data_9FIZ
# 
_entry.id   9FIZ 
# 
_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   9FIZ         pdb_00009fiz 10.2210/pdb9fiz/pdb 
WWPDB D_1292139010 ?            ?                   
# 
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                        9FIZ 
_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' 42324.836 1  3.1.1.-,3.1.4.4 ? ? ? 
2 non-polymer syn 'CITRIC ACID'                   192.124   1  ?               ? ? ? 
3 non-polymer syn GLYCEROL                        92.094    13 ?               ? ? ? 
4 water       nat water                           18.015    59 ?               ? ? ? 
# 
_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
DIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDELCVQNDLSVKVFTIQNNTK
LLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHHHGSGSVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASE
KGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYP
PLATDLRRRFDTFKAFNSAKNSAANLASAAAALPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSI
DIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDELCVQNDLSVKVFTIQNNTK
LLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 GLYCEROL      GOL 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   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 GLY 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 GLU 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 
CIT non-polymer         . 'CITRIC ACID'   ?                               'C6 H8 O7'       192.124 
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 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
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 GLY 283 277 277 GLY GLY 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 GLU 301 295 295 GLU GLU 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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CIT ? ? CIT ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT 1  401 401 CIT CIT A . 
C 3 GOL 1  402 402 GOL GOL A . 
D 3 GOL 1  403 406 GOL GOL A . 
E 3 GOL 1  404 407 GOL GOL A . 
F 3 GOL 1  405 408 GOL GOL A . 
G 3 GOL 1  406 409 GOL GOL A . 
H 3 GOL 1  407 410 GOL GOL A . 
I 3 GOL 1  408 411 GOL GOL A . 
J 3 GOL 1  409 412 GOL GOL A . 
K 3 GOL 1  410 413 GOL GOL A . 
L 3 GOL 1  411 414 GOL GOL A . 
M 3 GOL 1  412 415 GOL GOL A . 
N 3 GOL 1  413 416 GOL GOL A . 
O 3 GOL 1  414 417 GOL GOL A . 
P 4 HOH 1  501 67  HOH HOH A . 
P 4 HOH 2  502 47  HOH HOH A . 
P 4 HOH 3  503 26  HOH HOH A . 
P 4 HOH 4  504 9   HOH HOH A . 
P 4 HOH 5  505 49  HOH HOH A . 
P 4 HOH 6  506 18  HOH HOH A . 
P 4 HOH 7  507 40  HOH HOH A . 
P 4 HOH 8  508 5   HOH HOH A . 
P 4 HOH 9  509 27  HOH HOH A . 
P 4 HOH 10 510 54  HOH HOH A . 
P 4 HOH 11 511 20  HOH HOH A . 
P 4 HOH 12 512 11  HOH HOH A . 
P 4 HOH 13 513 38  HOH HOH A . 
P 4 HOH 14 514 61  HOH HOH A . 
P 4 HOH 15 515 58  HOH HOH A . 
P 4 HOH 16 516 2   HOH HOH A . 
P 4 HOH 17 517 33  HOH HOH A . 
P 4 HOH 18 518 24  HOH HOH A . 
P 4 HOH 19 519 42  HOH HOH A . 
P 4 HOH 20 520 41  HOH HOH A . 
P 4 HOH 21 521 28  HOH HOH A . 
P 4 HOH 22 522 43  HOH HOH A . 
P 4 HOH 23 523 57  HOH HOH A . 
P 4 HOH 24 524 34  HOH HOH A . 
P 4 HOH 25 525 65  HOH HOH A . 
P 4 HOH 26 526 8   HOH HOH A . 
P 4 HOH 27 527 59  HOH HOH A . 
P 4 HOH 28 528 45  HOH HOH A . 
P 4 HOH 29 529 30  HOH HOH A . 
P 4 HOH 30 530 31  HOH HOH A . 
P 4 HOH 31 531 56  HOH HOH A . 
P 4 HOH 32 532 25  HOH HOH A . 
P 4 HOH 33 533 22  HOH HOH A . 
P 4 HOH 34 534 44  HOH HOH A . 
P 4 HOH 35 535 21  HOH HOH A . 
P 4 HOH 36 536 66  HOH HOH A . 
P 4 HOH 37 537 23  HOH HOH A . 
P 4 HOH 38 538 17  HOH HOH A . 
P 4 HOH 39 539 39  HOH HOH A . 
P 4 HOH 40 540 19  HOH HOH A . 
P 4 HOH 41 541 35  HOH HOH A . 
P 4 HOH 42 542 62  HOH HOH A . 
P 4 HOH 43 543 16  HOH HOH A . 
P 4 HOH 44 544 29  HOH HOH A . 
P 4 HOH 45 545 7   HOH HOH A . 
P 4 HOH 46 546 60  HOH HOH A . 
P 4 HOH 47 547 63  HOH HOH A . 
P 4 HOH 48 548 50  HOH HOH A . 
P 4 HOH 49 549 13  HOH HOH A . 
P 4 HOH 50 550 64  HOH HOH A . 
P 4 HOH 51 551 15  HOH HOH A . 
P 4 HOH 52 552 4   HOH HOH A . 
P 4 HOH 53 553 12  HOH HOH A . 
P 4 HOH 54 554 10  HOH HOH A . 
P 4 HOH 55 555 52  HOH HOH A . 
P 4 HOH 56 556 53  HOH HOH A . 
P 4 HOH 57 557 32  HOH HOH A . 
P 4 HOH 58 558 55  HOH HOH A . 
P 4 HOH 59 559 51  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21_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                     9FIZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     280.979 
_cell.length_a_esd                 ? 
_cell.length_b                     280.979 
_cell.length_b_esd                 ? 
_cell.length_c                     280.979 
_cell.length_c_esd                 ? 
_cell.volume                       22183066.829 
_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                         9FIZ 
_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                   9FIZ 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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 (cryoprotected with 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                          73.64 
_reflns.entry_id                                       9FIZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               49.67 
_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                                     29768 
_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                           96.14 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                80.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.20 
_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                                    2.60 
_reflns_shell.d_res_low                                     2.693 
_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                             2921 
_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                                  0.644 
_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                               89.35 
_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                                 9FIZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.60 
_refine.ls_d_res_low                             49.67 
_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                     28632 
_refine.ls_number_reflns_R_free                  1396 
_refine.ls_number_reflns_R_work                  27236 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.18 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2180 
_refine.ls_R_factor_R_free                       0.2586 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2159 
_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                 36.8533 
_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                            0.5764 
_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                       2.60 
_refine_hist.d_res_low                        49.67 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               3038 
_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        2888 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         91 
_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' ? 0.0020  ? 3024 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4839  ? 4079 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0424  ? 459  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0034  ? 514  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.4329 ? 1099 ? 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' 2.60 2.69  . . 102 1723 62.41  . . . . 0.8318 . . . . . . . . . . . 0.7399 
'X-RAY DIFFRACTION' 2.69 2.80  . . 118 2756 99.10  . . . . 0.6064 . . . . . . . . . . . 0.6473 
'X-RAY DIFFRACTION' 2.80 2.93  . . 148 2753 99.93  . . . . 0.3879 . . . . . . . . . . . 0.4312 
'X-RAY DIFFRACTION' 2.93 3.08  . . 148 2791 100.00 . . . . 0.2875 . . . . . . . . . . . 0.3607 
'X-RAY DIFFRACTION' 3.08 3.28  . . 141 2775 99.90  . . . . 0.2637 . . . . . . . . . . . 0.3228 
'X-RAY DIFFRACTION' 3.28 3.53  . . 139 2821 99.97  . . . . 0.2698 . . . . . . . . . . . 0.3365 
'X-RAY DIFFRACTION' 3.53 3.88  . . 150 2810 99.97  . . . . 0.1936 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 3.89 4.45  . . 139 2851 100.00 . . . . 0.1723 . . . . . . . . . . . 0.2389 
'X-RAY DIFFRACTION' 4.45 5.60  . . 143 2882 99.97  . . . . 0.1598 . . . . . . . . . . . 0.2070 
'X-RAY DIFFRACTION' 5.60 49.67 . . 168 3074 99.85  . . . . 0.1799 . . . . . . . . . . . 0.1965 
# 
_struct.entry_id                     9FIZ 
_struct.title                        'Structure of the F13 protein (mutant A295E) 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        9FIZ 
_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 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 4 ? 
# 
_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              9FIZ 
_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 9FIZ HIS A 1   ? UNP P04021 ?   ?   'expression tag'      -5  1  
1 9FIZ HIS A 2   ? UNP P04021 ?   ?   'expression tag'      -4  2  
1 9FIZ HIS A 3   ? UNP P04021 ?   ?   'expression tag'      -3  3  
1 9FIZ HIS A 4   ? UNP P04021 ?   ?   'expression tag'      -2  4  
1 9FIZ HIS A 5   ? UNP P04021 ?   ?   'expression tag'      -1  5  
1 9FIZ HIS A 6   ? UNP P04021 ?   ?   'expression tag'      0   6  
1 9FIZ HIS A 7   ? UNP P04021 ?   ?   'expression tag'      1   7  
1 9FIZ HIS A 8   ? UNP P04021 ?   ?   'expression tag'      2   8  
1 9FIZ GLY A 9   ? UNP P04021 ?   ?   'expression tag'      3   9  
1 9FIZ SER A 10  ? UNP P04021 ?   ?   'expression tag'      4   10 
1 9FIZ GLY A 11  ? UNP P04021 ?   ?   'expression tag'      5   11 
1 9FIZ ALA A 183 ? UNP P04021 TRP 177 conflict              177 12 
1 9FIZ ALA A 184 ? UNP P04021 LEU 178 conflict              178 13 
1 9FIZ ALA A 187 ? UNP P04021 CYS 181 conflict              181 14 
1 9FIZ ALA A 191 ? UNP P04021 CYS 185 conflict              185 15 
1 9FIZ ALA A 192 ? UNP P04021 CYS 186 conflict              186 16 
1 9FIZ GLU A 301 ? UNP P04021 ALA 295 'engineered mutation' 295 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)' 2380  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  28890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_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' 28_555 x,-y+1/2,-z+1/2 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
-1.0000000000 0.0000000000 140.4895000000 0.0000000000 0.0000000000 -1.0000000000 140.4895000000 
# 
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  ? ALA A 49  ? THR A 32  ALA A 43  1 ? 12 
HELX_P HELX_P3  AA3 PRO A 62  ? SER A 64  ? PRO A 56  SER A 58  5 ? 3  
HELX_P HELX_P4  AA4 THR A 65  ? LYS A 81  ? THR A 59  LYS A 75  1 ? 17 
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 GLY A 144 ? THR A 149 ? GLY A 138 THR A 143 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 ? ALA A 236 ? LEU A 218 ALA A 230 1 ? 13 
HELX_P HELX_P11 AB2 PRO A 261 ? GLY A 275 ? PRO A 255 GLY A 269 1 ? 15 
HELX_P HELX_P12 AB3 VAL A 290 ? LEU A 302 ? VAL A 284 LEU A 296 1 ? 13 
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   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 125 A . ? GLY 119 A CYS 126 A ? CYS 120 A 1 -4.12 
2 SER 213 A . ? SER 207 A PRO 214 A ? PRO 208 A 1 -2.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7  ? 
AA2 ? 11 ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? parallel      
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? parallel      
AA1 6  7  ? anti-parallel 
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? anti-parallel 
AA2 4  5  ? parallel      
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? parallel      
AA2 9  10 ? parallel      
AA2 10 11 ? anti-parallel 
AA3 1  2  ? parallel      
AA4 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  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  LEU A 123 ? SER A 130 ? LEU A 117 SER A 124 
AA1 6  GLY A 345 ? SER A 351 ? GLY A 339 SER A 345 
AA1 7  VAL A 208 ? SER A 213 ? VAL A 202 SER A 207 
AA2 1  ASN A 108 ? VAL A 112 ? ASN A 102 VAL A 106 
AA2 2  LYS A 84  ? ASP A 90  ? LYS A 78  ASP A 84  
AA2 3  TYR A 52  ? SER A 57  ? TYR A 46  SER A 51  
AA2 4  LEU A 123 ? SER A 130 ? LEU A 117 SER A 124 
AA2 5  GLY A 345 ? SER A 351 ? GLY A 339 SER A 345 
AA2 6  TYR A 328 ? ILE A 331 ? TYR A 322 ILE A 325 
AA2 7  LEU A 321 ? VAL A 324 ? LEU A 315 VAL A 318 
AA2 8  SER A 239 ? GLU A 243 ? SER A 233 GLU A 237 
AA2 9  LYS A 277 ? GLY A 283 ? LYS A 271 GLY A 277 
AA2 10 LEU A 308 ? PHE A 313 ? LEU A 302 PHE A 307 
AA2 11 LYS A 374 ? SER A 375 ? LYS A 368 SER A 369 
AA3 1  CYS A 60  ? ASN A 61  ? CYS A 54  ASN A 55  
AA3 2  PHE A 142 ? THR A 143 ? PHE A 136 THR A 137 
AA4 1  THR A 250 ? ARG A 252 ? THR A 244 ARG A 246 
AA4 2  SER A 257 ? TYR A 259 ? SER A 251 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  N LEU A 124 ? N LEU A 118 O GLY A 345 ? O GLY A 339 
AA1 6  7  O SER A 348 ? O SER A 342 N THR A 211 ? N THR A 205 
AA2 1  2  O ILE A 110 ? O ILE A 104 N VAL A 87  ? N VAL A 81  
AA2 2  3  O LEU A 88  ? O LEU A 82  N ILE A 55  ? N ILE A 49  
AA2 3  4  N TYR A 54  ? N TYR A 48  O VAL A 129 ? O VAL A 123 
AA2 4  5  N LEU A 124 ? N LEU A 118 O GLY A 345 ? O GLY A 339 
AA2 5  6  O PHE A 349 ? O PHE A 343 N ILE A 331 ? N ILE A 325 
AA2 6  7  O HIS A 330 ? O HIS A 324 N LEU A 322 ? N LEU A 316 
AA2 7  8  O LEU A 321 ? O LEU A 315 N GLU A 243 ? N GLU A 237 
AA2 8  9  N ILE A 242 ? N ILE A 236 O LEU A 281 ? O LEU A 275 
AA2 9  10 N LEU A 280 ? N LEU A 274 O SER A 309 ? O SER A 303 
AA2 10 11 N VAL A 312 ? N VAL A 306 O LYS A 374 ? O LYS A 368 
AA3 1  2  N ASN A 61  ? N ASN A 55  O PHE A 142 ? O PHE A 136 
AA4 1  2  N THR A 251 ? N THR A 245 O TYR A 258 ? O TYR A 252 
# 
_pdbx_entry_details.entry_id                   9FIZ 
_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 LYS A 45  ? ? -126.00 -57.58  
2  1 ASN A 55  ? ? -152.04 73.29   
3  1 ASP A 109 ? ? -151.32 83.75   
4  1 ASP A 125 ? ? 57.70   15.42   
5  1 GLU A 127 ? ? -140.72 -49.22  
6  1 HIS A 142 ? ? -130.07 -52.78  
7  1 LYS A 174 ? ? 53.85   -147.14 
8  1 HIS A 194 ? ? -119.31 -169.83 
9  1 THR A 232 ? ? -135.08 -62.94  
10 1 ASP A 248 ? ? 38.11   -105.62 
11 1 ASN A 337 ? ? -136.77 -35.61  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     549 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   P 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 -22.503034248  44.9232972607 43.894816888  0.477876096175 ? 0.0397978105202 ? 0.0924669852372  ? 
0.635234010182 ? -0.0325067110259 ? 0.599780713055 ? 1.81946768976 ? -0.338757891509 ? 0.969272919977 ? 2.48435438536 ? 
-0.264089494166 ? 3.32034155193 ? 0.105237335602   ? 0.153160034654   ? -0.237268133491  ? -0.177235231445 ? -0.064739827592  ? 
-0.189630594581 ? 0.252604606135  ? 0.131545249885  ? -0.0287894029914 ? 
2 'X-RAY DIFFRACTION' ? refined -12.401726917  54.1044088371 51.966185879  0.454305112091 ? 0.0179995704219 ? -0.0249645218172 ? 
0.768973960575 ? 0.0988743486694  ? 0.612271454821 ? 4.16621613441 ? 0.779702297995  ? -0.73762560156 ? 5.37389641324 ? 
1.26433959802   ? 2.28600628278 ? -0.0792280421675 ? -0.225185502029  ? -0.0536461019298 ? 0.449908614243  ? -0.0255992271306 ? 
-0.999978215549 ? 0.0660337565341 ? 0.673976435035  ? 0.0943207458043  ? 
3 'X-RAY DIFFRACTION' ? refined -30.3624549064 65.8893089766 56.2949868353 0.471444694393 ? 0.0142418093661 ? 0.0224254093171  ? 
0.522037910828 ? -0.0770573936472 ? 0.515957473066 ? 2.80999794759 ? -0.19145030477  ? 1.11962145046  ? 4.03526183823 ? 
0.798778299947  ? 4.59750484891 ? 0.0122529851835  ? -0.0807666771333 ? -0.0311351689523 ? 0.165272155932  ? -0.224231216523  ? 
0.329626245268  ? -0.344285956029 ? -0.487414958907 ? 0.176378907823   ? 
# 
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 224 A 229 ? ? 
;chain 'A' and (resid 138 through 229 )
;
3 'X-RAY DIFFRACTION' 3 A 225 A 230 ? A 367 A 372 ? ? 
;chain 'A' and (resid 230 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  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
GOL C1   C N N 158 
GOL O1   O N N 159 
GOL C2   C N N 160 
GOL O2   O N N 161 
GOL C3   C N N 162 
GOL O3   O N N 163 
GOL H11  H N N 164 
GOL H12  H N N 165 
GOL HO1  H N N 166 
GOL H2   H N N 167 
GOL HO2  H N N 168 
GOL H31  H N N 169 
GOL H32  H N N 170 
GOL HO3  H N N 171 
HIS N    N N N 172 
HIS CA   C N S 173 
HIS C    C N N 174 
HIS O    O N N 175 
HIS CB   C N N 176 
HIS CG   C Y N 177 
HIS ND1  N Y N 178 
HIS CD2  C Y N 179 
HIS CE1  C Y N 180 
HIS NE2  N Y N 181 
HIS OXT  O N N 182 
HIS H    H N N 183 
HIS H2   H N N 184 
HIS HA   H N N 185 
HIS HB2  H N N 186 
HIS HB3  H N N 187 
HIS HD1  H N N 188 
HIS HD2  H N N 189 
HIS HE1  H N N 190 
HIS HE2  H N N 191 
HIS HXT  H N N 192 
HOH O    O N N 193 
HOH H1   H N N 194 
HOH H2   H N N 195 
ILE N    N N N 196 
ILE CA   C N S 197 
ILE C    C N N 198 
ILE O    O N N 199 
ILE CB   C N S 200 
ILE CG1  C N N 201 
ILE CG2  C N N 202 
ILE CD1  C N N 203 
ILE OXT  O N N 204 
ILE H    H N N 205 
ILE H2   H N N 206 
ILE HA   H N N 207 
ILE HB   H N N 208 
ILE HG12 H N N 209 
ILE HG13 H N N 210 
ILE HG21 H N N 211 
ILE HG22 H N N 212 
ILE HG23 H N N 213 
ILE HD11 H N N 214 
ILE HD12 H N N 215 
ILE HD13 H N N 216 
ILE HXT  H N N 217 
LEU N    N N N 218 
LEU CA   C N S 219 
LEU C    C N N 220 
LEU O    O N N 221 
LEU CB   C N N 222 
LEU CG   C N N 223 
LEU CD1  C N N 224 
LEU CD2  C N N 225 
LEU OXT  O N N 226 
LEU H    H N N 227 
LEU H2   H N N 228 
LEU HA   H N N 229 
LEU HB2  H N N 230 
LEU HB3  H N N 231 
LEU HG   H N N 232 
LEU HD11 H N N 233 
LEU HD12 H N N 234 
LEU HD13 H N N 235 
LEU HD21 H N N 236 
LEU HD22 H N N 237 
LEU HD23 H N N 238 
LEU HXT  H N N 239 
LYS N    N N N 240 
LYS CA   C N S 241 
LYS C    C N N 242 
LYS O    O N N 243 
LYS CB   C N N 244 
LYS CG   C N N 245 
LYS CD   C N N 246 
LYS CE   C N N 247 
LYS NZ   N N N 248 
LYS OXT  O N N 249 
LYS H    H N N 250 
LYS H2   H N N 251 
LYS HA   H N N 252 
LYS HB2  H N N 253 
LYS HB3  H N N 254 
LYS HG2  H N N 255 
LYS HG3  H N N 256 
LYS HD2  H N N 257 
LYS HD3  H N N 258 
LYS HE2  H N N 259 
LYS HE3  H N N 260 
LYS HZ1  H N N 261 
LYS HZ2  H N N 262 
LYS HZ3  H N N 263 
LYS HXT  H N N 264 
MET N    N N N 265 
MET CA   C N S 266 
MET C    C N N 267 
MET O    O N N 268 
MET CB   C N N 269 
MET CG   C N N 270 
MET SD   S N N 271 
MET CE   C N N 272 
MET OXT  O N N 273 
MET H    H N N 274 
MET H2   H N N 275 
MET HA   H N N 276 
MET HB2  H N N 277 
MET HB3  H N N 278 
MET HG2  H N N 279 
MET HG3  H N N 280 
MET HE1  H N N 281 
MET HE2  H N N 282 
MET HE3  H N N 283 
MET HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
VAL N    N N N 407 
VAL CA   C N S 408 
VAL C    C N N 409 
VAL O    O N N 410 
VAL CB   C N N 411 
VAL CG1  C N N 412 
VAL CG2  C N N 413 
VAL OXT  O N N 414 
VAL H    H N N 415 
VAL H2   H N N 416 
VAL HA   H N N 417 
VAL HB   H N N 418 
VAL HG11 H N N 419 
VAL HG12 H N N 420 
VAL HG13 H N N 421 
VAL HG21 H N N 422 
VAL HG22 H N N 423 
VAL HG23 H N N 424 
VAL HXT  H N N 425 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
GOL C1  O1   sing N N 149 
GOL C1  C2   sing N N 150 
GOL C1  H11  sing N N 151 
GOL C1  H12  sing N N 152 
GOL O1  HO1  sing N N 153 
GOL C2  O2   sing N N 154 
GOL C2  C3   sing N N 155 
GOL C2  H2   sing N N 156 
GOL O2  HO2  sing N N 157 
GOL C3  O3   sing N N 158 
GOL C3  H31  sing N N 159 
GOL C3  H32  sing N N 160 
GOL O3  HO3  sing N N 161 
HIS N   CA   sing N N 162 
HIS N   H    sing N N 163 
HIS N   H2   sing N N 164 
HIS CA  C    sing N N 165 
HIS CA  CB   sing N N 166 
HIS CA  HA   sing N N 167 
HIS C   O    doub N N 168 
HIS C   OXT  sing N N 169 
HIS CB  CG   sing N N 170 
HIS CB  HB2  sing N N 171 
HIS CB  HB3  sing N N 172 
HIS CG  ND1  sing Y N 173 
HIS CG  CD2  doub Y N 174 
HIS ND1 CE1  doub Y N 175 
HIS ND1 HD1  sing N N 176 
HIS CD2 NE2  sing Y N 177 
HIS CD2 HD2  sing N N 178 
HIS CE1 NE2  sing Y N 179 
HIS CE1 HE1  sing N N 180 
HIS NE2 HE2  sing N N 181 
HIS OXT HXT  sing N N 182 
HOH O   H1   sing N N 183 
HOH O   H2   sing N N 184 
ILE N   CA   sing N N 185 
ILE N   H    sing N N 186 
ILE N   H2   sing N N 187 
ILE CA  C    sing N N 188 
ILE CA  CB   sing N N 189 
ILE CA  HA   sing N N 190 
ILE C   O    doub N N 191 
ILE C   OXT  sing N N 192 
ILE CB  CG1  sing N N 193 
ILE CB  CG2  sing N N 194 
ILE CB  HB   sing N N 195 
ILE CG1 CD1  sing N N 196 
ILE CG1 HG12 sing N N 197 
ILE CG1 HG13 sing N N 198 
ILE CG2 HG21 sing N N 199 
ILE CG2 HG22 sing N N 200 
ILE CG2 HG23 sing N N 201 
ILE CD1 HD11 sing N N 202 
ILE CD1 HD12 sing N N 203 
ILE CD1 HD13 sing N N 204 
ILE OXT HXT  sing N N 205 
LEU N   CA   sing N N 206 
LEU N   H    sing N N 207 
LEU N   H2   sing N N 208 
LEU CA  C    sing N N 209 
LEU CA  CB   sing N N 210 
LEU CA  HA   sing N N 211 
LEU C   O    doub N N 212 
LEU C   OXT  sing N N 213 
LEU CB  CG   sing N N 214 
LEU CB  HB2  sing N N 215 
LEU CB  HB3  sing N N 216 
LEU CG  CD1  sing N N 217 
LEU CG  CD2  sing N N 218 
LEU CG  HG   sing N N 219 
LEU CD1 HD11 sing N N 220 
LEU CD1 HD12 sing N N 221 
LEU CD1 HD13 sing N N 222 
LEU CD2 HD21 sing N N 223 
LEU CD2 HD22 sing N N 224 
LEU CD2 HD23 sing N N 225 
LEU OXT HXT  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
THR N   CA   sing N N 323 
THR N   H    sing N N 324 
THR N   H2   sing N N 325 
THR CA  C    sing N N 326 
THR CA  CB   sing N N 327 
THR CA  HA   sing N N 328 
THR C   O    doub N N 329 
THR C   OXT  sing N N 330 
THR CB  OG1  sing N N 331 
THR CB  CG2  sing N N 332 
THR CB  HB   sing N N 333 
THR OG1 HG1  sing N N 334 
THR CG2 HG21 sing N N 335 
THR CG2 HG22 sing N N 336 
THR CG2 HG23 sing N N 337 
THR OXT HXT  sing N N 338 
TRP N   CA   sing N N 339 
TRP N   H    sing N N 340 
TRP N   H2   sing N N 341 
TRP CA  C    sing N N 342 
TRP CA  CB   sing N N 343 
TRP CA  HA   sing N N 344 
TRP C   O    doub N N 345 
TRP C   OXT  sing N N 346 
TRP CB  CG   sing N N 347 
TRP CB  HB2  sing N N 348 
TRP CB  HB3  sing N N 349 
TRP CG  CD1  doub Y N 350 
TRP CG  CD2  sing Y N 351 
TRP CD1 NE1  sing Y N 352 
TRP CD1 HD1  sing N N 353 
TRP CD2 CE2  doub Y N 354 
TRP CD2 CE3  sing Y N 355 
TRP NE1 CE2  sing Y N 356 
TRP NE1 HE1  sing N N 357 
TRP CE2 CZ2  sing Y N 358 
TRP CE3 CZ3  doub Y N 359 
TRP CE3 HE3  sing N N 360 
TRP CZ2 CH2  doub Y N 361 
TRP CZ2 HZ2  sing N N 362 
TRP CZ3 CH2  sing Y N 363 
TRP CZ3 HZ3  sing N N 364 
TRP CH2 HH2  sing N N 365 
TRP OXT HXT  sing N N 366 
TYR N   CA   sing N N 367 
TYR N   H    sing N N 368 
TYR N   H2   sing N N 369 
TYR CA  C    sing N N 370 
TYR CA  CB   sing N N 371 
TYR CA  HA   sing N N 372 
TYR C   O    doub N N 373 
TYR C   OXT  sing N N 374 
TYR CB  CG   sing N N 375 
TYR CB  HB2  sing N N 376 
TYR CB  HB3  sing N N 377 
TYR CG  CD1  doub Y N 378 
TYR CG  CD2  sing Y N 379 
TYR CD1 CE1  sing Y N 380 
TYR CD1 HD1  sing N N 381 
TYR CD2 CE2  doub Y N 382 
TYR CD2 HD2  sing N N 383 
TYR CE1 CZ   doub Y N 384 
TYR CE1 HE1  sing N N 385 
TYR CE2 CZ   sing Y N 386 
TYR CE2 HE2  sing N N 387 
TYR CZ  OH   sing N N 388 
TYR OH  HH   sing N N 389 
TYR OXT HXT  sing N N 390 
VAL N   CA   sing N N 391 
VAL N   H    sing N N 392 
VAL N   H2   sing N N 393 
VAL CA  C    sing N N 394 
VAL CA  CB   sing N N 395 
VAL CA  HA   sing N N 396 
VAL C   O    doub N N 397 
VAL C   OXT  sing N N 398 
VAL CB  CG1  sing N N 399 
VAL CB  CG2  sing N N 400 
VAL CB  HB   sing N N 401 
VAL CG1 HG11 sing N N 402 
VAL CG1 HG12 sing N N 403 
VAL CG1 HG13 sing N N 404 
VAL CG2 HG21 sing N N 405 
VAL CG2 HG22 sing N N 406 
VAL CG2 HG23 sing N N 407 
VAL OXT HXT  sing N N 408 
# 
_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                    9FIZ 
_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]   0.003559 
_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]   0.003559 
_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]   0.003559 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 12  ? -2.36612  64.91934 31.44585 1.000 120.98382 ? 6   SER A N   1 
ATOM   2    C CA  . SER A 1 12  ? -3.32190  65.72588 32.19556 1.000 118.56408 ? 6   SER A CA  1 
ATOM   3    C C   . SER A 1 12  ? -4.46205  64.86082 32.71698 1.000 106.86009 ? 6   SER A C   1 
ATOM   4    O O   . SER A 1 12  ? -4.86402  63.89487 32.06924 1.000 116.36737 ? 6   SER A O   1 
ATOM   5    C CB  . SER A 1 12  ? -3.87436  66.85468 31.32474 1.000 127.96952 ? 6   SER A CB  1 
ATOM   6    O OG  . SER A 1 12  ? -4.64384  66.33755 30.25368 1.000 126.62637 ? 6   SER A OG  1 
ATOM   7    N N   . VAL A 1 13  ? -4.98153  65.21231 33.88879 1.000 104.85566 ? 7   VAL A N   1 
ATOM   8    C CA  . VAL A 1 13  ? -6.06512  64.45508 34.50991 1.000 102.73182 ? 7   VAL A CA  1 
ATOM   9    C C   . VAL A 1 13  ? -7.39893  65.08474 34.12202 1.000 92.38106  ? 7   VAL A C   1 
ATOM   10   O O   . VAL A 1 13  ? -7.52044  66.31825 34.09344 1.000 99.95127  ? 7   VAL A O   1 
ATOM   11   C CB  . VAL A 1 13  ? -5.89232  64.38470 36.03640 1.000 104.77155 ? 7   VAL A CB  1 
ATOM   12   C CG1 . VAL A 1 13  ? -4.63175  63.61103 36.38614 1.000 105.23163 ? 7   VAL A CG1 1 
ATOM   13   C CG2 . VAL A 1 13  ? -5.83670  65.77898 36.64011 1.000 119.98445 ? 7   VAL A CG2 1 
ATOM   14   N N   . PRO A 1 14  ? -8.41593  64.28773 33.80203 1.000 80.62823  ? 8   PRO A N   1 
ATOM   15   C CA  . PRO A 1 14  ? -9.69910  64.86709 33.39012 1.000 86.48745  ? 8   PRO A CA  1 
ATOM   16   C C   . PRO A 1 14  ? -10.46294 65.43276 34.57624 1.000 93.41280  ? 8   PRO A C   1 
ATOM   17   O O   . PRO A 1 14  ? -10.50434 64.83616 35.65503 1.000 86.48008  ? 8   PRO A O   1 
ATOM   18   C CB  . PRO A 1 14  ? -10.43834 63.67920 32.76501 1.000 84.61467  ? 8   PRO A CB  1 
ATOM   19   C CG  . PRO A 1 14  ? -9.87119  62.49047 33.46207 1.000 91.39870  ? 8   PRO A CG  1 
ATOM   20   C CD  . PRO A 1 14  ? -8.42464  62.81640 33.73925 1.000 88.30311  ? 8   PRO A CD  1 
ATOM   21   N N   . ALA A 1 15  ? -11.07222 66.59761 34.36235 1.000 87.37410  ? 9   ALA A N   1 
ATOM   22   C CA  . ALA A 1 15  ? -11.88302 67.22036 35.39922 1.000 79.66547  ? 9   ALA A CA  1 
ATOM   23   C C   . ALA A 1 15  ? -13.04979 66.31437 35.76760 1.000 89.88760  ? 9   ALA A C   1 
ATOM   24   O O   . ALA A 1 15  ? -13.73885 65.77937 34.89401 1.000 82.64948  ? 9   ALA A O   1 
ATOM   25   C CB  . ALA A 1 15  ? -12.39298 68.58069 34.92640 1.000 85.48071  ? 9   ALA A CB  1 
ATOM   26   N N   . GLY A 1 16  ? -13.26451 66.13629 37.06786 1.000 80.65533  ? 10  GLY A N   1 
ATOM   27   C CA  . GLY A 1 16  ? -14.29033 65.23779 37.54580 1.000 89.33439  ? 10  GLY A CA  1 
ATOM   28   C C   . GLY A 1 16  ? -13.90423 63.77621 37.56284 1.000 77.07626  ? 10  GLY A C   1 
ATOM   29   O O   . GLY A 1 16  ? -14.71124 62.94935 38.00478 1.000 81.52922  ? 10  GLY A O   1 
ATOM   30   N N   . ALA A 1 17  ? -12.70478 63.43156 37.09007 1.000 76.59071  ? 11  ALA A N   1 
ATOM   31   C CA  . ALA A 1 17  ? -12.19810 62.05796 37.12380 1.000 86.45019  ? 11  ALA A CA  1 
ATOM   32   C C   . ALA A 1 17  ? -13.16012 61.08614 36.44346 1.000 92.62663  ? 11  ALA A C   1 
ATOM   33   O O   . ALA A 1 17  ? -13.39247 59.97293 36.92073 1.000 82.63643  ? 11  ALA A O   1 
ATOM   34   C CB  . ALA A 1 17  ? -11.90166 61.61787 38.55881 1.000 85.22201  ? 11  ALA A CB  1 
ATOM   35   N N   . LYS A 1 18  ? -13.73120 61.52080 35.31731 1.000 91.63300  ? 12  LYS A N   1 
ATOM   36   C CA  . LYS A 1 18  ? -14.61854 60.69234 34.49763 1.000 79.53493  ? 12  LYS A CA  1 
ATOM   37   C C   . LYS A 1 18  ? -15.79407 60.14377 35.30143 1.000 81.52043  ? 12  LYS A C   1 
ATOM   38   O O   . LYS A 1 18  ? -16.29529 59.05154 35.02250 1.000 82.13940  ? 12  LYS A O   1 
ATOM   39   C CB  . LYS A 1 18  ? -13.84618 59.55088 33.82806 1.000 74.43043  ? 12  LYS A CB  1 
ATOM   40   C CG  . LYS A 1 18  ? -12.71695 60.02986 32.92185 1.000 78.53537  ? 12  LYS A CG  1 
ATOM   41   C CD  . LYS A 1 18  ? -11.88182 58.87149 32.39774 1.000 108.00360 ? 12  LYS A CD  1 
ATOM   42   C CE  . LYS A 1 18  ? -12.66747 57.99685 31.43111 1.000 115.49692 ? 12  LYS A CE  1 
ATOM   43   N NZ  . LYS A 1 18  ? -12.99911 58.69716 30.15963 1.000 108.16842 ? 12  LYS A NZ  1 
ATOM   44   N N   . CYS A 1 19  ? -16.24455 60.89980 36.29920 1.000 82.48785  ? 13  CYS A N   1 
ATOM   45   C CA  . CYS A 1 19  ? -17.34991 60.48397 37.14908 1.000 75.74697  ? 13  CYS A CA  1 
ATOM   46   C C   . CYS A 1 19  ? -18.68296 60.90177 36.54408 1.000 87.52489  ? 13  CYS A C   1 
ATOM   47   O O   . CYS A 1 19  ? -18.80756 61.98184 35.95888 1.000 88.49187  ? 13  CYS A O   1 
ATOM   48   C CB  . CYS A 1 19  ? -17.21181 61.08187 38.54972 1.000 79.54930  ? 13  CYS A CB  1 
ATOM   49   S SG  . CYS A 1 19  ? -15.86518 60.39546 39.53704 1.000 82.70641  ? 13  CYS A SG  1 
ATOM   50   N N   . ARG A 1 20  ? -19.67916 60.03459 36.69670 1.000 84.96398  ? 14  ARG A N   1 
ATOM   51   C CA  . ARG A 1 20  ? -21.03681 60.30306 36.25440 1.000 75.42147  ? 14  ARG A CA  1 
ATOM   52   C C   . ARG A 1 20  ? -21.99728 59.74401 37.29118 1.000 73.55391  ? 14  ARG A C   1 
ATOM   53   O O   . ARG A 1 20  ? -21.70486 58.74489 37.95339 1.000 78.91114  ? 14  ARG A O   1 
ATOM   54   C CB  . ARG A 1 20  ? -21.31035 59.68828 34.87811 1.000 73.23905  ? 14  ARG A CB  1 
ATOM   55   C CG  . ARG A 1 20  ? -21.02141 58.20250 34.81019 1.000 76.96390  ? 14  ARG A CG  1 
ATOM   56   C CD  . ARG A 1 20  ? -21.03401 57.70444 33.37861 1.000 101.04433 ? 14  ARG A CD  1 
ATOM   57   N NE  . ARG A 1 20  ? -22.28441 58.02750 32.70472 1.000 101.93722 ? 14  ARG A NE  1 
ATOM   58   C CZ  . ARG A 1 20  ? -22.60992 57.59948 31.49374 1.000 91.71497  ? 14  ARG A CZ  1 
ATOM   59   N NH1 . ARG A 1 20  ? -21.80357 56.81292 30.80006 1.000 99.63021  ? 14  ARG A NH1 1 
ATOM   60   N NH2 . ARG A 1 20  ? -23.77403 57.96830 30.96661 1.000 85.87191  ? 14  ARG A NH2 1 
ATOM   61   N N   . LEU A 1 21  ? -23.14276 60.40009 37.43482 1.000 75.61759  ? 15  LEU A N   1 
ATOM   62   C CA  . LEU A 1 21  ? -24.09314 59.99480 38.45782 1.000 78.96621  ? 15  LEU A CA  1 
ATOM   63   C C   . LEU A 1 21  ? -24.81684 58.71441 38.05482 1.000 67.75935  ? 15  LEU A C   1 
ATOM   64   O O   . LEU A 1 21  ? -24.99845 58.41620 36.87137 1.000 73.14340  ? 15  LEU A O   1 
ATOM   65   C CB  . LEU A 1 21  ? -25.09918 61.11271 38.72433 1.000 80.38703  ? 15  LEU A CB  1 
ATOM   66   C CG  . LEU A 1 21  ? -24.49024 62.37576 39.33615 1.000 73.38895  ? 15  LEU A CG  1 
ATOM   67   C CD1 . LEU A 1 21  ? -25.57161 63.37120 39.71748 1.000 66.03524  ? 15  LEU A CD1 1 
ATOM   68   C CD2 . LEU A 1 21  ? -23.63743 62.01973 40.54180 1.000 65.76904  ? 15  LEU A CD2 1 
ATOM   69   N N   . VAL A 1 22  ? -25.21660 57.94724 39.06471 1.000 71.31967  ? 16  VAL A N   1 
ATOM   70   C CA  . VAL A 1 22  ? -25.93019 56.68820 38.88591 1.000 63.63931  ? 16  VAL A CA  1 
ATOM   71   C C   . VAL A 1 22  ? -27.03578 56.63460 39.92703 1.000 64.25955  ? 16  VAL A C   1 
ATOM   72   O O   . VAL A 1 22  ? -26.79851 56.93713 41.10114 1.000 79.19825  ? 16  VAL A O   1 
ATOM   73   C CB  . VAL A 1 22  ? -24.99593 55.46873 39.02924 1.000 60.12141  ? 16  VAL A CB  1 
ATOM   74   C CG1 . VAL A 1 22  ? -25.79732 54.17944 39.04783 1.000 55.13314  ? 16  VAL A CG1 1 
ATOM   75   C CG2 . VAL A 1 22  ? -23.97339 55.43945 37.90524 1.000 66.11991  ? 16  VAL A CG2 1 
ATOM   76   N N   . GLU A 1 23  ? -28.24181 56.25722 39.50880 1.000 60.04536  ? 17  GLU A N   1 
ATOM   77   C CA  . GLU A 1 23  ? -29.33738 56.17363 40.46150 1.000 76.21081  ? 17  GLU A CA  1 
ATOM   78   C C   . GLU A 1 23  ? -30.32361 55.09480 40.04173 1.000 70.68666  ? 17  GLU A C   1 
ATOM   79   O O   . GLU A 1 23  ? -30.39329 54.70151 38.87485 1.000 59.38004  ? 17  GLU A O   1 
ATOM   80   C CB  . GLU A 1 23  ? -30.04885 57.52297 40.62035 1.000 81.89948  ? 17  GLU A CB  1 
ATOM   81   C CG  . GLU A 1 23  ? -30.33367 58.25934 39.32979 1.000 53.79140  ? 17  GLU A CG  1 
ATOM   82   C CD  . GLU A 1 23  ? -31.02296 59.58889 39.57696 1.000 79.79442  ? 17  GLU A CD  1 
ATOM   83   O OE1 . GLU A 1 23  ? -31.29101 59.91126 40.75438 1.000 73.99578  ? 17  GLU A OE1 1 
ATOM   84   O OE2 . GLU A 1 23  ? -31.29770 60.31112 38.59811 1.000 82.87427  ? 17  GLU A OE2 1 
ATOM   85   N N   . THR A 1 24  ? -31.07919 54.61348 41.02856 1.000 69.20867  ? 18  THR A N   1 
ATOM   86   C CA  . THR A 1 24  ? -32.16969 53.66818 40.81920 1.000 60.21457  ? 18  THR A CA  1 
ATOM   87   C C   . THR A 1 24  ? -33.47890 54.44143 40.92484 1.000 68.99974  ? 18  THR A C   1 
ATOM   88   O O   . THR A 1 24  ? -33.80381 54.97924 41.98795 1.000 78.56843  ? 18  THR A O   1 
ATOM   89   C CB  . THR A 1 24  ? -32.12490 52.53849 41.84649 1.000 62.42921  ? 18  THR A CB  1 
ATOM   90   O OG1 . THR A 1 24  ? -30.81846 51.95402 41.86612 1.000 69.82754  ? 18  THR A OG1 1 
ATOM   91   C CG2 . THR A 1 24  ? -33.14982 51.46523 41.50765 1.000 55.34305  ? 18  THR A CG2 1 
ATOM   92   N N   . LEU A 1 25  ? -34.22659 54.50445 39.82328 1.000 72.86642  ? 19  LEU A N   1 
ATOM   93   C CA  . LEU A 1 25  ? -35.49267 55.23329 39.76345 1.000 67.57549  ? 19  LEU A CA  1 
ATOM   94   C C   . LEU A 1 25  ? -36.60253 54.23133 39.47830 1.000 65.61564  ? 19  LEU A C   1 
ATOM   95   O O   . LEU A 1 25  ? -36.91173 53.94544 38.31047 1.000 77.46012  ? 19  LEU A O   1 
ATOM   96   C CB  . LEU A 1 25  ? -35.44189 56.33502 38.70764 1.000 67.99438  ? 19  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 25  ? -34.27007 57.30703 38.87540 1.000 61.94238  ? 19  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 25  ? -34.34031 58.44284 37.86136 1.000 66.58949  ? 19  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 25  ? -34.20481 57.84801 40.30210 1.000 60.27829  ? 19  LEU A CD2 1 
ATOM   100  N N   . PRO A 1 26  ? -37.22152 53.66943 40.51580 1.000 75.28343  ? 20  PRO A N   1 
ATOM   101  C CA  . PRO A 1 26  ? -38.22272 52.61829 40.30415 1.000 66.91360  ? 20  PRO A CA  1 
ATOM   102  C C   . PRO A 1 26  ? -39.39458 53.10126 39.46395 1.000 74.71293  ? 20  PRO A C   1 
ATOM   103  O O   . PRO A 1 26  ? -39.72392 54.28956 39.43487 1.000 88.42802  ? 20  PRO A O   1 
ATOM   104  C CB  . PRO A 1 26  ? -38.66574 52.26231 41.72721 1.000 72.17695  ? 20  PRO A CB  1 
ATOM   105  C CG  . PRO A 1 26  ? -37.50845 52.64885 42.58396 1.000 63.81395  ? 20  PRO A CG  1 
ATOM   106  C CD  . PRO A 1 26  ? -36.91306 53.86450 41.94189 1.000 64.21950  ? 20  PRO A CD  1 
ATOM   107  N N   . GLU A 1 27  ? -40.02772 52.14661 38.77655 1.000 73.71244  ? 21  GLU A N   1 
ATOM   108  C CA  . GLU A 1 27  ? -41.12017 52.47703 37.86661 1.000 69.54685  ? 21  GLU A CA  1 
ATOM   109  C C   . GLU A 1 27  ? -42.31122 53.07154 38.60806 1.000 61.82612  ? 21  GLU A C   1 
ATOM   110  O O   . GLU A 1 27  ? -42.98514 53.97132 38.09203 1.000 87.09977  ? 21  GLU A O   1 
ATOM   111  C CB  . GLU A 1 27  ? -41.54882 51.23350 37.08686 1.000 65.90913  ? 21  GLU A CB  1 
ATOM   112  C CG  . GLU A 1 27  ? -40.60668 50.82964 35.96511 1.000 83.18355  ? 21  GLU A CG  1 
ATOM   113  C CD  . GLU A 1 27  ? -39.39482 50.07246 36.45822 1.000 75.55023  ? 21  GLU A CD  1 
ATOM   114  O OE1 . GLU A 1 27  ? -39.39682 49.64669 37.63123 1.000 81.96860  ? 21  GLU A OE1 1 
ATOM   115  O OE2 . GLU A 1 27  ? -38.43944 49.90427 35.67217 1.000 69.46387  ? 21  GLU A OE2 1 
ATOM   116  N N   . ASN A 1 28  ? -42.59024 52.58256 39.81484 1.000 72.59172  ? 22  ASN A N   1 
ATOM   117  C CA  . ASN A 1 28  ? -43.73847 53.04209 40.58768 1.000 87.45065  ? 22  ASN A CA  1 
ATOM   118  C C   . ASN A 1 28  ? -43.50157 54.38471 41.27737 1.000 84.94333  ? 22  ASN A C   1 
ATOM   119  O O   . ASN A 1 28  ? -44.34011 54.80336 42.08250 1.000 94.47454  ? 22  ASN A O   1 
ATOM   120  C CB  . ASN A 1 28  ? -44.13589 51.98291 41.62289 1.000 70.63167  ? 22  ASN A CB  1 
ATOM   121  C CG  . ASN A 1 28  ? -42.95638 51.48946 42.43951 1.000 118.96359 ? 22  ASN A CG  1 
ATOM   122  O OD1 . ASN A 1 28  ? -41.89038 52.10531 42.44975 1.000 123.68232 ? 22  ASN A OD1 1 
ATOM   123  N ND2 . ASN A 1 28  ? -43.14308 50.37132 43.13091 1.000 141.08785 ? 22  ASN A ND2 1 
ATOM   124  N N   . MET A 1 29  ? -42.39493 55.06426 40.98490 1.000 79.55608  ? 23  MET A N   1 
ATOM   125  C CA  . MET A 1 29  ? -42.11059 56.38316 41.52766 1.000 69.54387  ? 23  MET A CA  1 
ATOM   126  C C   . MET A 1 29  ? -41.95193 57.37959 40.38610 1.000 76.40725  ? 23  MET A C   1 
ATOM   127  O O   . MET A 1 29  ? -41.63766 57.01075 39.25129 1.000 91.08564  ? 23  MET A O   1 
ATOM   128  C CB  . MET A 1 29  ? -40.85012 56.36673 42.39967 1.000 83.72629  ? 23  MET A CB  1 
ATOM   129  C CG  . MET A 1 29  ? -40.89137 55.33092 43.51170 1.000 72.28914  ? 23  MET A CG  1 
ATOM   130  S SD  . MET A 1 29  ? -39.41408 55.34779 44.54235 1.000 77.22958  ? 23  MET A SD  1 
ATOM   131  C CE  . MET A 1 29  ? -39.66960 53.87555 45.52701 1.000 61.24410  ? 23  MET A CE  1 
ATOM   132  N N   . ASP A 1 30  ? -42.17185 58.65512 40.69664 1.000 67.55950  ? 24  ASP A N   1 
ATOM   133  C CA  . ASP A 1 30  ? -42.21576 59.69628 39.67757 1.000 78.97716  ? 24  ASP A CA  1 
ATOM   134  C C   . ASP A 1 30  ? -40.84177 60.23900 39.30612 1.000 79.86857  ? 24  ASP A C   1 
ATOM   135  O O   . ASP A 1 30  ? -40.76015 61.16989 38.49813 1.000 91.98275  ? 24  ASP A O   1 
ATOM   136  C CB  . ASP A 1 30  ? -43.12194 60.84993 40.13338 1.000 85.74110  ? 24  ASP A CB  1 
ATOM   137  C CG  . ASP A 1 30  ? -42.59215 61.57411 41.36268 1.000 86.78555  ? 24  ASP A CG  1 
ATOM   138  O OD1 . ASP A 1 30  ? -41.55436 61.15963 41.92140 1.000 93.34150  ? 24  ASP A OD1 1 
ATOM   139  O OD2 . ASP A 1 30  ? -43.22480 62.56931 41.77252 1.000 93.07633  ? 24  ASP A OD2 1 
ATOM   140  N N   . PHE A 1 31  ? -39.76884 59.69325 39.87216 1.000 75.82470  ? 25  PHE A N   1 
ATOM   141  C CA  . PHE A 1 31  ? -38.43392 60.17955 39.55271 1.000 73.49885  ? 25  PHE A CA  1 
ATOM   142  C C   . PHE A 1 31  ? -38.03222 59.74381 38.15069 1.000 73.39330  ? 25  PHE A C   1 
ATOM   143  O O   . PHE A 1 31  ? -38.15615 58.56857 37.79235 1.000 85.50839  ? 25  PHE A O   1 
ATOM   144  C CB  . PHE A 1 31  ? -37.41531 59.66532 40.56687 1.000 69.14422  ? 25  PHE A CB  1 
ATOM   145  C CG  . PHE A 1 31  ? -37.75350 59.99528 41.98769 1.000 69.19319  ? 25  PHE A CG  1 
ATOM   146  C CD1 . PHE A 1 31  ? -37.63043 61.29066 42.46159 1.000 76.35441  ? 25  PHE A CD1 1 
ATOM   147  C CD2 . PHE A 1 31  ? -38.18148 59.00562 42.85558 1.000 70.05540  ? 25  PHE A CD2 1 
ATOM   148  C CE1 . PHE A 1 31  ? -37.93903 61.59381 43.77529 1.000 73.01478  ? 25  PHE A CE1 1 
ATOM   149  C CE2 . PHE A 1 31  ? -38.48947 59.30111 44.16540 1.000 75.62383  ? 25  PHE A CE2 1 
ATOM   150  C CZ  . PHE A 1 31  ? -38.36882 60.59652 44.62773 1.000 73.86160  ? 25  PHE A CZ  1 
ATOM   151  N N   . ARG A 1 32  ? -37.54969 60.69693 37.35974 1.000 68.43857  ? 26  ARG A N   1 
ATOM   152  C CA  . ARG A 1 32  ? -37.00989 60.43141 36.03667 1.000 73.58674  ? 26  ARG A CA  1 
ATOM   153  C C   . ARG A 1 32  ? -35.67109 61.13948 35.89915 1.000 71.70210  ? 26  ARG A C   1 
ATOM   154  O O   . ARG A 1 32  ? -35.42589 62.15964 36.54882 1.000 75.63032  ? 26  ARG A O   1 
ATOM   155  C CB  . ARG A 1 32  ? -37.96343 60.90420 34.92743 1.000 72.40421  ? 26  ARG A CB  1 
ATOM   156  C CG  . ARG A 1 32  ? -39.34022 60.25164 34.95131 1.000 87.83478  ? 26  ARG A CG  1 
ATOM   157  C CD  . ARG A 1 32  ? -39.24880 58.75319 34.70725 1.000 104.61773 ? 26  ARG A CD  1 
ATOM   158  N NE  . ARG A 1 32  ? -40.55984 58.13874 34.53099 1.000 110.69411 ? 26  ARG A NE  1 
ATOM   159  C CZ  . ARG A 1 32  ? -41.23383 57.51555 35.48827 1.000 112.07551 ? 26  ARG A CZ  1 
ATOM   160  N NH1 . ARG A 1 32  ? -40.75274 57.40893 36.71608 1.000 102.63984 ? 26  ARG A NH1 1 
ATOM   161  N NH2 . ARG A 1 32  ? -42.41859 56.98122 35.20500 1.000 121.99986 ? 26  ARG A NH2 1 
ATOM   162  N N   . SER A 1 33  ? -34.80390 60.58481 35.05580 1.000 70.56983  ? 27  SER A N   1 
ATOM   163  C CA  . SER A 1 33  ? -33.54177 61.22980 34.71005 1.000 69.17879  ? 27  SER A CA  1 
ATOM   164  C C   . SER A 1 33  ? -32.92835 60.48677 33.53308 1.000 78.45187  ? 27  SER A C   1 
ATOM   165  O O   . SER A 1 33  ? -33.35590 59.38644 33.17358 1.000 86.20968  ? 27  SER A O   1 
ATOM   166  C CB  . SER A 1 33  ? -32.56315 61.26057 35.88612 1.000 71.24634  ? 27  SER A CB  1 
ATOM   167  O OG  . SER A 1 33  ? -31.94288 60.00029 36.06637 1.000 78.56725  ? 27  SER A OG  1 
ATOM   168  N N   . ASP A 1 34  ? -31.91506 61.10946 32.93594 1.000 78.11480  ? 28  ASP A N   1 
ATOM   169  C CA  . ASP A 1 34  ? -31.13956 60.50048 31.86653 1.000 77.29299  ? 28  ASP A CA  1 
ATOM   170  C C   . ASP A 1 34  ? -29.84811 59.88094 32.37510 1.000 76.53100  ? 28  ASP A C   1 
ATOM   171  O O   . ASP A 1 34  ? -28.98376 59.52133 31.57022 1.000 87.41831  ? 28  ASP A O   1 
ATOM   172  C CB  . ASP A 1 34  ? -30.82765 61.53300 30.78313 1.000 75.71393  ? 28  ASP A CB  1 
ATOM   173  C CG  . ASP A 1 34  ? -32.07435 62.17492 30.21451 1.000 90.03745  ? 28  ASP A CG  1 
ATOM   174  O OD1 . ASP A 1 34  ? -33.14614 61.53321 30.24618 1.000 99.63602  ? 28  ASP A OD1 1 
ATOM   175  O OD2 . ASP A 1 34  ? -31.97987 63.32285 29.73245 1.000 103.89545 ? 28  ASP A OD2 1 
ATOM   176  N N   . HIS A 1 35  ? -29.69607 59.75434 33.68892 1.000 85.55940  ? 29  HIS A N   1 
ATOM   177  C CA  . HIS A 1 35  ? -28.47141 59.21183 34.24626 1.000 67.94580  ? 29  HIS A CA  1 
ATOM   178  C C   . HIS A 1 35  ? -28.40482 57.70129 34.04413 1.000 70.38658  ? 29  HIS A C   1 
ATOM   179  O O   . HIS A 1 35  ? -29.40403 57.03127 33.76849 1.000 87.51402  ? 29  HIS A O   1 
ATOM   180  C CB  . HIS A 1 35  ? -28.36425 59.54285 35.73465 1.000 77.59586  ? 29  HIS A CB  1 
ATOM   181  C CG  . HIS A 1 35  ? -28.24152 61.00648 36.02154 1.000 68.89109  ? 29  HIS A CG  1 
ATOM   182  N ND1 . HIS A 1 35  ? -27.16121 61.75735 35.61119 1.000 78.42868  ? 29  HIS A ND1 1 
ATOM   183  C CD2 . HIS A 1 35  ? -29.06011 61.85686 36.68491 1.000 80.01292  ? 29  HIS A CD2 1 
ATOM   184  C CE1 . HIS A 1 35  ? -27.32123 63.00803 36.00560 1.000 78.83135  ? 29  HIS A CE1 1 
ATOM   185  N NE2 . HIS A 1 35  ? -28.46535 63.09523 36.65973 1.000 68.79571  ? 29  HIS A NE2 1 
ATOM   186  N N   . LEU A 1 36  ? -27.19375 57.17396 34.17772 1.000 72.48276  ? 30  LEU A N   1 
ATOM   187  C CA  . LEU A 1 36  ? -26.97231 55.73700 34.13073 1.000 63.37945  ? 30  LEU A CA  1 
ATOM   188  C C   . LEU A 1 36  ? -27.69421 55.06359 35.29193 1.000 72.20145  ? 30  LEU A C   1 
ATOM   189  O O   . LEU A 1 36  ? -27.47571 55.41534 36.45490 1.000 72.90169  ? 30  LEU A O   1 
ATOM   190  C CB  . LEU A 1 36  ? -25.47083 55.46336 34.19432 1.000 71.00191  ? 30  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 36  ? -24.92040 54.06336 33.94456 1.000 80.27301  ? 30  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 36  ? -25.08569 53.68547 32.48517 1.000 68.06135  ? 30  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 36  ? -23.45731 54.00837 34.35678 1.000 70.53515  ? 30  LEU A CD2 1 
ATOM   194  N N   . THR A 1 37  ? -28.56696 54.10853 34.98537 1.000 72.45375  ? 31  THR A N   1 
ATOM   195  C CA  . THR A 1 37  ? -29.24550 53.40574 36.06178 1.000 66.05586  ? 31  THR A CA  1 
ATOM   196  C C   . THR A 1 37  ? -28.28350 52.44475 36.75228 1.000 72.11307  ? 31  THR A C   1 
ATOM   197  O O   . THR A 1 37  ? -27.27976 52.01024 36.18117 1.000 78.46428  ? 31  THR A O   1 
ATOM   198  C CB  . THR A 1 37  ? -30.46642 52.63971 35.54638 1.000 60.69782  ? 31  THR A CB  1 
ATOM   199  O OG1 . THR A 1 37  ? -30.04195 51.53524 34.73961 1.000 72.43459  ? 31  THR A OG1 1 
ATOM   200  C CG2 . THR A 1 37  ? -31.35791 53.54974 34.72198 1.000 69.61065  ? 31  THR A CG2 1 
ATOM   201  N N   . THR A 1 38  ? -28.59981 52.12674 38.00957 1.000 65.40114  ? 32  THR A N   1 
ATOM   202  C CA  . THR A 1 38  ? -27.79407 51.16700 38.75711 1.000 58.79077  ? 32  THR A CA  1 
ATOM   203  C C   . THR A 1 38  ? -27.70625 49.83565 38.02316 1.000 70.17835  ? 32  THR A C   1 
ATOM   204  O O   . THR A 1 38  ? -26.63712 49.21595 37.96701 1.000 68.63348  ? 32  THR A O   1 
ATOM   205  C CB  . THR A 1 38  ? -28.38200 50.96865 40.15300 1.000 62.91083  ? 32  THR A CB  1 
ATOM   206  O OG1 . THR A 1 38  ? -28.56663 52.24420 40.78001 1.000 77.78173  ? 32  THR A OG1 1 
ATOM   207  C CG2 . THR A 1 38  ? -27.45798 50.11923 41.00772 1.000 54.55500  ? 32  THR A CG2 1 
ATOM   208  N N   . PHE A 1 39  ? -28.82213 49.38558 37.44734 1.000 74.41032  ? 33  PHE A N   1 
ATOM   209  C CA  . PHE A 1 39  ? -28.82062 48.14308 36.68272 1.000 64.18797  ? 33  PHE A CA  1 
ATOM   210  C C   . PHE A 1 39  ? -27.87656 48.23497 35.48982 1.000 72.41734  ? 33  PHE A C   1 
ATOM   211  O O   . PHE A 1 39  ? -27.05930 47.33601 35.25745 1.000 78.05333  ? 33  PHE A O   1 
ATOM   212  C CB  . PHE A 1 39  ? -30.24240 47.82002 36.22877 1.000 59.84236  ? 33  PHE A CB  1 
ATOM   213  C CG  . PHE A 1 39  ? -30.34110 46.60350 35.36377 1.000 67.80130  ? 33  PHE A CG  1 
ATOM   214  C CD1 . PHE A 1 39  ? -30.22251 45.33756 35.91101 1.000 71.93487  ? 33  PHE A CD1 1 
ATOM   215  C CD2 . PHE A 1 39  ? -30.57040 46.72401 34.00397 1.000 59.88299  ? 33  PHE A CD2 1 
ATOM   216  C CE1 . PHE A 1 39  ? -30.32093 44.21305 35.11604 1.000 69.17231  ? 33  PHE A CE1 1 
ATOM   217  C CE2 . PHE A 1 39  ? -30.67035 45.60388 33.20333 1.000 62.79086  ? 33  PHE A CE2 1 
ATOM   218  C CZ  . PHE A 1 39  ? -30.54550 44.34647 33.75987 1.000 63.51596  ? 33  PHE A CZ  1 
ATOM   219  N N   . GLU A 1 40  ? -27.97916 49.31981 34.71722 1.000 76.96357  ? 34  GLU A N   1 
ATOM   220  C CA  . GLU A 1 40  ? -27.05385 49.53047 33.60804 1.000 66.36847  ? 34  GLU A CA  1 
ATOM   221  C C   . GLU A 1 40  ? -25.61205 49.58086 34.09489 1.000 74.76274  ? 34  GLU A C   1 
ATOM   222  O O   . GLU A 1 40  ? -24.70843 49.04310 33.44303 1.000 71.62140  ? 34  GLU A O   1 
ATOM   223  C CB  . GLU A 1 40  ? -27.40149 50.82151 32.86622 1.000 81.94993  ? 34  GLU A CB  1 
ATOM   224  C CG  . GLU A 1 40  ? -28.57787 50.72188 31.91256 1.000 83.96517  ? 34  GLU A CG  1 
ATOM   225  C CD  . GLU A 1 40  ? -28.87978 52.04800 31.23640 1.000 110.56903 ? 34  GLU A CD  1 
ATOM   226  O OE1 . GLU A 1 40  ? -28.62709 53.10324 31.85736 1.000 87.29393  ? 34  GLU A OE1 1 
ATOM   227  O OE2 . GLU A 1 40  ? -29.36020 52.03775 30.08320 1.000 113.51156 ? 34  GLU A OE2 1 
ATOM   228  N N   . CYS A 1 41  ? -25.37884 50.22139 35.24257 1.000 75.30567  ? 35  CYS A N   1 
ATOM   229  C CA  . CYS A 1 41  ? -24.01721 50.37841 35.74288 1.000 65.41051  ? 35  CYS A CA  1 
ATOM   230  C C   . CYS A 1 41  ? -23.39805 49.02989 36.08908 1.000 66.18598  ? 35  CYS A C   1 
ATOM   231  O O   . CYS A 1 41  ? -22.29895 48.70176 35.62717 1.000 74.13728  ? 35  CYS A O   1 
ATOM   232  C CB  . CYS A 1 41  ? -24.01191 51.30470 36.95803 1.000 77.37807  ? 35  CYS A CB  1 
ATOM   233  S SG  . CYS A 1 41  ? -22.37599 51.57511 37.66797 1.000 77.92287  ? 35  CYS A SG  1 
ATOM   234  N N   . PHE A 1 42  ? -24.09478 48.22938 36.90085 1.000 73.06445  ? 36  PHE A N   1 
ATOM   235  C CA  . PHE A 1 42  ? -23.56495 46.92260 37.27934 1.000 63.92345  ? 36  PHE A CA  1 
ATOM   236  C C   . PHE A 1 42  ? -23.39346 46.01481 36.06797 1.000 66.63260  ? 36  PHE A C   1 
ATOM   237  O O   . PHE A 1 42  ? -22.50446 45.15611 36.05722 1.000 77.74434  ? 36  PHE A O   1 
ATOM   238  C CB  . PHE A 1 42  ? -24.47568 46.26008 38.31462 1.000 62.83085  ? 36  PHE A CB  1 
ATOM   239  C CG  . PHE A 1 42  ? -24.50769 46.96634 39.64423 1.000 60.23109  ? 36  PHE A CG  1 
ATOM   240  C CD1 . PHE A 1 42  ? -23.57510 47.94277 39.95555 1.000 67.64710  ? 36  PHE A CD1 1 
ATOM   241  C CD2 . PHE A 1 42  ? -25.46925 46.64333 40.58731 1.000 66.16079  ? 36  PHE A CD2 1 
ATOM   242  C CE1 . PHE A 1 42  ? -23.60685 48.58815 41.17872 1.000 61.38276  ? 36  PHE A CE1 1 
ATOM   243  C CE2 . PHE A 1 42  ? -25.50451 47.28195 41.81172 1.000 62.88008  ? 36  PHE A CE2 1 
ATOM   244  C CZ  . PHE A 1 42  ? -24.57211 48.25649 42.10798 1.000 61.85664  ? 36  PHE A CZ  1 
ATOM   245  N N   . ASN A 1 43  ? -24.22946 46.18706 35.04161 1.000 69.32997  ? 37  ASN A N   1 
ATOM   246  C CA  . ASN A 1 43  ? -24.06106 45.41397 33.81563 1.000 67.49977  ? 37  ASN A CA  1 
ATOM   247  C C   . ASN A 1 43  ? -22.78721 45.81411 33.08145 1.000 76.09625  ? 37  ASN A C   1 
ATOM   248  O O   . ASN A 1 43  ? -22.08751 44.95731 32.52845 1.000 84.65947  ? 37  ASN A O   1 
ATOM   249  C CB  . ASN A 1 43  ? -25.28057 45.59194 32.91170 1.000 79.38885  ? 37  ASN A CB  1 
ATOM   250  C CG  . ASN A 1 43  ? -26.15207 44.35513 32.85861 1.000 92.31954  ? 37  ASN A CG  1 
ATOM   251  O OD1 . ASN A 1 43  ? -25.96344 43.41581 33.62910 1.000 110.13928 ? 37  ASN A OD1 1 
ATOM   252  N ND2 . ASN A 1 43  ? -27.11427 44.34845 31.94437 1.000 122.48151 ? 37  ASN A ND2 1 
ATOM   253  N N   . GLU A 1 44  ? -22.46844 47.11067 33.06829 1.000 75.13347  ? 38  GLU A N   1 
ATOM   254  C CA  . GLU A 1 44  ? -21.26360 47.57185 32.38489 1.000 70.71942  ? 38  GLU A CA  1 
ATOM   255  C C   . GLU A 1 44  ? -20.00541 47.07630 33.08618 1.000 77.22427  ? 38  GLU A C   1 
ATOM   256  O O   . GLU A 1 44  ? -19.03580 46.68189 32.42746 1.000 90.73848  ? 38  GLU A O   1 
ATOM   257  C CB  . GLU A 1 44  ? -21.26377 49.09858 32.30008 1.000 68.41264  ? 38  GLU A CB  1 
ATOM   258  C CG  . GLU A 1 44  ? -20.05989 49.69909 31.59207 1.000 75.36402  ? 38  GLU A CG  1 
ATOM   259  C CD  . GLU A 1 44  ? -20.23186 49.75581 30.08708 1.000 94.62331  ? 38  GLU A CD  1 
ATOM   260  O OE1 . GLU A 1 44  ? -21.18282 49.13143 29.57092 1.000 98.26619  ? 38  GLU A OE1 1 
ATOM   261  O OE2 . GLU A 1 44  ? -19.41944 50.43280 29.42100 1.000 102.34582 ? 38  GLU A OE2 1 
ATOM   262  N N   . ILE A 1 45  ? -20.00423 47.08596 34.42161 1.000 74.51652  ? 39  ILE A N   1 
ATOM   263  C CA  . ILE A 1 45  ? -18.83000 46.64691 35.17160 1.000 67.83029  ? 39  ILE A CA  1 
ATOM   264  C C   . ILE A 1 45  ? -18.54014 45.17540 34.90210 1.000 75.20653  ? 39  ILE A C   1 
ATOM   265  O O   . ILE A 1 45  ? -17.38341 44.77888 34.71175 1.000 93.86756  ? 39  ILE A O   1 
ATOM   266  C CB  . ILE A 1 45  ? -19.02576 46.92093 36.67384 1.000 68.81569  ? 39  ILE A CB  1 
ATOM   267  C CG1 . ILE A 1 45  ? -19.16094 48.42311 36.92544 1.000 68.70465  ? 39  ILE A CG1 1 
ATOM   268  C CG2 . ILE A 1 45  ? -17.87367 46.34328 37.47537 1.000 62.51860  ? 39  ILE A CG2 1 
ATOM   269  C CD1 . ILE A 1 45  ? -19.37811 48.77959 38.37648 1.000 71.30925  ? 39  ILE A CD1 1 
ATOM   270  N N   . ILE A 1 46  ? -19.58348 44.34503 34.87384 1.000 71.77301  ? 40  ILE A N   1 
ATOM   271  C CA  . ILE A 1 46  ? -19.39592 42.91878 34.62284 1.000 73.33868  ? 40  ILE A CA  1 
ATOM   272  C C   . ILE A 1 46  ? -18.97229 42.68202 33.17794 1.000 74.66796  ? 40  ILE A C   1 
ATOM   273  O O   . ILE A 1 46  ? -18.03715 41.92009 32.90379 1.000 81.73374  ? 40  ILE A O   1 
ATOM   274  C CB  . ILE A 1 46  ? -20.68006 42.14228 34.96708 1.000 71.08298  ? 40  ILE A CB  1 
ATOM   275  C CG1 . ILE A 1 46  ? -21.03677 42.32701 36.44242 1.000 72.28344  ? 40  ILE A CG1 1 
ATOM   276  C CG2 . ILE A 1 46  ? -20.51993 40.66593 34.63701 1.000 72.04825  ? 40  ILE A CG2 1 
ATOM   277  C CD1 . ILE A 1 46  ? -22.37911 41.73866 36.82086 1.000 80.66667  ? 40  ILE A CD1 1 
ATOM   278  N N   . THR A 1 47  ? -19.65414 43.33452 32.23313 1.000 78.42669  ? 41  THR A N   1 
ATOM   279  C CA  . THR A 1 47  ? -19.39126 43.09024 30.81761 1.000 75.10669  ? 41  THR A CA  1 
ATOM   280  C C   . THR A 1 47  ? -17.95001 43.42280 30.45114 1.000 74.81971  ? 41  THR A C   1 
ATOM   281  O O   . THR A 1 47  ? -17.31400 42.69620 29.67826 1.000 79.34501  ? 41  THR A O   1 
ATOM   282  C CB  . THR A 1 47  ? -20.36522 43.90158 29.96158 1.000 65.88225  ? 41  THR A CB  1 
ATOM   283  O OG1 . THR A 1 47  ? -21.70880 43.49930 30.25682 1.000 84.14771  ? 41  THR A OG1 1 
ATOM   284  C CG2 . THR A 1 47  ? -20.09297 43.68769 28.48283 1.000 78.28227  ? 41  THR A CG2 1 
ATOM   285  N N   . LEU A 1 48  ? -17.41316 44.50679 31.00590 1.000 85.11321  ? 42  LEU A N   1 
ATOM   286  C CA  . LEU A 1 48  ? -16.06273 44.94752 30.68625 1.000 79.34866  ? 42  LEU A CA  1 
ATOM   287  C C   . LEU A 1 48  ? -14.99205 44.28512 31.54319 1.000 88.30836  ? 42  LEU A C   1 
ATOM   288  O O   . LEU A 1 48  ? -13.80417 44.40738 31.22236 1.000 87.96515  ? 42  LEU A O   1 
ATOM   289  C CB  . LEU A 1 48  ? -15.95642 46.46948 30.83545 1.000 74.36491  ? 42  LEU A CB  1 
ATOM   290  C CG  . LEU A 1 48  ? -16.89148 47.30234 29.95729 1.000 80.38616  ? 42  LEU A CG  1 
ATOM   291  C CD1 . LEU A 1 48  ? -16.63913 48.78509 30.16179 1.000 70.07664  ? 42  LEU A CD1 1 
ATOM   292  C CD2 . LEU A 1 48  ? -16.72417 46.92725 28.49636 1.000 74.29048  ? 42  LEU A CD2 1 
ATOM   293  N N   . ALA A 1 49  ? -15.37700 43.58802 32.60993 1.000 79.47460  ? 43  ALA A N   1 
ATOM   294  C CA  . ALA A 1 49  ? -14.39897 43.03298 33.53647 1.000 79.68455  ? 43  ALA A CA  1 
ATOM   295  C C   . ALA A 1 49  ? -13.52606 41.98972 32.85299 1.000 89.72547  ? 43  ALA A C   1 
ATOM   296  O O   . ALA A 1 49  ? -14.02321 41.11436 32.13772 1.000 94.64891  ? 43  ALA A O   1 
ATOM   297  C CB  . ALA A 1 49  ? -15.10562 42.41570 34.74024 1.000 75.25266  ? 43  ALA A CB  1 
ATOM   298  N N   . LYS A 1 50  ? -12.21453 42.08716 33.08119 1.000 85.26076  ? 44  LYS A N   1 
ATOM   299  C CA  . LYS A 1 50  ? -11.26016 41.13305 32.54076 1.000 86.96648  ? 44  LYS A CA  1 
ATOM   300  C C   . LYS A 1 50  ? -10.40763 40.44485 33.59586 1.000 86.57995  ? 44  LYS A C   1 
ATOM   301  O O   . LYS A 1 50  ? -9.80475  39.41041 33.29003 1.000 83.32869  ? 44  LYS A O   1 
ATOM   302  C CB  . LYS A 1 50  ? -10.32668 41.81738 31.52668 1.000 71.35642  ? 44  LYS A CB  1 
ATOM   303  C CG  . LYS A 1 50  ? -11.04168 42.45272 30.34143 1.000 111.01938 ? 44  LYS A CG  1 
ATOM   304  C CD  . LYS A 1 50  ? -11.91676 41.44330 29.61158 1.000 130.89405 ? 44  LYS A CD  1 
ATOM   305  C CE  . LYS A 1 50  ? -12.76317 42.11845 28.54260 1.000 132.43071 ? 44  LYS A CE  1 
ATOM   306  N NZ  . LYS A 1 50  ? -13.76588 41.18821 27.95110 1.000 123.66334 ? 44  LYS A NZ  1 
ATOM   307  N N   . LYS A 1 51  ? -10.34090 40.97303 34.81847 1.000 78.25688  ? 45  LYS A N   1 
ATOM   308  C CA  . LYS A 1 51  ? -9.47178  40.39160 35.83484 1.000 84.24453  ? 45  LYS A CA  1 
ATOM   309  C C   . LYS A 1 51  ? -10.22756 40.06155 37.11783 1.000 85.65833  ? 45  LYS A C   1 
ATOM   310  O O   . LYS A 1 51  ? -10.22792 38.90649 37.55581 1.000 92.96111  ? 45  LYS A O   1 
ATOM   311  C CB  . LYS A 1 51  ? -8.29821  41.33105 36.13014 1.000 104.27903 ? 45  LYS A CB  1 
ATOM   312  C CG  . LYS A 1 51  ? -7.26643  41.39084 35.00833 1.000 104.82402 ? 45  LYS A CG  1 
ATOM   313  C CD  . LYS A 1 51  ? -6.11339  42.32604 35.34086 1.000 120.22417 ? 45  LYS A CD  1 
ATOM   314  C CE  . LYS A 1 51  ? -6.52888  43.78476 35.24545 1.000 115.21468 ? 45  LYS A CE  1 
ATOM   315  N NZ  . LYS A 1 51  ? -5.37322  44.69689 35.47238 1.000 103.53947 ? 45  LYS A NZ  1 
ATOM   316  N N   . TYR A 1 52  ? -10.87103 41.05399 37.73128 1.000 77.41592  ? 46  TYR A N   1 
ATOM   317  C CA  . TYR A 1 52  ? -11.56875 40.82274 38.98856 1.000 77.12247  ? 46  TYR A CA  1 
ATOM   318  C C   . TYR A 1 52  ? -12.78833 41.72796 39.08052 1.000 77.11408  ? 46  TYR A C   1 
ATOM   319  O O   . TYR A 1 52  ? -12.87837 42.75436 38.40293 1.000 81.59711  ? 46  TYR A O   1 
ATOM   320  C CB  . TYR A 1 52  ? -10.64971 41.05760 40.19853 1.000 73.10024  ? 46  TYR A CB  1 
ATOM   321  C CG  . TYR A 1 52  ? -10.31918 42.51610 40.46039 1.000 79.14984  ? 46  TYR A CG  1 
ATOM   322  C CD1 . TYR A 1 52  ? -11.18555 43.32977 41.18556 1.000 80.10725  ? 46  TYR A CD1 1 
ATOM   323  C CD2 . TYR A 1 52  ? -9.13653  43.07561 39.99570 1.000 80.74593  ? 46  TYR A CD2 1 
ATOM   324  C CE1 . TYR A 1 52  ? -10.89313 44.65670 41.42361 1.000 72.49521  ? 46  TYR A CE1 1 
ATOM   325  C CE2 . TYR A 1 52  ? -8.83166  44.40495 40.23721 1.000 83.12910  ? 46  TYR A CE2 1 
ATOM   326  C CZ  . TYR A 1 52  ? -9.71581  45.18912 40.95136 1.000 80.70880  ? 46  TYR A CZ  1 
ATOM   327  O OH  . TYR A 1 52  ? -9.42718  46.51202 41.19672 1.000 81.86658  ? 46  TYR A OH  1 
