB  . THR A 250 ? 2.84043 3.05749 3.32860 0.06254  0.08544  -0.18862 244 THR A CB  
1849 O OG1 . THR A 250 ? 2.74599 2.95110 3.24565 0.06258  0.06544  -0.18917 244 THR A OG1 
1850 C CG2 . THR A 250 ? 2.92193 3.18744 3.44499 0.05926  0.10196  -0.19630 244 THR A CG2 
1851 N N   . THR A 251 ? 2.93098 3.15092 3.36718 0.03988  0.12708  -0.16648 245 THR A N   
1852 C CA  . THR A 251 ? 2.88475 3.11182 3.30092 0.03996  0.14158  -0.16580 245 THR A CA  
1853 C C   . THR A 251 ? 3.11248 3.38182 3.55009 0.03844  0.15880  -0.17449 245 THR A C   
1854 O O   . THR A 251 ? 3.27514 3.57198 3.74778 0.03274  0.16124  -0.17684 245 THR A O   
1855 C CB  . THR A 251 ? 2.69683 2.90403 3.08353 0.02817  0.14649  -0.14904 245 THR A CB  
1856 O OG1 . THR A 251 ? 2.89251 3.10660 3.28995 0.01207  0.15126  -0.14003 245 THR A OG1 
1857 C CG2 . THR A 251 ? 2.54736 2.72074 2.91584 0.03339  0.13293  -0.14213 245 THR A CG2 
1858 N N   . ARG A 252 ? 3.04539 3.32186 3.46191 0.04380  0.17070  -0.17951 246 ARG A N   
1859 C CA  . ARG A 252 ? 3.10847 3.42720 3.53762 0.04641  0.19116  -0.18983 246 ARG A CA  
1860 C C   . ARG A 252 ? 3.26730 3.58803 3.66258 0.03217  0.20952  -0.17646 246 ARG A C   
1861 O O   . ARG A 252 ? 3.22778 3.52911 3.58439 0.03811  0.20947  -0.17783 246 ARG A O   
1862 C CB  . ARG A 252 ? 2.73480 3.05692 3.16243 0.07018  0.18750  -0.21222 246 ARG A CB  
1863 C CG  . ARG A 252 ? 2.99405 3.36304 3.43369 0.07906  0.21051  -0.22721 246 ARG A CG  
1864 C CD  . ARG A 252 ? 2.92477 3.29065 3.36490 0.10728  0.20173  -0.25323 246 ARG A CD  
1865 N NE  . ARG A 252 ? 2.99093 3.40387 3.43978 0.12068  0.22603  -0.27071 246 ARG A NE  
1866 C CZ  . ARG A 252 ? 3.08259 3.54688 3.58288 0.12888  0.23644  -0.28169 246 ARG A CZ  
1867 N NH1 . ARG A 252 ? 2.94920 3.42081 3.49568 0.12404  0.22132  -0.27708 246 ARG A NH1 
1868 N NH2 . ARG A 252 ? 3.15196 3.66327 3.65746 0.14325  0.26238  -0.29821 246 ARG A NH2 
1869 N N   . VAL A 253 ? 3.38271 3.72399 3.79133 0.01198  0.22250  -0.16240 247 VAL A N   
1870 C CA  . VAL A 253 ? 3.27336 3.61737 3.64937 -0.00441 0.24069  -0.14682 247 VAL A CA  
1871 C C   . VAL A 253 ? 3.53656 3.93404 3.92365 -0.00245 0.26867  -0.15610 247 VAL A C   
1872 O O   . VAL A 253 ? 3.51762 3.95993 3.95397 -0.00571 0.27802  -0.16085 247 VAL A O   
1873 C CB  . VAL A 253 ? 2.76781 3.09767 3.14795 -0.03014 0.23743  -0.12348 247 VAL A CB  
1874 C CG1 . VAL A 253 ? 2.48119 2.81034 2.82476 -0.04891 0.25497  -0.10464 247 VAL A CG1 
1875 C CG2 . VAL A 253 ? 2.60890 2.88765 2.97517 -0.02680 0.21183  -0.11755 247 VAL A CG2 
1876 N N   . ASP A 254 ? 3.67690 4.07169 4.01839 0.00380  0.28175  -0.15922 248 ASP A N   
1877 C CA  . ASP A 254 ? 3.85644 4.30027 4.19625 0.01128  0.31111  -0.17141 248 ASP A CA  
1878 C C   . ASP A 254 ? 3.72932 4.19973 4.11057 0.03871  0.30674  -0.20046 248 ASP A C   
1879 O O   . ASP A 254 ? 3.63860 4.07307 4.00847 0.05829  0.28363  -0.21503 248 ASP A O   
1880 C CB  . ASP A 254 ? 3.84817 4.33338 4.20480 -0.01642 0.33729  -0.15093 248 ASP A CB  
1881 C CG  . ASP A 254 ? 3.69932 4.14616 4.00811 -0.04225 0.33628  -0.12149 248 ASP A CG  
1882 O OD1 . ASP A 254 ? 3.76362 4.16977 4.01528 -0.03466 0.32817  -0.12070 248 ASP A OD1 
1883 O OD2 . ASP A 254 ? 3.48033 3.93517 3.80925 -0.07027 0.34059  -0.09901 248 ASP A OD2 
1884 N N   . GLY A 255 ? 3.64308 4.17483 4.07409 0.04081  0.32627  -0.20874 249 GLY A N   
1885 C CA  . GLY A 255 ? 3.47490 4.03077 3.94826 0.06945  0.31894  -0.23669 249 GLY A CA  
1886 C C   . GLY A 255 ? 3.46584 4.04000 4.00540 0.06260  0.30375  -0.23356 249 GLY A C   
1887 O O   . GLY A 255 ? 3.53632 4.14760 4.12458 0.08255  0.30203  -0.25360 249 GLY A O   
1888 N N   . ASN A 256 ? 3.43866 3.98426 3.97871 0.03631  0.29016  -0.20971 250 ASN A N   
1889 C CA  . ASN A 256 ? 3.29252 3.84707 3.88667 0.02680  0.27227  -0.20506 250 ASN A CA  
1890 C C   . ASN A 256 ? 3.10814 3.59536 3.67807 0.02539  0.24000  -0.19780 250 ASN A C   
1891 O O   . ASN A 256 ? 3.10951 3.55335 3.63147 0.01521  0.23710  -0.18333 250 ASN A O   
1892 C CB  . ASN A 256 ? 3.05328 3.64352 3.67609 -0.00672 0.28800  -0.18270 250 ASN A CB  
1893 C CG  . ASN A 256 ? 3.04871 3.71223 3.69362 -0.00926 0.32584  -0.18546 250 ASN A CG  
1894 O OD1 . ASN A 256 ? 3.00505 3.73028 3.71269 -0.00089 0.33363  -0.19819 250 ASN A OD1 
1895 N ND2 . ASN A 256 ? 3.08945 3.74853 3.68244 -0.01988 0.34981  -0.17338 250 ASN A ND2 
1896 N N   . SER A 257 ? 3.04258 3.52300 3.64541 0.03673  0.21599  -0.20775 251 SER A N   
1897 C CA  . SER A 257 ? 3.00045 3.42176 3.57982 0.03741  0.18782  -0.20184 251 SER A CA  
1898 C C   . SER A 257 ? 2.98329 3.38824 3.56633 0.01183  0.17968  -0.18198 251 SER A C   
1899 O O   . SER A 257 ? 3.00090 3.44131 3.62573 -0.00373 0.18343  -0.17724 251 SER A O   
1900 C CB  . SER A 257 ? 3.04685 3.46202 3.65186 0.05911  0.16409  -0.21873 251 SER A CB  
1901 O OG  . SER A 257 ? 2.75493 3.17722 3.35453 0.08408  0.16757  -0.23830 251 SER A OG  
1902 N N   . TYR A 258 ? 2.97967 3.33100 3.52026 0.00798  0.16742  -0.17093 252 TYR A N   
1903 C CA  . TYR A 258 ? 3.07265 3.39575 3.60602 -0.01142 0.15638  -0.15473 252 TYR A CA  
1904 C C   . TYR A 258 ? 3.05393 3.33377 3.57379 -0.00023 0.13045  -0.15805 252 TYR A C   
1905 O O   . TYR A 258 ? 2.96459 3.21859 3.45516 0.01482  0.12612  -0.16146 252 TYR A O   
1906 C CB  . TYR A 258 ? 3.10600 3.40435 3.59662 -0.02464 0.16729  -0.13774 252 TYR A CB  
1907 C CG  . TYR A 258 ? 3.33250 3.59296 3.81023 -0.04123 0.15327  -0.12264 252 TYR A CG  
1908 C CD1 . TYR A 258 ? 3.27957 3.55453 3.78473 -0.06513 0.15278  -0.11269 252 TYR A CD1 
1909 C CD2 . TYR A 258 ? 3.23486 3.44534 3.67409 -0.03264 0.13991  -0.11873 252 TYR A CD2 
1910 C CE1 . TYR A 258 ? 3.26743 3.49918 3.75697 -0.07950 0.13584  -0.10050 252 TYR A CE1 
1911 C CE2 . TYR A 258 ? 3.17741 3.34942 3.60137 -0.04318 0.12602  -0.10823 252 TYR A CE2 
1912 C CZ  . TYR A 258 ? 3.25920 3.43753 3.70580 -0.06634 0.12233  -0.09975 252 TYR A CZ  
1913 O OH  . TYR A 258 ? 3.05428 3.18604 3.48204 -0.07611 0.10449  -0.09084 252 TYR A OH  
1914 N N   . TYR A 259 ? 3.02462 3.29678 3.56441 -0.00887 0.11299  -0.15625 253 TYR A N   
1915 C CA  . TYR A 259 ? 2.88183 3.11461 3.40626 0.00171  0.08832  -0.16011 253 TYR A CA  
1916 C C   . TYR A 259 ? 2.91188 3.09911 3.40106 -0.00798 0.07995  -0.14824 253 TYR A C   
1917 O O   . TYR A 259 ? 2.86777 3.05466 3.36664 -0.02762 0.07884  -0.13949 253 TYR A O   
1918 C CB  . TYR A 259 ? 2.81593 3.06772 3.38352 0.00281  0.06943  -0.16971 253 TYR A CB  
1919 C CG  . TYR A 259 ? 2.83131 3.04030 3.37686 0.01387  0.04252  -0.17362 253 TYR A CG  
1920 C CD1 . TYR A 259 ? 2.78660 2.97591 3.30774 0.03358  0.03748  -0.17909 253 TYR A CD1 
1921 C CD2 . TYR A 259 ? 2.75347 2.93920 3.29929 0.00349  0.02101  -0.17118 253 TYR A CD2 
1922 C CE1 . TYR A 259 ? 2.85586 3.00630 3.35098 0.04249  0.01515  -0.18031 253 TYR A CE1 
1923 C CE2 . TYR A 259 ? 2.69541 2.83987 3.21271 0.01495  -0.00307 -0.17542 253 TYR A CE2 
1924 C CZ  . TYR A 259 ? 2.77601 2.90452 3.26695 0.03438  -0.00423 -0.17917 253 TYR A CZ  
1925 O OH  . TYR A 259 ? 2.90903 2.99663 3.36585 0.04458  -0.02596 -0.18106 253 TYR A OH  
1926 N N   . TRP A 260 ? 2.88249 3.03163 3.33168 0.00597  0.07383  -0.14781 254 TRP A N   
1927 C CA  . TRP A 260 ? 2.82852 2.93436 3.24102 0.00385  0.06720  -0.13970 254 TRP A CA  
1928 C C   . TRP A 260 ? 2.69931 2.77452 3.07900 0.02272  0.05833  -0.14335 254 TRP A C   
1929 O O   . TRP A 260 ? 2.59916 2.67269 2.95966 0.03269  0.06917  -0.14032 254 TRP A O   
1930 C CB  . TRP A 260 ? 2.85231 2.95561 3.24601 -0.00241 0.08390  -0.12853 254 TRP A CB  
1931 C CG  . TRP A 260 ? 2.88367 2.94443 3.24714 -0.00588 0.07551  -0.12045 254 TRP A CG  
1932 C CD1 . TRP A 260 ? 2.89296 2.93756 3.26037 -0.02419 0.06676  -0.11356 254 TRP A CD1 
1933 C CD2 . TRP A 260 ? 2.94922 2.97774 3.27532 0.01029  0.07399  -0.11876 254 TRP A CD2 
1934 N NE1 . TRP A 260 ? 2.84764 2.84506 3.17816 -0.01817 0.05757  -0.10938 254 TRP A NE1 
1935 C CE2 . TRP A 260 ? 2.98588 2.97640 3.29225 0.00463  0.06330  -0.11326 254 TRP A CE2 
1936 C CE3 . TRP A 260 ? 3.02801 3.05784 3.33821 0.02855  0.08024  -0.12089 254 TRP A CE3 
1937 C CZ2 . TRP A 260 ? 3.11864 3.07447 3.39006 0.02121  0.05969  -0.11252 254 TRP A CZ2 
1938 C CZ3 . TRP A 260 ? 3.09203 3.09454 3.37222 0.04191  0.07895  -0.11798 254 TRP A CZ3 
1939 C CH2 . TRP A 260 ? 3.06389 3.03066 3.32492 0.04047  0.06923  -0.11517 254 TRP A CH2 
1940 N N   . PRO A 261 ? 2.75081 2.80257 3.12262 0.02701  0.03848  -0.14897 255 PRO A N   
1941 C CA  . PRO A 261 ? 2.87640 2.90295 3.21417 0.04436  0.03267  -0.15123 255 PRO A CA  
1942 C C   . PRO A 261 ? 2.93571 2.92118 3.23038 0.05169  0.02806  -0.14934 255 PRO A C   
1943 O O   . PRO A 261 ? 3.14680 3.10892 3.41061 0.06475  0.02032  -0.15247 255 PRO A O   
1944 C CB  . PRO A 261 ? 3.06502 3.09220 3.41832 0.04653  0.01212  -0.15988 255 PRO A CB  
1945 C CG  . PRO A 261 ? 2.91820 2.95006 3.29947 0.03033  -0.00029 -0.16209 255 PRO A CG  
1946 C CD  . PRO A 261 ? 2.79271 2.84818 3.19244 0.01593  0.01975  -0.15412 255 PRO A CD  
1947 N N   . ASP A 262 ? 2.90257 2.87683 3.19140 0.04485  0.03239  -0.14441 256 ASP A N   
1948 C CA  . ASP A 262 ? 3.02369 2.95493 3.27198 0.05515  0.02509  -0.14577 256 ASP A CA  
1949 C C   . ASP A 262 ? 2.84474 2.77208 3.06206 0.07615  0.03771  -0.14470 256 ASP A C   
1950 O O   . ASP A 262 ? 2.83719 2.73739 3.01948 0.09081  0.03076  -0.15049 256 ASP A O   
1951 C CB  . ASP A 262 ? 2.91641 2.83452 3.16458 0.04491  0.02673  -0.13901 256 ASP A CB  
1952 C CG  . ASP A 262 ? 2.94909 2.86404 3.22291 0.02140  0.01185  -0.13787 256 ASP A CG  
1953 O OD1 . ASP A 262 ? 3.01238 2.93541 3.30564 0.01558  -0.00187 -0.14450 256 ASP A OD1 
1954 O OD2 . ASP A 262 ? 2.97641 2.88129 3.25234 0.00765  0.01267  -0.12899 256 ASP A OD2 
1955 N N   . ILE A 263 ? 2.69325 2.64905 2.92263 0.07731  0.05631  -0.13699 257 ILE A N   
1956 C CA  . ILE A 263 ? 2.66660 2.62863 2.87723 0.09327  0.06885  -0.13353 257 ILE A CA  
1957 C C   . ILE A 263 ? 2.56944 2.53935 2.77851 0.09524  0.06639  -0.13449 257 ILE A C   
1958 O O   . ILE A 263 ? 2.36941 2.33194 2.55116 0.10768  0.07112  -0.13261 257 ILE A O   
1959 C CB  . ILE A 263 ? 2.71117 2.70033 2.93861 0.09146  0.08449  -0.12457 257 ILE A CB  
1960 C CG1 . ILE A 263 ? 2.87255 2.84703 3.09559 0.09046  0.08362  -0.12205 257 ILE A CG1 
1961 C CG2 . ILE A 263 ? 2.75605 2.75893 2.97351 0.10462  0.09689  -0.11902 257 ILE A CG2 
1962 C CD1 . ILE A 263 ? 3.19683 3.19365 3.43247 0.08911  0.09471  -0.11322 257 ILE A CD1 
1963 N N   . TYR A 264 ? 2.55812 2.54277 2.79515 0.08384  0.05892  -0.13700 258 TYR A N   
1964 C CA  . TYR A 264 ? 2.74710 2.73364 2.98274 0.08626  0.05213  -0.13760 258 TYR A CA  
1965 C C   . TYR A 264 ? 2.76276 2.71689 2.96597 0.09378  0.03571  -0.14308 258 TYR A C   
1966 O O   . TYR A 264 ? 2.60531 2.55111 2.78827 0.09949  0.03215  -0.13997 258 TYR A O   
1967 C CB  . TYR A 264 ? 2.92303 2.93241 3.19847 0.07658  0.04596  -0.14209 258 TYR A CB  
1968 C CG  . TYR A 264 ? 3.20608 3.21373 3.48295 0.08043  0.03505  -0.14322 258 TYR A CG  
1969 C CD1 . TYR A 264 ? 2.94836 2.96334 3.22302 0.08209  0.04271  -0.13596 258 TYR A CD1 
1970 C CD2 . TYR A 264 ? 3.54271 3.53860 3.82401 0.08157  0.01358  -0.15089 258 TYR A CD2 
1971 C CE1 . TYR A 264 ? 2.96895 2.97470 3.24188 0.08476  0.02948  -0.13552 258 TYR A CE1 
1972 C CE2 . TYR A 264 ? 3.59252 3.58163 3.87294 0.08652  0.00002  -0.15129 258 TYR A CE2 
1973 C CZ  . TYR A 264 ? 3.24158 3.23331 3.51601 0.08807  0.00817  -0.14322 258 TYR A CZ  
1974 O OH  . TYR A 264 ? 2.86308 2.84064 3.13354 0.09218  -0.00837 -0.14218 258 TYR A OH  
1975 N N   . ASN A 265 ? 2.81727 2.74863 3.01116 0.09299  0.02356  -0.15045 259 ASN A N   
1976 C CA  . ASN A 265 ? 2.84873 2.74371 3.00714 0.10046  0.00365  -0.15794 259 ASN A CA  
1977 C C   . ASN A 265 ? 2.66632 2.53367 2.77179 0.11782  0.01167  -0.15887 259 ASN A C   