ATOM   328  N N   . ILE A 1 53  ? -13.72279 41.33627 39.94621 1.000 75.17491  ? 47  ILE A N   1 
ATOM   329  C CA  . ILE A 1 53  ? -14.84376 42.17677 40.35464 1.000 73.95309  ? 47  ILE A CA  1 
ATOM   330  C C   . ILE A 1 53  ? -14.98069 42.06130 41.86506 1.000 74.75193  ? 47  ILE A C   1 
ATOM   331  O O   . ILE A 1 53  ? -15.27750 40.97750 42.38264 1.000 78.69810  ? 47  ILE A O   1 
ATOM   332  C CB  . ILE A 1 53  ? -16.16157 41.77960 39.67019 1.000 67.49568  ? 47  ILE A CB  1 
ATOM   333  C CG1 . ILE A 1 53  ? -16.05807 41.91084 38.15272 1.000 72.63374  ? 47  ILE A CG1 1 
ATOM   334  C CG2 . ILE A 1 53  ? -17.30499 42.63745 40.18714 1.000 72.47821  ? 47  ILE A CG2 1 
ATOM   335  C CD1 . ILE A 1 53  ? -17.35026 41.58705 37.43694 1.000 70.49685  ? 47  ILE A CD1 1 
ATOM   336  N N   . TYR A 1 54  ? -14.76410 43.16790 42.56812 1.000 70.50878  ? 48  TYR A N   1 
ATOM   337  C CA  . TYR A 1 54  ? -14.87984 43.21738 44.01866 1.000 64.27137  ? 48  TYR A CA  1 
ATOM   338  C C   . TYR A 1 54  ? -16.12124 44.01294 44.39214 1.000 75.06476  ? 48  TYR A C   1 
ATOM   339  O O   . TYR A 1 54  ? -16.31668 45.12975 43.90107 1.000 71.55100  ? 48  TYR A O   1 
ATOM   340  C CB  . TYR A 1 54  ? -13.64000 43.84987 44.65457 1.000 73.28817  ? 48  TYR A CB  1 
ATOM   341  C CG  . TYR A 1 54  ? -12.35515 43.07906 44.44016 1.000 82.04858  ? 48  TYR A CG  1 
ATOM   342  C CD1 . TYR A 1 54  ? -12.37350 41.73746 44.08054 1.000 86.98998  ? 48  TYR A CD1 1 
ATOM   343  C CD2 . TYR A 1 54  ? -11.12136 43.69429 44.60828 1.000 78.73214  ? 48  TYR A CD2 1 
ATOM   344  C CE1 . TYR A 1 54  ? -11.19783 41.03384 43.88640 1.000 82.11665  ? 48  TYR A CE1 1 
ATOM   345  C CE2 . TYR A 1 54  ? -9.94258  43.00024 44.41658 1.000 80.29883  ? 48  TYR A CE2 1 
ATOM   346  C CZ  . TYR A 1 54  ? -9.98561  41.67025 44.05603 1.000 85.71470  ? 48  TYR A CZ  1 
ATOM   347  O OH  . TYR A 1 54  ? -8.81283  40.97343 43.86552 1.000 99.73125  ? 48  TYR A OH  1 
ATOM   348  N N   . ILE A 1 55  ? -16.95322 43.43821 45.25924 1.000 70.84262  ? 49  ILE A N   1 
ATOM   349  C CA  . ILE A 1 55  ? -18.21097 44.04473 45.67811 1.000 68.07142  ? 49  ILE A CA  1 
ATOM   350  C C   . ILE A 1 55  ? -18.26600 44.05218 47.19927 1.000 71.71671  ? 49  ILE A C   1 
ATOM   351  O O   . ILE A 1 55  ? -17.87772 43.07325 47.84630 1.000 74.04826  ? 49  ILE A O   1 
ATOM   352  C CB  . ILE A 1 55  ? -19.42374 43.28878 45.09639 1.000 70.67295  ? 49  ILE A CB  1 
ATOM   353  C CG1 . ILE A 1 55  ? -19.25630 43.08578 43.59002 1.000 66.44999  ? 49  ILE A CG1 1 
ATOM   354  C CG2 . ILE A 1 55  ? -20.71132 44.03702 45.39292 1.000 56.71360  ? 49  ILE A CG2 1 
ATOM   355  C CD1 . ILE A 1 55  ? -20.33998 42.24290 42.96686 1.000 67.78952  ? 49  ILE A CD1 1 
ATOM   356  N N   . ALA A 1 56  ? -18.75777 45.15190 47.77100 1.000 65.43644  ? 50  ALA A N   1 
ATOM   357  C CA  . ALA A 1 56  ? -18.85552 45.29398 49.22074 1.000 56.55609  ? 50  ALA A CA  1 
ATOM   358  C C   . ALA A 1 56  ? -20.13821 46.02886 49.57655 1.000 64.62328  ? 50  ALA A C   1 
ATOM   359  O O   . ALA A 1 56  ? -20.32213 47.18624 49.18748 1.000 71.76521  ? 50  ALA A O   1 
ATOM   360  C CB  . ALA A 1 56  ? -17.64297 46.03814 49.78708 1.000 62.93761  ? 50  ALA A CB  1 
ATOM   361  N N   . SER A 1 57  ? -21.01902 45.35520 50.31255 1.000 52.59029  ? 51  SER A N   1 
ATOM   362  C CA  . SER A 1 57  ? -22.19968 45.98278 50.88577 1.000 69.75016  ? 51  SER A CA  1 
ATOM   363  C C   . SER A 1 57  ? -22.58056 45.20908 52.13941 1.000 68.40322  ? 51  SER A C   1 
ATOM   364  O O   . SER A 1 57  ? -22.10517 44.09601 52.37284 1.000 78.39228  ? 51  SER A O   1 
ATOM   365  C CB  . SER A 1 57  ? -23.36388 46.03233 49.88646 1.000 77.08254  ? 51  SER A CB  1 
ATOM   366  O OG  . SER A 1 57  ? -23.97387 44.76260 49.73203 1.000 71.17243  ? 51  SER A OG  1 
ATOM   367  N N   . PHE A 1 58  ? -23.44209 45.81576 52.95423 1.000 72.11049  ? 52  PHE A N   1 
ATOM   368  C CA  . PHE A 1 58  ? -23.89129 45.18498 54.18972 1.000 61.29620  ? 52  PHE A CA  1 
ATOM   369  C C   . PHE A 1 58  ? -24.58767 43.86183 53.90299 1.000 64.82782  ? 52  PHE A C   1 
ATOM   370  O O   . PHE A 1 58  ? -24.09335 42.79455 54.28115 1.000 73.52593  ? 52  PHE A O   1 
ATOM   371  C CB  . PHE A 1 58  ? -24.82542 46.12357 54.95650 1.000 72.04364  ? 52  PHE A CB  1 
ATOM   372  C CG  . PHE A 1 58  ? -25.43629 45.50616 56.18198 1.000 71.35860  ? 52  PHE A CG  1 
ATOM   373  C CD1 . PHE A 1 58  ? -24.71852 45.42305 57.36278 1.000 75.35025  ? 52  PHE A CD1 1 
ATOM   374  C CD2 . PHE A 1 58  ? -26.73221 45.01781 56.15575 1.000 70.53492  ? 52  PHE A CD2 1 
ATOM   375  C CE1 . PHE A 1 58  ? -25.27953 44.85899 58.49299 1.000 69.46719  ? 52  PHE A CE1 1 
ATOM   376  C CE2 . PHE A 1 58  ? -27.29704 44.45284 57.28022 1.000 69.76901  ? 52  PHE A CE2 1 
ATOM   377  C CZ  . PHE A 1 58  ? -26.57038 44.37361 58.45082 1.000 68.41373  ? 52  PHE A CZ  1 
ATOM   378  N N   . CYS A 1 59  ? -25.73666 43.92808 53.24227 1.000 90.60791  ? 53  CYS A N   1 
ATOM   379  C CA  . CYS A 1 59  ? -26.48874 42.74543 52.86170 1.000 87.45028  ? 53  CYS A CA  1 
ATOM   380  C C   . CYS A 1 59  ? -26.10673 42.31621 51.44815 1.000 75.56816  ? 53  CYS A C   1 
ATOM   381  O O   . CYS A 1 59  ? -25.53222 43.08385 50.67353 1.000 69.30351  ? 53  CYS A O   1 
ATOM   382  C CB  . CYS A 1 59  ? -27.99210 43.02160 52.94611 1.000 64.68296  ? 53  CYS A CB  1 
ATOM   383  S SG  . CYS A 1 59  ? -29.01002 41.55716 53.22752 1.000 113.99997 ? 53  CYS A SG  1 
ATOM   384  N N   . CYS A 1 60  ? -26.42632 41.06661 51.12003 1.000 86.14106  ? 54  CYS A N   1 
ATOM   385  C CA  . CYS A 1 60  ? -26.29686 40.56804 49.75279 1.000 59.50201  ? 54  CYS A CA  1 
ATOM   386  C C   . CYS A 1 60  ? -27.49810 39.68052 49.46934 1.000 72.41516  ? 54  CYS A C   1 
ATOM   387  O O   . CYS A 1 60  ? -27.59231 38.57136 50.00360 1.000 85.72226  ? 54  CYS A O   1 
ATOM   388  C CB  . CYS A 1 60  ? -24.99278 39.80040 49.54500 1.000 63.13912  ? 54  CYS A CB  1 
ATOM   389  S SG  . CYS A 1 60  ? -24.74141 39.26129 47.82882 1.000 84.34815  ? 54  CYS A SG  1 
ATOM   390  N N   . ASN A 1 61  ? -28.41845 40.17048 48.63913 1.000 64.52239  ? 55  ASN A N   1 
ATOM   391  C CA  . ASN A 1 61  ? -29.63421 39.43209 48.29943 1.000 80.76551  ? 55  ASN A CA  1 
ATOM   392  C C   . ASN A 1 61  ? -30.09219 39.85841 46.91293 1.000 66.83980  ? 55  ASN A C   1 
ATOM   393  O O   . ASN A 1 61  ? -31.08136 40.58150 46.75577 1.000 80.47027  ? 55  ASN A O   1 
ATOM   394  C CB  . ASN A 1 61  ? -30.72274 39.67473 49.34347 1.000 63.17765  ? 55  ASN A CB  1 
ATOM   395  C CG  . ASN A 1 61  ? -31.91052 38.75580 49.16843 1.000 71.80068  ? 55  ASN A CG  1 
ATOM   396  O OD1 . ASN A 1 61  ? -31.80295 37.69123 48.55675 1.000 91.68480  ? 55  ASN A OD1 1 
ATOM   397  N ND2 . ASN A 1 61  ? -33.05422 39.15977 49.70909 1.000 67.61917  ? 55  ASN A ND2 1 
ATOM   398  N N   . PRO A 1 62  ? -29.38265 39.41984 45.86942 1.000 71.08403  ? 56  PRO A N   1 
ATOM   399  C CA  . PRO A 1 62  ? -29.73662 39.87490 44.51661 1.000 66.48753  ? 56  PRO A CA  1 
ATOM   400  C C   . PRO A 1 62  ? -31.03416 39.28256 44.00363 1.000 69.22151  ? 56  PRO A C   1 
ATOM   401  O O   . PRO A 1 62  ? -31.69293 39.90251 43.16029 1.000 84.36135  ? 56  PRO A O   1 
ATOM   402  C CB  . PRO A 1 62  ? -28.53990 39.42129 43.66404 1.000 68.04645  ? 56  PRO A CB  1 
ATOM   403  C CG  . PRO A 1 62  ? -27.46343 39.03085 44.64553 1.000 61.88793  ? 56  PRO A CG  1 
ATOM   404  C CD  . PRO A 1 62  ? -28.18068 38.57242 45.86962 1.000 71.98037  ? 56  PRO A CD  1 
ATOM   405  N N   . LEU A 1 63  ? -31.42999 38.11148 44.49245 1.000 67.11342  ? 57  LEU A N   1 
ATOM   406  C CA  . LEU A 1 63  ? -32.54545 37.37044 43.91896 1.000 68.53396  ? 57  LEU A CA  1 
ATOM   407  C C   . LEU A 1 63  ? -33.91213 37.90275 44.33582 1.000 70.19732  ? 57  LEU A C   1 
ATOM   408  O O   . LEU A 1 63  ? -34.92285 37.27484 44.00448 1.000 76.99932  ? 57  LEU A O   1 
ATOM   409  C CB  . LEU A 1 63  ? -32.43457 35.89082 44.29558 1.000 68.33520  ? 57  LEU A CB  1 
ATOM   410  C CG  . LEU A 1 63  ? -31.17958 35.17406 43.79717 1.000 64.46509  ? 57  LEU A CG  1 
ATOM   411  C CD1 . LEU A 1 63  ? -31.22476 33.69852 44.15691 1.000 59.00409  ? 57  LEU A CD1 1 
ATOM   412  C CD2 . LEU A 1 63  ? -31.03527 35.35797 42.29841 1.000 61.45190  ? 57  LEU A CD2 1 
ATOM   413  N N   . SER A 1 64  ? -33.98141 39.03524 45.03669 1.000 62.56796  ? 58  SER A N   1 
ATOM   414  C CA  . SER A 1 64  ? -35.26882 39.52159 45.51834 1.000 62.08260  ? 58  SER A CA  1 
ATOM   415  C C   . SER A 1 64  ? -36.09139 40.21780 44.43967 1.000 65.27352  ? 58  SER A C   1 
ATOM   416  O O   . SER A 1 64  ? -37.31200 40.33173 44.59513 1.000 67.46532  ? 58  SER A O   1 
ATOM   417  C CB  . SER A 1 64  ? -35.06643 40.46578 46.70585 1.000 67.10171  ? 58  SER A CB  1 
ATOM   418  O OG  . SER A 1 64  ? -34.14137 41.49034 46.39525 1.000 77.19737  ? 58  SER A OG  1 
ATOM   419  N N   . THR A 1 65  ? -35.46595 40.68803 43.36020 1.000 70.38009  ? 59  THR A N   1 
ATOM   420  C CA  . THR A 1 65  ? -36.18705 41.35830 42.28627 1.000 68.24222  ? 59  THR A CA  1 
ATOM   421  C C   . THR A 1 65  ? -35.70916 40.82709 40.94153 1.000 78.28801  ? 59  THR A C   1 
ATOM   422  O O   . THR A 1 65  ? -34.74865 40.05706 40.85441 1.000 73.96815  ? 59  THR A O   1 
ATOM   423  C CB  . THR A 1 65  ? -36.01094 42.88182 42.33605 1.000 73.67472  ? 59  THR A CB  1 
ATOM   424  O OG1 . THR A 1 65  ? -34.63779 43.21278 42.09774 1.000 68.06483  ? 59  THR A OG1 1 
ATOM   425  C CG2 . THR A 1 65  ? -36.44497 43.43703 43.68594 1.000 60.08585  ? 59  THR A CG2 1 
ATOM   426  N N   . THR A 1 66  ? -36.39196 41.26387 39.88005 1.000 77.77071  ? 60  THR A N   1 
ATOM   427  C CA  . THR A 1 66  ? -36.07629 40.78022 38.53887 1.000 67.78723  ? 60  THR A CA  1 
ATOM   428  C C   . THR A 1 66  ? -34.70925 41.27123 38.07395 1.000 67.90419  ? 60  THR A C   1 
ATOM   429  O O   . THR A 1 66  ? -33.87082 40.47487 37.63445 1.000 66.35201  ? 60  THR A O   1 
ATOM   430  C CB  . THR A 1 66  ? -37.16567 41.20994 37.55591 1.000 59.34190  ? 60  THR A CB  1 
ATOM   431  O OG1 . THR A 1 66  ? -38.34843 40.43221 37.78259 1.000 66.41341  ? 60  THR A OG1 1 
ATOM   432  C CG2 . THR A 1 66  ? -36.69926 41.01003 36.12152 1.000 55.82366  ? 60  THR A CG2 1 
ATOM   433  N N   . ARG A 1 67  ? -34.46659 42.58249 38.15613 1.000 73.60993  ? 61  ARG A N   1 
ATOM   434  C CA  . ARG A 1 67  ? -33.18798 43.12136 37.69983 1.000 64.42146  ? 61  ARG A CA  1 
ATOM   435  C C   . ARG A 1 67  ? -32.03518 42.63948 38.57180 1.000 74.81703  ? 61  ARG A C   1 
ATOM   436  O O   . ARG A 1 67  ? -30.93530 42.38341 38.06700 1.000 74.20531  ? 61  ARG A O   1 
ATOM   437  C CB  . ARG A 1 67  ? -33.23384 44.64757 37.67198 1.000 60.13298  ? 61  ARG A CB  1 
ATOM   438  C CG  . ARG A 1 67  ? -34.11283 45.22265 36.57709 1.000 64.97586  ? 61  ARG A CG  1 
ATOM   439  C CD  . ARG A 1 67  ? -34.01309 46.73757 36.54449 1.000 72.77518  ? 61  ARG A CD  1 
ATOM   440  N NE  . ARG A 1 67  ? -35.24565 47.35353 36.06888 1.000 72.44019  ? 61  ARG A NE  1 
ATOM   441  C CZ  . ARG A 1 67  ? -35.49813 47.63963 34.80038 1.000 60.57553  ? 61  ARG A CZ  1 
ATOM   442  N NH1 . ARG A 1 67  ? -34.62261 47.37484 33.84584 1.000 74.60619  ? 61  ARG A NH1 1 
ATOM   443  N NH2 . ARG A 1 67  ? -36.65796 48.20575 34.48212 1.000 70.58213  ? 61  ARG A NH2 1 
ATOM   444  N N   . GLY A 1 68  ? -32.26212 42.51531 39.88080 1.000 72.86762  ? 62  GLY A N   1 
ATOM   445  C CA  . GLY A 1 68  ? -31.21593 42.00515 40.75236 1.000 65.76347  ? 62  GLY A CA  1 
ATOM   446  C C   . GLY A 1 68  ? -30.76598 40.60687 40.37078 1.000 75.18818  ? 62  GLY A C   1 
ATOM   447  O O   . GLY A 1 68  ? -29.57012 40.30215 40.38595 1.000 74.27500  ? 62  GLY A O   1 
ATOM   448  N N   . ALA A 1 69  ? -31.71813 39.73761 40.01956 1.000 64.86818  ? 63  ALA A N   1 
ATOM   449  C CA  . ALA A 1 69  ? -31.36907 38.37880 39.61687 1.000 61.80820  ? 63  ALA A CA  1 
ATOM   450  C C   . ALA A 1 69  ? -30.62477 38.35364 38.28696 1.000 72.53447  ? 63  ALA A C   1 
ATOM   451  O O   . ALA A 1 69  ? -29.76482 37.49019 38.07858 1.000 74.47219  ? 63  ALA A O   1 
ATOM   452  C CB  . ALA A 1 69  ? -32.62601 37.51280 39.53678 1.000 56.23404  ? 63  ALA A CB  1 
ATOM   453  N N   . LEU A 1 70  ? -30.94121 39.27770 37.37565 1.000 75.08575  ? 64  LEU A N   1 
ATOM   454  C CA  . LEU A 1 70  ? -30.20528 39.34930 36.11660 1.000 68.15697  ? 64  LEU A CA  1 
ATOM   455  C C   . LEU A 1 70  ? -28.75104 39.73320 36.35348 1.000 71.74318  ? 64  LEU A C   1 
ATOM   456  O O   . LEU A 1 70  ? -27.84314 39.17653 35.72400 1.000 85.98460  ? 64  LEU A O   1 
ATOM   457  C CB  . LEU A 1 70  ? -30.87418 40.34441 35.16961 1.000 60.01357  ? 64  LEU A CB  1 
ATOM   458  C CG  . LEU A 1 70  ? -32.24709 39.93752 34.63898 1.000 70.16932  ? 64  LEU A CG  1 
ATOM   459  C CD1 . LEU A 1 70  ? -32.82362 41.01821 33.74103 1.000 71.95949  ? 64  LEU A CD1 1 
ATOM   460  C CD2 . LEU A 1 70  ? -32.13833 38.62196 33.89414 1.000 63.56923  ? 64  LEU A CD2 1 
ATOM   461  N N   . ILE A 1 71  ? -28.51193 40.68628 37.25802 1.000 67.48788  ? 65  ILE A N   1 
ATOM   462  C CA  . ILE A 1 71  ? -27.14370 41.04924 37.61680 1.000 74.14281  ? 65  ILE A CA  1 
ATOM   463  C C   . ILE A 1 71  ? -26.41240 39.84672 38.19773 1.000 74.43740  ? 65  ILE A C   1 
ATOM   464  O O   . ILE A 1 71  ? -25.23443 39.61133 37.89864 1.000 75.92283  ? 65  ILE A O   1 
ATOM   465  C CB  . ILE A 1 71  ? -27.14573 42.23835 38.59674 1.000 64.62578  ? 65  ILE A CB  1 
ATOM   466  C CG1 . ILE A 1 71  ? -27.73124 43.48398 37.92947 1.000 69.44654  ? 65  ILE A CG1 1 
ATOM   467  C CG2 . ILE A 1 71  ? -25.74300 42.51836 39.11281 1.000 67.86710  ? 65  ILE A CG2 1 
ATOM   468  C CD1 . ILE A 1 71  ? -27.01538 43.88450 36.66231 1.000 67.85381  ? 65  ILE A CD1 1 
ATOM   469  N N   . PHE A 1 72  ? -27.10293 39.05939 39.02638 1.000 69.06022  ? 66  PHE A N   1 
ATOM   470  C CA  . PHE A 1 72  ? -26.47272 37.89414 39.63750 1.000 72.34750  ? 66  PHE A CA  1 
ATOM   471  C C   . PHE A 1 72  ? -26.06104 36.87084 38.58519 1.000 75.22840  ? 66  PHE A C   1 
ATOM   472  O O   . PHE A 1 72  ? -24.99069 36.25960 38.68776 1.000 73.53633  ? 66  PHE A O   1 
ATOM   473  C CB  . PHE A 1 72  ? -27.41923 37.26188 40.65650 1.000 72.19719  ? 66  PHE A CB  1 
ATOM   474  C CG  . PHE A 1 72  ? -26.71655 36.60720 41.80960 1.000 77.50085  ? 66  PHE A CG  1 
ATOM   475  C CD1 . PHE A 1 72  ? -25.36814 36.82863 42.03153 1.000 83.13259  ? 66  PHE A CD1 1 
ATOM   476  C CD2 . PHE A 1 72  ? -27.40266 35.76698 42.66952 1.000 80.86456  ? 66  PHE A CD2 1 
ATOM   477  C CE1 . PHE A 1 72  ? -24.71811 36.22939 43.09369 1.000 79.81686  ? 66  PHE A CE1 1 
ATOM   478  C CE2 . PHE A 1 72  ? -26.75808 35.16277 43.73207 1.000 83.67706  ? 66  PHE A CE2 1 
ATOM   479  C CZ  . PHE A 1 72  ? -25.41367 35.39397 43.94407 1.000 77.45199  ? 66  PHE A CZ  1 
ATOM   480  N N   . ASP A 1 73  ? -26.89834 36.66848 37.56494 1.000 75.28131  ? 67  ASP A N   1 
ATOM   481  C CA  . ASP A 1 73  ? -26.55632 35.71607 36.51258 1.000 81.35945  ? 67  ASP A CA  1 
ATOM   482  C C   . ASP A 1 73  ? -25.37149 36.20150 35.68659 1.000 81.33701  ? 67  ASP A C   1 
ATOM   483  O O   . ASP A 1 73  ? -24.48435 35.41041 35.34472 1.000 79.04210  ? 67  ASP A O   1 
ATOM   484  C CB  . ASP A 1 73  ? -27.76736 35.45902 35.61774 1.000 87.49264  ? 67  ASP A CB  1 
ATOM   485  C CG  . ASP A 1 73  ? -28.72626 34.44966 36.21402 1.000 99.83632  ? 67  ASP A CG  1 
ATOM   486  O OD1 . ASP A 1 73  ? -28.41056 33.88822 37.28468 1.000 93.86403  ? 67  ASP A OD1 1 
ATOM   487  O OD2 . ASP A 1 73  ? -29.79434 34.21523 35.61066 1.000 130.54871 ? 67  ASP A OD2 1 
ATOM   488  N N   . LYS A 1 74  ? -25.34395 37.49410 35.34637 1.000 72.80003  ? 68  LYS A N   1 
ATOM   489  C CA  . LYS A 1 74  ? -24.17729 38.05359 34.66934 1.000 80.30183  ? 68  LYS A CA  1 
ATOM   490  C C   . LYS A 1 74  ? -22.91950 37.87324 35.50895 1.000 81.82781  ? 68  LYS A C   1 
ATOM   491  O O   . LYS A 1 74  ? -21.85972 37.50817 34.98623 1.000 83.73390  ? 68  LYS A O   1 
ATOM   492  C CB  . LYS A 1 74  ? -24.40412 39.53393 34.36224 1.000 78.30691  ? 68  LYS A CB  1 
ATOM   493  C CG  . LYS A 1 74  ? -25.12830 39.81223 33.05505 1.000 83.98711  ? 68  LYS A CG  1 
ATOM   494  C CD  . LYS A 1 74  ? -24.14757 40.15955 31.94432 1.000 104.30940 ? 68  LYS A CD  1 
ATOM   495  C CE  . LYS A 1 74  ? -24.87057 40.64743 30.69826 1.000 113.41585 ? 68  LYS A CE  1 
ATOM   496  N NZ  . LYS A 1 74  ? -23.92088 41.08650 29.63857 1.000 116.18283 ? 68  LYS A NZ  1 
ATOM   497  N N   . LEU A 1 75  ? -23.01922 38.12509 36.81591 1.000 82.41543  ? 69  LEU A N   1 
ATOM   498  C CA  . LEU A 1 75  ? -21.87685 37.91989 37.69905 1.000 79.37928  ? 69  LEU A CA  1 
ATOM   499  C C   . LEU A 1 75  ? -21.50720 36.44464 37.77855 1.000 78.03685  ? 69  LEU A C   1 
ATOM   500  O O   . LEU A 1 75  ? -20.32158 36.09238 37.79417 1.000 86.79536  ? 69  LEU A O   1 
ATOM   501  C CB  . LEU A 1 75  ? -22.18850 38.47436 39.08841 1.000 69.19956  ? 69  LEU A CB  1 
ATOM   502  C CG  . LEU A 1 75  ? -20.99142 38.73285 40.00033 1.000 75.99234  ? 69  LEU A CG  1 
ATOM   503  C CD1 . LEU A 1 75  ? -20.08654 39.78882 39.38821 1.000 67.13321  ? 69  LEU A CD1 1 
ATOM   504  C CD2 . LEU A 1 75  ? -21.45983 39.15482 41.38151 1.000 64.75936  ? 69  LEU A CD2 1 
ATOM   505  N N   . LYS A 1 76  ? -22.51361 35.56805 37.83111 1.000 77.74790  ? 70  LYS A N   1 
ATOM   506  C CA  . LYS A 1 76  ? -22.25891 34.13086 37.80952 1.000 77.33138  ? 70  LYS A CA  1 
ATOM   507  C C   . LYS A 1 76  ? -21.52910 33.72149 36.53591 1.000 83.79752  ? 70  LYS A C   1 
ATOM   508  O O   . LYS A 1 76  ? -20.57116 32.94033 36.58153 1.000 83.05240  ? 70  LYS A O   1 
ATOM   509  C CB  . LYS A 1 76  ? -23.58135 33.37371 37.94505 1.000 77.43318  ? 70  LYS A CB  1 
ATOM   510  C CG  . LYS A 1 76  ? -23.48605 31.86002 37.82145 1.000 70.91222  ? 70  LYS A CG  1 
ATOM   511  C CD  . LYS A 1 76  ? -24.83887 31.22258 38.11204 1.000 82.04202  ? 70  LYS A CD  1 
ATOM   512  C CE  . LYS A 1 76  ? -24.83175 29.72343 37.86333 1.000 82.20016  ? 70  LYS A CE  1 
ATOM   513  N NZ  . LYS A 1 76  ? -24.89078 29.39336 36.41208 1.000 83.96686  ? 70  LYS A NZ  1 
ATOM   514  N N   . GLU A 1 77  ? -21.96256 34.25173 35.38975 1.000 87.92067  ? 71  GLU A N   1 
ATOM   515  C CA  . GLU A 1 77  ? -21.31136 33.93358 34.12272 1.000 79.57761  ? 71  GLU A CA  1 
ATOM   516  C C   . GLU A 1 77  ? -19.87513 34.44304 34.09636 1.000 84.20234  ? 71  GLU A C   1 
ATOM   517  O O   . GLU A 1 77  ? -18.98910 33.80188 33.51809 1.000 84.93965  ? 71  GLU A O   1 
ATOM   518  C CB  . GLU A 1 77  ? -22.11751 34.52724 32.96766 1.000 81.21408  ? 71  GLU A CB  1 
ATOM   519  C CG  . GLU A 1 77  ? -21.51866 34.30216 31.59319 1.000 110.75977 ? 71  GLU A CG  1 
ATOM   520  C CD  . GLU A 1 77  ? -22.30498 35.00228 30.50392 1.000 108.83031 ? 71  GLU A CD  1 
ATOM   521  O OE1 . GLU A 1 77  ? -23.32187 35.64948 30.83051 1.000 98.33801  ? 71  GLU A OE1 1 
ATOM   522  O OE2 . GLU A 1 77  ? -21.90764 34.90795 29.32382 1.000 116.89245 ? 71  GLU A OE2 1 
ATOM   523  N N   . ALA A 1 78  ? -19.62428 35.59441 34.72206 1.000 80.32597  ? 72  ALA A N   1 
ATOM   524  C CA  . ALA A 1 78  ? -18.26650 36.12693 34.77772 1.000 78.67486  ? 72  ALA A CA  1 
ATOM   525  C C   . ALA A 1 78  ? -17.35325 35.22038 35.59584 1.000 88.83736  ? 72  ALA A C   1 
ATOM   526  O O   . ALA A 1 78  ? -16.24957 34.87311 35.15772 1.000 80.92944  ? 72  ALA A O   1 
ATOM   527  C CB  . ALA A 1 78  ? -18.28238 37.54187 35.35548 1.000 74.75013  ? 72  ALA A CB  1 
ATOM   528  N N   . SER A 1 79  ? -17.80290 34.82097 36.79122 1.000 86.42317  ? 73  SER A N   1 
ATOM   529  C CA  . SER A 1 79  ? -16.99271 33.94928 37.63870 1.000 81.98524  ? 73  SER A CA  1 
ATOM   530  C C   . SER A 1 79  ? -16.65610 32.63997 36.93987 1.000 96.20146  ? 73  SER A C   1 
ATOM   531  O O   . SER A 1 79  ? -15.59023 32.06156 37.18243 1.000 94.18804  ? 73  SER A O   1 
ATOM   532  C CB  . SER A 1 79  ? -17.71782 33.66119 38.95259 1.000 83.71489  ? 73  SER A CB  1 
ATOM   533  O OG  . SER A 1 79  ? -18.76223 32.72395 38.75638 1.000 91.25419  ? 73  SER A OG  1 
ATOM   534  N N   . GLU A 1 80  ? -17.54855 32.15718 36.07520 1.000 90.90691  ? 74  GLU A N   1 
ATOM   535  C CA  . GLU A 1 80  ? -17.29559 30.92915 35.33496 1.000 83.87294  ? 74  GLU A CA  1 
ATOM   536  C C   . GLU A 1 80  ? -16.32538 31.12954 34.17836 1.000 81.68945  ? 74  GLU A C   1 
ATOM   537  O O   . GLU A 1 80  ? -15.74382 30.15007 33.69944 1.000 93.62449  ? 74  GLU A O   1 
ATOM   538  C CB  . GLU A 1 80  ? -18.61487 30.35230 34.81587 1.000 82.83344  ? 74  GLU A CB  1 
ATOM   539  C CG  . GLU A 1 80  ? -19.58539 29.96004 35.91848 1.000 87.62148  ? 74  GLU A CG  1 
ATOM   540  C CD  . GLU A 1 80  ? -20.95256 29.57870 35.38661 1.000 99.67789  ? 74  GLU A CD  1 
ATOM   541  O OE1 . GLU A 1 80  ? -21.17650 29.71297 34.16514 1.000 95.13411  ? 74  GLU A OE1 1 
ATOM   542  O OE2 . GLU A 1 80  ? -21.80451 29.14577 36.19111 1.000 93.07708  ? 74  GLU A OE2 1 
ATOM   543  N N   . LYS A 1 81  ? -16.13744 32.36525 33.72089 1.000 99.23930  ? 75  LYS A N   1 
ATOM   544  C CA  . LYS A 1 81  ? -15.20315 32.66457 32.64493 1.000 85.54827  ? 75  LYS A CA  1 
ATOM   545  C C   . LYS A 1 81  ? -13.80935 33.01597 33.15253 1.000 97.46099  ? 75  LYS A C   1 
ATOM   546  O O   . LYS A 1 81  ? -12.95963 33.42918 32.35694 1.000 103.66661 ? 75  LYS A O   1 
ATOM   547  C CB  . LYS A 1 81  ? -15.74462 33.80256 31.77517 1.000 84.34604  ? 75  LYS A CB  1 
ATOM   548  C CG  . LYS A 1 81  ? -16.84736 33.37553 30.81873 1.000 94.57165  ? 75  LYS A CG  1 
ATOM   549  C CD  . LYS A 1 81  ? -17.33927 34.54348 29.97897 1.000 115.52695 ? 75  LYS A CD  1 
ATOM   550  C CE  . LYS A 1 81  ? -18.14626 34.06060 28.78294 1.000 123.74350 ? 75  LYS A CE  1 
ATOM   551  N NZ  . LYS A 1 81  ? -19.27662 33.18049 29.18610 1.000 125.92351 ? 75  LYS A NZ  1 
ATOM   552  N N   . GLY A 1 82  ? -13.55538 32.86484 34.45082 1.000 83.16680  ? 76  GLY A N   1 
ATOM   553  C CA  . GLY A 1 82  ? -12.23672 33.08354 35.00498 1.000 83.33428  ? 76  GLY A CA  1 
ATOM   554  C C   . GLY A 1 82  ? -12.05198 34.37782 35.76569 1.000 100.94724 ? 76  GLY A C   1 
ATOM   555  O O   . GLY A 1 82  ? -10.93587 34.64706 36.22694 1.000 106.60040 ? 76  GLY A O   1 
ATOM   556  N N   . ILE A 1 83  ? -13.09789 35.18419 35.91338 1.000 85.20093  ? 77  ILE A N   1 
ATOM   557  C CA  . ILE A 1 83  ? -12.99129 36.44130 36.64444 1.000 78.33839  ? 77  ILE A CA  1 
ATOM   558  C C   . ILE A 1 83  ? -13.02045 36.15194 38.13830 1.000 84.94480  ? 77  ILE A C   1 
ATOM   559  O O   . ILE A 1 83  ? -13.86748 35.39052 38.62112 1.000 81.32495  ? 77  ILE A O   1 
ATOM   560  C CB  . ILE A 1 83  ? -14.12231 37.40206 36.24817 1.000 78.98141  ? 77  ILE A CB  1 
ATOM   561  C CG1 . ILE A 1 83  ? -14.22766 37.50989 34.72687 1.000 67.74795  ? 77  ILE A CG1 1 
ATOM   562  C CG2 . ILE A 1 83  ? -13.88768 38.77202 36.86638 1.000 80.91322  ? 77  ILE A CG2 1 
ATOM   563  C CD1 . ILE A 1 83  ? -13.00395 38.10035 34.07315 1.000 78.50773  ? 77  ILE A CD1 1 
ATOM   564  N N   . LYS A 1 84  ? -12.09596 36.76033 38.87563 1.000 78.71622  ? 78  LYS A N   1 
ATOM   565  C CA  . LYS A 1 84  ? -12.06677 36.62611 40.32730 1.000 86.73970  ? 78  LYS A CA  1 
ATOM   566  C C   . LYS A 1 84  ? -13.15462 37.51702 40.91456 1.000 79.43670  ? 78  LYS A C   1 
ATOM   567  O O   . LYS A 1 84  ? -13.06391 38.74640 40.84632 1.000 89.60310  ? 78  LYS A O   1 
ATOM   568  C CB  . LYS A 1 84  ? -10.68915 36.99481 40.87202 1.000 79.00124  ? 78  LYS A CB  1 
ATOM   569  C CG  . LYS A 1 84  ? -10.50235 36.70037 42.35532 1.000 91.66539  ? 78  LYS A CG  1 
ATOM   570  C CD  . LYS A 1 84  ? -9.09011  37.03695 42.82128 1.000 105.98228 ? 78  LYS A CD  1 
ATOM   571  C CE  . LYS A 1 84  ? -8.88197  36.66816 44.28577 1.000 118.64582 ? 78  LYS A CE  1 
ATOM   572  N NZ  . LYS A 1 84  ? -7.50926  36.99983 44.76408 1.000 111.47334 ? 78  LYS A NZ  1 
ATOM   573  N N   . ILE A 1 85  ? -14.19164 36.90443 41.47806 1.000 78.53202  ? 79  ILE A N   1 
ATOM   574  C CA  . ILE A 1 85  ? -15.30414 37.62833 42.08405 1.000 74.99508  ? 79  ILE A CA  1 
ATOM   575  C C   . ILE A 1 85  ? -15.21394 37.45027 43.59248 1.000 75.51615  ? 79  ILE A C   1 
ATOM   576  O O   . ILE A 1 85  ? -15.24021 36.31952 44.09414 1.000 82.25767  ? 79  ILE A O   1 
ATOM   577  C CB  . ILE A 1 85  ? -16.66278 37.13718 41.56032 1.000 76.24142  ? 79  ILE A CB  1 
ATOM   578  C CG1 . ILE A 1 85  ? -16.64288 36.98460 40.03709 1.000 85.53602  ? 79  ILE A CG1 1 
ATOM   579  C CG2 . ILE A 1 85  ? -17.76619 38.09399 41.98327 1.000 78.26977  ? 79  ILE A CG2 1 
ATOM   580  C CD1 . ILE A 1 85  ? -16.66696 38.28906 39.28402 1.000 75.27777  ? 79  ILE A CD1 1 
ATOM   581  N N   . ILE A 1 86  ? -15.10679 38.56055 44.31590 1.000 72.19578  ? 80  ILE A N   1 
ATOM   582  C CA  . ILE A 1 86  ? -15.13071 38.55852 45.77287 1.000 67.75420  ? 80  ILE A CA  1 
ATOM   583  C C   . ILE A 1 86  ? -16.23873 39.49488 46.22779 1.000 78.34831  ? 80  ILE A C   1 
ATOM   584  O O   . ILE A 1 86  ? -16.26704 40.66733 45.83605 1.000 87.46180  ? 80  ILE A O   1 
ATOM   585  C CB  . ILE A 1 86  ? -13.77787 38.98044 46.37299 1.000 74.54828  ? 80  ILE A CB  1 
ATOM   586  C CG1 . ILE A 1 86  ? -12.65511 38.09367 45.83742 1.000 72.44790  ? 80  ILE A CG1 1 
ATOM   587  C CG2 . ILE A 1 86  ? -13.82331 38.89657 47.88889 1.000 69.70276  ? 80  ILE A CG2 1 
ATOM   588  C CD1 . ILE A 1 86  ? -11.30220 38.41364 46.42645 1.000 76.17626  ? 80  ILE A CD1 1 
ATOM   589  N N   . VAL A 1 87  ? -17.15046 38.97686 47.04501 1.000 70.75723  ? 81  VAL A N   1 
ATOM   590  C CA  . VAL A 1 87  ? -18.25427 39.75409 47.59466 1.000 65.83606  ? 81  VAL A CA  1 
ATOM   591  C C   . VAL A 1 87  ? -18.07245 39.82493 49.10350 1.000 63.66217  ? 81  VAL A C   1 
ATOM   592  O O   . VAL A 1 87  ? -18.02643 38.78786 49.77699 1.000 71.25087  ? 81  VAL A O   1 
ATOM   593  C CB  . VAL A 1 87  ? -19.61777 39.14540 47.23490 1.000 71.25743  ? 81  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 87  ? -20.73752 39.95052 47.86761 1.000 62.48805  ? 81  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 87  ? -19.78609 39.08629 45.72852 1.000 72.60099  ? 81  VAL A CG2 1 
ATOM   596  N N   . LEU A 1 88  ? -17.96218 41.04156 49.63150 1.000 70.61496  ? 82  LEU A N   1 
ATOM   597  C CA  . LEU A 1 88  ? -17.85107 41.26853 51.06703 1.000 64.36557  ? 82  LEU A CA  1 
ATOM   598  C C   . LEU A 1 88  ? -19.21430 41.67043 51.61191 1.000 69.60199  ? 82  LEU A C   1 
ATOM   599  O O   . LEU A 1 88  ? -19.82671 42.62450 51.12128 1.000 84.05850  ? 82  LEU A O   1 
ATOM   600  C CB  . LEU A 1 88  ? -16.82430 42.35476 51.38715 1.000 64.35762  ? 82  LEU A CB  1 
ATOM   601  C CG  . LEU A 1 88  ? -15.34356 42.11223 51.10710 1.000 70.75220  ? 82  LEU A CG  1 
ATOM   602  C CD1 . LEU A 1 88  ? -14.52517 43.28502 51.62207 1.000 78.89361  ? 82  LEU A CD1 1 
ATOM   603  C CD2 . LEU A 1 88  ? -14.87330 40.81951 51.73727 1.000 78.18247  ? 82  LEU A CD2 1 
ATOM   604  N N   . LEU A 1 89  ? -19.68053 40.95062 52.62480 1.000 64.39786  ? 83  LEU A N   1 
ATOM   605  C CA  . LEU A 1 89  ? -20.89445 41.30484 53.33983 1.000 72.89224  ? 83  LEU A CA  1 
ATOM   606  C C   . LEU A 1 89  ? -20.62797 41.22634 54.83420 1.000 72.89236  ? 83  LEU A C   1 
ATOM   607  O O   . LEU A 1 89  ? -19.76078 40.47481 55.28518 1.000 83.49937  ? 83  LEU A O   1 
ATOM   608  C CB  . LEU A 1 89  ? -22.05893 40.38711 52.95804 1.000 66.00786  ? 83  LEU A CB  1 
ATOM   609  C CG  . LEU A 1 89  ? -21.79957 38.88722 53.09346 1.000 71.86603  ? 83  LEU A CG  1 
ATOM   610  C CD1 . LEU A 1 89  ? -22.62418 38.29544 54.22345 1.000 85.47519  ? 83  LEU A CD1 1 
ATOM   611  C CD2 . LEU A 1 89  ? -22.09561 38.18082 51.78551 1.000 76.78435  ? 83  LEU A CD2 1 
ATOM   612  N N   . ASP A 1 90  ? -21.36811 42.01999 55.60043 1.000 64.12941  ? 84  ASP A N   1 
ATOM   613  C CA  . ASP A 1 90  ? -21.22539 41.97448 57.04739 1.000 68.37882  ? 84  ASP A CA  1 
ATOM   614  C C   . ASP A 1 90  ? -21.78512 40.66299 57.58263 1.000 71.43210  ? 84  ASP A C   1 
ATOM   615  O O   . ASP A 1 90  ? -22.75199 40.11602 57.04457 1.000 75.14449  ? 84  ASP A O   1 
ATOM   616  C CB  . ASP A 1 90  ? -21.93275 43.16527 57.69388 1.000 69.01357  ? 84  ASP A CB  1 
ATOM   617  C CG  . ASP A 1 90  ? -21.66579 43.26410 59.18322 1.000 76.00582  ? 84  ASP A CG  1 
ATOM   618  O OD1 . ASP A 1 90  ? -22.23028 42.45389 59.94762 1.000 78.10153  ? 84  ASP A OD1 1 
ATOM   619  O OD2 . ASP A 1 90  ? -20.87811 44.14470 59.58945 1.000 77.66572  ? 84  ASP A OD2 1 
ATOM   620  N N   . GLU A 1 91  ? -21.16839 40.15945 58.65444 1.000 69.82165  ? 85  GLU A N   1 
ATOM   621  C CA  . GLU A 1 91  ? -21.56822 38.88514 59.23985 1.000 74.29258  ? 85  GLU A CA  1 
ATOM   622  C C   . GLU A 1 91  ? -23.02017 38.87512 59.70313 1.000 73.94706  ? 85  GLU A C   1 
ATOM   623  O O   . GLU A 1 91  ? -23.54680 37.80159 60.01214 1.000 88.34384  ? 85  GLU A O   1 
ATOM   624  C CB  . GLU A 1 91  ? -20.63839 38.54574 60.40742 1.000 68.52526  ? 85  GLU A CB  1 
ATOM   625  C CG  . GLU A 1 91  ? -20.62836 37.07820 60.80261 1.000 88.22689  ? 85  GLU A CG  1 
ATOM   626  C CD  . GLU A 1 91  ? -19.56735 36.76824 61.83672 1.000 107.34727 ? 85  GLU A CD  1 
ATOM   627  O OE1 . GLU A 1 91  ? -18.98555 37.72211 62.39494 1.000 98.53616  ? 85  GLU A OE1 1 
ATOM   628  O OE2 . GLU A 1 91  ? -19.31094 35.57242 62.08803 1.000 131.41069 ? 85  GLU A OE2 1 
ATOM   629  N N   . ARG A 1 92  ? -23.67882 40.02971 59.75782 1.000 68.91084  ? 86  ARG A N   1 
ATOM   630  C CA  . ARG A 1 92  ? -25.08818 40.08954 60.11252 1.000 69.89230  ? 86  ARG A CA  1 
ATOM   631  C C   . ARG A 1 92  ? -26.00957 39.97282 58.90484 1.000 81.23425  ? 86  ARG A C   1 
ATOM   632  O O   . ARG A 1 92  ? -27.22122 39.81100 59.08418 1.000 99.87343  ? 86  ARG A O   1 
ATOM   633  C CB  . ARG A 1 92  ? -25.37848 41.38503 60.87536 1.000 73.49240  ? 86  ARG A CB  1 
ATOM   634  C CG  . ARG A 1 92  ? -24.48898 41.55880 62.09315 1.000 70.56181  ? 86  ARG A CG  1 
ATOM   635  C CD  . ARG A 1 92  ? -24.97964 42.65526 63.01633 1.000 86.91725  ? 86  ARG A CD  1 
ATOM   636  N NE  . ARG A 1 92  ? -24.11836 42.78768 64.18563 1.000 98.39837  ? 86  ARG A NE  1 
ATOM   637  C CZ  . ARG A 1 92  ? -24.35526 43.60136 65.20547 1.000 102.27977 ? 86  ARG A CZ  1 
ATOM   638  N NH1 . ARG A 1 92  ? -25.42297 44.38220 65.23400 1.000 104.19382 ? 86  ARG A NH1 1 
ATOM   639  N NH2 . ARG A 1 92  ? -23.50051 43.63057 66.22388 1.000 100.49384 ? 86  ARG A NH2 1 
ATOM   640  N N   . GLY A 1 93  ? -25.47150 40.04650 57.68895 1.000 81.74742  ? 87  GLY A N   1 
ATOM   641  C CA  . GLY A 1 93  ? -26.24488 39.75140 56.49795 1.000 98.43853  ? 87  GLY A CA  1 
ATOM   642  C C   . GLY A 1 93  ? -26.01611 38.32071 56.05754 1.000 96.41648  ? 87  GLY A C   1 
ATOM   643  O O   . GLY A 1 93  ? -26.13288 37.98781 54.87433 1.000 113.46807 ? 87  GLY A O   1 
ATOM   644  N N   . LYS A 1 94  ? -25.70406 37.46271 57.02816 1.000 90.74208  ? 88  LYS A N   1 
ATOM   645  C CA  . LYS A 1 94  ? -25.22634 36.10907 56.78324 1.000 91.08381  ? 88  LYS A CA  1 
ATOM   646  C C   . LYS A 1 94  ? -26.33886 35.11683 56.46825 1.000 110.05566 ? 88  LYS A C   1 
ATOM   647  O O   . LYS A 1 94  ? -26.03589 33.98112 56.08658 1.000 100.91318 ? 88  LYS A O   1 
ATOM   648  C CB  . LYS A 1 94  ? -24.44033 35.63291 58.00699 1.000 81.25947  ? 88  LYS A CB  1 
ATOM   649  C CG  . LYS A 1 94  ? -23.48534 34.48040 57.77763 1.000 99.95082  ? 88  LYS A CG  1 
ATOM   650  C CD  . LYS A 1 94  ? -22.59694 34.28777 58.99945 1.000 106.61606 ? 88  LYS A CD  1 
ATOM   651  C CE  . LYS A 1 94  ? -23.41963 34.24877 60.28193 1.000 99.24333  ? 88  LYS A CE  1 
ATOM   652  N NZ  . LYS A 1 94  ? -22.56023 34.23442 61.50007 1.000 119.15164 ? 88  LYS A NZ  1 
ATOM   653  N N   . ARG A 1 95  ? -27.60738 35.50669 56.61803 1.000 123.23226 ? 89  ARG A N   1 
ATOM   654  C CA  . ARG A 1 95  ? -28.70249 34.56535 56.39707 1.000 118.80906 ? 89  ARG A CA  1 
ATOM   655  C C   . ARG A 1 95  ? -28.66980 34.00393 54.98058 1.000 114.49686 ? 89  ARG A C   1 
ATOM   656  O O   . ARG A 1 95  ? -28.69455 32.78384 54.78174 1.000 104.98390 ? 89  ARG A O   1 
ATOM   657  C CB  . ARG A 1 95  ? -30.04454 35.24511 56.66980 1.000 129.31452 ? 89  ARG A CB  1 
ATOM   658  C CG  . ARG A 1 95  ? -30.14405 35.92144 58.02339 1.000 128.31099 ? 89  ARG A CG  1 
ATOM   659  C CD  . ARG A 1 95  ? -31.48709 36.61372 58.18571 1.000 120.43157 ? 89  ARG A CD  1 
ATOM   660  N NE  . ARG A 1 95  ? -31.47858 37.56379 59.29116 1.000 146.07802 ? 89  ARG A NE  1 
ATOM   661  C CZ  . ARG A 1 95  ? -31.16062 38.84580 59.17195 1.000 153.86863 ? 89  ARG A CZ  1 
ATOM   662  N NH1 . ARG A 1 95  ? -30.82509 39.36932 58.00364 1.000 139.71781 ? 89  ARG A NH1 1 
ATOM   663  N NH2 . ARG A 1 95  ? -31.17936 39.62216 60.25172 1.000 136.16462 ? 89  ARG A NH2 1 
ATOM   664  N N   . ASN A 1 96  ? -28.59705 34.88383 53.98140 1.000 99.64359  ? 90  ASN A N   1 
ATOM   665  C CA  . ASN A 1 96  ? -28.64867 34.47922 52.58136 1.000 86.45552  ? 90  ASN A CA  1 
ATOM   666  C C   . ASN A 1 96  ? -27.39457 33.75163 52.11388 1.000 93.56080  ? 90  ASN A C   1 
ATOM   667  O O   . ASN A 1 96  ? -27.35670 33.33205 50.95260 1.000 94.34666  ? 90  ASN A O   1 
ATOM   668  C CB  . ASN A 1 96  ? -28.88064 35.70534 51.69414 1.000 77.50913  ? 90  ASN A CB  1 
ATOM   669  C CG  . ASN A 1 96  ? -30.19009 36.40415 51.99314 1.000 126.98181 ? 90  ASN A CG  1 
ATOM   670  O OD1 . ASN A 1 96  ? -31.23699 36.04941 51.44504 1.000 111.40997 ? 90  ASN A OD1 1 
ATOM   671  N ND2 . ASN A 1 96  ? -30.13871 37.41062 52.86145 1.000 135.62213 ? 90  ASN A ND2 1 
ATOM   672  N N   . LEU A 1 97  ? -26.38905 33.57771 52.97729 1.000 88.65896  ? 91  LEU A N   1 
ATOM   673  C CA  . LEU A 1 97  ? -25.08124 33.11046 52.52125 1.000 85.06521  ? 91  LEU A CA  1 
ATOM   674  C C   . LEU A 1 97  ? -25.16679 31.74045 51.85719 1.000 88.46923  ? 91  LEU A C   1 
ATOM   675  O O   . LEU A 1 97  ? -24.55275 31.51329 50.80773 1.000 85.38178  ? 91  LEU A O   1 
ATOM   676  C CB  . LEU A 1 97  ? -24.10206 33.07866 53.69411 1.000 93.88008  ? 91  LEU A CB  1 
ATOM   677  C CG  . LEU A 1 97  ? -22.62584 32.88001 53.34933 1.000 96.78930  ? 91  LEU A CG  1 
ATOM   678  C CD1 . LEU A 1 97  ? -22.17446 33.93125 52.35158 1.000 76.25477  ? 91  LEU A CD1 1 
ATOM   679  C CD2 . LEU A 1 97  ? -21.77434 32.93583 54.60867 1.000 91.60929  ? 91  LEU A CD2 1 
ATOM   680  N N   . GLY A 1 98  ? -25.92118 30.81441 52.45065 1.000 97.00138  ? 92  GLY A N   1 
ATOM   681  C CA  . GLY A 1 98  ? -26.05990 29.49819 51.84892 1.000 89.94851  ? 92  GLY A CA  1 
ATOM   682  C C   . GLY A 1 98  ? -26.78317 29.54086 50.51676 1.000 85.76789  ? 92  GLY A C   1 
ATOM   683  O O   . GLY A 1 98  ? -26.43341 28.81075 49.58524 1.000 88.53331  ? 92  GLY A O   1 
ATOM   684  N N   . GLU A 1 99  ? -27.79929 30.39815 50.40778 1.000 81.26217  ? 93  GLU A N   1 
ATOM   685  C CA  . GLU A 1 99  ? -28.51885 30.54935 49.14759 1.000 72.06683  ? 93  GLU A CA  1 
ATOM   686  C C   . GLU A 1 99  ? -27.61699 31.12252 48.05989 1.000 80.96806  ? 93  GLU A C   1 
ATOM   687  O O   . GLU A 1 99  ? -27.68553 30.70069 46.89922 1.000 85.46357  ? 93  GLU A O   1 
ATOM   688  C CB  . GLU A 1 99  ? -29.74547 31.43638 49.36422 1.000 83.15082  ? 93  GLU A CB  1 
ATOM   689  C CG  . GLU A 1 99  ? -30.29647 32.08520 48.11303 1.000 76.74668  ? 93  GLU A CG  1 
ATOM   690  C CD  . GLU A 1 99  ? -31.40284 33.07284 48.42172 1.000 85.55644  ? 93  GLU A CD  1 
ATOM   691  O OE1 . GLU A 1 99  ? -32.20247 32.80367 49.34341 1.000 101.14620 ? 93  GLU A OE1 1 
ATOM   692  O OE2 . GLU A 1 99  ? -31.46875 34.12383 47.75006 1.000 92.40809  ? 93  GLU A OE2 1 
ATOM   693  N N   . LEU A 1 100 ? -26.75544 32.07700 48.41916 1.000 81.13316  ? 94  LEU A N   1 
ATOM   694  C CA  . LEU A 1 100 ? -25.87616 32.69992 47.43377 1.000 73.89140  ? 94  LEU A CA  1 
ATOM   695  C C   . LEU A 1 100 ? -24.85044 31.70659 46.90120 1.000 83.76584  ? 94  LEU A C   1 
ATOM   696  O O   . LEU A 1 100 ? -24.61522 31.62850 45.68955 1.000 83.57939  ? 94  LEU A O   1 
ATOM   697  C CB  . LEU A 1 100 ? -25.17415 33.90876 48.05175 1.000 74.81241  ? 94  LEU A CB  1 
ATOM   698  C CG  . LEU A 1 100 ? -26.06790 35.00936 48.61995 1.000 78.68525  ? 94  LEU A CG  1 
ATOM   699  C CD1 . LEU A 1 100 ? -25.23784 36.05107 49.35304 1.000 66.14126  ? 94  LEU A CD1 1 
ATOM   700  C CD2 . LEU A 1 100 ? -26.88414 35.64620 47.51344 1.000 58.78686  ? 94  LEU A CD2 1 
ATOM   701  N N   . GLN A 1 101 ? -24.22447 30.94065 47.79692 1.000 77.64170  ? 95  GLN A N   1 
ATOM   702  C CA  . GLN A 1 101 ? -23.18150 30.01057 47.37854 1.000 73.80476  ? 95  GLN A CA  1 
ATOM   703  C C   . GLN A 1 101 ? -23.73738 28.88362 46.51640 1.000 82.60935  ? 95  GLN A C   1 
ATOM   704  O O   . GLN A 1 101 ? -23.05019 28.40709 45.60521 1.000 82.00485  ? 95  GLN A O   1 
ATOM   705  C CB  . GLN A 1 101 ? -22.46623 29.44795 48.60659 1.000 72.30229  ? 95  GLN A CB  1 
ATOM   706  C CG  . GLN A 1 101 ? -21.75502 30.51047 49.43348 1.000 87.63014  ? 95  GLN A CG  1 
ATOM   707  C CD  . GLN A 1 101 ? -21.23926 29.98114 50.75697 1.000 88.33508  ? 95  GLN A CD  1 
ATOM   708  O OE1 . GLN A 1 101 ? -21.74233 28.98657 51.28052 1.000 98.45209  ? 95  GLN A OE1 1 
ATOM   709  N NE2 . GLN A 1 101 ? -20.22885 30.64629 51.30626 1.000 91.59289  ? 95  GLN A NE2 1 
ATOM   710  N N   . SER A 1 102 ? -24.97208 28.44823 46.78001 1.000 90.87188  ? 96  SER A N   1 
ATOM   711  C CA  . SER A 1 102 ? -25.57530 27.40766 45.95398 1.000 80.23741  ? 96  SER A CA  1 
ATOM   712  C C   . SER A 1 102 ? -25.88195 27.91379 44.55005 1.000 85.57418  ? 96  SER A C   1 
ATOM   713  O O   . SER A 1 102 ? -25.89720 27.12532 43.59798 1.000 84.78464  ? 96  SER A O   1 
ATOM   714  C CB  . SER A 1 102 ? -26.84635 26.87807 46.61870 1.000 79.89857  ? 96  SER A CB  1 
ATOM   715  O OG  . SER A 1 102 ? -26.56600 26.34609 47.90328 1.000 105.10019 ? 96  SER A OG  1 
ATOM   716  N N   . HIS A 1 103 ? -26.12649 29.21591 44.40054 1.000 85.34425  ? 97  HIS A N   1 
ATOM   717  C CA  . HIS A 1 103 ? -26.40492 29.79726 43.09373 1.000 86.35519  ? 97  HIS A CA  1 
ATOM   718  C C   . HIS A 1 103 ? -25.13726 30.13569 42.32194 1.000 87.81434  ? 97  HIS A C   1 
ATOM   719  O O   . HIS A 1 103 ? -25.13223 30.05229 41.08767 1.000 83.45724  ? 97  HIS A O   1 
ATOM   720  C CB  . HIS A 1 103 ? -27.26033 31.05847 43.24964 1.000 80.40554  ? 97  HIS A CB  1 
ATOM   721  C CG  . HIS A 1 103 ? -27.86660 31.53917 41.96837 1.000 82.65234  ? 97  HIS A CG  1 
ATOM   722  N ND1 . HIS A 1 103 ? -28.82258 30.82064 41.28322 1.000 88.72772  ? 97  HIS A ND1 1 
ATOM   723  C CD2 . HIS A 1 103 ? -27.65109 32.66327 41.24502 1.000 78.88136  ? 97  HIS A CD2 1 
ATOM   724  C CE1 . HIS A 1 103 ? -29.17152 31.48193 40.19416 1.000 85.18770  ? 97  HIS A CE1 1 
ATOM   725  N NE2 . HIS A 1 103 ? -28.47534 32.60337 40.14723 1.000 85.06107  ? 97  HIS A NE2 1 
ATOM   726  N N   . CYS A 1 104 ? -24.06375 30.50704 43.01909 1.000 88.14023  ? 98  CYS A N   1 
ATOM   727  C CA  . CYS A 1 104 ? -22.79361 30.86862 42.38834 1.000 85.27535  ? 98  CYS A CA  1 
ATOM   728  C C   . CYS A 1 104 ? -21.65463 30.21830 43.15551 1.000 75.27062  ? 98  CYS A C   1 
ATOM   729  O O   . CYS A 1 104 ? -21.00997 30.84859 44.00218 1.000 85.78239  ? 98  CYS A O   1 
ATOM   730  C CB  . CYS A 1 104 ? -22.61734 32.38651 42.33803 1.000 93.85825  ? 98  CYS A CB  1 
ATOM   731  S SG  . CYS A 1 104 ? -23.93664 33.25553 41.47381 1.000 107.53101 ? 98  CYS A SG  1 
ATOM   732  N N   . PRO A 1 105 ? -21.37275 28.94216 42.88025 1.000 75.20019  ? 99  PRO A N   1 
ATOM   733  C CA  . PRO A 1 105 ? -20.29217 28.25254 43.60285 1.000 87.94798  ? 99  PRO A CA  1 
ATOM   734  C C   . PRO A 1 105 ? -18.90053 28.77163 43.27880 1.000 90.18891  ? 99  PRO A C   1 
ATOM   735  O O   . PRO A 1 105 ? -17.94990 28.40282 43.97995 1.000 88.61587  ? 99  PRO A O   1 
ATOM   736  C CB  . PRO A 1 105 ? -20.45277 26.79263 43.16069 1.000 76.77310  ? 99  PRO A CB  1 
ATOM   737  C CG  . PRO A 1 105 ? -21.12279 26.88107 41.82684 1.000 89.14415  ? 99  PRO A CG  1 
ATOM   738  C CD  . PRO A 1 105 ? -22.04676 28.06207 41.91119 1.000 82.56074  ? 99  PRO A CD  1 
ATOM   739  N N   . ASP A 1 106 ? -18.74519 29.61003 42.25440 1.000 91.16786  ? 100 ASP A N   1 
ATOM   740  C CA  . ASP A 1 106 ? -17.43789 30.12287 41.86878 1.000 84.70931  ? 100 ASP A CA  1 
ATOM   741  C C   . ASP A 1 106 ? -17.17910 31.54227 42.35541 1.000 86.99346  ? 100 ASP A C   1 
ATOM   742  O O   . ASP A 1 106 ? -16.07086 32.05339 42.16209 1.000 94.22166  ? 100 ASP A O   1 
ATOM   743  C CB  . ASP A 1 106 ? -17.27709 30.06686 40.34499 1.000 86.14062  ? 100 ASP A CB  1 
ATOM   744  C CG  . ASP A 1 106 ? -17.21161 28.64518 39.82019 1.000 96.12238  ? 100 ASP A CG  1 
ATOM   745  O OD1 . ASP A 1 106 ? -16.62354 27.78392 40.50806 1.000 87.80940  ? 100 ASP A OD1 1 
ATOM   746  O OD2 . ASP A 1 106 ? -17.74986 28.38746 38.72386 1.000 118.87129 ? 100 ASP A OD2 1 
ATOM   747  N N   . ILE A 1 107 ? -18.15956 32.18579 42.96677 1.000 79.32891  ? 101 ILE A N   1 
ATOM   748  C CA  . ILE A 1 107 ? -17.97182 33.49384 43.58020 1.000 75.37315  ? 101 ILE A CA  1 
ATOM   749  C C   . ILE A 1 107 ? -17.54496 33.28942 45.02497 1.000 64.44298  ? 101 ILE A C   1 
ATOM   750  O O   . ILE A 1 107 ? -18.09599 32.44092 45.73642 1.000 80.83126  ? 101 ILE A O   1 
ATOM   751  C CB  . ILE A 1 107 ? -19.25946 34.33425 43.48739 1.000 81.93086  ? 101 ILE A CB  1 
ATOM   752  C CG1 . ILE A 1 107 ? -19.57468 34.66646 42.02766 1.000 83.63619  ? 101 ILE A CG1 1 
ATOM   753  C CG2 . ILE A 1 107 ? -19.13454 35.60390 44.31533 1.000 73.61116  ? 101 ILE A CG2 1 
ATOM   754  C CD1 . ILE A 1 107 ? -20.82682 35.49244 41.84545 1.000 82.35945  ? 101 ILE A CD1 1 
ATOM   755  N N   . ASN A 1 108 ? -16.54985 34.05569 45.46111 1.000 80.87258  ? 102 ASN A N   1 
ATOM   756  C CA  . ASN A 1 108 ? -16.05468 33.97508 46.83073 1.000 75.54952  ? 102 ASN A CA  1 
ATOM   757  C C   . ASN A 1 108 ? -16.79943 34.99867 47.67949 1.000 76.36442  ? 102 ASN A C   1 
ATOM   758  O O   . ASN A 1 108 ? -16.59026 36.20732 47.53392 1.000 86.55051  ? 102 ASN A O   1 
ATOM   759  C CB  . ASN A 1 108 ? -14.54716 34.21138 46.87817 1.000 86.77400  ? 102 ASN A CB  1 
ATOM   760  C CG  . ASN A 1 108 ? -13.98634 34.13470 48.28883 1.000 89.72562  ? 102 ASN A CG  1 
ATOM   761  O OD1 . ASN A 1 108 ? -14.61397 33.58082 49.19193 1.000 96.62386  ? 102 ASN A OD1 1 
ATOM   762  N ND2 . ASN A 1 108 ? -12.79603 34.69173 48.48255 1.000 110.96545 ? 102 ASN A ND2 1 
ATOM   763  N N   . PHE A 1 109 ? -17.67027 34.51532 48.56047 1.000 77.27361  ? 103 PHE A N   1 
ATOM   764  C CA  . PHE A 1 109 ? -18.38414 35.35920 49.50882 1.000 67.35836  ? 103 PHE A CA  1 
ATOM   765  C C   . PHE A 1 109 ? -17.65269 35.34103 50.84524 1.000 83.39863  ? 103 PHE A C   1 
ATOM   766  O O   . PHE A 1 109 ? -17.30654 34.26883 51.35314 1.000 91.39860  ? 103 PHE A O   1 
ATOM   767  C CB  . PHE A 1 109 ? -19.82639 34.88349 49.68682 1.000 74.84249  ? 103 PHE A CB  1 
ATOM   768  C CG  . PHE A 1 109 ? -20.63899 34.91787 48.42375 1.000 69.71915  ? 103 PHE A CG  1 
ATOM   769  C CD1 . PHE A 1 109 ? -21.33665 36.05943 48.06434 1.000 69.91758  ? 103 PHE A CD1 1 
ATOM   770  C CD2 . PHE A 1 109 ? -20.71106 33.80668 47.59968 1.000 75.80120  ? 103 PHE A CD2 1 
ATOM   771  C CE1 . PHE A 1 109 ? -22.08645 36.09390 46.90484 1.000 63.77536  ? 103 PHE A CE1 1 
ATOM   772  C CE2 . PHE A 1 109 ? -21.45948 33.83501 46.43837 1.000 76.77217  ? 103 PHE A CE2 1 
ATOM   773  C CZ  . PHE A 1 109 ? -22.14806 34.98030 46.09112 1.000 83.25161  ? 103 PHE A CZ  1 
ATOM   774  N N   . ILE A 1 110 ? -17.42343 36.52476 51.41144 1.000 70.73742  ? 104 ILE A N   1 
ATOM   775  C CA  . ILE A 1 110 ? -16.65321 36.67937 52.64115 1.000 70.86339  ? 104 ILE A CA  1 
ATOM   776  C C   . ILE A 1 110 ? -17.46227 37.51540 53.62295 1.000 82.29761  ? 104 ILE A C   1 
ATOM   777  O O   . ILE A 1 110 ? -17.83246 38.65473 53.31447 1.000 82.14266  ? 104 ILE A O   1 
ATOM   778  C CB  . ILE A 1 110 ? -15.28675 37.33449 52.38217 1.000 69.75700  ? 104 ILE A CB  1 
ATOM   779  C CG1 . ILE A 1 110 ? -14.40945 36.42996 51.51580 1.000 60.47160  ? 104 ILE A CG1 1 
ATOM   780  C CG2 . ILE A 1 110 ? -14.59533 37.67039 53.69422 1.000 78.22223  ? 104 ILE A CG2 1 
ATOM   781  C CD1 . ILE A 1 110 ? -13.08069 37.05106 51.14606 1.000 79.75085  ? 104 ILE A CD1 1 
ATOM   782  N N   . THR A 1 111 ? -17.73075 36.95712 54.80128 1.000 77.80210  ? 105 THR A N   1 
ATOM   783  C CA  . THR A 1 111 ? -18.37019 37.71685 55.86486 1.000 68.25467  ? 105 THR A CA  1 
ATOM   784  C C   . THR A 1 111 ? -17.32190 38.49744 56.64448 1.000 70.21259  ? 105 THR A C   1 
ATOM   785  O O   . THR A 1 111 ? -16.24182 37.98531 56.95084 1.000 83.07860  ? 105 THR A O   1 
ATOM   786  C CB  . THR A 1 111 ? -19.15086 36.79886 56.80658 1.000 74.97733  ? 105 THR A CB  1 
ATOM   787  O OG1 . THR A 1 111 ? -18.24646 35.93244 57.50363 1.000 87.79049  ? 105 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 111 ? -20.14784 35.96418 56.02092 1.000 77.94814  ? 105 THR A CG2 1 
ATOM   789  N N   . VAL A 1 112 ? -17.64833 39.74519 56.96132 1.000 78.01548  ? 106 VAL A N   1 
ATOM   790  C CA  . VAL A 1 112 ? -16.72210 40.67543 57.59140 1.000 76.58347  ? 106 VAL A CA  1 
ATOM   791  C C   . VAL A 1 112 ? -17.29982 41.11789 58.92822 1.000 80.27978  ? 106 VAL A C   1 
ATOM   792  O O   . VAL A 1 112 ? -18.51399 41.31319 59.05636 1.000 86.02061  ? 106 VAL A O   1 
ATOM   793  C CB  . VAL A 1 112 ? -16.45043 41.89047 56.67781 1.000 81.19648  ? 106 VAL A CB  1 
ATOM   794  C CG1 . VAL A 1 112 ? -15.57261 42.90969 57.37641 1.000 96.38815  ? 106 VAL A CG1 1 
ATOM   795  C CG2 . VAL A 1 112 ? -15.80761 41.44083 55.37396 1.000 86.11334  ? 106 VAL A CG2 1 
ATOM   796  N N   . ASN A 1 113 ? -16.42697 41.25920 59.92642 1.000 74.68495  ? 107 ASN A N   1 
ATOM   797  C CA  . ASN A 1 113 ? -16.77552 41.84940 61.21885 1.000 65.31659  ? 107 ASN A CA  1 
ATOM   798  C C   . ASN A 1 113 ? -15.68749 42.86450 61.56175 1.000 75.41613  ? 107 ASN A C   1 
ATOM   799  O O   . ASN A 1 113 ? -14.63009 42.49903 62.08371 1.000 74.78405  ? 107 ASN A O   1 
ATOM   800  C CB  . ASN A 1 113 ? -16.90906 40.78382 62.30347 1.000 73.18855  ? 107 ASN A CB  1 
ATOM   801  C CG  . ASN A 1 113 ? -17.39897 41.35063 63.62764 1.000 78.64279  ? 107 ASN A CG  1 
ATOM   802  O OD1 . ASN A 1 113 ? -17.42412 42.56492 63.82846 1.000 76.14883  ? 107 ASN A OD1 1 
ATOM   803  N ND2 . ASN A 1 113 ? -17.78241 40.46643 64.54333 1.000 74.84082  ? 107 ASN A ND2 1 
ATOM   804  N N   . ILE A 1 114 ? -15.95117 44.14394 61.27304 1.000 73.12800  ? 108 ILE A N   1 
ATOM   805  C CA  . ILE A 1 114 ? -14.96466 45.19751 61.50909 1.000 71.95668  ? 108 ILE A CA  1 
ATOM   806  C C   . ILE A 1 114 ? -14.88070 45.62349 62.96321 1.000 71.80874  ? 108 ILE A C   1 
ATOM   807  O O   . ILE A 1 114 ? -14.09914 46.52756 63.28648 1.000 83.39871  ? 108 ILE A O   1 
ATOM   808  C CB  . ILE A 1 114 ? -15.26654 46.45831 60.67570 1.000 64.67493  ? 108 ILE A CB  1 
ATOM   809  C CG1 . ILE A 1 114 ? -16.58108 47.08519 61.13707 1.000 60.24914  ? 108 ILE A CG1 1 
ATOM   810  C CG2 . ILE A 1 114 ? -15.32428 46.12307 59.19807 1.000 61.99303  ? 108 ILE A CG2 1 
ATOM   811  C CD1 . ILE A 1 114 ? -16.89447 48.38869 60.46327 1.000 64.61922  ? 108 ILE A CD1 1 
ATOM   812  N N   . ASP A 1 115 ? -15.66243 45.01236 63.85226 1.000 72.01970  ? 109 ASP A N   1 
ATOM   813  C CA  . ASP A 1 115 ? -15.68649 45.43178 65.25484 1.000 63.53107  ? 109 ASP A CA  1 
ATOM   814  C C   . ASP A 1 115 ? -16.04288 44.20672 66.09804 1.000 82.39567  ? 109 ASP A C   1 
ATOM   815  O O   . ASP A 1 115 ? -17.20408 44.00101 66.45278 1.000 101.19000 ? 109 ASP A O   1 
ATOM   816  C CB  . ASP A 1 115 ? -16.67223 46.57090 65.47327 1.000 73.89047  ? 109 ASP A CB  1 
ATOM   817  C CG  . ASP A 1 115 ? -16.73004 47.03085 66.92071 1.000 87.17145  ? 109 ASP A CG  1 
ATOM   818  O OD1 . ASP A 1 115 ? -15.84501 46.64496 67.71253 1.000 91.64915  ? 109 ASP A OD1 1 
ATOM   819  O OD2 . ASP A 1 115 ? -17.66843 47.77871 67.26941 1.000 85.18783  ? 109 ASP A OD2 1 
ATOM   820  N N   . LYS A 1 116 ? -15.03295 43.40028 66.41135 1.000 86.21316  ? 110 LYS A N   1 
ATOM   821  C CA  . LYS A 1 116 ? -15.23291 42.27687 67.31426 1.000 89.50955  ? 110 LYS A CA  1 
ATOM   822  C C   . LYS A 1 116 ? -14.99715 42.64548 68.77127 1.000 87.85087  ? 110 LYS A C   1 
ATOM   823  O O   . LYS A 1 116 ? -15.30377 41.83876 69.65510 1.000 108.35355 ? 110 LYS A O   1 
ATOM   824  C CB  . LYS A 1 116 ? -14.32717 41.10602 66.91817 1.000 93.17364  ? 110 LYS A CB  1 
ATOM   825  C CG  . LYS A 1 116 ? -14.60622 40.58340 65.51696 1.000 105.91834 ? 110 LYS A CG  1 
ATOM   826  C CD  . LYS A 1 116 ? -13.98823 39.21783 65.26730 1.000 120.78927 ? 110 LYS A CD  1 
ATOM   827  C CE  . LYS A 1 116 ? -14.32702 38.72316 63.86566 1.000 129.56959 ? 110 LYS A CE  1 
ATOM   828  N NZ  . LYS A 1 116 ? -13.72421 37.39707 63.55624 1.000 140.13096 ? 110 LYS A NZ  1 
ATOM   829  N N   . LYS A 1 117 ? -14.47172 43.84228 69.04215 1.000 95.26501  ? 111 LYS A N   1 
ATOM   830  C CA  . LYS A 1 117 ? -14.30942 44.27878 70.42443 1.000 101.05864 ? 111 LYS A CA  1 
ATOM   831  C C   . LYS A 1 117 ? -15.64957 44.65191 71.04871 1.000 105.14515 ? 111 LYS A C   1 
ATOM   832  O O   . LYS A 1 117 ? -15.93206 44.27899 72.19345 1.000 114.01888 ? 111 LYS A O   1 
ATOM   833  C CB  . LYS A 1 117 ? -13.33888 45.45774 70.49415 1.000 98.11015  ? 111 LYS A CB  1 
ATOM   834  C CG  . LYS A 1 117 ? -13.09561 45.96772 71.90741 1.000 116.67545 ? 111 LYS A CG  1 
ATOM   835  C CD  . LYS A 1 117 ? -12.11607 47.13262 71.92955 1.000 124.32518 ? 111 LYS A CD  1 
ATOM   836  C CE  . LYS A 1 117 ? -12.64971 48.32299 71.14927 1.000 120.70592 ? 111 LYS A CE  1 
ATOM   837  N NZ  . LYS A 1 117 ? -11.74191 49.50209 71.22827 1.000 123.03720 ? 111 LYS A NZ  1 
ATOM   838  N N   . ASN A 1 118 ? -16.49087 45.38252 70.31320 1.000 97.22483  ? 112 ASN A N   1 
ATOM   839  C CA  . ASN A 1 118 ? -17.76645 45.84972 70.83521 1.000 91.92792  ? 112 ASN A CA  1 
ATOM   840  C C   . ASN A 1 118 ? -18.97391 45.38745 70.03277 1.000 96.11546  ? 112 ASN A C   1 
ATOM   841  O O   . ASN A 1 118 ? -20.10520 45.59116 70.48925 1.000 89.56026  ? 112 ASN A O   1 
ATOM   842  C CB  . ASN A 1 118 ? -17.77793 47.38391 70.91758 1.000 100.71130 ? 112 ASN A CB  1 
ATOM   843  C CG  . ASN A 1 118 ? -16.65707 47.92456 71.78218 1.000 115.24980 ? 112 ASN A CG  1 
ATOM   844  O OD1 . ASN A 1 118 ? -15.82786 48.71064 71.32490 1.000 111.59960 ? 112 ASN A OD1 1 
ATOM   845  N ND2 . ASN A 1 118 ? -16.62133 47.49643 73.03924 1.000 107.74528 ? 112 ASN A ND2 1 
ATOM   846  N N   . ASN A 1 119 ? -18.77050 44.77452 68.86506 1.000 87.77753  ? 113 ASN A N   1 
ATOM   847  C CA  . ASN A 1 119 ? -19.85796 44.23046 68.04902 1.000 89.22051  ? 113 ASN A CA  1 
ATOM   848  C C   . ASN A 1 119 ? -20.93375 45.27821 67.77990 1.000 88.69486  ? 113 ASN A C   1 
ATOM   849  O O   . ASN A 1 119 ? -22.13344 45.01557 67.88625 1.000 93.55601  ? 113 ASN A O   1 
ATOM   850  C CB  . ASN A 1 119 ? -20.45171 42.97600 68.69054 1.000 75.02126  ? 113 ASN A CB  1 
ATOM   851  C CG  . ASN A 1 119 ? -19.50498 41.79112 68.62594 1.000 113.85013 ? 113 ASN A CG  1 
ATOM   852  O OD1 . ASN A 1 119 ? -19.45113 41.07826 67.62288 1.000 107.16441 ? 113 ASN A OD1 1 
ATOM   853  N ND2 . ASN A 1 119 ? -18.74792 41.57902 69.69592 1.000 113.01342 ? 113 ASN A ND2 1 
ATOM   854  N N   . VAL A 1 120 ? -20.48999 46.48680 67.43120 1.000 81.50339  ? 114 VAL A N   1 
ATOM   855  C CA  . VAL A 1 120 ? -21.37291 47.56297 67.01076 1.000 64.82721  ? 114 VAL A CA  1 
ATOM   856  C C   . VAL A 1 120 ? -21.09487 47.98916 65.57634 1.000 72.99773  ? 114 VAL A C   1 
ATOM   857  O O   . VAL A 1 120 ? -22.02914 48.21734 64.79924 1.000 84.76322  ? 114 VAL A O   1 
ATOM   858  C CB  . VAL A 1 120 ? -21.26734 48.77385 67.96366 1.000 79.90837  ? 114 VAL A CB  1 
ATOM   859  C CG1 . VAL A 1 120 ? -22.04736 49.96101 67.41384 1.000 60.88325  ? 114 VAL A CG1 1 
ATOM   860  C CG2 . VAL A 1 120 ? -21.76502 48.39971 69.34938 1.000 71.34392  ? 114 VAL A CG2 1 
ATOM   861  N N   . GLY A 1 121 ? -19.82256 48.08703 65.20094 1.000 72.87400  ? 115 GLY A N   1 
ATOM   862  C CA  . GLY A 1 121 ? -19.48204 48.53921 63.86448 1.000 74.20178  ? 115 GLY A CA  1 
ATOM   863  C C   . GLY A 1 121 ? -19.93288 47.55082 62.80374 1.000 69.51964  ? 115 GLY A C   1 
ATOM   864  O O   . GLY A 1 121 ? -19.76165 46.33810 62.93601 1.000 81.47137  ? 115 GLY A O   1 
ATOM   865  N N   . LEU A 1 122 ? -20.51574 48.08599 61.73575 1.000 73.33931  ? 116 LEU A N   1 
ATOM   866  C CA  . LEU A 1 122 ? -21.03430 47.28927 60.63637 1.000 67.96372  ? 116 LEU A CA  1 
ATOM   867  C C   . LEU A 1 122 ? -20.33681 47.67159 59.33952 1.000 74.24062  ? 116 LEU A C   1 
ATOM   868  O O   . LEU A 1 122 ? -19.92139 48.81946 59.15308 1.000 71.51599  ? 116 LEU A O   1 
ATOM   869  C CB  . LEU A 1 122 ? -22.54418 47.48163 60.47526 1.000 61.34187  ? 116 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 122 ? -23.41231 47.08339 61.66531 1.000 67.01283  ? 116 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 122 ? -24.87508 47.34961 61.35607 1.000 63.17765  ? 116 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 122 ? -23.18643 45.62258 62.00722 1.000 70.26420  ? 116 LEU A CD2 1 
ATOM   873  N N   . LEU A 1 123 ? -20.21038 46.69704 58.44326 1.000 63.42324  ? 117 LEU A N   1 
ATOM   874  C CA  . LEU A 1 123 ? -19.71792 46.96471 57.09923 1.000 59.16504  ? 117 LEU A CA  1 
ATOM   875  C C   . LEU A 1 123 ? -20.87387 47.44789 56.23573 1.000 68.90013  ? 117 LEU A C   1 
ATOM   876  O O   . LEU A 1 123 ? -21.89874 46.76778 56.12654 1.000 71.89861  ? 117 LEU A O   1 
ATOM   877  C CB  . LEU A 1 123 ? -19.08670 45.71598 56.49082 1.000 59.82399  ? 117 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 123 ? -18.79502 45.82649 54.99097 1.000 69.19577  ? 117 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 123 ? -17.71144 46.86149 54.73068 1.000 63.34525  ? 117 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 123 ? -18.41403 44.47750 54.39851 1.000 68.47657  ? 117 LEU A CD2 1 
ATOM   881  N N   . LEU A 1 124 ? -20.71767 48.62259 55.63158 1.000 67.87024  ? 118 LEU A N   1 
ATOM   882  C CA  . LEU A 1 124 ? -21.71246 49.14657 54.70705 1.000 68.54447  ? 118 LEU A CA  1 
ATOM   883  C C   . LEU A 1 124 ? -21.26269 49.11541 53.25761 1.000 65.80762  ? 118 LEU A C   1 
ATOM   884  O O   . LEU A 1 124 ? -22.10780 49.04389 52.36413 1.000 77.55277  ? 118 LEU A O   1 
ATOM   885  C CB  . LEU A 1 124 ? -22.08335 50.58895 55.07771 1.000 57.79330  ? 118 LEU A CB  1 
ATOM   886  C CG  . LEU A 1 124 ? -22.67382 50.80336 56.47180 1.000 55.84536  ? 118 LEU A CG  1 
ATOM   887  C CD1 . LEU A 1 124 ? -23.16549 52.23336 56.62630 1.000 61.10156  ? 118 LEU A CD1 1 
ATOM   888  C CD2 . LEU A 1 124 ? -23.79572 49.81440 56.73183 1.000 59.13209  ? 118 LEU A CD2 1 
ATOM   889  N N   . GLY A 1 125 ? -19.96865 49.14689 53.00926 1.000 70.37468  ? 119 GLY A N   1 
ATOM   890  C CA  . GLY A 1 125 ? -19.44882 49.28019 51.65246 1.000 70.99027  ? 119 GLY A CA  1 
ATOM   891  C C   . GLY A 1 125 ? -19.22376 50.74507 51.30377 1.000 68.51834  ? 119 GLY A C   1 
ATOM   892  O O   . GLY A 1 125 ? -18.39519 51.40404 51.92451 1.000 70.55590  ? 119 GLY A O   1 
ATOM   893  N N   . CYS A 1 126 ? -19.96147 51.24278 50.31751 1.000 73.16313  ? 120 CYS A N   1 
ATOM   894  C CA  . CYS A 1 126 ? -20.88569 50.44458 49.52070 1.000 63.01928  ? 120 CYS A CA  1 
ATOM   895  C C   . CYS A 1 126 ? -20.50938 50.66433 48.06586 1.000 66.49781  ? 120 CYS A C   1 
ATOM   896  O O   . CYS A 1 126 ? -20.80428 51.71976 47.50685 1.000 78.29952  ? 120 CYS A O   1 
ATOM   897  C CB  . CYS A 1 126 ? -22.33535 50.85769 49.78922 1.000 66.24293  ? 120 CYS A CB  1 
ATOM   898  S SG  . CYS A 1 126 ? -23.58593 50.05020 48.76386 1.000 73.08560  ? 120 CYS A SG  1 
ATOM   899  N N   . PHE A 1 127 ? -19.84314 49.69085 47.44796 1.000 65.46812  ? 121 PHE A N   1 
ATOM   900  C CA  . PHE A 1 127 ? -19.18776 49.99105 46.18411 1.000 61.57894  ? 121 PHE A CA  1 
ATOM   901  C C   . PHE A 1 127 ? -18.87301 48.72182 45.40518 1.000 65.67240  ? 121 PHE A C   1 
ATOM   902  O O   . PHE A 1 127 ? -18.85298 47.61409 45.94948 1.000 68.36266  ? 121 PHE A O   1 
ATOM   903  C CB  . PHE A 1 127 ? -17.90208 50.79550 46.41907 1.000 71.66599  ? 121 PHE A CB  1 
ATOM   904  C CG  . PHE A 1 127 ? -16.86471 50.06775 47.22603 1.000 66.21285  ? 121 PHE A CG  1 
ATOM   905  C CD1 . PHE A 1 127 ? -16.87113 50.13585 48.60979 1.000 68.42936  ? 121 PHE A CD1 1 
ATOM   906  C CD2 . PHE A 1 127 ? -15.87478 49.32624 46.60057 1.000 72.27299  ? 121 PHE A CD2 1 
ATOM   907  C CE1 . PHE A 1 127 ? -15.91643 49.47196 49.35470 1.000 65.30812  ? 121 PHE A CE1 1 
ATOM   908  C CE2 . PHE A 1 127 ? -14.91607 48.65855 47.33999 1.000 65.20416  ? 121 PHE A CE2 1 
ATOM   909  C CZ  . PHE A 1 127 ? -14.93689 48.73176 48.71855 1.000 82.67688  ? 121 PHE A CZ  1 
ATOM   910  N N   . TRP A 1 128 ? -18.62810 48.91581 44.11015 1.000 69.21147  ? 122 TRP A N   1 
ATOM   911  C CA  . TRP A 1 128 ? -18.03596 47.91960 43.23224 1.000 67.17453  ? 122 TRP A CA  1 
ATOM   912  C C   . TRP A 1 128 ? -16.71798 48.46359 42.69982 1.000 66.23450  ? 122 TRP A C   1 
ATOM   913  O O   . TRP A 1 128 ? -16.52656 49.67866 42.60589 1.000 73.80582  ? 122 TRP A O   1 
ATOM   914  C CB  . TRP A 1 128 ? -18.94707 47.57293 42.04389 1.000 67.83969  ? 122 TRP A CB  1 
ATOM   915  C CG  . TRP A 1 128 ? -20.24893 46.91225 42.39417 1.000 66.93372  ? 122 TRP A CG  1 
ATOM   916  C CD1 . TRP A 1 128 ? -21.04791 47.17962 43.46653 1.000 67.85176  ? 122 TRP A CD1 1 
ATOM   917  C CD2 . TRP A 1 128 ? -20.90079 45.86862 41.65873 1.000 75.30872  ? 122 TRP A CD2 1 
ATOM   918  N NE1 . TRP A 1 128 ? -22.15791 46.36917 43.44441 1.000 69.59374  ? 122 TRP A NE1 1 
ATOM   919  C CE2 . TRP A 1 128 ? -22.09041 45.55391 42.34529 1.000 58.11848  ? 122 TRP A CE2 1 
ATOM   920  C CE3 . TRP A 1 128 ? -20.59210 45.16903 40.48640 1.000 73.03620  ? 122 TRP A CE3 1 
ATOM   921  C CZ2 . TRP A 1 128 ? -22.97218 44.57087 41.89900 1.000 68.65547  ? 122 TRP A CZ2 1 
ATOM   922  C CZ3 . TRP A 1 128 ? -21.46891 44.19275 40.04474 1.000 68.89180  ? 122 TRP A CZ3 1 
ATOM   923  C CH2 . TRP A 1 128 ? -22.64447 43.90367 40.74920 1.000 72.74679  ? 122 TRP A CH2 1 
ATOM   924  N N   . VAL A 1 129 ? -15.81003 47.55906 42.34785 1.000 65.79150  ? 123 VAL A N   1 
ATOM   925  C CA  . VAL A 1 129 ? -14.54912 47.93655 41.71647 1.000 64.62640  ? 123 VAL A CA  1 
ATOM   926  C C   . VAL A 1 129 ? -14.04815 46.74225 40.91738 1.000 69.24636  ? 123 VAL A C   1 
ATOM   927  O O   . VAL A 1 129 ? -14.19794 45.59178 41.33932 1.000 73.51952  ? 123 VAL A O   1 
ATOM   928  C CB  . VAL A 1 129 ? -13.51305 48.41719 42.75840 1.000 68.54964  ? 123 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 129 ? -13.28098 47.35657 43.81816 1.000 71.39740  ? 123 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 129 ? -12.20405 48.80847 42.08233 1.000 69.23930  ? 123 VAL A CG2 1 
ATOM   931  N N   . SER A 1 130 ? -13.47008 47.01780 39.74844 1.000 67.50166  ? 124 SER A N   1 
ATOM   932  C CA  . SER A 1 130 ? -13.05929 45.96516 38.83044 1.000 72.64237  ? 124 SER A CA  1 
ATOM   933  C C   . SER A 1 130 ? -11.82394 46.39255 38.05035 1.000 78.83148  ? 124 SER A C   1 
ATOM   934  O O   . SER A 1 130 ? -11.73766 47.53183 37.58393 1.000 83.77694  ? 124 SER A O   1 
ATOM   935  C CB  . SER A 1 130 ? -14.18920 45.61377 37.85649 1.000 68.91525  ? 124 SER A CB  1 
ATOM   936  O OG  . SER A 1 130 ? -13.69866 44.86558 36.75798 1.000 71.82121  ? 124 SER A OG  1 
ATOM   937  N N   . ASP A 1 131 ? -10.87037 45.46781 37.92095 1.000 73.43470  ? 125 ASP A N   1 
ATOM   938  C CA  . ASP A 1 131 ? -9.70814  45.60094 37.04057 1.000 75.46033  ? 125 ASP A CA  1 
ATOM   939  C C   . ASP A 1 131 ? -8.86260  46.83494 37.34041 1.000 79.27366  ? 125 ASP A C   1 
ATOM   940  O O   . ASP A 1 131 ? -8.02709  47.22193 36.51731 1.000 85.41549  ? 125 ASP A O   1 
ATOM   941  C CB  . ASP A 1 131 ? -10.13052 45.61377 35.56585 1.000 89.73499  ? 125 ASP A CB  1 
ATOM   942  C CG  . ASP A 1 131 ? -10.69165 44.28280 35.10649 1.000 85.36054  ? 125 ASP A CG  1 
ATOM   943  O OD1 . ASP A 1 131 ? -10.78963 43.35634 35.93817 1.000 78.17986  ? 125 ASP A OD1 1 
ATOM   944  O OD2 . ASP A 1 131 ? -11.03235 44.16304 33.91059 1.000 81.24286  ? 125 ASP A OD2 1 
ATOM   945  N N   . ASP A 1 132 ? -9.05346  47.45831 38.50482 1.000 73.79156  ? 126 ASP A N   1 
ATOM   946  C CA  . ASP A 1 132 ? -8.37399  48.71050 38.84249 1.000 82.98541  ? 126 ASP A CA  1 
ATOM   947  C C   . ASP A 1 132 ? -8.59934  49.76104 37.75749 1.000 91.16524  ? 126 ASP A C   1 
ATOM   948  O O   . ASP A 1 132 ? -7.69193  50.50936 37.38747 1.000 84.22417  ? 126 ASP A O   1 
ATOM   949  C CB  . ASP A 1 132 ? -6.87754  48.48578 39.07945 1.000 67.59121  ? 126 ASP A CB  1 
ATOM   950  C CG  . ASP A 1 132 ? -6.58422  47.84141 40.42303 1.000 88.63550  ? 126 ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 132 ? -7.51806  47.69704 41.24039 1.000 90.95251  ? 126 ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 132 ? -5.41225  47.48291 40.66284 1.000 83.43473  ? 126 ASP A OD2 1 
ATOM   953  N N   . GLU A 1 133 ? -9.82470  49.80651 37.23130 1.000 85.88409  ? 127 GLU A N   1 
ATOM   954  C CA  . GLU A 1 133 ? -10.15661 50.71697 36.14094 1.000 77.56517  ? 127 GLU A CA  1 
ATOM   955  C C   . GLU A 1 133 ? -11.54569 51.31964 36.31165 1.000 82.26243  ? 127 GLU A C   1 
ATOM   956  O O   . GLU A 1 133 ? -11.71461 52.53831 36.20394 1.000 95.10773  ? 127 GLU A O   1 
ATOM   957  C CB  . GLU A 1 133 ? -10.06419 49.99698 34.79426 1.000 78.37225  ? 127 GLU A CB  1 
ATOM   958  C CG  . GLU A 1 133 ? -8.64817  49.78830 34.28912 1.000 84.58186  ? 127 GLU A CG  1 
ATOM   959  C CD  . GLU A 1 133 ? -8.61383  49.04954 32.96785 1.000 105.62916 ? 127 GLU A CD  1 
ATOM   960  O OE1 . GLU A 1 133 ? -9.68969  48.61845 32.50110 1.000 102.10110 ? 127 GLU A OE1 1 
ATOM   961  O OE2 . GLU A 1 133 ? -7.51381  48.89918 32.39602 1.000 130.34824 ? 127 GLU A OE2 1 
ATOM   962  N N   . ARG A 1 134 ? -12.54269 50.47967 36.57416 1.000 80.80015  ? 128 ARG A N   1 
ATOM   963  C CA  . ARG A 1 134 ? -13.92270 50.91304 36.73137 1.000 69.76870  ? 128 ARG A CA  1 
ATOM   964  C C   . ARG A 1 134 ? -14.39015 50.67835 38.16052 1.000 71.00519  ? 128 ARG A C   1 
ATOM   965  O O   . ARG A 1 134 ? -13.90135 49.77929 38.85052 1.000 82.03018  ? 128 ARG A O   1 
ATOM   966  C CB  . ARG A 1 134 ? -14.84576 50.17045 35.76293 1.000 69.23557  ? 128 ARG A CB  1 
ATOM   967  C CG  . ARG A 1 134 ? -14.68210 50.58010 34.31760 1.000 85.08127  ? 128 ARG A CG  1 
ATOM   968  C CD  . ARG A 1 134 ? -15.21659 49.51033 33.39128 1.000 82.30093  ? 128 ARG A CD  1 
ATOM   969  N NE  . ARG A 1 134 ? -14.47397 48.26557 33.53540 1.000 88.35604  ? 128 ARG A NE  1 
ATOM   970  C CZ  . ARG A 1 134 ? -13.29492 48.03579 32.97612 1.000 86.35662  ? 128 ARG A CZ  1 
ATOM   971  N NH1 . ARG A 1 134 ? -12.69616 48.94860 32.22930 1.000 84.46294  ? 128 ARG A NH1 1 
ATOM   972  N NH2 . ARG A 1 134 ? -12.69986 46.86313 33.17430 1.000 107.49738 ? 128 ARG A NH2 1 
ATOM   973  N N   . CYS A 1 135 ? -15.35299 51.48752 38.59632 1.000 66.27559  ? 129 CYS A N   1 
ATOM   974  C CA  . CYS A 1 135 ? -15.87750 51.35478 39.94709 1.000 69.22400  ? 129 CYS A CA  1 
ATOM   975  C C   . CYS A 1 135 ? -17.22542 52.05191 40.04624 1.000 70.92949  ? 129 CYS A C   1 
ATOM   976  O O   . CYS A 1 135 ? -17.51607 52.99939 39.31188 1.000 67.60865  ? 129 CYS A O   1 
ATOM   977  C CB  . CYS A 1 135 ? -14.91003 51.93404 40.98301 1.000 66.73826  ? 129 CYS A CB  1 
ATOM   978  S SG  . CYS A 1 135 ? -14.76302 53.73402 40.92165 1.000 76.56792  ? 129 CYS A SG  1 
ATOM   979  N N   . TYR A 1 136 ? -18.04655 51.55568 40.96591 1.000 71.89161  ? 130 TYR A N   1 
ATOM   980  C CA  . TYR A 1 136 ? -19.25530 52.23115 41.41203 1.000 65.56253  ? 130 TYR A CA  1 
ATOM   981  C C   . TYR A 1 136 ? -19.12812 52.50154 42.90198 1.000 72.25550  ? 130 TYR A C   1 
ATOM   982  O O   . TYR A 1 136 ? -18.61881 51.66124 43.64477 1.000 75.11115  ? 130 TYR A O   1 
ATOM   983  C CB  . TYR A 1 136 ? -20.51067 51.38981 41.14087 1.000 68.77996  ? 130 TYR A CB  1 
ATOM   984  C CG  . TYR A 1 136 ? -21.73673 51.85096 41.90338 1.000 63.33849  ? 130 TYR A CG  1 
ATOM   985  C CD1 . TYR A 1 136 ? -22.55607 52.85245 41.39899 1.000 71.68791  ? 130 TYR A CD1 1 
ATOM   986  C CD2 . TYR A 1 136 ? -22.07612 51.28241 43.12734 1.000 61.56991  ? 130 TYR A CD2 1 
ATOM   987  C CE1 . TYR A 1 136 ? -23.67570 53.27864 42.09276 1.000 62.99814  ? 130 TYR A CE1 1 
ATOM   988  C CE2 . TYR A 1 136 ? -23.19305 51.70441 43.82920 1.000 62.68643  ? 130 TYR A CE2 1 
ATOM   989  C CZ  . TYR A 1 136 ? -23.98856 52.70093 43.30613 1.000 64.51660  ? 130 TYR A CZ  1 
ATOM   990  O OH  . TYR A 1 136 ? -25.10137 53.12149 43.99933 1.000 72.41265  ? 130 TYR A OH  1 
ATOM   991  N N   . VAL A 1 137 ? -19.58107 53.67254 43.33818 1.000 70.02124  ? 131 VAL A N   1 
ATOM   992  C CA  . VAL A 1 137 ? -19.66070 53.98931 44.75929 1.000 66.82558  ? 131 VAL A CA  1 
ATOM   993  C C   . VAL A 1 137 ? -20.95016 54.76099 45.00116 1.000 61.21747  ? 131 VAL A C   1 
ATOM   994  O O   . VAL A 1 137 ? -21.32302 55.63515 44.21158 1.000 69.24939  ? 131 VAL A O   1 
ATOM   995  C CB  . VAL A 1 137 ? -18.42410 54.77535 45.25164 1.000 67.86654  ? 131 VAL A CB  1 
ATOM   996  C CG1 . VAL A 1 137 ? -18.26555 56.08979 44.49446 1.000 70.24076  ? 131 VAL A CG1 1 
ATOM   997  C CG2 . VAL A 1 137 ? -18.50984 55.01666 46.75571 1.000 57.41571  ? 131 VAL A CG2 1 
ATOM   998  N N   . GLY A 1 138 ? -21.64552 54.41527 46.08037 1.000 50.36945  ? 132 GLY A N   1 
ATOM   999  C CA  . GLY A 1 138 ? -22.92422 55.02549 46.37817 1.000 70.43290  ? 132 GLY A CA  1 
ATOM   1000 C C   . GLY A 1 138 ? -23.65875 54.33795 47.50883 1.000 65.06539  ? 132 GLY A C   1 
ATOM   1001 O O   . GLY A 1 138 ? -23.04456 53.92646 48.49712 1.000 66.73111  ? 132 GLY A O   1 
ATOM   1002 N N   . ASN A 1 139 ? -24.97955 54.20082 47.37396 1.000 70.89981  ? 133 ASN A N   1 
ATOM   1003 C CA  . ASN A 1 139 ? -25.80367 53.62373 48.42959 1.000 65.67612  ? 133 ASN A CA  1 
ATOM   1004 C C   . ASN A 1 139 ? -26.72694 52.52823 47.90765 1.000 68.16929  ? 133 ASN A C   1 
ATOM   1005 O O   . ASN A 1 139 ? -27.75869 52.24944 48.52669 1.000 73.51501  ? 133 ASN A O   1 
ATOM   1006 C CB  . ASN A 1 139 ? -26.61894 54.71363 49.12719 1.000 55.70941  ? 133 ASN A CB  1 
ATOM   1007 C CG  . ASN A 1 139 ? -27.25661 55.67521 48.14785 1.000 70.14429  ? 133 ASN A CG  1 
ATOM   1008 O OD1 . ASN A 1 139 ? -28.26275 55.35795 47.51520 1.000 76.12847  ? 133 ASN A OD1 1 
ATOM   1009 N ND2 . ASN A 1 139 ? -26.67317 56.86035 48.01752 1.000 67.86940  ? 133 ASN A ND2 1 
ATOM   1010 N N   . ALA A 1 140 ? -26.38189 51.90253 46.78574 1.000 71.90705  ? 134 ALA A N   1 
ATOM   1011 C CA  . ALA A 1 140 ? -27.14665 50.78470 46.23839 1.000 60.00630  ? 134 ALA A CA  1 
ATOM   1012 C C   . ALA A 1 140 ? -26.42178 49.49521 46.60599 1.000 68.59943  ? 134 ALA A C   1 
ATOM   1013 O O   . ALA A 1 140 ? -25.43403 49.12224 45.96821 1.000 71.38403  ? 134 ALA A O   1 
ATOM   1014 C CB  . ALA A 1 140 ? -27.31213 50.92041 44.72896 1.000 69.19604  ? 134 ALA A CB  1 
ATOM   1015 N N   . SER A 1 141 ? -26.91385 48.81597 47.63922 1.000 68.58611  ? 135 SER A N   1 
ATOM   1016 C CA  . SER A 1 141 ? -26.33064 47.54989 48.05129 1.000 67.16294  ? 135 SER A CA  1 
ATOM   1017 C C   . SER A 1 141 ? -26.51865 46.49582 46.96240 1.000 65.80968  ? 135 SER A C   1 
ATOM   1018 O O   . SER A 1 141 ? -27.31620 46.65004 46.03315 1.000 69.43023  ? 135 SER A O   1 
ATOM   1019 C CB  . SER A 1 141 ? -26.95686 47.06750 49.35861 1.000 59.31870  ? 135 SER A CB  1 
ATOM   1020 O OG  . SER A 1 141 ? -26.59069 47.90120 50.44194 1.000 96.43304  ? 135 SER A OG  1 
ATOM   1021 N N   . PHE A 1 142 ? -25.76485 45.40369 47.08585 1.000 67.21834  ? 136 PHE A N   1 
ATOM   1022 C CA  . PHE A 1 142 ? -25.89023 44.27633 46.16363 1.000 69.66428  ? 136 PHE A CA  1 
ATOM   1023 C C   . PHE A 1 142 ? -27.13005 43.45067 46.52068 1.000 77.90231  ? 136 PHE A C   1 
ATOM   1024 O O   . PHE A 1 142 ? -27.06855 42.26623 46.85176 1.000 74.40374  ? 136 PHE A O   1 
ATOM   1025 C CB  . PHE A 1 142 ? -24.62502 43.42822 46.18355 1.000 59.71634  ? 136 PHE A CB  1 
ATOM   1026 C CG  . PHE A 1 142 ? -24.55726 42.40738 45.07767 1.000 74.58136  ? 136 PHE A CG  1 
ATOM   1027 C CD1 . PHE A 1 142 ? -25.47305 42.42323 44.03493 1.000 66.74646  ? 136 PHE A CD1 1 
ATOM   1028 C CD2 . PHE A 1 142 ? -23.57804 41.42858 45.08444 1.000 73.65013  ? 136 PHE A CD2 1 
ATOM   1029 C CE1 . PHE A 1 142 ? -25.41071 41.48582 43.02190 1.000 73.44844  ? 136 PHE A CE1 1 
ATOM   1030 C CE2 . PHE A 1 142 ? -23.51014 40.48962 44.07347 1.000 77.58081  ? 136 PHE A CE2 1 
ATOM   1031 C CZ  . PHE A 1 142 ? -24.42714 40.51802 43.04135 1.000 73.42202  ? 136 PHE A CZ  1 
ATOM   1032 N N   . THR A 1 143 ? -28.27746 44.11646 46.45444 1.000 60.83547  ? 137 THR A N   1 
ATOM   1033 C CA  . THR A 1 143 ? -29.56198 43.49954 46.73197 1.000 63.56416  ? 137 THR A CA  1 
ATOM   1034 C C   . THR A 1 143 ? -30.51047 43.80358 45.58515 1.000 64.31561  ? 137 THR A C   1 
ATOM   1035 O O   . THR A 1 143 ? -30.38322 44.82959 44.91130 1.000 76.93547  ? 137 THR A O   1 
ATOM   1036 C CB  . THR A 1 143 ? -30.16316 44.00692 48.04592 1.000 67.74552  ? 137 THR A CB  1 
ATOM   1037 O OG1 . THR A 1 143 ? -30.43603 45.41034 47.93488 1.000 69.50251  ? 137 THR A OG1 1 
ATOM   1038 C CG2 . THR A 1 143 ? -29.19565 43.77246 49.19815 1.000 69.88045  ? 137 THR A CG2 1 
ATOM   1039 N N   . GLY A 1 144 ? -31.46252 42.89653 45.36576 1.000 70.38958  ? 138 GLY A N   1 
ATOM   1040 C CA  . GLY A 1 144 ? -32.46797 43.13636 44.34463 1.000 73.88334  ? 138 GLY A CA  1 
ATOM   1041 C C   . GLY A 1 144 ? -33.25171 44.41240 44.58724 1.000 65.95497  ? 138 GLY A C   1 
ATOM   1042 O O   . GLY A 1 144 ? -33.67061 45.08478 43.64215 1.000 80.85491  ? 138 GLY A O   1 
ATOM   1043 N N   . GLY A 1 145 ? -33.45453 44.76725 45.85705 1.000 69.86999  ? 139 GLY A N   1 
ATOM   1044 C CA  . GLY A 1 145 ? -34.15132 46.00664 46.16447 1.000 63.71080  ? 139 GLY A CA  1 
ATOM   1045 C C   . GLY A 1 145 ? -33.39907 47.23562 45.68854 1.000 72.17934  ? 139 GLY A C   1 
ATOM   1046 O O   . GLY A 1 145 ? -33.95643 48.09355 44.99904 1.000 85.63619  ? 139 GLY A O   1 
ATOM   1047 N N   . SER A 1 146 ? -32.11688 47.33617 46.04815 1.000 75.13624  ? 140 SER A N   1 
ATOM   1048 C CA  . SER A 1 146 ? -31.32406 48.49991 45.66420 1.000 70.60768  ? 140 SER A CA  1 
ATOM   1049 C C   . SER A 1 146 ? -31.10843 48.59180 44.15915 1.000 62.29236  ? 140 SER A C   1 
ATOM   1050 O O   . SER A 1 146 ? -30.81949 49.68141 43.65259 1.000 72.41579  ? 140 SER A O   1 
ATOM   1051 C CB  . SER A 1 146 ? -29.97089 48.47662 46.37636 1.000 62.93683  ? 140 SER A CB  1 
ATOM   1052 O OG  . SER A 1 146 ? -30.12852 48.56259 47.78145 1.000 68.42729  ? 140 SER A OG  1 
ATOM   1053 N N   . ILE A 1 147 ? -31.24069 47.48017 43.43657 1.000 70.13830  ? 141 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 147 ? -31.03905 47.48846 41.99253 1.000 64.90097  ? 141 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 147 ? -32.32230 47.79444 41.22431 1.000 74.07433  ? 141 ILE A C   1 
ATOM   1056 O O   . ILE A 1 147 ? -32.25108 48.27055 40.08108 1.000 70.27410  ? 141 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 147 ? -30.43474 46.13849 41.55367 1.000 63.38570  ? 141 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 147 ? -29.07696 45.91831 42.22999 1.000 72.10807  ? 141 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 147 ? -30.27792 46.04292 40.03804 1.000 53.29681  ? 141 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 147 ? -28.42231 44.59858 41.86656 1.000 63.93001  ? 141 ILE A CD1 1 
ATOM   1061 N N   . HIS A 1 148 ? -33.49113 47.58414 41.83211 1.000 71.45957  ? 142 HIS A N   1 
ATOM   1062 C CA  . HIS A 1 148 ? -34.73570 47.59742 41.07362 1.000 63.64905  ? 142 HIS A CA  1 
ATOM   1063 C C   . HIS A 1 148 ? -35.81032 48.48561 41.69278 1.000 70.77095  ? 142 HIS A C   1 
ATOM   1064 O O   . HIS A 1 148 ? -36.37661 49.34606 41.00990 1.000 77.68235  ? 142 HIS A O   1 
ATOM   1065 C CB  . HIS A 1 148 ? -35.25635 46.16431 40.93325 1.000 70.29089  ? 142 HIS A CB  1 
ATOM   1066 C CG  . HIS A 1 148 ? -36.38838 46.01241 39.96341 1.000 72.56837  ? 142 HIS A CG  1 
ATOM   1067 N ND1 . HIS A 1 148 ? -36.43470 44.99306 39.03699 1.000 65.89038  ? 142 HIS A ND1 1 
ATOM   1068 C CD2 . HIS A 1 148 ? -37.52478 46.72924 39.78927 1.000 73.83967  ? 142 HIS A CD2 1 
ATOM   1069 C CE1 . HIS A 1 148 ? -37.54269 45.09618 38.32498 1.000 82.10361  ? 142 HIS A CE1 1 
ATOM   1070 N NE2 . HIS A 1 148 ? -38.22259 46.14109 38.76179 1.000 82.60724  ? 142 HIS A NE2 1 
ATOM   1071 N N   . THR A 1 149 ? -36.10875 48.28298 42.97713 1.000 75.59821  ? 143 THR A N   1 
ATOM   1072 C CA  . THR A 1 149 ? -37.32440 48.82090 43.57431 1.000 62.00192  ? 143 THR A CA  1 
ATOM   1073 C C   . THR A 1 149 ? -37.09521 49.90824 44.61720 1.000 65.37529  ? 143 THR A C   1 
ATOM   1074 O O   . THR A 1 149 ? -38.06988 50.52890 45.05775 1.000 77.25610  ? 143 THR A O   1 
ATOM   1075 C CB  . THR A 1 149 ? -38.13673 47.68499 44.21266 1.000 55.02309  ? 143 THR A CB  1 
ATOM   1076 O OG1 . THR A 1 149 ? -37.40917 47.14396 45.32071 1.000 76.08984  ? 143 THR A OG1 1 
ATOM   1077 C CG2 . THR A 1 149 ? -38.38246 46.57845 43.19960 1.000 66.47233  ? 143 THR A CG2 1 
ATOM   1078 N N   . ILE A 1 150 ? -35.85440 50.15978 45.02334 1.000 75.28000  ? 144 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 150 ? -35.53812 51.15318 46.04396 1.000 69.67697  ? 144 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 150 ? -34.74304 52.27457 45.39298 1.000 59.00057  ? 144 ILE A C   1 
ATOM   1081 O O   . ILE A 1 150 ? -33.81249 52.01596 44.62076 1.000 81.27055  ? 144 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 150 ? -34.75318 50.53014 47.21158 1.000 73.90590  ? 144 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 150 ? -35.56680 49.41309 47.86673 1.000 73.18316  ? 144 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 150 ? -34.38034 51.59162 48.23851 1.000 64.55426  ? 144 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 150 ? -34.79642 48.63607 48.90875 1.000 70.72812  ? 144 ILE A CD1 1 
ATOM   1086 N N   . LYS A 1 151 ? -35.10821 53.51605 45.70079 1.000 64.31230  ? 145 LYS A N   1 
ATOM   1087 C CA  . LYS A 1 151 ? -34.37452 54.65803 45.17386 1.000 66.18525  ? 145 LYS A CA  1 
ATOM   1088 C C   . LYS A 1 151 ? -32.97335 54.70097 45.76949 1.000 70.04905  ? 145 LYS A C   1 
ATOM   1089 O O   . LYS A 1 151 ? -32.80523 54.64588 46.99133 1.000 74.92931  ? 145 LYS A O   1 
ATOM   1090 C CB  . LYS A 1 151 ? -35.11818 55.95762 45.47801 1.000 61.25397  ? 145 LYS A CB  1 
ATOM   1091 C CG  . LYS A 1 151 ? -34.40574 57.20187 44.97682 1.000 50.53214  ? 145 LYS A CG  1 
ATOM   1092 C CD  . LYS A 1 151 ? -35.19692 58.45816 45.28868 1.000 56.07294  ? 145 LYS A CD  1 
ATOM   1093 C CE  . LYS A 1 151 ? -34.54809 59.68605 44.66641 1.000 63.52475  ? 145 LYS A CE  1 
ATOM   1094 N NZ  . LYS A 1 151 ? -33.12534 59.83487 45.07898 1.000 77.23953  ? 145 LYS A NZ  1 
ATOM   1095 N N   . THR A 1 152 ? -31.96465 54.78064 44.90381 1.000 74.19060  ? 146 THR A N   1 
ATOM   1096 C CA  . THR A 1 152 ? -30.57396 54.88800 45.32273 1.000 70.67785  ? 146 THR A CA  1 
ATOM   1097 C C   . THR A 1 152 ? -29.89330 55.99308 44.52714 1.000 63.66712  ? 146 THR A C   1 
ATOM   1098 O O   . THR A 1 152 ? -30.43886 56.51611 43.55288 1.000 68.58348  ? 146 THR A O   1 
ATOM   1099 C CB  . THR A 1 152 ? -29.80479 53.56885 45.13278 1.000 65.28663  ? 146 THR A CB  1 
ATOM   1100 O OG1 . THR A 1 152 ? -29.57990 53.33651 43.73627 1.000 78.94399  ? 146 THR A OG1 1 
ATOM   1101 C CG2 . THR A 1 152 ? -30.57377 52.39215 45.72169 1.000 67.15081  ? 146 THR A CG2 1 
ATOM   1102 N N   . LEU A 1 153 ? -28.68365 56.34706 44.95623 1.000 63.91222  ? 147 LEU A N   1 
ATOM   1103 C CA  . LEU A 1 153 ? -27.84988 57.30996 44.24958 1.000 59.47608  ? 147 LEU A CA  1 
ATOM   1104 C C   . LEU A 1 153 ? -26.38837 56.92775 44.42208 1.000 69.38651  ? 147 LEU A C   1 
ATOM   1105 O O   . LEU A 1 153 ? -25.95789 56.56823 45.52175 1.000 73.25691  ? 147 LEU A O   1 
ATOM   1106 C CB  . LEU A 1 153 ? -28.07349 58.74164 44.75391 1.000 62.01399  ? 147 LEU A CB  1 
ATOM   1107 C CG  . LEU A 1 153 ? -27.19379 59.81225 44.10203 1.000 64.11003  ? 147 LEU A CG  1 
ATOM   1108 C CD1 . LEU A 1 153 ? -27.47152 59.89050 42.60899 1.000 60.59208  ? 147 LEU A CD1 1 
ATOM   1109 C CD2 . LEU A 1 153 ? -27.40015 61.16719 44.76272 1.000 61.41573  ? 147 LEU A CD2 1 
ATOM   1110 N N   . GLY A 1 154 ? -25.63172 57.00417 43.33122 1.000 71.80788  ? 148 GLY A N   1 
ATOM   1111 C CA  . GLY A 1 154 ? -24.22302 56.66702 43.37308 1.000 64.02859  ? 148 GLY A CA  1 
ATOM   1112 C C   . GLY A 1 154 ? -23.47411 57.32707 42.23646 1.000 59.56473  ? 148 GLY A C   1 
ATOM   1113 O O   . GLY A 1 154 ? -24.03932 58.07710 41.43745 1.000 65.70981  ? 148 GLY A O   1 
ATOM   1114 N N   . VAL A 1 155 ? -22.17672 57.03772 42.17735 1.000 66.54883  ? 149 VAL A N   1 
ATOM   1115 C CA  . VAL A 1 155 ? -21.29039 57.58425 41.15831 1.000 67.15752  ? 149 VAL A CA  1 
ATOM   1116 C C   . VAL A 1 155 ? -20.55593 56.43372 40.48517 1.000 72.03636  ? 149 VAL A C   1 
ATOM   1117 O O   . VAL A 1 155 ? -20.17578 55.45949 41.14394 1.000 68.68932  ? 149 VAL A O   1 
ATOM   1118 C CB  . VAL A 1 155 ? -20.28601 58.59124 41.75784 1.000 70.21934  ? 149 VAL A CB  1 
ATOM   1119 C CG1 . VAL A 1 155 ? -19.52178 59.30046 40.65434 1.000 69.81758  ? 149 VAL A CG1 1 
ATOM   1120 C CG2 . VAL A 1 155 ? -20.99938 59.59363 42.65573 1.000 64.15932  ? 149 VAL A CG2 1 
ATOM   1121 N N   . TYR A 1 156 ? -20.36163 56.54288 39.17235 1.000 66.50649  ? 150 TYR A N   1 
ATOM   1122 C CA  . TYR A 1 156 ? -19.59225 55.57403 38.40263 1.000 64.24772  ? 150 TYR A CA  1 
ATOM   1123 C C   . TYR A 1 156 ? -18.46945 56.28998 37.66821 1.000 71.64363  ? 150 TYR A C   1 
ATOM   1124 O O   . TYR A 1 156 ? -18.69492 57.33350 37.04684 1.000 83.23133  ? 150 TYR A O   1 
ATOM   1125 C CB  . TYR A 1 156 ? -20.47485 54.82286 37.40312 1.000 67.33411  ? 150 TYR A CB  1 
ATOM   1126 C CG  . TYR A 1 156 ? -19.69235 54.05752 36.35788 1.000 70.36479  ? 150 TYR A CG  1 
ATOM   1127 C CD1 . TYR A 1 156 ? -19.08012 52.84875 36.66488 1.000 80.47768  ? 150 TYR A CD1 1 
ATOM   1128 C CD2 . TYR A 1 156 ? -19.56983 54.54219 35.06271 1.000 71.12258  ? 150 TYR A CD2 1 
ATOM   1129 C CE1 . TYR A 1 156 ? -18.36252 52.14727 35.71211 1.000 68.30292  ? 150 TYR A CE1 1 
ATOM   1130 C CE2 . TYR A 1 156 ? -18.85784 53.84889 34.10463 1.000 70.57539  ? 150 TYR A CE2 1 
ATOM   1131 C CZ  . TYR A 1 156 ? -18.25651 52.65236 34.43382 1.000 73.66322  ? 150 TYR A CZ  1 
ATOM   1132 O OH  . TYR A 1 156 ? -17.54728 51.95894 33.47992 1.000 66.82028  ? 150 TYR A OH  1 
ATOM   1133 N N   . SER A 1 157 ? -17.26747 55.72250 37.73153 1.000 83.62980  ? 151 SER A N   1 
ATOM   1134 C CA  . SER A 1 157 ? -16.11434 56.26752 37.03222 1.000 85.29769  ? 151 SER A CA  1 
ATOM   1135 C C   . SER A 1 157 ? -15.28873 55.13520 36.44414 1.000 77.00019  ? 151 SER A C   1 
ATOM   1136 O O   . SER A 1 157 ? -15.04333 54.12390 37.10782 1.000 86.28118  ? 151 SER A O   1 
ATOM   1137 C CB  . SER A 1 157 ? -15.23646 57.11281 37.96213 1.000 78.85910  ? 151 SER A CB  1 
ATOM   1138 O OG  . SER A 1 157 ? -14.00672 57.43463 37.33617 1.000 78.13013  ? 151 SER A OG  1 
ATOM   1139 N N   . ASP A 1 158 ? -14.86942 55.30941 35.19112 1.000 77.50961  ? 152 ASP A N   1 
ATOM   1140 C CA  . ASP A 1 158 ? -13.92988 54.40396 34.54295 1.000 81.90324  ? 152 ASP A CA  1 
ATOM   1141 C C   . ASP A 1 158 ? -12.52038 54.98399 34.50509 1.000 88.07286  ? 152 ASP A C   1 
ATOM   1142 O O   . ASP A 1 158 ? -11.75067 54.69847 33.58085 1.000 92.20255  ? 152 ASP A O   1 
ATOM   1143 C CB  . ASP A 1 158 ? -14.40602 54.05664 33.13287 1.000 78.09427  ? 152 ASP A CB  1 
ATOM   1144 C CG  . ASP A 1 158 ? -14.67889 55.28362 32.29302 1.000 84.79775  ? 152 ASP A CG  1 
ATOM   1145 O OD1 . ASP A 1 158 ? -15.00777 56.34111 32.87171 1.000 100.27308 ? 152 ASP A OD1 1 
ATOM   1146 O OD2 . ASP A 1 158 ? -14.57038 55.18886 31.05275 1.000 86.43354  ? 152 ASP A OD2 1 
ATOM   1147 N N   . TYR A 1 159 ? -12.17189 55.80156 35.50040 1.000 92.73677  ? 153 TYR A N   1 
ATOM   1148 C CA  . TYR A 1 159 ? -10.84741 56.39972 35.58345 1.000 88.39084  ? 153 TYR A CA  1 
ATOM   1149 C C   . TYR A 1 159 ? -9.97042  55.51293 36.46006 1.000 86.71285  ? 153 TYR A C   1 
ATOM   1150 O O   . TYR A 1 159 ? -10.23435 55.40309 37.66703 1.000 78.66732  ? 153 TYR A O   1 
ATOM   1151 C CB  . TYR A 1 159 ? -10.93150 57.81020 36.15271 1.000 79.60196  ? 153 TYR A CB  1 
ATOM   1152 C CG  . TYR A 1 159 ? -9.65247  58.60414 36.02925 1.000 78.13083  ? 153 TYR A CG  1 
ATOM   1153 C CD1 . TYR A 1 159 ? -9.02703  58.75933 34.79984 1.000 91.31239  ? 153 TYR A CD1 1 
ATOM   1154 C CD2 . TYR A 1 159 ? -9.07693  59.20948 37.13852 1.000 83.79316  ? 153 TYR A CD2 1 
ATOM   1155 C CE1 . TYR A 1 159 ? -7.85717  59.48503 34.67914 1.000 83.66058  ? 153 TYR A CE1 1 
ATOM   1156 C CE2 . TYR A 1 159 ? -7.90835  59.93966 37.02757 1.000 79.81570  ? 153 TYR A CE2 1 
ATOM   1157 C CZ  . TYR A 1 159 ? -7.30367  60.07401 35.79562 1.000 88.44896  ? 153 TYR A CZ  1 
ATOM   1158 O OH  . TYR A 1 159 ? -6.14070  60.79946 35.67868 1.000 100.65595 ? 153 TYR A OH  1 
ATOM   1159 N N   . PRO A 1 160 ? -8.94441  54.86819 35.91071 1.000 84.86293  ? 154 PRO A N   1 
ATOM   1160 C CA  . PRO A 1 160 ? -8.17662  53.86922 36.67605 1.000 67.64093  ? 154 PRO A CA  1 
ATOM   1161 C C   . PRO A 1 160 ? -7.57496  54.43079 37.95438 1.000 82.28442  ? 154 PRO A C   1 
ATOM   1162 O O   . PRO A 1 160 ? -7.63521  53.75695 38.99494 1.000 88.06603  ? 154 PRO A O   1 
ATOM   1163 C CB  . PRO A 1 160 ? -7.08988  53.42702 35.68304 1.000 75.60526  ? 154 PRO A CB  1 
ATOM   1164 C CG  . PRO A 1 160 ? -7.70405  53.65968 34.34286 1.000 70.36459  ? 154 PRO A CG  1 
ATOM   1165 C CD  . PRO A 1 160 ? -8.57339  54.88107 34.48490 1.000 77.74585  ? 154 PRO A CD  1 
ATOM   1166 N N   . PRO A 1 161 ? -6.97451  55.63674 37.94661 1.000 84.57610  ? 155 PRO A N   1 
ATOM   1167 C CA  . PRO A 1 161 ? -6.41798  56.14640 39.21464 1.000 78.80956  ? 155 PRO A CA  1 
ATOM   1168 C C   . PRO A 1 161 ? -7.44381  56.26460 40.32798 1.000 82.85330  ? 155 PRO A C   1 
ATOM   1169 O O   . PRO A 1 161 ? -7.11263  56.02566 41.49589 1.000 90.36052  ? 155 PRO A O   1 
ATOM   1170 C CB  . PRO A 1 161 ? -5.85010  57.51601 38.82063 1.000 74.79765  ? 155 PRO A CB  1 
ATOM   1171 C CG  . PRO A 1 161 ? -5.52203  57.37812 37.40066 1.000 72.45233  ? 155 PRO A CG  1 
ATOM   1172 C CD  . PRO A 1 161 ? -6.63859  56.55123 36.83649 1.000 85.20368  ? 155 PRO A CD  1 
ATOM   1173 N N   . LEU A 1 162 ? -8.68601  56.62290 40.00132 1.000 87.34991  ? 156 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 162 ? -9.71555  56.73043 41.02886 1.000 77.07947  ? 156 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 162 ? -10.21794 55.35610 41.45592 1.000 80.02387  ? 156 LEU A C   1 
ATOM   1176 O O   . LEU A 1 162 ? -10.36409 55.08521 42.65274 1.000 77.07506  ? 156 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 162 ? -10.87678 57.58776 40.52681 1.000 77.71931  ? 156 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 162 ? -11.99011 57.81587 41.54922 1.000 81.47475  ? 156 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 162 ? -11.50634 58.74638 42.64902 1.000 84.10833  ? 156 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 162 ? -13.24108 58.36208 40.88331 1.000 72.29687  ? 156 LEU A CD2 1 
ATOM   1181 N N   . ALA A 1 163 ? -10.49388 54.47786 40.48807 1.000 79.81548  ? 157 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 163 ? -10.96263 53.13616 40.82003 1.000 75.77240  ? 157 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 163 ? -9.93176  52.38227 41.64869 1.000 76.65394  ? 157 ALA A C   1 
ATOM   1184 O O   . ALA A 1 163 ? -10.28549 51.66293 42.59066 1.000 83.44853  ? 157 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 163 ? -11.28986 52.36315 39.54404 1.000 70.67748  ? 157 ALA A CB  1 
ATOM   1186 N N   . THR A 1 164 ? -8.64877  52.53636 41.31194 1.000 83.77874  ? 158 THR A N   1 
ATOM   1187 C CA  . THR A 1 164 ? -7.59572  51.88311 42.08296 1.000 76.15242  ? 158 THR A CA  1 
ATOM   1188 C C   . THR A 1 164 ? -7.61151  52.34207 43.53535 1.000 82.27629  ? 158 THR A C   1 
ATOM   1189 O O   . THR A 1 164 ? -7.45574  51.52849 44.45366 1.000 89.59451  ? 158 THR A O   1 
ATOM   1190 C CB  . THR A 1 164 ? -6.23099  52.15898 41.45040 1.000 80.30482  ? 158 THR A CB  1 
ATOM   1191 O OG1 . THR A 1 164 ? -6.21207  51.65131 40.11027 1.000 84.21574  ? 158 THR A OG1 1 
ATOM   1192 C CG2 . THR A 1 164 ? -5.12496  51.49474 42.25507 1.000 73.80070  ? 158 THR A CG2 1 
ATOM   1193 N N   . ASP A 1 165 ? -7.80659  53.64303 43.76427 1.000 83.07040  ? 159 ASP A N   1 
ATOM   1194 C CA  . ASP A 1 165 ? -7.87702  54.14400 45.13213 1.000 80.76920  ? 159 ASP A CA  1 
ATOM   1195 C C   . ASP A 1 165 ? -9.07051  53.55992 45.87723 1.000 78.58703  ? 159 ASP A C   1 
ATOM   1196 O O   . ASP A 1 165 ? -9.01471  53.38341 47.09978 1.000 80.51434  ? 159 ASP A O   1 
ATOM   1197 C CB  . ASP A 1 165 ? -7.94315  55.67141 45.13048 1.000 71.21140  ? 159 ASP A CB  1 
ATOM   1198 C CG  . ASP A 1 165 ? -7.16259  56.28951 46.27540 1.000 94.24522  ? 159 ASP A CG  1 
ATOM   1199 O OD1 . ASP A 1 165 ? -6.31647  55.58768 46.87174 1.000 82.94528  ? 159 ASP A OD1 1 
ATOM   1200 O OD2 . ASP A 1 165 ? -7.39614  57.47765 46.57963 1.000 101.77915 ? 159 ASP A OD2 1 
ATOM   1201 N N   . LEU A 1 166 ? -10.15405 53.24837 45.16225 1.000 81.93175  ? 160 LEU A N   1 
ATOM   1202 C CA  . LEU A 1 166 ? -11.29817 52.61094 45.80535 1.000 79.31025  ? 160 LEU A CA  1 
ATOM   1203 C C   . LEU A 1 166 ? -11.00253 51.15278 46.13391 1.000 82.57746  ? 160 LEU A C   1 
ATOM   1204 O O   . LEU A 1 166 ? -11.46543 50.63468 47.15702 1.000 75.11310  ? 160 LEU A O   1 
ATOM   1205 C CB  . LEU A 1 166 ? -12.53401 52.72184 44.91419 1.000 76.10336  ? 160 LEU A CB  1 
ATOM   1206 C CG  . LEU A 1 166 ? -13.82878 52.18199 45.52293 1.000 78.04395  ? 160 LEU A CG  1 
ATOM   1207 C CD1 . LEU A 1 166 ? -14.07434 52.81254 46.88624 1.000 61.82920  ? 160 LEU A CD1 1 
ATOM   1208 C CD2 . LEU A 1 166 ? -15.00346 52.43056 44.59185 1.000 68.35366  ? 160 LEU A CD2 1 
ATOM   1209 N N   . ARG A 1 167 ? -10.23174 50.47543 45.27844 1.000 85.07723  ? 161 ARG A N   1 
ATOM   1210 C CA  . ARG A 1 167 ? -9.84983  49.09487 45.55791 1.000 70.55072  ? 161 ARG A CA  1 
ATOM   1211 C C   . ARG A 1 167 ? -9.02763  48.99296 46.83551 1.000 82.41257  ? 161 ARG A C   1 
ATOM   1212 O O   . ARG A 1 167 ? -9.06283  47.96129 47.51657 1.000 83.08966  ? 161 ARG A O   1 
ATOM   1213 C CB  . ARG A 1 167 ? -9.07474  48.51677 44.37055 1.000 71.41780  ? 161 ARG A CB  1 
ATOM   1214 C CG  . ARG A 1 167 ? -8.76969  47.02581 44.46253 1.000 75.13302  ? 161 ARG A CG  1 
ATOM   1215 C CD  . ARG A 1 167 ? -7.38533  46.77085 45.03180 1.000 76.09622  ? 161 ARG A CD  1 
ATOM   1216 N NE  . ARG A 1 167 ? -6.34069  47.36756 44.20886 1.000 80.34625  ? 161 ARG A NE  1 
ATOM   1217 C CZ  . ARG A 1 167 ? -5.08127  47.51077 44.59577 1.000 82.74992  ? 161 ARG A CZ  1 
ATOM   1218 N NH1 . ARG A 1 167 ? -4.68017  47.12251 45.79473 1.000 94.36102  ? 161 ARG A NH1 1 
ATOM   1219 N NH2 . ARG A 1 167 ? -4.20404  48.06148 43.76158 1.000 84.97593  ? 161 ARG A NH2 1 
ATOM   1220 N N   . ARG A 1 168 ? -8.27994  50.04598 47.17486 1.000 87.45795  ? 162 ARG A N   1 
ATOM   1221 C CA  . ARG A 1 168 ? -7.52345  50.03761 48.42159 1.000 81.50310  ? 162 ARG A CA  1 
ATOM   1222 C C   . ARG A 1 168 ? -8.44656  50.00011 49.63268 1.000 69.35753  ? 162 ARG A C   1 
ATOM   1223 O O   . ARG A 1 168 ? -8.09481  49.41464 50.66380 1.000 71.93038  ? 162 ARG A O   1 
ATOM   1224 C CB  . ARG A 1 168 ? -6.59468  51.25232 48.48116 1.000 68.92383  ? 162 ARG A CB  1 
ATOM   1225 C CG  . ARG A 1 168 ? -5.23323  51.01684 47.83544 1.000 95.90101  ? 162 ARG A CG  1 
ATOM   1226 C CD  . ARG A 1 168 ? -4.36470  52.26454 47.88201 1.000 94.53783  ? 162 ARG A CD  1 
ATOM   1227 N NE  . ARG A 1 168 ? -4.62118  53.15823 46.75904 1.000 96.31305  ? 162 ARG A NE  1 
ATOM   1228 C CZ  . ARG A 1 168 ? -3.79773  53.32676 45.73336 1.000 92.97312  ? 162 ARG A CZ  1 
ATOM   1229 N NH1 . ARG A 1 168 ? -2.63740  52.69475 45.66758 1.000 80.32834  ? 162 ARG A NH1 1 
ATOM   1230 N NH2 . ARG A 1 168 ? -4.14464  54.15490 44.75194 1.000 94.92177  ? 162 ARG A NH2 1 
ATOM   1231 N N   . ARG A 1 169 ? -9.62900  50.61210 49.52984 1.000 68.08476  ? 163 ARG A N   1 
ATOM   1232 C CA  . ARG A 1 169 ? -10.61611 50.47886 50.59595 1.000 74.74227  ? 163 ARG A CA  1 
ATOM   1233 C C   . ARG A 1 169 ? -11.09549 49.03861 50.72612 1.000 73.67486  ? 163 ARG A C   1 
ATOM   1234 O O   . ARG A 1 169 ? -11.38526 48.57801 51.83650 1.000 81.94525  ? 163 ARG A O   1 
ATOM   1235 C CB  . ARG A 1 169 ? -11.80228 51.41078 50.34136 1.000 63.29707  ? 163 ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 169 ? -11.42409 52.83129 49.92817 1.000 71.25169  ? 163 ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 169 ? -10.52046 53.48266 50.95080 1.000 79.76183  ? 163 ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 169 ? -10.45931 54.93408 50.81730 1.000 75.47073  ? 163 ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 169 ? -9.52184  55.59261 50.14916 1.000 71.79914  ? 163 ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 169 ? -8.56852  54.95817 49.48734 1.000 98.95789  ? 163 ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 169 ? -9.53571  56.92231 50.15321 1.000 84.66297  ? 163 ARG A NH2 1 
ATOM   1242 N N   . PHE A 1 170 ? -11.17859 48.31658 49.60621 1.000 78.19292  ? 164 PHE A N   1 
ATOM   1243 C CA  . PHE A 1 170 ? -11.57157 46.91181 49.64464 1.000 73.25569  ? 164 PHE A CA  1 
ATOM   1244 C C   . PHE A 1 170 ? -10.51100 46.06030 50.33248 1.000 80.51863  ? 164 PHE A C   1 
ATOM   1245 O O   . PHE A 1 170 ? -10.83919 45.09118 51.02815 1.000 89.98424  ? 164 PHE A O   1 
ATOM   1246 C CB  . PHE A 1 170 ? -11.82950 46.41159 48.22310 1.000 75.18482  ? 164 PHE A CB  1 
ATOM   1247 C CG  . PHE A 1 170 ? -12.32794 44.99564 48.15165 1.000 76.07276  ? 164 PHE A CG  1 
ATOM   1248 C CD1 . PHE A 1 170 ? -13.68451 44.72513 48.19124 1.000 78.88082  ? 164 PHE A CD1 1 
ATOM   1249 C CD2 . PHE A 1 170 ? -11.44223 43.93677 48.02212 1.000 78.65856  ? 164 PHE A CD2 1 
ATOM   1250 C CE1 . PHE A 1 170 ? -14.14907 43.42682 48.11411 1.000 84.29472  ? 164 PHE A CE1 1 
ATOM   1251 C CE2 . PHE A 1 170 ? -11.90153 42.63567 47.94695 1.000 78.80823  ? 164 PHE A CE2 1 
ATOM   1252 C CZ  . PHE A 1 170 ? -13.25724 42.38132 47.99344 1.000 81.19188  ? 164 PHE A CZ  1 
ATOM   1253 N N   . ASP A 1 171 ? -9.23336  46.40055 50.14037 1.000 83.88762  ? 165 ASP A N   1 
ATOM   1254 C CA  . ASP A 1 171 ? -8.16047  45.66771 50.80681 1.000 74.16206  ? 165 ASP A CA  1 
ATOM   1255 C C   . ASP A 1 171 ? -8.28909  45.75630 52.32210 1.000 85.98710  ? 165 ASP A C   1 
ATOM   1256 O O   . ASP A 1 171 ? -8.03210  44.77809 53.03427 1.000 93.51762  ? 165 ASP A O   1 
ATOM   1257 C CB  . ASP A 1 171 ? -6.79962  46.20018 50.35642 1.000 87.32059  ? 165 ASP A CB  1 
ATOM   1258 C CG  . ASP A 1 171 ? -6.50889  45.90169 48.89689 1.000 100.15736 ? 165 ASP A CG  1 
ATOM   1259 O OD1 . ASP A 1 171 ? -6.97190  44.85206 48.39911 1.000 87.02853  ? 165 ASP A OD1 1 
ATOM   1260 O OD2 . ASP A 1 171 ? -5.80970  46.71128 48.24894 1.000 86.88519  ? 165 ASP A OD2 1 
ATOM   1261 N N   . THR A 1 172 ? -8.68750  46.92181 52.83360 1.000 92.73809  ? 166 THR A N   1 
ATOM   1262 C CA  . THR A 1 172 ? -8.84300  47.08416 54.27524 1.000 81.24014  ? 166 THR A CA  1 
ATOM   1263 C C   . THR A 1 172 ? -9.97728  46.21512 54.80736 1.000 90.35058  ? 166 THR A C   1 
ATOM   1264 O O   . THR A 1 172 ? -9.80669  45.48405 55.79043 1.000 95.10428  ? 166 THR A O   1 
ATOM   1265 C CB  . THR A 1 172 ? -9.09405  48.55457 54.60945 1.000 76.40028  ? 166 THR A CB  1 
ATOM   1266 O OG1 . THR A 1 172 ? -8.11715  49.36789 53.95003 1.000 85.19276  ? 166 THR A OG1 1 
ATOM   1267 C CG2 . THR A 1 172 ? -9.00965  48.78329 56.10969 1.000 78.20856  ? 166 THR A CG2 1 
ATOM   1268 N N   . PHE A 1 173 ? -11.14478 46.27910 54.16335 1.000 81.58627  ? 167 PHE A N   1 
ATOM   1269 C CA  . PHE A 1 173 ? -12.31097 45.55870 54.66379 1.000 77.50974  ? 167 PHE A CA  1 
ATOM   1270 C C   . PHE A 1 173 ? -12.12332 44.04913 54.57008 1.000 81.88382  ? 167 PHE A C   1 
ATOM   1271 O O   . PHE A 1 173 ? -12.51792 43.31468 55.48325 1.000 85.00047  ? 167 PHE A O   1 
ATOM   1272 C CB  . PHE A 1 173 ? -13.55873 45.99187 53.89647 1.000 78.72451  ? 167 PHE A CB  1 
ATOM   1273 C CG  . PHE A 1 173 ? -14.00220 47.39436 54.19941 1.000 64.67575  ? 167 PHE A CG  1 
ATOM   1274 C CD1 . PHE A 1 173 ? -13.92393 47.89736 55.48726 1.000 65.13756  ? 167 PHE A CD1 1 
ATOM   1275 C CD2 . PHE A 1 173 ? -14.49633 48.21040 53.19440 1.000 65.03870  ? 167 PHE A CD2 1 
ATOM   1276 C CE1 . PHE A 1 173 ? -14.33475 49.18816 55.76862 1.000 71.43337  ? 167 PHE A CE1 1 
ATOM   1277 C CE2 . PHE A 1 173 ? -14.90710 49.50042 53.46762 1.000 57.60459  ? 167 PHE A CE2 1 
ATOM   1278 C CZ  . PHE A 1 173 ? -14.82632 49.99069 54.75685 1.000 64.05417  ? 167 PHE A CZ  1 
ATOM   1279 N N   . LYS A 1 174 ? -11.52844 43.56544 53.47497 1.000 74.50237  ? 168 LYS A N   1 
ATOM   1280 C CA  . LYS A 1 174 ? -11.34161 42.12641 53.31412 1.000 68.83346  ? 168 LYS A CA  1 
ATOM   1281 C C   . LYS A 1 174 ? -10.50590 41.54168 54.44455 1.000 72.82208  ? 168 LYS A C   1 
ATOM   1282 O O   . LYS A 1 174 ? -10.65647 40.36244 54.78529 1.000 76.15182  ? 168 LYS A O   1 
ATOM   1283 C CB  . LYS A 1 174 ? -10.69058 41.82401 51.96255 1.000 69.24035  ? 168 LYS A CB  1 
ATOM   1284 C CG  . LYS A 1 174 ? -10.56313 40.33580 51.65911 1.000 64.77393  ? 168 LYS A CG  1 
ATOM   1285 C CD  . LYS A 1 174 ? -9.66335  40.06951 50.46343 1.000 86.65273  ? 168 LYS A CD  1 
ATOM   1286 C CE  . LYS A 1 174 ? -9.39745  38.57653 50.30821 1.000 101.47298 ? 168 LYS A CE  1 
ATOM   1287 N NZ  . LYS A 1 174 ? -8.41131  38.27129 49.23452 1.000 95.30557  ? 168 LYS A NZ  1 
ATOM   1288 N N   . ALA A 1 175 ? -9.63863  42.35263 55.05060 1.000 82.87808  ? 169 ALA A N   1 
ATOM   1289 C CA  . ALA A 1 175 ? -8.77136  41.88148 56.12148 1.000 76.97001  ? 169 ALA A CA  1 
ATOM   1290 C C   . ALA A 1 175 ? -9.53197  41.48639 57.38071 1.000 86.59741  ? 169 ALA A C   1 
ATOM   1291 O O   . ALA A 1 175 ? -8.94570  40.84198 58.25618 1.000 105.95767 ? 169 ALA A O   1 
ATOM   1292 C CB  . ALA A 1 175 ? -7.73713  42.95507 56.45921 1.000 77.23032  ? 169 ALA A CB  1 
ATOM   1293 N N   . PHE A 1 176 ? -10.81063 41.84554 57.49804 1.000 97.08629  ? 170 PHE A N   1 
ATOM   1294 C CA  . PHE A 1 176 ? -11.60199 41.52948 58.68039 1.000 95.35072  ? 170 PHE A CA  1 
ATOM   1295 C C   . PHE A 1 176 ? -12.50054 40.31721 58.47205 1.000 94.69925  ? 170 PHE A C   1 
ATOM   1296 O O   . PHE A 1 176 ? -13.57187 40.22347 59.08196 1.000 100.09027 ? 170 PHE A O   1 
ATOM   1297 C CB  . PHE A 1 176 ? -12.42232 42.74476 59.10403 1.000 82.97784  ? 170 PHE A CB  1 
ATOM   1298 C CG  . PHE A 1 176 ? -11.58447 43.88581 59.58917 1.000 99.59867  ? 170 PHE A CG  1 
ATOM   1299 C CD1 . PHE A 1 176 ? -11.21615 43.96989 60.92106 1.000 90.05377  ? 170 PHE A CD1 1 
ATOM   1300 C CD2 . PHE A 1 176 ? -11.14464 44.86290 58.71193 1.000 88.30746  ? 170 PHE A CD2 1 
ATOM   1301 C CE1 . PHE A 1 176 ? -10.43632 45.01242 61.37195 1.000 86.79190  ? 170 PHE A CE1 1 
ATOM   1302 C CE2 . PHE A 1 176 ? -10.36305 45.90996 59.15829 1.000 91.48137  ? 170 PHE A CE2 1 
ATOM   1303 C CZ  . PHE A 1 176 ? -10.00770 45.98194 60.48879 1.000 90.83815  ? 170 PHE A CZ  1 
ATOM   1304 N N   . ASN A 1 177 ? -12.07908 39.38540 57.62152 1.000 91.87938  ? 171 ASN A N   1 
ATOM   1305 C CA  . ASN A 1 177 ? -12.81065 38.14028 57.45492 1.000 95.94186  ? 171 ASN A CA  1 
ATOM   1306 C C   . ASN A 1 177 ? -12.85746 37.37816 58.77407 1.000 104.90028 ? 171 ASN A C   1 
ATOM   1307 O O   . ASN A 1 177 ? -11.97475 37.50736 59.62652 1.000 119.96853 ? 171 ASN A O   1 
ATOM   1308 C CB  . ASN A 1 177 ? -12.15829 37.28379 56.36767 1.000 101.04802 ? 171 ASN A CB  1 
ATOM   1309 C CG  . ASN A 1 177 ? -12.89712 35.97906 56.12598 1.000 117.74123 ? 171 ASN A CG  1 
ATOM   1310 O OD1 . ASN A 1 177 ? -14.07002 35.84009 56.47588 1.000 119.10939 ? 171 ASN A OD1 1 
ATOM   1311 N ND2 . ASN A 1 177 ? -12.21228 35.01569 55.52080 1.000 105.28735 ? 171 ASN A ND2 1 
ATOM   1312 N N   . SER A 1 178 ? -13.91361 36.58547 58.94225 1.000 111.10152 ? 172 SER A N   1 
ATOM   1313 C CA  . SER A 1 178 ? -14.09619 35.78044 60.14850 1.000 115.35113 ? 172 SER A CA  1 
ATOM   1314 C C   . SER A 1 178 ? -13.46534 34.40399 59.93215 1.000 120.06805 ? 172 SER A C   1 
ATOM   1315 O O   . SER A 1 178 ? -14.13921 33.38804 59.75300 1.000 129.31380 ? 172 SER A O   1 
ATOM   1316 C CB  . SER A 1 178 ? -15.57630 35.67571 60.49399 1.000 115.09974 ? 172 SER A CB  1 
ATOM   1317 O OG  . SER A 1 178 ? -16.25137 36.89777 60.23933 1.000 95.96484  ? 172 SER A OG  1 
ATOM   1318 N N   . ALA A 1 179 ? -12.13214 34.38746 59.95069 1.000 127.41261 ? 173 ALA A N   1 
ATOM   1319 C CA  . ALA A 1 179 ? -11.39704 33.15019 59.69475 1.000 131.52676 ? 173 ALA A CA  1 
ATOM   1320 C C   . ALA A 1 179 ? -9.98987  33.27227 60.26519 1.000 150.70235 ? 173 ALA A C   1 
ATOM   1321 O O   . ALA A 1 179 ? -9.15525  33.98364 59.69675 1.000 135.61556 ? 173 ALA A O   1 
ATOM   1322 C CB  . ALA A 1 179 ? -11.35552 32.84730 58.20070 1.000 122.50703 ? 173 ALA A CB  1 
ATOM   1323 N N   . LYS A 1 180 ? -9.74140  32.58517 61.37349 1.000 168.03979 ? 174 LYS A N   1 
ATOM   1324 C CA  . LYS A 1 180 ? -8.40799  32.35966 61.94385 1.000 162.03679 ? 174 LYS A CA  1 
ATOM   1325 C C   . LYS A 1 180 ? -7.68715  33.69689 62.14052 1.000 172.02662 ? 174 LYS A C   1 
ATOM   1326 O O   . LYS A 1 180 ? -8.32167  34.71587 62.43099 1.000 179.07065 ? 174 LYS A O   1 
ATOM   1327 C CB  . LYS A 1 180 ? -7.67430  31.35646 61.07288 1.000 159.18568 ? 174 LYS A CB  1 
ATOM   1328 C CG  . LYS A 1 180 ? -8.19317  29.93364 61.22373 1.000 154.63532 ? 174 LYS A CG  1 
ATOM   1329 C CD  . LYS A 1 180 ? -7.94495  29.11336 59.97123 1.000 139.17156 ? 174 LYS A CD  1 
ATOM   1330 C CE  . LYS A 1 180 ? -8.73312  29.66901 58.79637 1.000 140.67029 ? 174 LYS A CE  1 
ATOM   1331 N NZ  . LYS A 1 180 ? -10.18669 29.77782 59.10554 1.000 123.22837 ? 174 LYS A NZ  1 
ATOM   1332 N N   . ASN A 1 181 ? -6.36047  33.70814 61.99229 1.000 176.15258 ? 175 ASN A N   1 
ATOM   1333 C CA  . ASN A 1 181 ? -5.58714  34.92688 62.20750 1.000 178.38709 ? 175 ASN A CA  1 
ATOM   1334 C C   . ASN A 1 181 ? -5.90899  35.95100 61.12624 1.000 184.76611 ? 175 ASN A C   1 
ATOM   1335 O O   . ASN A 1 181 ? -5.66954  35.71139 59.93810 1.000 190.69697 ? 175 ASN A O   1 
ATOM   1336 C CB  . ASN A 1 181 ? -4.08708  34.62585 62.23654 1.000 179.03093 ? 175 ASN A CB  1 
ATOM   1337 C CG  . ASN A 1 181 ? -3.63272  33.73320 61.09211 1.000 174.72533 ? 175 ASN A CG  1 
ATOM   1338 O OD1 . ASN A 1 181 ? -3.07334  32.65943 61.31762 1.000 173.98341 ? 175 ASN A OD1 1 
ATOM   1339 N ND2 . ASN A 1 181 ? -3.86158  34.17579 59.86062 1.000 180.80190 ? 175 ASN A ND2 1 
ATOM   1340 N N   . SER A 1 182 ? -6.45358  37.09061 61.53934 1.000 190.18204 ? 176 SER A N   1 
ATOM   1341 C CA  . SER A 1 182 ? -6.80842  38.15700 60.61739 1.000 184.42131 ? 176 SER A CA  1 
ATOM   1342 C C   . SER A 1 182 ? -6.68896  39.48427 61.35286 1.000 171.79511 ? 176 SER A C   1 
ATOM   1343 O O   . SER A 1 182 ? -6.29475  39.53803 62.52166 1.000 177.42247 ? 176 SER A O   1 
ATOM   1344 C CB  . SER A 1 182 ? -8.21972  37.95369 60.05265 1.000 176.27718 ? 176 SER A CB  1 
ATOM   1345 O OG  . SER A 1 182 ? -8.33299  36.71330 59.37544 1.000 160.64983 ? 176 SER A OG  1 
ATOM   1346 N N   . ALA A 1 183 ? -7.02958  40.56603 60.65178 1.000 152.72949 ? 177 ALA A N   1 
ATOM   1347 C CA  . ALA A 1 183 ? -7.10480  41.87208 61.29059 1.000 142.90215 ? 177 ALA A CA  1 
ATOM   1348 C C   . ALA A 1 183 ? -8.30321  41.99396 62.22152 1.000 150.94783 ? 177 ALA A C   1 
ATOM   1349 O O   . ALA A 1 183 ? -8.37107  42.95568 62.99434 1.000 151.48806 ? 177 ALA A O   1 
ATOM   1350 C CB  . ALA A 1 183 ? -7.15236  42.97475 60.23142 1.000 121.67582 ? 177 ALA A CB  1 
ATOM   1351 N N   . ALA A 1 184 ? -9.24169  41.04709 62.16830 1.000 150.11475 ? 178 ALA A N   1 
ATOM   1352 C CA  . ALA A 1 184 ? -10.40187 41.04942 63.04730 1.000 144.75921 ? 178 ALA A CA  1 
ATOM   1353 C C   . ALA A 1 184 ? -10.23972 40.14775 64.26313 1.000 170.11970 ? 178 ALA A C   1 
ATOM   1354 O O   . ALA A 1 184 ? -10.97215 40.32217 65.24283 1.000 172.07527 ? 178 ALA A O   1 
ATOM   1355 C CB  . ALA A 1 184 ? -11.65584 40.62377 62.27269 1.000 127.74211 ? 178 ALA A CB  1 
ATOM   1356 N N   . ASN A 1 185 ? -9.30112  39.19776 64.22935 1.000 194.03707 ? 179 ASN A N   1 
ATOM   1357 C CA  . ASN A 1 185 ? -9.11490  38.25335 65.32191 1.000 193.84421 ? 179 ASN A CA  1 
ATOM   1358 C C   . ASN A 1 185 ? -7.80135  38.42366 66.07119 1.000 188.18361 ? 179 ASN A C   1 
ATOM   1359 O O   . ASN A 1 185 ? -7.69711  37.95456 67.20882 1.000 191.48160 ? 179 ASN A O   1 
ATOM   1360 C CB  . ASN A 1 185 ? -9.20313  36.81183 64.79828 1.000 203.87109 ? 179 ASN A CB  1 
ATOM   1361 C CG  . ASN A 1 185 ? -10.51925 36.52643 64.10139 1.000 197.60574 ? 179 ASN A CG  1 
ATOM   1362 O OD1 . ASN A 1 185 ? -11.55606 37.08382 64.45908 1.000 190.63811 ? 179 ASN A OD1 1 
ATOM   1363 N ND2 . ASN A 1 185 ? -10.48325 35.65705 63.09827 1.000 194.70287 ? 179 ASN A ND2 1 
ATOM   1364 N N   . LEU A 1 186 ? -6.80538  39.07292 65.47260 1.000 182.88903 ? 180 LEU A N   1 
ATOM   1365 C CA  . LEU A 1 186 ? -5.52435  39.30612 66.12110 1.000 190.49574 ? 180 LEU A CA  1 
ATOM   1366 C C   . LEU A 1 186 ? -5.13704  40.77228 65.98535 1.000 192.67554 ? 180 LEU A C   1 
ATOM   1367 O O   . LEU A 1 186 ? -5.59162  41.47795 65.08120 1.000 169.06998 ? 180 LEU A O   1 
ATOM   1368 C CB  . LEU A 1 186 ? -4.41739  38.41738 65.53368 1.000 177.33490 ? 180 LEU A CB  1 
ATOM   1369 C CG  . LEU A 1 186 ? -4.49338  36.91608 65.81844 1.000 171.74256 ? 180 LEU A CG  1 
ATOM   1370 C CD1 . LEU A 1 186 ? -3.23090  36.22870 65.33005 1.000 180.74030 ? 180 LEU A CD1 1 
ATOM   1371 C CD2 . LEU A 1 186 ? -4.70776  36.65202 67.30018 1.000 168.08280 ? 180 LEU A CD2 1 
ATOM   1372 N N   . ALA A 1 187 ? -4.28368  41.22363 66.90559 1.000 213.47694 ? 181 ALA A N   1 
ATOM   1373 C CA  . ALA A 1 187 ? -3.78633  42.59245 66.88790 1.000 199.52293 ? 181 ALA A CA  1 
ATOM   1374 C C   . ALA A 1 187 ? -2.47041  42.73878 66.13591 1.000 208.82738 ? 181 ALA A C   1 
ATOM   1375 O O   . ALA A 1 187 ? -2.16793  43.83719 65.65536 1.000 206.73212 ? 181 ALA A O   1 
ATOM   1376 C CB  . ALA A 1 187 ? -3.61470  43.11264 68.31910 1.000 185.30720 ? 181 ALA A CB  1 
ATOM   1377 N N   . SER A 1 188 ? -1.68353  41.66438 66.02235 1.000 219.80360 ? 182 SER A N   1 
ATOM   1378 C CA  . SER A 1 188 ? -0.43638  41.73791 65.26739 1.000 213.95824 ? 182 SER A CA  1 
ATOM   1379 C C   . SER A 1 188 ? -0.69142  41.78862 63.76670 1.000 209.09539 ? 182 SER A C   1 
ATOM   1380 O O   . SER A 1 188 ? 0.08526   42.40437 63.02733 1.000 193.95286 ? 182 SER A O   1 
ATOM   1381 C CB  . SER A 1 188 ? 0.46149   40.54867 65.61126 1.000 207.75973 ? 182 SER A CB  1 
ATOM   1382 O OG  . SER A 1 188 ? -0.13086  39.32524 65.20986 1.000 200.32282 ? 182 SER A OG  1 
ATOM   1383 N N   . ALA A 1 189 ? -1.76282  41.14896 63.30052 1.000 199.41014 ? 183 ALA A N   1 
ATOM   1384 C CA  . ALA A 1 189 ? -2.13852  41.18391 61.89484 1.000 178.23660 ? 183 ALA A CA  1 
ATOM   1385 C C   . ALA A 1 189 ? -3.03074  42.36895 61.54822 1.000 176.92918 ? 183 ALA A C   1 
ATOM   1386 O O   . ALA A 1 189 ? -3.26176  42.62367 60.36106 1.000 178.96251 ? 183 ALA A O   1 
ATOM   1387 C CB  . ALA A 1 189 ? -2.84164  39.87896 61.50364 1.000 162.71747 ? 183 ALA A CB  1 
ATOM   1388 N N   . ALA A 1 190 ? -3.53414  43.09491 62.54780 1.000 176.18252 ? 184 ALA A N   1 
ATOM   1389 C CA  . ALA A 1 190 ? -4.35180  44.27892 62.31139 1.000 168.71734 ? 184 ALA A CA  1 
ATOM   1390 C C   . ALA A 1 190 ? -3.52253  45.55677 62.28887 1.000 175.82307 ? 184 ALA A C   1 
ATOM   1391 O O   . ALA A 1 190 ? -3.77582  46.44405 61.46638 1.000 160.27970 ? 184 ALA A O   1 
ATOM   1392 C CB  . ALA A 1 190 ? -5.44447  44.38860 63.37736 1.000 165.37955 ? 184 ALA A CB  1 
ATOM   1393 N N   . ALA A 1 191 ? -2.53627  45.67002 63.18293 1.000 186.03665 ? 185 ALA A N   1 
ATOM   1394 C CA  . ALA A 1 191 ? -1.64461  46.82349 63.17146 1.000 167.65118 ? 185 ALA A CA  1 
ATOM   1395 C C   . ALA A 1 191 ? -0.65090  46.77101 62.01904 1.000 167.04043 ? 185 ALA A C   1 
ATOM   1396 O O   . ALA A 1 191 ? -0.04323  47.79650 61.69339 1.000 155.10308 ? 185 ALA A O   1 
ATOM   1397 C CB  . ALA A 1 191 ? -0.89552  46.92675 64.50099 1.000 136.52719 ? 185 ALA A CB  1 
ATOM   1398 N N   . ALA A 1 192 ? -0.46890  45.60318 61.40178 1.000 170.41487 ? 186 ALA A N   1 
ATOM   1399 C CA  . ALA A 1 192 ? 0.39698   45.44720 60.24271 1.000 139.41634 ? 186 ALA A CA  1 
ATOM   1400 C C   . ALA A 1 192 ? -0.34222  45.66322 58.92897 1.000 134.43169 ? 186 ALA A C   1 
ATOM   1401 O O   . ALA A 1 192 ? 0.12834   45.20538 57.88192 1.000 134.17622 ? 186 ALA A O   1 
ATOM   1402 C CB  . ALA A 1 192 ? 1.05042   44.06338 60.25325 1.000 126.16730 ? 186 ALA A CB  1 
ATOM   1403 N N   . LEU A 1 193 ? -1.48697  46.34647 58.96267 1.000 131.69171 ? 187 LEU A N   1 
ATOM   1404 C CA  . LEU A 1 193 ? -2.29945  46.54838 57.77183 1.000 127.32079 ? 187 LEU A CA  1 
ATOM   1405 C C   . LEU A 1 193 ? -1.94822  47.89173 57.14667 1.000 143.15018 ? 187 LEU A C   1 
ATOM   1406 O O   . LEU A 1 193 ? -2.25128  48.93688 57.74347 1.000 138.05706 ? 187 LEU A O   1 
ATOM   1407 C CB  . LEU A 1 193 ? -3.78160  46.49772 58.12576 1.000 104.31902 ? 187 LEU A CB  1 
ATOM   1408 C CG  . LEU A 1 193 ? -4.83480  46.16827 57.05977 1.000 120.32390 ? 187 LEU A CG  1 
ATOM   1409 C CD1 . LEU A 1 193 ? -6.20522  46.04535 57.71590 1.000 116.41844 ? 187 LEU A CD1 1 
ATOM   1410 C CD2 . LEU A 1 193 ? -4.88242  47.18706 55.91692 1.000 100.49439 ? 187 LEU A CD2 1 
ATOM   1411 N N   . PRO A 1 194 ? -1.32097  47.92512 55.96637 1.000 136.95107 ? 188 PRO A N   1 
ATOM   1412 C CA  . PRO A 1 194 ? -1.19082  49.19775 55.24487 1.000 114.31484 ? 188 PRO A CA  1 
ATOM   1413 C C   . PRO A 1 194 ? -2.54645  49.71861 54.79282 1.000 121.03375 ? 188 PRO A C   1 
ATOM   1414 O O   . PRO A 1 194 ? -3.11595  49.21580 53.81759 1.000 138.26413 ? 188 PRO A O   1 
ATOM   1415 C CB  . PRO A 1 194 ? -0.29048  48.84047 54.05262 1.000 104.54145 ? 188 PRO A CB  1 
ATOM   1416 C CG  . PRO A 1 194 ? 0.38550   47.56239 54.44203 1.000 92.51589  ? 188 PRO A CG  1 
ATOM   1417 C CD  . PRO A 1 194 ? -0.60947  46.83118 55.28499 1.000 98.47543  ? 188 PRO A CD  1 
ATOM   1418 N N   . VAL A 1 195 ? -3.07503  50.71455 55.50518 1.000 114.31615 ? 189 VAL A N   1 
ATOM   1419 C CA  . VAL A 1 195 ? -4.37377  51.29452 55.18297 1.000 101.09504 ? 189 VAL A CA  1 
ATOM   1420 C C   . VAL A 1 195 ? -4.14267  52.47749 54.25085 1.000 105.12796 ? 189 VAL A C   1 
ATOM   1421 O O   . VAL A 1 195 ? -4.24683  53.64179 54.65853 1.000 110.88897 ? 189 VAL A O   1 
ATOM   1422 C CB  . VAL A 1 195 ? -5.13165  51.70685 56.45972 1.000 86.65453  ? 189 VAL A CB  1 
ATOM   1423 C CG1 . VAL A 1 195 ? -6.57150  52.04708 56.13818 1.000 107.06239 ? 189 VAL A CG1 1 
ATOM   1424 C CG2 . VAL A 1 195 ? -5.06524  50.60241 57.50371 1.000 100.99978 ? 189 VAL A CG2 1 
ATOM   1425 N N   . SER A 1 196 ? -3.83230  52.18092 52.99147 1.000 97.11929  ? 190 SER A N   1 
ATOM   1426 C CA  . SER A 1 196 ? -3.31920  53.18764 52.08008 1.000 90.11156  ? 190 SER A CA  1 
ATOM   1427 C C   . SER A 1 196 ? -4.44661  53.98143 51.42902 1.000 93.91780  ? 190 SER A C   1 
ATOM   1428 O O   . SER A 1 196 ? -5.60003  53.54687 51.36070 1.000 98.91641  ? 190 SER A O   1 
ATOM   1429 C CB  . SER A 1 196 ? -2.46063  52.54039 50.99238 1.000 81.37353  ? 190 SER A CB  1 
ATOM   1430 O OG  . SER A 1 196 ? -1.42026  51.75854 51.54943 1.000 104.67495 ? 190 SER A OG  1 
ATOM   1431 N N   . THR A 1 197 ? -4.08372  55.16830 50.94668 1.000 86.58165  ? 191 THR A N   1 
ATOM   1432 C CA  . THR A 1 197 ? -4.93410  55.98544 50.09479 1.000 81.71011  ? 191 THR A CA  1 
ATOM   1433 C C   . THR A 1 197 ? -4.03585  56.87595 49.24864 1.000 93.41800  ? 191 THR A C   1 
ATOM   1434 O O   . THR A 1 197 ? -3.00922  57.36712 49.72626 1.000 94.39113  ? 191 THR A O   1 
ATOM   1435 C CB  . THR A 1 197 ? -5.91872  56.84000 50.90322 1.000 89.00491  ? 191 THR A CB  1 
ATOM   1436 O OG1 . THR A 1 197 ? -6.59946  57.74404 50.02377 1.000 73.46323  ? 191 THR A OG1 1 
ATOM   1437 C CG2 . THR A 1 197 ? -5.19046  57.63882 51.97497 1.000 83.91378  ? 191 THR A CG2 1 
ATOM   1438 N N   . ALA A 1 198 ? -4.41641  57.06809 47.98898 1.000 95.73116  ? 192 ALA A N   1 
ATOM   1439 C CA  . ALA A 1 198 ? -3.63393  57.91824 47.10379 1.000 86.27108  ? 192 ALA A CA  1 
ATOM   1440 C C   . ALA A 1 198 ? -4.10963  59.36131 47.11033 1.000 96.27688  ? 192 ALA A C   1 
ATOM   1441 O O   . ALA A 1 198 ? -3.30060  60.27280 46.90566 1.000 92.49459  ? 192 ALA A O   1 
ATOM   1442 C CB  . ALA A 1 198 ? -3.67174  57.37360 45.67368 1.000 93.12900  ? 192 ALA A CB  1 
ATOM   1443 N N   . TYR A 1 199 ? -5.39613  59.59437 47.35374 1.000 82.79280  ? 193 TYR A N   1 
ATOM   1444 C CA  . TYR A 1 199 ? -5.96888  60.92873 47.26749 1.000 83.12608  ? 193 TYR A CA  1 
ATOM   1445 C C   . TYR A 1 199 ? -6.80400  61.21148 48.50462 1.000 90.38011  ? 193 TYR A C   1 
ATOM   1446 O O   . TYR A 1 199 ? -7.65185  60.39848 48.88696 1.000 103.46575 ? 193 TYR A O   1 
ATOM   1447 C CB  . TYR A 1 199 ? -6.81952  61.07342 46.00315 1.000 67.99452  ? 193 TYR A CB  1 
ATOM   1448 C CG  . TYR A 1 199 ? -6.07806  60.69289 44.74316 1.000 90.16250  ? 193 TYR A CG  1 
ATOM   1449 C CD1 . TYR A 1 199 ? -5.09599  61.52198 44.21962 1.000 90.69916  ? 193 TYR A CD1 1 
ATOM   1450 C CD2 . TYR A 1 199 ? -6.35299  59.50237 44.08106 1.000 80.83384  ? 193 TYR A CD2 1 
ATOM   1451 C CE1 . TYR A 1 199 ? -4.41101  61.18173 43.07150 1.000 91.07137  ? 193 TYR A CE1 1 
ATOM   1452 C CE2 . TYR A 1 199 ? -5.67298  59.15378 42.92646 1.000 79.52541  ? 193 TYR A CE2 1 
ATOM   1453 C CZ  . TYR A 1 199 ? -4.70198  59.99903 42.42803 1.000 83.11104  ? 193 TYR A CZ  1 
ATOM   1454 O OH  . TYR A 1 199 ? -4.01337  59.66829 41.28310 1.000 87.07265  ? 193 TYR A OH  1 
ATOM   1455 N N   . HIS A 1 200 ? -6.55222  62.35503 49.12875 1.000 86.79089  ? 194 HIS A N   1 
ATOM   1456 C CA  . HIS A 1 200 ? -7.36179  62.86296 50.22460 1.000 90.39035  ? 194 HIS A CA  1 
ATOM   1457 C C   . HIS A 1 200 ? -7.94734  64.21380 49.81692 1.000 90.42011  ? 194 HIS A C   1 
ATOM   1458 O O   . HIS A 1 200 ? -7.86298  64.62748 48.65659 1.000 84.14338  ? 194 HIS A O   1 
ATOM   1459 C CB  . HIS A 1 200 ? -6.54206  62.97966 51.51312 1.000 92.23570  ? 194 HIS A CB  1 
ATOM   1460 C CG  . HIS A 1 200 ? -5.18204  62.36081 51.43461 1.000 89.04345  ? 194 HIS A CG  1 
ATOM   1461 N ND1 . HIS A 1 200 ? -4.05384  63.08451 51.11488 1.000 116.14486 ? 194 HIS A ND1 1 
ATOM   1462 C CD2 . HIS A 1 200 ? -4.76512  61.09148 51.65379 1.000 101.14270 ? 194 HIS A CD2 1 
ATOM   1463 C CE1 . HIS A 1 200 ? -3.00148  62.28616 51.13239 1.000 135.68579 ? 194 HIS A CE1 1 
ATOM   1464 N NE2 . HIS A 1 200 ? -3.40591  61.07113 51.45590 1.000 115.07378 ? 194 HIS A NE2 1 
ATOM   1465 N N   . ILE A 1 201 ? -8.54182  64.90767 50.79070 1.000 95.56249  ? 195 ILE A N   1 
ATOM   1466 C CA  . ILE A 1 201 ? -9.03517  66.25735 50.53783 1.000 83.76913  ? 195 ILE A CA  1 
ATOM   1467 C C   . ILE A 1 201 ? -7.87541  67.19944 50.24784 1.000 81.92989  ? 195 ILE A C   1 
ATOM   1468 O O   . ILE A 1 201 ? -8.03795  68.19820 49.53589 1.000 86.72737  ? 195 ILE A O   1 