1978 O O   . ASN A 265 ? 2.80350 2.64719 2.86675 0.12884  0.00496  -0.16121 259 ASN A O   
1979 C CB  . ASN A 265 ? 3.15140 3.03294 3.32857 0.08911  -0.01910 -0.16669 259 ASN A CB  
1980 C CG  . ASN A 265 ? 3.13146 3.04492 3.36191 0.07533  -0.02806 -0.16788 259 ASN A CG  
1981 O OD1 . ASN A 265 ? 3.07757 3.00414 3.31634 0.07920  -0.03013 -0.16702 259 ASN A OD1 
1982 N ND2 . ASN A 265 ? 3.06700 2.99345 3.33434 0.05949  -0.03342 -0.16944 259 ASN A ND2 
1983 N N   . SER A 266 ? 2.62335 2.49295 2.72811 0.12228  0.02569  -0.15746 260 SER A N   
1984 C CA  . SER A 266 ? 2.79971 2.64731 2.85806 0.14338  0.03460  -0.16087 260 SER A CA  
1985 C C   . SER A 266 ? 2.94040 2.80956 2.98126 0.15390  0.05587  -0.15158 260 SER A C   
1986 O O   . SER A 266 ? 2.91645 2.76945 2.91157 0.17265  0.06312  -0.15492 260 SER A O   
1987 C CB  . SER A 266 ? 2.54856 2.39611 2.61618 0.14734  0.04302  -0.16076 260 SER A CB  
1988 O OG  . SER A 266 ? 2.63551 2.52483 2.74082 0.13941  0.06120  -0.14897 260 SER A OG  
1989 N N   . ILE A 267 ? 2.86137 2.76637 2.93663 0.14174  0.06603  -0.13977 261 ILE A N   
1990 C CA  . ILE A 267 ? 2.92530 2.85031 2.98845 0.14575  0.08357  -0.12751 261 ILE A CA  
1991 C C   . ILE A 267 ? 2.82182 2.72498 2.85325 0.14503  0.07069  -0.12635 261 ILE A C   
1992 O O   . ILE A 267 ? 2.82328 2.72119 2.81384 0.15491  0.08174  -0.12027 261 ILE A O   
1993 C CB  . ILE A 267 ? 2.73780 2.70170 2.84719 0.13194  0.09439  -0.11569 261 ILE A CB  
1994 C CG1 . ILE A 267 ? 2.56152 2.54315 2.69568 0.13376  0.10456  -0.11615 261 ILE A CG1 
1995 C CG2 . ILE A 267 ? 2.70503 2.68870 2.80620 0.13119  0.10985  -0.10031 261 ILE A CG2 
1996 C CD1 . ILE A 267 ? 2.68773 2.70069 2.86388 0.11967  0.10948  -0.10790 261 ILE A CD1 
1997 N N   . ILE A 268 ? 2.61698 2.50863 2.66633 0.13397  0.04727  -0.13154 262 ILE A N   
1998 C CA  . ILE A 268 ? 2.81565 2.68145 2.83468 0.13451  0.02884  -0.13119 262 ILE A CA  
1999 C C   . ILE A 268 ? 2.83604 2.66125 2.79700 0.14925  0.01841  -0.14164 262 ILE A C   
2000 O O   . ILE A 268 ? 2.63733 2.44028 2.54886 0.15603  0.01458  -0.13753 262 ILE A O   
2001 C CB  . ILE A 268 ? 2.82734 2.69468 2.88692 0.12251  0.00418  -0.13686 262 ILE A CB  
2002 C CG1 . ILE A 268 ? 2.66927 2.57215 2.77723 0.11178  0.01465  -0.12894 262 ILE A CG1 
2003 C CG2 . ILE A 268 ? 2.90107 2.73784 2.92977 0.12507  -0.02053 -0.13728 262 ILE A CG2 
2004 C CD1 . ILE A 268 ? 2.99850 2.90910 3.14848 0.10443  -0.00587 -0.13637 262 ILE A CD1 
2005 N N   . GLU A 269 ? 2.86110 2.67154 2.82205 0.15432  0.01224  -0.15498 263 GLU A N   
2006 C CA  . GLU A 269 ? 2.91190 2.67790 2.81343 0.17076  0.00080  -0.16787 263 GLU A CA  
2007 C C   . GLU A 269 ? 2.88761 2.65463 2.73769 0.19069  0.02796  -0.16354 263 GLU A C   
2008 O O   . GLU A 269 ? 3.00332 2.73336 2.78943 0.20675  0.02108  -0.17216 263 GLU A O   
2009 C CB  . GLU A 269 ? 3.06367 2.81170 2.97883 0.17078  -0.01119 -0.18140 263 GLU A CB  
2010 C CG  . GLU A 269 ? 3.39502 3.08652 3.25213 0.18515  -0.03404 -0.19855 263 GLU A CG  
2011 C CD  . GLU A 269 ? 3.44610 3.11483 3.31768 0.18246  -0.04803 -0.20965 263 GLU A CD  
2012 O OE1 . GLU A 269 ? 3.11329 2.81133 3.03019 0.17395  -0.03306 -0.20262 263 GLU A OE1 
2013 O OE2 . GLU A 269 ? 3.82678 3.44434 3.66162 0.18785  -0.07633 -0.22471 263 GLU A OE2 
2014 N N   . ALA A 270 ? 2.69095 2.50163 2.56769 0.19028  0.05852  -0.15060 264 ALA A N   
2015 C CA  . ALA A 270 ? 2.81452 2.63910 2.65322 0.20817  0.08802  -0.14461 264 ALA A CA  
2016 C C   . ALA A 270 ? 3.02130 2.85410 2.83426 0.20161  0.09693  -0.12707 264 ALA A C   
2017 O O   . ALA A 270 ? 3.38982 3.21449 3.14529 0.21684  0.11201  -0.12493 264 ALA A O   
2018 C CB  . ALA A 270 ? 2.87571 2.74664 2.75925 0.21003  0.11440  -0.13758 264 ALA A CB  
2019 N N   . ALA A 271 ? 2.71357 2.56011 2.56494 0.17967  0.08760  -0.11424 265 ALA A N   
2020 C CA  . ALA A 271 ? 2.95862 2.80946 2.78840 0.17044  0.09399  -0.09426 265 ALA A CA  
2021 C C   . ALA A 271 ? 3.16109 2.96223 2.93258 0.17366  0.06814  -0.09797 265 ALA A C   
2022 O O   . ALA A 271 ? 3.37654 3.16789 3.09513 0.17587  0.07795  -0.08439 265 ALA A O   
2023 C CB  . ALA A 271 ? 2.75191 2.62848 2.64118 0.14810  0.08987  -0.08083 265 ALA A CB  
2024 N N   . ILE A 272 ? 3.05483 2.82540 2.83504 0.17284  0.03446  -0.11484 266 ILE A N   
2025 C CA  . ILE A 272 ? 3.24878 2.97203 2.98109 0.17492  0.00288  -0.11907 266 ILE A CA  
2026 C C   . ILE A 272 ? 3.33413 3.01784 2.99645 0.19590  -0.00213 -0.13554 266 ILE A C   
2027 O O   . ILE A 272 ? 3.29670 2.95156 2.88588 0.20525  -0.00209 -0.13086 266 ILE A O   
2028 C CB  . ILE A 272 ? 3.13483 2.84996 2.91786 0.16330  -0.03348 -0.12888 266 ILE A CB  
2029 C CG1 . ILE A 272 ? 3.19896 2.94545 3.03905 0.14693  -0.03092 -0.11466 266 ILE A CG1 
2030 C CG2 . ILE A 272 ? 3.33386 2.99893 3.06928 0.16805  -0.07118 -0.13629 266 ILE A CG2 
2031 C CD1 . ILE A 272 ? 3.06937 2.81417 2.96000 0.13911  -0.06380 -0.12459 266 ILE A CD1 
2032 N N   . ASN A 273 ? 3.25150 2.92942 2.93113 0.20347  -0.00772 -0.15480 267 ASN A N   
2033 C CA  . ASN A 273 ? 3.47905 3.10945 3.09258 0.22398  -0.02042 -0.17453 267 ASN A CA  
2034 C C   . ASN A 273 ? 3.56599 3.20433 3.12618 0.24702  0.01679  -0.17408 267 ASN A C   
2035 O O   . ASN A 273 ? 3.64729 3.24686 3.12613 0.26596  0.01369  -0.18275 267 ASN A O   
2036 C CB  . ASN A 273 ? 3.57340 3.18957 3.22384 0.22203  -0.04222 -0.19382 267 ASN A CB  
2037 C CG  . ASN A 273 ? 3.49196 3.10643 3.19683 0.20026  -0.07748 -0.19521 267 ASN A CG  
2038 O OD1 . ASN A 273 ? 3.34946 2.98076 3.11523 0.18798  -0.08384 -0.19979 267 ASN A OD1 
2039 N ND2 . ASN A 273 ? 3.60218 3.19826 3.28575 0.19577  -0.10019 -0.19036 267 ASN A ND2 
2040 N N   . ARG A 274 ? 3.51381 3.20350 3.11798 0.24719  0.05175  -0.16485 268 ARG A N   
2041 C CA  . ARG A 274 ? 3.65579 3.36447 3.22398 0.27107  0.08885  -0.16567 268 ARG A CA  
2042 C C   . ARG A 274 ? 3.76896 3.52548 3.33772 0.26399  0.12489  -0.13887 268 ARG A C   
2043 O O   . ARG A 274 ? 3.82452 3.60804 3.36826 0.28289  0.16002  -0.13668 268 ARG A O   
2044 C CB  . ARG A 274 ? 3.53985 3.27069 3.15567 0.28037  0.10006  -0.17637 268 ARG A CB  
2045 C CG  . ARG A 274 ? 3.58213 3.25839 3.18018 0.29171  0.06818  -0.20288 268 ARG A CG  
2046 C CD  . ARG A 274 ? 3.31312 3.00364 2.95070 0.30180  0.07732  -0.21162 268 ARG A CD  
2047 N NE  . ARG A 274 ? 3.17899 2.88693 2.89242 0.27489  0.06342  -0.20456 268 ARG A NE  
2048 C CZ  . ARG A 274 ? 3.22946 2.99047 3.00361 0.26403  0.08480  -0.18950 268 ARG A CZ  
2049 N NH1 . ARG A 274 ? 3.24305 3.04887 3.02065 0.27563  0.11958  -0.17881 268 ARG A NH1 
2050 N NH2 . ARG A 274 ? 3.22767 2.99866 3.06048 0.24072  0.07077  -0.18497 268 ARG A NH2 
2051 N N   . GLY A 275 ? 3.82049 3.58829 3.41809 0.23762  0.11647  -0.11849 269 GLY A N   
2052 C CA  . GLY A 275 ? 3.63020 3.43492 3.22473 0.22606  0.14539  -0.09024 269 GLY A CA  
2053 C C   . GLY A 275 ? 3.55355 3.42368 3.20139 0.22563  0.18301  -0.07923 269 GLY A C   
2054 O O   . GLY A 275 ? 3.58951 3.49384 3.21745 0.22813  0.21694  -0.06187 269 GLY A O   
2055 N N   . VAL A 276 ? 3.51986 3.40996 3.23561 0.22165  0.17739  -0.08778 270 VAL A N   
2056 C CA  . VAL A 276 ? 3.44922 3.39899 3.21865 0.22262  0.20733  -0.07938 270 VAL A CA  
2057 C C   . VAL A 276 ? 3.27539 3.26155 3.09268 0.19289  0.21374  -0.05215 270 VAL A C   
2058 O O   . VAL A 276 ? 3.07710 3.04595 2.92214 0.17263  0.18789  -0.04924 270 VAL A O   
2059 C CB  . VAL A 276 ? 3.25895 3.20837 3.07426 0.22975  0.19542  -0.09823 270 VAL A CB  
2060 C CG1 . VAL A 276 ? 3.04734 3.05678 2.92234 0.22857  0.22023  -0.08808 270 VAL A CG1 
2061 C CG2 . VAL A 276 ? 3.12695 3.03628 2.89292 0.25946  0.18820  -0.12435 270 VAL A CG2 
2062 N N   . LYS A 277 ? 3.36886 3.40597 3.19694 0.19062  0.24747  -0.03257 271 LYS A N   
2063 C CA  . LYS A 277 ? 3.23520 3.30797 3.11287 0.16094  0.25284  -0.00594 271 LYS A CA  
2064 C C   . LYS A 277 ? 3.06878 3.16562 3.02080 0.15368  0.24386  -0.01211 271 LYS A C   
2065 O O   . LYS A 277 ? 2.67678 2.81411 2.66095 0.16631  0.26239  -0.01605 271 LYS A O   
2066 C CB  . LYS A 277 ? 3.19023 3.31640 3.06410 0.15879  0.29192  0.01768  271 LYS A CB  
2067 C CG  . LYS A 277 ? 3.39135 3.49620 3.18580 0.16257  0.30446  0.02871  271 LYS A CG  
2068 C CD  . LYS A 277 ? 3.70078 3.86738 3.50181 0.15248  0.34528  0.05830  271 LYS A CD  
2069 C CE  . LYS A 277 ? 3.64772 3.79278 3.36206 0.15487  0.36044  0.07197  271 LYS A CE  
2070 N NZ  . LYS A 277 ? 3.32832 3.53785 3.05212 0.13905  0.40199  0.10584  271 LYS A NZ  
2071 N N   . ILE A 278 ? 3.08813 3.16009 3.06563 0.13524  0.21502  -0.01354 272 ILE A N   
2072 C CA  . ILE A 278 ? 2.93550 3.02143 2.97259 0.12884  0.20360  -0.02161 272 ILE A CA  
2073 C C   . ILE A 278 ? 2.81357 2.91966 2.89222 0.10153  0.19938  -0.00150 272 ILE A C   
2074 O O   . ILE A 278 ? 2.92039 3.00213 2.98222 0.08576  0.18631  0.01018  272 ILE A O   
2075 C CB  . ILE A 278 ? 2.84953 2.89229 2.88322 0.13243  0.17446  -0.04334 272 ILE A CB  
2076 C CG1 . ILE A 278 ? 3.05182 3.06687 3.04090 0.15700  0.17379  -0.06266 272 ILE A CG1 
2077 C CG2 . ILE A 278 ? 2.71459 2.77345 2.80339 0.12578  0.16649  -0.05021 272 ILE A CG2 
2078 C CD1 . ILE A 278 ? 2.93349 2.90825 2.92120 0.15739  0.14438  -0.08177 272 ILE A CD1 
2079 N N   . ARG A 279 ? 2.75034 2.89640 2.88094 0.09654  0.20717  0.00221  273 ARG A N   
2080 C CA  . ARG A 279 ? 2.87814 3.04029 3.05080 0.07114  0.19889  0.01806  273 ARG A CA  
2081 C C   . ARG A 279 ? 2.78794 2.95078 3.00017 0.07097  0.18341  0.00311  273 ARG A C   
2082 O O   . ARG A 279 ? 2.57748 2.76356 2.80860 0.08438  0.19252  -0.00529 273 ARG A O   
2083 C CB  . ARG A 279 ? 2.80017 3.01585 2.99856 0.06127  0.22315  0.04143  273 ARG A CB  
2084 C CG  . ARG A 279 ? 2.79442 3.01460 2.95267 0.05723  0.24237  0.06097  273 ARG A CG  
2085 C CD  . ARG A 279 ? 2.73629 3.02020 2.93014 0.04521  0.26901  0.08566  273 ARG A CD  
2086 N NE  . ARG A 279 ? 2.74169 3.07320 2.96489 0.06846  0.28893  0.07452  273 ARG A NE  
2087 C CZ  . ARG A 279 ? 2.97874 3.37685 3.24478 0.06481  0.31279  0.09090  273 ARG A CZ  
2088 N NH1 . ARG A 279 ? 3.09341 3.52111 3.37974 0.03507  0.32137  0.12131  273 ARG A NH1 
2089 N NH2 . ARG A 279 ? 3.03418 3.47031 3.32576 0.09113  0.32682  0.07721  273 ARG A NH2 
2090 N N   . LEU A 280 ? 2.83798 2.97417 3.05980 0.05742  0.15992  -0.00037 274 LEU A N   
2091 C CA  . LEU A 280 ? 2.76489 2.89832 3.01578 0.05722  0.14586  -0.01521 274 LEU A CA  
2092 C C   . LEU A 280 ? 2.79148 2.93568 3.07576 0.03735  0.13544  -0.00475 274 LEU A C   
2093 O O   . LEU A 280 ? 2.81982 2.94791 3.09893 0.02208  0.12517  0.00723  274 LEU A O   
2094 C CB  . LEU A 280 ? 2.62915 2.72432 2.86383 0.06233  0.12718  -0.03316 274 LEU A CB  
2095 C CG  . LEU A 280 ? 2.71195 2.78841 2.91267 0.07931  0.13026  -0.04474 274 LEU A CG  
2096 C CD1 . LEU A 280 ? 3.25130 3.29704 3.44743 0.08046  0.10915  -0.06044 274 LEU A CD1 
2097 C CD2 . LEU A 280 ? 2.92118 3.01501 3.12722 0.09369  0.14371  -0.05245 274 LEU A CD2 
2098 N N   . LEU A 281 ? 2.75018 2.91633 3.06527 0.03760  0.13499  -0.00935 275 LEU A N   
2099 C CA  . LEU A 281 ? 2.65697 2.83118 3.00236 0.02018  0.12179  -0.00246 275 LEU A CA  
2100 C C   . LEU A 281 ? 2.60108 2.76326 2.95396 0.02561  0.10886  -0.02170 275 LEU A C   
2101 O O   . LEU A 281 ? 2.44587 2.62774 2.81231 0.03264  0.11383  -0.02586 275 LEU A O   
2102 C CB  . LEU A 281 ? 2.55297 2.77305 2.92960 0.01326  0.13420  0.01489  275 LEU A CB  
2103 C CG  . LEU A 281 ? 2.50959 2.73872 2.91975 -0.00737 0.11719  0.02384  275 LEU A CG  
2104 C CD1 . LEU A 281 ? 2.47196 2.67176 2.87385 -0.02813 0.10153  0.03517  275 LEU A CD1 
2105 C CD2 . LEU A 281 ? 2.66400 2.94702 3.11269 -0.01235 0.12961  0.04035  275 LEU A CD2 
2106 N N   . VAL A 282 ? 2.69914 2.82942 3.04188 0.02341  0.09244  -0.03312 276 VAL A N   
2107 C CA  . VAL A 282 ? 2.77273 2.89395 3.11933 0.02845  0.08309  -0.05138 276 VAL A CA  
2108 C C   . VAL A 282 ? 2.67571 2.78310 3.03222 0.01679  0.06351  -0.05278 276 VAL A C   
2109 O O   . VAL A 282 ? 2.65994 2.76030 3.02117 0.00317  0.05475  -0.03886 276 VAL A O   
2110 C CB  . VAL A 282 ? 2.71169 2.81302 3.04171 0.03965  0.08172  -0.06765 276 VAL A CB  
2111 C CG1 . VAL A 282 ? 2.91423 3.02116 3.23054 0.05025  0.09630  -0.06715 276 VAL A CG1 
2112 C CG2 . VAL A 282 ? 2.43642 2.51076 2.75751 0.03659  0.06711  -0.06870 276 VAL A CG2 
2113 N N   . CYS A 283 ? 2.60353 2.70442 2.96008 0.02162  0.05603  -0.06927 277 CYS A N   
2114 C CA  . CYS A 283 ? 2.58901 2.67079 2.94813 0.01474  0.03559  -0.07562 277 CYS A CA  
2115 C C   . CYS A 283 ? 2.74366 2.79377 3.09218 0.01874  0.02235  -0.08545 277 CYS A C   
2116 O O   . CYS A 283 ? 2.76778 2.81369 3.10851 0.02736  0.02863  -0.08914 277 CYS A O   
2117 C CB  . CYS A 283 ? 2.60122 2.68646 2.95642 0.02123  0.03385  -0.09120 277 CYS A CB  
2118 S SG  . CYS A 283 ? 3.73808 3.85417 4.10327 0.01929  0.04332  -0.08091 277 CYS A SG  
2119 N N   . ASN A 284 ? 2.89954 2.92421 3.24755 0.01341  0.00046  -0.09056 278 ASN A N   
2120 C CA  . ASN A 284 ? 3.07881 3.07051 3.41735 0.02232  -0.01563 -0.10464 278 ASN A CA  
2121 C C   . ASN A 284 ? 3.34119 3.34064 3.67629 0.04197  -0.00831 -0.13026 278 ASN A C   
2122 O O   . ASN A 284 ? 3.40746 3.43029 3.74257 0.04517  0.00567  -0.13607 278 ASN A O   
2123 C CB  . ASN A 284 ? 3.12084 3.07714 3.45719 0.01301  -0.04389 -0.10503 278 ASN A CB  
2124 C CG  . ASN A 284 ? 3.48784 3.44298 3.82130 0.01637  -0.05177 -0.12108 278 ASN A CG  
2125 O OD1 . ASN A 284 ? 3.51097 3.49587 3.84817 0.01552  -0.03715 -0.11968 278 ASN A OD1 
2126 N ND2 . ASN A 284 ? 3.86152 3.77790 4.18405 0.02181  -0.07699 -0.13722 278 ASN A ND2 
2127 N N   . TRP A 285 ? 3.32877 3.30973 3.66193 0.05496  -0.01815 -0.14450 279 TRP A N   
2128 C CA  . TRP A 285 ? 3.46314 3.46036 3.80057 0.07319  -0.00843 -0.16699 279 TRP A CA  
2129 C C   . TRP A 285 ? 3.49319 3.46640 3.82784 0.08850  -0.02709 -0.18997 279 TRP A C   
2130 O O   . TRP A 285 ? 3.39774 3.33281 3.72630 0.08649  -0.05173 -0.18815 279 TRP A O   
2131 C CB  . TRP A 285 ? 3.37271 3.38126 3.71806 0.07890  -0.00032 -0.16518 279 TRP A CB  
2132 C CG  . TRP A 285 ? 3.52191 3.49892 3.86437 0.08142  -0.02116 -0.16155 279 TRP A CG  
2133 C CD1 . TRP A 285 ? 3.63846 3.60194 3.98855 0.09832  -0.03646 -0.17887 279 TRP A CD1 
2134 C CD2 . TRP A 285 ? 3.57928 3.53408 3.90913 0.06697  -0.02962 -0.13810 279 TRP A CD2 
2135 N NE1 . TRP A 285 ? 3.85739 3.78548 4.19730 0.09527  -0.05722 -0.16724 279 TRP A NE1 
2136 C CE2 . TRP A 285 ? 3.83659 3.75865 4.16165 0.07468  -0.05205 -0.14114 279 TRP A CE2 
2137 C CE3 . TRP A 285 ? 3.27894 3.24122 3.60195 0.04892  -0.01956 -0.11431 279 TRP A CE3 
2138 C CZ2 . TRP A 285 ? 3.75247 3.64461 4.05978 0.06241  -0.06455 -0.11913 279 TRP A CZ2 
2139 C CZ3 . TRP A 285 ? 3.44065 3.38057 3.75038 0.03717  -0.02840 -0.09328 279 TRP A CZ3 
2140 C CH2 . TRP A 285 ? 3.60289 3.50582 3.90175 0.04266  -0.05065 -0.09475 279 TRP A CH2 
2141 N N   . ASP A 286 ? 3.47023 3.46562 3.80825 0.10424  -0.01487 -0.21150 280 ASP A N   
2142 C CA  . ASP A 286 ? 3.57692 3.55622 3.91233 0.12494  -0.02829 -0.23798 280 ASP A CA  
2143 C C   . ASP A 286 ? 3.51052 3.47759 3.86157 0.13914  -0.04238 -0.24536 280 ASP A C   
2144 O O   . ASP A 286 ? 3.34432 3.33745 3.71344 0.14087  -0.03080 -0.24176 280 ASP A O   
2145 C CB  . ASP A 286 ? 3.58987 3.60501 3.92457 0.13793  -0.00567 -0.25737 280 ASP A CB  
2146 C CG  . ASP A 286 ? 3.81706 3.81990 4.14590 0.16354  -0.01589 -0.28799 280 ASP A CG  
2147 O OD1 . ASP A 286 ? 3.96323 3.92029 4.28278 0.16956  -0.04497 -0.29446 280 ASP A OD1 
2148 O OD2 . ASP A 286 ? 3.70049 3.73905 4.03316 0.17799  0.00534  -0.30553 280 ASP A OD2 
2149 N N   . LYS A 287 ? 3.55945 3.48266 3.90258 0.14945  -0.07109 -0.25583 281 LYS A N   
2150 C CA  . LYS A 287 ? 3.46028 3.36608 3.81669 0.16644  -0.08980 -0.26458 281 LYS A CA  
2151 C C   . LYS A 287 ? 3.59008 3.53591 3.97154 0.19353  -0.07649 -0.29181 281 LYS A C   
2152 O O   . LYS A 287 ? 3.45383 3.40397 3.85702 0.20638  -0.08579 -0.29660 281 LYS A O   
2153 C CB  . LYS A 287 ? 3.30529 3.14819 3.64471 0.17220  -0.12678 -0.27017 281 LYS A CB  
2154 C CG  . LYS A 287 ? 3.08192 2.88712 3.40231 0.14193  -0.14170 -0.24009 281 LYS A CG  
2155 C CD  . LYS A 287 ? 3.22239 2.95984 3.52596 0.14507  -0.18175 -0.24472 281 LYS A CD  
2156 C CE  . LYS A 287 ? 3.37061 3.07602 3.66037 0.11017  -0.19542 -0.21121 281 LYS A CE  
2157 N NZ  . LYS A 287 ? 3.78012 3.41318 4.05267 0.10887  -0.23794 -0.21300 281 LYS A NZ  
2158 N N   . ASN A 288 ? 3.70059 3.67786 4.07987 0.20196  -0.05507 -0.30872 282 ASN A N   
2159 C CA  . ASN A 288 ? 3.78767 3.81374 4.19352 0.22515  -0.03621 -0.33242 282 ASN A CA  
2160 C C   . ASN A 288 ? 3.73326 3.81351 4.16422 0.21172  -0.00831 -0.31902 282 ASN A C   
2161 O O   . ASN A 288 ? 3.89400 4.02077 4.35658 0.22634  0.00675  -0.33397 282 ASN A O   
2162 C CB  . ASN A 288 ? 3.75940 3.79652 4.14568 0.23928  -0.02251 -0.35513 282 ASN A CB  
2163 C CG  . ASN A 288 ? 3.82030 3.79689 4.17640 0.25202  -0.05336 -0.37034 282 ASN A CG  
2164 O OD1 . ASN A 288 ? 3.94825 3.90245 4.27084 0.24186  -0.05566 -0.36857 282 ASN A OD1 
2165 N ND2 . ASN A 288 ? 3.84888 3.79499 4.21632 0.27436  -0.08079 -0.38542 282 ASN A ND2 
2166 N N   . ASP A 289 ? 3.41615 3.49208 3.83558 0.18477  -0.00189 -0.29181 283 ASP A N   
2167 C CA  . ASP A 289 ? 3.16140 3.27786 3.59892 0.17101  0.02018  -0.27869 283 ASP A CA  
2168 C C   . ASP A 289 ? 3.23251 3.34093 3.68923 0.17065  0.00389  -0.27063 283 ASP A C   
2169 O O   . ASP A 289 ? 2.98837 3.05958 3.42618 0.15945  -0.01191 -0.25307 283 ASP A O   
2170 C CB  . ASP A 289 ? 2.71519 2.82792 3.12807 0.14687  0.03343  -0.25643 283 ASP A CB  
2171 C CG  . ASP A 289 ? 2.94068 3.08886 3.36725 0.13385  0.05482  -0.24491 283 ASP A CG  
2172 O OD1 . ASP A 289 ? 3.01240 3.19418 3.46931 0.14083  0.06236  -0.25446 283 ASP A OD1 
2173 O OD2 . ASP A 289 ? 3.22969 3.37192 3.63881 0.11676  0.06244  -0.22637 283 ASP A OD2 
2174 N N   . VAL A 290 ? 3.37565 3.52095 3.86979 0.18239  0.00764  -0.28282 284 VAL A N   
2175 C CA  . VAL A 290 ? 3.30346 3.44102 3.81574 0.18350  -0.01160 -0.27713 284 VAL A CA  
2176 C C   . VAL A 290 ? 3.12541 3.26428 3.62784 0.16013  -0.00338 -0.25457 284 VAL A C   
2177 O O   . VAL A 290 ? 3.20303 3.31665 3.69873 0.15689  -0.02207 -0.24437 284 VAL A O   
2178 C CB  . VAL A 290 ? 3.01745 3.19923 3.58012 0.20332  -0.01265 -0.29771 284 VAL A CB  
2179 C CG1 . VAL A 290 ? 3.10863 3.28330 3.67902 0.23271  -0.02455 -0.32301 284 VAL A CG1 
2180 C CG2 . VAL A 290 ? 2.80785 3.05096 3.39671 0.19375  0.01989  -0.29894 284 VAL A CG2 
2181 N N   . TYR A 291 ? 2.99887 3.16250 3.49580 0.14513  0.02268  -0.24700 285 TYR A N   
2182 C CA  . TYR A 291 ? 2.96767 3.12705 3.45209 0.12594  0.02884  -0.22777 285 TYR A CA  
2183 C C   . TYR A 291 ? 2.83299 2.95032 3.27756 0.11674  0.02213  -0.21030 285 TYR A C   
2184 O O   . TYR A 291 ? 2.68250 2.78439 3.11276 0.10824  0.01803  -0.19685 285 TYR A O   
2185 C CB  . TYR A 291 ? 2.96736 3.16049 3.45639 0.11337  0.05581  -0.22417 285 TYR A CB  
2186 C CG  . TYR A 291 ? 3.13412 3.37489 3.66618 0.11482  0.06521  -0.23440 285 TYR A CG  
2187 C CD1 . TYR A 291 ? 3.18539 3.43541 3.75016 0.12046  0.04781  -0.23998 285 TYR A CD1 
2188 C CD2 . TYR A 291 ? 3.23006 3.50845 3.77069 0.10934  0.09096  -0.23712 285 TYR A CD2 
2189 C CE1 . TYR A 291 ? 3.10579 3.40660 3.71867 0.11977  0.05588  -0.24811 285 TYR A CE1 
2190 C CE2 . TYR A 291 ? 3.26928 3.59813 3.85355 0.10762  0.10239  -0.24375 285 TYR A CE2 
2191 C CZ  . TYR A 291 ? 3.21356 3.55615 3.83790 0.11244  0.08482  -0.24930 285 TYR A CZ  
2192 O OH  . TYR A 291 ? 3.24563 3.64539 3.92191 0.10882  0.09563  -0.25477 285 TYR A OH  
2193 N N   . SER A 292 ? 2.88342 2.98330 3.31008 0.11827  0.02081  -0.21053 286 SER A N   
2194 C CA  . SER A 292 ? 2.87700 2.94447 3.27373 0.10742  0.01506  -0.19234 286 SER A CA  
2195 C C   . SER A 292 ? 3.00282 3.03340 3.38998 0.11164  -0.01012 -0.18785 286 SER A C   
2196 O O   . SER A 292 ? 3.07256 3.08209 3.43729 0.10109  -0.01326 -0.16911 286 SER A O   
2197 C CB  . SER A 292 ? 2.88092 2.94456 3.26500 0.10370  0.02050  -0.19250 286 SER A CB  
2198 O OG  . SER A 292 ? 2.94170 3.03401 3.32683 0.09859  0.04231  -0.19330 286 SER A OG  
2199 N N   . MET A 293 ? 2.97008 2.99211 3.37221 0.12786  -0.02799 -0.20434 287 MET A N   
2200 C CA  . MET A 293 ? 3.11946 3.10029 3.51006 0.13252  -0.05602 -0.19925 287 MET A CA  
2201 C C   . MET A 293 ? 2.99903 2.97761 3.38820 0.13167  -0.06317 -0.19178 287 MET A C   
2202 O O   . MET A 293 ? 3.01485 2.95882 3.37542 0.12449  -0.07616 -0.17468 287 MET A O   
2203 C CB  . MET A 293 ? 3.09384 3.06417 3.50205 0.15442  -0.07604 -0.22155 287 MET A CB  
2204 C CG  . MET A 293 ? 3.11969 3.07552 3.51832 0.15703  -0.07746 -0.23005 287 MET A CG  
2205 S SD  . MET A 293 ? 3.81018 3.71095 4.17197 0.13603  -0.09469 -0.20459 287 MET A SD  
2206 C CE  . MET A 293 ? 3.23356 3.08559 3.58658 0.14419  -0.13041 -0.19900 287 MET A CE  
2207 N N   . ALA A 294 ? 2.86625 2.88074 3.28431 0.13772  -0.05568 -0.20368 288 ALA A N   
2208 C CA  . ALA A 294 ? 2.96481 2.97534 3.38094 0.13611  -0.06578 -0.19823 288 ALA A CA  
2209 C C   . ALA A 294 ? 3.08270 3.08421 3.46493 0.11939  -0.05121 -0.17888 288 ALA A C   
2210 O O   . ALA A 294 ? 3.21901 3.19435 3.57468 0.11714  -0.06345 -0.16851 288 ALA A O   
2211 C CB  . ALA A 294 ? 3.00218 3.05691 3.46348 0.14298  -0.06199 -0.21459 288 ALA A CB  
2212 N N   . THR A 295 ? 3.11854 3.14030 3.49867 0.10970  -0.02590 -0.17468 289 THR A N   
2213 C CA  . THR A 295 ? 3.06915 3.08393 3.41942 0.09796  -0.01179 -0.15816 289 THR A CA  
2214 C C   . THR A 295 ? 3.04868 3.03251 3.36533 0.09235  -0.01648 -0.14059 289 THR A C   
2215 O O   . THR A 295 ? 2.93158 2.90041 3.21796 0.08819  -0.01419 -0.12751 289 THR A O   
2216 C CB  . THR A 295 ? 2.84710 2.88952 3.20544 0.09090  0.01285  -0.15798 289 THR A CB  
2217 O OG1 . THR A 295 ? 2.57679 2.64859 2.96527 0.09268  0.01849  -0.17107 289 THR A OG1 
2218 C CG2 . THR A 295 ? 2.86684 2.90350 3.19832 0.08338  0.02595  -0.14363 289 THR A CG2 
2219 N N   . ALA A 296 ? 3.12628 3.09963 3.44644 0.09172  -0.02332 -0.13991 290 ALA A N   
2220 C CA  . ALA A 296 ? 3.30386 3.24902 3.59660 0.08173  -0.02889 -0.12018 290 ALA A CA  
2221 C C   . ALA A 296 ? 3.16649 3.07562 3.43505 0.08468  -0.05101 -0.11261 290 ALA A C   
2222 O O   . ALA A 296 ? 3.23364 3.12637 3.46875 0.07540  -0.04740 -0.09265 290 ALA A O   
2223 C CB  . ALA A 296 ? 3.51529 3.45170 3.81824 0.07880  -0.03650 -0.12230 290 ALA A CB  
2224 N N   . ARG A 297 ? 2.87996 2.77760 3.16407 0.09853  -0.07403 -0.12803 291 ARG A N   
2225 C CA  . ARG A 297 ? 2.93202 2.79162 3.19142 0.10288  -0.09981 -0.12118 291 ARG A CA  
2226 C C   . ARG A 297 ? 3.08054 2.94203 3.31784 0.10282  -0.09537 -0.11711 291 ARG A C   
2227 O O   . ARG A 297 ? 2.93838 2.76540 3.13584 0.10102  -0.10918 -0.10345 291 ARG A O   
2228 C CB  . ARG A 297 ? 2.88065 2.73134 3.16835 0.12136  -0.12773 -0.14107 291 ARG A CB  
2229 C CG  . ARG A 297 ? 2.78933 2.61410 3.08127 0.12431  -0.14348 -0.14319 291 ARG A CG  
2230 C CD  . ARG A 297 ? 2.88444 2.69359 3.19905 0.14730  -0.17512 -0.16270 291 ARG A CD  
2231 N NE  . ARG A 297 ? 3.20784 3.06658 3.57183 0.16376  -0.16470 -0.18997 291 ARG A NE  
2232 C CZ  . ARG A 297 ? 3.19624 3.06884 3.58511 0.17554  -0.16133 -0.20869 291 ARG A CZ  
2233 N NH1 . ARG A 297 ? 2.76842 2.60424 3.13874 0.17320  -0.17194 -0.20518 291 ARG A NH1 
2234 N NH2 . ARG A 297 ? 3.27737 3.20123 3.70907 0.18932  -0.14735 -0.23124 291 ARG A NH2 
2235 N N   . SER A 298 ? 3.20671 3.10342 3.46463 0.10436  -0.07799 -0.12838 292 SER A N   
2236 C CA  . SER A 298 ? 3.13561 3.02859 3.36849 0.10393  -0.07491 -0.12567 292 SER A CA  
2237 C C   . SER A 298 ? 2.96238 2.84565 3.15089 0.09447  -0.05481 -0.10576 292 SER A C   