ATOM   1469 C CB  . ILE A 1 201 ? -9.88892  66.74672 51.72672 1.000 74.34194  ? 195 ILE A CB  1 
ATOM   1470 C CG1 . ILE A 1 201 ? -10.58726 68.06673 51.38926 1.000 76.50620  ? 195 ILE A CG1 1 
ATOM   1471 C CG2 . ILE A 1 201 ? -9.03704  66.89977 52.97732 1.000 80.97177  ? 195 ILE A CG2 1 
ATOM   1472 C CD1 . ILE A 1 201 ? -11.53084 68.55517 52.47190 1.000 75.13380  ? 195 ILE A CD1 1 
ATOM   1473 N N   . LYS A 1 202 ? -6.68569  66.89250 50.77479 1.000 94.08545  ? 196 LYS A N   1 
ATOM   1474 C CA  . LYS A 1 202 ? -5.51925  67.73067 50.51746 1.000 102.84231 ? 196 LYS A CA  1 
ATOM   1475 C C   . LYS A 1 202 ? -5.03908  67.60697 49.07722 1.000 103.20997 ? 196 LYS A C   1 
ATOM   1476 O O   . LYS A 1 202 ? -4.48847  68.56762 48.52732 1.000 113.74979 ? 196 LYS A O   1 
ATOM   1477 C CB  . LYS A 1 202 ? -4.38517  67.37177 51.47817 1.000 104.85530 ? 196 LYS A CB  1 
ATOM   1478 C CG  . LYS A 1 202 ? -4.62582  67.77082 52.92384 1.000 111.87705 ? 196 LYS A CG  1 
ATOM   1479 C CD  . LYS A 1 202 ? -3.50121  67.26508 53.81554 1.000 138.13726 ? 196 LYS A CD  1 
ATOM   1480 C CE  . LYS A 1 202 ? -3.78786  67.52538 55.28388 1.000 145.47377 ? 196 LYS A CE  1 
ATOM   1481 N NZ  . LYS A 1 202 ? -2.67043  67.05062 56.14630 1.000 143.61979 ? 196 LYS A NZ  1 
ATOM   1482 N N   . ASN A 1 203 ? -5.22479  66.44333 48.45529 1.000 100.68279 ? 197 ASN A N   1 
ATOM   1483 C CA  . ASN A 1 203 ? -4.81768  66.21813 47.06700 1.000 88.15054  ? 197 ASN A CA  1 
ATOM   1484 C C   . ASN A 1 203 ? -5.88362  65.40342 46.34867 1.000 92.05398  ? 197 ASN A C   1 
ATOM   1485 O O   . ASN A 1 203 ? -5.75206  64.18627 46.17059 1.000 98.71364  ? 197 ASN A O   1 
ATOM   1486 C CB  . ASN A 1 203 ? -3.44935  65.53136 46.99581 1.000 95.63839  ? 197 ASN A CB  1 
ATOM   1487 C CG  . ASN A 1 203 ? -3.40038  64.22955 47.77617 1.000 103.13990 ? 197 ASN A CG  1 
ATOM   1488 O OD1 . ASN A 1 203 ? -4.09460  64.06418 48.77959 1.000 111.26267 ? 197 ASN A OD1 1 
ATOM   1489 N ND2 . ASN A 1 203 ? -2.58327  63.29290 47.30857 1.000 109.07569 ? 197 ASN A ND2 1 
ATOM   1490 N N   . PRO A 1 204 ? -6.96498  66.04685 45.91810 1.000 89.84175  ? 198 PRO A N   1 
ATOM   1491 C CA  . PRO A 1 204 ? -7.96909  65.33938 45.11879 1.000 88.08250  ? 198 PRO A CA  1 
ATOM   1492 C C   . PRO A 1 204 ? -7.42864  65.00174 43.73818 1.000 78.11641  ? 198 PRO A C   1 
ATOM   1493 O O   . PRO A 1 204 ? -6.46665  65.59797 43.24920 1.000 88.01004  ? 198 PRO A O   1 
ATOM   1494 C CB  . PRO A 1 204 ? -9.13000  66.33805 45.02845 1.000 88.87846  ? 198 PRO A CB  1 
ATOM   1495 C CG  . PRO A 1 204 ? -8.86215  67.35836 46.10191 1.000 83.20731  ? 198 PRO A CG  1 
ATOM   1496 C CD  . PRO A 1 204 ? -7.37471  67.42734 46.22074 1.000 83.40143  ? 198 PRO A CD  1 
ATOM   1497 N N   . ILE A 1 205 ? -8.06355  64.01919 43.10868 1.000 83.66385  ? 199 ILE A N   1 
ATOM   1498 C CA  . ILE A 1 205 ? -7.74085  63.62374 41.74282 1.000 84.67711  ? 199 ILE A CA  1 
ATOM   1499 C C   . ILE A 1 205 ? -8.85857  64.14507 40.84743 1.000 90.45406  ? 199 ILE A C   1 
ATOM   1500 O O   . ILE A 1 205 ? -9.99749  63.66448 40.90508 1.000 82.40908  ? 199 ILE A O   1 
ATOM   1501 C CB  . ILE A 1 205 ? -7.55342  62.10384 41.60750 1.000 76.88609  ? 199 ILE A CB  1 
ATOM   1502 C CG1 . ILE A 1 205 ? -7.37973  61.71018 40.14035 1.000 82.49340  ? 199 ILE A CG1 1 
ATOM   1503 C CG2 . ILE A 1 205 ? -8.69168  61.33430 42.26739 1.000 72.45744  ? 199 ILE A CG2 1 
ATOM   1504 C CD1 . ILE A 1 205 ? -6.08979  62.20674 39.53196 1.000 78.91425  ? 199 ILE A CD1 1 
ATOM   1505 N N   . GLY A 1 206 ? -8.54387  65.15228 40.03767 1.000 95.56477  ? 200 GLY A N   1 
ATOM   1506 C CA  . GLY A 1 206 ? -9.53653  65.76832 39.17993 1.000 78.03334  ? 200 GLY A CA  1 
ATOM   1507 C C   . GLY A 1 206 ? -10.70880 66.34754 39.94675 1.000 93.11696  ? 200 GLY A C   1 
ATOM   1508 O O   . GLY A 1 206 ? -11.81542 66.46184 39.40957 1.000 95.84714  ? 200 GLY A O   1 
ATOM   1509 N N   . GLY A 1 207 ? -10.47874 66.71254 41.20624 1.000 90.28455  ? 201 GLY A N   1 
ATOM   1510 C CA  . GLY A 1 207 ? -11.52296 67.24851 42.05266 1.000 69.20422  ? 201 GLY A CA  1 
ATOM   1511 C C   . GLY A 1 207 ? -12.31834 66.22446 42.82801 1.000 79.74659  ? 201 GLY A C   1 
ATOM   1512 O O   . GLY A 1 207 ? -13.33992 66.58408 43.42378 1.000 84.15036  ? 201 GLY A O   1 
ATOM   1513 N N   . VAL A 1 208 ? -11.88482 64.96660 42.84752 1.000 87.87532  ? 202 VAL A N   1 
ATOM   1514 C CA  . VAL A 1 208 ? -12.60117 63.88361 43.50916 1.000 76.50122  ? 202 VAL A CA  1 
ATOM   1515 C C   . VAL A 1 208 ? -11.67768 63.24591 44.53795 1.000 82.95860  ? 202 VAL A C   1 
ATOM   1516 O O   . VAL A 1 208 ? -10.46959 63.12482 44.30655 1.000 89.71439  ? 202 VAL A O   1 
ATOM   1517 C CB  . VAL A 1 208 ? -13.09506 62.83526 42.48872 1.000 80.43731  ? 202 VAL A CB  1 
ATOM   1518 C CG1 . VAL A 1 208 ? -13.78435 61.68151 43.19161 1.000 68.47000  ? 202 VAL A CG1 1 
ATOM   1519 C CG2 . VAL A 1 208 ? -14.02639 63.47812 41.46791 1.000 70.25123  ? 202 VAL A CG2 1 
ATOM   1520 N N   . PHE A 1 209 ? -12.24446 62.84772 45.67657 1.000 82.89794  ? 203 PHE A N   1 
ATOM   1521 C CA  . PHE A 1 209 ? -11.48381 62.14022 46.69835 1.000 82.92651  ? 203 PHE A CA  1 
ATOM   1522 C C   . PHE A 1 209 ? -12.44229 61.35447 47.58227 1.000 74.83551  ? 203 PHE A C   1 
ATOM   1523 O O   . PHE A 1 209 ? -13.62705 61.68093 47.69179 1.000 80.80354  ? 203 PHE A O   1 
ATOM   1524 C CB  . PHE A 1 209 ? -10.63239 63.10145 47.53778 1.000 85.16683  ? 203 PHE A CB  1 
ATOM   1525 C CG  . PHE A 1 209 ? -11.43379 64.08566 48.34251 1.000 78.59866  ? 203 PHE A CG  1 
ATOM   1526 C CD1 . PHE A 1 209 ? -11.86377 65.27603 47.77928 1.000 76.35235  ? 203 PHE A CD1 1 
ATOM   1527 C CD2 . PHE A 1 209 ? -11.74570 63.82610 49.66711 1.000 85.85641  ? 203 PHE A CD2 1 
ATOM   1528 C CE1 . PHE A 1 209 ? -12.59792 66.18474 48.51996 1.000 69.93116  ? 203 PHE A CE1 1 
ATOM   1529 C CE2 . PHE A 1 209 ? -12.47815 64.73021 50.41164 1.000 83.12233  ? 203 PHE A CE2 1 
ATOM   1530 C CZ  . PHE A 1 209 ? -12.90408 65.91125 49.83805 1.000 77.68186  ? 203 PHE A CZ  1 
ATOM   1531 N N   . PHE A 1 210 ? -11.90894 60.31199 48.21340 1.000 82.56805  ? 204 PHE A N   1 
ATOM   1532 C CA  . PHE A 1 210 ? -12.67803 59.45886 49.10711 1.000 70.83234  ? 204 PHE A CA  1 
ATOM   1533 C C   . PHE A 1 210 ? -12.37140 59.79492 50.55871 1.000 73.14369  ? 204 PHE A C   1 
ATOM   1534 O O   . PHE A 1 210 ? -11.23014 60.10668 50.91124 1.000 88.89003  ? 204 PHE A O   1 
ATOM   1535 C CB  . PHE A 1 210 ? -12.37717 57.97813 48.86345 1.000 68.81636  ? 204 PHE A CB  1 
ATOM   1536 C CG  . PHE A 1 210 ? -12.79433 57.48324 47.51090 1.000 73.92031  ? 204 PHE A CG  1 
ATOM   1537 C CD1 . PHE A 1 210 ? -14.13347 57.41316 47.16519 1.000 69.22529  ? 204 PHE A CD1 1 
ATOM   1538 C CD2 . PHE A 1 210 ? -11.84682 57.06545 46.59199 1.000 81.41724  ? 204 PHE A CD2 1 
ATOM   1539 C CE1 . PHE A 1 210 ? -14.51863 56.95096 45.92141 1.000 69.31268  ? 204 PHE A CE1 1 
ATOM   1540 C CE2 . PHE A 1 210 ? -12.22556 56.60030 45.34741 1.000 79.00230  ? 204 PHE A CE2 1 
ATOM   1541 C CZ  . PHE A 1 210 ? -13.56333 56.54354 45.01150 1.000 74.45828  ? 204 PHE A CZ  1 
ATOM   1542 N N   . THR A 1 211 ? -13.39892 59.73087 51.39402 1.000 74.36117  ? 205 THR A N   1 
ATOM   1543 C CA  . THR A 1 211 ? -13.24126 59.75997 52.83671 1.000 72.65010  ? 205 THR A CA  1 
ATOM   1544 C C   . THR A 1 211 ? -13.72102 58.43809 53.41470 1.000 72.20654  ? 205 THR A C   1 
ATOM   1545 O O   . THR A 1 211 ? -14.44606 57.67804 52.76653 1.000 71.46971  ? 205 THR A O   1 
ATOM   1546 C CB  . THR A 1 211 ? -14.00537 60.92807 53.45952 1.000 73.64483  ? 205 THR A CB  1 
ATOM   1547 O OG1 . THR A 1 211 ? -15.30943 61.01671 52.87324 1.000 75.95383  ? 205 THR A OG1 1 
ATOM   1548 C CG2 . THR A 1 211 ? -13.24964 62.21683 53.21909 1.000 64.14827  ? 205 THR A CG2 1 
ATOM   1549 N N   . ASP A 1 212 ? -13.30793 58.16746 54.64862 1.000 66.47590  ? 206 ASP A N   1 
ATOM   1550 C CA  . ASP A 1 212 ? -13.41233 56.82375 55.19095 1.000 66.29841  ? 206 ASP A CA  1 
ATOM   1551 C C   . ASP A 1 212 ? -13.90343 56.86443 56.62990 1.000 66.82408  ? 206 ASP A C   1 
ATOM   1552 O O   . ASP A 1 212 ? -13.98511 57.92366 57.25652 1.000 75.14169  ? 206 ASP A O   1 
ATOM   1553 C CB  . ASP A 1 212 ? -12.06626 56.10492 55.09210 1.000 71.55937  ? 206 ASP A CB  1 
ATOM   1554 C CG  . ASP A 1 212 ? -11.56490 56.02490 53.66702 1.000 75.34409  ? 206 ASP A CG  1 
ATOM   1555 O OD1 . ASP A 1 212 ? -12.23212 55.36253 52.84692 1.000 90.35299  ? 206 ASP A OD1 1 
ATOM   1556 O OD2 . ASP A 1 212 ? -10.52996 56.65152 53.35651 1.000 86.31288  ? 206 ASP A OD2 1 
ATOM   1557 N N   . SER A 1 213 ? -14.22131 55.67676 57.14768 1.000 68.03487  ? 207 SER A N   1 
ATOM   1558 C CA  . SER A 1 213 ? -14.79683 55.49213 58.47272 1.000 73.50626  ? 207 SER A CA  1 
ATOM   1559 C C   . SER A 1 213 ? -14.73186 54.01056 58.81052 1.000 69.53917  ? 207 SER A C   1 
ATOM   1560 O O   . SER A 1 213 ? -14.74260 53.17388 57.89780 1.000 74.62211  ? 207 SER A O   1 
ATOM   1561 C CB  . SER A 1 213 ? -16.24867 55.99392 58.50964 1.000 72.88991  ? 207 SER A CB  1 
ATOM   1562 O OG  . SER A 1 213 ? -16.82598 55.88664 59.79773 1.000 74.32817  ? 207 SER A OG  1 
ATOM   1563 N N   . PRO A 1 214 ? -14.65907 53.64328 60.10210 1.000 68.68748  ? 208 PRO A N   1 
ATOM   1564 C CA  . PRO A 1 214 ? -14.59007 54.48580 61.30641 1.000 74.55936  ? 208 PRO A CA  1 
ATOM   1565 C C   . PRO A 1 214 ? -13.17145 54.95881 61.59376 1.000 76.89456  ? 208 PRO A C   1 
ATOM   1566 O O   . PRO A 1 214 ? -12.26985 54.75642 60.78516 1.000 87.32842  ? 208 PRO A O   1 
ATOM   1567 C CB  . PRO A 1 214 ? -15.12439 53.55081 62.39785 1.000 76.01678  ? 208 PRO A CB  1 
ATOM   1568 C CG  . PRO A 1 214 ? -14.64604 52.19667 61.96498 1.000 66.66101  ? 208 PRO A CG  1 
ATOM   1569 C CD  . PRO A 1 214 ? -14.71001 52.21184 60.45108 1.000 67.36106  ? 208 PRO A CD  1 
ATOM   1570 N N   . GLU A 1 215 ? -12.94308 55.59074 62.74727 1.000 78.49860  ? 209 GLU A N   1 
ATOM   1571 C CA  . GLU A 1 215 ? -11.63432 56.17867 63.00927 1.000 80.83784  ? 209 GLU A CA  1 
ATOM   1572 C C   . GLU A 1 215 ? -10.57195 55.11831 63.27264 1.000 93.53718  ? 209 GLU A C   1 
ATOM   1573 O O   . GLU A 1 215 ? -9.40942  55.30875 62.89767 1.000 107.33375 ? 209 GLU A O   1 
ATOM   1574 C CB  . GLU A 1 215 ? -11.71322 57.15320 64.18496 1.000 81.79494  ? 209 GLU A CB  1 
ATOM   1575 C CG  . GLU A 1 215 ? -10.46708 58.01291 64.34175 1.000 95.60960  ? 209 GLU A CG  1 
ATOM   1576 C CD  . GLU A 1 215 ? -10.60945 59.07571 65.41398 1.000 110.15056 ? 209 GLU A CD  1 
ATOM   1577 O OE1 . GLU A 1 215 ? -11.55716 58.98790 66.22183 1.000 107.62550 ? 209 GLU A OE1 1 
ATOM   1578 O OE2 . GLU A 1 215 ? -9.77238  60.00310 65.44628 1.000 135.63991 ? 209 GLU A OE2 1 
ATOM   1579 N N   . HIS A 1 216 ? -10.93693 54.00053 63.90137 1.000 92.40246  ? 210 HIS A N   1 
ATOM   1580 C CA  . HIS A 1 216 ? -9.95125  52.97437 64.22497 1.000 96.88798  ? 210 HIS A CA  1 
ATOM   1581 C C   . HIS A 1 216 ? -9.55963  52.12462 63.01973 1.000 88.22292  ? 210 HIS A C   1 
ATOM   1582 O O   . HIS A 1 216 ? -8.81536  51.15156 63.18433 1.000 98.39420  ? 210 HIS A O   1 
ATOM   1583 C CB  . HIS A 1 216 ? -10.45795 52.08149 65.36518 1.000 103.33626 ? 210 HIS A CB  1 
ATOM   1584 C CG  . HIS A 1 216 ? -11.62009 51.21290 64.99565 1.000 123.17205 ? 210 HIS A CG  1 
ATOM   1585 N ND1 . HIS A 1 216 ? -11.47233 49.89993 64.60299 1.000 123.65409 ? 210 HIS A ND1 1 
ATOM   1586 C CD2 . HIS A 1 216 ? -12.95043 51.46450 64.97252 1.000 121.55366 ? 210 HIS A CD2 1 
ATOM   1587 C CE1 . HIS A 1 216 ? -12.66066 49.38207 64.34741 1.000 95.24705  ? 210 HIS A CE1 1 
ATOM   1588 N NE2 . HIS A 1 216 ? -13.57464 50.31072 64.56349 1.000 101.98963 ? 210 HIS A NE2 1 
ATOM   1589 N N   . LEU A 1 217 ? -10.03094 52.47618 61.81987 1.000 86.79926  ? 211 LEU A N   1 
ATOM   1590 C CA  . LEU A 1 217 ? -9.59036  51.84635 60.57965 1.000 82.21846  ? 211 LEU A CA  1 
ATOM   1591 C C   . LEU A 1 217 ? -8.99631  52.85962 59.60518 1.000 94.09253  ? 211 LEU A C   1 
ATOM   1592 O O   . LEU A 1 217 ? -8.83900  52.55440 58.41949 1.000 91.48489  ? 211 LEU A O   1 
ATOM   1593 C CB  . LEU A 1 217 ? -10.74348 51.09920 59.90686 1.000 88.56298  ? 211 LEU A CB  1 
ATOM   1594 C CG  . LEU A 1 217 ? -11.55301 50.07964 60.70488 1.000 85.08999  ? 211 LEU A CG  1 
ATOM   1595 C CD1 . LEU A 1 217 ? -12.43626 49.28248 59.76287 1.000 80.53797  ? 211 LEU A CD1 1 
ATOM   1596 C CD2 . LEU A 1 217 ? -10.65126 49.16052 61.49810 1.000 84.70449  ? 211 LEU A CD2 1 
ATOM   1597 N N   . LEU A 1 218 ? -8.66719  54.06354 60.07766 1.000 92.39384  ? 212 LEU A N   1 
ATOM   1598 C CA  . LEU A 1 218 ? -8.16092  55.11239 59.19922 1.000 100.25581 ? 212 LEU A CA  1 
ATOM   1599 C C   . LEU A 1 218 ? -6.71520  54.90063 58.78482 1.000 99.63230  ? 212 LEU A C   1 
ATOM   1600 O O   . LEU A 1 218 ? -6.31107  55.38799 57.72271 1.000 99.70688  ? 212 LEU A O   1 
ATOM   1601 C CB  . LEU A 1 218 ? -8.26869  56.47897 59.87940 1.000 97.60728  ? 212 LEU A CB  1 
ATOM   1602 C CG  . LEU A 1 218 ? -9.61080  57.20367 59.87055 1.000 80.99984  ? 212 LEU A CG  1 
ATOM   1603 C CD1 . LEU A 1 218 ? -9.49211  58.49070 60.66602 1.000 97.49300  ? 212 LEU A CD1 1 
ATOM   1604 C CD2 . LEU A 1 218 ? -10.03027 57.48772 58.44384 1.000 80.14101  ? 212 LEU A CD2 1 
ATOM   1605 N N   . GLY A 1 219 ? -5.93151  54.19037 59.58792 1.000 104.94721 ? 213 GLY A N   1 
ATOM   1606 C CA  . GLY A 1 219 ? -4.49898  54.25900 59.40033 1.000 111.94194 ? 213 GLY A CA  1 
ATOM   1607 C C   . GLY A 1 219 ? -4.02713  55.64797 59.77555 1.000 112.50422 ? 213 GLY A C   1 
ATOM   1608 O O   . GLY A 1 219 ? -4.57830  56.29546 60.67273 1.000 100.32300 ? 213 GLY A O   1 
ATOM   1609 N N   . TYR A 1 220 ? -3.01907  56.13486 59.06055 1.000 117.80465 ? 214 TYR A N   1 
ATOM   1610 C CA  . TYR A 1 220 ? -2.44562  57.43533 59.35792 1.000 92.22380  ? 214 TYR A CA  1 
ATOM   1611 C C   . TYR A 1 220 ? -2.56076  58.43359 58.21459 1.000 92.35552  ? 214 TYR A C   1 
ATOM   1612 O O   . TYR A 1 220 ? -2.12025  59.57737 58.37163 1.000 94.48209  ? 214 TYR A O   1 
ATOM   1613 C CB  . TYR A 1 220 ? -0.97427  57.27902 59.76099 1.000 103.46113 ? 214 TYR A CB  1 
ATOM   1614 C CG  . TYR A 1 220 ? -0.77134  56.39201 60.96991 1.000 128.28196 ? 214 TYR A CG  1 
ATOM   1615 C CD1 . TYR A 1 220 ? -1.26513  56.76012 62.21500 1.000 128.32960 ? 214 TYR A CD1 1 
ATOM   1616 C CD2 . TYR A 1 220 ? -0.08051  55.19159 60.86884 1.000 130.63281 ? 214 TYR A CD2 1 
ATOM   1617 C CE1 . TYR A 1 220 ? -1.08131  55.95598 63.32393 1.000 141.05898 ? 214 TYR A CE1 1 
ATOM   1618 C CE2 . TYR A 1 220 ? 0.10988   54.38133 61.97328 1.000 141.07418 ? 214 TYR A CE2 1 
ATOM   1619 C CZ  . TYR A 1 220 ? -0.39288  54.76878 63.19743 1.000 161.80198 ? 214 TYR A CZ  1 
ATOM   1620 O OH  . TYR A 1 220 ? -0.20688  53.96666 64.29929 1.000 174.81678 ? 214 TYR A OH  1 
ATOM   1621 N N   . SER A 1 221 ? -3.14528  58.05275 57.08082 1.000 94.94345  ? 215 SER A N   1 
ATOM   1622 C CA  . SER A 1 221 ? -3.25525  58.95452 55.94180 1.000 91.60540  ? 215 SER A CA  1 
ATOM   1623 C C   . SER A 1 221 ? -4.68347  59.22817 55.49947 1.000 98.05620  ? 215 SER A C   1 
ATOM   1624 O O   . SER A 1 221 ? -4.93689  60.28572 54.91855 1.000 104.15226 ? 215 SER A O   1 
ATOM   1625 C CB  . SER A 1 221 ? -2.46687  58.40315 54.74212 1.000 87.63579  ? 215 SER A CB  1 
ATOM   1626 O OG  . SER A 1 221 ? -2.95484  57.13317 54.34828 1.000 109.26721 ? 215 SER A OG  1 
ATOM   1627 N N   . ARG A 1 222 ? -5.61722  58.31571 55.75192 1.000 88.90033  ? 216 ARG A N   1 
ATOM   1628 C CA  . ARG A 1 222 ? -6.98113  58.49449 55.27637 1.000 90.98572  ? 216 ARG A CA  1 
ATOM   1629 C C   . ARG A 1 222 ? -7.69517  59.59212 56.05737 1.000 83.93965  ? 216 ARG A C   1 
ATOM   1630 O O   . ARG A 1 222 ? -7.35656  59.89490 57.20492 1.000 77.54948  ? 216 ARG A O   1 
ATOM   1631 C CB  . ARG A 1 222 ? -7.76336  57.18485 55.38477 1.000 80.02500  ? 216 ARG A CB  1 
ATOM   1632 C CG  . ARG A 1 222 ? -7.30003  56.10964 54.41665 1.000 80.94413  ? 216 ARG A CG  1 
ATOM   1633 C CD  . ARG A 1 222 ? -8.17083  54.86584 54.48930 1.000 94.09859  ? 216 ARG A CD  1 
ATOM   1634 N NE  . ARG A 1 222 ? -7.79165  53.88734 53.47706 1.000 89.42029  ? 216 ARG A NE  1 
ATOM   1635 C CZ  . ARG A 1 222 ? -8.34304  52.68880 53.34690 1.000 84.44988  ? 216 ARG A CZ  1 
ATOM   1636 N NH1 . ARG A 1 222 ? -9.31064  52.28208 54.15202 1.000 82.96946  ? 216 ARG A NH1 1 
ATOM   1637 N NH2 . ARG A 1 222 ? -7.91077  51.87690 52.38614 1.000 79.18544  ? 216 ARG A NH2 1 
ATOM   1638 N N   . ASP A 1 223 ? -8.69808  60.18854 55.41661 1.000 80.46977  ? 217 ASP A N   1 
ATOM   1639 C CA  . ASP A 1 223 ? -9.50689  61.23071 56.03330 1.000 77.72497  ? 217 ASP A CA  1 
ATOM   1640 C C   . ASP A 1 223 ? -10.72026 60.61226 56.71199 1.000 78.22595  ? 217 ASP A C   1 
ATOM   1641 O O   . ASP A 1 223 ? -11.42733 59.79711 56.11034 1.000 87.09505  ? 217 ASP A O   1 
ATOM   1642 C CB  . ASP A 1 223 ? -9.96954  62.25284 54.99460 1.000 91.28932  ? 217 ASP A CB  1 
ATOM   1643 C CG  . ASP A 1 223 ? -8.83181  63.07097 54.42804 1.000 96.97423  ? 217 ASP A CG  1 
ATOM   1644 O OD1 . ASP A 1 223 ? -7.78032  63.18584 55.09422 1.000 101.63185 ? 217 ASP A OD1 1 
ATOM   1645 O OD2 . ASP A 1 223 ? -9.00103  63.61104 53.31552 1.000 82.77234  ? 217 ASP A OD2 1 
ATOM   1646 N N   . LEU A 1 224 ? -10.96203 61.00551 57.95880 1.000 78.94436  ? 218 LEU A N   1 
ATOM   1647 C CA  . LEU A 1 224 ? -12.18495 60.60739 58.64106 1.000 70.98588  ? 218 LEU A CA  1 
ATOM   1648 C C   . LEU A 1 224 ? -13.36070 61.36931 58.04255 1.000 72.25497  ? 218 LEU A C   1 
ATOM   1649 O O   . LEU A 1 224 ? -13.35671 62.60485 58.01540 1.000 75.61005  ? 218 LEU A O   1 
ATOM   1650 C CB  . LEU A 1 224 ? -12.07037 60.87600 60.13855 1.000 66.67646  ? 218 LEU A CB  1 
ATOM   1651 C CG  . LEU A 1 224 ? -13.21372 60.34871 61.00724 1.000 71.82815  ? 218 LEU A CG  1 
ATOM   1652 C CD1 . LEU A 1 224 ? -13.43901 58.87053 60.74738 1.000 74.56244  ? 218 LEU A CD1 1 
ATOM   1653 C CD2 . LEU A 1 224 ? -12.92200 60.59105 62.47754 1.000 69.82477  ? 218 LEU A CD2 1 
ATOM   1654 N N   . ASP A 1 225 ? -14.36185 60.63170 57.55314 1.000 81.35034  ? 219 ASP A N   1 
ATOM   1655 C CA  . ASP A 1 225 ? -15.51740 61.26448 56.92320 1.000 65.32148  ? 219 ASP A CA  1 
ATOM   1656 C C   . ASP A 1 225 ? -16.19875 62.24248 57.87165 1.000 73.06627  ? 219 ASP A C   1 
ATOM   1657 O O   . ASP A 1 225 ? -16.73740 63.26910 57.44108 1.000 78.20077  ? 219 ASP A O   1 
ATOM   1658 C CB  . ASP A 1 225 ? -16.50826 60.19628 56.46236 1.000 63.52635  ? 219 ASP A CB  1 
ATOM   1659 C CG  . ASP A 1 225 ? -17.48097 60.71300 55.42089 1.000 80.38455  ? 219 ASP A CG  1 
ATOM   1660 O OD1 . ASP A 1 225 ? -17.16403 61.72108 54.75410 1.000 72.42037  ? 219 ASP A OD1 1 
ATOM   1661 O OD2 . ASP A 1 225 ? -18.56442 60.11018 55.27091 1.000 85.69017  ? 219 ASP A OD2 1 
ATOM   1662 N N   . THR A 1 226 ? -16.17560 61.94034 59.17119 1.000 70.95540  ? 220 THR A N   1 
ATOM   1663 C CA  . THR A 1 226 ? -16.79689 62.81261 60.16203 1.000 61.36274  ? 220 THR A CA  1 
ATOM   1664 C C   . THR A 1 226 ? -16.22403 64.22497 60.10236 1.000 70.27307  ? 220 THR A C   1 
ATOM   1665 O O   . THR A 1 226 ? -16.96674 65.21253 60.13070 1.000 79.33572  ? 220 THR A O   1 
ATOM   1666 C CB  . THR A 1 226 ? -16.60842 62.21957 61.55808 1.000 72.47757  ? 220 THR A CB  1 
ATOM   1667 O OG1 . THR A 1 226 ? -17.11891 60.88102 61.58151 1.000 82.98479  ? 220 THR A OG1 1 
ATOM   1668 C CG2 . THR A 1 226 ? -17.33550 63.05537 62.59189 1.000 62.66474  ? 220 THR A CG2 1 
ATOM   1669 N N   . ASP A 1 227 ? -14.89671 64.33858 60.01646 1.000 77.43549  ? 221 ASP A N   1 
ATOM   1670 C CA  . ASP A 1 227 ? -14.26438 65.65500 60.02523 1.000 77.00609  ? 221 ASP A CA  1 
ATOM   1671 C C   . ASP A 1 227 ? -14.50585 66.40124 58.71797 1.000 86.34611  ? 221 ASP A C   1 
ATOM   1672 O O   . ASP A 1 227 ? -14.71896 67.61944 58.72340 1.000 81.43674  ? 221 ASP A O   1 
ATOM   1673 C CB  . ASP A 1 227 ? -12.76559 65.51636 60.29649 1.000 79.57648  ? 221 ASP A CB  1 
ATOM   1674 C CG  . ASP A 1 227 ? -12.47200 64.96990 61.68134 1.000 91.52180  ? 221 ASP A CG  1 
ATOM   1675 O OD1 . ASP A 1 227 ? -13.28637 65.20658 62.59884 1.000 93.59692  ? 221 ASP A OD1 1 
ATOM   1676 O OD2 . ASP A 1 227 ? -11.42791 64.30511 61.85517 1.000 97.28946  ? 221 ASP A OD2 1 
ATOM   1677 N N   . VAL A 1 228 ? -14.47884 65.69195 57.58931 1.000 77.36070  ? 222 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 228 ? -14.68678 66.34450 56.29991 1.000 77.33568  ? 222 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 228 ? -16.11394 66.86943 56.18991 1.000 73.17280  ? 222 VAL A C   1 
ATOM   1680 O O   . VAL A 1 228 ? -16.34434 68.00380 55.75358 1.000 82.32446  ? 222 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 228 ? -14.34301 65.37817 55.15308 1.000 73.54134  ? 222 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 228 ? -14.85423 65.91770 53.82773 1.000 58.98087  ? 222 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 228 ? -12.84365 65.16818 55.09700 1.000 68.89838  ? 222 VAL A CG2 1 
ATOM   1684 N N   . VAL A 1 229 ? -17.09157 66.05780 56.59673 1.000 72.94643  ? 223 VAL A N   1 
ATOM   1685 C CA  . VAL A 1 229 ? -18.49129 66.46820 56.50480 1.000 71.04912  ? 223 VAL A CA  1 
ATOM   1686 C C   . VAL A 1 229 ? -18.75043 67.68554 57.38465 1.000 79.94701  ? 223 VAL A C   1 
ATOM   1687 O O   . VAL A 1 229 ? -19.39407 68.65476 56.96364 1.000 86.14760  ? 223 VAL A O   1 
ATOM   1688 C CB  . VAL A 1 229 ? -19.41726 65.29573 56.87531 1.000 68.47773  ? 223 VAL A CB  1 
ATOM   1689 C CG1 . VAL A 1 229 ? -20.82620 65.79534 57.15791 1.000 63.05446  ? 223 VAL A CG1 1 
ATOM   1690 C CG2 . VAL A 1 229 ? -19.42625 64.26507 55.75908 1.000 64.26221  ? 223 VAL A CG2 1 
ATOM   1691 N N   . ILE A 1 230 ? -18.24785 67.65592 58.62016 1.000 80.86151  ? 224 ILE A N   1 
ATOM   1692 C CA  . ILE A 1 230 ? -18.50963 68.74824 59.55248 1.000 70.71898  ? 224 ILE A CA  1 
ATOM   1693 C C   . ILE A 1 230 ? -17.81187 70.02590 59.09954 1.000 76.88500  ? 224 ILE A C   1 
ATOM   1694 O O   . ILE A 1 230 ? -18.37651 71.12248 59.19498 1.000 85.69970  ? 224 ILE A O   1 
ATOM   1695 C CB  . ILE A 1 230 ? -18.09433 68.34032 60.97746 1.000 72.06596  ? 224 ILE A CB  1 
ATOM   1696 C CG1 . ILE A 1 230 ? -19.04588 67.27277 61.51646 1.000 70.13932  ? 224 ILE A CG1 1 
ATOM   1697 C CG2 . ILE A 1 230 ? -18.07526 69.54444 61.90211 1.000 70.29156  ? 224 ILE A CG2 1 
ATOM   1698 C CD1 . ILE A 1 230 ? -18.75780 66.87027 62.93980 1.000 68.66307  ? 224 ILE A CD1 1 
ATOM   1699 N N   . ASP A 1 231 ? -16.58090 69.91011 58.59420 1.000 79.04421  ? 225 ASP A N   1 
ATOM   1700 C CA  . ASP A 1 231 ? -15.87746 71.09074 58.10063 1.000 82.37952  ? 225 ASP A CA  1 
ATOM   1701 C C   . ASP A 1 231 ? -16.62975 71.74032 56.94647 1.000 74.10511  ? 225 ASP A C   1 
ATOM   1702 O O   . ASP A 1 231 ? -16.73439 72.97022 56.87947 1.000 85.32320  ? 225 ASP A O   1 
ATOM   1703 C CB  . ASP A 1 231 ? -14.45704 70.72356 57.67201 1.000 87.84474  ? 225 ASP A CB  1 
ATOM   1704 C CG  . ASP A 1 231 ? -13.54071 70.46759 58.85047 1.000 115.64329 ? 225 ASP A CG  1 
ATOM   1705 O OD1 . ASP A 1 231 ? -13.80607 71.01292 59.94276 1.000 106.38640 ? 225 ASP A OD1 1 
ATOM   1706 O OD2 . ASP A 1 231 ? -12.55067 69.72537 58.68341 1.000 134.81098 ? 225 ASP A OD2 1 
ATOM   1707 N N   . LYS A 1 232 ? -17.16382 70.93068 56.02919 1.000 76.69850  ? 226 LYS A N   1 
ATOM   1708 C CA  . LYS A 1 232 ? -17.92533 71.48350 54.91393 1.000 75.84936  ? 226 LYS A CA  1 
ATOM   1709 C C   . LYS A 1 232 ? -19.20107 72.16045 55.39785 1.000 86.53991  ? 226 LYS A C   1 
ATOM   1710 O O   . LYS A 1 232 ? -19.55398 73.24698 54.92392 1.000 88.44065  ? 226 LYS A O   1 
ATOM   1711 C CB  . LYS A 1 232 ? -18.24844 70.38454 53.90296 1.000 67.08872  ? 226 LYS A CB  1 
ATOM   1712 C CG  . LYS A 1 232 ? -17.02993 69.85235 53.17474 1.000 72.83728  ? 226 LYS A CG  1 
ATOM   1713 C CD  . LYS A 1 232 ? -16.29778 70.97647 52.46257 1.000 71.85164  ? 226 LYS A CD  1 
ATOM   1714 C CE  . LYS A 1 232 ? -15.03276 70.47847 51.78722 1.000 73.15484  ? 226 LYS A CE  1 
ATOM   1715 N NZ  . LYS A 1 232 ? -14.28603 71.59303 51.13971 1.000 86.66934  ? 226 LYS A NZ  1 
ATOM   1716 N N   . LEU A 1 233 ? -19.90804 71.53328 56.34152 1.000 76.81965  ? 227 LEU A N   1 
ATOM   1717 C CA  . LEU A 1 233 ? -21.10550 72.15467 56.89748 1.000 76.32896  ? 227 LEU A CA  1 
ATOM   1718 C C   . LEU A 1 233 ? -20.77811 73.45362 57.62371 1.000 80.33288  ? 227 LEU A C   1 
ATOM   1719 O O   . LEU A 1 233 ? -21.57028 74.40214 57.58480 1.000 101.11079 ? 227 LEU A O   1 
ATOM   1720 C CB  . LEU A 1 233 ? -21.81547 71.18274 57.84147 1.000 70.75472  ? 227 LEU A CB  1 
ATOM   1721 C CG  . LEU A 1 233 ? -22.48342 69.95290 57.22421 1.000 73.13727  ? 227 LEU A CG  1 
ATOM   1722 C CD1 . LEU A 1 233 ? -22.98641 69.02201 58.31346 1.000 72.96129  ? 227 LEU A CD1 1 
ATOM   1723 C CD2 . LEU A 1 233 ? -23.62359 70.37129 56.31529 1.000 70.71891  ? 227 LEU A CD2 1 
ATOM   1724 N N   . LYS A 1 234 ? -19.62185 73.51955 58.28733 1.000 86.01897  ? 228 LYS A N   1 
ATOM   1725 C CA  . LYS A 1 234 ? -19.22368 74.73747 58.98245 1.000 91.08533  ? 228 LYS A CA  1 
ATOM   1726 C C   . LYS A 1 234 ? -18.70505 75.81247 58.03808 1.000 84.27736  ? 228 LYS A C   1 
ATOM   1727 O O   . LYS A 1 234 ? -18.74989 76.99725 58.38740 1.000 93.57034  ? 228 LYS A O   1 
ATOM   1728 C CB  . LYS A 1 234 ? -18.15552 74.42670 60.03389 1.000 72.31378  ? 228 LYS A CB  1 
ATOM   1729 C CG  . LYS A 1 234 ? -18.67647 73.67027 61.24232 1.000 87.18108  ? 228 LYS A CG  1 
ATOM   1730 C CD  . LYS A 1 234 ? -17.60055 73.52237 62.30430 1.000 93.00255  ? 228 LYS A CD  1 
ATOM   1731 C CE  . LYS A 1 234 ? -18.15902 72.88866 63.56704 1.000 106.36876 ? 228 LYS A CE  1 
ATOM   1732 N NZ  . LYS A 1 234 ? -19.30989 73.66187 64.11088 1.000 110.78972 ? 228 LYS A NZ  1 
ATOM   1733 N N   . SER A 1 235 ? -18.21349 75.43141 56.86016 1.000 87.92389  ? 229 SER A N   1 
ATOM   1734 C CA  . SER A 1 235 ? -17.70334 76.39048 55.89070 1.000 86.06047  ? 229 SER A CA  1 
ATOM   1735 C C   . SER A 1 235 ? -18.76564 76.86600 54.90947 1.000 92.70903  ? 229 SER A C   1 
ATOM   1736 O O   . SER A 1 235 ? -18.47471 77.73750 54.08251 1.000 90.97481  ? 229 SER A O   1 
ATOM   1737 C CB  . SER A 1 235 ? -16.53009 75.78482 55.10963 1.000 100.61323 ? 229 SER A CB  1 
ATOM   1738 O OG  . SER A 1 235 ? -16.97668 74.78971 54.20291 1.000 97.05680  ? 229 SER A OG  1 
ATOM   1739 N N   . ALA A 1 236 ? -19.97780 76.31904 54.97835 1.000 89.46581  ? 230 ALA A N   1 
ATOM   1740 C CA  . ALA A 1 236 ? -21.02960 76.71246 54.05184 1.000 79.95772  ? 230 ALA A CA  1 
ATOM   1741 C C   . ALA A 1 236 ? -21.36042 78.18944 54.21209 1.000 80.84937  ? 230 ALA A C   1 
ATOM   1742 O O   . ALA A 1 236 ? -21.48558 78.69984 55.32841 1.000 89.12515  ? 230 ALA A O   1 
ATOM   1743 C CB  . ALA A 1 236 ? -22.28108 75.86676 54.27867 1.000 82.03080  ? 230 ALA A CB  1 
ATOM   1744 N N   . LYS A 1 237 ? -21.49865 78.87806 53.08039 1.000 90.81626  ? 231 LYS A N   1 
ATOM   1745 C CA  . LYS A 1 237 ? -21.78546 80.30208 53.07159 1.000 82.89459  ? 231 LYS A CA  1 
ATOM   1746 C C   . LYS A 1 237 ? -23.13583 80.65469 52.46893 1.000 79.84835  ? 231 LYS A C   1 
ATOM   1747 O O   . LYS A 1 237 ? -23.58981 81.79082 52.64650 1.000 84.91182  ? 231 LYS A O   1 
ATOM   1748 C CB  . LYS A 1 237 ? -20.69296 81.06435 52.30499 1.000 80.02810  ? 231 LYS A CB  1 
ATOM   1749 C CG  . LYS A 1 237 ? -19.29246 80.90171 52.87235 1.000 105.13333 ? 231 LYS A CG  1 
ATOM   1750 C CD  . LYS A 1 237 ? -18.27639 81.64639 52.01807 1.000 122.24791 ? 231 LYS A CD  1 
ATOM   1751 C CE  . LYS A 1 237 ? -16.86704 81.50797 52.56957 1.000 135.86347 ? 231 LYS A CE  1 
ATOM   1752 N NZ  . LYS A 1 237 ? -15.88165 82.27109 51.75159 1.000 137.42465 ? 231 LYS A NZ  1 
ATOM   1753 N N   . THR A 1 238 ? -23.78962 79.73042 51.76643 1.000 87.40897  ? 232 THR A N   1 
ATOM   1754 C CA  . THR A 1 238 ? -25.03679 80.05963 51.08827 1.000 84.65866  ? 232 THR A CA  1 
ATOM   1755 C C   . THR A 1 238 ? -26.10310 78.99193 51.30021 1.000 86.78770  ? 232 THR A C   1 
ATOM   1756 O O   . THR A 1 238 ? -27.15186 79.26887 51.89052 1.000 87.20698  ? 232 THR A O   1 
ATOM   1757 C CB  . THR A 1 238 ? -24.79399 80.26061 49.59033 1.000 85.68157  ? 232 THR A CB  1 
ATOM   1758 O OG1 . THR A 1 238 ? -23.76883 81.24359 49.39610 1.000 85.56189  ? 232 THR A OG1 1 
ATOM   1759 C CG2 . THR A 1 238 ? -26.06957 80.72793 48.90643 1.000 79.67046  ? 232 THR A CG2 1 
ATOM   1760 N N   . SER A 1 239 ? -25.85290 77.77317 50.82470 1.000 84.47896  ? 233 SER A N   1 
ATOM   1761 C CA  . SER A 1 239 ? -26.86737 76.73067 50.81259 1.000 70.55102  ? 233 SER A CA  1 
ATOM   1762 C C   . SER A 1 239 ? -26.32075 75.43455 51.39072 1.000 82.31421  ? 233 SER A C   1 
ATOM   1763 O O   . SER A 1 239 ? -25.13003 75.13195 51.27408 1.000 79.04400  ? 233 SER A O   1 
ATOM   1764 C CB  . SER A 1 239 ? -27.38256 76.46500 49.39259 1.000 83.55108  ? 233 SER A CB  1 
ATOM   1765 O OG  . SER A 1 239 ? -26.39174 75.82421 48.60597 1.000 101.78551 ? 233 SER A OG  1 
ATOM   1766 N N   . ILE A 1 240 ? -27.21574 74.66729 52.01082 1.000 74.66668  ? 234 ILE A N   1 
ATOM   1767 C CA  . ILE A 1 240 ? -26.93757 73.30006 52.43749 1.000 67.21987  ? 234 ILE A CA  1 
ATOM   1768 C C   . ILE A 1 240 ? -28.16241 72.46709 52.08659 1.000 71.81359  ? 234 ILE A C   1 
ATOM   1769 O O   . ILE A 1 240 ? -29.23856 72.67129 52.65909 1.000 82.62842  ? 234 ILE A O   1 
ATOM   1770 C CB  . ILE A 1 240 ? -26.62868 73.19071 53.93680 1.000 78.91635  ? 234 ILE A CB  1 
ATOM   1771 C CG1 . ILE A 1 240 ? -25.27069 73.81412 54.25725 1.000 63.86613  ? 234 ILE A CG1 1 
ATOM   1772 C CG2 . ILE A 1 240 ? -26.66806 71.73267 54.37976 1.000 65.62208  ? 234 ILE A CG2 1 
ATOM   1773 C CD1 . ILE A 1 240 ? -24.95580 73.83934 55.73288 1.000 65.25555  ? 234 ILE A CD1 1 
ATOM   1774 N N   . ASP A 1 241 ? -28.00839 71.54140 51.14659 1.000 73.52840  ? 235 ASP A N   1 
ATOM   1775 C CA  . ASP A 1 241 ? -29.06050 70.60354 50.78180 1.000 73.99427  ? 235 ASP A CA  1 
ATOM   1776 C C   . ASP A 1 241 ? -28.64080 69.20564 51.20999 1.000 75.11238  ? 235 ASP A C   1 
ATOM   1777 O O   . ASP A 1 241 ? -27.52475 68.76917 50.90892 1.000 71.35153  ? 235 ASP A O   1 
ATOM   1778 C CB  . ASP A 1 241 ? -29.33862 70.63817 49.27761 1.000 75.93528  ? 235 ASP A CB  1 
ATOM   1779 C CG  . ASP A 1 241 ? -29.90015 71.96869 48.81787 1.000 83.12515  ? 235 ASP A CG  1 
ATOM   1780 O OD1 . ASP A 1 241 ? -30.59741 72.63276 49.61413 1.000 91.30052  ? 235 ASP A OD1 1 
ATOM   1781 O OD2 . ASP A 1 241 ? -29.64667 72.34874 47.65622 1.000 84.04830  ? 235 ASP A OD2 1 
ATOM   1782 N N   . ILE A 1 242 ? -29.52689 68.51350 51.91922 1.000 66.19200  ? 236 ILE A N   1 
ATOM   1783 C CA  . ILE A 1 242 ? -29.25518 67.17423 52.42215 1.000 66.93020  ? 236 ILE A CA  1 
ATOM   1784 C C   . ILE A 1 242 ? -30.45327 66.28604 52.12816 1.000 71.46838  ? 236 ILE A C   1 
ATOM   1785 O O   . ILE A 1 242 ? -31.60332 66.68080 52.35159 1.000 76.41421  ? 236 ILE A O   1 
ATOM   1786 C CB  . ILE A 1 242 ? -28.94773 67.17886 53.93469 1.000 70.40099  ? 236 ILE A CB  1 
ATOM   1787 C CG1 . ILE A 1 242 ? -27.62411 67.89156 54.21382 1.000 70.50458  ? 236 ILE A CG1 1 
ATOM   1788 C CG2 . ILE A 1 242 ? -28.92618 65.75640 54.48211 1.000 66.30358  ? 236 ILE A CG2 1 
ATOM   1789 C CD1 . ILE A 1 242 ? -27.25767 67.93653 55.67578 1.000 61.65789  ? 236 ILE A CD1 1 
ATOM   1790 N N   . GLU A 1 243 ? -30.18165 65.08612 51.61845 1.000 66.96267  ? 237 GLU A N   1 
ATOM   1791 C CA  . GLU A 1 243 ? -31.19258 64.04429 51.44892 1.000 66.02615  ? 237 GLU A CA  1 
ATOM   1792 C C   . GLU A 1 243 ? -30.63535 62.79109 52.11518 1.000 68.28402  ? 237 GLU A C   1 
ATOM   1793 O O   . GLU A 1 243 ? -29.89706 62.02012 51.49590 1.000 75.22749  ? 237 GLU A O   1 
ATOM   1794 C CB  . GLU A 1 243 ? -31.52969 63.80925 49.98140 1.000 63.81649  ? 237 GLU A CB  1 
ATOM   1795 C CG  . GLU A 1 243 ? -32.60366 62.75254 49.76780 1.000 57.39919  ? 237 GLU A CG  1 
ATOM   1796 C CD  . GLU A 1 243 ? -32.97871 62.58928 48.31016 1.000 72.05960  ? 237 GLU A CD  1 
ATOM   1797 O OE1 . GLU A 1 243 ? -32.89891 63.58671 47.56476 1.000 69.17774  ? 237 GLU A OE1 1 
ATOM   1798 O OE2 . GLU A 1 243 ? -33.34754 61.46472 47.90843 1.000 69.99625  ? 237 GLU A OE2 1 
ATOM   1799 N N   . HIS A 1 244 ? -30.98035 62.60246 53.38537 1.000 65.85340  ? 238 HIS A N   1 
ATOM   1800 C CA  . HIS A 1 244 ? -30.57124 61.44153 54.16044 1.000 63.88649  ? 238 HIS A CA  1 
ATOM   1801 C C   . HIS A 1 244 ? -31.80923 60.77324 54.74294 1.000 63.08901  ? 238 HIS A C   1 
ATOM   1802 O O   . HIS A 1 244 ? -32.94283 61.20826 54.52035 1.000 77.51929  ? 238 HIS A O   1 
ATOM   1803 C CB  . HIS A 1 244 ? -29.58541 61.83145 55.26946 1.000 69.55702  ? 238 HIS A CB  1 
ATOM   1804 C CG  . HIS A 1 244 ? -28.15308 61.81597 54.83641 1.000 75.88126  ? 238 HIS A CG  1 
ATOM   1805 N ND1 . HIS A 1 244 ? -27.19543 61.04739 55.46244 1.000 69.20963  ? 238 HIS A ND1 1 
ATOM   1806 C CD2 . HIS A 1 244 ? -27.51697 62.46804 53.83479 1.000 66.86169  ? 238 HIS A CD2 1 
ATOM   1807 C CE1 . HIS A 1 244 ? -26.03025 61.23044 54.86785 1.000 74.10645  ? 238 HIS A CE1 1 
ATOM   1808 N NE2 . HIS A 1 244 ? -26.19795 62.08758 53.87693 1.000 69.16142  ? 238 HIS A NE2 1 
ATOM   1809 N N   . LEU A 1 245 ? -31.58478 59.70015 55.49951 1.000 63.65275  ? 239 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 245 ? -32.69657 58.99801 56.12722 1.000 59.53831  ? 239 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 245 ? -33.16971 59.71755 57.38344 1.000 74.57468  ? 239 LEU A C   1 
ATOM   1812 O O   . LEU A 1 245 ? -34.37520 59.77604 57.65010 1.000 71.92228  ? 239 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 245 ? -32.29084 57.56092 56.45362 1.000 51.39383  ? 239 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 245 ? -33.40032 56.63863 56.95580 1.000 59.81040  ? 239 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 245 ? -34.57305 56.63474 55.98561 1.000 47.09085  ? 239 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 245 ? -32.86694 55.23016 57.15969 1.000 61.22039  ? 239 LEU A CD2 1 
ATOM   1817 N N   . ALA A 1 246 ? -32.24091 60.27573 58.15779 1.000 69.47127  ? 240 ALA A N   1 
ATOM   1818 C CA  . ALA A 1 246 ? -32.58680 60.98096 59.38332 1.000 69.91121  ? 240 ALA A CA  1 
ATOM   1819 C C   . ALA A 1 246 ? -31.42954 61.88055 59.78741 1.000 73.89515  ? 240 ALA A C   1 
ATOM   1820 O O   . ALA A 1 246 ? -30.26200 61.54702 59.57046 1.000 84.73486  ? 240 ALA A O   1 
ATOM   1821 C CB  . ALA A 1 246 ? -32.92022 60.00693 60.51727 1.000 59.47929  ? 240 ALA A CB  1 
ATOM   1822 N N   . ILE A 1 247 ? -31.77113 63.02810 60.37247 1.000 80.02106  ? 241 ILE A N   1 
ATOM   1823 C CA  . ILE A 1 247 ? -30.77969 63.96337 60.89328 1.000 74.65571  ? 241 ILE A CA  1 
ATOM   1824 C C   . ILE A 1 247 ? -31.05827 64.18317 62.37546 1.000 68.82349  ? 241 ILE A C   1 
ATOM   1825 O O   . ILE A 1 247 ? -30.95967 65.30550 62.88185 1.000 96.27346  ? 241 ILE A O   1 
ATOM   1826 C CB  . ILE A 1 247 ? -30.79467 65.29685 60.12027 1.000 71.23189  ? 241 ILE A CB  1 
ATOM   1827 C CG1 . ILE A 1 247 ? -30.93559 65.05502 58.61785 1.000 77.08270  ? 241 ILE A CG1 1 
ATOM   1828 C CG2 . ILE A 1 247 ? -29.51038 66.06714 60.35825 1.000 88.79973  ? 241 ILE A CG2 1 
ATOM   1829 C CD1 . ILE A 1 247 ? -29.66974 64.55137 57.95746 1.000 74.13751  ? 241 ILE A CD1 1 
ATOM   1830 N N   . VAL A 1 248 ? -31.41952 63.11851 63.08195 1.000 83.11398  ? 242 VAL A N   1 
ATOM   1831 C CA  . VAL A 1 248 ? -31.70641 63.22513 64.50972 1.000 81.07959  ? 242 VAL A CA  1 
ATOM   1832 C C   . VAL A 1 248 ? -30.39634 63.13413 65.28324 1.000 79.93411  ? 242 VAL A C   1 
ATOM   1833 O O   . VAL A 1 248 ? -29.47077 62.42837 64.85687 1.000 88.11715  ? 242 VAL A O   1 
ATOM   1834 C CB  . VAL A 1 248 ? -32.70216 62.14683 64.96607 1.000 85.56389  ? 242 VAL A CB  1 
ATOM   1835 C CG1 . VAL A 1 248 ? -34.07268 62.40367 64.36016 1.000 94.63225  ? 242 VAL A CG1 1 
ATOM   1836 C CG2 . VAL A 1 248 ? -32.19659 60.75987 64.59375 1.000 74.69521  ? 242 VAL A CG2 1 
ATOM   1837 N N   . PRO A 1 249 ? -30.26206 63.83874 66.40838 1.000 79.51996  ? 243 PRO A N   1 
ATOM   1838 C CA  . PRO A 1 249 ? -29.04750 63.71911 67.22066 1.000 76.72981  ? 243 PRO A CA  1 
ATOM   1839 C C   . PRO A 1 249 ? -29.02505 62.50150 68.12899 1.000 75.29650  ? 243 PRO A C   1 
ATOM   1840 O O   . PRO A 1 249 ? -28.05615 62.33155 68.87703 1.000 88.77593  ? 243 PRO A O   1 
ATOM   1841 C CB  . PRO A 1 249 ? -29.06949 65.01223 68.04428 1.000 87.36340  ? 243 PRO A CB  1 
ATOM   1842 C CG  . PRO A 1 249 ? -30.52186 65.29398 68.22123 1.000 78.44472  ? 243 PRO A CG  1 
ATOM   1843 C CD  . PRO A 1 249 ? -31.18431 64.85782 66.93952 1.000 87.37892  ? 243 PRO A CD  1 
ATOM   1844 N N   . THR A 1 250 ? -30.05145 61.65433 68.08884 1.000 74.36077  ? 244 THR A N   1 
ATOM   1845 C CA  . THR A 1 250 ? -30.15146 60.50125 68.97326 1.000 79.68207  ? 244 THR A CA  1 
ATOM   1846 C C   . THR A 1 250 ? -30.45546 59.25540 68.15590 1.000 81.60085  ? 244 THR A C   1 
ATOM   1847 O O   . THR A 1 250 ? -31.38903 59.25222 67.34790 1.000 103.26053 ? 244 THR A O   1 
ATOM   1848 C CB  . THR A 1 250 ? -31.23977 60.70951 70.03299 1.000 70.85266  ? 244 THR A CB  1 
ATOM   1849 O OG1 . THR A 1 250 ? -31.00845 61.94341 70.72312 1.000 97.40889  ? 244 THR A OG1 1 
ATOM   1850 C CG2 . THR A 1 250 ? -31.23027 59.57085 71.03673 1.000 68.18359  ? 244 THR A CG2 1 
ATOM   1851 N N   . THR A 1 251 ? -29.66843 58.20304 68.36721 1.000 83.36615  ? 245 THR A N   1 
ATOM   1852 C CA  . THR A 1 251 ? -29.89862 56.90967 67.74161 1.000 76.47591  ? 245 THR A CA  1 
ATOM   1853 C C   . THR A 1 251 ? -29.87586 55.82632 68.80772 1.000 90.59855  ? 245 THR A C   1 
ATOM   1854 O O   . THR A 1 251 ? -29.24117 55.97851 69.85476 1.000 103.10910 ? 245 THR A O   1 
ATOM   1855 C CB  . THR A 1 251 ? -28.85376 56.60188 66.66667 1.000 74.31883  ? 245 THR A CB  1 
ATOM   1856 O OG1 . THR A 1 251 ? -27.54298 56.86772 67.18153 1.000 100.92643 ? 245 THR A OG1 1 
ATOM   1857 C CG2 . THR A 1 251 ? -29.09761 57.45771 65.44266 1.000 76.46358  ? 245 THR A CG2 1 
ATOM   1858 N N   . ARG A 1 252 ? -30.57207 54.72825 68.53486 1.000 93.61359  ? 246 ARG A N   1 
ATOM   1859 C CA  . ARG A 1 252 ? -30.73483 53.64854 69.50389 1.000 112.16400 ? 246 ARG A CA  1 
ATOM   1860 C C   . ARG A 1 252 ? -29.90562 52.45229 69.04804 1.000 122.10563 ? 246 ARG A C   1 
ATOM   1861 O O   . ARG A 1 252 ? -30.27539 51.75142 68.10164 1.000 123.95364 ? 246 ARG A O   1 
ATOM   1862 C CB  . ARG A 1 252 ? -32.20573 53.27693 69.66644 1.000 106.58684 ? 246 ARG A CB  1 
ATOM   1863 C CG  . ARG A 1 252 ? -32.53639 52.69249 71.03091 1.000 129.26838 ? 246 ARG A CG  1 
ATOM   1864 C CD  . ARG A 1 252 ? -33.90017 52.02470 71.04454 1.000 136.86782 ? 246 ARG A CD  1 
ATOM   1865 N NE  . ARG A 1 252 ? -33.90927 50.79554 70.26060 1.000 149.34693 ? 246 ARG A NE  1 
ATOM   1866 C CZ  . ARG A 1 252 ? -34.93456 49.95765 70.19246 1.000 147.76072 ? 246 ARG A CZ  1 
ATOM   1867 N NH1 . ARG A 1 252 ? -36.05883 50.18591 70.85150 1.000 150.02700 ? 246 ARG A NH1 1 
ATOM   1868 N NH2 . ARG A 1 252 ? -34.82803 48.86148 69.44692 1.000 139.57482 ? 246 ARG A NH2 1 
ATOM   1869 N N   . VAL A 1 253 ? -28.78261 52.22740 69.72207 1.000 134.51579 ? 247 VAL A N   1 
ATOM   1870 C CA  . VAL A 1 253 ? -27.97486 51.03103 69.51718 1.000 138.34855 ? 247 VAL A CA  1 
ATOM   1871 C C   . VAL A 1 253 ? -28.44668 49.97963 70.51285 1.000 144.30012 ? 247 VAL A C   1 
ATOM   1872 O O   . VAL A 1 253 ? -28.44151 50.22063 71.72517 1.000 159.20609 ? 247 VAL A O   1 
ATOM   1873 C CB  . VAL A 1 253 ? -26.47749 51.32844 69.68808 1.000 123.78348 ? 247 VAL A CB  1 
ATOM   1874 C CG1 . VAL A 1 253 ? -25.65682 50.06837 69.46045 1.000 112.21736 ? 247 VAL A CG1 1 
ATOM   1875 C CG2 . VAL A 1 253 ? -26.04253 52.43337 68.73542 1.000 97.88148  ? 247 VAL A CG2 1 
ATOM   1876 N N   . ASP A 1 254 ? -28.84250 48.81224 69.99652 1.000 136.24103 ? 248 ASP A N   1 
ATOM   1877 C CA  . ASP A 1 254 ? -29.49107 47.74129 70.75333 1.000 149.81406 ? 248 ASP A CA  1 
ATOM   1878 C C   . ASP A 1 254 ? -30.47138 48.27657 71.79663 1.000 152.70463 ? 248 ASP A C   1 
ATOM   1879 O O   . ASP A 1 254 ? -31.56394 48.73316 71.44457 1.000 144.44639 ? 248 ASP A O   1 
ATOM   1880 C CB  . ASP A 1 254 ? -28.44830 46.80961 71.39684 1.000 159.17845 ? 248 ASP A CB  1 
ATOM   1881 C CG  . ASP A 1 254 ? -27.38525 47.55110 72.19031 1.000 170.69823 ? 248 ASP A CG  1 
ATOM   1882 O OD1 . ASP A 1 254 ? -27.67656 47.96146 73.33351 1.000 167.84154 ? 248 ASP A OD1 1 
ATOM   1883 O OD2 . ASP A 1 254 ? -26.26125 47.72114 71.67344 1.000 173.14376 ? 248 ASP A OD2 1 
ATOM   1884 N N   . GLY A 1 255 ? -30.09852 48.23103 73.07374 1.000 152.46523 ? 249 GLY A N   1 
ATOM   1885 C CA  . GLY A 1 255 ? -31.00424 48.60892 74.14164 1.000 151.85641 ? 249 GLY A CA  1 
ATOM   1886 C C   . GLY A 1 255 ? -31.06508 50.09188 74.45014 1.000 144.08529 ? 249 GLY A C   1 
ATOM   1887 O O   . GLY A 1 255 ? -32.14200 50.69449 74.40727 1.000 132.50461 ? 249 GLY A O   1 
ATOM   1888 N N   . ASN A 1 256 ? -29.92167 50.69177 74.76325 1.000 140.55421 ? 250 ASN A N   1 
ATOM   1889 C CA  . ASN A 1 256 ? -29.87537 52.07011 75.22630 1.000 144.59554 ? 250 ASN A CA  1 
ATOM   1890 C C   . ASN A 1 256 ? -29.68710 53.04044 74.06352 1.000 123.86480 ? 250 ASN A C   1 
ATOM   1891 O O   . ASN A 1 256 ? -29.22630 52.67448 72.98011 1.000 103.20399 ? 250 ASN A O   1 
ATOM   1892 C CB  . ASN A 1 256 ? -28.75451 52.24826 76.24949 1.000 135.49380 ? 250 ASN A CB  1 
ATOM   1893 C CG  . ASN A 1 256 ? -28.97596 51.42062 77.49794 1.000 146.62611 ? 250 ASN A CG  1 
ATOM   1894 O OD1 . ASN A 1 256 ? -29.49616 51.91399 78.49852 1.000 153.87879 ? 250 ASN A OD1 1 
ATOM   1895 N ND2 . ASN A 1 256 ? -28.59236 50.14997 77.44213 1.000 138.15326 ? 250 ASN A ND2 1 
ATOM   1896 N N   . SER A 1 257 ? -30.05331 54.29524 74.30880 1.000 121.74689 ? 251 SER A N   1 
ATOM   1897 C CA  . SER A 1 257 ? -29.97544 55.34594 73.30594 1.000 99.96329  ? 251 SER A CA  1 
ATOM   1898 C C   . SER A 1 257 ? -28.62091 56.04541 73.35958 1.000 99.36803  ? 251 SER A C   1 
ATOM   1899 O O   . SER A 1 257 ? -27.90476 55.99624 74.36286 1.000 94.53714  ? 251 SER A O   1 
ATOM   1900 C CB  . SER A 1 257 ? -31.09812 56.36409 73.50426 1.000 88.91542  ? 251 SER A CB  1 
ATOM   1901 O OG  . SER A 1 257 ? -32.36747 55.74572 73.39195 1.000 114.62633 ? 251 SER A OG  1 
ATOM   1902 N N   . TYR A 1 258 ? -28.28132 56.71269 72.25754 1.000 85.07113  ? 252 TYR A N   1 
ATOM   1903 C CA  . TYR A 1 258 ? -26.97797 57.34416 72.08758 1.000 80.06520  ? 252 TYR A CA  1 
ATOM   1904 C C   . TYR A 1 258 ? -27.16498 58.74624 71.52742 1.000 90.17013  ? 252 TYR A C   1 
ATOM   1905 O O   . TYR A 1 258 ? -27.67915 58.91105 70.41581 1.000 88.47567  ? 252 TYR A O   1 
ATOM   1906 C CB  . TYR A 1 258 ? -26.08325 56.50945 71.16725 1.000 85.72463  ? 252 TYR A CB  1 
ATOM   1907 C CG  . TYR A 1 258 ? -24.70607 57.09429 70.95101 1.000 101.80468 ? 252 TYR A CG  1 
ATOM   1908 C CD1 . TYR A 1 258 ? -23.80988 57.21870 72.00464 1.000 98.65397  ? 252 TYR A CD1 1 
ATOM   1909 C CD2 . TYR A 1 258 ? -24.29699 57.51055 69.69078 1.000 86.05428  ? 252 TYR A CD2 1 
ATOM   1910 C CE1 . TYR A 1 258 ? -22.54832 57.74949 71.81118 1.000 88.85212  ? 252 TYR A CE1 1 
ATOM   1911 C CE2 . TYR A 1 258 ? -23.03562 58.04160 69.48715 1.000 88.92793  ? 252 TYR A CE2 1 
ATOM   1912 C CZ  . TYR A 1 258 ? -22.16612 58.15841 70.55125 1.000 93.36934  ? 252 TYR A CZ  1 
ATOM   1913 O OH  . TYR A 1 258 ? -20.91022 58.68611 70.35833 1.000 103.82536 ? 252 TYR A OH  1 
ATOM   1914 N N   . TYR A 1 259 ? -26.73653 59.74761 72.29313 1.000 82.00451  ? 253 TYR A N   1 
ATOM   1915 C CA  . TYR A 1 259 ? -26.84553 61.14651 71.90251 1.000 79.76088  ? 253 TYR A CA  1 
ATOM   1916 C C   . TYR A 1 259 ? -25.55948 61.58891 71.21287 1.000 71.77585  ? 253 TYR A C   1 
ATOM   1917 O O   . TYR A 1 259 ? -24.46235 61.39185 71.74524 1.000 80.39596  ? 253 TYR A O   1 
ATOM   1918 C CB  . TYR A 1 259 ? -27.13098 62.01773 73.12963 1.000 81.55905  ? 253 TYR A CB  1 
ATOM   1919 C CG  . TYR A 1 259 ? -27.38661 63.47823 72.82050 1.000 88.09269  ? 253 TYR A CG  1 
ATOM   1920 C CD1 . TYR A 1 259 ? -28.46112 63.86205 72.02917 1.000 83.42037  ? 253 TYR A CD1 1 
ATOM   1921 C CD2 . TYR A 1 259 ? -26.56334 64.47430 73.33375 1.000 92.24993  ? 253 TYR A CD2 1 
ATOM   1922 C CE1 . TYR A 1 259 ? -28.70150 65.19563 71.74407 1.000 83.17342  ? 253 TYR A CE1 1 
ATOM   1923 C CE2 . TYR A 1 259 ? -26.79755 65.81214 73.05538 1.000 86.10566  ? 253 TYR A CE2 1 
ATOM   1924 C CZ  . TYR A 1 259 ? -27.86761 66.16559 72.26033 1.000 85.33072  ? 253 TYR A CZ  1 
ATOM   1925 O OH  . TYR A 1 259 ? -28.10416 67.49250 71.98108 1.000 89.79205  ? 253 TYR A OH  1 
ATOM   1926 N N   . TRP A 1 260 ? -25.69982 62.18213 70.02623 1.000 78.71189  ? 254 TRP A N   1 
ATOM   1927 C CA  . TRP A 1 260 ? -24.56529 62.60783 69.21365 1.000 69.23510  ? 254 TRP A CA  1 
ATOM   1928 C C   . TRP A 1 260 ? -25.01165 63.71542 68.26601 1.000 69.49648  ? 254 TRP A C   1 
ATOM   1929 O O   . TRP A 1 260 ? -25.47181 63.43487 67.15165 1.000 82.84756  ? 254 TRP A O   1 
ATOM   1930 C CB  . TRP A 1 260 ? -23.99169 61.42240 68.43449 1.000 68.82668  ? 254 TRP A CB  1 
ATOM   1931 C CG  . TRP A 1 260 ? -22.65635 61.67654 67.79730 1.000 76.10134  ? 254 TRP A CG  1 
ATOM   1932 C CD1 . TRP A 1 260 ? -21.43305 61.58247 68.39457 1.000 76.59362  ? 254 TRP A CD1 1 
ATOM   1933 C CD2 . TRP A 1 260 ? -22.40882 62.04609 66.43442 1.000 79.22001  ? 254 TRP A CD2 1 
ATOM   1934 N NE1 . TRP A 1 260 ? -20.44074 61.87819 67.49180 1.000 76.34277  ? 254 TRP A NE1 1 
ATOM   1935 C CE2 . TRP A 1 260 ? -21.01353 62.16518 66.28102 1.000 75.60120  ? 254 TRP A CE2 1 
ATOM   1936 C CE3 . TRP A 1 260 ? -23.23158 62.29327 65.33126 1.000 80.83908  ? 254 TRP A CE3 1 
ATOM   1937 C CZ2 . TRP A 1 260 ? -20.42374 62.51791 65.07000 1.000 69.34036  ? 254 TRP A CZ2 1 
ATOM   1938 C CZ3 . TRP A 1 260 ? -22.64422 62.64024 64.12964 1.000 81.52811  ? 254 TRP A CZ3 1 
ATOM   1939 C CH2 . TRP A 1 260 ? -21.25434 62.75145 64.00865 1.000 70.07745  ? 254 TRP A CH2 1 
ATOM   1940 N N   . PRO A 1 261 ? -24.90076 64.97986 68.66994 1.000 70.81975  ? 255 PRO A N   1 
ATOM   1941 C CA  . PRO A 1 261 ? -25.47886 66.06141 67.86517 1.000 75.22867  ? 255 PRO A CA  1 
ATOM   1942 C C   . PRO A 1 261 ? -24.46688 66.78129 66.98968 1.000 72.73825  ? 255 PRO A C   1 
ATOM   1943 O O   . PRO A 1 261 ? -24.71226 67.92035 66.58146 1.000 81.54134  ? 255 PRO A O   1 
ATOM   1944 C CB  . PRO A 1 261 ? -26.04041 67.00055 68.93488 1.000 80.01132  ? 255 PRO A CB  1 
ATOM   1945 C CG  . PRO A 1 261 ? -25.02594 66.88387 70.04546 1.000 72.49058  ? 255 PRO A CG  1 
ATOM   1946 C CD  . PRO A 1 261 ? -24.47471 65.46194 69.99574 1.000 66.92219  ? 255 PRO A CD  1 
ATOM   1947 N N   . ASP A 1 262 ? -23.33622 66.13494 66.69298 1.000 76.43681  ? 256 ASP A N   1 
ATOM   1948 C CA  . ASP A 1 262 ? -22.24415 66.82163 66.00536 1.000 64.91222  ? 256 ASP A CA  1 
ATOM   1949 C C   . ASP A 1 262 ? -22.68695 67.35675 64.64795 1.000 75.70597  ? 256 ASP A C   1 
ATOM   1950 O O   . ASP A 1 262 ? -22.47382 68.53372 64.33312 1.000 82.42863  ? 256 ASP A O   1 
ATOM   1951 C CB  . ASP A 1 262 ? -21.04635 65.88346 65.85288 1.000 77.57677  ? 256 ASP A CB  1 
ATOM   1952 C CG  . ASP A 1 262 ? -20.47866 65.44085 67.18772 1.000 78.53511  ? 256 ASP A CG  1 
ATOM   1953 O OD1 . ASP A 1 262 ? -21.12968 65.69057 68.22386 1.000 81.08334  ? 256 ASP A OD1 1 
ATOM   1954 O OD2 . ASP A 1 262 ? -19.37863 64.84829 67.20136 1.000 91.37347  ? 256 ASP A OD2 1 
ATOM   1955 N N   . ILE A 1 263 ? -23.30788 66.50649 63.82817 1.000 68.89979  ? 257 ILE A N   1 
ATOM   1956 C CA  . ILE A 1 263 ? -23.78783 66.96135 62.52718 1.000 64.96300  ? 257 ILE A CA  1 
ATOM   1957 C C   . ILE A 1 263 ? -25.04151 67.81073 62.68935 1.000 73.21766  ? 257 ILE A C   1 
ATOM   1958 O O   . ILE A 1 263 ? -25.20286 68.83908 62.01943 1.000 78.42905  ? 257 ILE A O   1 
ATOM   1959 C CB  . ILE A 1 263 ? -24.03121 65.75845 61.59915 1.000 66.64381  ? 257 ILE A CB  1 
ATOM   1960 C CG1 . ILE A 1 263 ? -22.73359 64.97554 61.39658 1.000 72.48111  ? 257 ILE A CG1 1 
ATOM   1961 C CG2 . ILE A 1 263 ? -24.59171 66.21588 60.25959 1.000 70.56361  ? 257 ILE A CG2 1 
ATOM   1962 C CD1 . ILE A 1 263 ? -22.88420 63.77087 60.49898 1.000 70.04440  ? 257 ILE A CD1 1 
ATOM   1963 N N   . TYR A 1 264 ? -25.94511 67.39431 63.58148 1.000 59.99341  ? 258 TYR A N   1 
ATOM   1964 C CA  . TYR A 1 264 ? -27.16303 68.15590 63.84396 1.000 69.64537  ? 258 TYR A CA  1 
ATOM   1965 C C   . TYR A 1 264 ? -26.84892 69.60189 64.21458 1.000 78.45027  ? 258 TYR A C   1 
ATOM   1966 O O   . TYR A 1 264 ? -27.51716 70.53083 63.74611 1.000 74.91335  ? 258 TYR A O   1 
ATOM   1967 C CB  . TYR A 1 264 ? -27.95796 67.46877 64.95668 1.000 77.15416  ? 258 TYR A CB  1 
ATOM   1968 C CG  . TYR A 1 264 ? -29.30080 68.08620 65.28645 1.000 74.77381  ? 258 TYR A CG  1 
ATOM   1969 C CD1 . TYR A 1 264 ? -30.42680 67.78589 64.53453 1.000 75.11889  ? 258 TYR A CD1 1 
ATOM   1970 C CD2 . TYR A 1 264 ? -29.44781 68.94308 66.37011 1.000 88.38085  ? 258 TYR A CD2 1 
ATOM   1971 C CE1 . TYR A 1 264 ? -31.65851 68.33470 64.83702 1.000 85.66789  ? 258 TYR A CE1 1 
ATOM   1972 C CE2 . TYR A 1 264 ? -30.67683 69.49512 66.68394 1.000 83.18358  ? 258 TYR A CE2 1 
ATOM   1973 C CZ  . TYR A 1 264 ? -31.77839 69.18860 65.91162 1.000 86.05371  ? 258 TYR A CZ  1 
ATOM   1974 O OH  . TYR A 1 264 ? -33.00558 69.73332 66.21497 1.000 97.23064  ? 258 TYR A OH  1 
ATOM   1975 N N   . ASN A 1 265 ? -25.82061 69.81388 65.04125 1.000 71.08798  ? 259 ASN A N   1 
ATOM   1976 C CA  . ASN A 1 265 ? -25.46115 71.17244 65.43879 1.000 69.66920  ? 259 ASN A CA  1 
ATOM   1977 C C   . ASN A 1 265 ? -24.85034 71.95398 64.28360 1.000 69.80578  ? 259 ASN A C   1 
ATOM   1978 O O   . ASN A 1 265 ? -25.15837 73.13669 64.10096 1.000 76.16875  ? 259 ASN A O   1 
ATOM   1979 C CB  . ASN A 1 265 ? -24.49010 71.14472 66.61501 1.000 62.48226  ? 259 ASN A CB  1 
ATOM   1980 C CG  . ASN A 1 265 ? -25.15049 70.73286 67.90563 1.000 80.86271  ? 259 ASN A CG  1 
ATOM   1981 O OD1 . ASN A 1 265 ? -26.37224 70.79762 68.04702 1.000 83.70428  ? 259 ASN A OD1 1 
ATOM   1982 N ND2 . ASN A 1 265 ? -24.34059 70.31292 68.86485 1.000 65.25302  ? 259 ASN A ND2 1 
ATOM   1983 N N   . SER A 1 266 ? -23.96709 71.32005 63.50667 1.000 71.81969  ? 260 SER A N   1 
ATOM   1984 C CA  . SER A 1 266 ? -23.30937 72.02433 62.40975 1.000 68.79437  ? 260 SER A CA  1 
ATOM   1985 C C   . SER A 1 266 ? -24.31156 72.52902 61.38232 1.000 78.38176  ? 260 SER A C   1 
ATOM   1986 O O   . SER A 1 266 ? -24.06087 73.53854 60.71320 1.000 89.92465  ? 260 SER A O   1 
ATOM   1987 C CB  . SER A 1 266 ? -22.27972 71.11395 61.74362 1.000 73.17560  ? 260 SER A CB  1 
ATOM   1988 O OG  . SER A 1 266 ? -21.16104 70.92313 62.58917 1.000 89.49942  ? 260 SER A OG  1 
ATOM   1989 N N   . ILE A 1 267 ? -25.44800 71.84669 61.24566 1.000 76.70823  ? 261 ILE A N   1 
ATOM   1990 C CA  . ILE A 1 267 ? -26.48366 72.30126 60.32506 1.000 67.64567  ? 261 ILE A CA  1 
ATOM   1991 C C   . ILE A 1 267 ? -27.22403 73.49757 60.91040 1.000 75.35697  ? 261 ILE A C   1 
ATOM   1992 O O   . ILE A 1 267 ? -27.35105 74.54673 60.26813 1.000 84.28363  ? 261 ILE A O   1 
ATOM   1993 C CB  . ILE A 1 267 ? -27.44220 71.14369 59.99645 1.000 76.59091  ? 261 ILE A CB  1 
ATOM   1994 C CG1 . ILE A 1 267 ? -26.67788 70.00866 59.31631 1.000 70.35963  ? 261 ILE A CG1 1 
ATOM   1995 C CG2 . ILE A 1 267 ? -28.58377 71.62013 59.11853 1.000 66.67739  ? 261 ILE A CG2 1 
ATOM   1996 C CD1 . ILE A 1 267 ? -27.46017 68.73221 59.22408 1.000 58.20730  ? 261 ILE A CD1 1 
ATOM   1997 N N   . ILE A 1 268 ? -27.71252 73.36056 62.14536 1.000 70.79505  ? 262 ILE A N   1 
ATOM   1998 C CA  . ILE A 1 268 ? -28.45800 74.44364 62.78246 1.000 68.42827  ? 262 ILE A CA  1 
ATOM   1999 C C   . ILE A 1 268 ? -27.57931 75.67717 62.95100 1.000 77.33033  ? 262 ILE A C   1 
ATOM   2000 O O   . ILE A 1 268 ? -28.02504 76.81062 62.72769 1.000 82.36149  ? 262 ILE A O   1 
ATOM   2001 C CB  . ILE A 1 268 ? -29.03641 73.96591 64.12653 1.000 70.05454  ? 262 ILE A CB  1 
ATOM   2002 C CG1 . ILE A 1 268 ? -30.15490 72.95312 63.88630 1.000 81.10262  ? 262 ILE A CG1 1 
ATOM   2003 C CG2 . ILE A 1 268 ? -29.54504 75.13736 64.94530 1.000 84.35451  ? 262 ILE A CG2 1 
ATOM   2004 C CD1 . ILE A 1 268 ? -30.89521 72.56447 65.13752 1.000 108.29458 ? 262 ILE A CD1 1 
ATOM   2005 N N   . GLU A 1 269 ? -26.31851 75.47732 63.34538 1.000 80.00730  ? 263 GLU A N   1 
ATOM   2006 C CA  . GLU A 1 269 ? -25.38505 76.59359 63.45930 1.000 81.21509  ? 263 GLU A CA  1 
ATOM   2007 C C   . GLU A 1 269 ? -25.27302 77.35567 62.14459 1.000 81.91766  ? 263 GLU A C   1 
ATOM   2008 O O   . GLU A 1 269 ? -25.21428 78.59087 62.13435 1.000 79.86109  ? 263 GLU A O   1 
ATOM   2009 C CB  . GLU A 1 269 ? -24.01348 76.07999 63.89955 1.000 85.77530  ? 263 GLU A CB  1 
ATOM   2010 C CG  . GLU A 1 269 ? -22.96464 77.16079 64.09179 1.000 105.45296 ? 263 GLU A CG  1 
ATOM   2011 C CD  . GLU A 1 269 ? -21.58071 76.58976 64.33222 1.000 106.71735 ? 263 GLU A CD  1 
ATOM   2012 O OE1 . GLU A 1 269 ? -21.31626 75.45669 63.87753 1.000 96.22695  ? 263 GLU A OE1 1 
ATOM   2013 O OE2 . GLU A 1 269 ? -20.75782 77.27243 64.97744 1.000 127.76288 ? 263 GLU A OE2 1 
ATOM   2014 N N   . ALA A 1 270 ? -25.25585 76.63310 61.02219 1.000 67.66942  ? 264 ALA A N   1 
ATOM   2015 C CA  . ALA A 1 270 ? -25.17537 77.28658 59.71997 1.000 74.34084  ? 264 ALA A CA  1 
ATOM   2016 C C   . ALA A 1 270 ? -26.41103 78.13454 59.44668 1.000 85.13113  ? 264 ALA A C   1 
ATOM   2017 O O   . ALA A 1 270 ? -26.31374 79.21511 58.85302 1.000 91.09889  ? 264 ALA A O   1 
ATOM   2018 C CB  . ALA A 1 270 ? -24.99245 76.24115 58.62103 1.000 67.52038  ? 264 ALA A CB  1 
ATOM   2019 N N   . ALA A 1 271 ? -27.58267 77.66507 59.87706 1.000 82.75360  ? 265 ALA A N   1 
ATOM   2020 C CA  . ALA A 1 271 ? -28.81876 78.39198 59.60996 1.000 75.45119  ? 265 ALA A CA  1 
ATOM   2021 C C   . ALA A 1 271 ? -28.97284 79.59735 60.53004 1.000 81.54821  ? 265 ALA A C   1 
ATOM   2022 O O   . ALA A 1 271 ? -29.25299 80.70789 60.06657 1.000 93.96545  ? 265 ALA A O   1 
ATOM   2023 C CB  . ALA A 1 271 ? -30.01963 77.45625 59.75152 1.000 70.80892  ? 265 ALA A CB  1 
ATOM   2024 N N   . ILE A 1 272 ? -28.78998 79.40031 61.83537 1.000 79.56442  ? 266 ILE A N   1 
ATOM   2025 C CA  . ILE A 1 272 ? -29.04957 80.47317 62.79039 1.000 82.91308  ? 266 ILE A CA  1 
ATOM   2026 C C   . ILE A 1 272 ? -27.91378 81.48829 62.79441 1.000 82.05499  ? 266 ILE A C   1 
ATOM   2027 O O   . ILE A 1 272 ? -28.14283 82.69813 62.68453 1.000 96.76429  ? 266 ILE A O   1 
ATOM   2028 C CB  . ILE A 1 272 ? -29.28638 79.89390 64.19670 1.000 88.38789  ? 266 ILE A CB  1 
ATOM   2029 C CG1 . ILE A 1 272 ? -30.44238 78.89297 64.17673 1.000 81.13785  ? 266 ILE A CG1 1 
ATOM   2030 C CG2 . ILE A 1 272 ? -29.56425 81.01280 65.18678 1.000 73.53434  ? 266 ILE A CG2 1 
ATOM   2031 C CD1 . ILE A 1 272 ? -30.85281 78.40768 65.55119 1.000 74.67886  ? 266 ILE A CD1 1 
ATOM   2032 N N   . ASN A 1 273 ? -26.67300 81.01690 62.92560 1.000 83.80182  ? 267 ASN A N   1 
ATOM   2033 C CA  . ASN A 1 273 ? -25.55075 81.93340 63.09049 1.000 79.29683  ? 267 ASN A CA  1 
ATOM   2034 C C   . ASN A 1 273 ? -25.11919 82.57776 61.78081 1.000 93.23141  ? 267 ASN A C   1 
ATOM   2035 O O   . ASN A 1 273 ? -24.64912 83.72091 61.78843 1.000 99.76266  ? 267 ASN A O   1 
ATOM   2036 C CB  . ASN A 1 273 ? -24.36357 81.20675 63.72183 1.000 79.23715  ? 267 ASN A CB  1 
ATOM   2037 C CG  . ASN A 1 273 ? -24.63686 80.78537 65.14520 1.000 77.20846  ? 267 ASN A CG  1 
ATOM   2038 O OD1 . ASN A 1 273 ? -24.21389 79.71838 65.58552 1.000 93.72334  ? 267 ASN A OD1 1 
ATOM   2039 N ND2 . ASN A 1 273 ? -25.36029 81.62151 65.87281 1.000 83.89837  ? 267 ASN A ND2 1 
ATOM   2040 N N   . ARG A 1 274 ? -25.26275 81.87781 60.65637 1.000 81.53768  ? 268 ARG A N   1 