2238 O O   . SER A 298 ? 2.91563 2.77453 3.06092 0.09575  -0.05971 -0.09761 292 SER A O   
2239 C CB  . SER A 298 ? 3.02298 2.95180 3.28969 0.10526  -0.06309 -0.14100 292 SER A CB  
2240 O OG  . SER A 298 ? 3.22175 3.16763 3.53304 0.11380  -0.07938 -0.15847 292 SER A OG  
2241 N N   . LEU A 299 ? 3.04092 2.94490 3.23935 0.08603  -0.03231 -0.09828 293 LEU A N   
2242 C CA  . LEU A 299 ? 3.20125 3.10572 3.36763 0.07762  -0.01166 -0.07876 293 LEU A CA  
2243 C C   . LEU A 299 ? 3.27942 3.15398 3.41482 0.06913  -0.02144 -0.05811 293 LEU A C   
2244 O O   . LEU A 299 ? 3.34757 3.21851 3.44637 0.06361  -0.00684 -0.04037 293 LEU A O   
2245 C CB  . LEU A 299 ? 3.33077 3.26903 3.52395 0.07087  0.01113  -0.07679 293 LEU A CB  
2246 C CG  . LEU A 299 ? 3.41389 3.37950 3.63234 0.07629  0.02303  -0.09252 293 LEU A CG  
2247 C CD1 . LEU A 299 ? 4.16200 4.15517 4.40134 0.06968  0.04116  -0.08827 293 LEU A CD1 
2248 C CD2 . LEU A 299 ? 3.55889 3.51999 3.75094 0.08307  0.03023  -0.09450 293 LEU A CD2 
2249 N N   . ASP A 300 ? 3.18956 3.04214 3.33769 0.06832  -0.04555 -0.05962 294 ASP A N   
2250 C CA  . ASP A 300 ? 3.32197 3.13840 3.43893 0.05765  -0.05899 -0.03762 294 ASP A CA  
2251 C C   . ASP A 300 ? 3.30125 3.08351 3.36795 0.06229  -0.07234 -0.02956 294 ASP A C   
2252 O O   . ASP A 300 ? 3.45553 3.21732 3.47911 0.05075  -0.06809 -0.00488 294 ASP A O   
2253 C CB  . ASP A 300 ? 3.22238 3.01596 3.36371 0.05901  -0.08628 -0.04438 294 ASP A CB  
2254 C CG  . ASP A 300 ? 3.34421 3.09694 3.45663 0.04320  -0.10116 -0.01870 294 ASP A CG  
2255 O OD1 . ASP A 300 ? 3.38075 3.14550 3.49340 0.02438  -0.08436 0.00019  294 ASP A OD1 
2256 O OD2 . ASP A 300 ? 3.62490 3.33308 3.71620 0.04858  -0.13159 -0.01634 294 ASP A OD2 
2257 N N   . ALA A 301 ? 2.97147 2.74798 3.04202 0.07794  -0.08893 -0.04911 295 ALA A N   
2258 C CA  . ALA A 301 ? 2.86879 2.60936 2.88842 0.08365  -0.10618 -0.04375 295 ALA A CA  
2259 C C   . ALA A 301 ? 2.90644 2.65667 2.88474 0.08379  -0.08043 -0.03799 295 ALA A C   
2260 O O   . ALA A 301 ? 2.71259 2.43013 2.63283 0.08615  -0.08877 -0.02828 295 ALA A O   
2261 C CB  . ALA A 301 ? 3.08864 2.82154 3.13213 0.09974  -0.13692 -0.06708 295 ALA A CB  
2262 N N   . LEU A 302 ? 2.95698 2.74830 2.96014 0.08324  -0.05072 -0.04450 296 LEU A N   
2263 C CA  . LEU A 302 ? 3.08930 2.89085 3.05633 0.08731  -0.02542 -0.04171 296 LEU A CA  
2264 C C   . LEU A 302 ? 3.36609 3.17849 3.30545 0.07611  0.00229  -0.01602 296 LEU A C   
2265 O O   . LEU A 302 ? 3.28211 3.08991 3.17103 0.08129  0.01852  -0.00880 296 LEU A O   
2266 C CB  . LEU A 302 ? 3.06533 2.90295 3.07181 0.09318  -0.00886 -0.05989 296 LEU A CB  
2267 C CG  . LEU A 302 ? 3.05335 2.88832 3.08862 0.10147  -0.03076 -0.08350 296 LEU A CG  
2268 C CD1 . LEU A 302 ? 3.08020 2.94942 3.15315 0.10241  -0.01246 -0.09580 296 LEU A CD1 
2269 C CD2 . LEU A 302 ? 3.15154 2.95110 3.13940 0.11111  -0.05007 -0.08977 296 LEU A CD2 
2270 N N   . CYS A 303 ? 3.52721 3.35540 3.49896 0.06092  0.00803  -0.00244 297 CYS A N   
2271 C CA  . CYS A 303 ? 3.57767 3.42180 3.53196 0.04607  0.03316  0.02486  297 CYS A CA  
2272 C C   . CYS A 303 ? 3.60158 3.40607 3.49477 0.03832  0.02396  0.04783  297 CYS A C   
2273 O O   . CYS A 303 ? 3.59318 3.41089 3.45141 0.03132  0.05028  0.06898  297 CYS A O   
2274 C CB  . CYS A 303 ? 3.52644 3.39138 3.53155 0.02901  0.03459  0.03378  297 CYS A CB  
2275 S SG  . CYS A 303 ? 3.41877 3.33118 3.48690 0.03564  0.04873  0.01205  297 CYS A SG  
2276 N N   . VAL A 304 ? 3.51316 3.27048 3.39231 0.04004  -0.01273 0.04480  298 VAL A N   
2277 C CA  . VAL A 304 ? 3.39645 3.10790 3.21206 0.03238  -0.02648 0.06804  298 VAL A CA  
2278 C C   . VAL A 304 ? 3.39248 3.07954 3.14526 0.04938  -0.03020 0.06005  298 VAL A C   
2279 O O   . VAL A 304 ? 3.53671 3.19022 3.22231 0.04401  -0.03282 0.08138  298 VAL A O   
2280 C CB  . VAL A 304 ? 3.24817 2.91330 3.07411 0.02783  -0.06908 0.06992  298 VAL A CB  
2281 C CG1 . VAL A 304 ? 3.25103 2.93215 3.13131 0.01174  -0.06840 0.07648  298 VAL A CG1 
2282 C CG2 . VAL A 304 ? 2.85426 2.50568 2.70244 0.04988  -0.09974 0.03802  298 VAL A CG2 
2283 N N   . GLN A 305 ? 3.27664 2.97648 3.04565 0.06844  -0.03178 0.03090  299 GLN A N   
2284 C CA  . GLN A 305 ? 3.38384 3.05536 3.09475 0.08513  -0.04128 0.01943  299 GLN A CA  
2285 C C   . GLN A 305 ? 3.54808 3.24767 3.23355 0.09579  -0.00477 0.01357  299 GLN A C   
2286 O O   . GLN A 305 ? 3.58115 3.25389 3.19589 0.10695  -0.00393 0.01310  299 GLN A O   
2287 C CB  . GLN A 305 ? 3.21661 2.87415 2.96084 0.09855  -0.07691 -0.00962 299 GLN A CB  
2288 C CG  . GLN A 305 ? 3.74397 3.36339 3.43079 0.11381  -0.09848 -0.02232 299 GLN A CG  
2289 C CD  . GLN A 305 ? 3.95527 3.52260 3.56231 0.11145  -0.11592 -0.00155 299 GLN A CD  
2290 O OE1 . GLN A 305 ? 3.86863 3.41511 3.47743 0.10012  -0.13282 0.01660  299 GLN A OE1 
2291 N NE2 . GLN A 305 ? 4.17330 3.71465 3.70479 0.12273  -0.11343 -0.00418 299 GLN A NE2 
2292 N N   . ASN A 306 ? 3.46340 3.21339 3.20126 0.09461  0.02369  0.00834  300 ASN A N   
2293 C CA  . ASN A 306 ? 3.36827 3.14750 3.08846 0.10723  0.05846  0.00261  300 ASN A CA  
2294 C C   . ASN A 306 ? 3.35522 3.18563 3.10710 0.09404  0.09495  0.02327  300 ASN A C   
2295 O O   . ASN A 306 ? 3.31705 3.15463 3.09981 0.07322  0.09092  0.04217  300 ASN A O   
2296 C CB  . ASN A 306 ? 2.98670 2.77518 2.74165 0.12240  0.05245  -0.02781 300 ASN A CB  
2297 C CG  . ASN A 306 ? 3.18721 2.92897 2.91248 0.13377  0.01642  -0.04745 300 ASN A CG  
2298 O OD1 . ASN A 306 ? 3.34132 3.07037 3.10280 0.12863  -0.01469 -0.05561 300 ASN A OD1 
2299 N ND2 . ASN A 306 ? 3.13840 2.85524 2.79791 0.15032  0.01945  -0.05601 300 ASN A ND2 
2300 N N   . ASP A 307 ? 3.50413 3.36940 3.24950 0.10709  0.12853  0.01892  301 ASP A N   
2301 C CA  . ASP A 307 ? 3.55001 3.47226 3.33111 0.09702  0.16398  0.03723  301 ASP A CA  
2302 C C   . ASP A 307 ? 3.25577 3.20954 3.11515 0.09504  0.16142  0.02379  301 ASP A C   
2303 O O   . ASP A 307 ? 3.16495 3.14653 3.04404 0.11078  0.17780  0.00902  301 ASP A O   
2304 C CB  . ASP A 307 ? 3.68623 3.63506 3.42611 0.11564  0.20125  0.03783  301 ASP A CB  
2305 C CG  . ASP A 307 ? 3.68686 3.69085 3.44503 0.10008  0.23763  0.06760  301 ASP A CG  
2306 O OD1 . ASP A 307 ? 3.83135 3.86724 3.65651 0.08011  0.23746  0.07900  301 ASP A OD1 
2307 O OD2 . ASP A 307 ? 3.71039 3.72681 3.41556 0.10728  0.26613  0.07980  301 ASP A OD2 
2308 N N   . LEU A 308 ? 3.28675 3.23177 3.18700 0.07666  0.13868  0.02861  302 LEU A N   
2309 C CA  . LEU A 308 ? 3.29837 3.26799 3.26628 0.07269  0.13355  0.01731  302 LEU A CA  
2310 C C   . LEU A 308 ? 3.51461 3.49715 3.51882 0.04764  0.13004  0.03838  302 LEU A C   
2311 O O   . LEU A 308 ? 3.71742 3.66987 3.69917 0.03345  0.11494  0.05485  302 LEU A O   
2312 C CB  . LEU A 308 ? 2.83248 2.77178 2.81373 0.08061  0.10312  -0.00753 302 LEU A CB  
2313 C CG  . LEU A 308 ? 2.73248 2.69231 2.77610 0.07645  0.09640  -0.01980 302 LEU A CG  
2314 C CD1 . LEU A 308 ? 2.54534 2.54260 2.61185 0.08534  0.11979  -0.02648 302 LEU A CD1 
2315 C CD2 . LEU A 308 ? 2.86038 2.79395 2.91414 0.08271  0.06864  -0.04098 302 LEU A CD2 
2316 N N   . SER A 309 ? 3.44027 3.46295 3.49791 0.04209  0.14090  0.03809  303 SER A N   
2317 C CA  . SER A 309 ? 3.52609 3.56007 3.62134 0.01809  0.13447  0.05555  303 SER A CA  
2318 C C   . SER A 309 ? 3.39072 3.44065 3.53856 0.01954  0.12556  0.03837  303 SER A C   
2319 O O   . SER A 309 ? 3.39640 3.47399 3.56128 0.03341  0.13955  0.02528  303 SER A O   
2320 C CB  . SER A 309 ? 3.72016 3.79730 3.82258 0.00364  0.16271  0.08332  303 SER A CB  
2321 O OG  . SER A 309 ? 3.49911 3.56224 3.54716 0.00055  0.17374  0.10187  303 SER A OG  
2322 N N   . VAL A 310 ? 3.15263 3.18126 3.32155 0.00643  0.10113  0.03816  304 VAL A N   
2323 C CA  . VAL A 310 ? 2.86954 2.90671 3.07946 0.00818  0.09043  0.02084  304 VAL A CA  
2324 C C   . VAL A 310 ? 2.78512 2.82471 3.02292 -0.01408 0.07941  0.03563  304 VAL A C   
2325 O O   . VAL A 310 ? 2.81035 2.81876 3.03427 -0.02860 0.06302  0.04994  304 VAL A O   
2326 C CB  . VAL A 310 ? 2.73333 2.73755 2.93942 0.02062  0.06776  -0.00306 304 VAL A CB  
2327 C CG1 . VAL A 310 ? 2.82007 2.83473 3.06333 0.02170  0.05980  -0.01941 304 VAL A CG1 
2328 C CG2 . VAL A 310 ? 2.78539 2.78621 2.96804 0.03936  0.07472  -0.01734 304 VAL A CG2 
2329 N N   . LYS A 311 ? 2.75257 2.82453 3.02740 -0.01719 0.08509  0.03256  305 LYS A N   
2330 C CA  . LYS A 311 ? 2.74341 2.81514 3.04697 -0.03743 0.06961  0.04201  305 LYS A CA  
2331 C C   . LYS A 311 ? 2.70661 2.78237 3.03390 -0.02872 0.05973  0.01930  305 LYS A C   
2332 O O   . LYS A 311 ? 2.64955 2.74613 2.98071 -0.01234 0.07308  0.00505  305 LYS A O   
2333 C CB  . LYS A 311 ? 2.65258 2.76736 2.97937 -0.05594 0.08672  0.06875  305 LYS A CB  
2334 C CG  . LYS A 311 ? 2.71008 2.82088 3.01275 -0.07113 0.09626  0.09652  305 LYS A CG  
2335 C CD  . LYS A 311 ? 2.66039 2.81928 2.99648 -0.09450 0.11151  0.12515  305 LYS A CD  
2336 C CE  . LYS A 311 ? 2.60911 2.76314 2.91829 -0.11390 0.12190  0.15643  305 LYS A CE  
2337 N NZ  . LYS A 311 ? 2.24861 2.45575 2.59747 -0.14099 0.13749  0.18737  305 LYS A NZ  
2338 N N   . VAL A 312 ? 2.76635 2.81780 3.10493 -0.03973 0.03503  0.01618  306 VAL A N   
2339 C CA  . VAL A 312 ? 2.73685 2.78557 3.08866 -0.03099 0.02391  -0.00639 306 VAL A CA  
2340 C C   . VAL A 312 ? 2.69391 2.75479 3.07241 -0.04917 0.01287  0.00334  306 VAL A C   
2341 O O   . VAL A 312 ? 2.66041 2.72278 3.04985 -0.07143 0.00713  0.02670  306 VAL A O   
2342 C CB  . VAL A 312 ? 2.75329 2.75833 3.09012 -0.02058 0.00173  -0.02722 306 VAL A CB  
2343 C CG1 . VAL A 312 ? 2.84059 2.83807 3.15777 -0.00338 0.00961  -0.03699 306 VAL A CG1 
2344 C CG2 . VAL A 312 ? 2.78073 2.74555 3.11267 -0.03685 -0.02472 -0.01599 306 VAL A CG2 
2345 N N   . PHE A 313 ? 2.77592 2.84524 3.16406 -0.04097 0.00878  -0.01380 307 PHE A N   
2346 C CA  . PHE A 313 ? 2.77199 2.84842 3.18251 -0.05586 -0.00707 -0.00897 307 PHE A CA  
2347 C C   . PHE A 313 ? 2.71661 2.76986 3.11520 -0.04351 -0.02297 -0.03581 307 PHE A C   
2348 O O   . PHE A 313 ? 2.70325 2.75458 3.08533 -0.02353 -0.01248 -0.05502 307 PHE A O   
2349 C CB  . PHE A 313 ? 2.67117 2.80067 3.10994 -0.05955 0.01060  0.00516  307 PHE A CB  
2350 C CG  . PHE A 313 ? 2.86293 3.01329 3.29501 -0.03699 0.02939  -0.00930 307 PHE A CG  
2351 C CD1 . PHE A 313 ? 2.93968 3.10301 3.35968 -0.02332 0.05338  -0.00829 307 PHE A CD1 
2352 C CD2 . PHE A 313 ? 2.64092 2.79323 3.07465 -0.03031 0.02088  -0.02312 307 PHE A CD2 
2353 C CE1 . PHE A 313 ? 2.68742 2.86316 3.10038 -0.00465 0.06698  -0.02048 307 PHE A CE1 
2354 C CE2 . PHE A 313 ? 2.45825 2.62461 2.88320 -0.01230 0.03629  -0.03325 307 PHE A CE2 
2355 C CZ  . PHE A 313 ? 2.47152 2.64870 2.88784 -0.00012 0.05864  -0.03169 307 PHE A CZ  
2356 N N   . THR A 314 ? 2.56125 2.59721 2.96739 -0.05654 -0.04864 -0.03654 308 THR A N   
2357 C CA  . THR A 314 ? 2.68550 2.69414 3.07318 -0.04486 -0.06610 -0.06270 308 THR A CA  
2358 C C   . THR A 314 ? 2.67790 2.70685 3.07521 -0.04809 -0.07177 -0.06423 308 THR A C   
2359 O O   . THR A 314 ? 2.72746 2.73534 3.10291 -0.03766 -0.08437 -0.08579 308 THR A O   
2360 C CB  . THR A 314 ? 3.05916 3.01459 3.43535 -0.05242 -0.09888 -0.06921 308 THR A CB  
2361 O OG1 . THR A 314 ? 3.02073 2.97425 3.41988 -0.08098 -0.11849 -0.04648 308 THR A OG1 
2362 C CG2 . THR A 314 ? 3.33663 3.26659 3.70013 -0.04605 -0.09748 -0.06926 308 THR A CG2 
2363 N N   . ILE A 315 ? 2.74922 2.81926 3.17737 -0.06057 -0.06316 -0.04253 309 ILE A N   
2364 C CA  . ILE A 315 ? 2.74942 2.83900 3.19041 -0.06355 -0.07315 -0.04247 309 ILE A CA  
2365 C C   . ILE A 315 ? 2.67468 2.77986 3.09726 -0.04130 -0.05361 -0.05594 309 ILE A C   
2366 O O   . ILE A 315 ? 2.64415 2.75660 3.05535 -0.02732 -0.02907 -0.05973 309 ILE A O   
2367 C CB  . ILE A 315 ? 2.40050 2.53478 2.88876 -0.08325 -0.07157 -0.01441 309 ILE A CB  
2368 C CG1 . ILE A 315 ? 2.17056 2.34637 2.67155 -0.07430 -0.03587 -0.00144 309 ILE A CG1 
2369 C CG2 . ILE A 315 ? 2.56545 2.68199 3.07213 -0.11100 -0.09398 0.00192  309 ILE A CG2 
2370 C CD1 . ILE A 315 ? 2.13156 2.36033 2.68099 -0.08974 -0.02797 0.02527  309 ILE A CD1 
2371 N N   . GLN A 316 ? 2.49265 2.59944 2.91027 -0.03955 -0.06748 -0.06224 310 GLN A N   
2372 C CA  . GLN A 316 ? 2.58319 2.70226 2.98207 -0.02214 -0.05227 -0.07045 310 GLN A CA  
2373 C C   . GLN A 316 ? 2.62794 2.79177 3.05828 -0.02000 -0.03358 -0.05210 310 GLN A C   
2374 O O   . GLN A 316 ? 2.58431 2.77502 3.04709 -0.02856 -0.04468 -0.03852 310 GLN A O   
2375 C CB  . GLN A 316 ? 2.67609 2.77824 3.05364 -0.02123 -0.07579 -0.08131 310 GLN A CB  
2376 C CG  . GLN A 316 ? 2.72458 2.78215 3.05857 -0.01445 -0.08807 -0.10566 310 GLN A CG  
2377 C CD  . GLN A 316 ? 3.06431 3.10307 3.36728 -0.01169 -0.11010 -0.11712 310 GLN A CD  
2378 O OE1 . GLN A 316 ? 3.25781 3.30250 3.57959 -0.02380 -0.13458 -0.10725 310 GLN A OE1 
2379 N NE2 . GLN A 316 ? 3.19028 3.20835 3.44537 0.00408  -0.10152 -0.13754 310 GLN A NE2 
2380 N N   . ASN A 317 ? 2.55099 2.72317 2.97318 -0.00732 -0.00681 -0.05282 311 ASN A N   
2381 C CA  . ASN A 317 ? 2.45196 2.66092 2.89774 -0.00056 0.01218  -0.03907 311 ASN A CA  
2382 C C   . ASN A 317 ? 2.52384 2.72494 2.94216 0.01738  0.03020  -0.04868 311 ASN A C   
2383 O O   . ASN A 317 ? 2.40452 2.58651 2.80125 0.02176  0.04093  -0.05821 311 ASN A O   
2384 C CB  . ASN A 317 ? 2.30237 2.52855 2.76985 -0.00797 0.02546  -0.02514 311 ASN A CB  
2385 C CG  . ASN A 317 ? 2.37788 2.64345 2.86639 0.00266  0.04706  -0.01349 311 ASN A CG  
2386 O OD1 . ASN A 317 ? 2.53133 2.81977 3.03572 0.01101  0.04530  -0.01084 311 ASN A OD1 
2387 N ND2 . ASN A 317 ? 2.41497 2.68632 2.90069 0.00458  0.06623  -0.00752 311 ASN A ND2 
2388 N N   . ASN A 318 ? 2.67880 2.89336 3.09976 0.02698  0.03086  -0.04544 312 ASN A N   
2389 C CA  . ASN A 318 ? 2.68060 2.88427 3.07642 0.04142  0.04458  -0.05129 312 ASN A CA  
2390 C C   . ASN A 318 ? 2.57697 2.80024 2.98744 0.05328  0.06274  -0.04406 312 ASN A C   
2391 O O   . ASN A 318 ? 2.44870 2.66058 2.84094 0.06546  0.07061  -0.04749 312 ASN A O   
2392 C CB  . ASN A 318 ? 2.85897 3.05487 3.23950 0.04603  0.03137  -0.05209 312 ASN A CB  
2393 C CG  . ASN A 318 ? 2.89274 3.06485 3.24693 0.03744  0.01471  -0.06197 312 ASN A CG  
2394 O OD1 . ASN A 318 ? 2.93047 3.08583 3.26887 0.03293  0.01792  -0.07282 312 ASN A OD1 
2395 N ND2 . ASN A 318 ? 2.77866 2.94783 3.12583 0.03744  -0.00458 -0.05952 312 ASN A ND2 
2396 N N   . THR A 319 ? 2.65050 2.90073 3.09031 0.04971  0.06934  -0.03402 313 THR A N   
2397 C CA  . THR A 319 ? 2.60167 2.87424 3.05309 0.06403  0.08775  -0.02826 313 THR A CA  
2398 C C   . THR A 319 ? 2.53311 2.77860 2.95172 0.07326  0.10170  -0.03789 313 THR A C   
2399 O O   . THR A 319 ? 2.67056 2.89699 3.07391 0.06475  0.10321  -0.04286 313 THR A O   
2400 C CB  . THR A 319 ? 2.47603 2.78374 2.96008 0.05516  0.09556  -0.01441 313 THR A CB  
2401 O OG1 . THR A 319 ? 2.58414 2.92050 3.10581 0.04400  0.08000  -0.00417 313 THR A OG1 
2402 C CG2 . THR A 319 ? 2.29396 2.62762 2.78514 0.07338  0.11792  -0.01029 313 THR A CG2 
2403 N N   . LYS A 320 ? 2.46727 2.70883 2.87602 0.09127  0.10867  -0.04093 314 LYS A N   
2404 C CA  . LYS A 320 ? 2.58962 2.80413 2.96893 0.10037  0.11849  -0.04975 314 LYS A CA  
2405 C C   . LYS A 320 ? 2.51418 2.74530 2.89858 0.12039  0.13178  -0.04773 314 LYS A C   
2406 O O   . LYS A 320 ? 2.44440 2.67272 2.82745 0.13740  0.12962  -0.04981 314 LYS A O   
2407 C CB  . LYS A 320 ? 2.52090 2.70336 2.87538 0.10167  0.11057  -0.05701 314 LYS A CB  
2408 C CG  . LYS A 320 ? 2.56566 2.73739 2.91275 0.08554  0.10026  -0.05981 314 LYS A CG  
2409 C CD  . LYS A 320 ? 2.75471 2.91962 3.09749 0.07442  0.10331  -0.06603 314 LYS A CD  
2410 C CE  . LYS A 320 ? 2.59424 2.74832 2.92646 0.06353  0.09497  -0.07259 314 LYS A CE  
2411 N NZ  . LYS A 320 ? 2.28517 2.45012 2.62806 0.05829  0.08179  -0.06812 314 LYS A NZ  
2412 N N   . LEU A 321 ? 2.43474 2.68085 2.82148 0.11977  0.14510  -0.04393 315 LEU A N   
2413 C CA  . LEU A 321 ? 2.36484 2.63423 2.75528 0.13946  0.16182  -0.04187 315 LEU A CA  
2414 C C   . LEU A 321 ? 2.56432 2.80622 2.91709 0.14656  0.17135  -0.04986 315 LEU A C   
2415 O O   . LEU A 321 ? 2.72326 2.94585 3.06104 0.13126  0.16802  -0.05039 315 LEU A O   
2416 C CB  . LEU A 321 ? 2.29571 2.61671 2.72361 0.13151  0.17174  -0.02624 315 LEU A CB  
2417 C CG  . LEU A 321 ? 2.48812 2.84573 2.92300 0.15042  0.19527  -0.02195 315 LEU A CG  
2418 C CD1 . LEU A 321 ? 2.37194 2.73842 2.81351 0.18057  0.19676  -0.03069 315 LEU A CD1 
2419 C CD2 . LEU A 321 ? 2.67602 3.08852 3.15332 0.13432  0.20482  -0.00237 315 LEU A CD2 
2420 N N   . LEU A 322 ? 2.66956 2.90733 3.00580 0.17171  0.18061  -0.05734 316 LEU A N   
2421 C CA  . LEU A 322 ? 2.68830 2.89816 2.98390 0.18200  0.18787  -0.06638 316 LEU A CA  
2422 C C   . LEU A 322 ? 2.72698 2.96140 3.01773 0.20984  0.20702  -0.06848 316 LEU A C   
2423 O O   . LEU A 322 ? 2.74413 2.98310 3.04332 0.23191  0.20586  -0.07481 316 LEU A O   
2424 C CB  . LEU A 322 ? 2.67716 2.83329 2.94236 0.18492  0.17189  -0.08061 316 LEU A CB  
2425 C CG  . LEU A 322 ? 2.61160 2.73244 2.83317 0.20217  0.17359  -0.09363 316 LEU A CG  
2426 C CD1 . LEU A 322 ? 2.46380 2.58150 2.66503 0.19238  0.17938  -0.09110 316 LEU A CD1 
2427 C CD2 . LEU A 322 ? 2.81086 2.88122 3.01227 0.20046  0.15403  -0.10486 316 LEU A CD2 
2428 N N   . ILE A 323 ? 2.75563 3.00512 3.03062 0.21021  0.22455  -0.06324 317 ILE A N   
2429 C CA  . ILE A 323 ? 2.89297 3.17068 3.15801 0.23738  0.24815  -0.06539 317 ILE A CA  
2430 C C   . ILE A 323 ? 2.91248 3.15103 3.11749 0.24621  0.25279  -0.07522 317 ILE A C   
2431 O O   . ILE A 323 ? 2.90043 3.12281 3.08770 0.22475  0.24900  -0.06809 317 ILE A O   
2432 C CB  . ILE A 323 ? 2.83571 3.18257 3.14190 0.22789  0.26986  -0.04474 317 ILE A CB  
2433 C CG1 . ILE A 323 ? 2.63646 3.01998 3.00314 0.21827  0.25987  -0.03571 317 ILE A CG1 
2434 C CG2 . ILE A 323 ? 2.36867 2.75191 2.66410 0.25789  0.29934  -0.04735 317 ILE A CG2 
2435 C CD1 . ILE A 323 ? 2.37834 2.83088 2.79423 0.20330  0.27625  -0.01364 317 ILE A CD1 
2436 N N   . VAL A 324 ? 2.90323 3.12279 3.07473 0.27920  0.25806  -0.09252 318 VAL A N   
2437 C CA  . VAL A 324 ? 2.98690 3.16077 3.09415 0.29141  0.25770  -0.10575 318 VAL A CA  
2438 C C   . VAL A 324 ? 3.11945 3.32218 3.20318 0.32464  0.28658  -0.11119 318 VAL A C   
2439 O O   . VAL A 324 ? 3.18809 3.40223 3.28142 0.35534  0.29177  -0.12327 318 VAL A O   
2440 C CB  . VAL A 324 ? 3.01875 3.12434 3.09597 0.29953  0.22958  -0.12618 318 VAL A CB  
2441 C CG1 . VAL A 324 ? 3.23506 3.29266 3.24464 0.31481  0.22632  -0.14164 318 VAL A CG1 
2442 C CG2 . VAL A 324 ? 2.69204 2.77617 2.79189 0.26640  0.20572  -0.12018 318 VAL A CG2 
2443 N N   . ASP A 325 ? 3.21261 3.42695 3.26397 0.31977  0.30539  -0.10215 319 ASP A N   
2444 C CA  . ASP A 325 ? 3.41811 3.65574 3.43214 0.35085  0.33599  -0.10777 319 ASP A CA  
2445 C C   . ASP A 325 ? 3.17943 3.49622 3.24711 0.36868  0.36475  -0.10055 319 ASP A C   
2446 O O   . ASP A 325 ? 2.71144 3.04936 2.75569 0.40557  0.38910  -0.11264 319 ASP A O   
2447 C CB  . ASP A 325 ? 3.46833 3.64184 3.41680 0.38571  0.32375  -0.13820 319 ASP A CB  
2448 C CG  . ASP A 325 ? 3.40007 3.50097 3.29394 0.36961  0.29637  -0.14516 319 ASP A CG  
2449 O OD1 . ASP A 325 ? 3.42809 3.53060 3.33336 0.33479  0.28932  -0.12693 319 ASP A OD1 
2450 O OD2 . ASP A 325 ? 3.17600 3.21691 3.01692 0.39244  0.27940  -0.16949 319 ASP A OD2 
2451 N N   . ASP A 326 ? 3.17373 3.53593 3.31367 0.34471  0.36144  -0.08224 320 ASP A N   
2452 C CA  . ASP A 326 ? 3.21106 3.65274 3.41438 0.35816  0.38305  -0.07394 320 ASP A CA  
2453 C C   . ASP A 326 ? 2.96530 3.39958 3.16723 0.40462  0.38059  -0.09954 320 ASP A C   
2454 O O   . ASP A 326 ? 2.75337 3.25317 2.99252 0.43068  0.40443  -0.09953 320 ASP A O   
2455 C CB  . ASP A 326 ? 3.13052 3.64185 3.33838 0.35668  0.42419  -0.05504 320 ASP A CB  
2456 C CG  . ASP A 326 ? 3.22250 3.74129 3.43736 0.30882  0.42401  -0.02608 320 ASP A CG  
2457 O OD1 . ASP A 326 ? 3.14536 3.61832 3.36449 0.28040  0.39231  -0.02332 320 ASP A OD1 
2458 O OD2 . ASP A 326 ? 3.19888 3.76875 3.41404 0.30000  0.45563  -0.00578 320 ASP A OD2 
2459 N N   . GLU A 327 ? 2.98591 3.34100 3.14742 0.41517  0.35063  -0.12098 321 GLU A N   
2460 C CA  . GLU A 327 ? 2.89873 3.22725 3.04892 0.45792  0.34078  -0.14622 321 GLU A CA  
2461 C C   . GLU A 327 ? 2.85432 3.13865 3.02691 0.44790  0.30327  -0.15000 321 GLU A C   
2462 O O   . GLU A 327 ? 2.74253 3.02457 2.93179 0.47803  0.29438  -0.16228 321 GLU A O   
2463 C CB  . GLU A 327 ? 3.01111 3.27420 3.07641 0.48590  0.33895  -0.17137 321 GLU A CB  
2464 C CG  . GLU A 327 ? 3.20562 3.44149 3.25071 0.53714  0.33279  -0.19985 321 GLU A CG  
2465 C CD  . GLU A 327 ? 3.44497 3.61674 3.40159 0.56528  0.33138  -0.22554 321 GLU A CD  
2466 O OE1 . GLU A 327 ? 3.22360 3.37894 3.13597 0.54526  0.33752  -0.21957 321 GLU A OE1 
2467 O OE2 . GLU A 327 ? 3.75200 3.88559 3.68074 0.60826  0.32127  -0.25227 321 GLU A OE2 
2468 N N   . TYR A 328 ? 2.73227 2.98251 2.90490 0.40745  0.28156  -0.13931 322 TYR A N   
2469 C CA  . TYR A 328 ? 2.80464 3.01543 2.99432 0.39312  0.24921  -0.13981 322 TYR A CA  
2470 C C   . TYR A 328 ? 2.77065 3.01337 3.00694 0.35145  0.24476  -0.11697 322 TYR A C   
2471 O O   . TYR A 328 ? 2.59259 2.84403 2.82315 0.32476  0.25238  -0.10553 322 TYR A O   
2472 C CB  . TYR A 328 ? 3.05010 3.17478 3.18398 0.38793  0.22339  -0.15456 322 TYR A CB  
2473 C CG  . TYR A 328 ? 3.14967 3.23776 3.29912 0.36219  0.19397  -0.14945 322 TYR A CG  
2474 C CD1 . TYR A 328 ? 3.15925 3.22311 3.31760 0.37804  0.17545  -0.15535 322 TYR A CD1 
2475 C CD2 . TYR A 328 ? 3.00242 3.07960 3.15524 0.32324  0.18497  -0.13856 322 TYR A CD2 
2476 C CE1 . TYR A 328 ? 3.17984 3.21065 3.34675 0.35283  0.15099  -0.14820 322 TYR A CE1 
2477 C CE2 . TYR A 328 ? 3.01146 3.06079 3.17656 0.30070  0.16249  -0.13390 322 TYR A CE2 
2478 C CZ  . TYR A 328 ? 3.11283 3.13937 3.28310 0.31416  0.14665  -0.13764 322 TYR A CZ  
2479 O OH  . TYR A 328 ? 3.14770 3.14691 3.32483 0.29009  0.12657  -0.13057 322 TYR A OH  
2480 N N   . VAL A 329 ? 2.91728 3.17261 3.19564 0.34738  0.22995  -0.11114 323 VAL A N   
2481 C CA  . VAL A 329 ? 2.73204 3.01159 3.05079 0.31127  0.22164  -0.09262 323 VAL A CA  
2482 C C   . VAL A 329 ? 2.70115 2.92760 3.01050 0.29817  0.19215  -0.09577 323 VAL A C   
2483 O O   . VAL A 329 ? 2.76420 2.95403 3.05764 0.31927  0.17783  -0.10689 323 VAL A O   
2484 C CB  . VAL A 329 ? 2.44233 2.79690 2.82417 0.31492  0.23206  -0.07921 323 VAL A CB  
2485 C CG1 . VAL A 329 ? 2.31033 2.66433 2.71126 0.34458  0.21850  -0.08767 323 VAL A CG1 
2486 C CG2 . VAL A 329 ? 2.43008 2.80614 2.84711 0.27576  0.22285  -0.06079 323 VAL A CG2 
2487 N N   . HIS A 330 ? 2.70314 2.92372 3.01985 0.26335  0.18318  -0.08564 324 HIS A N   
2488 C CA  . HIS A 330 ? 2.82260 2.99918 3.12880 0.24692  0.15991  -0.08655 324 HIS A CA  
2489 C C   . HIS A 330 ? 2.68023 2.88418 3.01941 0.21938  0.15407  -0.07278 324 HIS A C   
2490 O O   . HIS A 330 ? 2.48879 2.70001 2.82952 0.19672  0.15835  -0.06759 324 HIS A O   
2491 C CB  . HIS A 330 ? 2.92601 3.05092 3.19092 0.23499  0.15345  -0.09499 324 HIS A CB  
2492 C CG  . HIS A 330 ? 2.77365 2.86282 3.03160 0.21431  0.13444  -0.09354 324 HIS A CG  
2493 N ND1 . HIS A 330 ? 2.93148 2.97815 3.17103 0.22267  0.11846  -0.09827 324 HIS A ND1 
2494 C CD2 . HIS A 330 ? 2.40284 2.49313 2.66840 0.18597  0.12991  -0.08744 324 HIS A CD2 
2495 C CE1 . HIS A 330 ? 2.67813 2.70506 2.91454 0.19783  0.10734  -0.09295 324 HIS A CE1 
2496 N NE2 . HIS A 330 ? 2.64900 2.70381 2.90139 0.17720  0.11501  -0.08785 324 HIS A NE2 