ATOM   2041 C CA  . ARG A 1 274 ? -24.74688 82.36845 59.38720 1.000 79.43176  ? 268 ARG A CA  1 
ATOM   2042 C C   . ARG A 1 274 ? -25.81405 82.57579 58.32158 1.000 85.45567  ? 268 ARG A C   1 
ATOM   2043 O O   . ARG A 1 274 ? -25.47304 82.97398 57.20195 1.000 99.50580  ? 268 ARG A O   1 
ATOM   2044 C CB  . ARG A 1 274 ? -23.66871 81.41574 58.85343 1.000 76.72304  ? 268 ARG A CB  1 
ATOM   2045 C CG  . ARG A 1 274 ? -22.58095 81.10096 59.86898 1.000 73.34886  ? 268 ARG A CG  1 
ATOM   2046 C CD  . ARG A 1 274 ? -21.34174 80.52905 59.20478 1.000 85.66725  ? 268 ARG A CD  1 
ATOM   2047 N NE  . ARG A 1 274 ? -21.63734 79.34911 58.40201 1.000 79.86725  ? 268 ARG A NE  1 
ATOM   2048 C CZ  . ARG A 1 274 ? -21.61721 78.10579 58.86104 1.000 76.71577  ? 268 ARG A CZ  1 
ATOM   2049 N NH1 . ARG A 1 274 ? -21.33370 77.84007 60.12577 1.000 97.51921  ? 268 ARG A NH1 1 
ATOM   2050 N NH2 . ARG A 1 274 ? -21.88477 77.10360 58.02916 1.000 88.84247  ? 268 ARG A NH2 1 
ATOM   2051 N N   . GLY A 1 275 ? -27.08467 82.32371 58.62637 1.000 86.76958  ? 269 GLY A N   1 
ATOM   2052 C CA  . GLY A 1 275 ? -28.14376 82.58622 57.66477 1.000 73.89799  ? 269 GLY A CA  1 
ATOM   2053 C C   . GLY A 1 275 ? -28.09087 81.72427 56.42398 1.000 88.11345  ? 269 GLY A C   1 
ATOM   2054 O O   . GLY A 1 275 ? -28.55857 82.14687 55.36097 1.000 90.80876  ? 269 GLY A O   1 
ATOM   2055 N N   . VAL A 1 276 ? -27.52715 80.52119 56.52827 1.000 87.85640  ? 270 VAL A N   1 
ATOM   2056 C CA  . VAL A 1 276 ? -27.46277 79.62042 55.38595 1.000 80.65522  ? 270 VAL A CA  1 
ATOM   2057 C C   . VAL A 1 276 ? -28.84811 79.06000 55.09729 1.000 77.72705  ? 270 VAL A C   1 
ATOM   2058 O O   . VAL A 1 276 ? -29.58332 78.66466 56.01233 1.000 88.39457  ? 270 VAL A O   1 
ATOM   2059 C CB  . VAL A 1 276 ? -26.44908 78.49473 55.65427 1.000 79.81521  ? 270 VAL A CB  1 
ATOM   2060 C CG1 . VAL A 1 276 ? -26.45788 77.47621 54.52268 1.000 81.55450  ? 270 VAL A CG1 1 
ATOM   2061 C CG2 . VAL A 1 276 ? -25.05586 79.07575 55.84346 1.000 78.31397  ? 270 VAL A CG2 1 
ATOM   2062 N N   . LYS A 1 277 ? -29.21725 79.03111 53.81891 1.000 87.77314  ? 271 LYS A N   1 
ATOM   2063 C CA  . LYS A 1 277 ? -30.47257 78.41643 53.40694 1.000 82.10691  ? 271 LYS A CA  1 
ATOM   2064 C C   . LYS A 1 277 ? -30.29376 76.90455 53.37655 1.000 78.63010  ? 271 LYS A C   1 
ATOM   2065 O O   . LYS A 1 277 ? -29.40855 76.39121 52.68427 1.000 85.15152  ? 271 LYS A O   1 
ATOM   2066 C CB  . LYS A 1 277 ? -30.91466 78.94128 52.04231 1.000 85.36331  ? 271 LYS A CB  1 
ATOM   2067 C CG  . LYS A 1 277 ? -32.26509 78.40150 51.58745 1.000 105.47132 ? 271 LYS A CG  1 
ATOM   2068 C CD  . LYS A 1 277 ? -32.76737 79.10368 50.33517 1.000 119.86066 ? 271 LYS A CD  1 
ATOM   2069 C CE  . LYS A 1 277 ? -34.13192 78.57210 49.91960 1.000 124.56019 ? 271 LYS A CE  1 
ATOM   2070 N NZ  . LYS A 1 277 ? -34.69614 79.31338 48.75851 1.000 115.60212 ? 271 LYS A NZ  1 
ATOM   2071 N N   . ILE A 1 278 ? -31.12627 76.19088 54.12771 1.000 86.16311  ? 272 ILE A N   1 
ATOM   2072 C CA  . ILE A 1 278 ? -30.97060 74.75469 54.31097 1.000 81.32743  ? 272 ILE A CA  1 
ATOM   2073 C C   . ILE A 1 278 ? -32.27293 74.06124 53.94408 1.000 83.62274  ? 272 ILE A C   1 
ATOM   2074 O O   . ILE A 1 278 ? -33.35479 74.50456 54.34578 1.000 85.23770  ? 272 ILE A O   1 
ATOM   2075 C CB  . ILE A 1 278 ? -30.55781 74.41143 55.75359 1.000 69.39097  ? 272 ILE A CB  1 
ATOM   2076 C CG1 . ILE A 1 278 ? -29.25387 75.12708 56.10169 1.000 75.81527  ? 272 ILE A CG1 1 
ATOM   2077 C CG2 . ILE A 1 278 ? -30.39962 72.90967 55.92390 1.000 71.22532  ? 272 ILE A CG2 1 
ATOM   2078 C CD1 . ILE A 1 278 ? -28.74619 74.81624 57.47285 1.000 76.43747  ? 272 ILE A CD1 1 
ATOM   2079 N N   . ARG A 1 279 ? -32.16544 72.97742 53.17865 1.000 76.33502  ? 273 ARG A N   1 
ATOM   2080 C CA  . ARG A 1 279 ? -33.30366 72.13954 52.82493 1.000 79.74306  ? 273 ARG A CA  1 
ATOM   2081 C C   . ARG A 1 279 ? -32.97711 70.70232 53.19689 1.000 81.38890  ? 273 ARG A C   1 
ATOM   2082 O O   . ARG A 1 279 ? -31.98549 70.14341 52.71583 1.000 71.64322  ? 273 ARG A O   1 
ATOM   2083 C CB  . ARG A 1 279 ? -33.63368 72.25563 51.33563 1.000 75.82492  ? 273 ARG A CB  1 
ATOM   2084 C CG  . ARG A 1 279 ? -34.06731 73.64898 50.92303 1.000 84.33061  ? 273 ARG A CG  1 
ATOM   2085 C CD  . ARG A 1 279 ? -34.40841 73.71183 49.44731 1.000 75.85982  ? 273 ARG A CD  1 
ATOM   2086 N NE  . ARG A 1 279 ? -33.25524 73.39845 48.61362 1.000 79.65302  ? 273 ARG A NE  1 
ATOM   2087 C CZ  . ARG A 1 279 ? -33.27088 73.39446 47.28798 1.000 85.47711  ? 273 ARG A CZ  1 
ATOM   2088 N NH1 . ARG A 1 279 ? -34.36764 73.68971 46.60877 1.000 84.78737  ? 273 ARG A NH1 1 
ATOM   2089 N NH2 . ARG A 1 279 ? -32.15886 73.08524 46.62702 1.000 82.07445  ? 273 ARG A NH2 1 
ATOM   2090 N N   . LEU A 1 280 ? -33.80472 70.11107 54.05232 1.000 72.25109  ? 274 LEU A N   1 
ATOM   2091 C CA  . LEU A 1 280 ? -33.60673 68.75180 54.53689 1.000 72.39277  ? 274 LEU A CA  1 
ATOM   2092 C C   . LEU A 1 280 ? -34.72379 67.86573 54.00257 1.000 85.35004  ? 274 LEU A C   1 
ATOM   2093 O O   . LEU A 1 280 ? -35.90555 68.13679 54.24336 1.000 81.86311  ? 274 LEU A O   1 
ATOM   2094 C CB  . LEU A 1 280 ? -33.57526 68.71936 56.06466 1.000 64.51526  ? 274 LEU A CB  1 
ATOM   2095 C CG  . LEU A 1 280 ? -32.54452 69.63493 56.72856 1.000 63.51713  ? 274 LEU A CG  1 
ATOM   2096 C CD1 . LEU A 1 280 ? -32.67058 69.57728 58.24254 1.000 58.49818  ? 274 LEU A CD1 1 
ATOM   2097 C CD2 . LEU A 1 280 ? -31.13272 69.27105 56.29085 1.000 61.11269  ? 274 LEU A CD2 1 
ATOM   2098 N N   . LEU A 1 281 ? -34.34816 66.81650 53.27605 1.000 72.00260  ? 275 LEU A N   1 
ATOM   2099 C CA  . LEU A 1 281 ? -35.28596 65.82359 52.75600 1.000 69.30924  ? 275 LEU A CA  1 
ATOM   2100 C C   . LEU A 1 281 ? -34.97562 64.51008 53.46539 1.000 71.39708  ? 275 LEU A C   1 
ATOM   2101 O O   . LEU A 1 281 ? -34.03730 63.79999 53.09133 1.000 75.65319  ? 275 LEU A O   1 
ATOM   2102 C CB  . LEU A 1 281 ? -35.16871 65.69583 51.24022 1.000 68.68236  ? 275 LEU A CB  1 
ATOM   2103 C CG  . LEU A 1 281 ? -36.08061 64.67518 50.55841 1.000 70.27745  ? 275 LEU A CG  1 
ATOM   2104 C CD1 . LEU A 1 281 ? -37.53885 64.94502 50.89227 1.000 62.25098  ? 275 LEU A CD1 1 
ATOM   2105 C CD2 . LEU A 1 281 ? -35.86271 64.69484 49.05498 1.000 64.80663  ? 275 LEU A CD2 1 
ATOM   2106 N N   . VAL A 1 282 ? -35.75923 64.19046 54.49268 1.000 71.13156  ? 276 VAL A N   1 
ATOM   2107 C CA  . VAL A 1 282 ? -35.45197 63.09495 55.39938 1.000 61.61423  ? 276 VAL A CA  1 
ATOM   2108 C C   . VAL A 1 282 ? -36.61048 62.10481 55.41062 1.000 67.69443  ? 276 VAL A C   1 
ATOM   2109 O O   . VAL A 1 282 ? -37.66787 62.33780 54.82624 1.000 77.41132  ? 276 VAL A O   1 
ATOM   2110 C CB  . VAL A 1 282 ? -35.15625 63.59254 56.82449 1.000 65.57531  ? 276 VAL A CB  1 
ATOM   2111 C CG1 . VAL A 1 282 ? -34.03506 64.61584 56.80279 1.000 63.62313  ? 276 VAL A CG1 1 
ATOM   2112 C CG2 . VAL A 1 282 ? -36.41283 64.18336 57.43930 1.000 64.24505  ? 276 VAL A CG2 1 
ATOM   2113 N N   . GLY A 1 283 ? -36.39177 60.98652 56.09526 1.000 67.83579  ? 277 GLY A N   1 
ATOM   2114 C CA  . GLY A 1 283 ? -37.42285 59.98170 56.23332 1.000 55.53575  ? 277 GLY A CA  1 
ATOM   2115 C C   . GLY A 1 283 ? -38.55410 60.44504 57.13005 1.000 75.13153  ? 277 GLY A C   1 
ATOM   2116 O O   . GLY A 1 283 ? -38.45836 61.43136 57.86134 1.000 94.00252  ? 277 GLY A O   1 
ATOM   2117 N N   . ASN A 1 284 ? -39.65541 59.70372 57.06709 1.000 72.57983  ? 278 ASN A N   1 
ATOM   2118 C CA  . ASN A 1 284 ? -40.85162 60.05448 57.81848 1.000 89.04775  ? 278 ASN A CA  1 
ATOM   2119 C C   . ASN A 1 284 ? -40.67662 59.72977 59.29750 1.000 104.72437 ? 278 ASN A C   1 
ATOM   2120 O O   . ASN A 1 284 ? -40.18598 58.65617 59.65900 1.000 101.04790 ? 278 ASN A O   1 
ATOM   2121 C CB  . ASN A 1 284 ? -42.06399 59.30947 57.25779 1.000 92.43257  ? 278 ASN A CB  1 
ATOM   2122 C CG  . ASN A 1 284 ? -43.37243 59.78616 57.85709 1.000 113.48539 ? 278 ASN A CG  1 
ATOM   2123 O OD1 . ASN A 1 284 ? -43.48917 60.93196 58.29133 1.000 103.39467 ? 278 ASN A OD1 1 
ATOM   2124 N ND2 . ASN A 1 284 ? -44.36732 58.90640 57.88118 1.000 131.45453 ? 278 ASN A ND2 1 
ATOM   2125 N N   . TRP A 1 285 ? -41.08265 60.66714 60.15288 1.000 109.72091 ? 279 TRP A N   1 
ATOM   2126 C CA  . TRP A 1 285 ? -41.01130 60.45662 61.59129 1.000 108.74366 ? 279 TRP A CA  1 
ATOM   2127 C C   . TRP A 1 285 ? -42.10181 59.48683 62.04194 1.000 129.10661 ? 279 TRP A C   1 
ATOM   2128 O O   . TRP A 1 285 ? -43.13335 59.31615 61.38580 1.000 137.52593 ? 279 TRP A O   1 
ATOM   2129 C CB  . TRP A 1 285 ? -41.15251 61.78178 62.34431 1.000 102.75523 ? 279 TRP A CB  1 
ATOM   2130 C CG  . TRP A 1 285 ? -40.46622 62.94281 61.68340 1.000 123.51971 ? 279 TRP A CG  1 
ATOM   2131 C CD1 . TRP A 1 285 ? -40.96885 63.72647 60.68638 1.000 137.08352 ? 279 TRP A CD1 1 
ATOM   2132 C CD2 . TRP A 1 285 ? -39.16082 63.46295 61.98095 1.000 143.72233 ? 279 TRP A CD2 1 
ATOM   2133 N NE1 . TRP A 1 285 ? -40.05773 64.69317 60.33736 1.000 148.51633 ? 279 TRP A NE1 1 
ATOM   2134 C CE2 . TRP A 1 285 ? -38.93979 64.55410 61.11657 1.000 133.86771 ? 279 TRP A CE2 1 
ATOM   2135 C CE3 . TRP A 1 285 ? -38.15683 63.10832 62.88701 1.000 147.33979 ? 279 TRP A CE3 1 
ATOM   2136 C CZ2 . TRP A 1 285 ? -37.75813 65.29524 61.13380 1.000 112.83418 ? 279 TRP A CZ2 1 
ATOM   2137 C CZ3 . TRP A 1 285 ? -36.98398 63.84742 62.90383 1.000 139.87760 ? 279 TRP A CZ3 1 
ATOM   2138 C CH2 . TRP A 1 285 ? -36.79521 64.92672 62.03234 1.000 127.34875 ? 279 TRP A CH2 1 
ATOM   2139 N N   . ASP A 1 286 ? -41.86479 58.85053 63.18461 1.000 142.95512 ? 280 ASP A N   1 
ATOM   2140 C CA  . ASP A 1 286 ? -42.78050 57.86140 63.72897 1.000 173.35610 ? 280 ASP A CA  1 
ATOM   2141 C C   . ASP A 1 286 ? -43.18232 58.24707 65.14746 1.000 170.34217 ? 280 ASP A C   1 
ATOM   2142 O O   . ASP A 1 286 ? -42.47784 58.99007 65.83663 1.000 176.39520 ? 280 ASP A O   1 
ATOM   2143 C CB  . ASP A 1 286 ? -42.15099 56.46097 63.71648 1.000 178.34014 ? 280 ASP A CB  1 
ATOM   2144 C CG  . ASP A 1 286 ? -43.17273 55.36075 63.91678 1.000 180.08676 ? 280 ASP A CG  1 
ATOM   2145 O OD1 . ASP A 1 286 ? -44.05484 55.20261 63.04744 1.000 174.95948 ? 280 ASP A OD1 1 
ATOM   2146 O OD2 . ASP A 1 286 ? -43.09246 54.65206 64.94049 1.000 179.53227 ? 280 ASP A OD2 1 
ATOM   2147 N N   . LYS A 1 287 ? -44.33432 57.73089 65.57843 1.000 163.76148 ? 281 LYS A N   1 
ATOM   2148 C CA  . LYS A 1 287 ? -44.86046 58.03590 66.90249 1.000 172.41339 ? 281 LYS A CA  1 
ATOM   2149 C C   . LYS A 1 287 ? -44.38055 57.07024 67.97788 1.000 189.29011 ? 281 LYS A C   1 
ATOM   2150 O O   . LYS A 1 287 ? -44.39168 57.43231 69.16028 1.000 172.58231 ? 281 LYS A O   1 
ATOM   2151 C CB  . LYS A 1 287 ? -46.39218 58.04553 66.87211 1.000 165.14897 ? 281 LYS A CB  1 
ATOM   2152 C CG  . LYS A 1 287 ? -46.97021 58.97395 65.81976 1.000 160.18960 ? 281 LYS A CG  1 
ATOM   2153 C CD  . LYS A 1 287 ? -46.40327 60.37669 65.95926 1.000 140.23379 ? 281 LYS A CD  1 
ATOM   2154 C CE  . LYS A 1 287 ? -46.68980 61.20690 64.72145 1.000 138.15137 ? 281 LYS A CE  1 
ATOM   2155 N NZ  . LYS A 1 287 ? -46.03749 60.62832 63.51410 1.000 123.07513 ? 281 LYS A NZ  1 
ATOM   2156 N N   . ASN A 1 288 ? -43.96443 55.85562 67.60270 1.000 204.32199 ? 282 ASN A N   1 
ATOM   2157 C CA  . ASN A 1 288 ? -43.40046 54.93342 68.58470 1.000 190.33424 ? 282 ASN A CA  1 
ATOM   2158 C C   . ASN A 1 288 ? -42.12335 55.49205 69.19651 1.000 183.91773 ? 282 ASN A C   1 
ATOM   2159 O O   . ASN A 1 288 ? -41.77737 55.15500 70.33479 1.000 171.98830 ? 282 ASN A O   1 
ATOM   2160 C CB  . ASN A 1 288 ? -43.13100 53.57191 67.94071 1.000 158.70673 ? 282 ASN A CB  1 
ATOM   2161 C CG  . ASN A 1 288 ? -44.38535 52.93677 67.36876 1.000 159.32261 ? 282 ASN A CG  1 
ATOM   2162 O OD1 . ASN A 1 288 ? -45.48458 53.12837 67.88830 1.000 159.92022 ? 282 ASN A OD1 1 
ATOM   2163 N ND2 . ASN A 1 288 ? -44.22529 52.17464 66.29228 1.000 156.51199 ? 282 ASN A ND2 1 
ATOM   2164 N N   . ASP A 1 289 ? -41.41358 56.33817 68.45903 1.000 177.74646 ? 283 ASP A N   1 
ATOM   2165 C CA  . ASP A 1 289 ? -40.25351 57.06712 68.95941 1.000 156.96620 ? 283 ASP A CA  1 
ATOM   2166 C C   . ASP A 1 289 ? -40.62858 58.54662 68.94239 1.000 154.98250 ? 283 ASP A C   1 
ATOM   2167 O O   . ASP A 1 289 ? -40.39055 59.25177 67.96031 1.000 143.49126 ? 283 ASP A O   1 
ATOM   2168 C CB  . ASP A 1 289 ? -39.01490 56.78558 68.11689 1.000 142.18210 ? 283 ASP A CB  1 
ATOM   2169 C CG  . ASP A 1 289 ? -37.78307 57.49137 68.64232 1.000 146.29873 ? 283 ASP A CG  1 
ATOM   2170 O OD1 . ASP A 1 289 ? -37.27038 57.08078 69.70453 1.000 138.74041 ? 283 ASP A OD1 1 
ATOM   2171 O OD2 . ASP A 1 289 ? -37.32906 58.45826 67.99519 1.000 163.04692 ? 283 ASP A OD2 1 
ATOM   2172 N N   . VAL A 1 290 ? -41.23032 59.01008 70.04164 1.000 168.98153 ? 284 VAL A N   1 
ATOM   2173 C CA  . VAL A 1 290 ? -41.66264 60.40267 70.12411 1.000 162.67085 ? 284 VAL A CA  1 
ATOM   2174 C C   . VAL A 1 290 ? -40.47354 61.35021 70.04737 1.000 164.69019 ? 284 VAL A C   1 
ATOM   2175 O O   . VAL A 1 290 ? -40.61401 62.49807 69.60946 1.000 167.31119 ? 284 VAL A O   1 
ATOM   2176 C CB  . VAL A 1 290 ? -42.48547 60.63567 71.40812 1.000 150.69602 ? 284 VAL A CB  1 
ATOM   2177 C CG1 . VAL A 1 290 ? -43.75153 59.80044 71.38275 1.000 152.92268 ? 284 VAL A CG1 1 
ATOM   2178 C CG2 . VAL A 1 290 ? -41.65642 60.31923 72.64744 1.000 135.30553 ? 284 VAL A CG2 1 
ATOM   2179 N N   . TYR A 1 291 ? -39.28682 60.88974 70.45357 1.000 155.37587 ? 285 TYR A N   1 
ATOM   2180 C CA  . TYR A 1 291 ? -38.10411 61.74468 70.45740 1.000 127.37298 ? 285 TYR A CA  1 
ATOM   2181 C C   . TYR A 1 291 ? -37.74576 62.24815 69.06615 1.000 135.93174 ? 285 TYR A C   1 
ATOM   2182 O O   . TYR A 1 291 ? -37.03152 63.24955 68.94581 1.000 147.54321 ? 285 TYR A O   1 
ATOM   2183 C CB  . TYR A 1 291 ? -36.92237 60.99047 71.06607 1.000 138.41692 ? 285 TYR A CB  1 
ATOM   2184 C CG  . TYR A 1 291 ? -37.24265 60.36482 72.40308 1.000 151.17181 ? 285 TYR A CG  1 
ATOM   2185 C CD1 . TYR A 1 291 ? -37.08949 61.08299 73.58021 1.000 142.48553 ? 285 TYR A CD1 1 
ATOM   2186 C CD2 . TYR A 1 291 ? -37.70911 59.05883 72.48704 1.000 152.98711 ? 285 TYR A CD2 1 
ATOM   2187 C CE1 . TYR A 1 291 ? -37.38507 60.51800 74.80246 1.000 141.03421 ? 285 TYR A CE1 1 
ATOM   2188 C CE2 . TYR A 1 291 ? -38.00865 58.48594 73.70499 1.000 125.17647 ? 285 TYR A CE2 1 
ATOM   2189 C CZ  . TYR A 1 291 ? -37.84439 59.22034 74.85847 1.000 139.36815 ? 285 TYR A CZ  1 
ATOM   2190 O OH  . TYR A 1 291 ? -38.13946 58.65293 76.07334 1.000 137.34509 ? 285 TYR A OH  1 
ATOM   2191 N N   . SER A 1 292 ? -38.21629 61.57597 68.01442 1.000 143.71083 ? 286 SER A N   1 
ATOM   2192 C CA  . SER A 1 292 ? -38.06315 62.12160 66.67215 1.000 132.53355 ? 286 SER A CA  1 
ATOM   2193 C C   . SER A 1 292 ? -38.99368 63.30628 66.44619 1.000 138.23748 ? 286 SER A C   1 
ATOM   2194 O O   . SER A 1 292 ? -38.65926 64.21856 65.68227 1.000 142.91953 ? 286 SER A O   1 
ATOM   2195 C CB  . SER A 1 292 ? -38.31607 61.03203 65.63142 1.000 126.73994 ? 286 SER A CB  1 
ATOM   2196 O OG  . SER A 1 292 ? -37.26322 60.08456 65.62365 1.000 123.56088 ? 286 SER A OG  1 
ATOM   2197 N N   . MET A 1 293 ? -40.15499 63.31671 67.10642 1.000 152.37930 ? 287 MET A N   1 
ATOM   2198 C CA  . MET A 1 293 ? -41.07890 64.43786 66.96222 1.000 163.25578 ? 287 MET A CA  1 
ATOM   2199 C C   . MET A 1 293 ? -40.49928 65.71254 67.56292 1.000 155.35157 ? 287 MET A C   1 
ATOM   2200 O O   . MET A 1 293 ? -40.59340 66.78785 66.95920 1.000 154.17658 ? 287 MET A O   1 
ATOM   2201 C CB  . MET A 1 293 ? -42.42053 64.10357 67.61543 1.000 168.60513 ? 287 MET A CB  1 
ATOM   2202 C CG  . MET A 1 293 ? -43.05943 62.81855 67.11727 1.000 165.47966 ? 287 MET A CG  1 
ATOM   2203 S SD  . MET A 1 293 ? -43.58925 62.92942 65.39957 1.000 200.67679 ? 287 MET A SD  1 
ATOM   2204 C CE  . MET A 1 293 ? -44.75139 64.28923 65.49692 1.000 144.06450 ? 287 MET A CE  1 
ATOM   2205 N N   . ALA A 1 294 ? -39.90216 65.61370 68.75381 1.000 140.55599 ? 288 ALA A N   1 
ATOM   2206 C CA  . ALA A 1 294 ? -39.29311 66.78591 69.37368 1.000 124.55950 ? 288 ALA A CA  1 
ATOM   2207 C C   . ALA A 1 294 ? -38.14733 67.32156 68.52632 1.000 124.69602 ? 288 ALA A C   1 
ATOM   2208 O O   . ALA A 1 294 ? -38.01420 68.53745 68.34565 1.000 137.33204 ? 288 ALA A O   1 
ATOM   2209 C CB  . ALA A 1 294 ? -38.80751 66.44497 70.78120 1.000 118.09521 ? 288 ALA A CB  1 
ATOM   2210 N N   . THR A 1 295 ? -37.30496 66.42787 68.00335 1.000 110.38254 ? 289 THR A N   1 
ATOM   2211 C CA  . THR A 1 295 ? -36.27618 66.84744 67.05960 1.000 110.40428 ? 289 THR A CA  1 
ATOM   2212 C C   . THR A 1 295 ? -36.89397 67.47935 65.82024 1.000 123.25883 ? 289 THR A C   1 
ATOM   2213 O O   . THR A 1 295 ? -36.33782 68.43305 65.26311 1.000 124.60011 ? 289 THR A O   1 
ATOM   2214 C CB  . THR A 1 295 ? -35.40203 65.65137 66.67717 1.000 113.20241 ? 289 THR A CB  1 
ATOM   2215 O OG1 . THR A 1 295 ? -34.75658 65.13778 67.84911 1.000 114.99377 ? 289 THR A OG1 1 
ATOM   2216 C CG2 . THR A 1 295 ? -34.34694 66.05511 65.65940 1.000 114.20138 ? 289 THR A CG2 1 
ATOM   2217 N N   . ALA A 1 296 ? -38.05083 66.97596 65.38764 1.000 136.93238 ? 290 ALA A N   1 
ATOM   2218 C CA  . ALA A 1 296 ? -38.74482 67.57999 64.25747 1.000 140.01474 ? 290 ALA A CA  1 
ATOM   2219 C C   . ALA A 1 296 ? -39.32373 68.93713 64.63540 1.000 128.99577 ? 290 ALA A C   1 
ATOM   2220 O O   . ALA A 1 296 ? -39.16145 69.91746 63.90023 1.000 130.84700 ? 290 ALA A O   1 
ATOM   2221 C CB  . ALA A 1 296 ? -39.84117 66.64141 63.75593 1.000 152.41602 ? 290 ALA A CB  1 
ATOM   2222 N N   . ARG A 1 297 ? -40.00109 69.01418 65.78510 1.000 128.37796 ? 291 ARG A N   1 
ATOM   2223 C CA  . ARG A 1 297 ? -40.56675 70.28618 66.22355 1.000 138.83006 ? 291 ARG A CA  1 
ATOM   2224 C C   . ARG A 1 297 ? -39.48345 71.32770 66.47154 1.000 145.99729 ? 291 ARG A C   1 
ATOM   2225 O O   . ARG A 1 297 ? -39.72911 72.52729 66.30256 1.000 155.76962 ? 291 ARG A O   1 
ATOM   2226 C CB  . ARG A 1 297 ? -41.41424 70.08658 67.48151 1.000 128.14561 ? 291 ARG A CB  1 
ATOM   2227 C CG  . ARG A 1 297 ? -42.70886 69.32558 67.23996 1.000 121.00660 ? 291 ARG A CG  1 
ATOM   2228 C CD  . ARG A 1 297 ? -43.68927 69.50421 68.38698 1.000 135.88541 ? 291 ARG A CD  1 
ATOM   2229 N NE  . ARG A 1 297 ? -43.25974 68.81170 69.59527 1.000 147.90687 ? 291 ARG A NE  1 
ATOM   2230 C CZ  . ARG A 1 297 ? -43.71275 67.62633 69.97927 1.000 145.24965 ? 291 ARG A CZ  1 
ATOM   2231 N NH1 . ARG A 1 297 ? -44.61835 66.97002 69.27227 1.000 137.56082 ? 291 ARG A NH1 1 
ATOM   2232 N NH2 . ARG A 1 297 ? -43.24827 67.08757 71.10269 1.000 137.85528 ? 291 ARG A NH2 1 
ATOM   2233 N N   . SER A 1 298 ? -38.28444 70.89669 66.87269 1.000 134.49077 ? 292 SER A N   1 
ATOM   2234 C CA  . SER A 1 298 ? -37.16789 71.83168 66.96757 1.000 119.28060 ? 292 SER A CA  1 
ATOM   2235 C C   . SER A 1 298 ? -36.75166 72.32490 65.58819 1.000 111.05500 ? 292 SER A C   1 
ATOM   2236 O O   . SER A 1 298 ? -36.50480 73.52103 65.39801 1.000 121.19443 ? 292 SER A O   1 
ATOM   2237 C CB  . SER A 1 298 ? -35.98450 71.17903 67.68343 1.000 125.84215 ? 292 SER A CB  1 
ATOM   2238 O OG  . SER A 1 298 ? -36.21337 71.08213 69.07835 1.000 108.72764 ? 292 SER A OG  1 
ATOM   2239 N N   . LEU A 1 299 ? -36.67050 71.41845 64.61240 1.000 115.34166 ? 293 LEU A N   1 
ATOM   2240 C CA  . LEU A 1 299 ? -36.34829 71.83038 63.25150 1.000 120.63469 ? 293 LEU A CA  1 
ATOM   2241 C C   . LEU A 1 299 ? -37.52217 72.53709 62.58835 1.000 130.62679 ? 293 LEU A C   1 
ATOM   2242 O O   . LEU A 1 299 ? -37.31761 73.38499 61.71277 1.000 113.49843 ? 293 LEU A O   1 
ATOM   2243 C CB  . LEU A 1 299 ? -35.92010 70.61906 62.42481 1.000 97.56001  ? 293 LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 299 ? -34.62823 69.94033 62.87997 1.000 105.61612 ? 293 LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 299 ? -34.40348 68.64350 62.12125 1.000 115.00594 ? 293 LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 299 ? -33.44807 70.88119 62.70172 1.000 87.74482  ? 293 LEU A CD2 1 
ATOM   2247 N N   . ASP A 1 300 ? -38.75140 72.20691 62.99232 1.000 154.03851 ? 294 ASP A N   1 
ATOM   2248 C CA  . ASP A 1 300 ? -39.92387 72.84733 62.40494 1.000 162.03722 ? 294 ASP A CA  1 
ATOM   2249 C C   . ASP A 1 300 ? -39.97136 74.33151 62.74570 1.000 161.06634 ? 294 ASP A C   1 
ATOM   2250 O O   . ASP A 1 300 ? -40.25635 75.16505 61.87785 1.000 176.92429 ? 294 ASP A O   1 
ATOM   2251 C CB  . ASP A 1 300 ? -41.19690 72.14601 62.88379 1.000 163.84352 ? 294 ASP A CB  1 
ATOM   2252 C CG  . ASP A 1 300 ? -42.43224 72.57798 62.11320 1.000 175.98185 ? 294 ASP A CG  1 
ATOM   2253 O OD1 . ASP A 1 300 ? -42.28643 73.25941 61.07693 1.000 197.00785 ? 294 ASP A OD1 1 
ATOM   2254 O OD2 . ASP A 1 300 ? -43.55262 72.23341 62.54560 1.000 155.83631 ? 294 ASP A OD2 1 
ATOM   2255 N N   . GLU A 1 301 ? -39.68513 74.68216 64.00138 1.000 134.96410 ? 295 GLU A N   1 
ATOM   2256 C CA  . GLU A 1 301 ? -39.80975 76.07270 64.42291 1.000 120.20405 ? 295 GLU A CA  1 
ATOM   2257 C C   . GLU A 1 301 ? -38.70640 76.94622 63.84274 1.000 126.83692 ? 295 GLU A C   1 
ATOM   2258 O O   . GLU A 1 301 ? -38.90001 78.15577 63.67970 1.000 128.88051 ? 295 GLU A O   1 
ATOM   2259 C CB  . GLU A 1 301 ? -39.81202 76.16000 65.94606 1.000 119.27498 ? 295 GLU A CB  1 
ATOM   2260 C CG  . GLU A 1 301 ? -41.00949 75.48818 66.59315 1.000 171.14142 ? 295 GLU A CG  1 
ATOM   2261 C CD  . GLU A 1 301 ? -41.16881 75.87701 68.04447 1.000 181.77163 ? 295 GLU A CD  1 
ATOM   2262 O OE1 . GLU A 1 301 ? -40.43592 76.78147 68.49154 1.000 174.31247 ? 295 GLU A OE1 1 
ATOM   2263 O OE2 . GLU A 1 301 ? -42.01979 75.28081 68.73719 1.000 172.27800 ? 295 GLU A OE2 1 
ATOM   2264 N N   . LEU A 1 302 ? -37.55284 76.36351 63.52198 1.000 119.38406 ? 296 LEU A N   1 
ATOM   2265 C CA  . LEU A 1 302 ? -36.48483 77.13643 62.90161 1.000 113.08707 ? 296 LEU A CA  1 
ATOM   2266 C C   . LEU A 1 302 ? -36.76735 77.46920 61.44343 1.000 123.35145 ? 296 LEU A C   1 
ATOM   2267 O O   . LEU A 1 302 ? -35.94278 78.13426 60.81096 1.000 121.34339 ? 296 LEU A O   1 
ATOM   2268 C CB  . LEU A 1 302 ? -35.16062 76.38089 63.01705 1.000 98.77285  ? 296 LEU A CB  1 
ATOM   2269 C CG  . LEU A 1 302 ? -34.73210 76.04180 64.44560 1.000 104.67797 ? 296 LEU A CG  1 
ATOM   2270 C CD1 . LEU A 1 302 ? -33.47948 75.18130 64.44622 1.000 88.52198  ? 296 LEU A CD1 1 
ATOM   2271 C CD2 . LEU A 1 302 ? -34.52141 77.31029 65.25986 1.000 97.04706  ? 296 LEU A CD2 1 
ATOM   2272 N N   . CYS A 1 303 ? -37.90088 77.03515 60.89873 1.000 145.05554 ? 297 CYS A N   1 
ATOM   2273 C CA  . CYS A 1 303 ? -38.25737 77.29375 59.51053 1.000 139.05195 ? 297 CYS A CA  1 
ATOM   2274 C C   . CYS A 1 303 ? -39.06663 78.57038 59.32644 1.000 149.21938 ? 297 CYS A C   1 
ATOM   2275 O O   . CYS A 1 303 ? -39.33644 78.95313 58.18291 1.000 152.59243 ? 297 CYS A O   1 
ATOM   2276 C CB  . CYS A 1 303 ? -39.04485 76.10919 58.94320 1.000 136.35160 ? 297 CYS A CB  1 
ATOM   2277 S SG  . CYS A 1 303 ? -38.14921 74.54469 58.96813 1.000 150.50327 ? 297 CYS A SG  1 
ATOM   2278 N N   . VAL A 1 304 ? -39.45493 79.23679 60.41167 1.000 144.29413 ? 298 VAL A N   1 
ATOM   2279 C CA  . VAL A 1 304 ? -40.33087 80.39642 60.29632 1.000 154.01250 ? 298 VAL A CA  1 
ATOM   2280 C C   . VAL A 1 304 ? -39.55134 81.70648 60.19026 1.000 163.04006 ? 298 VAL A C   1 
ATOM   2281 O O   . VAL A 1 304 ? -40.05758 82.67689 59.61770 1.000 179.62733 ? 298 VAL A O   1 
ATOM   2282 C CB  . VAL A 1 304 ? -41.32156 80.43529 61.47373 1.000 151.56063 ? 298 VAL A CB  1 
ATOM   2283 C CG1 . VAL A 1 304 ? -42.08492 79.12171 61.56527 1.000 139.80947 ? 298 VAL A CG1 1 
ATOM   2284 C CG2 . VAL A 1 304 ? -40.60366 80.72859 62.77664 1.000 141.94577 ? 298 VAL A CG2 1 
ATOM   2285 N N   . GLN A 1 305 ? -38.32992 81.76193 60.72337 1.000 149.40705 ? 299 GLN A N   1 
ATOM   2286 C CA  . GLN A 1 305 ? -37.51613 82.96763 60.61317 1.000 153.86932 ? 299 GLN A CA  1 
ATOM   2287 C C   . GLN A 1 305 ? -36.13645 82.65065 60.05020 1.000 141.12146 ? 299 GLN A C   1 
ATOM   2288 O O   . GLN A 1 305 ? -35.55219 83.47123 59.33373 1.000 138.96577 ? 299 GLN A O   1 
ATOM   2289 C CB  . GLN A 1 305 ? -37.38909 83.66443 61.96836 1.000 150.05596 ? 299 GLN A CB  1 
ATOM   2290 C CG  . GLN A 1 305 ? -38.65277 84.37786 62.41862 1.000 152.23693 ? 299 GLN A CG  1 
ATOM   2291 C CD  . GLN A 1 305 ? -38.44632 85.18123 63.68685 1.000 167.03635 ? 299 GLN A CD  1 
ATOM   2292 O OE1 . GLN A 1 305 ? -37.45119 85.00655 64.39096 1.000 154.72759 ? 299 GLN A OE1 1 
ATOM   2293 N NE2 . GLN A 1 305 ? -39.38550 86.07287 63.98222 1.000 171.17514 ? 299 GLN A NE2 1 
ATOM   2294 N N   . ASN A 1 306 ? -35.60106 81.47656 60.37511 1.000 136.06712 ? 300 ASN A N   1 
ATOM   2295 C CA  . ASN A 1 306 ? -34.36936 81.04147 59.74070 1.000 131.31777 ? 300 ASN A CA  1 
ATOM   2296 C C   . ASN A 1 306 ? -34.68535 80.37419 58.40560 1.000 118.83246 ? 300 ASN A C   1 
ATOM   2297 O O   . ASN A 1 306 ? -35.80703 79.92441 58.15238 1.000 107.04532 ? 300 ASN A O   1 
ATOM   2298 C CB  . ASN A 1 306 ? -33.59380 80.07982 60.64202 1.000 104.74812 ? 300 ASN A CB  1 
ATOM   2299 C CG  . ASN A 1 306 ? -33.45831 80.58940 62.06218 1.000 119.75260 ? 300 ASN A CG  1 
ATOM   2300 O OD1 . ASN A 1 306 ? -34.22588 80.20639 62.94630 1.000 127.88360 ? 300 ASN A OD1 1 
ATOM   2301 N ND2 . ASN A 1 306 ? -32.47899 81.45892 62.28951 1.000 125.02221 ? 300 ASN A ND2 1 
ATOM   2302 N N   . ASP A 1 307 ? -33.67784 80.32005 57.54058 1.000 102.59492 ? 301 ASP A N   1 
ATOM   2303 C CA  . ASP A 1 307 ? -33.85387 79.76560 56.20026 1.000 101.20420 ? 301 ASP A CA  1 
ATOM   2304 C C   . ASP A 1 307 ? -33.66673 78.24650 56.22400 1.000 105.85839 ? 301 ASP A C   1 
ATOM   2305 O O   . ASP A 1 307 ? -32.81400 77.67302 55.54565 1.000 99.29903  ? 301 ASP A O   1 
ATOM   2306 C CB  . ASP A 1 307 ? -32.89486 80.43726 55.22509 1.000 127.27692 ? 301 ASP A CB  1 
ATOM   2307 C CG  . ASP A 1 307 ? -33.56634 80.82468 53.92058 1.000 130.15933 ? 301 ASP A CG  1 
ATOM   2308 O OD1 . ASP A 1 307 ? -34.52034 80.12827 53.51023 1.000 124.56180 ? 301 ASP A OD1 1 
ATOM   2309 O OD2 . ASP A 1 307 ? -33.14029 81.82644 53.30792 1.000 140.40135 ? 301 ASP A OD2 1 
ATOM   2310 N N   . LEU A 1 308 ? -34.49298 77.59617 57.03766 1.000 88.98775  ? 302 LEU A N   1 
ATOM   2311 C CA  . LEU A 1 308 ? -34.51428 76.14616 57.15451 1.000 91.52491  ? 302 LEU A CA  1 
ATOM   2312 C C   . LEU A 1 308 ? -35.81438 75.61453 56.56701 1.000 101.90229 ? 302 LEU A C   1 
ATOM   2313 O O   . LEU A 1 308 ? -36.86295 76.25697 56.67699 1.000 118.08613 ? 302 LEU A O   1 
ATOM   2314 C CB  . LEU A 1 308 ? -34.37457 75.71195 58.61751 1.000 92.69690  ? 302 LEU A CB  1 
ATOM   2315 C CG  . LEU A 1 308 ? -34.28613 74.21467 58.92319 1.000 89.28709  ? 302 LEU A CG  1 
ATOM   2316 C CD1 . LEU A 1 308 ? -33.09012 73.60204 58.23309 1.000 76.00472  ? 302 LEU A CD1 1 
ATOM   2317 C CD2 . LEU A 1 308 ? -34.20827 73.97609 60.42063 1.000 101.97381 ? 302 LEU A CD2 1 
ATOM   2318 N N   . SER A 1 309 ? -35.73930 74.44997 55.92764 1.000 93.94477  ? 303 SER A N   1 
ATOM   2319 C CA  . SER A 1 309 ? -36.91218 73.81950 55.33971 1.000 92.93545  ? 303 SER A CA  1 
ATOM   2320 C C   . SER A 1 309 ? -36.76402 72.31204 55.46544 1.000 87.02491  ? 303 SER A C   1 
ATOM   2321 O O   . SER A 1 309 ? -35.66288 71.77723 55.31061 1.000 93.26122  ? 303 SER A O   1 
ATOM   2322 C CB  . SER A 1 309 ? -37.09208 74.21729 53.87007 1.000 92.89319  ? 303 SER A CB  1 
ATOM   2323 O OG  . SER A 1 309 ? -37.21951 75.62154 53.72961 1.000 93.08800  ? 303 SER A OG  1 
ATOM   2324 N N   . VAL A 1 310 ? -37.87333 71.63293 55.74794 1.000 73.15555  ? 304 VAL A N   1 
ATOM   2325 C CA  . VAL A 1 310 ? -37.86391 70.19632 56.00296 1.000 76.59959  ? 304 VAL A CA  1 
ATOM   2326 C C   . VAL A 1 310 ? -39.02244 69.54805 55.25969 1.000 84.32625  ? 304 VAL A C   1 
ATOM   2327 O O   . VAL A 1 310 ? -40.17819 69.95092 55.42615 1.000 95.54127  ? 304 VAL A O   1 
ATOM   2328 C CB  . VAL A 1 310 ? -37.95673 69.87906 57.50873 1.000 78.80770  ? 304 VAL A CB  1 
ATOM   2329 C CG1 . VAL A 1 310 ? -38.12271 68.38762 57.72156 1.000 74.52188  ? 304 VAL A CG1 1 
ATOM   2330 C CG2 . VAL A 1 310 ? -36.72254 70.38788 58.24177 1.000 80.73760  ? 304 VAL A CG2 1 
ATOM   2331 N N   . LYS A 1 311 ? -38.71412 68.54180 54.44668 1.000 81.15094  ? 305 LYS A N   1 
ATOM   2332 C CA  . LYS A 1 311 ? -39.71499 67.69582 53.81595 1.000 74.09048  ? 305 LYS A CA  1 
ATOM   2333 C C   . LYS A 1 311 ? -39.41075 66.23955 54.14088 1.000 69.93346  ? 305 LYS A C   1 
ATOM   2334 O O   . LYS A 1 311 ? -38.25857 65.87365 54.39156 1.000 76.21094  ? 305 LYS A O   1 
ATOM   2335 C CB  . LYS A 1 311 ? -39.75502 67.90425 52.29528 1.000 66.53662  ? 305 LYS A CB  1 
ATOM   2336 C CG  . LYS A 1 311 ? -40.26224 69.27272 51.87009 1.000 85.68593  ? 305 LYS A CG  1 
ATOM   2337 C CD  . LYS A 1 311 ? -40.47805 69.34778 50.36661 1.000 73.99334  ? 305 LYS A CD  1 
ATOM   2338 C CE  . LYS A 1 311 ? -41.15957 70.64948 49.97788 1.000 85.96020  ? 305 LYS A CE  1 
ATOM   2339 N NZ  . LYS A 1 311 ? -41.55717 70.66968 48.54386 1.000 86.65007  ? 305 LYS A NZ  1 
ATOM   2340 N N   . VAL A 1 312 ? -40.45034 65.40754 54.14163 1.000 69.69315  ? 306 VAL A N   1 
ATOM   2341 C CA  . VAL A 1 312 ? -40.31119 64.00473 54.51253 1.000 80.34676  ? 306 VAL A CA  1 
ATOM   2342 C C   . VAL A 1 312 ? -40.78696 63.12110 53.36887 1.000 83.86103  ? 306 VAL A C   1 
ATOM   2343 O O   . VAL A 1 312 ? -41.68746 63.48452 52.60463 1.000 74.75645  ? 306 VAL A O   1 
ATOM   2344 C CB  . VAL A 1 312 ? -41.08288 63.67001 55.80775 1.000 73.35714  ? 306 VAL A CB  1 
ATOM   2345 C CG1 . VAL A 1 312 ? -40.50250 64.43718 56.97953 1.000 78.61732  ? 306 VAL A CG1 1 
ATOM   2346 C CG2 . VAL A 1 312 ? -42.55753 63.98586 55.64254 1.000 81.27561  ? 306 VAL A CG2 1 
ATOM   2347 N N   . PHE A 1 313 ? -40.16937 61.94606 53.25825 1.000 75.40316  ? 307 PHE A N   1 
ATOM   2348 C CA  . PHE A 1 313 ? -40.58463 60.92414 52.30999 1.000 72.80368  ? 307 PHE A CA  1 
ATOM   2349 C C   . PHE A 1 313 ? -40.87447 59.62371 53.04778 1.000 70.08012  ? 307 PHE A C   1 
ATOM   2350 O O   . PHE A 1 313 ? -40.28346 59.33672 54.09338 1.000 83.07704  ? 307 PHE A O   1 
ATOM   2351 C CB  . PHE A 1 313 ? -39.51875 60.68491 51.22184 1.000 75.61590  ? 307 PHE A CB  1 
ATOM   2352 C CG  . PHE A 1 313 ? -38.17492 60.25775 51.75694 1.000 65.11102  ? 307 PHE A CG  1 
ATOM   2353 C CD1 . PHE A 1 313 ? -37.90695 58.92387 52.02818 1.000 71.41926  ? 307 PHE A CD1 1 
ATOM   2354 C CD2 . PHE A 1 313 ? -37.17199 61.18967 51.96546 1.000 69.95557  ? 307 PHE A CD2 1 
ATOM   2355 C CE1 . PHE A 1 313 ? -36.67223 58.53398 52.51598 1.000 61.16283  ? 307 PHE A CE1 1 
ATOM   2356 C CE2 . PHE A 1 313 ? -35.93467 60.80499 52.44895 1.000 66.25212  ? 307 PHE A CE2 1 
ATOM   2357 C CZ  . PHE A 1 313 ? -35.68478 59.47655 52.72488 1.000 61.47556  ? 307 PHE A CZ  1 
ATOM   2358 N N   . THR A 1 314 ? -41.79712 58.83923 52.49337 1.000 67.20442  ? 308 THR A N   1 
ATOM   2359 C CA  . THR A 1 314 ? -42.12126 57.52596 53.02661 1.000 68.22152  ? 308 THR A CA  1 
ATOM   2360 C C   . THR A 1 314 ? -41.67941 56.38889 52.11947 1.000 80.23384  ? 308 THR A C   1 
ATOM   2361 O O   . THR A 1 314 ? -41.74842 55.22741 52.53478 1.000 82.39718  ? 308 THR A O   1 
ATOM   2362 C CB  . THR A 1 314 ? -43.63082 57.40829 53.27832 1.000 73.95706  ? 308 THR A CB  1 
ATOM   2363 O OG1 . THR A 1 314 ? -44.33853 57.66568 52.05976 1.000 79.97105  ? 308 THR A OG1 1 
ATOM   2364 C CG2 . THR A 1 314 ? -44.07123 58.40464 54.33594 1.000 74.77373  ? 308 THR A CG2 1 
ATOM   2365 N N   . ILE A 1 315 ? -41.23550 56.68995 50.89687 1.000 76.07675  ? 309 ILE A N   1 
ATOM   2366 C CA  . ILE A 1 315 ? -40.77697 55.64727 49.98876 1.000 71.47092  ? 309 ILE A CA  1 
ATOM   2367 C C   . ILE A 1 315 ? -39.48758 55.02457 50.51016 1.000 72.08988  ? 309 ILE A C   1 
ATOM   2368 O O   . ILE A 1 315 ? -38.72825 55.62821 51.27758 1.000 68.91964  ? 309 ILE A O   1 
ATOM   2369 C CB  . ILE A 1 315 ? -40.57375 56.20761 48.57220 1.000 63.89523  ? 309 ILE A CB  1 
ATOM   2370 C CG1 . ILE A 1 315 ? -39.64104 57.41870 48.61982 1.000 66.58712  ? 309 ILE A CG1 1 
ATOM   2371 C CG2 . ILE A 1 315 ? -41.90084 56.56533 47.93234 1.000 63.20119  ? 309 ILE A CG2 1 
ATOM   2372 C CD1 . ILE A 1 315 ? -39.21424 57.90484 47.26699 1.000 63.12029  ? 309 ILE A CD1 1 
ATOM   2373 N N   . GLN A 1 316 ? -39.23977 53.78918 50.07826 1.000 62.44128  ? 310 GLN A N   1 
ATOM   2374 C CA  . GLN A 1 316 ? -37.93637 53.17365 50.27896 1.000 56.56038  ? 310 GLN A CA  1 
ATOM   2375 C C   . GLN A 1 316 ? -36.89447 53.98247 49.51985 1.000 58.99801  ? 310 GLN A C   1 
ATOM   2376 O O   . GLN A 1 316 ? -36.93060 54.04584 48.28705 1.000 80.06302  ? 310 GLN A O   1 
ATOM   2377 C CB  . GLN A 1 316 ? -37.94087 51.71629 49.81312 1.000 70.41350  ? 310 GLN A CB  1 
ATOM   2378 C CG  . GLN A 1 316 ? -38.76648 50.78281 50.68283 1.000 60.53131  ? 310 GLN A CG  1 
ATOM   2379 C CD  . GLN A 1 316 ? -38.87135 49.39085 50.09443 1.000 99.17467  ? 310 GLN A CD  1 
ATOM   2380 O OE1 . GLN A 1 316 ? -39.01933 49.22784 48.88264 1.000 99.11180  ? 310 GLN A OE1 1 
ATOM   2381 N NE2 . GLN A 1 316 ? -38.78938 48.37739 50.94924 1.000 114.78428 ? 310 GLN A NE2 1 
ATOM   2382 N N   . ASN A 1 317 ? -35.97310 54.61451 50.24111 1.000 64.62264  ? 311 ASN A N   1 
ATOM   2383 C CA  . ASN A 1 317 ? -35.00552 55.50865 49.61695 1.000 69.12862  ? 311 ASN A CA  1 
ATOM   2384 C C   . ASN A 1 317 ? -33.69050 55.41131 50.37122 1.000 66.78768  ? 311 ASN A C   1 
ATOM   2385 O O   . ASN A 1 317 ? -33.62605 55.76142 51.55323 1.000 69.90148  ? 311 ASN A O   1 
ATOM   2386 C CB  . ASN A 1 317 ? -35.52485 56.94864 49.60974 1.000 55.87434  ? 311 ASN A CB  1 
ATOM   2387 C CG  . ASN A 1 317 ? -34.55029 57.91553 48.97607 1.000 66.42929  ? 311 ASN A CG  1 
ATOM   2388 O OD1 . ASN A 1 317 ? -33.71622 57.52682 48.15761 1.000 82.57363  ? 311 ASN A OD1 1 
ATOM   2389 N ND2 . ASN A 1 317 ? -34.65080 59.18514 49.34844 1.000 61.03103  ? 311 ASN A ND2 1 
ATOM   2390 N N   . ASN A 1 318 ? -32.65050 54.93817 49.69009 1.000 69.80244  ? 312 ASN A N   1 
ATOM   2391 C CA  . ASN A 1 318 ? -31.32287 54.82276 50.27683 1.000 62.85659  ? 312 ASN A CA  1 
ATOM   2392 C C   . ASN A 1 318 ? -30.44656 56.03561 49.99932 1.000 62.59484  ? 312 ASN A C   1 
ATOM   2393 O O   . ASN A 1 318 ? -29.27370 56.03173 50.38634 1.000 70.95686  ? 312 ASN A O   1 
ATOM   2394 C CB  . ASN A 1 318 ? -30.61988 53.55934 49.76178 1.000 58.25673  ? 312 ASN A CB  1 
ATOM   2395 C CG  . ASN A 1 318 ? -31.27608 52.28243 50.25121 1.000 59.27559  ? 312 ASN A CG  1 
ATOM   2396 O OD1 . ASN A 1 318 ? -31.92829 52.26688 51.29395 1.000 86.07108  ? 312 ASN A OD1 1 
ATOM   2397 N ND2 . ASN A 1 318 ? -31.10008 51.20066 49.50116 1.000 74.84990  ? 312 ASN A ND2 1 
ATOM   2398 N N   . THR A 1 319 ? -30.98354 57.06542 49.34711 1.000 66.70233  ? 313 THR A N   1 
ATOM   2399 C CA  . THR A 1 319 ? -30.18466 58.22121 48.95937 1.000 60.13361  ? 313 THR A CA  1 
ATOM   2400 C C   . THR A 1 319 ? -29.53283 58.86853 50.17409 1.000 68.56398  ? 313 THR A C   1 
ATOM   2401 O O   . THR A 1 319 ? -30.19236 59.13968 51.18134 1.000 68.94127  ? 313 THR A O   1 
ATOM   2402 C CB  . THR A 1 319 ? -31.05954 59.24401 48.23058 1.000 60.82058  ? 313 THR A CB  1 
ATOM   2403 O OG1 . THR A 1 319 ? -31.77561 58.59987 47.16876 1.000 67.53232  ? 313 THR A OG1 1 
ATOM   2404 C CG2 . THR A 1 319 ? -30.20138 60.35843 47.65156 1.000 68.28159  ? 313 THR A CG2 1 
ATOM   2405 N N   . LYS A 1 320 ? -28.22522 59.09698 50.07618 1.000 67.42124  ? 314 LYS A N   1 
ATOM   2406 C CA  . LYS A 1 320 ? -27.46487 59.83361 51.08398 1.000 66.74142  ? 314 LYS A CA  1 
ATOM   2407 C C   . LYS A 1 320 ? -26.68211 60.91081 50.33906 1.000 71.91758  ? 314 LYS A C   1 
ATOM   2408 O O   . LYS A 1 320 ? -25.60470 60.64128 49.79883 1.000 73.71892  ? 314 LYS A O   1 
ATOM   2409 C CB  . LYS A 1 320 ? -26.54452 58.90882 51.87351 1.000 61.79742  ? 314 LYS A CB  1 
ATOM   2410 C CG  . LYS A 1 320 ? -27.25462 57.75246 52.56516 1.000 56.90114  ? 314 LYS A CG  1 
ATOM   2411 C CD  . LYS A 1 320 ? -28.18980 58.24828 53.65313 1.000 74.45256  ? 314 LYS A CD  1 
ATOM   2412 C CE  . LYS A 1 320 ? -28.75013 57.09640 54.46937 1.000 65.47009  ? 314 LYS A CE  1 
ATOM   2413 N NZ  . LYS A 1 320 ? -29.43318 56.09001 53.61124 1.000 65.99421  ? 314 LYS A NZ  1 
ATOM   2414 N N   . LEU A 1 321 ? -27.22760 62.12562 50.30470 1.000 64.27499  ? 315 LEU A N   1 
ATOM   2415 C CA  . LEU A 1 321 ? -26.70024 63.19823 49.47193 1.000 62.21841  ? 315 LEU A CA  1 
ATOM   2416 C C   . LEU A 1 321 ? -26.53772 64.46903 50.29062 1.000 71.13995  ? 315 LEU A C   1 
ATOM   2417 O O   . LEU A 1 321 ? -27.43538 64.84119 51.05256 1.000 73.42975  ? 315 LEU A O   1 
ATOM   2418 C CB  . LEU A 1 321 ? -27.62250 63.46012 48.27842 1.000 66.00362  ? 315 LEU A CB  1 
ATOM   2419 C CG  . LEU A 1 321 ? -27.26682 64.63752 47.37128 1.000 66.78528  ? 315 LEU A CG  1 
ATOM   2420 C CD1 . LEU A 1 321 ? -25.96879 64.36870 46.62619 1.000 70.37777  ? 315 LEU A CD1 1 
ATOM   2421 C CD2 . LEU A 1 321 ? -28.40286 64.92451 46.40309 1.000 58.04239  ? 315 LEU A CD2 1 
ATOM   2422 N N   . LEU A 1 322 ? -25.39658 65.13327 50.12206 1.000 66.60594  ? 316 LEU A N   1 
ATOM   2423 C CA  . LEU A 1 322 ? -25.12194 66.42206 50.74288 1.000 57.78667  ? 316 LEU A CA  1 
ATOM   2424 C C   . LEU A 1 322 ? -24.50849 67.33921 49.69820 1.000 61.81145  ? 316 LEU A C   1 
ATOM   2425 O O   . LEU A 1 322 ? -23.56398 66.94897 49.00506 1.000 76.75918  ? 316 LEU A O   1 
ATOM   2426 C CB  . LEU A 1 322 ? -24.18109 66.27599 51.94464 1.000 66.53279  ? 316 LEU A CB  1 
ATOM   2427 C CG  . LEU A 1 322 ? -23.41216 67.51672 52.41453 1.000 65.42430  ? 316 LEU A CG  1 
ATOM   2428 C CD1 . LEU A 1 322 ? -24.34659 68.62977 52.85962 1.000 58.79223  ? 316 LEU A CD1 1 
ATOM   2429 C CD2 . LEU A 1 322 ? -22.45025 67.15394 53.53362 1.000 71.93596  ? 316 LEU A CD2 1 
ATOM   2430 N N   . ILE A 1 323 ? -25.05283 68.54710 49.57641 1.000 63.97716  ? 317 ILE A N   1 
ATOM   2431 C CA  . ILE A 1 323 ? -24.55893 69.54582 48.63643 1.000 68.17663  ? 317 ILE A CA  1 
ATOM   2432 C C   . ILE A 1 323 ? -24.38086 70.85618 49.38891 1.000 67.18659  ? 317 ILE A C   1 
ATOM   2433 O O   . ILE A 1 323 ? -25.28644 71.29014 50.10942 1.000 77.52345  ? 317 ILE A O   1 
ATOM   2434 C CB  . ILE A 1 323 ? -25.51045 69.73101 47.43873 1.000 64.36209  ? 317 ILE A CB  1 
ATOM   2435 C CG1 . ILE A 1 323 ? -25.80813 68.38385 46.77384 1.000 71.47403  ? 317 ILE A CG1 1 
ATOM   2436 C CG2 . ILE A 1 323 ? -24.90981 70.69711 46.43309 1.000 60.83322  ? 317 ILE A CG2 1 
ATOM   2437 C CD1 . ILE A 1 323 ? -26.86137 68.45403 45.68740 1.000 67.34359  ? 317 ILE A CD1 1 
ATOM   2438 N N   . VAL A 1 324 ? -23.21929 71.48422 49.22171 1.000 76.22513  ? 318 VAL A N   1 
ATOM   2439 C CA  . VAL A 1 324 ? -22.86141 72.69442 49.95316 1.000 68.57575  ? 318 VAL A CA  1 
ATOM   2440 C C   . VAL A 1 324 ? -22.48854 73.77839 48.95207 1.000 85.86794  ? 318 VAL A C   1 
ATOM   2441 O O   . VAL A 1 324 ? -21.52434 73.61993 48.19314 1.000 88.95435  ? 318 VAL A O   1 
ATOM   2442 C CB  . VAL A 1 324 ? -21.70168 72.45022 50.93297 1.000 70.81840  ? 318 VAL A CB  1 
ATOM   2443 C CG1 . VAL A 1 324 ? -21.17683 73.77124 51.47067 1.000 67.64200  ? 318 VAL A CG1 1 
ATOM   2444 C CG2 . VAL A 1 324 ? -22.14786 71.54031 52.07074 1.000 69.33525  ? 318 VAL A CG2 1 
ATOM   2445 N N   . ASP A 1 325 ? -23.25436 74.87153 48.94684 1.000 79.92167  ? 319 ASP A N   1 
ATOM   2446 C CA  . ASP A 1 325 ? -22.92888 76.09837 48.21723 1.000 80.63899  ? 319 ASP A CA  1 
ATOM   2447 C C   . ASP A 1 325 ? -22.71531 75.87411 46.72329 1.000 84.60136  ? 319 ASP A C   1 
ATOM   2448 O O   . ASP A 1 325 ? -22.08499 76.70458 46.05980 1.000 105.78188 ? 319 ASP A O   1 
ATOM   2449 C CB  . ASP A 1 325 ? -21.69344 76.78477 48.81438 1.000 70.39939  ? 319 ASP A CB  1 
ATOM   2450 C CG  . ASP A 1 325 ? -21.97005 77.41483 50.16405 1.000 87.09586  ? 319 ASP A CG  1 
ATOM   2451 O OD1 . ASP A 1 325 ? -23.13014 77.35739 50.62302 1.000 103.83446 ? 319 ASP A OD1 1 
ATOM   2452 O OD2 . ASP A 1 325 ? -21.02668 77.97099 50.76392 1.000 91.63201  ? 319 ASP A OD2 1 
ATOM   2453 N N   . ASP A 1 326 ? -23.23408 74.77428 46.17450 1.000 81.16432  ? 320 ASP A N   1 
ATOM   2454 C CA  . ASP A 1 326 ? -23.02199 74.41615 44.77060 1.000 95.36414  ? 320 ASP A CA  1 
ATOM   2455 C C   . ASP A 1 326 ? -21.53579 74.37067 44.42031 1.000 81.84115  ? 320 ASP A C   1 
ATOM   2456 O O   . ASP A 1 326 ? -21.12901 74.75875 43.32217 1.000 94.02071  ? 320 ASP A O   1 
ATOM   2457 C CB  . ASP A 1 326 ? -23.77112 75.36853 43.83321 1.000 94.48845  ? 320 ASP A CB  1 
ATOM   2458 C CG  . ASP A 1 326 ? -25.26125 75.41346 44.11955 1.000 112.41592 ? 320 ASP A CG  1 
ATOM   2459 O OD1 . ASP A 1 326 ? -25.70627 74.73139 45.06705 1.000 109.12336 ? 320 ASP A OD1 1 
ATOM   2460 O OD2 . ASP A 1 326 ? -25.98743 76.13030 43.39972 1.000 102.07863 ? 320 ASP A OD2 1 
ATOM   2461 N N   . GLU A 1 327 ? -20.71639 73.91120 45.36789 1.000 86.25216  ? 321 GLU A N   1 
ATOM   2462 C CA  . GLU A 1 327 ? -19.28915 73.72460 45.15456 1.000 79.22266  ? 321 GLU A CA  1 
ATOM   2463 C C   . GLU A 1 327 ? -18.76774 72.40122 45.69249 1.000 82.88686  ? 321 GLU A C   1 
ATOM   2464 O O   . GLU A 1 327 ? -17.61978 72.04948 45.40118 1.000 88.44699  ? 321 GLU A O   1 
ATOM   2465 C CB  . GLU A 1 327 ? -18.48804 74.86398 45.80516 1.000 89.60977  ? 321 GLU A CB  1 
ATOM   2466 C CG  . GLU A 1 327 ? -18.79673 76.24971 45.26739 1.000 112.82018 ? 321 GLU A CG  1 
ATOM   2467 C CD  . GLU A 1 327 ? -17.96840 77.32642 45.94027 1.000 114.46993 ? 321 GLU A CD  1 
ATOM   2468 O OE1 . GLU A 1 327 ? -17.23455 76.99844 46.89611 1.000 105.86045 ? 321 GLU A OE1 1 
ATOM   2469 O OE2 . GLU A 1 327 ? -18.04869 78.49817 45.51453 1.000 130.74152 ? 321 GLU A OE2 1 
ATOM   2470 N N   . TYR A 1 328 ? -19.56367 71.66371 46.46213 1.000 69.87341  ? 322 TYR A N   1 
ATOM   2471 C CA  . TYR A 1 328 ? -19.14141 70.41887 47.08370 1.000 68.58329  ? 322 TYR A CA  1 
ATOM   2472 C C   . TYR A 1 328 ? -20.32646 69.46890 47.13679 1.000 78.66658  ? 322 TYR A C   1 
ATOM   2473 O O   . TYR A 1 328 ? -21.43637 69.87192 47.49544 1.000 77.59411  ? 322 TYR A O   1 
ATOM   2474 C CB  . TYR A 1 328 ? -18.59442 70.66732 48.49627 1.000 65.23917  ? 322 TYR A CB  1 
ATOM   2475 C CG  . TYR A 1 328 ? -18.34469 69.41804 49.31326 1.000 72.23850  ? 322 TYR A CG  1 
ATOM   2476 C CD1 . TYR A 1 328 ? -17.20160 68.65555 49.11846 1.000 69.59364  ? 322 TYR A CD1 1 
ATOM   2477 C CD2 . TYR A 1 328 ? -19.24263 69.01287 50.29389 1.000 75.49955  ? 322 TYR A CD2 1 
ATOM   2478 C CE1 . TYR A 1 328 ? -16.96390 67.51808 49.86717 1.000 76.57360  ? 322 TYR A CE1 1 
ATOM   2479 C CE2 . TYR A 1 328 ? -19.01351 67.87356 51.04820 1.000 75.25510  ? 322 TYR A CE2 1 
ATOM   2480 C CZ  . TYR A 1 328 ? -17.87199 67.13173 50.83043 1.000 81.26674  ? 322 TYR A CZ  1 
ATOM   2481 O OH  . TYR A 1 328 ? -17.63663 65.99875 51.57661 1.000 85.82222  ? 322 TYR A OH  1 
ATOM   2482 N N   . VAL A 1 329 ? -20.08997 68.21112 46.77347 1.000 76.17003  ? 323 VAL A N   1 
ATOM   2483 C CA  . VAL A 1 329 ? -21.11695 67.17768 46.80664 1.000 66.74813  ? 323 VAL A CA  1 
ATOM   2484 C C   . VAL A 1 329 ? -20.57574 65.97766 47.57069 1.000 63.86244  ? 323 VAL A C   1 
ATOM   2485 O O   . VAL A 1 329 ? -19.41666 65.58496 47.39550 1.000 67.34988  ? 323 VAL A O   1 
ATOM   2486 C CB  . VAL A 1 329 ? -21.57445 66.77382 45.38711 1.000 65.93124  ? 323 VAL A CB  1 
ATOM   2487 C CG1 . VAL A 1 329 ? -20.39614 66.31873 44.54853 1.000 74.16080  ? 323 VAL A CG1 1 
ATOM   2488 C CG2 . VAL A 1 329 ? -22.64627 65.69170 45.45172 1.000 64.80878  ? 323 VAL A CG2 1 
ATOM   2489 N N   . HIS A 1 330 ? -21.41747 65.40286 48.42739 1.000 75.68234  ? 324 HIS A N   1 
ATOM   2490 C CA  . HIS A 1 330 ? -21.04448 64.28488 49.28842 1.000 59.93199  ? 324 HIS A CA  1 
ATOM   2491 C C   . HIS A 1 330 ? -22.09552 63.19567 49.13544 1.000 70.19668  ? 324 HIS A C   1 
ATOM   2492 O O   . HIS A 1 330 ? -23.22688 63.34810 49.60814 1.000 88.75762  ? 324 HIS A O   1 
ATOM   2493 C CB  . HIS A 1 330 ? -20.92738 64.73408 50.74508 1.000 67.99948  ? 324 HIS A CB  1 
ATOM   2494 C CG  . HIS A 1 330 ? -20.75662 63.61025 51.72041 1.000 71.66056  ? 324 HIS A CG  1 
ATOM   2495 N ND1 . HIS A 1 330 ? -19.51966 63.16973 52.13941 1.000 66.64334  ? 324 HIS A ND1 1 
ATOM   2496 C CD2 . HIS A 1 330 ? -21.66750 62.85022 52.37438 1.000 73.23936  ? 324 HIS A CD2 1 
ATOM   2497 C CE1 . HIS A 1 330 ? -19.67529 62.18340 53.00421 1.000 64.48718  ? 324 HIS A CE1 1 
ATOM   2498 N NE2 . HIS A 1 330 ? -20.96888 61.96880 53.16325 1.000 76.11032  ? 324 HIS A NE2 1 
ATOM   2499 N N   . ILE A 1 331 ? -21.72374 62.10451 48.47436 1.000 58.44243  ? 325 ILE A N   1 
ATOM   2500 C CA  . ILE A 1 331 ? -22.59771 60.95726 48.26918 1.000 57.19551  ? 325 ILE A CA  1 
ATOM   2501 C C   . ILE A 1 331 ? -21.99832 59.77629 49.01573 1.000 65.08866  ? 325 ILE A C   1 
ATOM   2502 O O   . ILE A 1 331 ? -20.81918 59.45557 48.82832 1.000 72.21595  ? 325 ILE A O   1 
ATOM   2503 C CB  . ILE A 1 331 ? -22.76439 60.63569 46.77419 1.000 60.71223  ? 325 ILE A CB  1 
ATOM   2504 C CG1 . ILE A 1 331 ? -23.38837 61.82684 46.04467 1.000 58.44199  ? 325 ILE A CG1 1 
ATOM   2505 C CG2 . ILE A 1 331 ? -23.59745 59.38358 46.59584 1.000 55.11490  ? 325 ILE A CG2 1 
ATOM   2506 C CD1 . ILE A 1 331 ? -23.46332 61.65393 44.54993 1.000 64.50807  ? 325 ILE A CD1 1 
ATOM   2507 N N   . THR A 1 332 ? -22.80336 59.13059 49.85702 1.000 63.45005  ? 326 THR A N   1 
ATOM   2508 C CA  . THR A 1 332 ? -22.29232 58.09346 50.74222 1.000 62.47910  ? 326 THR A CA  1 
ATOM   2509 C C   . THR A 1 332 ? -23.34971 57.01175 50.92695 1.000 70.70698  ? 326 THR A C   1 
ATOM   2510 O O   . THR A 1 332 ? -24.44292 57.07421 50.35751 1.000 77.77888  ? 326 THR A O   1 
ATOM   2511 C CB  . THR A 1 332 ? -21.87743 58.68619 52.09144 1.000 70.97597  ? 326 THR A CB  1 
ATOM   2512 O OG1 . THR A 1 332 ? -21.29490 57.66240 52.90646 1.000 74.83594  ? 326 THR A OG1 1 
ATOM   2513 C CG2 . THR A 1 332 ? -23.08750 59.26852 52.80727 1.000 62.20515  ? 326 THR A CG2 1 
ATOM   2514 N N   . SER A 1 333 ? -23.00552 56.00303 51.73014 1.000 64.30028  ? 327 SER A N   1 
ATOM   2515 C CA  . SER A 1 333 ? -23.94900 54.97165 52.13477 1.000 59.63811  ? 327 SER A CA  1 
ATOM   2516 C C   . SER A 1 333 ? -24.34813 55.07773 53.59644 1.000 57.44114  ? 327 SER A C   1 
ATOM   2517 O O   . SER A 1 333 ? -25.28498 54.39046 54.01791 1.000 72.77129  ? 327 SER A O   1 
ATOM   2518 C CB  . SER A 1 333 ? -23.36718 53.57394 51.87946 1.000 55.66779  ? 327 SER A CB  1 
ATOM   2519 O OG  . SER A 1 333 ? -22.34915 53.26261 52.81507 1.000 80.73162  ? 327 SER A OG  1 
ATOM   2520 N N   . ALA A 1 334 ? -23.66523 55.90684 54.37449 1.000 61.98610  ? 328 ALA A N   1 
ATOM   2521 C CA  . ALA A 1 334 ? -23.97727 56.07981 55.78149 1.000 61.79158  ? 328 ALA A CA  1 
ATOM   2522 C C   . ALA A 1 334 ? -24.96637 57.22145 55.97522 1.000 73.09487  ? 328 ALA A C   1 
ATOM   2523 O O   . ALA A 1 334 ? -25.09653 58.11745 55.13827 1.000 74.88815  ? 328 ALA A O   1 
ATOM   2524 C CB  . ALA A 1 334 ? -22.70818 56.34953 56.58534 1.000 63.43617  ? 328 ALA A CB  1 
ATOM   2525 N N   . ASN A 1 335 ? -25.67050 57.17289 57.09866 1.000 68.86759  ? 329 ASN A N   1 
ATOM   2526 C CA  . ASN A 1 335 ? -26.60951 58.21249 57.48408 1.000 64.71517  ? 329 ASN A CA  1 
ATOM   2527 C C   . ASN A 1 335 ? -25.95095 59.14794 58.49119 1.000 72.11117  ? 329 ASN A C   1 
ATOM   2528 O O   . ASN A 1 335 ? -25.09591 58.73768 59.28029 1.000 73.26030  ? 329 ASN A O   1 
ATOM   2529 C CB  . ASN A 1 335 ? -27.88154 57.59776 58.07395 1.000 63.34965  ? 329 ASN A CB  1 
ATOM   2530 C CG  . ASN A 1 335 ? -28.94853 58.63081 58.37257 1.000 71.58560  ? 329 ASN A CG  1 
ATOM   2531 O OD1 . ASN A 1 335 ? -29.57090 59.17985 57.46334 1.000 77.89929  ? 329 ASN A OD1 1 
ATOM   2532 N ND2 . ASN A 1 335 ? -29.17568 58.89091 59.65458 1.000 76.50038  ? 329 ASN A ND2 1 
ATOM   2533 N N   . PHE A 1 336 ? -26.35109 60.41845 58.45075 1.000 66.51291  ? 330 PHE A N   1 
ATOM   2534 C CA  . PHE A 1 336 ? -25.76664 61.44695 59.31208 1.000 66.52899  ? 330 PHE A CA  1 
ATOM   2535 C C   . PHE A 1 336 ? -26.27046 61.26933 60.74322 1.000 64.07850  ? 330 PHE A C   1 
ATOM   2536 O O   . PHE A 1 336 ? -27.16310 61.97525 61.21806 1.000 72.63089  ? 330 PHE A O   1 
ATOM   2537 C CB  . PHE A 1 336 ? -26.09751 62.83753 58.78108 1.000 63.20255  ? 330 PHE A CB  1 
ATOM   2538 C CG  . PHE A 1 336 ? -25.31166 63.22836 57.55914 1.000 71.83835  ? 330 PHE A CG  1 
ATOM   2539 C CD1 . PHE A 1 336 ? -24.10418 62.61573 57.26628 1.000 65.54420  ? 330 PHE A CD1 1 
ATOM   2540 C CD2 . PHE A 1 336 ? -25.77812 64.21743 56.70803 1.000 70.70536  ? 330 PHE A CD2 1 
ATOM   2541 C CE1 . PHE A 1 336 ? -23.37952 62.98067 56.14435 1.000 60.84617  ? 330 PHE A CE1 1 
ATOM   2542 C CE2 . PHE A 1 336 ? -25.05864 64.58662 55.58722 1.000 63.25574  ? 330 PHE A CE2 1 
ATOM   2543 C CZ  . PHE A 1 336 ? -23.85838 63.96717 55.30442 1.000 73.12685  ? 330 PHE A CZ  1 
ATOM   2544 N N   . ASP A 1 337 ? -25.67021 60.31493 61.45354 1.000 64.44525  ? 331 ASP A N   1 
ATOM   2545 C CA  . ASP A 1 337 ? -26.00616 60.09525 62.85389 1.000 72.38840  ? 331 ASP A CA  1 
ATOM   2546 C C   . ASP A 1 337 ? -24.79999 59.51316 63.58030 1.000 70.30042  ? 331 ASP A C   1 
ATOM   2547 O O   . ASP A 1 337 ? -23.78498 59.16774 62.97023 1.000 74.78055  ? 331 ASP A O   1 
ATOM   2548 C CB  . ASP A 1 337 ? -27.23362 59.18834 63.00037 1.000 79.09569  ? 331 ASP A CB  1 
ATOM   2549 C CG  . ASP A 1 337 ? -27.03365 57.82666 62.37212 1.000 77.14091  ? 331 ASP A CG  1 
ATOM   2550 O OD1 . ASP A 1 337 ? -25.94688 57.58422 61.81630 1.000 96.72848  ? 331 ASP A OD1 1 
ATOM   2551 O OD2 . ASP A 1 337 ? -27.96467 56.99803 62.42957 1.000 85.03674  ? 331 ASP A OD2 1 
ATOM   2552 N N   . GLY A 1 338 ? -24.93646 59.38709 64.90193 1.000 87.54877  ? 332 GLY A N   1 
ATOM   2553 C CA  . GLY A 1 338 ? -23.79838 59.00384 65.72259 1.000 75.88831  ? 332 GLY A CA  1 
ATOM   2554 C C   . GLY A 1 338 ? -23.39758 57.55219 65.55676 1.000 68.58474  ? 332 GLY A C   1 
ATOM   2555 O O   . GLY A 1 338 ? -22.20647 57.22875 65.52714 1.000 82.32608  ? 332 GLY A O   1 
ATOM   2556 N N   . THR A 1 339 ? -24.38140 56.65806 65.45697 1.000 73.69018  ? 333 THR A N   1 
ATOM   2557 C CA  . THR A 1 339 ? -24.07976 55.23964 65.30303 1.000 72.50532  ? 333 THR A CA  1 
ATOM   2558 C C   . THR A 1 339 ? -23.23923 54.98893 64.05757 1.000 76.79851  ? 333 THR A C   1 
ATOM   2559 O O   . THR A 1 339 ? -22.25356 54.24351 64.09823 1.000 74.69819  ? 333 THR A O   1 
ATOM   2560 C CB  . THR A 1 339 ? -25.37570 54.43656 65.24515 1.000 76.24563  ? 333 THR A CB  1 
ATOM   2561 O OG1 . THR A 1 339 ? -26.13945 54.68201 66.43175 1.000 95.18298  ? 333 THR A OG1 1 
ATOM   2562 C CG2 . THR A 1 339 ? -25.06941 52.95809 65.14041 1.000 65.97559  ? 333 THR A CG2 1 
ATOM   2563 N N   . HIS A 1 340 ? -23.60972 55.61575 62.93977 1.000 77.22753  ? 334 HIS A N   1 
ATOM   2564 C CA  . HIS A 1 340 ? -22.86978 55.42261 61.69678 1.000 69.95501  ? 334 HIS A CA  1 
ATOM   2565 C C   . HIS A 1 340 ? -21.47884 56.03968 61.77699 1.000 73.62528  ? 334 HIS A C   1 
ATOM   2566 O O   . HIS A 1 340 ? -20.46555 55.34255 61.64507 1.000 71.61345  ? 334 HIS A O   1 
ATOM   2567 C CB  . HIS A 1 340 ? -23.64574 56.01980 60.52208 1.000 59.50913  ? 334 HIS A CB  1 
ATOM   2568 C CG  . HIS A 1 340 ? -24.80221 55.18534 60.07060 1.000 64.37351  ? 334 HIS A CG  1 
ATOM   2569 N ND1 . HIS A 1 340 ? -24.79647 54.49510 58.87824 1.000 75.41833  ? 334 HIS A ND1 1 
ATOM   2570 C CD2 . HIS A 1 340 ? -26.00030 54.93004 60.64750 1.000 68.66340  ? 334 HIS A CD2 1 
ATOM   2571 C CE1 . HIS A 1 340 ? -25.94113 53.85068 58.73948 1.000 74.92406  ? 334 HIS A CE1 1 
ATOM   2572 N NE2 . HIS A 1 340 ? -26.68965 54.09858 59.79907 1.000 81.59755  ? 334 HIS A NE2 1 
ATOM   2573 N N   . TYR A 1 341 ? -21.40882 57.35227 61.99883 1.000 70.85365  ? 335 TYR A N   1 
ATOM   2574 C CA  . TYR A 1 341 ? -20.14583 58.06478 61.83698 1.000 77.82348  ? 335 TYR A CA  1 
ATOM   2575 C C   . TYR A 1 341 ? -19.15189 57.82191 62.96416 1.000 71.86417  ? 335 TYR A C   1 
ATOM   2576 O O   . TYR A 1 341 ? -18.10146 58.47312 62.98225 1.000 92.82235  ? 335 TYR A O   1 
ATOM   2577 C CB  . TYR A 1 341 ? -20.41609 59.56095 61.67401 1.000 61.47621  ? 335 TYR A CB  1 
ATOM   2578 C CG  . TYR A 1 341 ? -20.59240 59.92986 60.22219 1.000 67.79051  ? 335 TYR A CG  1 
ATOM   2579 C CD1 . TYR A 1 341 ? -21.77182 59.63602 59.55250 1.000 66.56143  ? 335 TYR A CD1 1 
ATOM   2580 C CD2 . TYR A 1 341 ? -19.56395 60.53069 59.50850 1.000 71.73065  ? 335 TYR A CD2 1 
ATOM   2581 C CE1 . TYR A 1 341 ? -21.93057 59.94845 58.21965 1.000 66.44573  ? 335 TYR A CE1 1 
ATOM   2582 C CE2 . TYR A 1 341 ? -19.71382 60.84895 58.17439 1.000 78.89612  ? 335 TYR A CE2 1 
ATOM   2583 C CZ  . TYR A 1 341 ? -20.89943 60.55529 57.53505 1.000 72.40601  ? 335 TYR A CZ  1 
ATOM   2584 O OH  . TYR A 1 341 ? -21.05710 60.86958 56.20465 1.000 81.43334  ? 335 TYR A OH  1 
ATOM   2585 N N   . GLN A 1 342 ? -19.42975 56.90189 63.88400 1.000 74.67985  ? 336 GLN A N   1 
ATOM   2586 C CA  . GLN A 1 342 ? -18.47680 56.55158 64.92293 1.000 65.67715  ? 336 GLN A CA  1 
ATOM   2587 C C   . GLN A 1 342 ? -18.17784 55.06368 65.00717 1.000 67.48234  ? 336 GLN A C   1 
ATOM   2588 O O   . GLN A 1 342 ? -17.28222 54.67808 65.76767 1.000 76.18053  ? 336 GLN A O   1 
ATOM   2589 C CB  . GLN A 1 342 ? -18.96950 57.03851 66.29469 1.000 65.35488  ? 336 GLN A CB  1 
ATOM   2590 C CG  . GLN A 1 342 ? -18.78814 58.52894 66.52217 1.000 79.79898  ? 336 GLN A CG  1 
ATOM   2591 C CD  . GLN A 1 342 ? -18.81777 58.89433 67.98952 1.000 93.17111  ? 336 GLN A CD  1 
ATOM   2592 O OE1 . GLN A 1 342 ? -19.43435 58.20295 68.79941 1.000 99.43912  ? 336 GLN A OE1 1 
ATOM   2593 N NE2 . GLN A 1 342 ? -18.13923 59.97976 68.34344 1.000 104.09864 ? 336 GLN A NE2 1 
ATOM   2594 N N   . ASN A 1 343 ? -18.87881 54.22051 64.24940 1.000 70.48238  ? 337 ASN A N   1 
ATOM   2595 C CA  . ASN A 1 343 ? -18.68140 52.78269 64.37805 1.000 85.09556  ? 337 ASN A CA  1 
ATOM   2596 C C   . ASN A 1 343 ? -18.61845 52.07545 63.02934 1.000 68.96914  ? 337 ASN A C   1 
ATOM   2597 O O   . ASN A 1 343 ? -17.86415 51.11149 62.86419 1.000 82.11662  ? 337 ASN A O   1 
ATOM   2598 C CB  . ASN A 1 343 ? -19.79798 52.17506 65.22999 1.000 74.37902  ? 337 ASN A CB  1 
ATOM   2599 C CG  . ASN A 1 343 ? -19.88080 52.79265 66.61003 1.000 82.24767  ? 337 ASN A CG  1 
ATOM   2600 O OD1 . ASN A 1 343 ? -18.89535 52.83554 67.34588 1.000 94.86337  ? 337 ASN A OD1 1 
ATOM   2601 N ND2 . ASN A 1 343 ? -21.05868 53.28956 66.96270 1.000 98.74347  ? 337 ASN A ND2 1 
ATOM   2602 N N   . HIS A 1 344 ? -19.39910 52.54323 62.06353 1.000 70.37700  ? 338 HIS A N   1 
ATOM   2603 C CA  . HIS A 1 344 ? -19.62374 51.80155 60.83252 1.000 86.24601  ? 338 HIS A CA  1 
ATOM   2604 C C   . HIS A 1 344 ? -18.51630 52.04040 59.81427 1.000 73.93314  ? 338 HIS A C   1 
ATOM   2605 O O   . HIS A 1 344 ? -17.92834 53.12271 59.73952 1.000 78.51446  ? 338 HIS A O   1 
ATOM   2606 C CB  . HIS A 1 344 ? -20.98158 52.16854 60.23329 1.000 75.96745  ? 338 HIS A CB  1 
ATOM   2607 C CG  . HIS A 1 344 ? -22.14043 51.67463 61.04163 1.000 74.67062  ? 338 HIS A CG  1 
ATOM   2608 N ND1 . HIS A 1 344 ? -22.00376 50.71590 62.02288 1.000 71.64972  ? 338 HIS A ND1 1 
ATOM   2609 C CD2 . HIS A 1 344 ? -23.45244 52.00754 61.02153 1.000 74.02775  ? 338 HIS A CD2 1 
ATOM   2610 C CE1 . HIS A 1 344 ? -23.18200 50.47716 62.57008 1.000 75.23774  ? 338 HIS A CE1 1 
ATOM   2611 N NE2 . HIS A 1 344 ? -24.07818 51.24796 61.98072 1.000 81.35828  ? 338 HIS A NE2 1 
ATOM   2612 N N   . GLY A 1 345 ? -18.23840 51.00182 59.02819 1.000 64.70767  ? 339 GLY A N   1 
ATOM   2613 C CA  . GLY A 1 345 ? -17.20525 51.04883 58.01398 1.000 63.76284  ? 339 GLY A CA  1 