2497 N N   . ILE A 331 ? 2.64746 2.86187 3.00961 0.22271  0.14144  -0.06782 325 ILE A N   
2498 C CA  . ILE A 331 ? 2.53923 2.77054 2.92524 0.19892  0.13063  -0.05720 325 ILE A CA  
2499 C C   . ILE A 331 ? 2.66110 2.84628 3.02189 0.19054  0.11138  -0.05902 325 ILE A C   
2500 O O   . ILE A 331 ? 2.84047 2.99816 3.18657 0.20786  0.10145  -0.06264 325 ILE A O   
2501 C CB  . ILE A 331 ? 2.49508 2.77987 2.92908 0.20717  0.12929  -0.04802 325 ILE A CB  
2502 C CG1 . ILE A 331 ? 2.42797 2.76473 2.88874 0.21391  0.15259  -0.04354 325 ILE A CG1 
2503 C CG2 . ILE A 331 ? 2.51844 2.81345 2.97144 0.18186  0.11360  -0.03868 325 ILE A CG2 
2504 C CD1 . ILE A 331 ? 2.37843 2.77857 2.89690 0.21858  0.15281  -0.03256 325 ILE A CD1 
2505 N N   . THR A 332 ? 2.65601 2.83153 3.00980 0.16464  0.10628  -0.05624 326 THR A N   
2506 C CA  . THR A 332 ? 2.83531 2.97268 3.16294 0.15350  0.09268  -0.05621 326 THR A CA  
2507 C C   . THR A 332 ? 2.76922 2.91860 3.10375 0.13160  0.08669  -0.05173 326 THR A C   
2508 O O   . THR A 332 ? 2.68854 2.87122 3.04993 0.12555  0.08880  -0.04837 326 THR A O   
2509 C CB  . THR A 332 ? 2.70961 2.80811 3.00565 0.14782  0.09644  -0.06353 326 THR A CB  
2510 O OG1 . THR A 332 ? 2.44913 2.51808 2.72326 0.13287  0.08662  -0.06047 326 THR A OG1 
2511 C CG2 . THR A 332 ? 2.69823 2.80863 2.99768 0.13504  0.10804  -0.06768 326 THR A CG2 
2512 N N   . SER A 333 ? 2.66404 2.78448 2.97193 0.11936  0.07881  -0.05146 327 SER A N   
2513 C CA  . SER A 333 ? 2.74404 2.86888 3.04771 0.10118  0.07410  -0.05100 327 SER A CA  
2514 C C   . SER A 333 ? 2.79477 2.90664 3.08162 0.08663  0.08381  -0.05821 327 SER A C   
2515 O O   . SER A 333 ? 2.87139 2.99272 3.16062 0.07560  0.08352  -0.06202 327 SER A O   
2516 C CB  . SER A 333 ? 3.03680 3.14409 3.32005 0.09932  0.05838  -0.04476 327 SER A CB  
2517 O OG  . SER A 333 ? 2.97917 3.05067 3.23096 0.09848  0.05845  -0.04256 327 SER A OG  
2518 N N   . ALA A 334 ? 2.71725 2.80767 2.98926 0.08722  0.09027  -0.06098 328 ALA A N   
2519 C CA  . ALA A 334 ? 2.77917 2.86382 3.04373 0.07434  0.09871  -0.06777 328 ALA A CA  
2520 C C   . ALA A 334 ? 2.79806 2.89622 3.07967 0.07707  0.10571  -0.07431 328 ALA A C   
2521 O O   . ALA A 334 ? 2.76540 2.87074 3.05668 0.08918  0.10761  -0.07293 328 ALA A O   
2522 C CB  . ALA A 334 ? 2.85566 2.91181 3.10064 0.07004  0.09924  -0.06612 328 ALA A CB  
2523 N N   . ASN A 335 ? 2.97089 3.07286 3.25449 0.06689  0.10973  -0.08135 329 ASN A N   
2524 C CA  . ASN A 335 ? 3.09069 3.19983 3.38601 0.06807  0.11291  -0.08680 329 ASN A CA  
2525 C C   . ASN A 335 ? 3.07122 3.16442 3.35973 0.06841  0.11507  -0.09185 329 ASN A C   
2526 O O   . ASN A 335 ? 2.99995 3.08193 3.28100 0.06117  0.11507  -0.09284 329 ASN A O   
2527 C CB  . ASN A 335 ? 3.21780 3.33691 3.52068 0.05996  0.11130  -0.09319 329 ASN A CB  
2528 C CG  . ASN A 335 ? 3.34627 3.46618 3.65811 0.06078  0.11100  -0.09784 329 ASN A CG  
2529 O OD1 . ASN A 335 ? 3.28053 3.40626 3.59929 0.06317  0.10964  -0.09227 329 ASN A OD1 
2530 N ND2 . ASN A 335 ? 3.55626 3.67170 3.86898 0.05804  0.11169  -0.10674 329 ASN A ND2 
2531 N N   . PHE A 336 ? 2.98357 3.07536 3.27348 0.07535  0.11592  -0.09387 330 PHE A N   
2532 C CA  . PHE A 336 ? 2.96107 3.03475 3.24226 0.07656  0.11359  -0.09995 330 PHE A CA  
2533 C C   . PHE A 336 ? 3.06372 3.14213 3.35615 0.06521  0.11113  -0.10711 330 PHE A C   
2534 O O   . PHE A 336 ? 3.18712 3.27356 3.48824 0.06503  0.10909  -0.11101 330 PHE A O   
2535 C CB  . PHE A 336 ? 2.88705 2.95807 3.16052 0.08739  0.11501  -0.10019 330 PHE A CB  
2536 C CG  . PHE A 336 ? 2.91721 2.98867 3.18158 0.10249  0.12040  -0.09547 330 PHE A CG  
2537 C CD1 . PHE A 336 ? 2.96042 3.02071 3.21905 0.10834  0.11813  -0.09422 330 PHE A CD1 
2538 C CD2 . PHE A 336 ? 3.09848 3.18236 3.35998 0.11164  0.12797  -0.09174 330 PHE A CD2 
2539 C CE1 . PHE A 336 ? 3.00499 3.06760 3.25859 0.12675  0.12206  -0.09213 330 PHE A CE1 
2540 C CE2 . PHE A 336 ? 3.06199 3.15442 3.31945 0.12842  0.13594  -0.08870 330 PHE A CE2 
2541 C CZ  . PHE A 336 ? 2.94862 3.03093 3.20382 0.13787  0.13236  -0.09031 330 PHE A CZ  
2542 N N   . ASP A 337 ? 2.97514 3.04948 3.26887 0.05581  0.11100  -0.10813 331 ASP A N   
2543 C CA  . ASP A 337 ? 2.85152 2.93851 3.16237 0.04593  0.11101  -0.11518 331 ASP A CA  
2544 C C   . ASP A 337 ? 2.89278 2.97217 3.20331 0.03365  0.11116  -0.11166 331 ASP A C   
2545 O O   . ASP A 337 ? 2.94872 3.00478 3.24175 0.03405  0.10785  -0.10468 331 ASP A O   
2546 C CB  . ASP A 337 ? 2.78887 2.89873 3.10984 0.04393  0.11684  -0.11879 331 ASP A CB  
2547 C CG  . ASP A 337 ? 2.82067 2.93305 3.12888 0.03992  0.12298  -0.11187 331 ASP A CG  
2548 O OD1 . ASP A 337 ? 2.61944 2.73418 2.92439 0.02969  0.12867  -0.10869 331 ASP A OD1 
2549 O OD2 . ASP A 337 ? 3.01522 3.12727 3.31652 0.04567  0.12099  -0.10827 331 ASP A OD2 
2550 N N   . GLY A 338 ? 2.66216 2.76182 2.99378 0.02265  0.11448  -0.11599 332 GLY A N   
2551 C CA  . GLY A 338 ? 2.74365 2.84148 3.08111 0.00594  0.11520  -0.11014 332 GLY A CA  
2552 C C   . GLY A 338 ? 2.76531 2.86814 3.08992 -0.00457 0.12672  -0.09952 332 GLY A C   
2553 O O   . GLY A 338 ? 2.64094 2.72140 2.95173 -0.01555 0.12340  -0.08825 332 GLY A O   
2554 N N   . THR A 339 ? 2.68508 2.81199 3.00943 -0.00107 0.13805  -0.10295 333 THR A N   
2555 C CA  . THR A 339 ? 2.72322 2.85469 3.02868 -0.01073 0.14911  -0.09337 333 THR A CA  
2556 C C   . THR A 339 ? 2.78553 2.88332 3.05984 -0.00700 0.14101  -0.08166 333 THR A C   
2557 O O   . THR A 339 ? 2.89462 2.97873 3.14885 -0.01900 0.14296  -0.06836 333 THR A O   
2558 C CB  . THR A 339 ? 2.74251 2.90114 3.04777 -0.00362 0.15976  -0.10318 333 THR A CB  
2559 O OG1 . THR A 339 ? 2.59986 2.79023 2.93716 -0.00262 0.16584  -0.11613 333 THR A OG1 
2560 C CG2 . THR A 339 ? 3.23480 3.39791 3.51345 -0.01353 0.17208  -0.09401 333 THR A CG2 
2561 N N   . HIS A 340 ? 2.73361 2.81878 3.00455 0.00960  0.13160  -0.08536 334 HIS A N   
2562 C CA  . HIS A 340 ? 2.92665 2.98810 3.17539 0.01740  0.12382  -0.07620 334 HIS A CA  
2563 C C   . HIS A 340 ? 2.86137 2.88841 3.09921 0.01608  0.11395  -0.06893 334 HIS A C   
2564 O O   . HIS A 340 ? 3.01556 3.01975 3.23215 0.01074  0.10927  -0.05705 334 HIS A O   
2565 C CB  . HIS A 340 ? 2.85841 2.92642 3.11383 0.03467  0.11935  -0.08167 334 HIS A CB  
2566 C CG  . HIS A 340 ? 2.89037 2.97934 3.14800 0.03573  0.12239  -0.08573 334 HIS A CG  
2567 N ND1 . HIS A 340 ? 3.03376 3.12258 3.28453 0.04277  0.11575  -0.08120 334 HIS A ND1 
2568 C CD2 . HIS A 340 ? 2.85376 2.96236 3.11973 0.03179  0.12878  -0.09523 334 HIS A CD2 
2569 C CE1 . HIS A 340 ? 3.06485 3.16809 3.31665 0.04116  0.11629  -0.08749 334 HIS A CE1 
2570 N NE2 . HIS A 340 ? 2.99174 3.10570 3.25081 0.03607  0.12470  -0.09692 334 HIS A NE2 
2571 N N   . TYR A 341 ? 2.61244 2.62999 2.86017 0.02157  0.10811  -0.07623 335 TYR A N   
2572 C CA  . TYR A 341 ? 2.87290 2.85090 3.10566 0.02516  0.09521  -0.07323 335 TYR A CA  
2573 C C   . TYR A 341 ? 2.94113 2.90120 3.17285 0.00253  0.09042  -0.06583 335 TYR A C   
2574 O O   . TYR A 341 ? 2.90851 2.82744 3.12489 0.00316  0.07574  -0.06312 335 TYR A O   
2575 C CB  . TYR A 341 ? 2.79689 2.76783 3.03268 0.04143  0.08974  -0.08501 335 TYR A CB  
2576 C CG  . TYR A 341 ? 2.82609 2.79983 3.05484 0.06477  0.09121  -0.08704 335 TYR A CG  
2577 C CD1 . TYR A 341 ? 2.78471 2.79248 3.02780 0.06971  0.10054  -0.08858 335 TYR A CD1 
2578 C CD2 . TYR A 341 ? 3.00812 2.95147 3.21809 0.08196  0.08261  -0.08737 335 TYR A CD2 
2579 C CE1 . TYR A 341 ? 3.11248 3.12981 3.35603 0.08758  0.10280  -0.08790 335 TYR A CE1 
2580 C CE2 . TYR A 341 ? 3.03908 2.99470 3.24936 0.10423  0.08670  -0.08904 335 TYR A CE2 
2581 C CZ  . TYR A 341 ? 3.18102 3.17663 3.41045 0.10517  0.09757  -0.08802 335 TYR A CZ  
2582 O OH  . TYR A 341 ? 3.31799 3.33240 3.55429 0.12403  0.10247  -0.08728 335 TYR A OH  
2583 N N   . GLN A 342 ? 2.81393 2.80379 3.06211 -0.01726 0.10202  -0.06254 336 GLN A N   
2584 C CA  . GLN A 342 ? 2.86768 2.84914 3.12046 -0.04335 0.10024  -0.05177 336 GLN A CA  
2585 C C   . GLN A 342 ? 2.92958 2.90758 3.16157 -0.05937 0.10814  -0.03395 336 GLN A C   
2586 O O   . GLN A 342 ? 2.95521 2.90404 3.17594 -0.07894 0.10027  -0.01914 336 GLN A O   
2587 C CB  . GLN A 342 ? 2.67171 2.69539 2.96253 -0.05617 0.10927  -0.05898 336 GLN A CB  
2588 C CG  . GLN A 342 ? 2.69489 2.71293 3.00355 -0.04713 0.09560  -0.07308 336 GLN A CG  
2589 C CD  . GLN A 342 ? 2.89271 2.87068 3.19780 -0.06018 0.07538  -0.06855 336 GLN A CD  
2590 O OE1 . GLN A 342 ? 2.95931 2.88888 3.23401 -0.04934 0.06061  -0.06783 336 GLN A OE1 
2591 N NE2 . GLN A 342 ? 2.68966 2.68794 3.02766 -0.08285 0.07317  -0.06634 336 GLN A NE2 
2592 N N   . ASN A 343 ? 2.95673 2.95909 3.17948 -0.05253 0.12123  -0.03426 337 ASN A N   
2593 C CA  . ASN A 343 ? 3.09196 3.09337 3.28890 -0.06781 0.13013  -0.01786 337 ASN A CA  
2594 C C   . ASN A 343 ? 3.04033 3.02263 3.20528 -0.05142 0.12328  -0.01418 337 ASN A C   
2595 O O   . ASN A 343 ? 3.02038 2.97200 3.15308 -0.06020 0.11675  0.00293  337 ASN A O   
2596 C CB  . ASN A 343 ? 2.96005 3.01409 3.17291 -0.07866 0.15414  -0.02182 337 ASN A CB  
2597 C CG  . ASN A 343 ? 2.86520 2.94873 3.12019 -0.09227 0.16030  -0.02725 337 ASN A CG  
2598 O OD1 . ASN A 343 ? 2.67096 2.77274 2.95493 -0.07864 0.15750  -0.04462 337 ASN A OD1 
2599 N ND2 . ASN A 343 ? 2.92577 3.01450 3.18538 -0.12057 0.16735  -0.01089 337 ASN A ND2 
2600 N N   . HIS A 344 ? 3.01500 3.01378 3.18906 -0.02925 0.12245  -0.02835 338 HIS A N   
2601 C CA  . HIS A 344 ? 2.92515 2.91487 3.07687 -0.01543 0.11505  -0.02532 338 HIS A CA  
2602 C C   . HIS A 344 ? 2.89584 2.84276 3.03218 -0.00406 0.09508  -0.01703 338 HIS A C   
2603 O O   . HIS A 344 ? 2.85576 2.78479 3.00348 0.00401  0.08681  -0.02181 338 HIS A O   
2604 C CB  . HIS A 344 ? 3.10238 3.12095 3.27426 0.00222  0.11699  -0.04113 338 HIS A CB  
2605 C CG  . HIS A 344 ? 3.08564 3.13948 3.26616 -0.00370 0.13245  -0.05102 338 HIS A CG  
2606 N ND1 . HIS A 344 ? 2.96551 3.03089 3.13191 -0.02041 0.14676  -0.04585 338 HIS A ND1 
2607 C CD2 . HIS A 344 ? 3.34170 3.42056 3.54238 0.00614  0.13557  -0.06609 338 HIS A CD2 
2608 C CE1 . HIS A 344 ? 3.19731 3.29504 3.37553 -0.01708 0.15859  -0.06008 338 HIS A CE1 
2609 N NE2 . HIS A 344 ? 3.48559 3.58819 3.68393 -0.00134 0.14996  -0.07245 338 HIS A NE2 
2610 N N   . GLY A 345 ? 2.99418 2.92292 3.10206 -0.00124 0.08576  -0.00581 339 GLY A N   
2611 C CA  . GLY A 345 ? 3.08192 2.97016 3.17500 0.01312  0.06448  0.00177  339 GLY A CA  
2612 C C   . GLY A 345 ? 3.08754 2.99203 3.19434 0.03862  0.05593  -0.00613 339 GLY A C   
2613 O O   . GLY A 345 ? 3.07420 3.00028 3.17731 0.03883  0.05728  -0.00645 339 GLY A O   
2614 N N   . PHE A 346 ? 3.08587 2.98071 3.20875 0.06021  0.04671  -0.01281 340 PHE A N   
2615 C CA  . PHE A 346 ? 2.99871 2.91806 3.14438 0.08429  0.04135  -0.01967 340 PHE A CA  
2616 C C   . PHE A 346 ? 2.80904 2.70634 2.96063 0.10905  0.03041  -0.02389 340 PHE A C   
2617 O O   . PHE A 346 ? 2.94079 2.80191 3.07817 0.10735  0.02651  -0.02455 340 PHE A O   
2618 C CB  . PHE A 346 ? 2.97641 2.94263 3.15295 0.08399  0.05725  -0.03194 340 PHE A CB  
2619 C CG  . PHE A 346 ? 2.87815 2.84702 3.06604 0.08045  0.06916  -0.04156 340 PHE A CG  
2620 C CD1 . PHE A 346 ? 2.66346 2.63405 2.84658 0.05896  0.07949  -0.04237 340 PHE A CD1 
2621 C CD2 . PHE A 346 ? 2.92694 2.89862 3.12988 0.09968  0.06978  -0.05009 340 PHE A CD2 
2622 C CE1 . PHE A 346 ? 2.64141 2.61420 2.83707 0.05605  0.08611  -0.05122 340 PHE A CE1 
2623 C CE2 . PHE A 346 ? 2.94875 2.91821 3.15593 0.09679  0.07741  -0.05901 340 PHE A CE2 
2624 C CZ  . PHE A 346 ? 2.79621 2.76515 3.00101 0.07462  0.08353  -0.05945 340 PHE A CZ  
2625 N N   . VAL A 347 ? 2.43120 2.35169 2.60508 0.13269  0.02474  -0.02746 341 VAL A N   
2626 C CA  . VAL A 347 ? 2.78426 2.69628 2.96908 0.16256  0.01840  -0.03492 341 VAL A CA  
2627 C C   . VAL A 347 ? 2.76964 2.73490 2.99212 0.17541  0.03470  -0.04545 341 VAL A C   
2628 O O   . VAL A 347 ? 2.42545 2.43225 2.67121 0.16880  0.03957  -0.04295 341 VAL A O   
2629 C CB  . VAL A 347 ? 2.86806 2.76063 3.04773 0.18277  -0.00460 -0.02765 341 VAL A CB  
2630 C CG1 . VAL A 347 ? 2.81461 2.74803 3.01594 0.18210  -0.00910 -0.02193 341 VAL A CG1 
2631 C CG2 . VAL A 347 ? 2.85022 2.73749 3.04316 0.21884  -0.00945 -0.03866 341 VAL A CG2 
2632 N N   . SER A 348 ? 2.96002 2.92085 3.18477 0.19229  0.04222  -0.05658 342 SER A N   
2633 C CA  . SER A 348 ? 2.94962 2.95704 3.20244 0.20250  0.06043  -0.06463 342 SER A CA  
2634 C C   . SER A 348 ? 2.63810 2.65986 2.90671 0.23849  0.06025  -0.07104 342 SER A C   
2635 O O   . SER A 348 ? 2.56415 2.54582 2.81334 0.25897  0.04689  -0.07563 342 SER A O   
2636 C CB  . SER A 348 ? 2.95429 2.95007 3.19296 0.19264  0.07259  -0.07323 342 SER A CB  
2637 O OG  . SER A 348 ? 3.07368 3.06469 3.30521 0.16221  0.07435  -0.06877 342 SER A OG  
2638 N N   . PHE A 349 ? 2.56650 2.64636 2.87143 0.24616  0.07512  -0.07114 343 PHE A N   
2639 C CA  . PHE A 349 ? 2.60673 2.71727 2.93527 0.28063  0.08135  -0.07706 343 PHE A CA  
2640 C C   . PHE A 349 ? 2.67453 2.78706 2.98898 0.29374  0.10141  -0.08913 343 PHE A C   
2641 O O   . PHE A 349 ? 2.66103 2.79472 2.97776 0.27545  0.11734  -0.08730 343 PHE A O   
2642 C CB  . PHE A 349 ? 2.75240 2.93130 3.13296 0.27919  0.08667  -0.06759 343 PHE A CB  
2643 C CG  . PHE A 349 ? 2.75122 2.97807 3.16628 0.31306  0.09861  -0.07239 343 PHE A CG  
2644 C CD1 . PHE A 349 ? 2.77598 3.00083 3.20444 0.34390  0.08299  -0.07550 343 PHE A CD1 
2645 C CD2 . PHE A 349 ? 2.87449 3.15011 3.30867 0.31480  0.12582  -0.07311 343 PHE A CD2 
2646 C CE1 . PHE A 349 ? 2.87039 3.14686 3.33569 0.37839  0.09606  -0.08150 343 PHE A CE1 
2647 C CE2 . PHE A 349 ? 2.97119 3.29877 3.43846 0.34618  0.14134  -0.07688 343 PHE A CE2 
2648 C CZ  . PHE A 349 ? 2.86198 3.19309 3.34748 0.37926  0.12733  -0.08218 343 PHE A CZ  
2649 N N   . ASN A 350 ? 2.74685 2.83291 3.04250 0.32678  0.09849  -0.10204 344 ASN A N   
2650 C CA  . ASN A 350 ? 2.88487 2.96588 3.15745 0.34475  0.11532  -0.11617 344 ASN A CA  
2651 C C   . ASN A 350 ? 2.88184 2.99598 3.17250 0.38847  0.12542  -0.12586 344 ASN A C   
2652 O O   . ASN A 350 ? 2.74016 2.83367 3.03313 0.41368  0.10778  -0.13067 344 ASN A O   
2653 C CB  . ASN A 350 ? 2.91378 2.91656 3.13361 0.34296  0.09960  -0.12717 344 ASN A CB  
2654 C CG  . ASN A 350 ? 2.84634 2.82192 3.05487 0.30125  0.08964  -0.11726 344 ASN A CG  
2655 O OD1 . ASN A 350 ? 3.05888 3.03562 3.25722 0.28233  0.09890  -0.11847 344 ASN A OD1 
2656 N ND2 . ASN A 350 ? 2.71946 2.67173 2.92912 0.28789  0.07083  -0.10723 344 ASN A ND2 
2657 N N   . SER A 351 ? 2.86872 3.03480 3.17182 0.39814  0.15391  -0.12816 345 SER A N   
2658 C CA  . SER A 351 ? 2.74950 2.96132 3.07480 0.44024  0.17027  -0.13713 345 SER A CA  
2659 C C   . SER A 351 ? 2.76466 2.99303 3.06339 0.45283  0.19962  -0.14652 345 SER A C   
2660 O O   . SER A 351 ? 2.58281 2.82144 2.87251 0.42296  0.21239  -0.13728 345 SER A O   
2661 C CB  . SER A 351 ? 2.79761 3.09171 3.19337 0.43697  0.17806  -0.12131 345 SER A CB  
2662 O OG  . SER A 351 ? 2.85465 3.20196 3.27957 0.47923  0.19563  -0.13001 345 SER A OG  
2663 N N   . ILE A 352 ? 2.93991 3.16800 3.22253 0.49909  0.20911  -0.16552 346 ILE A N   
2664 C CA  . ILE A 352 ? 3.05688 3.30365 3.30877 0.51861  0.23934  -0.17629 346 ILE A CA  
2665 C C   . ILE A 352 ? 3.06526 3.40109 3.36286 0.55171  0.27069  -0.17648 346 ILE A C   
2666 O O   . ILE A 352 ? 3.03492 3.39102 3.30522 0.57749  0.29902  -0.18777 346 ILE A O   
2667 C CB  . ILE A 352 ? 3.22492 3.38669 3.40320 0.54610  0.22548  -0.20276 346 ILE A CB  
2668 C CG1 . ILE A 352 ? 3.50641 3.63901 3.68575 0.59052  0.20609  -0.22065 346 ILE A CG1 
2669 C CG2 . ILE A 352 ? 2.93617 3.02144 3.07530 0.50823  0.19842  -0.19999 346 ILE A CG2 
2670 C CD1 . ILE A 352 ? 3.68920 3.73169 3.79541 0.61960  0.18803  -0.24823 346 ILE A CD1 
2671 N N   . ASP A 353 ? 2.96729 3.35899 3.33421 0.55170  0.26610  -0.16406 347 ASP A N   
2672 C CA  . ASP A 353 ? 2.96233 3.45042 3.38703 0.58034  0.29509  -0.16186 347 ASP A CA  
2673 C C   . ASP A 353 ? 3.02281 3.58152 3.46590 0.55249  0.33204  -0.14242 347 ASP A C   
2674 O O   . ASP A 353 ? 3.00572 3.57876 3.47370 0.50492  0.32662  -0.11944 347 ASP A O   
2675 C CB  . ASP A 353 ? 2.68596 3.21432 3.18379 0.58025  0.27482  -0.15068 347 ASP A CB  
2676 C CG  . ASP A 353 ? 2.75714 3.39268 3.32662 0.61034  0.30211  -0.14815 347 ASP A CG  
2677 O OD1 . ASP A 353 ? 2.69802 3.34195 3.26014 0.66411  0.31276  -0.17047 347 ASP A OD1 
2678 O OD2 . ASP A 353 ? 2.74613 3.45830 3.38112 0.58062  0.31204  -0.12431 347 ASP A OD2 
2679 N N   . LYS A 354 ? 3.05044 3.65023 3.47745 0.58271  0.36913  -0.15162 348 LYS A N   
2680 C CA  . LYS A 354 ? 3.05570 3.71503 3.48815 0.55611  0.40570  -0.13162 348 LYS A CA  
2681 C C   . LYS A 354 ? 3.12723 3.87983 3.65118 0.52578  0.41452  -0.10216 348 LYS A C   
2682 O O   . LYS A 354 ? 2.96387 3.73467 3.49653 0.47968  0.42196  -0.07788 348 LYS A O   
2683 C CB  . LYS A 354 ? 3.26899 3.96251 3.66826 0.59919  0.44646  -0.14702 348 LYS A CB  
2684 C CG  . LYS A 354 ? 3.09402 3.69583 3.39020 0.61512  0.44205  -0.17038 348 LYS A CG  
2685 C CD  . LYS A 354 ? 2.87420 3.44334 3.12880 0.56573  0.44213  -0.15241 348 LYS A CD  
2686 C CE  . LYS A 354 ? 2.93726 3.42413 3.09126 0.58284  0.43892  -0.17502 348 LYS A CE  
2687 N NZ  . LYS A 354 ? 2.76179 3.22153 2.87709 0.53806  0.43879  -0.15726 348 LYS A NZ  
2688 N N   . GLN A 355 ? 3.19800 4.00778 3.79150 0.55107  0.41047  -0.10398 349 GLN A N   
2689 C CA  . GLN A 355 ? 2.99046 3.89003 3.67600 0.52220  0.41429  -0.07653 349 GLN A CA  
2690 C C   . GLN A 355 ? 2.94373 3.79910 3.64036 0.47334  0.37520  -0.06080 349 GLN A C   
2691 O O   . GLN A 355 ? 2.91980 3.82137 3.66184 0.43094  0.37787  -0.03485 349 GLN A O   
2692 C CB  . GLN A 355 ? 2.75512 3.72568 3.51406 0.56468  0.41528  -0.08439 349 GLN A CB  
2693 C CG  . GLN A 355 ? 2.91077 3.95320 3.67747 0.61186  0.46145  -0.09648 349 GLN A CG  
2694 C CD  . GLN A 355 ? 3.45997 4.57798 4.30757 0.65667  0.46077  -0.10534 349 GLN A CD  
2695 O OE1 . GLN A 355 ? 3.79122 4.88222 4.66882 0.66246  0.41944  -0.10936 349 GLN A OE1 
2696 N NE2 . GLN A 355 ? 3.66629 4.88143 4.54946 0.68950  0.50679  -0.10802 349 GLN A NE2 
2697 N N   . LEU A 356 ? 2.98141 3.74646 3.63532 0.47825  0.33858  -0.07597 350 LEU A N   
2698 C CA  . LEU A 356 ? 2.85043 3.57151 3.50657 0.43499  0.30414  -0.06329 350 LEU A CA  
2699 C C   . LEU A 356 ? 2.85527 3.53162 3.46082 0.39463  0.30804  -0.05474 350 LEU A C   
2700 O O   . LEU A 356 ? 2.81852 3.49621 3.44431 0.35259  0.29439  -0.03702 350 LEU A O   
2701 C CB  . LEU A 356 ? 2.85282 3.49623 3.47971 0.45245  0.26634  -0.07969 350 LEU A CB  
2702 C CG  . LEU A 356 ? 2.96284 3.56664 3.59410 0.41438  0.23082  -0.06795 350 LEU A CG  
2703 C CD1 . LEU A 356 ? 2.70377 3.38244 3.41452 0.39559  0.22444  -0.04820 350 LEU A CD1 
2704 C CD2 . LEU A 356 ? 2.90377 3.43258 3.50120 0.43376  0.19751  -0.08215 350 LEU A CD2 
2705 N N   . VAL A 357 ? 2.87228 3.50671 3.41119 0.40833  0.32392  -0.06823 351 VAL A N   
2706 C CA  . VAL A 357 ? 2.82327 3.41948 3.31641 0.37315  0.32725  -0.06008 351 VAL A CA  
2707 C C   . VAL A 357 ? 2.81916 3.48659 3.34560 0.34716  0.35557  -0.03558 351 VAL A C   
2708 O O   . VAL A 357 ? 2.82758 3.47911 3.34767 0.30631  0.34864  -0.01970 351 VAL A O   
2709 C CB  . VAL A 357 ? 2.80491 3.33544 3.21709 0.39600  0.33243  -0.08157 351 VAL A CB  
2710 C CG1 . VAL A 357 ? 2.95142 3.44752 3.31916 0.36218  0.33511  -0.07273 351 VAL A CG1 
2711 C CG2 . VAL A 357 ? 2.66786 3.12132 3.04865 0.41304  0.29980  -0.10194 351 VAL A CG2 
2712 N N   . SER A 358 ? 2.74036 3.48776 3.30418 0.36996  0.38740  -0.03136 352 SER A N   
2713 C CA  . SER A 358 ? 2.69876 3.51977 3.29891 0.34206  0.41595  -0.00404 352 SER A CA  
2714 C C   . SER A 358 ? 2.70606 3.55758 3.37356 0.29963  0.39449  0.01946  352 SER A C   
2715 O O   . SER A 358 ? 2.53302 3.39381 3.20565 0.25838  0.39831  0.04232  352 SER A O   
2716 C CB  . SER A 358 ? 2.82953 3.74011 3.46488 0.37691  0.45597  -0.00435 352 SER A CB  
2717 O OG  . SER A 358 ? 2.85249 3.81163 3.55831 0.40066  0.44505  -0.00988 352 SER A OG  
2718 N N   . GLU A 359 ? 2.75199 3.61427 3.46801 0.30946  0.36884  0.01401  353 GLU A N   
2719 C CA  . GLU A 359 ? 2.75311 3.63167 3.52366 0.27066  0.34194  0.03267  353 GLU A CA  
2720 C C   . GLU A 359 ? 2.73499 3.52836 3.45618 0.23782  0.31344  0.03207  353 GLU A C   
2721 O O   . GLU A 359 ? 2.63678 3.43603 3.38310 0.19781  0.29948  0.05029  353 GLU A O   
2722 C CB  . GLU A 359 ? 2.76656 3.66929 3.59144 0.29218  0.31797  0.02531  353 GLU A CB  
2723 C CG  . GLU A 359 ? 2.75426 3.75982 3.65289 0.31913  0.34195  0.03013  353 GLU A CG  
2724 C CD  . GLU A 359 ? 2.77166 3.86265 3.74812 0.28078  0.35036  0.06066  353 GLU A CD  
2725 O OE1 . GLU A 359 ? 2.72120 3.78337 3.69524 0.23456  0.32977  0.07636  353 GLU A OE1 
2726 O OE2 . GLU A 359 ? 2.87009 4.05777 3.91179 0.29705  0.37696  0.06877  353 GLU A OE2 
2727 N N   . ALA A 360 ? 2.75788 3.47267 3.41087 0.25445  0.30367  0.01089  354 ALA A N   
2728 C CA  . ALA A 360 ? 2.75013 3.39086 3.35831 0.22609  0.28062  0.00914  354 ALA A CA  
2729 C C   . ALA A 360 ? 2.69141 3.32359 3.26894 0.20088  0.29697  0.02127  354 ALA A C   
2730 O O   . ALA A 360 ? 2.49023 3.09406 3.06237 0.16696  0.28003  0.03053  354 ALA A O   
2731 C CB  . ALA A 360 ? 2.68254 3.24848 3.23368 0.24917  0.26586  -0.01486 354 ALA A CB  
2732 N N   . LYS A 361 ? 2.71126 3.36407 3.26405 0.21888  0.32869  0.02063  355 LYS A N   
2733 C CA  . LYS A 361 ? 2.66255 3.31138 3.18542 0.19486  0.34498  0.03597  355 LYS A CA  
2734 C C   . LYS A 361 ? 2.72619 3.43205 3.30647 0.15768  0.34885  0.06590  355 LYS A C   
2735 O O   . LYS A 361 ? 2.74989 3.43086 3.31229 0.12445  0.34281  0.08091  355 LYS A O   
2736 C CB  . LYS A 361 ? 2.71731 3.38200 3.19976 0.22420  0.38003  0.02978  355 LYS A CB  
2737 C CG  . LYS A 361 ? 2.72205 3.37159 3.15784 0.20273  0.39578  0.04473  355 LYS A CG  
2738 C CD  . LYS A 361 ? 2.81152 3.36986 3.17914 0.19823  0.37221  0.02998  355 LYS A CD  
2739 C CE  . LYS A 361 ? 2.88816 3.42790 3.20229 0.18335  0.38644  0.04313  355 LYS A CE  
2740 N NZ  . LYS A 361 ? 2.80639 3.26204 3.05330 0.18710  0.36462  0.02527  355 LYS A NZ  
2741 N N   . LYS A 362 ? 2.71966 3.50039 3.37092 0.16246  0.35596  0.07508  356 LYS A N   
2742 C CA  . LYS A 362 ? 2.62838 3.46448 3.34269 0.12405  0.35440  0.10423  356 LYS A CA  
2743 C C   . LYS A 362 ? 2.59138 3.37799 3.31196 0.09069  0.31327  0.10712  356 LYS A C   
2744 O O   . LYS A 362 ? 2.51615 3.30881 3.25512 0.05156  0.30597  0.12953  356 LYS A O   
2745 C CB  . LYS A 362 ? 2.50652 3.43454 3.30184 0.13919  0.36583  0.11041  356 LYS A CB  
2746 C CG  . LYS A 362 ? 2.45488 3.44720 3.32655 0.09816  0.36100  0.14127  356 LYS A CG  
2747 C CD  . LYS A 362 ? 2.26125 3.34748 3.21926 0.11661  0.36882  0.14482  356 LYS A CD  
2748 C CE  . LYS A 362 ? 2.29076 3.44263 3.33094 0.07236  0.36005  0.17651  356 LYS A CE  
2749 N NZ  . LYS A 362 ? 2.43228 3.68264 3.56509 0.09055  0.36566  0.18020  356 LYS A NZ  
2750 N N   . ILE A 363 ? 2.60012 3.33514 3.30233 0.10561  0.28598  0.08488  357 ILE A N   
2751 C CA  . ILE A 363 ? 2.69062 3.37843 3.39233 0.07850  0.24909  0.08438  357 ILE A CA  
2752 C C   . ILE A 363 ? 2.57906 3.19919 3.22088 0.06082  0.24305  0.08239  357 ILE A C   
2753 O O   . ILE A 363 ? 2.57781 3.17556 3.22461 0.02906  0.22255  0.09238  357 ILE A O   
2754 C CB  . ILE A 363 ? 2.78472 3.44287 3.48308 0.10001  0.22491  0.06339  357 ILE A CB  
2755 C CG1 . ILE A 363 ? 2.91937 3.64429 3.68255 0.11652  0.22459  0.06694  357 ILE A CG1 
2756 C CG2 . ILE A 363 ? 2.64536 3.25087 3.33101 0.07528  0.19027  0.06009  357 ILE A CG2 