ATOM   2614 C C   . GLY A 1 345 ? -17.76038 51.29188 56.62817 1.000 69.04410  ? 339 GLY A C   1 
ATOM   2615 O O   . GLY A 1 345 ? -18.47165 50.44935 56.07246 1.000 69.99054  ? 339 GLY A O   1 
ATOM   2616 N N   . PHE A 1 346 ? -17.43748 52.44944 56.06183 1.000 67.10403  ? 340 PHE A N   1 
ATOM   2617 C CA  . PHE A 1 346 ? -17.93240 52.83505 54.75109 1.000 68.34756  ? 340 PHE A CA  1 
ATOM   2618 C C   . PHE A 1 346 ? -16.91273 53.75756 54.10052 1.000 72.55488  ? 340 PHE A C   1 
ATOM   2619 O O   . PHE A 1 346 ? -15.94873 54.19767 54.73127 1.000 78.02545  ? 340 PHE A O   1 
ATOM   2620 C CB  . PHE A 1 346 ? -19.30333 53.51424 54.85030 1.000 66.63468  ? 340 PHE A CB  1 
ATOM   2621 C CG  . PHE A 1 346 ? -19.34396 54.65592 55.82736 1.000 68.26974  ? 340 PHE A CG  1 
ATOM   2622 C CD1 . PHE A 1 346 ? -19.65555 54.43603 57.16029 1.000 67.53302  ? 340 PHE A CD1 1 
ATOM   2623 C CD2 . PHE A 1 346 ? -19.06934 55.94868 55.41350 1.000 67.27526  ? 340 PHE A CD2 1 
ATOM   2624 C CE1 . PHE A 1 346 ? -19.69079 55.48517 58.06109 1.000 66.14765  ? 340 PHE A CE1 1 
ATOM   2625 C CE2 . PHE A 1 346 ? -19.10403 57.00128 56.30730 1.000 67.07323  ? 340 PHE A CE2 1 
ATOM   2626 C CZ  . PHE A 1 346 ? -19.41729 56.77087 57.63197 1.000 66.34747  ? 340 PHE A CZ  1 
ATOM   2627 N N   . VAL A 1 347 ? -17.13044 54.03839 52.81997 1.000 70.41858  ? 341 VAL A N   1 
ATOM   2628 C CA  . VAL A 1 347 ? -16.32501 54.99558 52.07378 1.000 75.93023  ? 341 VAL A CA  1 
ATOM   2629 C C   . VAL A 1 347 ? -17.26986 55.98053 51.40132 1.000 74.54911  ? 341 VAL A C   1 
ATOM   2630 O O   . VAL A 1 347 ? -18.28888 55.58424 50.82403 1.000 63.70592  ? 341 VAL A O   1 
ATOM   2631 C CB  . VAL A 1 347 ? -15.40828 54.30025 51.04243 1.000 77.84432  ? 341 VAL A CB  1 
ATOM   2632 C CG1 . VAL A 1 347 ? -16.19096 53.28913 50.22129 1.000 69.11179  ? 341 VAL A CG1 1 
ATOM   2633 C CG2 . VAL A 1 347 ? -14.73036 55.32779 50.14631 1.000 66.72189  ? 341 VAL A CG2 1 
ATOM   2634 N N   . SER A 1 348 ? -16.94083 57.26544 51.49324 1.000 73.49680  ? 342 SER A N   1 
ATOM   2635 C CA  . SER A 1 348 ? -17.80069 58.33829 51.01515 1.000 63.47913  ? 342 SER A CA  1 
ATOM   2636 C C   . SER A 1 348 ? -17.18313 59.00182 49.79265 1.000 73.16767  ? 342 SER A C   1 
ATOM   2637 O O   . SER A 1 348 ? -15.98835 59.31910 49.78641 1.000 80.86752  ? 342 SER A O   1 
ATOM   2638 C CB  . SER A 1 348 ? -18.03662 59.37630 52.11376 1.000 73.03783  ? 342 SER A CB  1 
ATOM   2639 O OG  . SER A 1 348 ? -18.78650 58.82635 53.18337 1.000 83.72766  ? 342 SER A OG  1 
ATOM   2640 N N   . PHE A 1 349 ? -18.00466 59.21425 48.76803 1.000 70.67965  ? 343 PHE A N   1 
ATOM   2641 C CA  . PHE A 1 349 ? -17.57799 59.91906 47.56828 1.000 57.74516  ? 343 PHE A CA  1 
ATOM   2642 C C   . PHE A 1 349 ? -17.64528 61.42226 47.80210 1.000 73.45643  ? 343 PHE A C   1 
ATOM   2643 O O   . PHE A 1 349 ? -18.67207 61.94468 48.24813 1.000 72.32162  ? 343 PHE A O   1 
ATOM   2644 C CB  . PHE A 1 349 ? -18.45996 59.52277 46.38245 1.000 70.94048  ? 343 PHE A CB  1 
ATOM   2645 C CG  . PHE A 1 349 ? -18.23074 60.34797 45.14368 1.000 74.36081  ? 343 PHE A CG  1 
ATOM   2646 C CD1 . PHE A 1 349 ? -17.29311 59.96137 44.20102 1.000 71.79502  ? 343 PHE A CD1 1 
ATOM   2647 C CD2 . PHE A 1 349 ? -18.96433 61.50298 44.91550 1.000 67.88855  ? 343 PHE A CD2 1 
ATOM   2648 C CE1 . PHE A 1 349 ? -17.08569 60.71563 43.06111 1.000 76.74082  ? 343 PHE A CE1 1 
ATOM   2649 C CE2 . PHE A 1 349 ? -18.75697 62.26128 43.78189 1.000 62.36064  ? 343 PHE A CE2 1 
ATOM   2650 C CZ  . PHE A 1 349 ? -17.81728 61.86732 42.85331 1.000 74.26616  ? 343 PHE A CZ  1 
ATOM   2651 N N   . ASN A 1 350 ? -16.55264 62.11656 47.49623 1.000 74.21488  ? 344 ASN A N   1 
ATOM   2652 C CA  . ASN A 1 350 ? -16.49318 63.56714 47.59844 1.000 71.87590  ? 344 ASN A CA  1 
ATOM   2653 C C   . ASN A 1 350 ? -15.97881 64.14615 46.29105 1.000 75.15332  ? 344 ASN A C   1 
ATOM   2654 O O   . ASN A 1 350 ? -15.02262 63.62847 45.70619 1.000 81.52181  ? 344 ASN A O   1 
ATOM   2655 C CB  . ASN A 1 350 ? -15.59156 64.01600 48.75262 1.000 63.85104  ? 344 ASN A CB  1 
ATOM   2656 C CG  . ASN A 1 350 ? -16.13025 63.60594 50.10397 1.000 74.16692  ? 344 ASN A CG  1 
ATOM   2657 O OD1 . ASN A 1 350 ? -17.34006 63.50628 50.29830 1.000 118.35981 ? 344 ASN A OD1 1 
ATOM   2658 N ND2 . ASN A 1 350 ? -15.23521 63.36509 51.04693 1.000 81.27348  ? 344 ASN A ND2 1 
ATOM   2659 N N   . SER A 1 351 ? -16.61697 65.22064 45.83525 1.000 73.68010  ? 345 SER A N   1 
ATOM   2660 C CA  . SER A 1 351 ? -16.18399 65.89426 44.62143 1.000 75.10059  ? 345 SER A CA  1 
ATOM   2661 C C   . SER A 1 351 ? -16.44699 67.38577 44.74445 1.000 86.72151  ? 345 SER A C   1 
ATOM   2662 O O   . SER A 1 351 ? -17.45271 67.80160 45.32726 1.000 85.60009  ? 345 SER A O   1 
ATOM   2663 C CB  . SER A 1 351 ? -16.89588 65.34282 43.38434 1.000 71.23338  ? 345 SER A CB  1 
ATOM   2664 O OG  . SER A 1 351 ? -16.48377 66.03490 42.21924 1.000 87.67917  ? 345 SER A OG  1 
ATOM   2665 N N   . ILE A 1 352 ? -15.53210 68.18121 44.19436 1.000 83.79449  ? 346 ILE A N   1 
ATOM   2666 C CA  . ILE A 1 352 ? -15.68998 69.62564 44.10598 1.000 88.38023  ? 346 ILE A CA  1 
ATOM   2667 C C   . ILE A 1 352 ? -15.72424 70.09024 42.65219 1.000 85.52100  ? 346 ILE A C   1 
ATOM   2668 O O   . ILE A 1 352 ? -15.55954 71.27260 42.37342 1.000 85.24236  ? 346 ILE A O   1 
ATOM   2669 C CB  . ILE A 1 352 ? -14.58924 70.35843 44.89487 1.000 78.24965  ? 346 ILE A CB  1 
ATOM   2670 C CG1 . ILE A 1 352 ? -13.21399 70.07463 44.28605 1.000 83.04769  ? 346 ILE A CG1 1 
ATOM   2671 C CG2 . ILE A 1 352 ? -14.62594 69.94478 46.35454 1.000 80.50863  ? 346 ILE A CG2 1 
ATOM   2672 C CD1 . ILE A 1 352 ? -12.08923 70.84708 44.93292 1.000 73.80655  ? 346 ILE A CD1 1 
ATOM   2673 N N   . ASP A 1 353 ? -15.92610 69.16152 41.72104 1.000 77.76750  ? 347 ASP A N   1 
ATOM   2674 C CA  . ASP A 1 353 ? -16.05228 69.51715 40.31445 1.000 85.73552  ? 347 ASP A CA  1 
ATOM   2675 C C   . ASP A 1 353 ? -17.37784 70.23364 40.09266 1.000 97.77302  ? 347 ASP A C   1 
ATOM   2676 O O   . ASP A 1 353 ? -18.44242 69.69472 40.41246 1.000 88.34053  ? 347 ASP A O   1 
ATOM   2677 C CB  . ASP A 1 353 ? -15.95547 68.27090 39.43825 1.000 75.26055  ? 347 ASP A CB  1 
ATOM   2678 C CG  . ASP A 1 353 ? -16.02529 68.59316 37.95932 1.000 87.61002  ? 347 ASP A CG  1 
ATOM   2679 O OD1 . ASP A 1 353 ? -15.12153 69.29716 37.45980 1.000 97.64169  ? 347 ASP A OD1 1 
ATOM   2680 O OD2 . ASP A 1 353 ? -16.98103 68.13958 37.29508 1.000 96.89027  ? 347 ASP A OD2 1 
ATOM   2681 N N   . LYS A 1 354 ? -17.30806 71.44902 39.54240 1.000 112.22380 ? 348 LYS A N   1 
ATOM   2682 C CA  . LYS A 1 354 ? -18.50282 72.27458 39.38703 1.000 100.45996 ? 348 LYS A CA  1 
ATOM   2683 C C   . LYS A 1 354 ? -19.57101 71.56818 38.56202 1.000 92.65329  ? 348 LYS A C   1 
ATOM   2684 O O   . LYS A 1 354 ? -20.75637 71.59650 38.91361 1.000 89.42629  ? 348 LYS A O   1 
ATOM   2685 C CB  . LYS A 1 354 ? -18.13101 73.61136 38.74502 1.000 119.38368 ? 348 LYS A CB  1 
ATOM   2686 C CG  . LYS A 1 354 ? -17.40376 74.57296 39.67052 1.000 134.23329 ? 348 LYS A CG  1 
ATOM   2687 C CD  . LYS A 1 354 ? -18.35969 75.19056 40.67786 1.000 115.28122 ? 348 LYS A CD  1 
ATOM   2688 C CE  . LYS A 1 354 ? -17.73022 76.38781 41.37083 1.000 122.37083 ? 348 LYS A CE  1 
ATOM   2689 N NZ  . LYS A 1 354 ? -18.73505 77.16636 42.14558 1.000 127.91121 ? 348 LYS A NZ  1 
ATOM   2690 N N   . GLN A 1 355 ? -19.17116 70.92448 37.46368 1.000 94.58439  ? 349 GLN A N   1 
ATOM   2691 C CA  . GLN A 1 355 ? -20.14812 70.27822 36.59381 1.000 95.62118  ? 349 GLN A CA  1 
ATOM   2692 C C   . GLN A 1 355 ? -20.80882 69.09238 37.28302 1.000 95.46027  ? 349 GLN A C   1 
ATOM   2693 O O   . GLN A 1 355 ? -22.01462 68.86886 37.12374 1.000 90.68959  ? 349 GLN A O   1 
ATOM   2694 C CB  . GLN A 1 355 ? -19.48321 69.83967 35.29041 1.000 95.04901  ? 349 GLN A CB  1 
ATOM   2695 C CG  . GLN A 1 355 ? -19.93765 70.63387 34.07869 1.000 126.01482 ? 349 GLN A CG  1 
ATOM   2696 C CD  . GLN A 1 355 ? -21.42270 70.48095 33.80751 1.000 130.65941 ? 349 GLN A CD  1 
ATOM   2697 O OE1 . GLN A 1 355 ? -22.00575 69.42342 34.05216 1.000 116.74290 ? 349 GLN A OE1 1 
ATOM   2698 N NE2 . GLN A 1 355 ? -22.04401 71.54130 33.30301 1.000 118.43731 ? 349 GLN A NE2 1 
ATOM   2699 N N   . LEU A 1 356 ? -20.03824 68.32195 38.05313 1.000 98.77341  ? 350 LEU A N   1 
ATOM   2700 C CA  . LEU A 1 356 ? -20.61005 67.17360 38.74793 1.000 85.49548  ? 350 LEU A CA  1 
ATOM   2701 C C   . LEU A 1 356 ? -21.51715 67.61641 39.89057 1.000 79.03104  ? 350 LEU A C   1 
ATOM   2702 O O   . LEU A 1 356 ? -22.58125 67.02516 40.11013 1.000 82.86451  ? 350 LEU A O   1 
ATOM   2703 C CB  . LEU A 1 356 ? -19.49259 66.26310 39.25618 1.000 92.14222  ? 350 LEU A CB  1 
ATOM   2704 C CG  . LEU A 1 356 ? -19.90770 64.95146 39.92324 1.000 86.58427  ? 350 LEU A CG  1 
ATOM   2705 C CD1 . LEU A 1 356 ? -20.93041 64.21647 39.07267 1.000 71.28626  ? 350 LEU A CD1 1 
ATOM   2706 C CD2 . LEU A 1 356 ? -18.68333 64.08170 40.16328 1.000 100.54909 ? 350 LEU A CD2 1 
ATOM   2707 N N   . VAL A 1 357 ? -21.11601 68.65671 40.62598 1.000 81.12539  ? 351 VAL A N   1 
ATOM   2708 C CA  . VAL A 1 357 ? -21.97763 69.20915 41.66864 1.000 71.96524  ? 351 VAL A CA  1 
ATOM   2709 C C   . VAL A 1 357 ? -23.27147 69.73517 41.06005 1.000 79.21847  ? 351 VAL A C   1 
ATOM   2710 O O   . VAL A 1 357 ? -24.35136 69.61117 41.65167 1.000 78.17879  ? 351 VAL A O   1 
ATOM   2711 C CB  . VAL A 1 357 ? -21.23055 70.30533 42.45365 1.000 80.08181  ? 351 VAL A CB  1 
ATOM   2712 C CG1 . VAL A 1 357 ? -22.16301 70.98743 43.44263 1.000 78.20852  ? 351 VAL A CG1 1 
ATOM   2713 C CG2 . VAL A 1 357 ? -20.03216 69.71594 43.17411 1.000 83.75714  ? 351 VAL A CG2 1 
ATOM   2714 N N   . SER A 1 358 ? -23.18281 70.32418 39.86456 1.000 90.73325  ? 352 SER A N   1 
ATOM   2715 C CA  . SER A 1 358 ? -24.37133 70.83640 39.18798 1.000 82.26520  ? 352 SER A CA  1 
ATOM   2716 C C   . SER A 1 358 ? -25.38260 69.72511 38.92918 1.000 85.24519  ? 352 SER A C   1 
ATOM   2717 O O   . SER A 1 358 ? -26.58250 69.89028 39.17863 1.000 77.12776  ? 352 SER A O   1 
ATOM   2718 C CB  . SER A 1 358 ? -23.97253 71.51416 37.87704 1.000 81.94827  ? 352 SER A CB  1 
ATOM   2719 O OG  . SER A 1 358 ? -25.11617 71.93282 37.15283 1.000 104.53500 ? 352 SER A OG  1 
ATOM   2720 N N   . GLU A 1 359 ? -24.91330 68.58079 38.42526 1.000 85.87060  ? 353 GLU A N   1 
ATOM   2721 C CA  . GLU A 1 359 ? -25.81403 67.46130 38.16493 1.000 78.44119  ? 353 GLU A CA  1 
ATOM   2722 C C   . GLU A 1 359 ? -26.46164 66.95748 39.45030 1.000 78.08063  ? 353 GLU A C   1 
ATOM   2723 O O   . GLU A 1 359 ? -27.62517 66.53731 39.44638 1.000 80.18852  ? 353 GLU A O   1 
ATOM   2724 C CB  . GLU A 1 359 ? -25.05570 66.33167 37.46911 1.000 72.58555  ? 353 GLU A CB  1 
ATOM   2725 C CG  . GLU A 1 359 ? -24.52828 66.68795 36.08985 1.000 78.59439  ? 353 GLU A CG  1 
ATOM   2726 C CD  . GLU A 1 359 ? -25.61789 66.72824 35.03425 1.000 100.14656 ? 353 GLU A CD  1 
ATOM   2727 O OE1 . GLU A 1 359 ? -26.77337 66.37128 35.34821 1.000 98.19695  ? 353 GLU A OE1 1 
ATOM   2728 O OE2 . GLU A 1 359 ? -25.31606 67.11472 33.88555 1.000 108.70368 ? 353 GLU A OE2 1 
ATOM   2729 N N   . ALA A 1 360 ? -25.72341 66.98909 40.56178 1.000 70.08666  ? 354 ALA A N   1 
ATOM   2730 C CA  . ALA A 1 360 ? -26.29630 66.56739 41.83676 1.000 67.27626  ? 354 ALA A CA  1 
ATOM   2731 C C   . ALA A 1 360 ? -27.33443 67.56574 42.33288 1.000 75.00266  ? 354 ALA A C   1 
ATOM   2732 O O   . ALA A 1 360 ? -28.37262 67.17132 42.87827 1.000 76.12846  ? 354 ALA A O   1 
ATOM   2733 C CB  . ALA A 1 360 ? -25.19349 66.38275 42.87871 1.000 58.80724  ? 354 ALA A CB  1 
ATOM   2734 N N   . LYS A 1 361 ? -27.06631 68.86362 42.16339 1.000 78.88581  ? 355 LYS A N   1 
ATOM   2735 C CA  . LYS A 1 361 ? -28.05168 69.87714 42.52653 1.000 71.82970  ? 355 LYS A CA  1 
ATOM   2736 C C   . LYS A 1 361 ? -29.34166 69.68847 41.73835 1.000 74.07176  ? 355 LYS A C   1 
ATOM   2737 O O   . LYS A 1 361 ? -30.44054 69.86646 42.27580 1.000 81.72767  ? 355 LYS A O   1 
ATOM   2738 C CB  . LYS A 1 361 ? -27.47502 71.27293 42.29106 1.000 67.53810  ? 355 LYS A CB  1 
ATOM   2739 C CG  . LYS A 1 361 ? -28.30731 72.40890 42.86688 1.000 82.27422  ? 355 LYS A CG  1 
ATOM   2740 C CD  . LYS A 1 361 ? -28.06986 72.56862 44.35848 1.000 84.10945  ? 355 LYS A CD  1 
ATOM   2741 C CE  . LYS A 1 361 ? -28.76374 73.81036 44.89622 1.000 102.59821 ? 355 LYS A CE  1 
ATOM   2742 N NZ  . LYS A 1 361 ? -28.36074 74.10194 46.30011 1.000 109.82500 ? 355 LYS A NZ  1 
ATOM   2743 N N   . LYS A 1 362 ? -29.22500 69.31765 40.46131 1.000 76.28028  ? 356 LYS A N   1 
ATOM   2744 C CA  . LYS A 1 362 ? -30.40750 69.02669 39.65730 1.000 75.48663  ? 356 LYS A CA  1 
ATOM   2745 C C   . LYS A 1 362 ? -31.19137 67.85520 40.23923 1.000 79.74239  ? 356 LYS A C   1 
ATOM   2746 O O   . LYS A 1 362 ? -32.42851 67.85382 40.22082 1.000 80.41749  ? 356 LYS A O   1 
ATOM   2747 C CB  . LYS A 1 362 ? -29.99100 68.74152 38.21293 1.000 75.91287  ? 356 LYS A CB  1 
ATOM   2748 C CG  . LYS A 1 362 ? -31.14207 68.49717 37.25310 1.000 104.20068 ? 356 LYS A CG  1 
ATOM   2749 C CD  . LYS A 1 362 ? -30.62367 68.18090 35.85682 1.000 114.89880 ? 356 LYS A CD  1 
ATOM   2750 C CE  . LYS A 1 362 ? -31.75998 67.89116 34.88927 1.000 101.30162 ? 356 LYS A CE  1 
ATOM   2751 N NZ  . LYS A 1 362 ? -31.25300 67.57799 33.52346 1.000 101.79280 ? 356 LYS A NZ  1 
ATOM   2752 N N   . ILE A 1 363 ? -30.48652 66.85452 40.77423 1.000 79.86573  ? 357 ILE A N   1 
ATOM   2753 C CA  . ILE A 1 363 ? -31.15662 65.71279 41.39441 1.000 66.34720  ? 357 ILE A CA  1 
ATOM   2754 C C   . ILE A 1 363 ? -31.93772 66.15712 42.62612 1.000 84.46729  ? 357 ILE A C   1 
ATOM   2755 O O   . ILE A 1 363 ? -33.11426 65.81271 42.79479 1.000 82.31340  ? 357 ILE A O   1 
ATOM   2756 C CB  . ILE A 1 363 ? -30.13761 64.61377 41.74528 1.000 68.60965  ? 357 ILE A CB  1 
ATOM   2757 C CG1 . ILE A 1 363 ? -29.52389 64.02033 40.47741 1.000 62.15861  ? 357 ILE A CG1 1 
ATOM   2758 C CG2 . ILE A 1 363 ? -30.79398 63.52744 42.57683 1.000 71.39083  ? 357 ILE A CG2 1 
ATOM   2759 C CD1 . ILE A 1 363 ? -30.51555 63.28021 39.61472 1.000 89.39716  ? 357 ILE A CD1 1 
ATOM   2760 N N   . PHE A 1 364 ? -31.29456 66.92755 43.50913 1.000 69.66930  ? 358 PHE A N   1 
ATOM   2761 C CA  . PHE A 1 364 ? -31.96935 67.34874 44.73372 1.000 74.95755  ? 358 PHE A CA  1 
ATOM   2762 C C   . PHE A 1 364 ? -33.18770 68.21333 44.43141 1.000 85.67157  ? 358 PHE A C   1 
ATOM   2763 O O   . PHE A 1 364 ? -34.23433 68.06639 45.07436 1.000 72.49570  ? 358 PHE A O   1 
ATOM   2764 C CB  . PHE A 1 364 ? -31.00739 68.09910 45.65264 1.000 63.74193  ? 358 PHE A CB  1 
ATOM   2765 C CG  . PHE A 1 364 ? -31.59355 68.40967 46.99825 1.000 70.65891  ? 358 PHE A CG  1 
ATOM   2766 C CD1 . PHE A 1 364 ? -31.50599 67.49193 48.02950 1.000 70.61299  ? 358 PHE A CD1 1 
ATOM   2767 C CD2 . PHE A 1 364 ? -32.25314 69.60588 47.22635 1.000 76.86536  ? 358 PHE A CD2 1 
ATOM   2768 C CE1 . PHE A 1 364 ? -32.05176 67.76478 49.26672 1.000 69.12316  ? 358 PHE A CE1 1 
ATOM   2769 C CE2 . PHE A 1 364 ? -32.80299 69.88421 48.46238 1.000 73.75358  ? 358 PHE A CE2 1 
ATOM   2770 C CZ  . PHE A 1 364 ? -32.70074 68.96219 49.48419 1.000 72.77086  ? 358 PHE A CZ  1 
ATOM   2771 N N   . GLU A 1 365 ? -33.06958 69.12966 43.46719 1.000 81.34690  ? 359 GLU A N   1 
ATOM   2772 C CA  . GLU A 1 365 ? -34.21323 69.95800 43.09822 1.000 70.54004  ? 359 GLU A CA  1 
ATOM   2773 C C   . GLU A 1 365 ? -35.38916 69.09523 42.66023 1.000 78.37027  ? 359 GLU A C   1 
ATOM   2774 O O   . GLU A 1 365 ? -36.53472 69.33742 43.05761 1.000 78.65407  ? 359 GLU A O   1 
ATOM   2775 C CB  . GLU A 1 365 ? -33.82403 70.94013 41.99173 1.000 65.33872  ? 359 GLU A CB  1 
ATOM   2776 C CG  . GLU A 1 365 ? -32.78464 71.97246 42.39682 1.000 69.92621  ? 359 GLU A CG  1 
ATOM   2777 C CD  . GLU A 1 365 ? -33.29282 72.95229 43.43838 1.000 82.81675  ? 359 GLU A CD  1 
ATOM   2778 O OE1 . GLU A 1 365 ? -34.51566 72.98380 43.69799 1.000 80.99414  ? 359 GLU A OE1 1 
ATOM   2779 O OE2 . GLU A 1 365 ? -32.46264 73.69830 43.99700 1.000 80.08194  ? 359 GLU A OE2 1 
ATOM   2780 N N   . ARG A 1 366 ? -35.12022 68.07510 41.84284 1.000 70.06457  ? 360 ARG A N   1 
ATOM   2781 C CA  . ARG A 1 366 ? -36.16531 67.14108 41.43746 1.000 73.94739  ? 360 ARG A CA  1 
ATOM   2782 C C   . ARG A 1 366 ? -36.80044 66.47013 42.65043 1.000 76.19000  ? 360 ARG A C   1 
ATOM   2783 O O   . ARG A 1 366 ? -38.02369 66.49828 42.82856 1.000 80.39119  ? 360 ARG A O   1 
ATOM   2784 C CB  . ARG A 1 366 ? -35.58612 66.08966 40.48800 1.000 70.28931  ? 360 ARG A CB  1 
ATOM   2785 C CG  . ARG A 1 366 ? -36.57147 65.00403 40.08520 1.000 57.68406  ? 360 ARG A CG  1 
ATOM   2786 C CD  . ARG A 1 366 ? -35.84396 63.78515 39.55413 1.000 70.17953  ? 360 ARG A CD  1 
ATOM   2787 N NE  . ARG A 1 366 ? -34.97640 63.19179 40.56468 1.000 71.78108  ? 360 ARG A NE  1 
ATOM   2788 C CZ  . ARG A 1 366 ? -34.07849 62.24669 40.32089 1.000 74.23972  ? 360 ARG A CZ  1 
ATOM   2789 N NH1 . ARG A 1 366 ? -33.89009 61.76979 39.10127 1.000 81.37803  ? 360 ARG A NH1 1 
ATOM   2790 N NH2 . ARG A 1 366 ? -33.34923 61.76997 41.32562 1.000 64.95818  ? 360 ARG A NH2 1 
ATOM   2791 N N   . ASP A 1 367 ? -35.97003 65.85850 43.50008 1.000 78.68932  ? 361 ASP A N   1 
ATOM   2792 C CA  . ASP A 1 367 ? -36.48780 65.14551 44.66404 1.000 76.39420  ? 361 ASP A CA  1 
ATOM   2793 C C   . ASP A 1 367 ? -37.24960 66.07975 45.59528 1.000 79.78610  ? 361 ASP A C   1 
ATOM   2794 O O   . ASP A 1 367 ? -38.24222 65.67744 46.21405 1.000 86.68520  ? 361 ASP A O   1 
ATOM   2795 C CB  . ASP A 1 367 ? -35.34277 64.46263 45.41149 1.000 67.04156  ? 361 ASP A CB  1 
ATOM   2796 C CG  . ASP A 1 367 ? -34.64777 63.40704 44.57287 1.000 80.72573  ? 361 ASP A CG  1 
ATOM   2797 O OD1 . ASP A 1 367 ? -35.11037 63.13971 43.44218 1.000 79.16172  ? 361 ASP A OD1 1 
ATOM   2798 O OD2 . ASP A 1 367 ? -33.63780 62.84270 45.04373 1.000 68.10638  ? 361 ASP A OD2 1 
ATOM   2799 N N   . TRP A 1 368 ? -36.80627 67.33526 45.69872 1.000 83.38654  ? 362 TRP A N   1 
ATOM   2800 C CA  . TRP A 1 368 ? -37.43722 68.27333 46.62324 1.000 77.94607  ? 362 TRP A CA  1 
ATOM   2801 C C   . TRP A 1 368 ? -38.88593 68.55197 46.23554 1.000 72.81758  ? 362 TRP A C   1 
ATOM   2802 O O   . TRP A 1 368 ? -39.75935 68.66241 47.10474 1.000 89.48140  ? 362 TRP A O   1 
ATOM   2803 C CB  . TRP A 1 368 ? -36.63066 69.57197 46.67531 1.000 81.77042  ? 362 TRP A CB  1 
ATOM   2804 C CG  . TRP A 1 368 ? -37.12336 70.55168 47.69088 1.000 81.71111  ? 362 TRP A CG  1 
ATOM   2805 C CD1 . TRP A 1 368 ? -37.79651 71.71232 47.44981 1.000 85.83015  ? 362 TRP A CD1 1 
ATOM   2806 C CD2 . TRP A 1 368 ? -36.98889 70.45337 49.11361 1.000 77.06940  ? 362 TRP A CD2 1 
ATOM   2807 N NE1 . TRP A 1 368 ? -38.08804 72.34441 48.63345 1.000 87.21300  ? 362 TRP A NE1 1 
ATOM   2808 C CE2 . TRP A 1 368 ? -37.60247 71.59247 49.67026 1.000 78.11967  ? 362 TRP A CE2 1 
ATOM   2809 C CE3 . TRP A 1 368 ? -36.40912 69.51311 49.97028 1.000 79.28180  ? 362 TRP A CE3 1 
ATOM   2810 C CZ2 . TRP A 1 368 ? -37.65275 71.81762 51.04398 1.000 81.09927  ? 362 TRP A CZ2 1 
ATOM   2811 C CZ3 . TRP A 1 368 ? -36.45999 69.73868 51.33432 1.000 85.26151  ? 362 TRP A CZ3 1 
ATOM   2812 C CH2 . TRP A 1 368 ? -37.07694 70.88172 51.85720 1.000 83.25839  ? 362 TRP A CH2 1 
ATOM   2813 N N   . VAL A 1 369 ? -39.16420 68.65934 44.93642 1.000 75.02893  ? 363 VAL A N   1 
ATOM   2814 C CA  . VAL A 1 369 ? -40.50861 68.95515 44.45421 1.000 82.93638  ? 363 VAL A CA  1 
ATOM   2815 C C   . VAL A 1 369 ? -41.23936 67.69593 43.99727 1.000 78.28806  ? 363 VAL A C   1 
ATOM   2816 O O   . VAL A 1 369 ? -42.29615 67.78951 43.36479 1.000 83.83300  ? 363 VAL A O   1 
ATOM   2817 C CB  . VAL A 1 369 ? -40.47063 70.00638 43.33386 1.000 67.49316  ? 363 VAL A CB  1 
ATOM   2818 C CG1 . VAL A 1 369 ? -41.76071 70.81565 43.31511 1.000 132.89634 ? 363 VAL A CG1 1 
ATOM   2819 C CG2 . VAL A 1 369 ? -39.27468 70.92319 43.51839 1.000 97.46166  ? 363 VAL A CG2 1 
ATOM   2820 N N   . SER A 1 370 ? -40.70227 66.51841 44.30367 1.000 78.23468  ? 364 SER A N   1 
ATOM   2821 C CA  . SER A 1 370 ? -41.37903 65.28049 43.95456 1.000 69.36247  ? 364 SER A CA  1 
ATOM   2822 C C   . SER A 1 370 ? -42.69057 65.15280 44.72508 1.000 79.98449  ? 364 SER A C   1 
ATOM   2823 O O   . SER A 1 370 ? -42.88604 65.75738 45.78367 1.000 82.22603  ? 364 SER A O   1 
ATOM   2824 C CB  . SER A 1 370 ? -40.48118 64.07928 44.24927 1.000 76.23804  ? 364 SER A CB  1 
ATOM   2825 O OG  . SER A 1 370 ? -41.17094 62.85936 44.03773 1.000 78.73799  ? 364 SER A OG  1 
ATOM   2826 N N   . SER A 1 371 ? -43.60591 64.35475 44.17119 1.000 65.29750  ? 365 SER A N   1 
ATOM   2827 C CA  . SER A 1 371 ? -44.83960 64.05201 44.88490 1.000 71.06993  ? 365 SER A CA  1 
ATOM   2828 C C   . SER A 1 371 ? -44.58144 63.21414 46.12799 1.000 71.24389  ? 365 SER A C   1 
ATOM   2829 O O   . SER A 1 371 ? -45.41878 63.19616 47.03583 1.000 98.12221  ? 365 SER A O   1 
ATOM   2830 C CB  . SER A 1 371 ? -45.82342 63.32659 43.96656 1.000 69.37880  ? 365 SER A CB  1 
ATOM   2831 O OG  . SER A 1 371 ? -45.37135 62.01836 43.66952 1.000 90.35534  ? 365 SER A OG  1 
ATOM   2832 N N   . HIS A 1 372 ? -43.44372 62.52666 46.18744 1.000 83.08027  ? 366 HIS A N   1 
ATOM   2833 C CA  . HIS A 1 372 ? -43.06722 61.71650 47.33628 1.000 77.34802  ? 366 HIS A CA  1 
ATOM   2834 C C   . HIS A 1 372 ? -42.41026 62.52839 48.44149 1.000 76.44923  ? 366 HIS A C   1 
ATOM   2835 O O   . HIS A 1 372 ? -41.98482 61.94586 49.44479 1.000 83.14682  ? 366 HIS A O   1 
ATOM   2836 C CB  . HIS A 1 372 ? -42.12890 60.59143 46.89545 1.000 69.18365  ? 366 HIS A CB  1 
ATOM   2837 C CG  . HIS A 1 372 ? -42.65604 59.78350 45.75209 1.000 77.27470  ? 366 HIS A CG  1 
ATOM   2838 N ND1 . HIS A 1 372 ? -43.88190 59.15477 45.78899 1.000 88.76720  ? 366 HIS A ND1 1 
ATOM   2839 C CD2 . HIS A 1 372 ? -42.12573 59.50292 44.53856 1.000 80.91204  ? 366 HIS A CD2 1 
ATOM   2840 C CE1 . HIS A 1 372 ? -44.08412 58.52122 44.64747 1.000 84.99067  ? 366 HIS A CE1 1 
ATOM   2841 N NE2 . HIS A 1 372 ? -43.03339 58.71622 43.87138 1.000 77.65185  ? 366 HIS A NE2 1 
ATOM   2842 N N   . SER A 1 373 ? -42.31015 63.84689 48.27854 1.000 85.89248  ? 367 SER A N   1 
ATOM   2843 C CA  . SER A 1 373 ? -41.71696 64.73442 49.27455 1.000 69.55156  ? 367 SER A CA  1 
ATOM   2844 C C   . SER A 1 373 ? -42.78686 65.71291 49.73662 1.000 84.96680  ? 367 SER A C   1 
ATOM   2845 O O   . SER A 1 373 ? -43.17414 66.61757 48.98843 1.000 88.43502  ? 367 SER A O   1 
ATOM   2846 C CB  . SER A 1 373 ? -40.50773 65.47607 48.70811 1.000 60.01036  ? 367 SER A CB  1 
ATOM   2847 O OG  . SER A 1 373 ? -39.48777 64.57276 48.32326 1.000 82.14184  ? 367 SER A OG  1 
ATOM   2848 N N   . LYS A 1 374 ? -43.26189 65.52797 50.96284 1.000 82.48966  ? 368 LYS A N   1 
ATOM   2849 C CA  . LYS A 1 374 ? -44.28107 66.37809 51.55496 1.000 82.15311  ? 368 LYS A CA  1 
ATOM   2850 C C   . LYS A 1 374 ? -43.65732 67.24402 52.63905 1.000 86.46254  ? 368 LYS A C   1 
ATOM   2851 O O   . LYS A 1 374 ? -42.75979 66.79862 53.36098 1.000 87.84203  ? 368 LYS A O   1 
ATOM   2852 C CB  . LYS A 1 374 ? -45.42035 65.53972 52.13908 1.000 70.87052  ? 368 LYS A CB  1 
ATOM   2853 C CG  . LYS A 1 374 ? -46.17272 64.72368 51.09963 1.000 87.93162  ? 368 LYS A CG  1 
ATOM   2854 C CD  . LYS A 1 374 ? -47.49229 64.20156 51.64590 1.000 111.68281 ? 368 LYS A CD  1 
ATOM   2855 C CE  . LYS A 1 374 ? -48.28205 63.48486 50.56234 1.000 116.77882 ? 368 LYS A CE  1 
ATOM   2856 N NZ  . LYS A 1 374 ? -49.59405 62.98191 51.05700 1.000 127.82898 ? 368 LYS A NZ  1 
ATOM   2857 N N   . SER A 1 375 ? -44.13060 68.48355 52.74089 1.000 97.04895  ? 369 SER A N   1 
ATOM   2858 C CA  . SER A 1 375 ? -43.61984 69.39870 53.75093 1.000 96.39178  ? 369 SER A CA  1 
ATOM   2859 C C   . SER A 1 375 ? -43.97062 68.89879 55.14550 1.000 104.01716 ? 369 SER A C   1 
ATOM   2860 O O   . SER A 1 375 ? -45.07136 68.39416 55.38532 1.000 95.36178  ? 369 SER A O   1 
ATOM   2861 C CB  . SER A 1 375 ? -44.18513 70.80270 53.53702 1.000 103.02098 ? 369 SER A CB  1 
ATOM   2862 O OG  . SER A 1 375 ? -43.65633 71.39483 52.36313 1.000 116.64899 ? 369 SER A OG  1 
ATOM   2863 N N   . LEU A 1 376 ? -43.02111 69.03961 56.06622 1.000 105.13841 ? 370 LEU A N   1 
ATOM   2864 C CA  . LEU A 1 376 ? -43.21804 68.56331 57.42746 1.000 100.31161 ? 370 LEU A CA  1 
ATOM   2865 C C   . LEU A 1 376 ? -44.33128 69.34504 58.11058 1.000 103.28002 ? 370 LEU A C   1 
ATOM   2866 O O   . LEU A 1 376 ? -44.29334 70.57738 58.17287 1.000 124.57996 ? 370 LEU A O   1 
ATOM   2867 C CB  . LEU A 1 376 ? -41.92193 68.68780 58.22510 1.000 105.13458 ? 370 LEU A CB  1 
ATOM   2868 C CG  . LEU A 1 376 ? -42.04618 68.37919 59.71800 1.000 112.96863 ? 370 LEU A CG  1 
ATOM   2869 C CD1 . LEU A 1 376 ? -42.48692 66.93878 59.93049 1.000 108.32193 ? 370 LEU A CD1 1 
ATOM   2870 C CD2 . LEU A 1 376 ? -40.74125 68.66483 60.44628 1.000 93.89725  ? 370 LEU A CD2 1 
ATOM   2871 N N   . LYS A 1 377 ? -45.32689 68.62345 58.61779 1.000 107.04315 ? 371 LYS A N   1 
ATOM   2872 C CA  . LYS A 1 377 ? -46.41905 69.21059 59.38055 1.000 125.77864 ? 371 LYS A CA  1 
ATOM   2873 C C   . LYS A 1 377 ? -46.56291 68.44150 60.68332 1.000 129.89185 ? 371 LYS A C   1 
ATOM   2874 O O   . LYS A 1 377 ? -46.57579 67.20636 60.67911 1.000 123.11725 ? 371 LYS A O   1 
ATOM   2875 C CB  . LYS A 1 377 ? -47.73446 69.18282 58.59324 1.000 119.34082 ? 371 LYS A CB  1 
ATOM   2876 C CG  . LYS A 1 377 ? -47.68684 69.94279 57.27734 1.000 135.88690 ? 371 LYS A CG  1 
ATOM   2877 C CD  . LYS A 1 377 ? -47.32919 71.40480 57.49380 1.000 145.62543 ? 371 LYS A CD  1 
ATOM   2878 C CE  . LYS A 1 377 ? -47.15286 72.13036 56.16918 1.000 144.08127 ? 371 LYS A CE  1 
ATOM   2879 N NZ  . LYS A 1 377 ? -46.75529 73.55266 56.36018 1.000 139.32472 ? 371 LYS A NZ  1 
ATOM   2880 N N   . ILE A 1 378 ? -46.65558 69.16921 61.79179 1.000 134.30318 ? 372 ILE A N   1 
ATOM   2881 C CA  . ILE A 1 378 ? -46.78118 68.55299 63.10721 1.000 145.26488 ? 372 ILE A CA  1 
ATOM   2882 C C   . ILE A 1 378 ? -47.97517 69.14474 63.84733 1.000 160.08548 ? 372 ILE A C   1 
ATOM   2883 O O   . ILE A 1 378 ? -48.19879 70.35552 63.82231 1.000 156.92067 ? 372 ILE A O   1 
ATOM   2884 C CB  . ILE A 1 378 ? -45.48918 68.72321 63.92689 1.000 136.27901 ? 372 ILE A CB  1 
ATOM   2885 C CG1 . ILE A 1 378 ? -44.29326 68.16287 63.15703 1.000 132.79739 ? 372 ILE A CG1 1 
ATOM   2886 C CG2 . ILE A 1 378 ? -45.61639 68.03506 65.27728 1.000 139.08158 ? 372 ILE A CG2 1 
ATOM   2887 C CD1 . ILE A 1 378 ? -42.96572 68.46733 63.79454 1.000 137.29861 ? 372 ILE A CD1 1 
ATOM   2888 O OXT . ILE A 1 378 ? -48.74508 68.42976 64.48911 1.000 162.64055 ? 372 ILE A OXT 1 
HETATM 2889 C C1  . CIT B 2 .   ? -31.88792 47.23511 50.86160 1.000 110.83667 ? 401 CIT A C1  1 
HETATM 2890 O O1  . CIT B 2 .   ? -31.19214 47.93130 50.08488 1.000 75.55213  ? 401 CIT A O1  1 
HETATM 2891 O O2  . CIT B 2 .   ? -32.85629 47.64829 51.53144 1.000 131.58869 ? 401 CIT A O2  1 
HETATM 2892 C C2  . CIT B 2 .   ? -31.52382 45.74398 51.01237 1.000 109.33160 ? 401 CIT A C2  1 
HETATM 2893 C C3  . CIT B 2 .   ? -32.51662 44.88353 51.82104 1.000 140.77370 ? 401 CIT A C3  1 
HETATM 2894 O O7  . CIT B 2 .   ? -33.80500 45.42764 51.62717 1.000 119.24033 ? 401 CIT A O7  1 
HETATM 2895 C C4  . CIT B 2 .   ? -32.50637 43.40714 51.37941 1.000 123.89225 ? 401 CIT A C4  1 
HETATM 2896 C C5  . CIT B 2 .   ? -33.09600 43.11791 49.99037 1.000 114.93255 ? 401 CIT A C5  1 
HETATM 2897 O O3  . CIT B 2 .   ? -33.69979 44.02279 49.39123 1.000 112.51963 ? 401 CIT A O3  1 
HETATM 2898 O O4  . CIT B 2 .   ? -32.92811 41.94724 49.54504 1.000 108.93210 ? 401 CIT A O4  1 
HETATM 2899 C C6  . CIT B 2 .   ? -32.06142 44.91913 53.31529 1.000 163.00888 ? 401 CIT A C6  1 
HETATM 2900 O O5  . CIT B 2 .   ? -31.32651 45.87793 53.64291 1.000 143.19772 ? 401 CIT A O5  1 
HETATM 2901 O O6  . CIT B 2 .   ? -32.44715 44.00620 54.07103 1.000 177.43342 ? 401 CIT A O6  1 
HETATM 2902 C C1  . GOL C 3 .   ? -27.43010 50.39055 58.48246 1.000 88.33399  ? 402 GOL A C1  1 
HETATM 2903 O O1  . GOL C 3 .   ? -27.91318 50.20203 59.79178 1.000 90.43525  ? 402 GOL A O1  1 
HETATM 2904 C C2  . GOL C 3 .   ? -28.05067 49.35897 57.56323 1.000 97.14253  ? 402 GOL A C2  1 
HETATM 2905 O O2  . GOL C 3 .   ? -27.43286 49.44615 56.29814 1.000 100.82722 ? 402 GOL A O2  1 
HETATM 2906 C C3  . GOL C 3 .   ? -27.89704 47.96874 58.15733 1.000 83.13930  ? 402 GOL A C3  1 
HETATM 2907 O O3  . GOL C 3 .   ? -28.62639 47.93620 59.36479 1.000 96.76538  ? 402 GOL A O3  1 
HETATM 2908 C C1  . GOL D 3 .   ? -25.82319 61.59069 32.30056 1.000 89.28088  ? 403 GOL A C1  1 
HETATM 2909 O O1  . GOL D 3 .   ? -25.66334 62.84670 31.68380 1.000 103.22079 ? 403 GOL A O1  1 
HETATM 2910 C C2  . GOL D 3 .   ? -24.67692 61.36244 33.26482 1.000 115.79273 ? 403 GOL A C2  1 
HETATM 2911 O O2  . GOL D 3 .   ? -24.61600 62.44563 34.16747 1.000 100.64379 ? 403 GOL A O2  1 
HETATM 2912 C C3  . GOL D 3 .   ? -24.85498 60.04228 33.99974 1.000 104.06475 ? 403 GOL A C3  1 
HETATM 2913 O O3  . GOL D 3 .   ? -24.84277 59.00491 33.04386 1.000 109.52814 ? 403 GOL A O3  1 
HETATM 2914 C C1  . GOL E 3 .   ? -38.86637 75.54587 50.62522 1.000 107.55033 ? 404 GOL A C1  1 
HETATM 2915 O O1  . GOL E 3 .   ? -39.99231 74.94549 50.02841 1.000 104.11209 ? 404 GOL A O1  1 
HETATM 2916 C C2  . GOL E 3 .   ? -38.11233 76.35356 49.58703 1.000 126.20609 ? 404 GOL A C2  1 
HETATM 2917 O O2  . GOL E 3 .   ? -36.88270 76.77417 50.13776 1.000 113.06928 ? 404 GOL A O2  1 
HETATM 2918 C C3  . GOL E 3 .   ? -37.90788 75.53249 48.32207 1.000 119.13251 ? 404 GOL A C3  1 
HETATM 2919 O O3  . GOL E 3 .   ? -36.78266 76.04132 47.63750 1.000 107.64142 ? 404 GOL A O3  1 
HETATM 2920 C C1  . GOL F 3 .   ? -31.45838 55.54024 62.83471 1.000 115.22201 ? 405 GOL A C1  1 
HETATM 2921 O O1  . GOL F 3 .   ? -32.03173 55.92006 61.60534 1.000 94.47707  ? 405 GOL A O1  1 
HETATM 2922 C C2  . GOL F 3 .   ? -30.30011 54.59604 62.58105 1.000 120.14449 ? 405 GOL A C2  1 
HETATM 2923 O O2  . GOL F 3 .   ? -29.33851 55.25846 61.78829 1.000 101.97378 ? 405 GOL A O2  1 
HETATM 2924 C C3  . GOL F 3 .   ? -29.70542 54.12154 63.89947 1.000 115.68490 ? 405 GOL A C3  1 
HETATM 2925 O O3  . GOL F 3 .   ? -28.55761 53.35136 63.61175 1.000 89.99933  ? 405 GOL A O3  1 
HETATM 2926 C C1  . GOL G 3 .   ? -1.53145  47.68397 46.34543 1.000 103.51660 ? 406 GOL A C1  1 
HETATM 2927 O O1  . GOL G 3 .   ? -0.91549  47.30095 45.13864 1.000 114.45166 ? 406 GOL A O1  1 
HETATM 2928 C C2  . GOL G 3 .   ? -0.96244  49.00972 46.80628 1.000 114.26483 ? 406 GOL A C2  1 
HETATM 2929 O O2  . GOL G 3 .   ? -1.17545  49.97269 45.79806 1.000 105.26085 ? 406 GOL A O2  1 
HETATM 2930 C C3  . GOL G 3 .   ? -1.60950  49.42732 48.11735 1.000 111.25401 ? 406 GOL A C3  1 
HETATM 2931 O O3  . GOL G 3 .   ? -0.98849  50.62052 48.54299 1.000 112.36964 ? 406 GOL A O3  1 
HETATM 2932 C C1  . GOL H 3 .   ? -9.74457  68.89025 57.27810 1.000 141.09829 ? 407 GOL A C1  1 
HETATM 2933 O O1  . GOL H 3 .   ? -10.92532 68.67829 56.53944 1.000 106.15776 ? 407 GOL A O1  1 
HETATM 2934 C C2  . GOL H 3 .   ? -9.70469  67.92939 58.44888 1.000 135.52854 ? 407 GOL A C2  1 
HETATM 2935 O O2  . GOL H 3 .   ? -9.41869  66.63720 57.95925 1.000 109.56463 ? 407 GOL A O2  1 
HETATM 2936 C C3  . GOL H 3 .   ? -8.67226  68.38323 59.47056 1.000 132.34092 ? 407 GOL A C3  1 
HETATM 2937 O O3  . GOL H 3 .   ? -8.87618  67.64295 60.65511 1.000 121.88327 ? 407 GOL A O3  1 
HETATM 2938 C C1  . GOL I 3 .   ? -38.96261 54.42215 34.95236 1.000 125.18293 ? 408 GOL A C1  1 
HETATM 2939 O O1  . GOL I 3 .   ? -38.11041 55.37076 35.55241 1.000 108.72994 ? 408 GOL A O1  1 
HETATM 2940 C C2  . GOL I 3 .   ? -38.16812 53.54441 34.00417 1.000 130.60553 ? 408 GOL A C2  1 
HETATM 2941 O O2  . GOL I 3 .   ? -37.91078 54.26539 32.81678 1.000 113.96973 ? 408 GOL A O2  1 
HETATM 2942 C C3  . GOL I 3 .   ? -36.88076 53.07728 34.67017 1.000 113.00612 ? 408 GOL A C3  1 
HETATM 2943 O O3  . GOL I 3 .   ? -36.39211 51.97253 33.93938 1.000 92.82438  ? 408 GOL A O3  1 
HETATM 2944 C C1  . GOL J 3 .   ? -18.85079 63.79423 30.76230 1.000 128.80451 ? 409 GOL A C1  1 
HETATM 2945 O O1  . GOL J 3 .   ? -17.93892 64.76660 31.21791 1.000 116.17634 ? 409 GOL A O1  1 
HETATM 2946 C C2  . GOL J 3 .   ? -19.36233 62.99105 31.94096 1.000 136.38315 ? 409 GOL A C2  1 
HETATM 2947 O O2  . GOL J 3 .   ? -20.37939 62.12355 31.48740 1.000 119.47638 ? 409 GOL A O2  1 
HETATM 2948 C C3  . GOL J 3 .   ? -18.21969 62.21688 32.58241 1.000 114.74488 ? 409 GOL A C3  1 
HETATM 2949 O O3  . GOL J 3 .   ? -17.89926 61.13376 31.73537 1.000 105.56672 ? 409 GOL A O3  1 
HETATM 2950 C C1  . GOL K 3 .   ? -15.16900 28.24565 45.52313 1.000 123.66814 ? 410 GOL A C1  1 
HETATM 2951 O O1  . GOL K 3 .   ? -13.79033 28.04862 45.31535 1.000 135.62404 ? 410 GOL A O1  1 
HETATM 2952 C C2  . GOL K 3 .   ? -15.44934 29.72047 45.73587 1.000 113.64901 ? 410 GOL A C2  1 
HETATM 2953 O O2  . GOL K 3 .   ? -15.07881 30.07339 47.05110 1.000 106.39786 ? 410 GOL A O2  1 
HETATM 2954 C C3  . GOL K 3 .   ? -14.69936 30.55705 44.71009 1.000 107.28694 ? 410 GOL A C3  1 
HETATM 2955 O O3  . GOL K 3 .   ? -13.39911 30.79342 45.20605 1.000 113.13181 ? 410 GOL A O3  1 
HETATM 2956 C C1  . GOL L 3 .   ? -6.11669  53.14792 62.75538 1.000 116.40850 ? 411 GOL A C1  1 
HETATM 2957 O O1  . GOL L 3 .   ? -5.43099  53.59776 63.90045 1.000 118.83334 ? 411 GOL A O1  1 
HETATM 2958 C C2  . GOL L 3 .   ? -5.34561  52.01310 62.11087 1.000 121.77950 ? 411 GOL A C2  1 
HETATM 2959 O O2  . GOL L 3 .   ? -3.97604  52.35093 62.07857 1.000 139.17525 ? 411 GOL A O2  1 
HETATM 2960 C C3  . GOL L 3 .   ? -5.57651  50.71247 62.86300 1.000 130.85609 ? 411 GOL A C3  1 
HETATM 2961 O O3  . GOL L 3 .   ? -5.12790  49.65890 62.03810 1.000 119.57984 ? 411 GOL A O3  1 
HETATM 2962 C C1  . GOL M 3 .   ? -4.79823  63.31556 58.59494 1.000 135.79153 ? 412 GOL A C1  1 
HETATM 2963 O O1  . GOL M 3 .   ? -4.79877  62.14243 59.37497 1.000 116.88780 ? 412 GOL A O1  1 
HETATM 2964 C C2  . GOL M 3 .   ? -4.44395  62.96798 57.16294 1.000 141.91140 ? 412 GOL A C2  1 
HETATM 2965 O O2  . GOL M 3 .   ? -5.18422  63.80215 56.29896 1.000 125.68658 ? 412 GOL A O2  1 
HETATM 2966 C C3  . GOL M 3 .   ? -2.94939  63.13326 56.93228 1.000 137.11883 ? 412 GOL A C3  1 
HETATM 2967 O O3  . GOL M 3 .   ? -2.64793  64.50903 57.02705 1.000 130.47058 ? 412 GOL A O3  1 
HETATM 2968 C C1  . GOL N 3 .   ? -42.88277 66.23616 38.58101 1.000 131.05249 ? 413 GOL A C1  1 
HETATM 2969 O O1  . GOL N 3 .   ? -43.30442 66.20307 39.92492 1.000 94.60280  ? 413 GOL A O1  1 
HETATM 2970 C C2  . GOL N 3 .   ? -42.37812 64.86582 38.17559 1.000 142.41448 ? 413 GOL A C2  1 
HETATM 2971 O O2  . GOL N 3 .   ? -43.47477 63.98455 38.06351 1.000 118.22144 ? 413 GOL A O2  1 
HETATM 2972 C C3  . GOL N 3 .   ? -41.58752 64.95174 36.87769 1.000 128.37703 ? 413 GOL A C3  1 
HETATM 2973 O O3  . GOL N 3 .   ? -42.24657 65.85478 36.01605 1.000 120.02895 ? 413 GOL A O3  1 
HETATM 2974 C C1  . GOL O 3 .   ? -40.95329 72.34396 57.63925 1.000 132.77541 ? 414 GOL A C1  1 
HETATM 2975 O O1  . GOL O 3 .   ? -40.62208 73.00138 58.83989 1.000 139.95636 ? 414 GOL A O1  1 
HETATM 2976 C C2  . GOL O 3 .   ? -41.82610 73.24858 56.79379 1.000 137.43255 ? 414 GOL A C2  1 
HETATM 2977 O O2  . GOL O 3 .   ? -42.97568 72.52811 56.40663 1.000 145.76925 ? 414 GOL A O2  1 
HETATM 2978 C C3  . GOL O 3 .   ? -41.05237 73.73530 55.57821 1.000 132.77523 ? 414 GOL A C3  1 
HETATM 2979 O O3  . GOL O 3 .   ? -41.08849 72.71452 54.60366 1.000 131.64294 ? 414 GOL A O3  1 
HETATM 2980 O O   . HOH P 4 .   ? -41.57998 73.09809 52.39257 1.000 144.11038 ? 501 HOH A O   1 
HETATM 2981 O O   . HOH P 4 .   ? -38.07549 79.28266 56.20751 1.000 110.47405 ? 502 HOH A O   1 
HETATM 2982 O O   . HOH P 4 .   ? -14.20611 34.46262 41.60711 1.000 84.41834  ? 503 HOH A O   1 
HETATM 2983 O O   . HOH P 4 .   ? -18.99320 49.87452 27.07318 1.000 91.29883  ? 504 HOH A O   1 
HETATM 2984 O O   . HOH P 4 .   ? -45.78664 71.62990 61.70226 1.000 116.53257 ? 505 HOH A O   1 
HETATM 2985 O O   . HOH P 4 .   ? -40.56167 47.88351 38.91082 1.000 67.88373  ? 506 HOH A O   1 
HETATM 2986 O O   . HOH P 4 .   ? -17.32781 52.28671 30.99086 1.000 87.41905  ? 507 HOH A O   1 
HETATM 2987 O O   . HOH P 4 .   ? -23.82825 47.27665 72.19700 1.000 100.30202 ? 508 HOH A O   1 
HETATM 2988 O O   . HOH P 4 .   ? -17.29724 37.47537 64.27711 1.000 93.12879  ? 509 HOH A O   1 
HETATM 2989 O O   . HOH P 4 .   ? -42.74656 59.06968 50.14682 1.000 69.27298  ? 510 HOH A O   1 
HETATM 2990 O O   . HOH P 4 .   ? -28.72583 65.62869 37.13780 1.000 69.28593  ? 511 HOH A O   1 
HETATM 2991 O O   . HOH P 4 .   ? -7.92047  36.12641 47.77700 1.000 88.33540  ? 512 HOH A O   1 
HETATM 2992 O O   . HOH P 4 .   ? -25.51585 64.98320 64.60605 1.000 67.70396  ? 513 HOH A O   1 
HETATM 2993 O O   . HOH P 4 .   ? -20.61323 53.82001 50.22307 1.000 64.98961  ? 514 HOH A O   1 
HETATM 2994 O O   . HOH P 4 .   ? -21.02326 28.64409 38.68766 1.000 81.46695  ? 515 HOH A O   1 
HETATM 2995 O O   . HOH P 4 .   ? -33.50681 52.97363 74.15073 1.000 98.82753  ? 516 HOH A O   1 
HETATM 2996 O O   . HOH P 4 .   ? -31.41017 50.09482 38.30278 1.000 64.60547  ? 517 HOH A O   1 
HETATM 2997 O O   . HOH P 4 .   ? -3.06086  43.41837 34.84825 1.000 97.71268  ? 518 HOH A O   1 
HETATM 2998 O O   . HOH P 4 .   ? -5.49537  59.50478 59.43943 1.000 84.34516  ? 519 HOH A O   1 
HETATM 2999 O O   . HOH P 4 .   ? -6.09881  56.24742 63.89119 1.000 91.81164  ? 520 HOH A O   1 
HETATM 3000 O O   . HOH P 4 .   ? -19.49375 33.68422 60.10392 1.000 98.90569  ? 521 HOH A O   1 
HETATM 3001 O O   . HOH P 4 .   ? -6.10296  65.28878 54.17939 1.000 89.46421  ? 522 HOH A O   1 
HETATM 3002 O O   . HOH P 4 .   ? -26.85009 51.24322 62.10247 1.000 72.09698  ? 523 HOH A O   1 
HETATM 3003 O O   . HOH P 4 .   ? -14.75045 72.22699 38.89668 1.000 86.15907  ? 524 HOH A O   1 
HETATM 3004 O O   . HOH P 4 .   ? -43.72014 69.21624 47.62164 1.000 96.92766  ? 525 HOH A O   1 
HETATM 3005 O O   . HOH P 4 .   ? -39.03625 63.28275 37.88423 1.000 77.36096  ? 526 HOH A O   1 
HETATM 3006 O O   . HOH P 4 .   ? -20.50245 30.99793 40.20115 1.000 83.88490  ? 527 HOH A O   1 
HETATM 3007 O O   . HOH P 4 .   ? -34.07138 72.42129 70.42950 1.000 99.32413  ? 528 HOH A O   1 
HETATM 3008 O O   . HOH P 4 .   ? -16.31712 34.22933 55.67810 1.000 83.87782  ? 529 HOH A O   1 
HETATM 3009 O O   . HOH P 4 .   ? -12.49764 30.28408 60.74989 1.000 109.53154 ? 530 HOH A O   1 
HETATM 3010 O O   . HOH P 4 .   ? -42.89437 61.41579 36.55434 1.000 91.71440  ? 531 HOH A O   1 
HETATM 3011 O O   . HOH P 4 .   ? -35.654   62.094   31.607   1.000 88.67077  ? 532 HOH A O   1 
HETATM 3012 O O   . HOH P 4 .   ? -0.85315  46.18270 42.45301 1.000 100.92465 ? 533 HOH A O   1 
HETATM 3013 O O   . HOH P 4 .   ? -14.98122 67.20913 63.88217 1.000 85.00019  ? 534 HOH A O   1 
HETATM 3014 O O   . HOH P 4 .   ? -6.91578  39.27318 46.91001 1.000 99.82225  ? 535 HOH A O   1 
HETATM 3015 O O   . HOH P 4 .   ? -45.05882 67.72455 46.02870 1.000 88.99833  ? 536 HOH A O   1 
HETATM 3016 O O   . HOH P 4 .   ? -5.53296  43.94357 38.31842 1.000 87.69589  ? 537 HOH A O   1 
HETATM 3017 O O   . HOH P 4 .   ? -8.86970  61.78609 63.18128 1.000 87.37337  ? 538 HOH A O   1 
HETATM 3018 O O   . HOH P 4 .   ? -4.80779  60.90913 32.69372 1.000 84.26618  ? 539 HOH A O   1 
HETATM 3019 O O   . HOH P 4 .   ? -17.83758 57.46393 32.58862 1.000 82.56425  ? 540 HOH A O   1 
HETATM 3020 O O   . HOH P 4 .   ? -41.28924 73.73815 47.48927 1.000 89.99854  ? 541 HOH A O   1 
HETATM 3021 O O   . HOH P 4 .   ? -44.58646 74.97388 54.50460 1.000 97.35084  ? 542 HOH A O   1 
HETATM 3022 O O   . HOH P 4 .   ? -17.63326 75.94226 65.59979 1.000 88.85816  ? 543 HOH A O   1 
HETATM 3023 O O   . HOH P 4 .   ? -24.64630 36.68368 62.80665 1.000 88.33764  ? 544 HOH A O   1 
HETATM 3024 O O   . HOH P 4 .   ? -26.78710 42.77410 67.69178 1.000 91.29172  ? 545 HOH A O   1 
HETATM 3025 O O   . HOH P 4 .   ? -26.18118 31.83119 34.71477 1.000 86.59419  ? 546 HOH A O   1 
HETATM 3026 O O   . HOH P 4 .   ? -47.36910 59.59893 44.54727 1.000 89.96263  ? 547 HOH A O   1 
HETATM 3027 O O   . HOH P 4 .   ? -28.05039 85.56270 61.01605 1.000 93.84617  ? 548 HOH A O   1 
HETATM 3028 O O   . HOH P 4 .   ? -28.80412 70.24475 70.24475 0.50  69.64597  ? 549 HOH A O   1 
HETATM 3029 O O   . HOH P 4 .   ? -45.70950 69.74847 50.04671 1.000 83.19303  ? 550 HOH A O   1 
HETATM 3030 O O   . HOH P 4 .   ? -18.15188 54.70657 70.13194 1.000 90.36693  ? 551 HOH A O   1 
HETATM 3031 O O   . HOH P 4 .   ? -20.68551 54.60031 70.28541 1.000 79.85060  ? 552 HOH A O   1 
HETATM 3032 O O   . HOH P 4 .   ? -31.258   68.706   70.634   1.000 85.15944  ? 553 HOH A O   1 
HETATM 3033 O O   . HOH P 4 .   ? -22.05805 53.41487 29.26458 1.000 77.85511  ? 554 HOH A O   1 
HETATM 3034 O O   . HOH P 4 .   ? -29.33846 85.57641 54.08766 1.000 98.55366  ? 555 HOH A O   1 
HETATM 3035 O O   . HOH P 4 .   ? -2.09595  60.30278 38.05817 1.000 86.43466  ? 556 HOH A O   1 
HETATM 3036 O O   . HOH P 4 .   ? -33.87284 51.10853 36.78757 1.000 75.60487  ? 557 HOH A O   1 
HETATM 3037 O O   . HOH P 4 .   ? -37.77460 65.44081 36.94430 1.000 84.41149  ? 558 HOH A O   1 
HETATM 3038 O O   . HOH P 4 .   ? -26.49483 84.86417 52.94195 1.000 86.40928  ? 559 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 12  ? 1.23331 1.81140 1.55213 -0.32500 0.31177  0.29326  6   SER A N   
2    C CA  . SER A 12  ? 1.24045 1.73786 1.52659 -0.33195 0.27850  0.28822  6   SER A CA  
3    C C   . SER A 12  ? 1.11128 1.57467 1.37424 -0.29377 0.26529  0.25885  6   SER A C   
4    O O   . SER A 12  ? 1.23274 1.71005 1.47864 -0.26441 0.28224  0.24640  6   SER A O   
5    C CB  . SER A 12  ? 1.39680 1.83765 1.62780 -0.35061 0.27825  0.30745  6   SER A CB  
6    O OG  . SER A 12  ? 1.39951 1.82819 1.58353 -0.32442 0.29568  0.30142  6   SER A OG  
7    N N   . VAL A 13  ? 1.10147 1.51985 1.36271 -0.29491 0.23488  0.24798  7   VAL A N   
8    C CA  . VAL A 13  ? 1.09123 1.47860 1.33351 -0.26209 0.22125  0.22184  7   VAL A CA  
9    C C   . VAL A 13  ? 1.00445 1.31986 1.18575 -0.25536 0.21034  0.22001  7   VAL A C   
10   O O   . VAL A 13  ? 1.12212 1.39376 1.28181 -0.27860 0.19750  0.23452  7   VAL A O   
11   C CB  . VAL A 13  ? 1.10771 1.49152 1.38161 -0.26358 0.19609  0.20988  7   VAL A CB  
12   C CG1 . VAL A 13  ? 1.06853 1.52663 1.40316 -0.26465 0.20619  0.20984  7   VAL A CG1 
13   C CG2 . VAL A 13  ? 1.31833 1.65610 1.58443 -0.29416 0.17181  0.22156  7   VAL A CG2 
14   N N   . PRO A 14  ? 0.87017 1.17070 1.02264 -0.22428 0.21381  0.20292  8   PRO A N   
15   C CA  . PRO A 14  ? 0.98373 1.22121 1.08119 -0.21631 0.20299  0.20130  8   PRO A CA  
16   C C   . PRO A 14  ? 1.09156 1.27781 1.17989 -0.21476 0.17329  0.19090  8   PRO A C   
17   O O   . PRO A 14  ? 0.99205 1.18875 1.10505 -0.20372 0.16296  0.17495  8   PRO A O   
18   C CB  . PRO A 14  ? 0.96272 1.21071 1.04154 -0.18398 0.21542  0.18472  8   PRO A CB  
19   C CG  . PRO A 14  ? 1.01792 1.31393 1.14088 -0.17062 0.22043  0.17013  8   PRO A CG  
20   C CD  . PRO A 14  ? 0.94861 1.28927 1.11724 -0.19538 0.22730  0.18501  8   PRO A CD  
21   N N   . ALA A 15  ? 1.04692 1.17606 1.09683 -0.22474 0.15965  0.20021  9   ALA A N   
22   C CA  . ALA A 15  ? 0.97220 1.04816 1.00656 -0.22010 0.13214  0.18970  9   ALA A CA  
23   C C   . ALA A 15  ? 1.10714 1.17723 1.13094 -0.18639 0.12773  0.16620  9   ALA A C   
24   O O   . ALA A 15  ? 1.02232 1.09438 1.02360 -0.16834 0.13835  0.16201  9   ALA A O   
25   C CB  . ALA A 15  ? 1.08141 1.09495 1.07152 -0.23230 0.11962  0.20366  9   ALA A CB  
26   N N   . GLY A 16  ? 0.98721 1.05060 1.02672 -0.17901 0.11164  0.15134  10  GLY A N   
27   C CA  . GLY A 16  ? 1.09878 1.16184 1.13369 -0.15027 0.10806  0.13053  10  GLY A CA  
28   C C   . GLY A 16  ? 0.91558 1.03187 0.98110 -0.13749 0.12351  0.12090  10  GLY A C   
29   O O   . GLY A 16  ? 0.97227 1.08931 1.03616 -0.11590 0.12036  0.10452  10  GLY A O   
30   N N   . ALA A 17  ? 0.88537 1.04609 0.97863 -0.14978 0.14010  0.13089  11  ALA A N   
31   C CA  . ALA A 17  ? 0.98322 1.19433 1.10717 -0.13652 0.15422  0.12180  11  ALA A CA  
32   C C   . ALA A 17  ? 1.06937 1.27919 1.17082 -0.11098 0.16297  0.10934  11  ALA A C   
33   O O   . ALA A 17  ? 0.93320 1.15865 1.04796 -0.09344 0.16302  0.09459  11  ALA A O   
34   C CB  . ALA A 17  ? 0.95353 1.17604 1.10848 -0.13378 0.14086  0.11102  11  ALA A CB  
35   N N   . LYS A 18  ? 1.07596 1.26437 1.14131 -0.10983 0.16879  0.11590  12  LYS A N   
36   C CA  . LYS A 18  ? 0.93192 1.11770 0.97235 -0.08820 0.17601  0.10555  12  LYS A CA  
37   C C   . LYS A 18  ? 0.96508 1.13157 1.00076 -0.06972 0.16089  0.08764  12  LYS A C   
38   O O   . LYS A 18  ? 0.97061 1.14743 1.00288 -0.05211 0.16560  0.07530  12  LYS A O   
39   C CB  . LYS A 18  ? 0.84653 1.07817 0.90331 -0.07984 0.19755  0.10259  12  LYS A CB  
40   C CG  . LYS A 18  ? 0.88830 1.14631 0.94938 -0.09659 0.21658  0.12088  12  LYS A CG  
41   C CD  . LYS A 18  ? 1.23814 1.54605 1.31945 -0.08502 0.23845  0.11596  12  LYS A CD  
42   C CE  . LYS A 18  ? 1.34725 1.64669 1.39441 -0.06215 0.24617  0.10370  12  LYS A CE  
43   N NZ  . LYS A 18  ? 1.27557 1.55526 1.27908 -0.06747 0.25412  0.11570  12  LYS A NZ  
44   N N   . CYS A 19  ? 0.98729 1.12524 1.02163 -0.07394 0.14269  0.08623  13  CYS A N   
45   C CA  . CYS A 19  ? 0.90811 1.03082 0.93911 -0.05780 0.12951  0.07091  13  CYS A CA  
46   C C   . CYS A 19  ? 1.07989 1.17057 1.07508 -0.04682 0.12233  0.06857  13  CYS A C   
47   O O   . CYS A 19  ? 1.10918 1.17309 1.08001 -0.05440 0.11873  0.07956  13  CYS A O   
48   C CB  . CYS A 19  ? 0.95653 1.06521 1.00077 -0.06487 0.11397  0.06908  13  CYS A CB  
49   S SG  . CYS A 19  ? 0.96887 1.11599 1.05760 -0.07303 0.11668  0.06784  13  CYS A SG  
50   N N   . ARG A 20  ? 1.04724 1.14088 1.04013 -0.02939 0.11921  0.05490  14  ARG A N   
51   C CA  . ARG A 20  ? 0.94344 1.01335 0.90888 -0.01696 0.11036  0.05070  14  ARG A CA  
52   C C   . ARG A 20  ? 0.91551 0.98730 0.89190 -0.00412 0.10075  0.03680  14  ARG A C   
53   O O   . ARG A 20  ? 0.96811 1.06230 0.96786 -0.00217 0.10453  0.02949  14  ARG A O   
54   C CB  . ARG A 20  ? 0.91940 0.99709 0.86626 -0.00996 0.11965  0.05034  14  ARG A CB  
55   C CG  . ARG A 20  ? 0.95049 1.05862 0.91516 -0.00313 0.12988  0.04023  14  ARG A CG  
56   C CD  . ARG A 20  ? 1.26126 1.37453 1.20343 0.00211  0.14014  0.04054  14  ARG A CD  
57   N NE  . ARG A 20  ? 1.29017 1.38072 1.20226 0.01080  0.12956  0.03865  14  ARG A NE  
58   C CZ  . ARG A 20  ? 1.16975 1.25882 1.05618 0.01773  0.13331  0.03657  14  ARG A CZ  
59   N NH1 . ARG A 20  ? 1.26441 1.37205 1.14903 0.01848  0.14880  0.03508  14  ARG A NH1 
60   N NH2 . ARG A 20  ? 1.11094 1.17972 0.97208 0.02550  0.12056  0.03530  14  ARG A NH2 
61   N N   . LEU A 21  ? 0.95503 1.00382 0.91427 0.00508  0.08850  0.03394  15  LEU A N   
62   C CA  . LEU A 21  ? 0.99244 1.04573 0.96218 0.01671  0.08065  0.02225  15  LEU A CA  
63   C C   . LEU A 21  ? 0.84150 0.91605 0.81700 0.02619  0.08421  0.01345  15  LEU A C   
64   O O   . LEU A 21  ? 0.91383 0.98986 0.87543 0.02841  0.08778  0.01470  15  LEU A O   
65   C CB  . LEU A 21  ? 1.02581 1.05150 0.97704 0.02600  0.06720  0.02140  15  LEU A CB  
66   C CG  . LEU A 21  ? 0.94915 0.94661 0.89269 0.01749  0.06001  0.02767  15  LEU A CG  
67   C CD1 . LEU A 21  ? 0.87178 0.84081 0.79645 0.03158  0.04605  0.02364  15  LEU A CD1 
68   C CD2 . LEU A 21  ? 0.84054 0.85099 0.80740 0.00904  0.06184  0.02459  15  LEU A CD2 
69   N N   . VAL A 22  ? 0.87546 0.96468 0.86969 0.03079  0.08252  0.00483  16  VAL A N   
70   C CA  . VAL A 22  ? 0.76947 0.87676 0.77178 0.03713  0.08383  -0.00332 16  VAL A CA  
71   C C   . VAL A 22  ? 0.77277 0.88497 0.78384 0.04485  0.07633  -0.00967 16  VAL A C   
72   O O   . VAL A 22  ? 0.95970 1.07033 0.97914 0.04369  0.07490  -0.01017 16  VAL A O   
73   C CB  . VAL A 22  ? 0.71324 0.83815 0.73296 0.03194  0.09308  -0.00560 16  VAL A CB  
74   C CG1 . VAL A 22  ? 0.64348 0.78060 0.67073 0.03714  0.09156  -0.01414 16  VAL A CG1 
75   C CG2 . VAL A 22  ? 0.79145 0.91775 0.80306 0.02698  0.10292  -0.00021 16  VAL A CG2 
76   N N   . GLU A 23  ? 0.71750 0.83738 0.72656 0.05256  0.07145  -0.01440 17  GLU A N   
77   C CA  . GLU A 23  ? 0.91461 1.04609 0.93496 0.05971  0.06635  -0.01950 17  GLU A CA  
78   C C   . GLU A 23  ? 0.83526 0.98588 0.86464 0.06139  0.06399  -0.02454 17  GLU A C   
79   O O   . GLU A 23  ? 0.69574 0.84453 0.71590 0.06041  0.06261  -0.02515 17  GLU A O   
80   C CB  . GLU A 23  ? 0.99533 1.11329 1.00319 0.07042  0.05834  -0.01875 17  GLU A CB  
81   C CG  . GLU A 23  ? 0.65185 0.75360 0.63838 0.07512  0.05239  -0.01492 17  GLU A CG  
82   C CD  . GLU A 23  ? 0.99126 1.07576 0.96480 0.08802  0.04295  -0.01454 17  GLU A CD  
83   O OE1 . GLU A 23  ? 0.91460 1.00131 0.89560 0.09408  0.04204  -0.01860 17  GLU A OE1 
84   O OE2 . GLU A 23  ? 1.04286 1.10973 0.99625 0.09337  0.03606  -0.01040 17  GLU A OE2 
85   N N   . THR A 24  ? 0.80482 0.97354 0.85125 0.06297  0.06330  -0.02786 18  THR A N   
86   C CA  . THR A 24  ? 0.67977 0.86929 0.73882 0.06237  0.05948  -0.03156 18  THR A CA  
87   C C   . THR A 24  ? 0.78584 0.98796 0.84788 0.07397  0.05246  -0.03286 18  THR A C   
88   O O   . THR A 24  ? 0.90274 1.11178 0.97072 0.08046  0.05435  -0.03318 18  THR A O   
89   C CB  . THR A 24  ? 0.69701 0.90062 0.77439 0.05432  0.06432  -0.03228 18  THR A CB  
90   O OG1 . THR A 24  ? 0.79577 0.98667 0.87069 0.04700  0.07016  -0.03117 18  THR A OG1 
91   C CG2 . THR A 24  ? 0.59691 0.81877 0.68711 0.04930  0.05942  -0.03482 18  THR A CG2 
92   N N   . LEU A 25  ? 0.83542 1.04091 0.89226 0.07815  0.04388  -0.03413 19  LEU A N   
93   C CA  . LEU A 25  ? 0.76209 0.98210 0.82337 0.09144  0.03536  -0.03545 19  LEU A CA  
94   C C   . LEU A 25  ? 0.72032 0.97063 0.80215 0.08697  0.02924  -0.03828 19  LEU A C   
95   O O   . LEU A 25  ? 0.87359 1.12157 0.94797 0.08548  0.02006  -0.03967 19  LEU A O   
96   C CB  . LEU A 25  ? 0.78370 0.97996 0.81982 0.10118  0.02738  -0.03320 19  LEU A CB  
97   C CG  . LEU A 25  ? 0.72505 0.88831 0.74017 0.10126  0.03234  -0.02870 19  LEU A CG  
98   C CD1 . LEU A 25  ? 0.80135 0.93892 0.78983 0.11026  0.02348  -0.02450 19  LEU A CD1 
99   C CD2 . LEU A 25  ? 0.70109 0.86523 0.72397 0.10640  0.03686  -0.03003 19  LEU A CD2 
100  N N   . PRO A 26  ? 0.82493 1.10380 0.93170 0.08350  0.03355  -0.03868 20  PRO A N   
101  C CA  . PRO A 26  ? 0.70148 1.01004 0.83089 0.07446  0.02768  -0.03980 20  PRO A CA  
102  C C   . PRO A 26  ? 0.79237 1.11915 0.92724 0.08472  0.01415  -0.04161 20  PRO A C   
103  O O   . PRO A 26  ? 0.96872 1.29440 1.09675 0.10228  0.01104  -0.04176 20  PRO A O   
104  C CB  . PRO A 26  ? 0.75089 1.08759 0.90392 0.07106  0.03708  -0.03751 20  PRO A CB  
105  C CG  . PRO A 26  ? 0.65800 0.97051 0.79612 0.07265  0.04790  -0.03616 20  PRO A CG  
106  C CD  . PRO A 26  ? 0.68131 0.96428 0.79446 0.08482  0.04436  -0.03735 20  PRO A CD  
107  N N   . GLU A 27  ? 0.77075 1.11256 0.91742 0.07374  0.00428  -0.04324 21  GLU A N   
108  C CA  . GLU A 27  ? 0.71003 1.06998 0.86246 0.08177  -0.01172 -0.04514 21  GLU A CA  
109  C C   . GLU A 27  ? 0.58823 0.99116 0.76972 0.09443  -0.01201 -0.04402 21  GLU A C   
110  O O   . GLU A 27  ? 0.90606 1.31723 1.08610 0.11179  -0.02246 -0.04515 21  GLU A O   
111  C CB  . GLU A 27  ? 0.65880 1.02620 0.81924 0.06476  -0.02365 -0.04776 21  GLU A CB  
112  C CG  . GLU A 27  ? 0.90286 1.22874 1.02899 0.05921  -0.02777 -0.05128 21  GLU A CG  
113  C CD  . GLU A 27  ? 0.81735 1.11886 0.93436 0.04783  -0.01402 -0.05115 21  GLU A CD  
114  O OE1 . GLU A 27  ? 0.88653 1.20313 1.02477 0.04056  -0.00424 -0.04809 21  GLU A OE1 
115  O OE2 . GLU A 27  ? 0.76091 1.02939 0.84901 0.04712  -0.01283 -0.05381 21  GLU A OE2 
116  N N   . ASN A 28  ? 0.70663 1.13789 0.91364 0.08727  -0.00043 -0.04153 22  ASN A N   
117  C CA  . ASN A 28  ? 0.86906 1.34779 1.10588 0.09928  0.00241  -0.04048 22  ASN A CA  
118  C C   . ASN A 28  ? 0.84579 1.31353 1.06813 0.12318  0.01075  -0.04207 22  ASN A C   
119  O O   . ASN A 28  ? 0.94698 1.45209 1.19053 0.13630  0.01648  -0.04234 22  ASN A O   
120  C CB  . ASN A 28  ? 0.63431 1.14811 0.90127 0.08126  0.01306  -0.03582 22  ASN A CB  
121  C CG  . ASN A 28  ? 1.26226 1.74542 1.51239 0.06970  0.02725  -0.03341 22  ASN A CG  
122  O OD1 . ASN A 28  ? 1.34517 1.78832 1.56587 0.07785  0.03139  -0.03551 22  ASN A OD1 
123  N ND2 . ASN A 28  ? 1.52977 2.03185 1.79908 0.04985  0.03379  -0.02809 22  ASN A ND2 
124  N N   . MET A 29  ? 0.80598 1.22402 0.99277 0.12898  0.01146  -0.04321 23  MET A N   
125  C CA  . MET A 29  ? 0.69195 1.09018 0.86022 0.15017  0.01577  -0.04514 23  MET A CA  
126  C C   . MET A 29  ? 0.79904 1.16387 0.94021 0.16377  0.00215  -0.04589 23  MET A C   
127  O O   . MET A 29  ? 0.99523 1.34214 1.12348 0.15390  -0.00659 -0.04442 23  MET A O   
128  C CB  . MET A 29  ? 0.88813 1.25501 1.03807 0.14240  0.02900  -0.04413 23  MET A CB  
129  C CG  . MET A 29  ? 0.72754 1.12080 0.89832 0.12781  0.04182  -0.04187 23  MET A CG  
130  S SD  . MET A 29  ? 0.80969 1.16649 0.95819 0.12061  0.05421  -0.04077 23  MET A SD  
131  C CE  . MET A 29  ? 0.58801 0.97751 0.76147 0.10100  0.06513  -0.03596 23  MET A CE  
132  N N   . ASP A 30  ? 0.69456 1.04841 0.82398 0.18725  0.00012  -0.04814 24  ASP A N   
133  C CA  . ASP A 30  ? 0.85786 1.18105 0.96186 0.20278  -0.01447 -0.04759 24  ASP A CA  
134  C C   . ASP A 30  ? 0.90168 1.16628 0.96668 0.19613  -0.01321 -0.04393 24  ASP A C   
135  O O   . ASP A 30  ? 1.07457 1.30700 1.11336 0.20721  -0.02441 -0.04149 24  ASP A O   
136  C CB  . ASP A 30  ? 0.93860 1.27297 1.04620 0.23316  -0.01934 -0.05179 24  ASP A CB  
137  C CG  . ASP A 30  ? 0.96357 1.27659 1.05730 0.24296  -0.00804 -0.05516 24  ASP A CG  
138  O OD1 . ASP A 30  ? 1.05591 1.34993 1.14071 0.22516  0.00327  -0.05359 24  ASP A OD1 
139  O OD2 . ASP A 30  ? 1.04372 1.35824 1.13452 0.26993  -0.01166 -0.06009 24  ASP A OD2 
140  N N   . PHE A 31  ? 0.85625 1.10732 0.91743 0.17817  -0.00039 -0.04254 25  PHE A N   
141  C CA  . PHE A 31  ? 0.85354 1.05590 0.88318 0.17006  0.00168  -0.03821 25  PHE A CA  
142  C C   . PHE A 31  ? 0.86193 1.04993 0.87675 0.15822  -0.00392 -0.03382 25  PHE A C   
143  O O   . PHE A 31  ? 1.00335 1.21296 1.03262 0.14517  -0.00254 -0.03498 25  PHE A O   
144  C CB  . PHE A 31  ? 0.79869 0.99622 0.83226 0.15510  0.01587  -0.03814 25  PHE A CB  
145  C CG  . PHE A 31  ? 0.79147 1.00228 0.83528 0.16565  0.02232  -0.04279 25  PHE A CG  
146  C CD1 . PHE A 31  ? 0.89852 1.08059 0.92201 0.18175  0.01888  -0.04502 25  PHE A CD1 
147  C CD2 . PHE A 31  ? 0.78067 1.02989 0.85123 0.15922  0.03162  -0.04478 25  PHE A CD2 
148  C CE1 . PHE A 31  ? 0.85111 1.04362 0.87949 0.19336  0.02497  -0.05087 25  PHE A CE1 
149  C CE2 . PHE A 31  ? 0.84495 1.10722 0.92118 0.16949  0.03902  -0.04873 25  PHE A CE2 
150  C CZ  . PHE A 31  ? 0.83920 1.07358 0.89362 0.18758  0.03592  -0.05263 25  PHE A CZ  
151  N N   . ARG A 32  ? 0.82270 0.97177 0.80589 0.16275  -0.01047 -0.02865 26  ARG A N   
152  C CA  . ARG A 32  ? 0.90146 1.03173 0.86277 0.15231  -0.01356 -0.02345 26  ARG A CA  
153  C C   . ARG A 32  ? 0.90089 0.98920 0.83426 0.14405  -0.00732 -0.01594 26  ARG A C   
154  O O   . ARG A 32  ? 0.96124 1.02687 0.88550 0.15088  -0.00793 -0.01427 26  ARG A O   
155  C CB  . ARG A 32  ? 0.89165 1.01975 0.83963 0.16628  -0.03069 -0.02206 26  ARG A CB  
156  C CG  . ARG A 32  ? 1.06163 1.23534 1.04034 0.17361  -0.03945 -0.02865 26  ARG A CG  
157  C CD  . ARG A 32  ? 1.26083 1.45819 1.25599 0.15453  -0.03491 -0.03194 26  ARG A CD  