2757 C CD1 . ILE A 363 ? 2.85288 3.63163 3.68446 0.08477  0.21239  0.08946  357 ILE A CD1 
2758 N N   . PHE A 364 ? 2.44147 3.02616 3.02621 0.08224  0.25798  0.06851  358 PHE A N   
2759 C CA  . PHE A 364 ? 2.53055 3.05261 3.06119 0.06836  0.24980  0.06546  358 PHE A CA  
2760 C C   . PHE A 364 ? 2.39485 2.93203 2.92642 0.03981  0.26061  0.09075  358 PHE A C   
2761 O O   . PHE A 364 ? 2.34993 2.84402 2.86389 0.01543  0.24129  0.09584  358 PHE A O   
2762 C CB  . PHE A 364 ? 2.63622 3.11891 3.10839 0.09733  0.26035  0.04535  358 PHE A CB  
2763 C CG  . PHE A 364 ? 2.83539 3.25494 3.25630 0.08590  0.24812  0.03999  358 PHE A CG  
2764 C CD1 . PHE A 364 ? 2.82495 3.19507 3.23268 0.08252  0.22214  0.02454  358 PHE A CD1 
2765 C CD2 . PHE A 364 ? 2.69544 3.10728 3.08169 0.07913  0.26257  0.05100  358 PHE A CD2 
2766 C CE1 . PHE A 364 ? 2.49533 2.81429 2.86387 0.07423  0.21037  0.01873  358 PHE A CE1 
2767 C CE2 . PHE A 364 ? 2.70653 3.06031 3.04856 0.07044  0.24746  0.04581  358 PHE A CE2 
2768 C CZ  . PHE A 364 ? 2.53346 2.84314 2.87045 0.06883  0.22110  0.02894  358 PHE A CZ  
2769 N N   . GLU A 365 ? 2.38607 2.98363 2.93671 0.04302  0.29160  0.10725  359 GLU A N   
2770 C CA  . GLU A 365 ? 2.41359 3.02921 2.96624 0.01189  0.30345  0.13633  359 GLU A CA  
2771 C C   . GLU A 365 ? 2.38191 3.01102 2.98805 -0.02653 0.27929  0.15590  359 GLU A C   
2772 O O   . GLU A 365 ? 2.15047 2.75645 2.74551 -0.05866 0.27063  0.17556  359 GLU A O   
2773 C CB  . GLU A 365 ? 2.54576 3.23343 3.11156 0.02395  0.34590  0.15071  359 GLU A CB  
2774 C CG  . GLU A 365 ? 2.51933 3.18834 3.02250 0.06212  0.36975  0.13134  359 GLU A CG  
2775 C CD  . GLU A 365 ? 2.78018 3.38630 3.20894 0.05246  0.36819  0.13425  359 GLU A CD  
2776 O OE1 . GLU A 365 ? 2.90762 3.49744 3.33617 0.01592  0.35684  0.15704  359 GLU A OE1 
2777 O OE2 . GLU A 365 ? 2.97993 3.54948 3.34955 0.08168  0.37522  0.11359  359 GLU A OE2 
2778 N N   . ARG A 366 ? 2.41271 3.07371 3.07398 -0.02368 0.26476  0.15069  360 ARG A N   
2779 C CA  . ARG A 366 ? 2.56100 3.22809 3.27016 -0.05894 0.23583  0.16578  360 ARG A CA  
2780 C C   . ARG A 366 ? 2.47719 3.06073 3.14733 -0.07207 0.20012  0.15316  360 ARG A C   
2781 O O   . ARG A 366 ? 2.44689 3.00788 3.12228 -0.10562 0.18070  0.16920  360 ARG A O   
2782 C CB  . ARG A 366 ? 2.61597 3.33281 3.38749 -0.04860 0.22555  0.16037  360 ARG A CB  
2783 C CG  . ARG A 366 ? 2.53161 3.25145 3.35128 -0.08312 0.19028  0.17276  360 ARG A CG  
2784 C CD  . ARG A 366 ? 2.26234 3.00616 3.12340 -0.06682 0.17068  0.15928  360 ARG A CD  
2785 N NE  . ARG A 366 ? 2.58807 3.26982 3.39742 -0.03953 0.15682  0.12922  360 ARG A NE  
2786 C CZ  . ARG A 366 ? 2.72708 3.41090 3.55120 -0.02096 0.13903  0.11444  360 ARG A CZ  
2787 N NH1 . ARG A 366 ? 2.75020 3.49450 3.64097 -0.02335 0.12996  0.12428  360 ARG A NH1 
2788 N NH2 . ARG A 366 ? 2.63357 3.25815 3.40520 -0.00050 0.12910  0.09059  360 ARG A NH2 
2789 N N   . ASP A 367 ? 2.50461 3.04166 3.13607 -0.04564 0.19087  0.12447  361 ASP A N   
2790 C CA  . ASP A 367 ? 2.63013 3.09564 3.22702 -0.05312 0.16076  0.10955  361 ASP A CA  
2791 C C   . ASP A 367 ? 2.69734 3.11432 3.24319 -0.06009 0.16305  0.11218  361 ASP A C   
2792 O O   . ASP A 367 ? 2.62798 2.99206 3.15461 -0.07271 0.13699  0.10618  361 ASP A O   
2793 C CB  . ASP A 367 ? 2.60073 3.03959 3.17630 -0.02465 0.15312  0.08086  361 ASP A CB  
2794 C CG  . ASP A 367 ? 2.48739 2.96574 3.10672 -0.01570 0.14640  0.07788  361 ASP A CG  
2795 O OD1 . ASP A 367 ? 2.55162 3.08089 3.22336 -0.03156 0.14566  0.09659  361 ASP A OD1 
2796 O OD2 . ASP A 367 ? 2.50254 2.96103 3.10487 0.00609  0.14041  0.05816  361 ASP A OD2 
2797 N N   . TRP A 368 ? 2.73604 3.16831 3.25736 -0.05013 0.19216  0.11993  362 TRP A N   
2798 C CA  . TRP A 368 ? 2.80206 3.18529 3.27036 -0.05518 0.19164  0.12272  362 TRP A CA  
2799 C C   . TRP A 368 ? 2.67503 3.05079 3.15204 -0.09225 0.18119  0.15122  362 TRP A C   
2800 O O   . TRP A 368 ? 2.62767 2.94443 3.07247 -0.10309 0.15928  0.15009  362 TRP A O   
2801 C CB  . TRP A 368 ? 2.81108 3.20864 3.24287 -0.03251 0.22398  0.12177  362 TRP A CB  
2802 C CG  . TRP A 368 ? 2.96704 3.31390 3.34071 -0.03665 0.22161  0.12544  362 TRP A CG  
2803 C CD1 . TRP A 368 ? 2.88875 3.24129 3.24073 -0.05366 0.23634  0.15165  362 TRP A CD1 
2804 C CD2 . TRP A 368 ? 2.86098 3.14445 3.19140 -0.02417 0.20182  0.10343  362 TRP A CD2 
2805 N NE1 . TRP A 368 ? 2.94566 3.23700 3.23948 -0.05104 0.22421  0.14662  362 TRP A NE1 
2806 C CE2 . TRP A 368 ? 2.94503 3.19595 3.22878 -0.03258 0.20257  0.11647  362 TRP A CE2 
2807 C CE3 . TRP A 368 ? 2.48079 2.73458 2.80876 -0.00765 0.18384  0.07535  362 TRP A CE3 
2808 C CZ2 . TRP A 368 ? 2.98970 3.18093 3.22936 -0.02317 0.18320  0.10071  362 TRP A CZ2 
2809 C CZ3 . TRP A 368 ? 2.51309 2.71323 2.80089 -0.00005 0.16815  0.06064  362 TRP A CZ3 
2810 C CH2 . TRP A 368 ? 2.87468 3.04461 3.12108 -0.00688 0.16656  0.07246  362 TRP A CH2 
2811 N N   . VAL A 369 ? 2.56072 2.99580 3.08325 -0.11236 0.19526  0.17765  363 VAL A N   
2812 C CA  . VAL A 369 ? 2.69559 3.12694 3.23044 -0.15250 0.18582  0.20960  363 VAL A CA  
2813 C C   . VAL A 369 ? 2.63204 3.06167 3.21689 -0.17813 0.15209  0.21386  363 VAL A C   
2814 O O   . VAL A 369 ? 2.81013 3.24462 3.41872 -0.21529 0.14154  0.24257  363 VAL A O   
2815 C CB  . VAL A 369 ? 2.75214 3.25169 3.30444 -0.16416 0.22417  0.24086  363 VAL A CB  
2816 C CG1 . VAL A 369 ? 2.78959 3.28155 3.28062 -0.13762 0.25503  0.23483  363 VAL A CG1 
2817 C CG2 . VAL A 369 ? 2.77709 3.36148 3.39905 -0.15776 0.24064  0.24323  363 VAL A CG2 
2818 N N   . SER A 370 ? 2.31144 2.73105 2.90945 -0.16036 0.13342  0.18671  364 SER A N   
2819 C CA  . SER A 370 ? 2.28453 2.69709 2.92191 -0.18148 0.09874  0.18717  364 SER A CA  
2820 C C   . SER A 370 ? 2.48643 2.82167 3.09330 -0.20174 0.06333  0.18660  364 SER A C   
2821 O O   . SER A 370 ? 2.56250 2.84549 3.11732 -0.19118 0.06216  0.17726  364 SER A O   
2822 C CB  . SER A 370 ? 2.28165 2.69605 2.92795 -0.15497 0.08810  0.15752  364 SER A CB  
2823 O OG  . SER A 370 ? 2.37199 2.77505 3.04875 -0.17396 0.05236  0.15629  364 SER A OG  
2824 N N   . SER A 371 ? 2.47945 2.80616 3.12043 -0.23014 0.03122  0.19584  365 SER A N   
2825 C CA  . SER A 371 ? 2.60846 2.85771 3.22229 -0.24836 -0.00699 0.19389  365 SER A CA  
2826 C C   . SER A 371 ? 2.61963 2.81007 3.19131 -0.21817 -0.02541 0.15475  365 SER A C   
2827 O O   . SER A 371 ? 2.84998 2.97398 3.38384 -0.21872 -0.04675 0.14674  365 SER A O   
2828 C CB  . SER A 371 ? 2.59526 2.84658 3.25517 -0.28497 -0.04040 0.21052  365 SER A CB  
2829 O OG  . SER A 371 ? 2.48116 2.75417 3.16978 -0.27319 -0.05399 0.19088  365 SER A OG  
2830 N N   . HIS A 372 ? 2.46772 2.68240 3.04579 -0.19152 -0.01748 0.13098  366 HIS A N   
2831 C CA  . HIS A 372 ? 2.54081 2.70923 3.08086 -0.16384 -0.02943 0.09585  366 HIS A CA  
2832 C C   . HIS A 372 ? 2.56437 2.71487 3.06238 -0.13973 -0.00792 0.08443  366 HIS A C   
2833 O O   . HIS A 372 ? 2.47948 2.58960 2.94701 -0.12017 -0.01826 0.05806  366 HIS A O   
2834 C CB  . HIS A 372 ? 2.42961 2.62858 2.98628 -0.14594 -0.02731 0.07818  366 HIS A CB  
2835 C CG  . HIS A 372 ? 2.63118 2.85540 3.23284 -0.16760 -0.04881 0.08956  366 HIS A CG  
2836 N ND1 . HIS A 372 ? 2.87971 3.05906 3.47918 -0.18415 -0.08890 0.08334  366 HIS A ND1 
2837 C CD2 . HIS A 372 ? 2.39291 2.68260 3.04445 -0.17432 -0.03824 0.10568  366 HIS A CD2 
2838 C CE1 . HIS A 372 ? 2.58770 2.80234 3.23336 -0.20269 -0.10390 0.09613  366 HIS A CE1 
2839 N NE2 . HIS A 372 ? 2.38337 2.66831 3.06453 -0.19699 -0.07324 0.11031  366 HIS A NE2 
2840 N N   . SER A 373 ? 2.66397 2.84478 3.15962 -0.14043 0.02113  0.10312  367 SER A N   
2841 C CA  . SER A 373 ? 2.76220 2.92674 3.21693 -0.11800 0.03968  0.09298  367 SER A CA  
2842 C C   . SER A 373 ? 2.98411 3.10351 3.41000 -0.13331 0.02819  0.10784  367 SER A C   
2843 O O   . SER A 373 ? 2.80380 2.94094 3.22562 -0.14768 0.04508  0.13446  367 SER A O   
2844 C CB  . SER A 373 ? 2.50554 2.72507 2.96617 -0.10446 0.07697  0.10045  367 SER A CB  
2845 O OG  . SER A 373 ? 2.31191 2.56775 2.79872 -0.08945 0.08353  0.08752  367 SER A OG  
2846 N N   . LYS A 374 ? 3.06071 3.12092 3.46453 -0.12892 -0.00083 0.09053  368 LYS A N   
2847 C CA  . LYS A 374 ? 3.20212 3.21029 3.57422 -0.13796 -0.01677 0.10085  368 LYS A CA  
2848 C C   . LYS A 374 ? 3.11659 3.11541 3.45163 -0.11416 -0.00063 0.09102  368 LYS A C   
2849 O O   . LYS A 374 ? 2.92532 2.93904 3.25717 -0.08828 0.01174  0.06692  368 LYS A O   
2850 C CB  . LYS A 374 ? 3.09779 3.04473 3.46217 -0.13824 -0.05681 0.08354  368 LYS A CB  
2851 C CG  . LYS A 374 ? 3.25685 3.19150 3.64681 -0.16866 -0.08291 0.09886  368 LYS A CG  
2852 C CD  . LYS A 374 ? 3.27709 3.13822 3.64835 -0.16636 -0.12512 0.08149  368 LYS A CD  
2853 C CE  . LYS A 374 ? 3.09717 2.93522 3.48904 -0.19998 -0.15648 0.09881  368 LYS A CE  
2854 N NZ  . LYS A 374 ? 3.13492 2.89265 3.50315 -0.19536 -0.20058 0.08047  368 LYS A NZ  
2855 N N   . SER A 375 ? 3.21915 3.19033 3.52434 -0.12491 -0.00308 0.11130  369 SER A N   
2856 C CA  . SER A 375 ? 3.02523 2.98289 3.29114 -0.10456 0.00776  0.10426  369 SER A CA  
2857 C C   . SER A 375 ? 3.17101 3.08686 3.42481 -0.08057 -0.01579 0.07219  369 SER A C   
2858 O O   . SER A 375 ? 3.02532 2.90818 3.28944 -0.08198 -0.04402 0.06032  369 SER A O   
2859 C CB  . SER A 375 ? 3.16568 3.09722 3.39650 -0.12321 0.00656  0.13529  369 SER A CB  
2860 O OG  . SER A 375 ? 3.59477 3.51144 3.78305 -0.10307 0.01482  0.12829  369 SER A OG  
2861 N N   . LEU A 376 ? 3.28574 3.20477 3.51844 -0.05761 -0.00417 0.05736  370 LEU A N   
2862 C CA  . LEU A 376 ? 3.24305 3.13411 3.47093 -0.03455 -0.02276 0.02789  370 LEU A CA  
2863 C C   . LEU A 376 ? 3.32284 3.15455 3.52763 -0.03743 -0.05535 0.03254  370 LEU A C   
2864 O O   . LEU A 376 ? 3.45955 3.26939 3.62997 -0.04253 -0.05699 0.05069  370 LEU A O   
2865 C CB  . LEU A 376 ? 3.14425 3.05335 3.35750 -0.01366 -0.00481 0.01449  370 LEU A CB  
2866 C CG  . LEU A 376 ? 3.07987 2.97033 3.29474 0.00862  -0.02143 -0.01407 370 LEU A CG  
2867 C CD1 . LEU A 376 ? 2.93539 2.84367 3.18463 0.01640  -0.02283 -0.03679 370 LEU A CD1 
2868 C CD2 . LEU A 376 ? 3.05501 2.95707 3.25191 0.02349  -0.00794 -0.02185 370 LEU A CD2 
2869 N N   . LYS A 377 ? 3.13381 2.93655 3.35361 -0.03239 -0.08241 0.01555  371 LYS A N   
2870 C CA  . LYS A 377 ? 3.38196 3.12354 3.58326 -0.03032 -0.11836 0.01543  371 LYS A CA  
2871 C C   . LYS A 377 ? 3.46463 3.19669 3.67897 0.00017  -0.13390 -0.02114 371 LYS A C   
2872 O O   . LYS A 377 ? 3.28990 3.04457 3.53046 0.01006  -0.12896 -0.04350 371 LYS A O   
2873 C CB  . LYS A 377 ? 3.34361 3.05102 3.54968 -0.05398 -0.14164 0.03115  371 LYS A CB  
2874 C CG  . LYS A 377 ? 3.23907 2.95425 3.43507 -0.08835 -0.12952 0.07219  371 LYS A CG  
2875 C CD  . LYS A 377 ? 3.25949 2.93227 3.46100 -0.11488 -0.15956 0.08893  371 LYS A CD  
2876 C CE  . LYS A 377 ? 3.44698 3.13173 3.64217 -0.15296 -0.14656 0.13375  371 LYS A CE  
2877 N NZ  . LYS A 377 ? 3.21882 2.85824 3.42102 -0.18362 -0.17957 0.15298  371 LYS A NZ  
2878 N N   . ILE A 378 ? 3.64401 3.34534 3.84011 0.01519  -0.15226 -0.02658 372 ILE A N   
2879 C CA  . ILE A 378 ? 3.54831 3.24611 3.76263 0.04508  -0.16759 -0.06015 372 ILE A CA  
2880 C C   . ILE A 378 ? 3.80661 3.44120 4.00497 0.05401  -0.20903 -0.06117 372 ILE A C   
2881 O O   . ILE A 378 ? 3.88896 3.48760 4.05365 0.04354  -0.22225 -0.03747 372 ILE A O   
2882 C CB  . ILE A 378 ? 3.21063 2.94608 3.42999 0.06057  -0.14888 -0.07206 372 ILE A CB  
2883 C CG1 . ILE A 378 ? 2.97466 2.76627 3.20984 0.05451  -0.11165 -0.07351 372 ILE A CG1 
2884 C CG2 . ILE A 378 ? 2.72389 2.46102 2.96861 0.08929  -0.16569 -0.10383 372 ILE A CG2 
2885 C CD1 . ILE A 378 ? 2.97652 2.79910 3.21437 0.06634  -0.09534 -0.08340 372 ILE A CD1 
2886 O OXT . ILE A 378 ? 4.06701 3.68311 4.28306 0.07346  -0.23092 -0.08597 372 ILE A OXT 
# 