158  N NE  . ARG A 32  ? 1.31487 1.55341 1.33760 0.15789  -0.04634 -0.03669 26  ARG A NE  
159  C CZ  . ARG A 32  ? 1.30610 1.58563 1.36664 0.15518  -0.04170 -0.04058 26  ARG A CZ  
160  N NH1 . ARG A 32  ? 1.18129 1.46472 1.25384 0.15075  -0.02606 -0.04091 26  ARG A NH1 
161  N NH2 . ARG A 32  ? 1.41014 1.72855 1.49675 0.15591  -0.05348 -0.04347 26  ARG A NH2 
162  N N   . SER A 33  ? 0.89422 0.97296 0.81415 0.12913  -0.00141 -0.01165 27  SER A N   
163  C CA  . SER A 33  ? 0.89660 0.94078 0.79110 0.11933  0.00489  -0.00242 27  SER A CA  
164  C C   . SER A 33  ? 1.01920 1.06256 0.89904 0.10773  0.01052  0.00085  27  SER A C   
165  O O   . SER A 33  ? 1.10616 1.17272 0.99670 0.10603  0.00998  -0.00577 27  SER A O   
166  C CB  . SER A 33  ? 0.91933 0.96071 0.82700 0.10944  0.01635  -0.00244 27  SER A CB  
167  O OG  . SER A 33  ? 0.99862 1.06215 0.92443 0.09627  0.02811  -0.00568 27  SER A OG  
168  N N   . ASP A 34  ? 1.03283 1.04840 0.88677 0.09946  0.01594  0.01121  28  ASP A N   
169  C CA  . ASP A 34  ? 1.02842 1.04288 0.86548 0.08896  0.02508  0.01507  28  ASP A CA  
170  C C   . ASP A 34  ? 1.00988 1.03488 0.86307 0.07438  0.04245  0.01534  28  ASP A C   
171  O O   . ASP A 34  ? 1.15273 1.17665 0.99213 0.06609  0.05315  0.01966  28  ASP A O   
172  C CB  . ASP A 34  ? 1.03270 1.01409 0.82999 0.08837  0.02190  0.02826  28  ASP A CB  
173  C CG  . ASP A 34  ? 1.22464 1.19305 1.00331 0.10468  0.00269  0.02882  28  ASP A CG  
174  O OD1 . ASP A 34  ? 1.33308 1.32505 1.12759 0.11463  -0.00681 0.01845  28  ASP A OD1 
175  O OD2 . ASP A 34  ? 1.42139 1.35604 1.17013 0.10711  -0.00379 0.04034  28  ASP A OD2 
176  N N   . HIS A 35  ? 1.11113 1.14742 0.99232 0.07236  0.04542  0.01081  29  HIS A N   
177  C CA  . HIS A 35  ? 0.87895 0.92563 0.77705 0.05983  0.05951  0.01136  29  HIS A CA  
178  C C   . HIS A 35  ? 0.89722 0.96823 0.80892 0.05811  0.06617  0.00266  29  HIS A C   
179  O O   . HIS A 35  ? 1.10989 1.19140 1.02385 0.06489  0.05864  -0.00509 29  HIS A O   
180  C CB  . HIS A 35  ? 0.99330 1.04183 0.91315 0.05907  0.05843  0.00895  29  HIS A CB  
181  C CG  . HIS A 35  ? 0.89788 0.91690 0.80277 0.05965  0.05161  0.01637  29  HIS A CG  
182  N ND1 . HIS A 35  ? 1.03047 1.02898 0.92048 0.04730  0.05612  0.02812  29  HIS A ND1 
183  C CD2 . HIS A 35  ? 1.04439 1.04955 0.94618 0.07122  0.04021  0.01359  29  HIS A CD2 
184  C CE1 . HIS A 35  ? 1.04993 1.01858 0.92672 0.04981  0.04607  0.03242  29  HIS A CE1 
185  N NE2 . HIS A 35  ? 0.92008 0.89125 0.80259 0.06595  0.03633  0.02287  29  HIS A NE2 
186  N N   . LEU A 36  ? 0.91787 0.99711 0.83904 0.04887  0.07938  0.00409  30  LEU A N   
187  C CA  . LEU A 36  ? 0.79203 0.88985 0.72625 0.04827  0.08570  -0.00457 30  LEU A CA  
188  C C   . LEU A 36  ? 0.89047 1.00210 0.85076 0.05068  0.07975  -0.01286 30  LEU A C   
189  O O   . LEU A 36  ? 0.89304 1.00699 0.86990 0.04832  0.08015  -0.01134 30  LEU A O   
190  C CB  . LEU A 36  ? 0.88325 0.98870 0.82580 0.04014  0.10068  -0.00059 30  LEU A CB  
191  C CG  . LEU A 36  ? 0.99304 1.11332 0.94365 0.04145  0.10946  -0.00843 30  LEU A CG  
192  C CD1 . LEU A 36  ? 0.84989 0.96448 0.77165 0.04658  0.11170  -0.01120 30  LEU A CD1 
193  C CD2 . LEU A 36  ? 0.85989 0.99254 0.82759 0.03487  0.12257  -0.00352 30  LEU A CD2 
194  N N   . THR A 37  ? 0.89014 1.01021 0.85256 0.05442  0.07369  -0.02112 31  THR A N   
195  C CA  . THR A 37  ? 0.79587 0.93076 0.78319 0.05415  0.06936  -0.02698 31  THR A CA  
196  C C   . THR A 37  ? 0.86479 1.00643 0.86875 0.04829  0.07845  -0.02906 31  THR A C   
197  O O   . THR A 37  ? 0.94838 1.08708 0.94582 0.04663  0.08690  -0.02919 31  THR A O   
198  C CB  . THR A 37  ? 0.72538 0.86810 0.71276 0.05671  0.05879  -0.03402 31  THR A CB  
199  O OG1 . THR A 37  ? 0.87854 1.01716 0.85648 0.05418  0.06138  -0.03965 31  THR A OG1 
200  C CG2 . THR A 37  ? 0.84610 0.98292 0.81587 0.06421  0.04825  -0.03195 31  THR A CG2 
201  N N   . THR A 38  ? 0.76945 0.92111 0.79439 0.04643  0.07684  -0.03038 32  THR A N   
202  C CA  . THR A 38  ? 0.67906 0.83550 0.71922 0.04186  0.08287  -0.03186 32  THR A CA  
203  C C   . THR A 38  ? 0.82517 0.97961 0.86167 0.04143  0.08309  -0.03843 32  THR A C   
204  O O   . THR A 38  ? 0.80562 0.95801 0.84413 0.04139  0.09028  -0.03962 32  THR A O   
205  C CB  . THR A 38  ? 0.72192 0.88825 0.78015 0.04004  0.07980  -0.03178 32  THR A CB  
206  O OG1 . THR A 38  ? 0.91116 1.07614 0.96806 0.04314  0.07845  -0.02786 32  THR A OG1 
207  C CG2 . THR A 38  ? 0.61133 0.77913 0.68238 0.03591  0.08473  -0.03146 32  THR A CG2 
208  N N   . PHE A 39  ? 0.88051 1.03518 0.91156 0.04186  0.07413  -0.04332 33  PHE A N   
209  C CA  . PHE A 39  ? 0.75639 0.90324 0.77922 0.04137  0.07147  -0.05107 33  PHE A CA  
210  C C   . PHE A 39  ? 0.87160 1.00804 0.87189 0.04688  0.07897  -0.05290 33  PHE A C   
211  O O   . PHE A 39  ? 0.94594 1.07651 0.94322 0.04929  0.08463  -0.05784 33  PHE A O   
212  C CB  . PHE A 39  ? 0.70111 0.85076 0.72187 0.03918  0.05798  -0.05540 33  PHE A CB  
213  C CG  . PHE A 39  ? 0.81064 0.94701 0.81849 0.03791  0.05183  -0.06456 33  PHE A CG  
214  C CD1 . PHE A 39  ? 0.86158 0.99176 0.87986 0.03238  0.04997  -0.06840 33  PHE A CD1 
215  C CD2 . PHE A 39  ? 0.72235 0.84871 0.70423 0.04255  0.04649  -0.06948 33  PHE A CD2 
216  C CE1 . PHE A 39  ? 0.83765 0.94963 0.84095 0.03166  0.04235  -0.07805 33  PHE A CE1 
217  C CE2 . PHE A 39  ? 0.76986 0.88019 0.73571 0.04219  0.03930  -0.07967 33  PHE A CE2 
218  C CZ  . PHE A 39  ? 0.77818 0.88021 0.75492 0.03681  0.03691  -0.08450 33  PHE A CZ  
219  N N   . GLU A 40  ? 0.93586 1.06967 0.91873 0.04987  0.07944  -0.04860 34  GLU A N   
220  C CA  . GLU A 40  ? 0.81181 0.93828 0.77161 0.05404  0.08904  -0.04780 34  GLU A CA  
221  C C   . GLU A 40  ? 0.91158 1.04523 0.88384 0.05310  0.10354  -0.04330 34  GLU A C   
222  O O   . GLU A 40  ? 0.87481 1.00852 0.83796 0.05752  0.11343  -0.04651 34  GLU A O   
223  C CB  . GLU A 40  ? 1.01800 1.13861 0.95711 0.05560  0.08670  -0.04061 34  GLU A CB  
224  C CG  . GLU A 40  ? 1.05295 1.16591 0.97143 0.05932  0.07307  -0.04563 34  GLU A CG  
225  C CD  . GLU A 40  ? 1.40002 1.50446 1.29665 0.06224  0.06965  -0.03707 34  GLU A CD  
226  O OE1 . GLU A 40  ? 1.10246 1.20693 1.00738 0.06035  0.07282  -0.02789 34  GLU A OE1 
227  O OE2 . GLU A 40  ? 1.44987 1.54448 1.31857 0.06660  0.06251  -0.03952 34  GLU A OE2 
228  N N   . CYS A 41  ? 0.90900 1.05009 0.90218 0.04822  0.10452  -0.03639 35  CYS A N   
229  C CA  . CYS A 41  ? 0.77579 0.92607 0.78344 0.04587  0.11576  -0.03120 35  CYS A CA  
230  C C   . CYS A 41  ? 0.77945 0.93479 0.80052 0.04956  0.11932  -0.03821 35  CYS A C   
231  O O   . CYS A 41  ? 0.87778 1.04023 0.89887 0.05374  0.13030  -0.03884 35  CYS A O   
232  C CB  . CYS A 41  ? 0.92086 1.07404 0.94511 0.03987  0.11239  -0.02402 35  CYS A CB  
233  S SG  . CYS A 41  ? 0.91658 1.08249 0.96164 0.03454  0.12213  -0.01717 35  CYS A SG  
234  N N   . PHE A 42  ? 0.86388 1.01595 0.89629 0.04859  0.11026  -0.04299 36  PHE A N   
235  C CA  . PHE A 42  ? 0.74514 0.89591 0.78775 0.05234  0.11120  -0.04894 36  PHE A CA  
236  C C   . PHE A 42  ? 0.78931 0.93007 0.81235 0.06081  0.11373  -0.05858 36  PHE A C   
237  O O   . PHE A 42  ? 0.92867 1.06928 0.95598 0.06831  0.11916  -0.06333 36  PHE A O   
238  C CB  . PHE A 42  ? 0.72904 0.87496 0.78329 0.04738  0.10036  -0.05034 36  PHE A CB  
239  C CG  . PHE A 42  ? 0.68731 0.84245 0.75875 0.04164  0.09908  -0.04245 36  PHE A CG  
240  C CD1 . PHE A 42  ? 0.77602 0.93999 0.85428 0.04085  0.10547  -0.03591 36  PHE A CD1 
241  C CD2 . PHE A 42  ? 0.75975 0.91469 0.83937 0.03640  0.09131  -0.04152 36  PHE A CD2 
242  C CE1 . PHE A 42  ? 0.69141 0.85972 0.78113 0.03625  0.10248  -0.03031 36  PHE A CE1 
243  C CE2 . PHE A 42  ? 0.71203 0.87436 0.80276 0.03298  0.09078  -0.03539 36  PHE A CE2 
244  C CZ  . PHE A 42  ? 0.69636 0.86333 0.79058 0.03357  0.09555  -0.03064 36  PHE A CZ  
245  N N   . ASN A 43  ? 0.83428 0.96572 0.83422 0.06131  0.10893  -0.06230 37  ASN A N   
246  C CA  . ASN A 43  ? 0.82349 0.94271 0.79848 0.07024  0.11087  -0.07250 37  ASN A CA  
247  C C   . ASN A 43  ? 0.93162 1.06177 0.89792 0.07781  0.12810  -0.07007 37  ASN A C   
248  O O   . ASN A 43  ? 1.04434 1.17121 1.00112 0.08886  0.13507  -0.07859 37  ASN A O   
249  C CB  . ASN A 43  ? 0.98600 1.09335 0.93707 0.06830  0.09962  -0.07638 37  ASN A CB  
250  C CG  . ASN A 43  ? 1.15713 1.24713 1.10347 0.06684  0.08487  -0.08722 37  ASN A CG  
251  O OD1 . ASN A 43  ? 1.37957 1.46412 1.34111 0.06577  0.08233  -0.09025 37  ASN A OD1 
252  N ND2 . ASN A 43  ? 1.54987 1.62955 1.47432 0.06589  0.07357  -0.09248 37  ASN A ND2 
253  N N   . GLU A 44  ? 0.91410 1.05726 0.88336 0.07210  0.13528  -0.05829 38  GLU A N   
254  C CA  . GLU A 44  ? 0.85524 1.01293 0.81884 0.07582  0.15274  -0.05311 38  GLU A CA  
255  C C   . GLU A 44  ? 0.92201 1.09838 0.91378 0.07985  0.16247  -0.05268 38  GLU A C   
256  O O   . GLU A 44  ? 1.09062 1.27889 1.07814 0.08971  0.17639  -0.05578 38  GLU A O   
257  C CB  . GLU A 44  ? 0.82512 0.98821 0.78604 0.06557  0.15560  -0.03887 38  GLU A CB  
258  C CG  . GLU A 44  ? 0.90923 1.08910 0.86516 0.06499  0.17403  -0.03006 38  GLU A CG  
259  C CD  . GLU A 44  ? 1.16939 1.34042 1.08544 0.07107  0.18032  -0.03193 38  GLU A CD  
260  O OE1 . GLU A 44  ? 1.22965 1.38130 1.12272 0.07773  0.16952  -0.04288 38  GLU A OE1 
261  O OE2 . GLU A 44  ? 1.26608 1.44968 1.17291 0.06816  0.19560  -0.02183 38  GLU A OE2 
262  N N   . ILE A 45  ? 0.87686 1.05749 0.89694 0.07360  0.15526  -0.04900 39  ILE A N   
263  C CA  . ILE A 45  ? 0.77681 0.97547 0.82497 0.07750  0.16150  -0.04787 39  ILE A CA  
264  C C   . ILE A 45  ? 0.87419 1.06526 0.91805 0.09290  0.16223  -0.06090 39  ILE A C   
265  O O   . ILE A 45  ? 1.10105 1.30989 1.15560 0.10357  0.17382  -0.06275 39  ILE A O   
266  C CB  . ILE A 45  ? 0.78070 0.98035 0.85364 0.06808  0.15096  -0.04199 39  ILE A CB  
267  C CG1 . ILE A 45  ? 0.77693 0.98139 0.85215 0.05503  0.15036  -0.03032 39  ILE A CG1 
268  C CG2 . ILE A 45  ? 0.68628 0.90233 0.78681 0.07329  0.15395  -0.04155 39  ILE A CG2 
269  C CD1 . ILE A 45  ? 0.80404 1.00738 0.89801 0.04715  0.14009  -0.02581 39  ILE A CD1 
270  N N   . ILE A 46  ? 0.84460 1.00920 0.87324 0.09452  0.14931  -0.07016 40  ILE A N   
271  C CA  . ILE A 46  ? 0.87263 1.02110 0.89280 0.10858  0.14687  -0.08334 40  ILE A CA  
272  C C   . ILE A 46  ? 0.89900 1.04655 0.89150 0.12229  0.15847  -0.09213 40  ILE A C   
273  O O   . ILE A 46  ? 0.98659 1.13900 0.97992 0.13871  0.16718  -0.09975 40  ILE A O   
274  C CB  . ILE A 46  ? 0.85708 0.97580 0.86795 0.10270  0.12846  -0.08945 40  ILE A CB  
275  C CG1 . ILE A 46  ? 0.86244 0.98483 0.89917 0.09051  0.11965  -0.08024 40  ILE A CG1 
276  C CG2 . ILE A 46  ? 0.88212 0.97605 0.87934 0.11628  0.12357  -0.10351 40  ILE A CG2 
277  C CD1 . ILE A 46  ? 0.97783 1.07825 1.00889 0.08093  0.10354  -0.08277 40  ILE A CD1 
278  N N   . THR A 47  ? 0.95752 1.09890 0.92344 0.11736  0.15868  -0.09136 41  THR A N   
279  C CA  . THR A 47  ? 0.92844 1.06487 0.86040 0.13029  0.16850  -0.10024 41  THR A CA  
280  C C   . THR A 47  ? 0.91093 1.07965 0.85223 0.13964  0.19135  -0.09548 41  THR A C   
281  O O   . THR A 47  ? 0.97354 1.14289 0.89832 0.15779  0.20193  -0.10632 41  THR A O   
282  C CB  . THR A 47  ? 0.82486 0.95087 0.72750 0.12175  0.16354  -0.09713 41  THR A CB  
283  O OG1 . THR A 47  ? 1.06620 1.16737 0.96366 0.11397  0.14212  -0.10238 41  THR A OG1 
284  C CG2 . THR A 47  ? 0.99753 1.11720 0.85964 0.13512  0.17372  -0.10575 41  THR A CG2 
285  N N   . LEU A 48  ? 1.02310 1.21958 0.99124 0.12758  0.19902  -0.07959 42  LEU A N   
286  C CA  . LEU A 48  ? 0.93322 1.16617 0.91550 0.13192  0.22056  -0.07208 42  LEU A CA  
287  C C   . LEU A 48  ? 1.02685 1.28195 1.04651 0.14140  0.22462  -0.07386 42  LEU A C   
288  O O   . LEU A 48  ? 1.00598 1.29587 1.04042 0.14884  0.24304  -0.07017 42  LEU A O   
289  C CB  . LEU A 48  ? 0.86081 1.11101 0.85370 0.11213  0.22514  -0.05323 42  LEU A CB  
290  C CG  . LEU A 48  ? 0.95573 1.18642 0.91215 0.10347  0.22187  -0.04857 42  LEU A CG  
291  C CD1 . LEU A 48  ? 0.81690 1.06128 0.78441 0.08490  0.22607  -0.02942 42  LEU A CD1 
292  C CD2 . LEU A 48  ? 0.89252 1.12035 0.80983 0.11716  0.23481  -0.05608 42  LEU A CD2 
293  N N   . ALA A 49  ? 0.91554 1.15319 0.95094 0.14144  0.20800  -0.07857 43  ALA A N   
294  C CA  . ALA A 49  ? 0.89998 1.15668 0.97099 0.14970  0.20869  -0.07846 43  ALA A CA  
295  C C   . ALA A 49  ? 1.02624 1.29110 1.09182 0.17562  0.22057  -0.09129 43  ALA A C   
296  O O   . ALA A 49  ? 1.10970 1.34426 1.14227 0.18898  0.21706  -0.10607 43  ALA A O   
297  C CB  . ALA A 49  ? 0.84965 1.07948 0.93013 0.14496  0.18779  -0.08080 43  ALA A CB  
298  N N   . LYS A 50  ? 0.94481 1.25133 1.04338 0.18333  0.23387  -0.08613 44  LYS A N   
299  C CA  . LYS A 50  ? 0.96093 1.28261 1.06079 0.21113  0.24653  -0.09799 44  LYS A CA  
300  C C   . LYS A 50  ? 0.93801 1.27510 1.07654 0.22333  0.24053  -0.09894 44  LYS A C   
301  O O   . LYS A 50  ? 0.89724 1.23507 1.03381 0.25040  0.24536  -0.11199 44  LYS A O   
302  C CB  . LYS A 50  ? 0.74713 1.11459 0.84950 0.21480  0.27337  -0.09186 44  LYS A CB  
303  C CG  . LYS A 50  ? 1.26887 1.62151 1.32785 0.20619  0.28107  -0.09071 44  LYS A CG  
304  C CD  . LYS A 50  ? 1.55266 1.85702 1.56370 0.22199  0.27232  -0.11029 44  LYS A CD  
305  C CE  . LYS A 50  ? 1.59284 1.87892 1.56000 0.21142  0.27486  -0.10833 44  LYS A CE  
306  N NZ  . LYS A 50  ? 1.51380 1.74924 1.43560 0.22222  0.26054  -0.12694 44  LYS A NZ  
307  N N   . LYS A 51  ? 0.81839 1.16570 0.98932 0.20597  0.22918  -0.08627 45  LYS A N   
308  C CA  . LYS A 51  ? 0.87623 1.24067 1.08400 0.21723  0.22233  -0.08566 45  LYS A CA  
309  C C   . LYS A 51  ? 0.90565 1.23384 1.11514 0.20671  0.19788  -0.08355 45  LYS A C   
310  O O   . LYS A 51  ? 1.00763 1.31043 1.21404 0.22290  0.18632  -0.09244 45  LYS A O   
311  C CB  . LYS A 51  ? 1.09538 1.51923 1.34751 0.20865  0.23385  -0.07117 45  LYS A CB  
312  C CG  . LYS A 51  ? 1.08436 1.55416 1.34431 0.22419  0.25990  -0.07294 45  LYS A CG  
313  C CD  . LYS A 51  ? 1.24254 1.77433 1.55109 0.21184  0.27011  -0.05674 45  LYS A CD  
314  C CE  . LYS A 51  ? 1.17950 1.71454 1.48359 0.17864  0.27224  -0.04065 45  LYS A CE  
315  N NZ  . LYS A 51  ? 0.99651 1.59070 1.34682 0.16424  0.28204  -0.02445 45  LYS A NZ  
316  N N   . TYR A 52  ? 0.80170 1.12568 1.01407 0.18050  0.19000  -0.07168 46  TYR A N   
317  C CA  . TYR A 52  ? 0.80724 1.10201 1.02106 0.17006  0.16926  -0.06839 46  TYR A CA  
318  C C   . TYR A 52  ? 0.81987 1.09519 1.01492 0.14634  0.16361  -0.06215 46  TYR A C   
319  O O   . TYR A 52  ? 0.87367 1.16360 1.06305 0.13550  0.17396  -0.05683 46  TYR A O   
320  C CB  . TYR A 52  ? 0.73408 1.05648 0.98691 0.16740  0.16249  -0.05876 46  TYR A CB  
321  C CG  . TYR A 52  ? 0.79316 1.14762 1.06656 0.14592  0.16686  -0.04499 46  TYR A CG  
322  C CD1 . TYR A 52  ? 0.81427 1.15017 1.07927 0.12413  0.15585  -0.03745 46  TYR A CD1 
323  C CD2 . TYR A 52  ? 0.78795 1.19091 1.08911 0.14741  0.18170  -0.03947 46  TYR A CD2 
324  C CE1 . TYR A 52  ? 0.70549 1.06359 0.98542 0.10519  0.15775  -0.02602 46  TYR A CE1 
325  C CE2 . TYR A 52  ? 0.80394 1.23172 1.12287 0.12524  0.18368  -0.02620 46  TYR A CE2 
326  C CZ  . TYR A 52  ? 0.78608 1.18794 1.09255 0.10455  0.17071  -0.02010 46  TYR A CZ  
327  O OH  . TYR A 52  ? 0.79022 1.20979 1.11054 0.08312  0.17061  -0.00800 46  TYR A OH  
328  N N   . ILE A 53  ? 0.80934 1.05207 0.99490 0.13889  0.14708  -0.06210 47  ILE A N   
329  C CA  . ILE A 53  ? 0.80205 1.03100 0.97684 0.11800  0.13987  -0.05535 47  ILE A CA  
330  C C   . ILE A 53  ? 0.81030 1.03145 0.99849 0.11070  0.12544  -0.04883 47  ILE A C   
331  O O   . ILE A 53  ? 0.87051 1.06707 1.05259 0.11691  0.11514  -0.05266 47  ILE A O   
332  C CB  . ILE A 53  ? 0.74212 0.93807 0.88434 0.11559  0.13566  -0.06297 47  ILE A CB  
333  C CG1 . ILE A 53  ? 0.81200 1.01279 0.93497 0.12329  0.14885  -0.06977 47  ILE A CG1 
334  C CG2 . ILE A 53  ? 0.81021 0.99744 0.94620 0.09645  0.12813  -0.05581 47  ILE A CG2 
335  C CD1 . ILE A 53  ? 0.80612 0.97562 0.89682 0.12006  0.14235  -0.07743 47  ILE A CD1 
336  N N   . TYR A 54  ? 0.74551 0.98460 0.94890 0.09732  0.12404  -0.03884 48  TYR A N   
337  C CA  . TYR A 54  ? 0.66569 0.89843 0.87790 0.08997  0.11079  -0.03247 48  TYR A CA  
338  C C   . TYR A 54  ? 0.81290 1.03045 1.00877 0.07406  0.10611  -0.02870 48  TYR A C   
339  O O   . TYR A 54  ? 0.76672 0.99296 0.95893 0.06529  0.11196  -0.02586 48  TYR A O   
340  C CB  . TYR A 54  ? 0.75990 1.02346 1.00125 0.08798  0.11005  -0.02521 48  TYR A CB  
341  C CG  . TYR A 54  ? 0.85595 1.14165 1.11987 0.10537  0.11378  -0.02814 48  TYR A CG  
342  C CD1 . TYR A 54  ? 0.92733 1.19575 1.18214 0.12354  0.11332  -0.03711 48  TYR A CD1 
343  C CD2 . TYR A 54  ? 0.79071 1.11483 1.08592 0.10397  0.11681  -0.02208 48  TYR A CD2 
344  C CE1 . TYR A 54  ? 0.85191 1.14090 1.12724 0.14309  0.11671  -0.04086 48  TYR A CE1 
345  C CE2 . TYR A 54  ? 0.79350 1.14408 1.11342 0.12168  0.12070  -0.02473 48  TYR A CE2 
346  C CZ  . TYR A 54  ? 0.87147 1.20442 1.18088 0.14285  0.12106  -0.03457 48  TYR A CZ  
347  O OH  . TYR A 54  ? 1.03207 1.39144 1.36582 0.16407  0.12490  -0.03831 48  TYR A OH  
348  N N   . ILE A 55  ? 0.77020 0.96549 0.95600 0.07095  0.09583  -0.02809 49  ILE A N   
349  C CA  . ILE A 55  ? 0.74370 0.92746 0.91524 0.05851  0.09205  -0.02521 49  ILE A CA  
350  C C   . ILE A 55  ? 0.79034 0.96962 0.96495 0.05356  0.08220  -0.01885 49  ILE A C   
351  O O   . ILE A 55  ? 0.82143 0.99243 0.99963 0.05935  0.07559  -0.01777 49  ILE A O   
352  C CB  . ILE A 55  ? 0.78981 0.95264 0.94280 0.05792  0.09088  -0.03061 49  ILE A CB  
353  C CG1 . ILE A 55  ? 0.73857 0.90210 0.88413 0.06552  0.09902  -0.03843 49  ILE A CG1 
354  C CG2 . ILE A 55  ? 0.61746 0.77712 0.76028 0.04652  0.08880  -0.02767 49  ILE A CG2 
355  C CD1 . ILE A 55  ? 0.76923 0.91018 0.89628 0.06509  0.09502  -0.04511 49  ILE A CD1 
356  N N   . ALA A 56  ? 0.71134 0.89355 0.88140 0.04406  0.08064  -0.01487 50  ALA A N   
357  C CA  . ALA A 56  ? 0.60118 0.77881 0.76888 0.03981  0.07201  -0.00955 50  ALA A CA  
358  C C   . ALA A 56  ? 0.71055 0.88222 0.86262 0.03229  0.07240  -0.00867 50  ALA A C   
359  O O   . ALA A 56  ? 0.80011 0.97709 0.94955 0.02902  0.07557  -0.00961 50  ALA A O   
360  C CB  . ALA A 56  ? 0.67234 0.86443 0.85456 0.03892  0.06768  -0.00617 50  ALA A CB  
361  N N   . SER A 57  ? 0.56514 0.72614 0.70690 0.02996  0.06932  -0.00630 51  SER A N   
362  C CA  . SER A 57  ? 0.78681 0.94739 0.91599 0.02470  0.07024  -0.00482 51  SER A CA  
363  C C   . SER A 57  ? 0.77524 0.92784 0.89593 0.02212  0.06589  0.00112  51  SER A C   
364  O O   . SER A 57  ? 0.90416 1.04722 1.02718 0.02371  0.06153  0.00401  51  SER A O   
365  C CB  . SER A 57  ? 0.88031 1.04274 1.00574 0.02273  0.07573  -0.00847 51  SER A CB  
366  O OG  . SER A 57  ? 0.80847 0.96305 0.93271 0.02006  0.07476  -0.00774 51  SER A OG  
367  N N   . PHE A 58  ? 0.82507 0.98079 0.93401 0.01912  0.06728  0.00322  52  PHE A N   
368  C CA  . PHE A 58  ? 0.69379 0.84415 0.79104 0.01578  0.06531  0.01027  52  PHE A CA  
369  C C   . PHE A 58  ? 0.74024 0.88408 0.83884 0.00999  0.06657  0.01426  52  PHE A C   
370  O O   . PHE A 58  ? 0.85575 0.98520 0.95270 0.00937  0.06093  0.01930  52  PHE A O   
371  C CB  . PHE A 58  ? 0.83160 0.99042 0.91532 0.01542  0.06960  0.01043  52  PHE A CB  
372  C CG  . PHE A 58  ? 0.82821 0.98547 0.89762 0.01140  0.07078  0.01863  52  PHE A CG  
373  C CD1 . PHE A 58  ? 0.88657 1.03399 0.94241 0.01315  0.06421  0.02308  52  PHE A CD1 
374  C CD2 . PHE A 58  ? 0.81452 0.98166 0.88383 0.00499  0.07820  0.02276  52  PHE A CD2 
375  C CE1 . PHE A 58  ? 0.81862 0.96365 0.85717 0.00919  0.06615  0.03198  52  PHE A CE1 
376  C CE2 . PHE A 58  ? 0.80897 0.97705 0.86488 -0.00046 0.08110  0.03226  52  PHE A CE2 
377  C CZ  . PHE A 58  ? 0.80168 0.95751 0.84021 0.00195  0.07567  0.03712  52  PHE A CZ  
378  N N   . CYS A 59  ? 1.06286 1.21567 1.16415 0.00554  0.07228  0.01224  53  CYS A N   
379  C CA  . CYS A 59  ? 1.02411 1.17073 1.12788 -0.00275 0.07188  0.01547  53  CYS A CA  
380  C C   . CYS A 59  ? 0.87370 1.01181 0.98573 0.00025  0.06956  0.00782  53  CYS A C   
381  O O   . CYS A 59  ? 0.79101 0.93462 0.90759 0.00763  0.07136  0.00078  53  CYS A O   
382  C CB  . CYS A 59  ? 0.72924 0.89456 0.83386 -0.01008 0.07816  0.01774  53  CYS A CB  
383  S SG  . CYS A 59  ? 1.35530 1.51558 1.46059 -0.02640 0.07698  0.02794  53  CYS A SG  
384  N N   . CYS A 60  ? 1.01296 1.13554 1.12447 -0.00594 0.06533  0.00952  54  CYS A N   
385  C CA  . CYS A 60  ? 0.67808 0.79018 0.79254 -0.00322 0.06279  0.00097  54  CYS A CA  
386  C C   . CYS A 60  ? 0.84429 0.94945 0.95771 -0.01640 0.05910  0.00326  54  CYS A C   
387  O O   . CYS A 60  ? 1.02102 1.10657 1.12946 -0.02398 0.05337  0.01000  54  CYS A O   
388  C CB  . CYS A 60  ? 0.73127 0.82300 0.84473 0.00680  0.05789  -0.00210 54  CYS A CB  
389  S SG  . CYS A 60  ? 1.00469 1.08344 1.11671 0.01417  0.05660  -0.01490 54  CYS A SG  
390  N N   . ASN A 61  ? 0.73766 0.85812 0.85577 -0.01996 0.06101  -0.00156 55  ASN A N   
391  C CA  . ASN A 61  ? 0.94279 1.06214 1.06379 -0.03432 0.05608  0.00034  55  ASN A CA  
392  C C   . ASN A 61  ? 0.76326 0.89010 0.88625 -0.03159 0.05436  -0.00994 55  ASN A C   
393  O O   . ASN A 61  ? 0.92472 1.07700 1.05578 -0.03506 0.05671  -0.00956 55  ASN A O   
394  C CB  . ASN A 61  ? 0.70969 0.85311 0.83766 -0.04597 0.06090  0.01119  55  ASN A CB  
395  C CG  . ASN A 61  ? 0.81642 0.96056 0.95112 -0.06459 0.05523  0.01626  55  ASN A CG  
396  O OD1 . ASN A 61  ? 1.07930 1.19530 1.20901 -0.07068 0.04531  0.01351  55  ASN A OD1 
397  N ND2 . ASN A 61  ? 0.74870 0.92545 0.89507 -0.07371 0.06111  0.02351  55  ASN A ND2 
398  N N   . PRO A 62  ? 0.82718 0.93230 0.94140 -0.02376 0.05007  -0.01954 56  PRO A N   
399  C CA  . PRO A 62  ? 0.76833 0.87871 0.87919 -0.01981 0.04846  -0.02929 56  PRO A CA  
400  C C   . PRO A 62  ? 0.80195 0.91256 0.91559 -0.03396 0.03887  -0.03025 56  PRO A C   
401  O O   . PRO A 62  ? 0.98836 1.11387 1.10311 -0.03308 0.03706  -0.03518 56  PRO A O   
402  C CB  . PRO A 62  ? 0.80047 0.88660 0.89839 -0.00683 0.04777  -0.03883 56  PRO A CB  
403  C CG  . PRO A 62  ? 0.72534 0.80116 0.82496 -0.00128 0.05032  -0.03380 56  PRO A CG  
404  C CD  . PRO A 62  ? 0.85091 0.92751 0.95651 -0.01538 0.04718  -0.02236 56  PRO A CD  
405  N N   . LEU A 63  ? 0.78030 0.87451 0.89519 -0.04793 0.03141  -0.02485 57  LEU A N   
406  C CA  . LEU A 63  ? 0.79912 0.88827 0.91658 -0.06396 0.01937  -0.02621 57  LEU A CA  
407  C C   . LEU A 63  ? 0.80010 0.92877 0.93831 -0.07720 0.02099  -0.01792 57  LEU A C   
408  O O   . LEU A 63  ? 0.88295 1.01372 1.02895 -0.09394 0.01043  -0.01669 57  LEU A O   
409  C CB  . LEU A 63  ? 0.81124 0.86383 0.92136 -0.07590 0.00952  -0.02236 57  LEU A CB  
410  C CG  . LEU A 63  ? 0.78303 0.79385 0.87249 -0.06113 0.00555  -0.03223 57  LEU A CG  
411  C CD1 . LEU A 63  ? 0.73055 0.70041 0.81092 -0.07336 -0.00697 -0.02823 57  LEU A CD1 
412  C CD2 . LEU A 63  ? 0.75206 0.75463 0.82821 -0.04999 0.00156  -0.04821 57  LEU A CD2 
413  N N   . SER A 64  ? 0.68971 0.85015 0.83744 -0.06983 0.03314  -0.01274 58  SER A N   
414  C CA  . SER A 64  ? 0.66325 0.86416 0.83144 -0.07929 0.03629  -0.00516 58  SER A CA  
415  C C   . SER A 64  ? 0.69376 0.91677 0.86956 -0.07573 0.03085  -0.01266 58  SER A C   
416  O O   . SER A 64  ? 0.70354 0.96003 0.89980 -0.08587 0.02915  -0.00758 58  SER A O   
417  C CB  . SER A 64  ? 0.71810 0.94165 0.88981 -0.07038 0.05061  0.00172  58  SER A CB  
418  O OG  . SER A 64  ? 0.85150 1.06963 1.01201 -0.05101 0.05567  -0.00580 58  SER A OG  
419  N N   . THR A 65  ? 0.76885 0.97619 0.92909 -0.06143 0.02817  -0.02377 59  THR A N   
420  C CA  . THR A 65  ? 0.73550 0.95934 0.89805 -0.05673 0.02147  -0.03047 59  THR A CA  
421  C C   . THR A 65  ? 0.88094 1.07174 1.02190 -0.05364 0.01090  -0.04200 59  THR A C   
422  O O   . THR A 65  ? 0.84277 0.99991 0.96778 -0.05194 0.01078  -0.04567 59  THR A O   
423  C CB  . THR A 65  ? 0.79837 1.04129 0.95964 -0.03884 0.03094  -0.03125 59  THR A CB  
424  O OG1 . THR A 65  ? 0.74272 0.95972 0.88371 -0.02595 0.03717  -0.03563 59  THR A OG1 
425  C CG2 . THR A 65  ? 0.61084 0.88349 0.78866 -0.03873 0.04170  -0.02196 59  THR A CG2 
426  N N   . THR A 66  ? 0.87167 1.07262 1.01064 -0.05101 0.00173  -0.04816 60  THR A N   
427  C CA  . THR A 66  ? 0.76344 0.93411 0.87805 -0.04786 -0.00923 -0.05988 60  THR A CA  
428  C C   . THR A 66  ? 0.78031 0.92949 0.87025 -0.02939 0.00120  -0.06550 60  THR A C   
429  O O   . THR A 66  ? 0.77785 0.89477 0.84844 -0.02614 0.00007  -0.07258 60  THR A O   
430  C CB  . THR A 66  ? 0.64966 0.83832 0.76674 -0.04897 -0.02257 -0.06415 60  THR A CB  
431  O OG1 . THR A 66  ? 0.72653 0.93076 0.86611 -0.06943 -0.03555 -0.06053 60  THR A OG1 
432  C CG2 . THR A 66  ? 0.62658 0.78377 0.71069 -0.04059 -0.03131 -0.07680 60  THR A CG2 
433  N N   . ARG A 67  ? 0.84652 1.01333 0.93699 -0.01703 0.01129  -0.06234 61  ARG A N   
434  C CA  . ARG A 67  ? 0.74235 0.89308 0.81229 -0.00234 0.02158  -0.06565 61  ARG A CA  
435  C C   . ARG A 67  ? 0.87755 1.01549 0.94967 -0.00078 0.03184  -0.06292 61  ARG A C   
436  O O   . ARG A 67  ? 0.88171 1.00017 0.93758 0.00800  0.03687  -0.06823 61  ARG A O   
437  C CB  . ARG A 67  ? 0.68172 0.85098 0.75208 0.00772  0.02820  -0.06126 61  ARG A CB  
438  C CG  . ARG A 67  ? 0.74389 0.92000 0.80490 0.01119  0.01772  -0.06466 61  ARG A CG  
439  C CD  . ARG A 67  ? 0.84066 1.02689 0.89757 0.02265  0.02386  -0.05981 61  ARG A CD  
440  N NE  . ARG A 67  ? 0.82924 1.03297 0.89019 0.02526  0.01237  -0.05964 61  ARG A NE  
441  C CZ  . ARG A 67  ? 0.68908 0.88385 0.72867 0.03069  0.00305  -0.06375 61  ARG A CZ  
442  N NH1 . ARG A 67  ? 0.88503 1.05399 0.89568 0.03395  0.00546  -0.06857 61  ARG A NH1 
443  N NH2 . ARG A 67  ? 0.80718 1.02068 0.85395 0.03408  -0.00890 -0.06293 61  ARG A NH2 
444  N N   . GLY A 68  ? 0.84216 0.99261 0.93387 -0.00819 0.03519  -0.05449 62  GLY A N   
445  C CA  . GLY A 68  ? 0.75604 0.89355 0.84912 -0.00679 0.04227  -0.05130 62  GLY A CA  
446  C C   . GLY A 68  ? 0.88953 0.99598 0.97130 -0.00891 0.03561  -0.05755 62  GLY A C   
447  O O   . GLY A 68  ? 0.88598 0.97636 0.95977 0.00069  0.04109  -0.06027 62  GLY A O   
448  N N   . ALA A 69  ? 0.76197 0.85936 0.84336 -0.02115 0.02271  -0.06020 63  ALA A N   
449  C CA  . ALA A 69  ? 0.74024 0.80117 0.80702 -0.02316 0.01365  -0.06744 63  ALA A CA  
450  C C   . ALA A 69  ? 0.89109 0.93239 0.93250 -0.00780 0.01389  -0.08079 63  ALA A C   
451  O O   . ALA A 69  ? 0.93007 0.94236 0.95717 0.00037  0.01327  -0.08768 63  ALA A O   
452  C CB  . ALA A 69  ? 0.66981 0.72469 0.74214 -0.04282 -0.00224 -0.06671 63  ALA A CB  
453  N N   . LEU A 70  ? 0.92101 0.97713 0.95477 -0.00246 0.01491  -0.08445 64  LEU A N   
454  C CA  . LEU A 70  ? 0.84759 0.88787 0.85420 0.01251  0.01777  -0.09564 64  LEU A CA  
455  C C   . LEU A 70  ? 0.89235 0.93552 0.89805 0.02738  0.03464  -0.09409 64  LEU A C   
456  O O   . LEU A 70  ? 1.08515 1.10905 1.07282 0.03989  0.03829  -0.10314 64  LEU A O   
457  C CB  . LEU A 70  ? 0.74232 0.79823 0.73970 0.01430  0.01513  -0.09715 64  LEU A CB  
458  C CG  . LEU A 70  ? 0.87222 0.92595 0.86795 0.00182  -0.00399 -0.10119 64  LEU A CG  
459  C CD1 . LEU A 70  ? 0.89258 0.96275 0.87881 0.00654  -0.00693 -0.10168 64  LEU A CD1 
460  C CD2 . LEU A 70  ? 0.80935 0.82494 0.78104 0.00122  -0.01630 -0.11432 64  LEU A CD2 
461  N N   . ILE A 71  ? 0.82357 0.89177 0.84889 0.02661  0.04464  -0.08314 65  ILE A N   
462  C CA  . ILE A 71  ? 0.90443 0.97855 0.93411 0.03758  0.05860  -0.08027 65  ILE A CA  
463  C C   . ILE A 71  ? 0.91356 0.96843 0.94629 0.04114  0.05727  -0.08256 65  ILE A C   
464  O O   . ILE A 71  ? 0.93586 0.98572 0.96315 0.05486  0.06517  -0.08715 65  ILE A O   
465  C CB  . ILE A 71  ? 0.76885 0.86877 0.81786 0.03372  0.06560  -0.06860 65  ILE A CB  
466  C CG1 . ILE A 71  ? 0.82729 0.94148 0.86989 0.03384  0.06667  -0.06683 65  ILE A CG1 
467  C CG2 . ILE A 71  ? 0.80497 0.91136 0.86231 0.04185  0.07691  -0.06494 65  ILE A CG2 
468  C CD1 . ILE A 71  ? 0.81550 0.92532 0.83732 0.04399  0.07363  -0.07165 65  ILE A CD1 
469  N N   . PHE A 72  ? 0.84600 0.89045 0.88753 0.02922  0.04722  -0.07876 66  PHE A N   
470  C CA  . PHE A 72  ? 0.89524 0.91631 0.93733 0.03219  0.04369  -0.07943 66  PHE A CA  
471  C C   . PHE A 72  ? 0.95016 0.93919 0.96899 0.04339  0.03839  -0.09369 66  PHE A C   
472  O O   . PHE A 72  ? 0.93444 0.90955 0.95006 0.05745  0.04162  -0.09776 66  PHE A O   
473  C CB  . PHE A 72  ? 0.89219 0.90626 0.94472 0.01435  0.03352  -0.07081 66  PHE A CB  
474  C CG  . PHE A 72  ? 0.96099 0.96307 1.02062 0.01592  0.03351  -0.06390 66  PHE A CG  
475  C CD1 . PHE A 72  ? 1.02953 1.03654 1.09259 0.03220  0.04237  -0.06448 66  PHE A CD1 
476  C CD2 . PHE A 72  ? 1.00747 0.99440 1.07062 0.00046  0.02401  -0.05579 66  PHE A CD2 
477  C CE1 . PHE A 72  ? 0.98915 0.98522 1.05831 0.03487  0.04023  -0.05796 66  PHE A CE1 
478  C CE2 . PHE A 72  ? 1.04683 1.01974 1.11278 0.00234  0.02286  -0.04831 66  PHE A CE2 
479  C CZ  . PHE A 72  ? 0.96580 0.94269 1.03433 0.02052  0.03018  -0.04986 66  PHE A CZ  
480  N N   . ASP A 73  ? 0.96072 0.93745 0.96217 0.03878  0.02934  -0.10221 67  ASP A N   
481  C CA  . ASP A 73  ? 1.05834 1.00093 1.03202 0.05051  0.02325  -0.11782 67  ASP A CA  
482  C C   . ASP A 73  ? 1.05872 1.01142 1.02029 0.07242  0.03890  -0.12509 67  ASP A C   
483  O O   . ASP A 73  ? 1.04121 0.97295 0.98909 0.08940  0.04099  -0.13513 67  ASP A O   
484  C CB  . ASP A 73  ? 1.14656 1.07456 1.10320 0.03917  0.00799  -0.12528 67  ASP A CB  
485  C CG  . ASP A 73  ? 1.30855 1.21363 1.27115 0.01926  -0.01011 -0.12210 67  ASP A CG  
486  O OD1 . ASP A 73  ? 1.23172 1.12758 1.20711 0.01567  -0.01028 -0.11428 67  ASP A OD1 
487  O OD2 . ASP A 73  ? 1.70314 1.59960 1.65752 0.00626  -0.02491 -0.12659 67  ASP A OD2 
488  N N   . LYS A 74  ? 0.93851 0.92311 0.90445 0.07268  0.05015  -0.11979 68  LYS A N   
489  C CA  . LYS A 74  ? 1.03094 1.03083 0.98933 0.09018  0.06726  -0.12288 68  LYS A CA  
490  C C   . LYS A 74  ? 1.04000 1.05032 1.01877 0.10049  0.07735  -0.11850 68  LYS A C   
491  O O   . LYS A 74  ? 1.06733 1.07626 1.03791 0.11907  0.08675  -0.12634 68  LYS A O   
492  C CB  . LYS A 74  ? 0.99444 1.02444 0.95643 0.08479  0.07601  -0.11422 68  LYS A CB  
493  C CG  . LYS A 74  ? 1.07868 1.10084 1.01161 0.08474  0.07118  -0.12130 68  LYS A CG  
494  C CD  . LYS A 74  ? 1.34162 1.36947 1.25220 0.10098  0.08674  -0.12647 68  LYS A CD  
495  C CE  . LYS A 74  ? 1.46927 1.49134 1.34867 0.10021  0.08226  -0.13065 68  LYS A CE  
496  N NZ  . LYS A 74  ? 1.50952 1.53980 1.36509 0.11464  0.09978  -0.13303 68  LYS A NZ  
497  N N   . LEU A 75  ? 1.03455 1.05712 1.03974 0.08967  0.07535  -0.10620 69  LEU A N   
498  C CA  . LEU A 75  ? 0.98652 1.01811 1.01142 0.09854  0.08143  -0.10153 69  LEU A CA  
499  C C   . LEU A 75  ? 0.98381 0.98181 0.99942 0.11000  0.07294  -0.11060 69  LEU A C   
500  O O   . LEU A 75  ? 1.09162 1.09359 1.11263 0.12809  0.07998  -0.11424 69  LEU A O   
501  C CB  . LEU A 75  ? 0.84438 0.89154 0.89335 0.08396  0.07877  -0.08713 69  LEU A CB  
502  C CG  . LEU A 75  ? 0.91647 0.98299 0.98790 0.09085  0.08569  -0.07988 69  LEU A CG  
503  C CD1 . LEU A 75  ? 0.79185 0.88908 0.86983 0.09796  0.10087  -0.07877 69  LEU A CD1 
504  C CD2 . LEU A 75  ? 0.76619 0.84075 0.85362 0.07633  0.08049  -0.06735 69  LEU A CD2 
505  N N   . LYS A 76  ? 0.99570 0.96029 0.99807 0.09966  0.05696  -0.11405 70  LYS A N   
506  C CA  . LYS A 76  ? 1.00907 0.93234 0.99683 0.10970  0.04608  -0.12347 70  LYS A CA  
507  C C   . LYS A 76  ? 1.10311 1.01403 1.06679 0.13318  0.05209  -0.14061 70  LYS A C   
508  O O   . LYS A 76  ? 1.09946 0.99584 1.06032 0.15347  0.05328  -0.14765 70  LYS A O   
509  C CB  . LYS A 76  ? 1.02530 0.91511 1.00169 0.09004  0.02711  -0.12345 70  LYS A CB  
510  C CG  . LYS A 76  ? 0.96722 0.80439 0.92273 0.09724  0.01218  -0.13371 70  LYS A CG  
511  C CD  . LYS A 76  ? 1.11930 0.92843 1.06949 0.07150  -0.00686 -0.12948 70  LYS A CD  
512  C CE  . LYS A 76  ? 1.14991 0.89887 1.07445 0.07621  -0.02459 -0.14047 70  LYS A CE  
513  N NZ  . LYS A 76  ? 1.19127 0.91569 1.08340 0.08827  -0.02936 -0.16086 70  LYS A NZ  
514  N N   . GLU A 77  ? 1.15955 1.07672 1.10432 0.13238  0.05610  -0.14753 71  GLU A N   
515  C CA  . GLU A 77  ? 1.06642 0.97368 0.98349 0.15502  0.06367  -0.16392 71  GLU A CA  
516  C C   . GLU A 77  ? 1.10739 1.05130 1.04061 0.17467  0.08504  -0.16182 71  GLU A C   
517  O O   . GLU A 77  ? 1.12413 1.05938 1.04381 0.19925  0.09170  -0.17446 71  GLU A O   
518  C CB  . GLU A 77  ? 1.09470 1.00384 0.98722 0.14804  0.06326  -0.16908 71  GLU A CB  
519  C CG  . GLU A 77  ? 1.48334 1.38359 1.34143 0.17076  0.07243  -0.18560 71  GLU A CG  
520  C CD  . GLU A 77  ? 1.46618 1.37008 1.29879 0.16310  0.07156  -0.18833 71  GLU A CD  
521  O OE1 . GLU A 77  ? 1.32581 1.23997 1.17061 0.14108  0.06298  -0.17770 71  GLU A OE1 
522  O OE2 . GLU A 77  ? 1.58165 1.47873 1.38101 0.18037  0.07943  -0.20109 71  GLU A OE2 
523  N N   . ALA A 78  ? 1.03452 1.02027 0.99723 0.16436  0.09562  -0.14618 72  ALA A N   
524  C CA  . ALA A 78  ? 0.99373 1.01828 0.97727 0.17877  0.11448  -0.14201 72  ALA A CA  
525  C C   . ALA A 78  ? 1.11864 1.13705 1.11973 0.19426  0.11144  -0.14347 72  ALA A C   
526  O O   . ALA A 78  ? 1.01412 1.04430 1.01653 0.21813  0.12268  -0.15135 72  ALA A O   
527  C CB  . ALA A 78  ? 0.92218 0.98593 0.93205 0.16123  0.12220  -0.12480 72  ALA A CB  
528  N N   . SER A 79  ? 1.08951 1.09047 1.10370 0.18189  0.09637  -0.13551 73  SER A N   
529  C CA  . SER A 79  ? 1.03185 1.02278 1.06043 0.19609  0.09062  -0.13532 73  SER A CA  
530  C C   . SER A 79  ? 1.23333 1.18583 1.23605 0.22054  0.08552  -0.15328 73  SER A C   
531  O O   . SER A 79  ? 1.20327 1.15873 1.21672 0.24352  0.08787  -0.15723 73  SER A O   
532  C CB  . SER A 79  ? 1.05741 1.02822 1.09516 0.17678  0.07402  -0.12353 73  SER A CB  
533  O OG  . SER A 79  ? 1.17788 1.10007 1.18929 0.16848  0.05782  -0.12992 73  SER A OG  
534  N N   . GLU A 80  ? 1.19016 1.10556 1.15833 0.21702  0.07719  -0.16495 74  GLU A N   
535  C CA  . GLU A 80  ? 1.12580 0.99804 1.06295 0.24050  0.07072  -0.18429 74  GLU A CA  
536  C C   . GLU A 80  ? 1.09346 0.99031 1.02006 0.26786  0.09092  -0.19718 74  GLU A C   
537  O O   . GLU A 80  ? 1.25997 1.13041 1.16692 0.29550  0.08975  -0.21353 74  GLU A O   
538  C CB  . GLU A 80  ? 1.14070 0.96321 1.04339 0.22503  0.05241  -0.19260 74  GLU A CB  
539  C CG  . GLU A 80  ? 1.20724 1.00316 1.11882 0.19851  0.03253  -0.18026 74  GLU A CG  
540  C CD  . GLU A 80  ? 1.38136 1.13979 1.26615 0.17825  0.01530  -0.18593 74  GLU A CD  
541  O OE1 . GLU A 80  ? 1.33427 1.08784 1.19256 0.18434  0.01789  -0.19940 74  GLU A OE1 
542  O OE2 . GLU A 80  ? 1.30366 1.03895 1.19390 0.15555  -0.00109 -0.17631 74  GLU A OE2 
543  N N   . LYS A 81  ? 1.29586 1.24137 1.23341 0.26135  0.10958  -0.18999 75  LYS A N   
544  C CA  . LYS A 81  ? 1.11510 1.09100 1.04435 0.28440  0.13185  -0.19887 75  LYS A CA  
545  C C   . LYS A 81  ? 1.23529 1.26278 1.20501 0.29922  0.14857  -0.19088 75  LYS A C   
546  O O   . LYS A 81  ? 1.30072 1.36607 1.27207 0.31519  0.17040  -0.19417 75  LYS A O   
547  C CB  . LYS A 81  ? 1.09706 1.09526 1.01244 0.26864  0.14281  -0.19433 75  LYS A CB  
548  C CG  . LYS A 81  ? 1.25741 1.21015 1.12574 0.26427  0.13013  -0.20790 75  LYS A CG  
549  C CD  . LYS A 81  ? 1.51972 1.49554 1.37423 0.25030  0.14007  -0.20202 75  LYS A CD  
550  C CE  . LYS A 81  ? 1.65463 1.58958 1.45748 0.25398  0.13018  -0.21892 75  LYS A CE  
551  N NZ  . LYS A 81  ? 1.70310 1.58684 1.49458 0.24008  0.10168  -0.22462 75  LYS A NZ  
552  N N   . GLY A 82  ? 1.04203 1.07363 1.04430 0.29370  0.13868  -0.17988 76  GLY A N   
553  C CA  . GLY A 82  ? 1.01518 1.09359 1.05755 0.30813  0.15013  -0.17295 76  GLY A CA  
554  C C   . GLY A 82  ? 1.20953 1.33605 1.28995 0.28464  0.15636  -0.15244 76  GLY A C   
555  O O   . GLY A 82  ? 1.25460 1.42433 1.37140 0.29383  0.16486  -0.14569 76  GLY A O   
556  N N   . ILE A 83  ? 1.01444 1.13485 1.08796 0.25551  0.15136  -0.14288 77  ILE A N   
557  C CA  . ILE A 83  ? 0.90424 1.06331 1.00895 0.23345  0.15540  -0.12469 77  ILE A CA  
558  C C   . ILE A 83  ? 0.98380 1.13305 1.11067 0.22567  0.13862  -0.11546 77  ILE A C   
559  O O   . ILE A 83  ? 0.95822 1.06343 1.06832 0.22004  0.12145  -0.11765 77  ILE A O   
560  C CB  . ILE A 83  ? 0.92015 1.07381 1.00697 0.20862  0.15550  -0.11896 77  ILE A CB  
561  C CG1 . ILE A 83  ? 0.78861 0.94141 0.84410 0.21739  0.16866  -0.12923 77  ILE A CG1 
562  C CG2 . ILE A 83  ? 0.92207 1.11444 1.03782 0.18909  0.16119  -0.10180 77  ILE A CG2 
563  C CD1 . ILE A 83  ? 0.90374 1.10525 0.97395 0.22928  0.19216  -0.12679 77  ILE A CD1 
564  N N   . LYS A 84  ? 0.87898 1.06923 1.04266 0.22413  0.14297  -0.10440 78  LYS A N   
565  C CA  . LYS A 84  ? 0.97609 1.16038 1.15924 0.21607  0.12721  -0.09441 78  LYS A CA  
566  C C   . LYS A 84  ? 0.88796 1.06444 1.06583 0.18656  0.12059  -0.08346 78  LYS A C   
567  O O   . LYS A 84  ? 1.00237 1.20965 1.19248 0.17244  0.12930  -0.07516 78  LYS A O   
568  C CB  . LYS A 84  ? 0.84854 1.08066 1.07248 0.22468  0.13238  -0.08725 78  LYS A CB  
569  C CG  . LYS A 84  ? 1.00575 1.23008 1.24704 0.22143  0.11442  -0.07845 78  LYS A CG  
570  C CD  . LYS A 84  ? 1.15630 1.43077 1.43977 0.23099  0.11762  -0.07232 78  LYS A CD  
571  C CE  . LYS A 84  ? 1.31599 1.57950 1.61251 0.23001  0.09754  -0.06423 78  LYS A CE  
572  N NZ  . LYS A 84  ? 1.19384 1.50806 1.53358 0.23867  0.09768  -0.05826 78  LYS A NZ  
573  N N   . ILE A 85  ? 0.89647 1.03165 1.05574 0.17737  0.10536  -0.08322 79  ILE A N   
574  C CA  . ILE A 85  ? 0.85584 0.98390 1.00973 0.15206  0.09919  -0.07377 79  ILE A CA  
575  C C   . ILE A 85  ? 0.85971 0.98256 1.02699 0.14594  0.08633  -0.06348 79  ILE A C   
576  O O   . ILE A 85  ? 0.95749 1.05040 1.11753 0.15356  0.07464  -0.06501 79  ILE A O   
577  C CB  . ILE A 85  ? 0.89415 0.98491 1.01776 0.14337  0.09266  -0.07987 79  ILE A CB  
578  C CG1 . ILE A 85  ? 1.01953 1.10695 1.12349 0.15476  0.10225  -0.09284 79  ILE A CG1 
579  C CG2 . ILE A 85  ? 0.91890 1.01421 1.04079 0.11971  0.09041  -0.07072 79  ILE A CG2 
580  C CD1 . ILE A 85  ? 0.87891 0.99729 0.98402 0.14699  0.11623  -0.08973 79  ILE A CD1 
581  N N   . ILE A 86  ? 0.80369 0.95220 0.98722 0.13234  0.08752  -0.05297 80  ILE A N   
582  C CA  . ILE A 86  ? 0.74652 0.89022 0.93762 0.12452  0.07544  -0.04291 80  ILE A CA  
583  C C   . ILE A 86  ? 0.88415 1.02656 1.06617 0.10300  0.07460  -0.03608 80  ILE A C   
584  O O   . ILE A 86  ? 0.99052 1.15505 1.17758 0.09512  0.08299  -0.03458 80  ILE A O   
585  C CB  . ILE A 86  ? 0.81182 0.98856 1.03212 0.13155  0.07504  -0.03769 80  ILE A CB  
586  C CG1 . ILE A 86  ? 0.77826 0.96324 1.01118 0.15609  0.07766  -0.04523 80  ILE A CG1 
587  C CG2 . ILE A 86  ? 0.75302 0.92009 0.97528 0.12471  0.06050  -0.02803 80  ILE A CG2 
588  C CD1 . ILE A 86  ? 0.80188 1.02404 1.06843 0.16388  0.07577  -0.03991 80  ILE A CD1 
589  N N   . VAL A 87  ? 0.80132 0.91773 0.96941 0.09403  0.06477  -0.03154 81  VAL A N   
590  C CA  . VAL A 87  ? 0.74168 0.85833 0.90146 0.07614  0.06417  -0.02526 81  VAL A CA  
591  C C   . VAL A 87  ? 0.71342 0.82926 0.87620 0.07153  0.05538  -0.01544 81  VAL A C   
592  O O   . VAL A 87  ? 0.81882 0.91302 0.97537 0.07475  0.04613  -0.01187 81  VAL A O   
593  C CB  . VAL A 87  ? 0.82478 0.91706 0.96562 0.06741  0.06182  -0.02745 81  VAL A CB  
594  C CG1 . VAL A 87  ? 0.71311 0.81205 0.84910 0.05132  0.06227  -0.02072 81  VAL A CG1 
595  C CG2 . VAL A 87  ? 0.84449 0.93550 0.97851 0.07256  0.06851  -0.03804 81  VAL A CG2 
596  N N   . LEU A 88  ? 0.79265 0.92861 0.96179 0.06426  0.05721  -0.01110 82  LEU A N   
597  C CA  . LEU A 88  ? 0.71448 0.84947 0.88164 0.05950  0.04870  -0.00280 82  LEU A CA  
598  C C   . LEU A 88  ? 0.78909 0.91658 0.93888 0.04638  0.04995  0.00115  82  LEU A C   
599  O O   . LEU A 88  ? 0.96928 1.10730 1.11726 0.04059  0.05699  -0.00162 82  LEU A O   
600  C CB  . LEU A 88  ? 0.70073 0.86036 0.88420 0.05994  0.04772  -0.00138 82  LEU A CB  
601  C CG  . LEU A 88  ? 0.76778 0.94537 0.97511 0.07200  0.04589  -0.00304 82  LEU A CG  
602  C CD1 . LEU A 88  ? 0.85788 1.05911 1.08061 0.06649  0.04232  0.00040  82  LEU A CD1 
603  C CD2 . LEU A 88  ? 0.86710 1.02913 1.07435 0.08329  0.03526  -0.00067 82  LEU A CD2 
604  N N   . LEU A 89  ? 0.73321 0.84353 0.87009 0.04245  0.04337  0.00823  83  LEU A N   
605  C CA  . LEU A 89  ? 0.84639 0.95499 0.96819 0.03096  0.04561  0.01348  83  LEU A CA  
606  C C   . LEU A 89  ? 0.85206 0.95451 0.96300 0.02987  0.03783  0.02224  83  LEU A C   
607  O O   . LEU A 89  ? 0.98968 1.08100 1.10192 0.03656  0.02867  0.02579  83  LEU A O   
608  C CB  . LEU A 89  ? 0.76691 0.86091 0.88017 0.02333  0.04759  0.01488  83  LEU A CB  
609  C CG  . LEU A 89  ? 0.85196 0.91868 0.95994 0.02558  0.03926  0.01864  83  LEU A CG  
610  C CD1 . LEU A 89  ? 1.03436 1.08713 1.12618 0.01392  0.03603  0.03081  83  LEU A CD1 
611  C CD2 . LEU A 89  ? 0.91760 0.97224 1.02762 0.02690  0.04032  0.01068  83  LEU A CD2 
612  N N   . ASP A 90  ? 0.74289 0.85235 0.84139 0.02311  0.04108  0.02528  84  ASP A N   
613  C CA  . ASP A 90  ? 0.80457 0.90698 0.88653 0.02204  0.03441  0.03340  84  ASP A CA  
614  C C   . ASP A 90  ? 0.85453 0.93692 0.92264 0.01656  0.03202  0.04354  84  ASP A C   
615  O O   . ASP A 90  ? 0.90281 0.98146 0.97088 0.00896  0.03803  0.04472  84  ASP A O   
616  C CB  . ASP A 90  ? 0.81323 0.92720 0.88177 0.01828  0.03981  0.03254  84  ASP A CB  
617  C CG  . ASP A 90  ? 0.91134 1.01787 0.95866 0.01895  0.03247  0.03911  84  ASP A CG  
618  O OD1 . ASP A 90  ? 0.94716 1.04299 0.97735 0.01426  0.03293  0.04881  84  ASP A OD1 
619  O OD2 . ASP A 90  ? 0.93146 1.04167 0.97781 0.02323  0.02545  0.03507  84  ASP A OD2 
620  N N   . GLU A 91  ? 0.84300 0.91129 0.89861 0.01940  0.02179  0.05165  85  GLU A N   
621  C CA  . GLU A 91  ? 0.91313 0.95719 0.95246 0.01376  0.01761  0.06357  85  GLU A CA  
622  C C   . GLU A 91  ? 0.91280 0.96061 0.93624 -0.00044 0.02816  0.07135  85  GLU A C   
623  O O   . GLU A 91  ? 1.10527 1.13418 1.11722 -0.00952 0.02678  0.08239  85  GLU A O   
624  C CB  . GLU A 91  ? 0.84967 0.87914 0.87484 0.02027  0.00388  0.07157  85  GLU A CB  
625  C CG  . GLU A 91  ? 1.11466 1.11169 1.12586 0.01858  -0.00494 0.08352  85  GLU A CG  
626  C CD  . GLU A 91  ? 1.36565 1.34834 1.36472 0.02823  -0.02105 0.09052  85  GLU A CD  
627  O OE1 . GLU A 91  ? 1.24866 1.24797 1.24730 0.03332  -0.02497 0.08698  85  GLU A OE1 
628  O OE2 . GLU A 91  ? 1.68374 1.63650 1.67278 0.03081  -0.03147 0.09949  85  GLU A OE2 
629  N N   . ARG A 92  ? 0.84115 0.91301 0.86414 -0.00248 0.03847  0.06636  86  ARG A N   
630  C CA  . ARG A 92  ? 0.85293 0.93666 0.86600 -0.01389 0.05041  0.07264  86  ARG A CA  
631  C C   . ARG A 92  ? 0.98641 1.08168 1.01845 -0.02084 0.05822  0.06766  86  ARG A C   
632  O O   . ARG A 92  ? 1.21917 1.32672 1.24885 -0.03208 0.06719  0.07408  86  ARG A O   
633  C CB  . ARG A 92  ? 0.89641 0.99944 0.89653 -0.00948 0.05701  0.06914  86  ARG A CB  
634  C CG  . ARG A 92  ? 0.87085 0.96137 0.84881 -0.00298 0.04732  0.07298  86  ARG A CG  
635  C CD  . ARG A 92  ? 1.08073 1.18468 1.03705 0.00041  0.05409  0.07064  86  ARG A CD  
636  N NE  . ARG A 92  ? 1.23932 1.32845 1.17092 0.00622  0.04253  0.07376  86  ARG A NE  
637  C CZ  . ARG A 92  ? 1.29652 1.38919 1.20045 0.01069  0.04491  0.07211  86  ARG A CZ  
638  N NH1 . ARG A 92  ? 1.31627 1.42814 1.21448 0.01186  0.05956  0.06716  86  ARG A NH1 
639  N NH2 . ARG A 92  ? 1.28723 1.36351 1.16757 0.01554  0.03143  0.07484  86  ARG A NH2 
640  N N   . GLY A 93  ? 0.98727 1.08091 1.03786 -0.01459 0.05497  0.05682  87  GLY A N   
641  C CA  . GLY A 93  ? 1.19227 1.29070 1.25725 -0.02085 0.05899  0.05211  87  GLY A CA  
642  C C   . GLY A 93  ? 1.17602 1.24583 1.24154 -0.02508 0.05044  0.05548  87  GLY A C   
643  O O   . GLY A 93  ? 1.39006 1.45487 1.46635 -0.02515 0.04905  0.04770  87  GLY A O   
644  N N   . LYS A 94  ? 1.11657 1.16420 1.16701 -0.02805 0.04369  0.06710  88  LYS A N   
645  C CA  . LYS A 94  ? 1.13400 1.14625 1.18052 -0.02806 0.03238  0.07042  88  LYS A CA  
646  C C   . LYS A 94  ? 1.37989 1.37765 1.42407 -0.04616 0.03185  0.07733  88  LYS A C   
647  O O   . LYS A 94  ? 1.27709 1.24031 1.31684 -0.04651 0.02126  0.07804  88  LYS A O   
648  C CB  . LYS A 94  ? 1.02227 1.01407 1.05115 -0.02344 0.02342  0.08138  88  LYS A CB  
649  C CG  . LYS A 94  ? 1.27202 1.22747 1.29818 -0.01394 0.00918  0.08152  88  LYS A CG  
650  C CD  . LYS A 94  ? 1.36609 1.30801 1.37682 -0.00579 -0.00069 0.09105  88  LYS A CD  
651  C CE  . LYS A 94  ? 1.28093 1.22195 1.26791 -0.02098 0.00323  0.10789  88  LYS A CE  
652  N NZ  . LYS A 94  ? 1.54290 1.47308 1.51123 -0.01226 -0.00677 0.11638  88  LYS A NZ  
653  N N   . ARG A 95  ? 1.53717 1.56026 1.58483 -0.06089 0.04208  0.08224  89  ARG A N   
654  C CA  . ARG A 95  ? 1.48411 1.49748 1.53261 -0.08166 0.04074  0.09078  89  ARG A CA  
655  C C   . ARG A 95  ? 1.43233 1.42723 1.49079 -0.08087 0.03253  0.07869  89  ARG A C   
656  O O   . ARG A 95  ? 1.32687 1.28469 1.37736 -0.08932 0.02150  0.08299  89  ARG A O   
657  C CB  . ARG A 95  ? 1.60040 1.65505 1.65791 -0.09487 0.05438  0.09593  89  ARG A CB  
658  C CG  . ARG A 95  ? 1.58498 1.66063 1.62963 -0.09298 0.06454  0.10534  89  ARG A CG  
659  C CD  . ARG A 95  ? 1.46659 1.58679 1.52246 -0.10230 0.07927  0.10826  89  ARG A CD  
660  N NE  . ARG A 95  ? 1.78837 1.93108 1.83085 -0.09324 0.08999  0.11083  89  ARG A NE  
661  C CZ  . ARG A 95  ? 1.88012 2.04120 1.92499 -0.07565 0.09420  0.09752  89  ARG A CZ  
662  N NH1 . ARG A 95  ? 1.69506 1.85757 1.75601 -0.06590 0.09002  0.08232  89  ARG A NH1 
663  N NH2 . ARG A 95  ? 1.65664 1.83244 1.68456 -0.06791 0.10236  0.09973  89  ARG A NH2 
664  N N   . ASN A 96  ? 1.23218 1.24911 1.30472 -0.07028 0.03698  0.06337  90  ASN A N   
665  C CA  . ASN A 96  ? 1.06768 1.07074 1.14650 -0.06871 0.03053  0.05073  90  ASN A CA  
666  C C   . ASN A 96  ? 1.17281 1.13890 1.24318 -0.05268 0.02037  0.04270  90  ASN A C   
667  O O   . ASN A 96  ? 1.18800 1.13803 1.25871 -0.04909 0.01478  0.03106  90  ASN A O   
668  C CB  . ASN A 96  ? 0.93841 0.97557 1.03101 -0.06070 0.03872  0.03806  90  ASN A CB  
669  C CG  . ASN A 96  ? 1.54899 1.62367 1.65207 -0.07339 0.04775  0.04375  90  ASN A CG  
670  O OD1 . ASN A 96  ? 1.34687 1.42791 1.45829 -0.08772 0.04522  0.04430  90  ASN A OD1 
671  N ND2 . ASN A 96  ? 1.64987 1.75032 1.75283 -0.06732 0.05755  0.04734  90  ASN A ND2 
672  N N   . LEU A 97  ? 1.11787 1.07077 1.18000 -0.04190 0.01732  0.04812  91  LEU A N   
673  C CA  . LEU A 97  ? 1.08132 1.00997 1.14080 -0.02146 0.00959  0.03885  91  LEU A CA  
674  C C   . LEU A 97  ? 1.14311 1.02666 1.19166 -0.02356 -0.00291 0.03540  91  LEU A C   
675  O O   . LEU A 97  ? 1.10778 0.97926 1.15709 -0.00806 -0.00588 0.02070  91  LEU A O   
676  C CB  . LEU A 97  ? 1.19691 1.11989 1.25022 -0.01139 0.00585  0.04748  91  LEU A CB  
677  C CG  . LEU A 97  ? 1.23566 1.14842 1.29347 0.01306  -0.00015 0.03807  91  LEU A CG  
678  C CD1 . LEU A 97  ? 0.95870 0.90449 1.03415 0.02476  0.00964  0.02345  91  LEU A CD1 
679  C CD2 . LEU A 97  ? 1.17181 1.08382 1.22510 0.02088  -0.00561 0.04796  91  LEU A CD2 
680  N N   . GLY A 98  ? 1.26412 1.12091 1.30058 -0.04277 -0.01038 0.04886  92  GLY A N   
681  C CA  . GLY A 98  ? 1.19562 1.00310 1.21891 -0.04698 -0.02469 0.04583  92  GLY A CA  
682  C C   . GLY A 98  ? 1.13964 0.95072 1.16842 -0.05326 -0.02502 0.03228  92  GLY A C   
683  O O   . GLY A 98  ? 1.18954 0.96600 1.20832 -0.04340 -0.03487 0.01939  92  GLY A O   
684  N N   . GLU A 99  ? 1.06402 0.91643 1.10715 -0.06811 -0.01503 0.03436  93  GLU A N   
685  C CA  . GLU A 99  ? 0.94301 0.80327 0.99194 -0.07367 -0.01634 0.02183  93  GLU A CA  
686  C C   . GLU A 99  ? 1.05292 0.92074 1.10276 -0.04827 -0.01210 0.00268  93  GLU A C   
687  O O   . GLU A 99  ? 1.11935 0.96684 1.16103 -0.04429 -0.01915 -0.01106 93  GLU A O   
688  C CB  . GLU A 99  ? 1.06160 0.96965 1.12810 -0.09170 -0.00632 0.02906  93  GLU A CB  
689  C CG  . GLU A 99  ? 0.96960 0.90077 1.04565 -0.09031 -0.00450 0.01518  93  GLU A CG  
690  C CD  . GLU A 99  ? 1.05777 1.03992 1.15306 -0.10282 0.00589  0.02220  93  GLU A CD  
691  O OE1 . GLU A 99  ? 1.24959 1.24253 1.35097 -0.12238 0.00759  0.03788  93  GLU A OE1 
692  O OE2 . GLU A 99  ? 1.13196 1.14360 1.23553 -0.09228 0.01273  0.01249  93  GLU A OE2 
693  N N   . LEU A 100 ? 1.04272 0.93902 1.10096 -0.03163 -0.00090 0.00187  94  LEU A N   
694  C CA  . LEU A 100 ? 0.94580 0.85472 1.00702 -0.00973 0.00530  -0.01366 94  LEU A CA  
695  C C   . LEU A 100 ? 1.08813 0.95832 1.13628 0.00926  -0.00299 -0.02403 94  LEU A C   
696  O O   . LEU A 100 ? 1.09029 0.95339 1.13196 0.02087  -0.00294 -0.03924 94  LEU A O   
697  C CB  . LEU A 100 ? 0.94060 0.88700 1.01494 0.00038  0.01737  -0.01008 94  LEU A CB  
698  C CG  . LEU A 100 ? 0.97363 0.95758 1.05848 -0.01309 0.02630  -0.00179 94  LEU A CG  
699  C CD1 . LEU A 100 ? 0.80355 0.81322 0.89629 -0.00265 0.03448  0.00137  94  LEU A CD1 
700  C CD2 . LEU A 100 ? 0.71376 0.71672 0.80315 -0.01735 0.03012  -0.01039 94  LEU A CD2 
701  N N   . GLN A 101 ? 1.02115 0.86549 1.06339 0.01439  -0.01029 -0.01617 95  GLN A N   
702  C CA  . GLN A 101 ? 0.98827 0.79678 1.01919 0.03658  -0.01842 -0.02617 95  GLN A CA  
703  C C   . GLN A 101 ? 1.12239 0.88346 1.13293 0.03193  -0.03159 -0.03544 95  GLN A C   
704  O O   . GLN A 101 ? 1.12551 0.86506 1.12524 0.05313  -0.03454 -0.05136 95  GLN A O   
705  C CB  . GLN A 101 ? 0.97629 0.76623 1.00463 0.04284  -0.02565 -0.01412 95  GLN A CB  
706  C CG  . GLN A 101 ? 1.15009 0.98310 1.19635 0.04992  -0.01557 -0.00710 95  GLN A CG  
707  C CD  . GLN A 101 ? 1.16690 0.98171 1.20772 0.05230  -0.02473 0.00699  95  GLN A CD  
708  O OE1 . GLN A 101 ? 1.31412 1.08892 1.33769 0.04052  -0.03628 0.01692  95  GLN A OE1 
709  N NE2 . GLN A 101 ? 1.19410 1.03726 1.24875 0.06653  -0.02075 0.00872  95  GLN A NE2 
710  N N   . SER A 102 ? 1.23430 0.97927 1.23915 0.00443  -0.03974 -0.02606 96  SER A N   
711  C CA  . SER A 102 ? 1.12156 0.82002 1.10707 -0.00377 -0.05481 -0.03481 96  SER A CA  
712  C C   . SER A 102 ? 1.18430 0.89864 1.16848 0.00081  -0.05064 -0.05240 96  SER A C   
713  O O   . SER A 102 ? 1.19451 0.86890 1.15803 0.00696  -0.06202 -0.06702 96  SER A O   
714  C CB  . SER A 102 ? 1.12262 0.80633 1.10684 -0.03807 -0.06431 -0.01818 96  SER A CB  
715  O OG  . SER A 102 ? 1.44970 1.11395 1.42968 -0.04272 -0.06858 -0.00072 96  SER A OG  
716  N N   . HIS A 103 ? 1.15713 0.92582 1.15974 -0.00135 -0.03559 -0.05148 97  HIS A N   
717  C CA  . HIS A 103 ? 1.16532 0.95077 1.16501 0.00340  -0.03134 -0.06630 97  HIS A CA  
718  C C   . HIS A 103 ? 1.18311 0.97581 1.17763 0.03419  -0.02132 -0.08092 97  HIS A C   
719  O O   . HIS A 103 ? 1.13662 0.91907 1.11531 0.04368  -0.02253 -0.09679 97  HIS A O   
720  C CB  . HIS A 103 ? 1.06570 0.90354 1.08580 -0.01171 -0.02069 -0.05823 97  HIS A CB  
721  C CG  . HIS A 103 ? 1.09179 0.94179 1.10683 -0.01285 -0.02094 -0.07038 97  HIS A CG  
722  N ND1 . HIS A 103 ? 1.18144 1.00541 1.18440 -0.02783 -0.03649 -0.07628 97  HIS A ND1 
723  C CD2 . HIS A 103 ? 1.03166 0.91512 1.05035 -0.00151 -0.00900 -0.07708 97  HIS A CD2 
724  C CE1 . HIS A 103 ? 1.13196 0.97396 1.13082 -0.02431 -0.03447 -0.08666 97  HIS A CE1 
725  N NE2 . HIS A 103 ? 1.11580 0.99302 1.12312 -0.00827 -0.01738 -0.08679 97  HIS A NE2 
726  N N   . CYS A 104 ? 1.17668 0.98828 1.18397 0.04955  -0.01164 -0.07563 98  CYS A N   
727  C CA  . CYS A 104 ? 1.13482 0.96182 1.14343 0.07757  -0.00036 -0.08701 98  CYS A CA  
728  C C   . CYS A 104 ? 1.01214 0.82364 1.02416 0.09543  -0.00335 -0.08410 98  CYS A C   
729  O O   . CYS A 104 ? 1.12839 0.97063 1.16032 0.09917  0.00417  -0.07426 98  CYS A O   
730  C CB  . CYS A 104 ? 1.21854 1.10083 1.24682 0.07724  0.01671  -0.08293 98  CYS A CB  
731  S SG  . CYS A 104 ? 1.38608 1.28855 1.41106 0.05920  0.01929  -0.08524 98  CYS A SG  
732  N N   . PRO A 105 ? 1.03467 0.79629 1.02631 0.10774  -0.01609 -0.09305 99  PRO A N   
733  C CA  . PRO A 105 ? 1.20131 0.94501 1.19530 0.12746  -0.02124 -0.09046 99  PRO A CA  
734  C C   . PRO A 105 ? 1.21232 0.99218 1.22227 0.15660  -0.00713 -0.09813 99  PRO A C   
735  O O   . PRO A 105 ? 1.19003 0.96761 1.20936 0.17318  -0.01043 -0.09419 99  PRO A O   
736  C CB  . PRO A 105 ? 1.09214 0.76884 1.05604 0.13435  -0.03918 -0.10100 99  PRO A CB  
737  C CG  . PRO A 105 ? 1.25663 0.92699 1.20345 0.13032  -0.03811 -0.11630 99  PRO A CG  
738  C CD  . PRO A 105 ? 1.15232 0.86844 1.11617 0.10454  -0.02853 -0.10630 99  PRO A CD  
739  N N   . ASP A 106 ? 1.21188 1.02625 1.22584 0.16278  0.00804  -0.10779 100 ASP A N   
740  C CA  . ASP A 106 ? 1.11151 0.96471 1.14235 0.18805  0.02322  -0.11395 100 ASP A CA  
741  C C   . ASP A 106 ? 1.11133 1.02246 1.17156 0.17760  0.03694  -0.10172 100 ASP A C   
742  O O   . ASP A 106 ? 1.18394 1.13260 1.26345 0.19436  0.04925  -0.10369 100 ASP A O   
743  C CB  . ASP A 106 ? 1.13633 0.98800 1.14862 0.20437  0.03227  -0.13275 100 ASP A CB  
744  C CG  . ASP A 106 ? 1.29216 1.08586 1.27419 0.22274  0.01908  -0.14837 100 ASP A CG  
745  O OD1 . ASP A 106 ? 1.19477 0.96309 1.17850 0.23696  0.00872  -0.14695 100 ASP A OD1 
746  O OD2 . ASP A 106 ? 1.59717 1.36783 1.55157 0.22354  0.01759  -0.16236 100 ASP A OD2 
747  N N   . ILE A 107 ? 1.01014 0.92963 1.07436 0.15081  0.03495  -0.08951 101 ILE A N   
748  C CA  . ILE A 107 ? 0.93651 0.90251 1.02481 0.14052  0.04476  -0.07793 101 ILE A CA  
749  C C   . ILE A 107 ? 0.79403 0.75903 0.89548 0.13915  0.03627  -0.06517 101 ILE A C   
750  O O   . ILE A 107 ? 1.01761 0.94696 1.10664 0.13097  0.02291  -0.05916 101 ILE A O   
751  C CB  . ILE A 107 ? 1.01773 0.99356 1.10171 0.11575  0.04713  -0.07268 101 ILE A CB  
752  C CG1 . ILE A 107 ? 1.04219 1.02269 1.11291 0.11863  0.05513  -0.08465 101 ILE A CG1 
753  C CG2 . ILE A 107 ? 0.89259 0.90699 0.99731 0.10530  0.05401  -0.06058 101 ILE A CG2 
754  C CD1 . ILE A 107 ? 1.02366 1.01478 1.09084 0.09733  0.05606  -0.08029 101 ILE A CD1 
755  N N   . ASN A 108 ? 0.98131 0.98462 1.10685 0.14626  0.04309  -0.06033 102 ASN A N   
756  C CA  . ASN A 108 ? 0.90898 0.91495 1.04661 0.14593  0.03413  -0.04852 102 ASN A CA  
757  C C   . ASN A 108 ? 0.91258 0.93547 1.05345 0.12241  0.03535  -0.03646 102 ASN A C   
758  O O   . ASN A 108 ? 1.02484 1.08379 1.17990 0.11748  0.04525  -0.03528 102 ASN A O   
759  C CB  . ASN A 108 ? 1.03141 1.07064 1.19496 0.16639  0.03827  -0.05023 102 ASN A CB  
760  C CG  . ASN A 108 ? 1.06382 1.10611 1.23924 0.16700  0.02642  -0.03843 102 ASN A CG  
761  O OD1 . ASN A 108 ? 1.16735 1.17750 1.32642 0.15720  0.01428  -0.02998 102 ASN A OD1 
762  N ND2 . ASN A 108 ? 1.31019 1.39217 1.51383 0.17766  0.02951  -0.03708 102 ASN A ND2 
763  N N   . PHE A 109 ? 0.93797 0.93381 1.06426 0.10813  0.02551  -0.02735 103 PHE A N   
764  C CA  . PHE A 109 ? 0.80765 0.81755 0.93411 0.08864  0.02650  -0.01598 103 PHE A CA  
765  C C   . PHE A 109 ? 1.00786 1.02078 1.14013 0.09218  0.01808  -0.00568 103 PHE A C   
766  O O   . PHE A 109 ? 1.12117 1.10584 1.24571 0.10020  0.00656  -0.00204 103 PHE A O   
767  C CB  . PHE A 109 ? 0.91705 0.90174 1.02489 0.06969  0.02271  -0.01096 103 PHE A CB  
768  C CG  . PHE A 109 ? 0.85514 0.83705 0.95682 0.06447  0.02802  -0.02069 103 PHE A CG  
769  C CD1 . PHE A 109 ? 0.84686 0.85638 0.95330 0.05387  0.03750  -0.02140 103 PHE A CD1 
770  C CD2 . PHE A 109 ? 0.94748 0.89634 1.03628 0.07110  0.02181  -0.02960 103 PHE A CD2 
771  C CE1 . PHE A 109 ? 0.77216 0.77914 0.87187 0.04968  0.04041  -0.02994 103 PHE A CE1 
772  C CE2 . PHE A 109 ? 0.96386 0.90879 1.04434 0.06614  0.02460  -0.03914 103 PHE A CE2 
773  C CZ  . PHE A 109 ? 1.03375 1.00912 1.12030 0.05523  0.03376  -0.03885 103 PHE A CZ  
774  N N   . ILE A 110 ? 0.83347 0.87734 0.97688 0.08644  0.02217  -0.00115 104 ILE A N   
775  C CA  . ILE A 110 ? 0.83098 0.88162 0.97988 0.08983  0.01318  0.00735  104 ILE A CA  
776  C C   . ILE A 110 ? 0.97734 1.03436 1.11524 0.07248  0.01415  0.01601  104 ILE A C   
777  O O   . ILE A 110 ? 0.96638 1.04569 1.10897 0.06463  0.02335  0.01302  104 ILE A O   
778  C CB  . ILE A 110 ? 0.79666 0.88139 0.97240 0.10274  0.01509  0.00281  104 ILE A CB  
779  C CG1 . ILE A 110 ? 0.67638 0.75794 0.86333 0.12382  0.01491  -0.00574 104 ILE A CG1 
780  C CG2 . ILE A 110 ? 0.89889 0.99311 1.08008 0.10294  0.00382  0.01152  104 ILE A CG2 
781  C CD1 . ILE A 110 ? 0.89657 1.01917 1.11443 0.13600  0.01944  -0.00971 104 ILE A CD1 
782  N N   . THR A 111 ? 0.93296 0.96916 1.05400 0.06766  0.00477  0.02677  105 THR A N   
783  C CA  . THR A 111 ? 0.81406 0.85731 0.92200 0.05451  0.00583  0.03483  105 THR A CA  
784  C C   . THR A 111 ? 0.82985 0.89169 0.94622 0.06051  -0.00110 0.03623  105 THR A C   
785  O O   . THR A 111 ? 0.99109 1.04974 1.11577 0.07280  -0.01226 0.03776  105 THR A O   
786  C CB  . THR A 111 ? 0.91721 0.93133 1.00025 0.04522  0.00021  0.04720  105 THR A CB  
787  O OG1 . THR A 111 ? 1.08806 1.08166 1.16591 0.05587  -0.01428 0.05361  105 THR A OG1 
788  C CG2 . THR A 111 ? 0.96333 0.95795 1.04039 0.03692  0.00443  0.04624  105 THR A CG2 
789  N N   . VAL A 112 ? 0.92317 1.00371 1.03735 0.05229  0.00415  0.03524  106 VAL A N   
790  C CA  . VAL A 112 ? 0.89657 0.99469 1.01857 0.05505  -0.00306 0.03482  106 VAL A CA  
791  C C   . VAL A 112 ? 0.95490 1.04520 1.05017 0.04704  -0.00685 0.04174  106 VAL A C   
792  O O   . VAL A 112 ? 1.03474 1.12077 1.11287 0.03795  0.00263  0.04344  106 VAL A O   
793  C CB  . VAL A 112 ? 0.93967 1.06402 1.08140 0.05328  0.00538  0.02591  106 VAL A CB  
794  C CG1 . VAL A 112 ? 1.12472 1.26433 1.27326 0.05232  -0.00382 0.02602  106 VAL A CG1 
795  C CG2 . VAL A 112 ? 0.99059 1.12507 1.15625 0.06245  0.01058  0.01950  106 VAL A CG2 
796  N N   . ASN A 113 ? 0.88538 0.97543 0.97688 0.05130  -0.02095 0.04556  107 ASN A N   
797  C CA  . ASN A 113 ? 0.77805 0.86197 0.84171 0.04578  -0.02594 0.05016  107 ASN A CA  
798  C C   . ASN A 113 ? 0.89690 0.99648 0.97209 0.04814  -0.03765 0.04536  107 ASN A C   
799  O O   . ASN A 113 ? 0.88650 0.98619 0.96876 0.05502  -0.05357 0.04868  107 ASN A O   
800  C CB  . ASN A 113 ? 0.89473 0.95388 0.93221 0.04696  -0.03495 0.06232  107 ASN A CB  
801  C CG  . ASN A 113 ? 0.97770 1.03002 0.98034 0.04167  -0.03739 0.06721  107 ASN A CG  
802  O OD1 . ASN A 113 ? 0.94332 1.00772 0.94227 0.03956  -0.03624 0.06003  107 ASN A OD1 
803  N ND2 . ASN A 113 ? 0.94636 0.97679 0.92046 0.03985  -0.04105 0.07961  107 ASN A ND2 
804  N N   . ILE A 114 ? 0.86321 0.97496 0.94036 0.04209  -0.03130 0.03785  108 ILE A N   
805  C CA  . ILE A 114 ? 0.84024 0.96481 0.92898 0.04082  -0.04299 0.03316  108 ILE A CA  
806  C C   . ILE A 114 ? 0.85299 0.96419 0.91122 0.03960  -0.05723 0.03541  108 ILE A C   
807  O O   . ILE A 114 ? 0.99571 1.11353 1.05954 0.03688  -0.07002 0.03124  108 ILE A O   
808  C CB  . ILE A 114 ? 0.74113 0.87705 0.83917 0.03405  -0.03293 0.02483  108 ILE A CB  
809  C CG1 . ILE A 114 ? 0.70062 0.82296 0.76561 0.03031  -0.02431 0.02258  108 ILE A CG1 
810  C CG2 . ILE A 114 ? 0.69387 0.84304 0.81855 0.03533  -0.01907 0.02229  108 ILE A CG2 
811  C CD1 . ILE A 114 ? 0.75298 0.88054 0.82172 0.02556  -0.01756 0.01460  108 ILE A CD1 
812  N N   . ASP A 115 ? 0.87327 0.96535 0.89780 0.04057  -0.05575 0.04214  109 ASP A N   
813  C CA  . ASP A 115 ? 0.78267 0.86037 0.77085 0.04038  -0.06751 0.04391  109 ASP A CA  
814  C C   . ASP A 115 ? 1.03669 1.09576 0.99821 0.04337  -0.06954 0.05626  109 ASP A C   
815  O O   . ASP A 115 ? 1.28695 1.33670 1.22110 0.04005  -0.05632 0.06070  109 ASP A O   
816  C CB  . ASP A 115 ? 0.92338 0.99749 0.88663 0.03641  -0.05718 0.03661  109 ASP A CB  
817  C CG  . ASP A 115 ? 1.11148 1.16881 1.03183 0.03814  -0.06842 0.03658  109 ASP A CG  
818  O OD1 . ASP A 115 ? 1.17317 1.22300 1.08608 0.04083  -0.08743 0.04140  109 ASP A OD1 
819  O OD2 . ASP A 115 ? 1.09749 1.14913 0.99013 0.03825  -0.05860 0.03127  109 ASP A OD2 
820  N N   . LYS A 116 ? 1.08349 1.13824 1.05398 0.04960  -0.08634 0.06261  110 LYS A N   
821  C CA  . LYS A 116 ? 1.14264 1.17445 1.08387 0.05251  -0.09226 0.07583  110 LYS A CA  
822  C C   . LYS A 116 ? 1.13941 1.15731 1.04121 0.05372  -0.10806 0.07922  110 LYS A C   
823  O O   . LYS A 116 ? 1.41742 1.41395 1.28558 0.05476  -0.11154 0.09148  110 LYS A O   
824  C CB  . LYS A 116 ? 1.18140 1.21048 1.14829 0.06148  -0.10333 0.08154  110 LYS A CB  
825  C CG  . LYS A 116 ? 1.32962 1.36675 1.32804 0.06190  -0.08804 0.07806  110 LYS A CG  
826  C CD  . LYS A 116 ? 1.51798 1.54214 1.52932 0.07266  -0.09728 0.08464  110 LYS A CD  
827  C CE  . LYS A 116 ? 1.61923 1.64770 1.65613 0.07357  -0.08217 0.07927  110 LYS A CE  
828  N NZ  . LYS A 116 ? 1.75486 1.76694 1.80254 0.08659  -0.09136 0.08340  110 LYS A NZ  
829  N N   . LYS A 117 ? 1.23012 1.25704 1.13247 0.05285  -0.11835 0.06899  111 LYS A N   
830  C CA  . LYS A 117 ? 1.32309 1.33401 1.18266 0.05413  -0.13407 0.06999  111 LYS A CA  
831  C C   . LYS A 117 ? 1.39432 1.39296 1.20775 0.05090  -0.11684 0.07022  111 LYS A C   
832  O O   . LYS A 117 ? 1.52791 1.50773 1.29655 0.05287  -0.12113 0.07888  111 LYS A O   
833  C CB  . LYS A 117 ? 1.27733 1.29896 1.15145 0.05271  -0.15228 0.05812  111 LYS A CB  
834  C CG  . LYS A 117 ? 1.53423 1.53669 1.36222 0.05425  -0.17205 0.05688  111 LYS A CG  
835  C CD  . LYS A 117 ? 1.62264 1.63382 1.46733 0.05010  -0.19262 0.04497  111 LYS A CD  
836  C CE  . LYS A 117 ? 1.57087 1.58892 1.42648 0.04310  -0.17751 0.03225  111 LYS A CE  
837  N NZ  . LYS A 117 ? 1.59553 1.61642 1.46290 0.03619  -0.19873 0.02162  111 LYS A NZ  
838  N N   . ASN A 118 ? 1.28685 1.29731 1.10994 0.04691  -0.09694 0.06127  112 ASN A N   
839  C CA  . ASN A 118 ? 1.23427 1.23965 1.01892 0.04619  -0.07944 0.05964  112 ASN A CA  
840  C C   . ASN A 118 ? 1.27894 1.29615 1.07685 0.04175  -0.05320 0.06371  112 ASN A C   
841  O O   . ASN A 118 ? 1.20521 1.22342 0.97425 0.04142  -0.03679 0.06493  112 ASN A O   
842  C CB  . ASN A 118 ? 1.34859 1.35451 1.12347 0.04777  -0.08231 0.04317  112 ASN A CB  
843  C CG  . ASN A 118 ? 1.54286 1.53516 1.30095 0.05005  -0.11020 0.03819  112 ASN A CG  
844  O OD1 . ASN A 118 ? 1.48614 1.48392 1.27021 0.04717  -0.12359 0.02861  112 ASN A OD1 
845  N ND2 . ASN A 118 ? 1.46846 1.44298 1.18239 0.05405  -0.11989 0.04555  112 ASN A ND2 
846  N N   . ASN A 119 ? 1.15582 1.18334 0.99599 0.03883  -0.04912 0.06548  113 ASN A N   
847  C CA  . ASN A 119 ? 1.16618 1.20327 1.02052 0.03337  -0.02767 0.06949  113 ASN A CA  
848  C C   . ASN A 119 ? 1.15662 1.20770 1.00568 0.03284  -0.01015 0.05981  113 ASN A C   
849  O O   . ASN A 119 ? 1.21991 1.27790 1.05689 0.02934  0.00750  0.06513  113 ASN A O   
850  C CB  . ASN A 119 ? 0.99848 1.02255 0.82943 0.02889  -0.02251 0.08651  113 ASN A CB  
851  C CG  . ASN A 119 ? 1.49149 1.49975 1.33454 0.03061  -0.03834 0.09604  113 ASN A CG  
852  O OD1 . ASN A 119 ? 1.39623 1.40599 1.26954 0.02889  -0.03521 0.09714  113 ASN A OD1 
853  N ND2 . ASN A 119 ? 1.49492 1.48650 1.31257 0.03561  -0.05653 0.10224  113 ASN A ND2 
854  N N   . VAL A 120 ? 1.06064 1.11634 0.91977 0.03629  -0.01586 0.04596  114 VAL A N   
855  C CA  . VAL A 120 ? 0.84637 0.91239 0.70438 0.03818  -0.00219 0.03522  114 VAL A CA  
856  C C   . VAL A 120 ? 0.93243 1.01007 0.83108 0.03596  -0.00023 0.02751  114 VAL A C   
857  O O   . VAL A 120 ? 1.07359 1.16355 0.98347 0.03536  0.01519  0.02436  114 VAL A O   
858  C CB  . VAL A 120 ? 1.05304 1.10699 0.87613 0.04494  -0.01041 0.02507  114 VAL A CB  
859  C CG1 . VAL A 120 ? 0.80935 0.87010 0.63383 0.04935  0.00084  0.01247  114 VAL A CG1 
860  C CG2 . VAL A 120 ? 0.96307 1.00763 0.74004 0.04844  -0.00778 0.03233  114 VAL A CG2 
861  N N   . GLY A 121 ? 0.92380 0.99990 0.84518 0.03472  -0.01552 0.02514  115 GLY A N   
862  C CA  . GLY A 121 ? 0.92476 1.01265 0.88192 0.03214  -0.01293 0.01885  115 GLY A CA  
863  C C   . GLY A 121 ? 0.85355 0.95236 0.83552 0.02983  0.00003  0.02388  115 GLY A C   
864  O O   . GLY A 121 ? 1.00489 1.10030 0.99035 0.02939  -0.00166 0.03272  115 GLY A O   
865  N N   . LEU A 122 ? 0.89364 1.00240 0.89052 0.02867  0.01150  0.01791  116 LEU A N   
866  C CA  . LEU A 122 ? 0.81555 0.93344 0.83332 0.02630  0.02299  0.02048  116 LEU A CA  
867  C C   . LEU A 122 ? 0.88228 1.00900 0.92952 0.02565  0.02263  0.01487  116 LEU A C   
868  O O   . LEU A 122 ? 0.84653 0.97432 0.89643 0.02520  0.01863  0.00868  116 LEU A O   
869  C CB  . LEU A 122 ? 0.73269 0.85763 0.74039 0.02561  0.03819  0.01951  116 LEU A CB  
870  C CG  . LEU A 122 ? 0.81453 0.93722 0.79444 0.02532  0.04338  0.02635  116 LEU A CG  
871  C CD1 . LEU A 122 ? 0.76132 0.89948 0.73967 0.02509  0.05921  0.02483  116 LEU A CD1 
872  C CD2 . LEU A 122 ? 0.85859 0.97300 0.83813 0.02052  0.04014  0.03823  116 LEU A CD2 
873  N N   . LEU A 123 ? 0.73718 0.86835 0.80427 0.02534  0.02676  0.01733  117 LEU A N   
874  C CA  . LEU A 123 ? 0.67151 0.81301 0.76348 0.02546  0.03027  0.01238  117 LEU A CA  
875  C C   . LEU A 123 ? 0.79395 0.93993 0.88401 0.02371  0.04244  0.00812  117 LEU A C   
876  O O   . LEU A 123 ? 0.83395 0.97926 0.91861 0.02232  0.04953  0.01042  117 LEU A O   
877  C CB  . LEU A 123 ? 0.67337 0.81601 0.78367 0.02879  0.02936  0.01498  117 LEU A CB  
878  C CG  . LEU A 123 ? 0.78123 0.93514 0.91275 0.03012  0.03683  0.00972  117 LEU A CG  
879  C CD1 . LEU A 123 ? 0.69755 0.86470 0.84458 0.02907  0.03304  0.00717  117 LEU A CD1 
880  C CD2 . LEU A 123 ? 0.76928 0.92007 0.91245 0.03608  0.03729  0.01050  117 LEU A CD2 
881  N N   . LEU A 124 ? 0.77800 0.92816 0.87260 0.02303  0.04364  0.00272  118 LEU A N   
882  C CA  . LEU A 124 ? 0.78569 0.93952 0.87917 0.02299  0.05315  -0.00126 118 LEU A CA  
883  C C   . LEU A 124 ? 0.74261 0.90335 0.85444 0.02231  0.05753  -0.00330 118 LEU A C   
884  O O   . LEU A 124 ? 0.89042 1.05390 1.00233 0.02274  0.06486  -0.00545 118 LEU A O   
885  C CB  . LEU A 124 ? 0.65660 0.80466 0.73462 0.02429  0.05141  -0.00576 118 LEU A CB  
886  C CG  . LEU A 124 ? 0.64212 0.78350 0.69625 0.02758  0.04914  -0.00584 118 LEU A CG  
887  C CD1 . LEU A 124 ? 0.71703 0.85007 0.75448 0.03211  0.04826  -0.01263 118 LEU A CD1 
888  C CD2 . LEU A 124 ? 0.68267 0.83182 0.73226 0.02806  0.05795  -0.00164 118 LEU A CD2 
889  N N   . GLY A 125 ? 0.79368 0.95937 0.92086 0.02149  0.05330  -0.00244 119 GLY A N   
890  C CA  . GLY A 125 ? 0.79326 0.96820 0.93585 0.02107  0.05923  -0.00394 119 GLY A CA  
891  C C   . GLY A 125 ? 0.76285 0.93702 0.90352 0.01605  0.05852  -0.00479 119 GLY A C   
892  O O   . GLY A 125 ? 0.78762 0.96142 0.93176 0.01165  0.05021  -0.00322 119 GLY A O   
893  N N   . CYS A 126 ? 0.82469 0.99645 0.95873 0.01612  0.06552  -0.00686 120 CYS A N   
894  C CA  . CYS A 126 ? 0.69664 0.86986 0.82794 0.02024  0.07308  -0.00907 120 CYS A CA  
895  C C   . CYS A 126 ? 0.73677 0.91581 0.87403 0.01965  0.08002  -0.00947 120 CYS A C   
896  O O   . CYS A 126 ? 0.89072 1.06483 1.01948 0.01739  0.08131  -0.00926 120 CYS A O   
897  C CB  . CYS A 126 ? 0.74517 0.91173 0.86003 0.02225  0.07374  -0.01136 120 CYS A CB  
898  S SG  . CYS A 126 ? 0.83099 1.00157 0.94436 0.02466  0.08014  -0.01393 120 CYS A SG  
899  N N   . PHE A 127 ? 0.71675 0.90465 0.86609 0.02276  0.08443  -0.00997 121 PHE A N   
900  C CA  . PHE A 127 ? 0.66262 0.85954 0.81756 0.02235  0.09216  -0.00945 121 PHE A CA  
901  C C   . PHE A 127 ? 0.71049 0.91339 0.87137 0.03014  0.09825  -0.01318 121 PHE A C   
902  O O   . PHE A 127 ? 0.74433 0.94388 0.90926 0.03515  0.09463  -0.01513 121 PHE A O   
903  C CB  . PHE A 127 ? 0.78162 0.99000 0.95136 0.01588  0.09061  -0.00414 121 PHE A CB  
904  C CG  . PHE A 127 ? 0.70190 0.92260 0.89128 0.01832  0.08584  -0.00289 121 PHE A CG  
905  C CD1 . PHE A 127 ? 0.73280 0.94640 0.92080 0.01639  0.07453  -0.00181 121 PHE A CD1 
906  C CD2 . PHE A 127 ? 0.76616 1.00589 0.97399 0.02420  0.09234  -0.00303 121 PHE A CD2 
907  C CE1 . PHE A 127 ? 0.68424 0.90822 0.88895 0.01941  0.06804  -0.00009 121 PHE A CE1 
908  C CE2 . PHE A 127 ? 0.66594 0.91816 0.89336 0.02871  0.08653  -0.00188 121 PHE A CE2 
909  C CZ  . PHE A 127 ? 0.89055 1.13430 1.11650 0.02585  0.07348  0.00002  121 PHE A CZ  
910  N N   . TRP A 128 ? 0.75421 0.96317 0.91233 0.03162  0.10722  -0.01409 122 TRP A N   
911  C CA  . TRP A 128 ? 0.72426 0.94108 0.88699 0.04074  0.11482  -0.01839 122 TRP A CA  
912  C C   . TRP A 128 ? 0.69957 0.93935 0.87769 0.03946  0.12364  -0.01375 122 TRP A C   
913  O O   . TRP A 128 ? 0.79395 1.03805 0.97228 0.02929  0.12481  -0.00715 122 TRP A O   
914  C CB  . TRP A 128 ? 0.74351 0.94867 0.88542 0.04479  0.11899  -0.02439 122 TRP A CB  
915  C CG  . TRP A 128 ? 0.74190 0.92904 0.87224 0.04471  0.11080  -0.02871 122 TRP A CG  
916  C CD1 . TRP A 128 ? 0.75565 0.93670 0.88571 0.03877  0.10293  -0.02589 122 TRP A CD1 
917  C CD2 . TRP A 128 ? 0.85650 1.03081 0.97408 0.04997  0.10977  -0.03637 122 TRP A CD2 
918  N NE1 . TRP A 128 ? 0.78447 0.95394 0.90583 0.03867  0.09823  -0.02983 122 TRP A NE1 
919  C CE2 . TRP A 128 ? 0.64373 0.80706 0.75745 0.04451  0.10092  -0.03637 122 TRP A CE2 
920  C CE3 . TRP A 128 ? 0.83219 1.00289 0.93997 0.05877  0.11524  -0.04359 122 TRP A CE3 
921  C CZ2 . TRP A 128 ? 0.78542 0.93447 0.88870 0.04484  0.09589  -0.04233 122 TRP A CZ2 
922  C CZ3 . TRP A 128 ? 0.79081 0.94268 0.88409 0.06090  0.10918  -0.05125 122 TRP A CZ3 
923  C CH2 . TRP A 128 ? 0.84342 0.98468 0.93595 0.05263  0.09886  -0.05010 122 TRP A CH2 
924  N N   . VAL A 129 ? 0.68464 0.93924 0.87590 0.04988  0.12978  -0.01689 123 VAL A N   
925  C CA  . VAL A 129 ? 0.65431 0.93806 0.86314 0.05011  0.14113  -0.01252 123 VAL A CA  
926  C C   . VAL A 129 ? 0.70936 1.00198 0.91971 0.06752  0.15050  -0.02051 123 VAL A C   
927  O O   . VAL A 129 ? 0.76782 1.04786 0.97772 0.07872  0.14397  -0.02746 123 VAL A O   
928  C CB  . VAL A 129 ? 0.68743 0.99173 0.92541 0.04280  0.13493  -0.00504 123 VAL A CB  
929  C CG1 . VAL A 129 ? 0.72037 1.02194 0.97046 0.05240  0.12444  -0.00877 123 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.67622 1.01711 0.93744 0.04095  0.14738  0.00091  123 VAL A CG2 
931  N N   . SER A 130 ? 0.68120 0.99315 0.89040 0.07020  0.16588  -0.01943 124 SER A N   
932  C CA  . SER A 130 ? 0.74577 1.06443 0.94988 0.08905  0.17672  -0.02876 124 SER A CA  
933  C C   . SER A 130 ? 0.80500 1.16392 1.02631 0.09099  0.19480  -0.02326 124 SER A C   
934  O O   . SER A 130 ? 0.86507 1.23459 1.08348 0.07631  0.20214  -0.01336 124 SER A O   
935  C CB  . SER A 130 ? 0.72109 1.00999 0.88739 0.09354  0.17774  -0.03740 124 SER A CB  
936  O OG  . SER A 130 ? 0.75884 1.05525 0.91479 0.11087  0.19073  -0.04615 124 SER A OG  
937  N N   . ASP A 131 ? 0.72313 1.10458 0.96247 0.10946  0.20194  -0.02914 125 ASP A N   
938  C CA  . ASP A 131 ? 0.72916 1.15362 0.98438 0.11675  0.22247  -0.02631 125 ASP A CA  
939  C C   . ASP A 131 ? 0.75447 1.21641 1.04116 0.09654  0.22699  -0.00993 125 ASP A C   
940  O O   . ASP A 131 ? 0.81608 1.31535 1.11397 0.09577  0.24584  -0.00369 125 ASP A O   
941  C CB  . ASP A 131 ? 0.92524 1.34058 1.14370 0.12258  0.23781  -0.03126 125 ASP A CB  
942  C CG  . ASP A 131 ? 0.88982 1.27382 1.07967 0.14505  0.23492  -0.04903 125 ASP A CG  
943  O OD1 . ASP A 131 ? 0.80165 1.16879 1.00004 0.15492  0.22105  -0.05636 125 ASP A OD1 
944  O OD2 . ASP A 131 ? 0.85223 1.22588 1.00874 0.15230  0.24548  -0.05541 125 ASP A OD2 
945  N N   . ASP A 132 ? 0.68369 1.13621 0.98384 0.07958  0.20999  -0.00269 126 ASP A N   
946  C CA  . ASP A 132 ? 0.78290 1.26175 1.10842 0.05699  0.20998  0.01250  126 ASP A CA  
947  C C   . ASP A 132 ? 0.89382 1.37191 1.19813 0.04215  0.22341  0.02157  126 ASP A C   
948  O O   . ASP A 132 ? 0.78706 1.30072 1.11236 0.02929  0.23485  0.03391  126 ASP A O   
949  C CB  . ASP A 132 ? 0.55399 1.08707 0.92711 0.06187  0.21629  0.01704  126 ASP A CB  
950  C CG  . ASP A 132 ? 0.81254 1.34533 1.20988 0.06929  0.19724  0.01307  126 ASP A CG  
951  O OD1 . ASP A 132 ? 0.86260 1.35357 1.23961 0.06708  0.17991  0.00878  126 ASP A OD1 
952  O OD2 . ASP A 132 ? 0.71896 1.29529 1.15588 0.07769  0.19974  0.01488  126 ASP A OD2 
953  N N   . GLU A 133 ? 0.85440 1.29203 1.11677 0.04340  0.22143  0.01628  127 GLU A N   
954  C CA  . GLU A 133 ? 0.76048 1.19091 0.99574 0.03222  0.23248  0.02425  127 GLU A CA  
955  C C   . GLU A 133 ? 0.84692 1.22990 1.04877 0.02333  0.21790  0.02363  127 GLU A C   
956  O O   . GLU A 133 ? 1.01586 1.38895 1.20886 0.00509  0.21577  0.03521  127 GLU A O   
957  C CB  . GLU A 133 ? 0.77484 1.21436 0.98859 0.05018  0.25172  0.01699  127 GLU A CB  
958  C CG  . GLU A 133 ? 0.82582 1.31925 1.06866 0.05646  0.27262  0.02156  127 GLU A CG  
959  C CD  . GLU A 133 ? 1.09971 1.59863 1.31509 0.07723  0.29196  0.01224  127 GLU A CD  
960  O OE1 . GLU A 133 ? 1.08224 1.54038 1.25676 0.08643  0.28620  0.00120  127 GLU A OE1 
961  O OE2 . GLU A 133 ? 1.39098 1.93617 1.62549 0.08460  0.31270  0.01564  127 GLU A OE2 
962  N N   . ARG A 134 ? 0.84411 1.19792 1.02801 0.03608  0.20745  0.01064  128 ARG A N   
963  C CA  . ARG A 134 ? 0.72693 1.04146 0.88251 0.03072  0.19417  0.00869  128 ARG A CA  
964  C C   . ARG A 134 ? 0.74340 1.04313 0.91134 0.02953  0.17626  0.00474  128 ARG A C   
965  O O   . ARG A 134 ? 0.87240 1.18323 1.06115 0.03817  0.17316  -0.00044 128 ARG A O   
966  C CB  . ARG A 134 ? 0.73833 1.03198 0.86032 0.04423  0.19658  -0.00226 128 ARG A CB  
967  C CG  . ARG A 134 ? 0.94539 1.24437 1.04294 0.04445  0.21201  0.00200  128 ARG A CG  
968  C CD  . ARG A 134 ? 0.92409 1.20955 0.99342 0.06206  0.21543  -0.01192 128 ARG A CD  
969  N NE  . ARG A 134 ? 0.98965 1.29150 1.07598 0.07866  0.22115  -0.02219 128 ARG A NE  
970  C CZ  . ARG A 134 ? 0.94958 1.28414 1.04745 0.08701  0.23943  -0.02101 128 ARG A CZ  
971  N NH1 . ARG A 134 ? 0.91927 1.27578 1.01416 0.07785  0.25511  -0.00868 128 ARG A NH1 
972  N NH2 . ARG A 134 ? 1.20854 1.55453 1.32135 0.10531  0.24225  -0.03185 128 ARG A NH2 
973  N N   . CYS A 135 ? 0.69705 0.97108 0.85004 0.02017  0.16458  0.00728  129 CYS A N   
974  C CA  . CYS A 135 ? 0.73664 0.99675 0.89681 0.01907  0.14916  0.00402  129 CYS A CA  
975  C C   . CYS A 135 ? 0.77598 1.00738 0.91164 0.01513  0.13983  0.00350  129 CYS A C   
976  O O   . CYS A 135 ? 0.74285 0.96485 0.86111 0.00918  0.14222  0.00898  129 CYS A O   
977  C CB  . CYS A 135 ? 0.69134 0.96616 0.87826 0.00860  0.14347  0.01134  129 CYS A CB  
978  S SG  . CYS A 135 ? 0.82072 1.08689 1.00162 -0.01143 0.14037  0.02386  129 CYS A SG  
979  N N   . TYR A 136 ? 0.79284 1.01138 0.92733 0.01921  0.12933  -0.00258 130 TYR A N   
980  C CA  . TYR A 136 ? 0.72490 0.92261 0.84357 0.01663  0.11962  -0.00313 130 TYR A CA  
981  C C   . TYR A 136 ? 0.80662 1.00188 0.93688 0.01251  0.10977  -0.00195 130 TYR A C   
982  O O   . TYR A 136 ? 0.83445 1.03902 0.98041 0.01531  0.10785  -0.00391 130 TYR A O   
983  C CB  . TYR A 136 ? 0.77355 0.96105 0.87873 0.02484  0.11680  -0.01122 130 TYR A CB  
984  C CG  . TYR A 136 ? 0.71158 0.88624 0.80876 0.02427  0.10703  -0.01249 130 TYR A CG  
985  C CD1 . TYR A 136 ? 0.82688 0.99006 0.90687 0.02398  0.10414  -0.01084 130 TYR A CD1 
986  C CD2 . TYR A 136 ? 0.68618 0.86107 0.79212 0.02526  0.10110  -0.01495 130 TYR A CD2 
987  C CE1 . TYR A 136 ? 0.72123 0.87666 0.79576 0.02642  0.09619  -0.01279 130 TYR A CE1 
988  C CE2 . TYR A 136 ? 0.70495 0.87289 0.80395 0.02598  0.09461  -0.01604 130 TYR A CE2 
989  C CZ  . TYR A 136 ? 0.73561 0.89543 0.82030 0.02744  0.09248  -0.01557 130 TYR A CZ  
990  O OH  . TYR A 136 ? 0.83837 0.99504 0.91795 0.03103  0.08692  -0.01745 130 TYR A OH  
991  N N   . VAL A 137 ? 0.78679 0.96714 0.90656 0.00711  0.10268  0.00091  131 VAL A N   
992  C CA  . VAL A 137 ? 0.74762 0.92087 0.87057 0.00508  0.09245  0.00017  131 VAL A CA  
993  C C   . VAL A 137 ? 0.68998 0.84368 0.79233 0.00853  0.08640  -0.00248 131 VAL A C   
994  O O   . VAL A 137 ? 0.80037 0.94243 0.88836 0.00766  0.08679  -0.00014 131 VAL A O   
995  C CB  . VAL A 137 ? 0.75537 0.93234 0.89091 -0.00582 0.08819  0.00640  131 VAL A CB  
996  C CG1 . VAL A 137 ? 0.79300 0.95818 0.91764 -0.01499 0.08876  0.01306  131 VAL A CG1 
997  C CG2 . VAL A 137 ? 0.62666 0.79380 0.76107 -0.00657 0.07608  0.00401  131 VAL A CG2 
998  N N   . GLY A 138 ? 0.55417 0.70520 0.65444 0.01354  0.08121  -0.00695 132 GLY A N   
999  C CA  . GLY A 138 ? 0.81782 0.95670 0.90161 0.01981  0.07705  -0.01043 132 GLY A CA  
1000 C C   . GLY A 138 ? 0.74783 0.89198 0.83237 0.02510  0.07523  -0.01439 132 GLY A C   
1001 O O   . GLY A 138 ? 0.76582 0.91277 0.85689 0.02264  0.07253  -0.01373 132 GLY A O   
1002 N N   . ASN A 139 ? 0.82279 0.97009 0.90099 0.03197  0.07651  -0.01764 133 ASN A N   
1003 C CA  . ASN A 139 ? 0.75377 0.90928 0.83234 0.03584  0.07659  -0.01979 133 ASN A CA  
1004 C C   . ASN A 139 ? 0.77806 0.94783 0.86423 0.03634  0.08065  -0.02056 133 ASN A C   
1005 O O   . ASN A 139 ? 0.84229 1.02223 0.92871 0.03920  0.08169  -0.02141 133 ASN A O   
1006 C CB  . ASN A 139 ? 0.63480 0.78310 0.69880 0.04409  0.07327  -0.02311 133 ASN A CB  
1007 C CG  . ASN A 139 ? 0.82308 0.96384 0.87824 0.05023  0.07159  -0.02470 133 ASN A CG  
1008 O OD1 . ASN A 139 ? 0.89363 1.04659 0.95231 0.05468  0.07378  -0.02592 133 ASN A OD1 
1009 N ND2 . ASN A 139 ? 0.80546 0.92465 0.84862 0.04979  0.06615  -0.02409 133 ASN A ND2 
1010 N N   . ALA A 140 ? 0.82306 0.99421 0.91487 0.03320  0.08285  -0.02033 134 ALA A N   
1011 C CA  . ALA A 140 ? 0.66756 0.84741 0.76499 0.03194  0.08412  -0.02189 134 ALA A CA  
1012 C C   . ALA A 140 ? 0.77378 0.95291 0.87977 0.02738  0.08503  -0.02054 134 ALA A C   
1013 O O   . ALA A 140 ? 0.80953 0.98437 0.91836 0.02704  0.08670  -0.02108 134 ALA A O   
1014 C CB  . ALA A 140 ? 0.78654 0.96384 0.87876 0.03339  0.08430  -0.02407 134 ALA A CB  
1015 N N   . SER A 141 ? 0.77107 0.95457 0.88032 0.02475  0.08423  -0.01834 135 SER A N   
1016 C CA  . SER A 141 ? 0.75292 0.93133 0.86763 0.02102  0.08324  -0.01609 135 SER A CA  
1017 C C   . SER A 141 ? 0.73656 0.91033 0.85358 0.01916  0.08249  -0.01927 135 SER A C   
1018 O O   . SER A 141 ? 0.78206 0.95931 0.89666 0.01907  0.08209  -0.02265 135 SER A O   
1019 C CB  . SER A 141 ? 0.65258 0.83484 0.76642 0.01719  0.08268  -0.01124 135 SER A CB  
1020 O OG  . SER A 141 ? 1.12477 1.30703 1.23222 0.02016  0.08233  -0.00946 135 SER A OG  
1021 N N   . PHE A 142 ? 0.75678 0.92044 0.87676 0.01877  0.08081  -0.01877 136 PHE A N   
1022 C CA  . PHE A 142 ? 0.79185 0.94477 0.91031 0.01812  0.07850  -0.02310 136 PHE A CA  
1023 C C   . PHE A 142 ? 0.89666 1.04786 1.01542 0.00864  0.07412  -0.02040 136 PHE A C   
1024 O O   . PHE A 142 ? 0.85730 0.99415 0.97555 0.00440  0.06977  -0.01829 136 PHE A O   
1025 C CB  . PHE A 142 ? 0.66903 0.81004 0.78988 0.02380  0.07764  -0.02423 136 PHE A CB  
1026 C CG  . PHE A 142 ? 0.86415 0.99038 0.97922 0.02724  0.07566  -0.03144 136 PHE A CG  
1027 C CD1 . PHE A 142 ? 0.76807 0.89276 0.87523 0.02445  0.07437  -0.03673 136 PHE A CD1 
1028 C CD2 . PHE A 142 ? 0.85662 0.96918 0.97256 0.03477  0.07380  -0.03374 136 PHE A CD2 
1029 C CE1 . PHE A 142 ? 0.86195 0.96938 0.95937 0.02811  0.07109  -0.04483 136 PHE A CE1 
1030 C CE2 . PHE A 142 ? 0.91526 1.01042 1.02204 0.04027  0.07154  -0.04219 136 PHE A CE2 
1031 C CZ  . PHE A 142 ? 0.86743 0.95879 0.96348 0.03644  0.07009  -0.04808 136 PHE A CZ  
1032 N N   . THR A 143 ? 0.67481 0.84149 0.79517 0.00514  0.07491  -0.01978 137 THR A N   
1033 C CA  . THR A 143 ? 0.70527 0.87923 0.83065 -0.00539 0.07179  -0.01627 137 THR A CA  
1034 C C   . THR A 143 ? 0.71119 0.89463 0.83789 -0.00619 0.06860  -0.02164 137 THR A C   
1035 O O   . THR A 143 ? 0.87077 1.05930 0.99312 0.00223  0.07050  -0.02579 137 THR A O   
1036 C CB  . THR A 143 ? 0.75087 0.94286 0.88030 -0.00807 0.07635  -0.00882 137 THR A CB  
1037 O OG1 . THR A 143 ? 0.76825 0.97558 0.89695 0.00047  0.08009  -0.01169 137 THR A OG1 
1038 C CG2 . THR A 143 ? 0.78321 0.96435 0.90758 -0.00663 0.07776  -0.00353 137 THR A CG2 
1039 N N   . GLY A 144 ? 0.79232 0.94752 0.93464 -0.00559 0.19803  -0.15858 138 GLY A N   
1040 C CA  . GLY A 144 ? 0.81883 1.00429 0.98411 -0.01018 0.18215  -0.18513 138 GLY A CA  
1041 C C   . GLY A 144 ? 0.70917 0.91037 0.88645 -0.00939 0.16275  -0.18446 138 GLY A C   
1042 O O   . GLY A 144 ? 0.88676 1.11582 1.06954 -0.00693 0.13648  -0.19245 138 GLY A O   
1043 N N   . GLY A 145 ? 0.76436 0.94607 0.94431 -0.01118 0.17527  -0.17479 139 GLY A N   
1044 C CA  . GLY A 145 ? 0.67696 0.87105 0.87271 -0.00984 0.16025  -0.17566 139 GLY A CA  
1045 C C   . GLY A 145 ? 0.78889 0.99510 0.95849 0.00001  0.13216  -0.15343 139 GLY A C   
1046 O O   . GLY A 145 ? 0.94675 1.17538 1.13165 0.00402  0.10733  -0.15862 139 GLY A O   
1047 N N   . SER A 146 ? 0.84385 1.03468 0.97630 0.00405  0.13508  -0.12775 140 SER A N   
1048 C CA  . SER A 146 ? 0.79105 0.99071 0.90100 0.01093  0.11270  -0.10630 140 SER A CA  
1049 C C   . SER A 146 ? 0.68166 0.90365 0.78152 0.01427  0.09359  -0.10723 140 SER A C   
1050 O O   . SER A 146 ? 0.81136 1.04204 0.89807 0.01859  0.07282  -0.09270 140 SER A O   
1051 C CB  . SER A 146 ? 0.70991 0.89188 0.78952 0.01320  0.12054  -0.08193 140 SER A CB  
1052 O OG  . SER A 146 ? 0.78767 0.94754 0.86472 0.00963  0.13388  -0.07853 140 SER A OG  
1053 N N   . ILE A 147 ? 0.77785 1.00651 0.88057 0.01124  0.10141  -0.12423 141 ILE A N   
1054 C CA  . ILE A 147 ? 0.71110 0.95946 0.79538 0.01228  0.08542  -0.12796 141 ILE A CA  
1055 C C   . ILE A 147 ? 0.81320 1.08347 0.91782 0.01146  0.06237  -0.14801 141 ILE A C   
1056 O O   . ILE A 147 ? 0.76788 1.05347 0.84874 0.01372  0.03960  -0.14424 141 ILE A O   
1057 C CB  . ILE A 147 ? 0.69618 0.94057 0.77162 0.00907  0.10586  -0.13881 141 ILE A CB  
1058 C CG1 . ILE A 147 ? 0.81775 1.04407 0.87796 0.01301  0.12299  -0.11638 141 ILE A CG1 
1059 C CG2 . ILE A 147 ? 0.57009 0.83400 0.62095 0.00743  0.09337  -0.14815 141 ILE A CG2 
1060 C CD1 . ILE A 147 ? 0.71641 0.93643 0.77620 0.01237  0.14453  -0.12617 141 ILE A CD1 
1061 N N   . HIS A 148 ? 0.76495 1.03720 0.91299 0.00823  0.06680  -0.16829 142 HIS A N   
1062 C CA  . HIS A 148 ? 0.64727 0.94508 0.82602 0.00700  0.04550  -0.19353 142 HIS A CA  
1063 C C   . HIS A 148 ? 0.72000 1.02489 0.94408 0.01049  0.03399  -0.19868 142 HIS A C   
1064 O O   . HIS A 148 ? 0.79765 1.12180 1.03213 0.01759  0.00121  -0.19804 142 HIS A O   
1065 C CB  . HIS A 148 ? 0.72215 1.02322 0.92537 -0.00311 0.06465  -0.22551 142 HIS A CB  
1066 C CG  . HIS A 148 ? 0.73111 1.06322 0.96294 -0.00601 0.04011  -0.25525 142 HIS A CG  
1067 N ND1 . HIS A 148 ? 0.64542 0.98838 0.86973 -0.01361 0.04099  -0.27948 142 HIS A ND1 
1068 C CD2 . HIS A 148 ? 0.72594 1.08182 0.99781 -0.00220 0.01265  -0.26677 142 HIS A CD2 
1069 C CE1 . HIS A 148 ? 0.83060 1.20400 1.08496 -0.01521 0.01270  -0.30454 142 HIS A CE1 
1070 N NE2 . HIS A 148 ? 0.82329 1.20590 1.10951 -0.00736 -0.00588 -0.29642 142 HIS A NE2 
1071 N N   . THR A 149 ? 0.77774 1.06589 1.02876 0.00576  0.06113  -0.20389 143 THR A N   
1072 C CA  . THR A 149 ? 0.58395 0.88126 0.89058 0.00574  0.05932  -0.22036 143 THR A CA  
1073 C C   . THR A 149 ? 0.63349 0.91298 0.93750 0.01000  0.06480  -0.20189 143 THR A C   
1074 O O   . THR A 149 ? 0.76516 1.05296 1.11726 0.01151  0.06246  -0.21558 143 THR A O   
1075 C CB  . THR A 149 ? 0.48304 0.77667 0.83091 -0.00706 0.09113  -0.24971 143 THR A CB  
1076 O OG1 . THR A 149 ? 0.77143 1.02966 1.08997 -0.01325 0.12661  -0.23612 143 THR A OG1 
1077 C CG2 . THR A 149 ? 0.62008 0.93044 0.97512 -0.01314 0.08709  -0.27244 143 THR A CG2 
1078 N N   . ILE A 150 ? 0.78303 1.04003 1.03723 0.01156  0.07212  -0.17422 144 ILE A N   
1079 C CA  . ILE A 150 ? 0.72053 0.95937 0.96750 0.01347  0.07766  -0.15888 144 ILE A CA  
1080 C C   . ILE A 150 ? 0.59402 0.83504 0.81269 0.02275  0.05002  -0.13275 144 ILE A C   
1081 O O   . ILE A 150 ? 0.88836 1.13095 1.06860 0.02419  0.04246  -0.11725 144 ILE A O   
1082 C CB  . ILE A 150 ? 0.79484 1.00425 1.00900 0.00594  0.10872  -0.14910 144 ILE A CB  
1083 C CG1 . ILE A 150 ? 0.78050 0.98118 1.01894 -0.00477 0.13947  -0.17220 144 ILE A CG1 
1084 C CG2 . ILE A 150 ? 0.68666 0.87861 0.88751 0.00643  0.11155  -0.13565 144 ILE A CG2 
1085 C CD1 . ILE A 150 ? 0.77337 0.94118 0.97280 -0.01123 0.16758  -0.15910 144 ILE A CD1 
1086 N N   . LYS A 151 ? 0.65475 0.89413 0.89470 0.02822  0.03779  -0.12883 145 LYS A N   
1087 C CA  . LYS A 151 ? 0.68783 0.92331 0.90360 0.03564  0.01452  -0.10267 145 LYS A CA  
1088 C C   . LYS A 151 ? 0.75852 0.97395 0.92907 0.03083  0.02861  -0.08136 145 LYS A C   
1089 O O   . LYS A 151 ? 0.82650 1.02555 0.99493 0.02497  0.04935  -0.08468 145 LYS A O   
1090 C CB  . LYS A 151 ? 0.61242 0.84627 0.86868 0.04273  0.00113  -0.10522 145 LYS A CB  
1091 C CG  . LYS A 151 ? 0.48709 0.71100 0.72191 0.04962  -0.02114 -0.07709 145 LYS A CG  
1092 C CD  . LYS A 151 ? 0.54307 0.76212 0.82533 0.05794  -0.03345 -0.08116 145 LYS A CD  
1093 C CE  . LYS A 151 ? 0.64852 0.85380 0.91133 0.06483  -0.05652 -0.05133 145 LYS A CE  
1094 N NZ  . LYS A 151 ? 0.84416 1.03100 1.05959 0.05553  -0.04182 -0.03201 145 LYS A NZ  
1095 N N   . THR A 152 ? 0.82242 1.04005 0.95644 0.03254  0.01744  -0.06048 146 THR A N   
1096 C CA  . THR A 152 ? 0.79369 0.99829 0.89345 0.02872  0.02695  -0.04050 146 THR A CA  
1097 C C   . THR A 152 ? 0.71104 0.91477 0.79326 0.03179  0.00789  -0.01701 146 THR A C   
1098 O O   . THR A 152 ? 0.76945 0.98036 0.85605 0.03745  -0.01292 -0.01327 146 THR A O   
1099 C CB  . THR A 152 ? 0.73257 0.93997 0.80806 0.02524  0.04252  -0.04017 146 THR A CB  
1100 O OG1 . THR A 152 ? 0.90642 1.12830 0.96480 0.02729  0.03131  -0.03597 146 THR A OG1 
1101 C CG2 . THR A 152 ? 0.75119 0.95618 0.84405 0.02173  0.06164  -0.06240 146 THR A CG2 
1102 N N   . LEU A 153 ? 0.72402 0.91800 0.78635 0.02754  0.01452  -0.00040 147 LEU A N   
1103 C CA  . LEU A 153 ? 0.67473 0.86552 0.71957 0.02708  0.00294  0.02281  147 LEU A CA  
1104 C C   . LEU A 153 ? 0.80696 0.99901 0.83040 0.02101  0.01626  0.03450  147 LEU A C   
1105 O O   . LEU A 153 ? 0.85632 1.04379 0.88332 0.01797  0.02776  0.02993  147 LEU A O   
1106 C CB  . LEU A 153 ? 0.70563 0.88081 0.76981 0.02794  -0.00705 0.02925  147 LEU A CB  
1107 C CG  . LEU A 153 ? 0.74034 0.90648 0.78908 0.02544  -0.01618 0.05470  147 LEU A CG  
1108 C CD1 . LEU A 153 ? 0.70078 0.87194 0.72950 0.03021  -0.03166 0.06740  147 LEU A CD1 
1109 C CD2 . LEU A 153 ? 0.70437 0.85116 0.77799 0.02537  -0.02269 0.05762  147 LEU A CD2 
1110 N N   . GLY A 154 ? 0.84288 1.04137 0.84413 0.01919  0.01447  0.04940  148 GLY A N   
1111 C CA  . GLY A 154 ? 0.74607 0.95020 0.73653 0.01382  0.02789  0.05891  148 GLY A CA  
1112 C C   . GLY A 154 ? 0.69585 0.90135 0.66599 0.00912  0.02623  0.07807  148 GLY A C   
1113 O O   . GLY A 154 ? 0.78028 0.97829 0.73811 0.01046  0.01264  0.08732  148 GLY A O   
1114 N N   . VAL A 155 ? 0.78213 0.99655 0.74988 0.00358  0.04065  0.08474  149 VAL A N   
1115 C CA  . VAL A 155 ? 0.79526 1.01143 0.74498 -0.00405 0.04690  0.10191  149 VAL A CA  
1116 C C   . VAL A 155 ? 0.85468 1.08844 0.79393 -0.00556 0.06626  0.09524  149 VAL A C   
1117 O O   . VAL A 155 ? 0.80225 1.04627 0.76137 -0.00181 0.07576  0.08340  149 VAL A O   
1118 C CB  . VAL A 155 ? 0.82912 1.04054 0.79836 -0.01225 0.04896  0.11499  149 VAL A CB  
1119 C CG1 . VAL A 155 ? 0.83130 1.03952 0.78192 -0.02232 0.05769  0.13416  149 VAL A CG1 
1120 C CG2 . VAL A 155 ? 0.75287 0.94616 0.73873 -0.01061 0.03283  0.11502  149 VAL A CG2 
1121 N N   . TYR A 156 ? 0.79520 1.03008 0.70167 -0.01096 0.07274  0.10293  150 TYR A N   
1122 C CA  . TYR A 156 ? 0.76518 1.01576 0.66018 -0.01457 0.09553  0.09495  150 TYR A CA  
1123 C C   . TYR A 156 ? 0.86292 1.11405 0.74516 -0.02697 0.11173  0.11215  150 TYR A C   
1124 O O   . TYR A 156 ? 1.02494 1.25955 0.87792 -0.03293 0.10384  0.13064  150 TYR A O   
1125 C CB  . TYR A 156 ? 0.81543 1.06784 0.67512 -0.01209 0.09323  0.08144  150 TYR A CB  
1126 C CG  . TYR A 156 ? 0.85726 1.12183 0.69446 -0.01890 0.11887  0.07340  150 TYR A CG  
1127 C CD1 . TYR A 156 ? 0.97082 1.25006 0.83690 -0.01566 0.13943  0.05511  150 TYR A CD1 
1128 C CD2 . TYR A 156 ? 0.88591 1.14483 0.67160 -0.02858 0.12366  0.08410  150 TYR A CD2 
1129 C CE1 . TYR A 156 ? 0.81790 1.10825 0.66905 -0.02177 0.16612  0.04411  150 TYR A CE1 
1130 C CE2 . TYR A 156 ? 0.88351 1.15276 0.64527 -0.03669 0.15125  0.07363  150 TYR A CE2 
1131 C CZ  . TYR A 156 ? 0.90489 1.19106 0.70292 -0.03319 0.17343  0.05180  150 TYR A CZ  
1132 O OH  . TYR A 156 ? 0.82092 1.11741 0.60053 -0.04113 0.20396  0.03786  150 TYR A OH  
1133 N N   . SER A 157 ? 1.00051 1.26960 0.90744 -0.03076 0.13519  0.10644  151 SER A N   
1134 C CA  . SER A 157 ? 1.02140 1.29519 0.92434 -0.04447 0.15741  0.11860  151 SER A CA  
1135 C C   . SER A 157 ? 0.90673 1.20185 0.81707 -0.04628 0.18723  0.10213  151 SER A C   
1136 O O   . SER A 157 ? 1.00639 1.31657 0.95533 -0.03640 0.19070  0.08589  151 SER A O   
1137 C CB  . SER A 157 ? 0.92328 1.20058 0.87243 -0.04965 0.15580  0.12920  151 SER A CB  
1138 O OG  . SER A 157 ? 0.90751 1.19522 0.86586 -0.06384 0.18270  0.13605  151 SER A OG  
1139 N N   . ASP A 158 ? 0.92650 1.22022 0.79829 -0.05900 0.20993  0.10662  152 ASP A N   
1140 C CA  . ASP A 158 ? 0.97217 1.28609 0.85369 -0.06395 0.24518  0.09006  152 ASP A CA  
1141 C C   . ASP A 158 ? 1.03369 1.36097 0.95170 -0.07692 0.27098  0.09880  152 ASP A C   
1142 O O   . ASP A 158 ? 1.08571 1.42320 0.99437 -0.08816 0.30612  0.09158  152 ASP A O   
1143 C CB  . ASP A 158 ? 0.95059 1.25570 0.76094 -0.07135 0.25808  0.08312  152 ASP A CB  
1144 C CG  . ASP A 158 ? 1.06473 1.34539 0.81181 -0.08450 0.25292  0.10932  152 ASP A CG  
1145 O OD1 . ASP A 158 ? 1.26340 1.52827 1.01825 -0.08296 0.22885  0.13099  152 ASP A OD1 
1146 O OD2 . ASP A 158 ? 1.10740 1.38206 0.79462 -0.09651 0.27331  0.10837  152 ASP A OD2 
1147 N N   . TYR A 159 ? 1.07795 1.40616 1.03946 -0.07696 0.25551  0.11177  153 TYR A N   
1148 C CA  . TYR A 159 ? 1.00236 1.34627 1.00982 -0.09013 0.27669  0.11799  153 TYR A CA  
1149 C C   . TYR A 159 ? 0.94390 1.32117 1.02963 -0.07938 0.28034  0.10007  153 TYR A C   
1150 O O   . TYR A 159 ? 0.83083 1.21029 0.94788 -0.06645 0.25119  0.09908  153 TYR A O   
1151 C CB  . TYR A 159 ? 0.89492 1.22112 0.90847 -0.09767 0.25690  0.13964  153 TYR A CB  
1152 C CG  . TYR A 159 ? 0.85928 1.19681 0.91253 -0.11638 0.28114  0.14744  153 TYR A CG  
1153 C CD1 . TYR A 159 ? 1.03538 1.37168 1.06240 -0.13422 0.31996  0.15192  153 TYR A CD1 
1154 C CD2 . TYR A 159 ? 0.90625 1.25542 1.02209 -0.11812 0.26643  0.14878  153 TYR A CD2 
1155 C CE1 . TYR A 159 ? 0.92115 1.26808 0.98949 -0.15360 0.34621  0.15782  153 TYR A CE1 
1156 C CE2 . TYR A 159 ? 0.83703 1.19899 0.99661 -0.13697 0.28866  0.15320  153 TYR A CE2 
1157 C CZ  . TYR A 159 ? 0.95374 1.31464 1.09229 -0.15484 0.32980  0.15796  153 TYR A CZ  
1158 O OH  . TYR A 159 ? 1.08792 1.46175 1.27479 -0.17576 0.35588  0.16122  153 TYR A OH  
1159 N N   . PRO A 160 ? 0.90122 1.30362 1.01956 -0.08372 0.31475  0.08589  154 PRO A N   
1160 C CA  . PRO A 160 ? 0.64706 1.08066 0.84233 -0.06920 0.31571  0.06854  154 PRO A CA  
1161 C C   . PRO A 160 ? 0.80612 1.25502 1.06530 -0.06614 0.29089  0.07587  154 PRO A C   
1162 O O   . PRO A 160 ? 0.86494 1.32223 1.15894 -0.04819 0.26678  0.07016  154 PRO A O   
1163 C CB  . PRO A 160 ? 0.73133 1.18855 0.95277 -0.07941 0.36261  0.05378  154 PRO A CB  
1164 C CG  . PRO A 160 ? 0.70265 1.13486 0.83602 -0.09381 0.38378  0.05718  154 PRO A CG  
1165 C CD  . PRO A 160 ? 0.82494 1.22542 0.90363 -0.10046 0.35519  0.08319  154 PRO A CD  
1166 N N   . PRO A 161 ? 0.82875 1.28044 1.10431 -0.08384 0.29536  0.08806  155 PRO A N   
1167 C CA  . PRO A 161 ? 0.72981 1.19785 1.06675 -0.08172 0.26840  0.09092  155 PRO A CA  
1168 C C   . PRO A 161 ? 0.79675 1.24308 1.10822 -0.06879 0.22594  0.09710  155 PRO A C   
1169 O O   . PRO A 161 ? 0.87182 1.33368 1.22780 -0.05823 0.20069  0.09288  155 PRO A O   
1170 C CB  . PRO A 161 ? 0.67792 1.14267 1.02139 -0.10659 0.28362  0.10298  155 PRO A CB  
1171 C CG  . PRO A 161 ? 0.65723 1.12124 0.97439 -0.12017 0.32850  0.10146  155 PRO A CG  
1172 C CD  . PRO A 161 ? 0.85002 1.29164 1.09569 -0.10775 0.32670  0.09852  155 PRO A CD  
1173 N N   . LEU A 162 ? 0.88897 1.30006 1.12986 -0.06941 0.21724  0.10649  156 LEU A N   
1174 C CA  . LEU A 162 ? 0.77299 1.16359 0.99209 -0.05822 0.18193  0.10954  156 LEU A CA  
1175 C C   . LEU A 162 ? 0.81059 1.20311 1.02683 -0.03807 0.17315  0.09788  156 LEU A C   
1176 O O   . LEU A 162 ? 0.76756 1.16023 1.00071 -0.02716 0.14831  0.09598  156 LEU A O   
1177 C CB  . LEU A 162 ? 0.81417 1.16897 0.96984 -0.06447 0.17539  0.12228  156 LEU A CB  
1178 C CG  . LEU A 162 ? 0.87486 1.20838 1.01242 -0.05474 0.14321  0.12311  156 LEU A CG  
1179 C CD1 . LEU A 162 ? 0.89528 1.23136 1.06909 -0.06130 0.12553  0.12561  156 LEU A CD1 
1180 C CD2 . LEU A 162 ? 0.78813 1.09032 0.86851 -0.05592 0.13764  0.13248  156 LEU A CD2 
1181 N N   . ALA A 163 ? 0.81654 1.20782 1.00826 -0.03420 0.19432  0.08968  157 ALA A N   
1182 C CA  . ALA A 163 ? 0.76558 1.15549 0.95793 -0.01653 0.18987  0.07753  157 ALA A CA  
1183 C C   . ALA A 163 ? 0.74630 1.16130 1.00491 -0.00468 0.18621  0.07161  157 ALA A C   
1184 O O   . ALA A 163 ? 0.83266 1.24038 1.09762 0.01032  0.16716  0.07018  157 ALA A O   
1185 C CB  . ALA A 163 ? 0.71296 1.09965 0.87281 -0.01735 0.21638  0.06585  157 ALA A CB  
1186 N N   . THR A 164 ? 0.80971 1.25387 1.11963 -0.01122 0.20426  0.06880  158 THR A N   
1187 C CA  . THR A 164 ? 0.67944 1.15186 1.06214 0.00143  0.19689  0.06365  158 THR A CA  
1188 C C   . THR A 164 ? 0.75349 1.22389 1.14875 0.00646  0.15731  0.07342  158 THR A C   
1189 O O   . THR A 164 ? 0.83680 1.31068 1.25670 0.02378  0.13759  0.07328  158 THR A O   
1190 C CB  . THR A 164 ? 0.70032 1.20797 1.14293 -0.00934 0.22367  0.05738  158 THR A CB  
1191 O OG1 . THR A 164 ? 0.75571 1.26355 1.18055 -0.01472 0.26377  0.04582  158 THR A OG1 
1192 C CG2 . THR A 164 ? 0.57826 1.11948 1.10635 0.00591  0.21168  0.05153  158 THR A CG2 
1193 N N   . ASP A 165 ? 0.77300 1.23484 1.14846 -0.00882 0.14541  0.08206  159 ASP A N   
1194 C CA  . ASP A 165 ? 0.74369 1.20147 1.12370 -0.00671 0.10928  0.08769  159 ASP A CA  
1195 C C   . ASP A 165 ? 0.74280 1.16966 1.07349 0.00644  0.09026  0.09000  159 ASP A C   
1196 O O   . ASP A 165 ? 0.76587 1.19095 1.10235 0.01477  0.06268  0.09262  159 ASP A O   
1197 C CB  . ASP A 165 ? 0.62947 1.07926 0.99698 -0.02699 0.10488  0.09359  159 ASP A CB  
1198 C CG  . ASP A 165 ? 0.90053 1.36903 1.31133 -0.03135 0.07753  0.09244  159 ASP A CG  
1199 O OD1 . ASP A 165 ? 0.73169 1.22786 1.19200 -0.01989 0.06432  0.08806  159 ASP A OD1 
1200 O OD2 . ASP A 165 ? 1.00506 1.46026 1.40182 -0.04590 0.06779  0.09518  159 ASP A OD2 
1201 N N   . LEU A 166 ? 0.80976 1.21230 1.09098 0.00744  0.10473  0.08845  160 LEU A N   
1202 C CA  . LEU A 166 ? 0.79898 1.17386 1.04059 0.01852  0.09187  0.08810  160 LEU A CA  
1203 C C   . LEU A 166 ? 0.83127 1.21018 1.09613 0.03666  0.09313  0.08459  160 LEU A C   
1204 O O   . LEU A 166 ? 0.74781 1.10879 0.99736 0.04668  0.07555  0.08829  160 LEU A O   
1205 C CB  . LEU A 166 ? 0.78298 1.13498 0.97362 0.01374  0.10488  0.08520  160 LEU A CB  
1206 C CG  . LEU A 166 ? 0.82887 1.15333 0.98311 0.02192  0.09465  0.08221  160 LEU A CG  
1207 C CD1 . LEU A 166 ? 0.63025 0.94261 0.77637 0.02068  0.06984  0.08751  160 LEU A CD1 
1208 C CD2 . LEU A 166 ? 0.72515 1.03348 0.83849 0.01646  0.10338  0.07793  160 LEU A CD2 
1209 N N   . ARG A 167 ? 0.84375 1.24340 1.14540 0.04075  0.11582  0.07752  161 ARG A N   
1210 C CA  . ARG A 167 ? 0.64791 1.05066 0.98203 0.05951  0.11804  0.07411  161 ARG A CA  
1211 C C   . ARG A 167 ? 0.78110 1.19609 1.15411 0.07041  0.08830  0.08394  161 ARG A C   
1212 O O   . ARG A 167 ? 0.79150 1.19404 1.17149 0.08766  0.07760  0.08855  161 ARG A O   
1213 C CB  . ARG A 167 ? 0.63793 1.06365 1.01198 0.06043  0.15073  0.06135  161 ARG A CB  
1214 C CG  . ARG A 167 ? 0.67301 1.09792 1.08379 0.08053  0.15880  0.05475  161 ARG A CG  
1215 C CD  . ARG A 167 ? 0.64883 1.10493 1.13756 0.09293  0.14717  0.05840  161 ARG A CD  
1216 N NE  . ARG A 167 ? 0.67451 1.16806 1.21023 0.08126  0.16832  0.04942  161 ARG A NE  
1217 C CZ  . ARG A 167 ? 0.66797 1.19772 1.27842 0.08611  0.15841  0.05027  161 ARG A CZ  
1218 N NH1 . ARG A 167 ? 0.80265 1.33663 1.44601 0.10371  0.12297  0.06126  161 ARG A NH1 
1219 N NH2 . ARG A 167 ? 0.67112 1.23365 1.32393 0.07232  0.18427  0.03996  161 ARG A NH2 
1220 N N   . ARG A 168 ? 0.82906 1.26695 1.22699 0.06023  0.07353  0.08757  162 ARG A N   
1221 C CA  . ARG A 168 ? 0.73819 1.18982 1.16873 0.06907  0.03946  0.09553  162 ARG A CA  
1222 C C   . ARG A 168 ? 0.61533 1.03228 0.98766 0.07296  0.01281  0.10510  162 ARG A C   
1223 O O   . ARG A 168 ? 0.64575 1.06031 1.02696 0.08704  -0.01319 0.11420  162 ARG A O   
1224 C CB  . ARG A 168 ? 0.55505 1.03902 1.02472 0.05360  0.03036  0.09335  162 ARG A CB  
1225 C CG  . ARG A 168 ? 0.85403 1.38202 1.40775 0.05580  0.04588  0.08542  162 ARG A CG  
1226 C CD  . ARG A 168 ? 0.81263 1.37170 1.40767 0.03709  0.03970  0.08169  162 ARG A CD  
1227 N NE  . ARG A 168 ? 0.84416 1.39769 1.41760 0.01520  0.07272  0.07789  162 ARG A NE  
1228 C CZ  . ARG A 168 ? 0.77707 1.35773 1.39776 0.00492  0.10525  0.06978  162 ARG A CZ  
1229 N NH1 . ARG A 168 ? 0.57640 1.19656 1.27915 0.01442  0.11075  0.06124  162 ARG A NH1 
1230 N NH2 . ARG A 168 ? 0.81808 1.38499 1.40352 -0.01534 0.13353  0.07068  162 ARG A NH2 
1231 N N   . ARG A 169 ? 0.62841 1.01757 0.94092 0.06081  0.01909  0.10344  163 ARG A N   
1232 C CA  . ARG A 169 ? 0.74296 1.09713 0.99978 0.06343  0.00222  0.10925  163 ARG A CA  
1233 C C   . ARG A 169 ? 0.74173 1.07204 0.98553 0.08014  0.01006  0.11307  163 ARG A C   
1234 O O   . ARG A 169 ? 0.86376 1.17056 1.07923 0.08775  -0.00785 0.12271  163 ARG A O   
1235 C CB  . ARG A 169 ? 0.62158 0.95404 0.82938 0.04799  0.01098  0.10374  163 ARG A CB  
1236 C CG  . ARG A 169 ? 0.71186 1.06169 0.93369 0.03072  0.01078  0.10034  163 ARG A CG  
1237 C CD  . ARG A 169 ? 0.80633 1.17324 1.05101 0.02622  -0.01710 0.10229  163 ARG A CD  
1238 N NE  . ARG A 169 ? 0.74975 1.12097 0.99683 0.00732  -0.01863 0.09782  163 ARG A NE  
1239 C CZ  . ARG A 169 ? 0.67879 1.07748 0.97178 -0.00306 -0.01057 0.09591  163 ARG A CZ  
1240 N NH1 . ARG A 169 ? 0.99661 1.42444 1.33890 0.00313  0.00193  0.09596  163 ARG A NH1 
1241 N NH2 . ARG A 169 ? 0.84291 1.23844 1.13545 -0.02080 -0.01269 0.09290  163 ARG A NH2 
1242 N N   . PHE A 170 ? 0.79195 1.12545 1.05357 0.08471  0.03798  0.10519  164 PHE A N   
1243 C CA  . PHE A 170 ? 0.73839 1.04868 0.99631 0.09977  0.04859  0.10629  164 PHE A CA  
1244 C C   . PHE A 170 ? 0.81290 1.13151 1.11493 0.11909  0.03140  0.11789  164 PHE A C   
1245 O O   . PHE A 170 ? 0.94823 1.23690 1.23386 0.13208  0.02533  0.12812  164 PHE A O   
1246 C CB  . PHE A 170 ? 0.75756 1.07240 1.02672 0.09809  0.08253  0.09072  164 PHE A CB  
1247 C CG  . PHE A 170 ? 0.77809 1.06693 1.04539 0.11076  0.09739  0.08726  164 PHE A CG  
1248 C CD1 . PHE A 170 ? 0.84027 1.09685 1.06000 0.10546  0.10600  0.08216  164 PHE A CD1 
1249 C CD2 . PHE A 170 ? 0.79068 1.08754 1.11046 0.12765  0.10419  0.08737  164 PHE A CD2 
1250 C CE1 . PHE A 170 ? 0.91666 1.14781 1.13834 0.11482  0.12184  0.07729  164 PHE A CE1 
1251 C CE2 . PHE A 170 ? 0.80149 1.07026 1.12261 0.13875  0.11968  0.08354  164 PHE A CE2 
1252 C CZ  . PHE A 170 ? 0.85974 1.09483 1.13035 0.13131  0.12899  0.07845  164 PHE A CZ  
1253 N N   . ASP A 171 ? 0.82253 1.18098 1.18383 0.12138  0.02351  0.11705  165 ASP A N   
1254 C CA  . ASP A 171 ? 0.67761 1.04949 1.09072 0.14155  0.00165  0.12813  165 ASP A CA  
1255 C C   . ASP A 171 ? 0.84747 1.19843 1.22121 0.14638  -0.03732 0.14670  165 ASP A C   
1256 O O   . ASP A 171 ? 0.94611 1.28044 1.32669 0.16588  -0.05412 0.16203  165 ASP A O   
1257 C CB  . ASP A 171 ? 0.80155 1.22556 1.29067 0.13981  -0.00070 0.12076  165 ASP A CB  
1258 C CG  . ASP A 171 ? 0.94376 1.38736 1.47440 0.13721  0.04077  0.10289  165 ASP A CG  
1259 O OD1 . ASP A 171 ? 0.78647 1.20849 1.31173 0.14684  0.06381  0.09771  165 ASP A OD1 
1260 O OD2 . ASP A 171 ? 0.75157 1.23071 1.31896 0.12413  0.05205  0.09297  165 ASP A OD2 
1261 N N   . THR A 172 ? 0.94841 1.29715 1.27807 0.12862  -0.05163 0.14572  166 THR A N   
1262 C CA  . THR A 172 ? 0.82547 1.15331 1.10797 0.12978  -0.08651 0.15999  166 THR A CA  
1263 C C   . THR A 172 ? 0.97988 1.25472 1.19831 0.13535  -0.07823 0.17018  166 THR A C   
1264 O O   . THR A 172 ? 1.05380 1.30628 1.25344 0.14931  -0.10039 0.18887  166 THR A O   
1265 C CB  . THR A 172 ? 0.77221 1.10740 1.02326 0.10736  -0.09719 0.15130  166 THR A CB  
1266 O OG1 . THR A 172 ? 0.84749 1.22878 1.16067 0.09909  -0.09694 0.14053  166 THR A OG1 
1267 C CG2 . THR A 172 ? 0.81434 1.13536 1.02187 0.10724  -0.13566 0.16233  166 THR A CG2 
1268 N N   . PHE A 173 ? 0.88704 1.14069 1.07218 0.12418  -0.04668 0.15863  167 PHE A N   
1269 C CA  . PHE A 173 ? 0.87088 1.07565 0.99849 0.12524  -0.03507 0.16468  167 PHE A CA  
1270 C C   . PHE A 173 ? 0.92525 1.11017 1.07579 0.14554  -0.02606 0.17547  167 PHE A C   
1271 O O   . PHE A 173 ? 0.99151 1.13597 1.10215 0.15264  -0.03248 0.19209  167 PHE A O   
1272 C CB  . PHE A 173 ? 0.89863 1.09290 0.99965 0.10914  -0.00517 0.14665  167 PHE A CB  
1273 C CG  . PHE A 173 ? 0.72954 0.92901 0.79884 0.09050  -0.01327 0.13846  167 PHE A CG  
1274 C CD1 . PHE A 173 ? 0.75198 0.93989 0.78307 0.08588  -0.03865 0.14655  167 PHE A CD1 
1275 C CD2 . PHE A 173 ? 0.72708 0.94083 0.80326 0.07775  0.00403  0.12253  167 PHE A CD2 
1276 C CE1 . PHE A 173 ? 0.83911 1.02989 0.84514 0.06848  -0.04367 0.13576  167 PHE A CE1 
1277 C CE2 . PHE A 173 ? 0.64025 0.85535 0.69311 0.06221  -0.00298 0.11554  167 PHE A CE2 
1278 C CZ  . PHE A 173 ? 0.73641 0.94023 0.75713 0.05739  -0.02542 0.12059  167 PHE A CZ  
1279 N N   . LYS A 174 ? 0.80250 1.01228 1.01596 0.15434  -0.00882 0.16596  168 LYS A N   
1280 C CA  . LYS A 174 ? 0.72742 0.91726 0.97068 0.17397  0.00284  0.17288  168 LYS A CA  
1281 C C   . LYS A 174 ? 0.77807 0.95742 1.03141 0.19421  -0.03155 0.19948  168 LYS A C   
1282 O O   . LYS A 174 ? 0.83369 0.97569 1.08404 0.20971  -0.02779 0.21405  168 LYS A O   
1283 C CB  . LYS A 174 ? 0.69783 0.92153 1.01146 0.17904  0.02692  0.15457  168 LYS A CB  
1284 C CG  . LYS A 174 ? 0.63632 0.83823 0.98657 0.19823  0.04496  0.15577  168 LYS A CG  
1285 C CD  . LYS A 174 ? 0.87509 1.11524 1.30207 0.20475  0.06605  0.13686  168 LYS A CD  
1286 C CE  . LYS A 174 ? 1.05516 1.27268 1.52767 0.22670  0.08074  0.13834  168 LYS A CE  
1287 N NZ  . LYS A 174 ? 0.93715 1.19282 1.49121 0.23460  0.10235  0.11821  168 LYS A NZ  
1288 N N   . ALA A 175 ? 0.89154 1.10149 1.15596 0.19409  -0.06678 0.20662  169 ALA A N   
1289 C CA  . ALA A 175 ? 0.81459 1.02035 1.08957 0.21387  -0.10701 0.23200  169 ALA A CA  
1290 C C   . ALA A 175 ? 0.98411 1.13318 1.17302 0.21439  -0.12130 0.25543  169 ALA A C   
1291 O O   . ALA A 175 ? 1.23531 1.36816 1.42244 0.23351  -0.15281 0.28149  169 ALA A O   
1292 C CB  . ALA A 175 ? 0.79122 1.04668 1.09651 0.20948  -0.14250 0.22938  169 ALA A CB  
1293 N N   . PHE A 176 ? 1.15078 1.26880 1.26926 0.19416  -0.09889 0.24742  170 PHE A N   
1294 C CA  . PHE A 176 ? 1.17579 1.23875 1.20835 0.19046  -0.10522 0.26684  170 PHE A CA  
1295 C C   . PHE A 176 ? 1.18989 1.20211 1.20614 0.19506  -0.07046 0.27230  170 PHE A C   
1296 O O   . PHE A 176 ? 1.29668 1.26433 1.24196 0.18224  -0.05566 0.27663  170 PHE A O   
1297 C CB  . PHE A 176 ? 1.04124 1.10212 1.00942 0.16418  -0.10282 0.25297  170 PHE A CB  
1298 C CG  . PHE A 176 ? 1.23749 1.33721 1.20959 0.15820  -0.14005 0.24999  170 PHE A CG  
1299 C CD1 . PHE A 176 ? 1.13929 1.22307 1.05928 0.16076  -0.17849 0.26964  170 PHE A CD1 
1300 C CD2 . PHE A 176 ? 1.05939 1.21009 1.08581 0.14903  -0.13685 0.22751  170 PHE A CD2 
1301 C CE1 . PHE A 176 ? 1.08337 1.20456 1.00976 0.15378  -0.21423 0.26334  170 PHE A CE1 
1302 C CE2 . PHE A 176 ? 1.08483 1.27045 1.12059 0.14171  -0.16952 0.22289  170 PHE A CE2 
1303 C CZ  . PHE A 176 ? 1.09683 1.26942 1.08519 0.14398  -0.20892 0.23909  170 PHE A CZ  
1304 N N   . ASN A 177 ? 1.12960 1.14771 1.21369 0.21192  -0.05482 0.26985  171 ASN A N   
1305 C CA  . ASN A 177 ? 1.20006 1.16832 1.27698 0.21758  -0.02362 0.27496  171 ASN A CA  
1306 C C   . ASN A 177 ? 1.35110 1.26226 1.37238 0.22867  -0.04264 0.31193  171 ASN A C   
1307 O O   . ASN A 177 ? 1.54293 1.45956 1.55577 0.24172  -0.08508 0.33590  171 ASN A O   
1308 C CB  . ASN A 177 ? 1.22917 1.21561 1.39458 0.23556  -0.00700 0.26477  171 ASN A CB  
1309 C CG  . ASN A 177 ? 1.45786 1.39250 1.62327 0.24032  0.02729  0.26596  171 ASN A CG  
1310 O OD1 . ASN A 177 ? 1.50897 1.40225 1.61439 0.22470  0.04754  0.26591  171 ASN A OD1 
1311 N ND2 . ASN A 177 ? 1.27517 1.21208 1.51319 0.26111  0.03609  0.26473  171 ASN A ND2 
1312 N N   . SER A 178 ? 1.46169 1.31677 1.44289 0.22226  -0.01117 0.31658  172 SER A N   
1313 C CA  . SER A 178 ? 1.55768 1.34789 1.47725 0.23008  -0.02111 0.35360  172 SER A CA  
1314 C C   . SER A 178 ? 1.60705 1.37129 1.58369 0.25830  -0.02049 0.37335  172 SER A C   
1315 O O   . SER A 178 ? 1.74052 1.45609 1.71673 0.25854  0.01345  0.37589  172 SER A O   
1316 C CB  . SER A 178 ? 1.59458 1.33574 1.44295 0.20598  0.01616  0.34805  172 SER A CB  
1317 O OG  . SER A 178 ? 1.34826 1.12281 1.17516 0.18105  0.02651  0.31799  172 SER A OG  
1318 N N   . ALA A 179 ? 1.66982 1.46833 1.70295 0.28248  -0.05871 0.38593  173 ALA A N   
1319 C CA  . ALA A 179 ? 1.70437 1.48547 1.80758 0.31273  -0.06105 0.40246  173 ALA A CA  
1320 C C   . ALA A 179 ? 1.92551 1.73614 2.06436 0.33878  -0.11749 0.42722  173 ALA A C   
1321 O O   . ALA A 179 ? 1.69005 1.56898 1.89374 0.34157  -0.13296 0.40656  173 ALA A O   
1322 C CB  . ALA A 179 ? 1.54928 1.36331 1.74211 0.31364  -0.02289 0.36495  173 ALA A CB  
1323 N N   . LYS A 180 ? 2.17623 1.93531 2.27321 0.35698  -0.14796 0.47131  174 LYS A N   
1324 C CA  . LYS A 180 ? 2.08035 1.85660 2.21971 0.38865  -0.20458 0.50095  174 LYS A CA  
1325 C C   . LYS A 180 ? 2.18111 2.02885 2.32626 0.38055  -0.24532 0.48730  174 LYS A C   
1326 O O   . LYS A 180 ? 2.29178 2.14809 2.36400 0.35168  -0.24145 0.47316  174 LYS A O   
1327 C CB  . LYS A 180 ? 2.00099 1.78750 2.25984 0.41787  -0.19277 0.49625  174 LYS A CB  
1328 C CG  . LYS A 180 ? 1.97422 1.67869 2.22253 0.43160  -0.16677 0.52138  174 LYS A CG  
1329 C CD  . LYS A 180 ? 1.73678 1.45318 2.09792 0.44563  -0.12787 0.49447  174 LYS A CD  
1330 C CE  . LYS A 180 ? 1.74159 1.49179 2.11145 0.41455  -0.07550 0.44238  174 LYS A CE  
1331 N NZ  . LYS A 180 ? 1.57117 1.27178 1.83917 0.38392  -0.04373 0.44060  174 LYS A NZ  
1332 N N   . ASN A 181 ? 2.18546 2.08504 2.42249 0.40548  -0.28357 0.48972  175 ASN A N   
1333 C CA  . ASN A 181 ? 2.18575 2.15393 2.43822 0.39813  -0.32420 0.47666  175 ASN A CA  
1334 C C   . ASN A 181 ? 2.23924 2.26060 2.52043 0.37001  -0.28570 0.42899  175 ASN A C   
1335 O O   . ASN A 181 ? 2.27470 2.32660 2.64431 0.37433  -0.25223 0.40315  175 ASN A O   
1336 C CB  . ASN A 181 ? 2.14300 2.15723 2.50213 0.43189  -0.37136 0.48791  175 ASN A CB  
1337 C CG  . ASN A 181 ? 2.04322 2.07220 2.52334 0.45322  -0.33811 0.47239  175 ASN A CG  
1338 O OD1 . ASN A 181 ? 2.03316 2.03423 2.54320 0.47920  -0.34912 0.48496  175 ASN A OD1 
1339 N ND2 . ASN A 181 ? 2.09118 2.15932 2.61915 0.43468  -0.28983 0.42986  175 ASN A ND2 
1340 N N   . SER A 182 ? 2.33070 2.36047 2.53489 0.34118  -0.28993 0.41759  176 SER A N   
1341 C CA  . SER A 182 ? 2.23733 2.31160 2.45824 0.31411  -0.25783 0.37696  176 SER A CA  
1342 C C   . SER A 182 ? 2.08554 2.18713 2.25476 0.29407  -0.29120 0.37123  176 SER A C   
1343 O O   . SER A 182 ? 2.17615 2.26588 2.29922 0.30112  -0.33898 0.39597  176 SER A O   
1344 C CB  . SER A 182 ? 2.16394 2.19742 2.33637 0.29424  -0.20083 0.36166  176 SER A CB  
1345 O OG  . SER A 182 ? 1.95861 1.96581 2.17954 0.31100  -0.16961 0.36364  176 SER A OG  
1346 N N   . ALA A 183 ? 1.83009 1.96691 2.00602 0.26869  -0.26639 0.33799  177 ALA A N   
1347 C CA  . ALA A 183 ? 1.71688 1.87252 1.84023 0.24584  -0.28928 0.32797  177 ALA A CA  
1348 C C   . ALA A 183 ? 1.87884 1.97567 1.88082 0.22846  -0.28170 0.33769  177 ALA A C   
1349 O O   . ALA A 183 ? 1.90243 2.00501 1.84841 0.21126  -0.30462 0.33263  177 ALA A O   
1350 C CB  . ALA A 183 ? 1.41710 1.62122 1.58481 0.22454  -0.26223 0.29187  177 ALA A CB  
1351 N N   . ALA A 184 ? 1.89999 1.94069 1.86299 0.23115  -0.24789 0.34908  178 ALA A N   
1352 C CA  . ALA A 184 ? 1.88860 1.87076 1.74083 0.21430  -0.23452 0.35829  178 ALA A CA  
1353 C C   . ALA A 184 ? 2.24902 2.17765 2.03711 0.23007  -0.26386 0.39927  178 ALA A C   
1354 O O   . ALA A 184 ? 2.32280 2.20707 2.00820 0.21448  -0.26307 0.40910  178 ALA A O   
1355 C CB  . ALA A 184 ? 1.68565 1.63714 1.53083 0.20303  -0.17602 0.34340  178 ALA A CB  
1356 N N   . ASN A 185 ? 2.53247 2.46244 2.37761 0.26059  -0.28899 0.42371  179 ASN A N   
1357 C CA  . ASN A 185 ? 2.56785 2.44214 2.35521 0.27914  -0.31870 0.46780  179 ASN A CA  
1358 C C   . ASN A 185 ? 2.48032 2.38554 2.28426 0.29863  -0.38818 0.48835  179 ASN A C   
1359 O O   . ASN A 185 ? 2.56279 2.42227 2.29037 0.30832  -0.42257 0.52532  179 ASN A O   
1360 C CB  . ASN A 185 ? 2.69217 2.52740 2.52660 0.30219  -0.29249 0.48598  179 ASN A CB  
1361 C CG  . ASN A 185 ? 2.62906 2.43139 2.44767 0.28309  -0.22645 0.46582  179 ASN A CG  
1362 O OD1 . ASN A 185 ? 2.57505 2.35469 2.31364 0.25568  -0.20321 0.45472  179 ASN A OD1 
1363 N ND2 . ASN A 185 ? 2.56587 2.36725 2.46470 0.29721  -0.19596 0.45839  179 ASN A ND2 
1364 N N   . LEU A 186 ? 2.35598 2.33666 2.25631 0.30389  -0.40993 0.46578  180 LEU A N   
1365 C CA  . LEU A 186 ? 2.42878 2.44923 2.35996 0.32109  -0.47758 0.47955  180 LEU A CA  
1366 C C   . LEU A 186 ? 2.42644 2.51379 2.38056 0.29831  -0.49233 0.44376  180 LEU A C   
1367 O O   . LEU A 186 ? 2.10907 2.22255 2.09227 0.27728  -0.44961 0.40911  180 LEU A O   
1368 C CB  . LEU A 186 ? 2.21106 2.26074 2.26612 0.35709  -0.49305 0.48884  180 LEU A CB  
1369 C CG  . LEU A 186 ? 2.16677 2.15125 2.20742 0.38477  -0.48606 0.52108  180 LEU A CG  
1370 C CD1 . LEU A 186 ? 2.22694 2.25007 2.39029 0.41782  -0.50121 0.51640  180 LEU A CD1 
1371 C CD2 . LEU A 186 ? 2.18238 2.10944 2.09456 0.38601  -0.51322 0.55024  180 LEU A CD2 
1372 N N   . ALA A 187 ? 2.68641 2.79971 2.62502 0.30209  -0.54930 0.44831  181 ALA A N   
1373 C CA  . ALA A 187 ? 2.47959 2.65610 2.44527 0.28118  -0.56991 0.41573  181 ALA A CA  
1374 C C   . ALA A 187 ? 2.52437 2.77775 2.63237 0.29634  -0.58485 0.39626  181 ALA A C   
1375 O O   . ALA A 187 ? 2.46235 2.77078 2.62174 0.27695  -0.58485 0.36631  181 ALA A O   
1376 C CB  . ALA A 187 ? 2.33521 2.50268 2.20294 0.27098  -0.60821 0.41665  181 ALA A CB  
1377 N N   . SER A 188 ? 2.64029 2.89730 2.81395 0.32927  -0.59449 0.41137  182 SER A N   
1378 C CA  . SER A 188 ? 2.49598 2.82505 2.80841 0.34280  -0.60152 0.39032  182 SER A CA  
1379 C C   . SER A 188 ? 2.39654 2.74952 2.79861 0.33746  -0.55192 0.37166  182 SER A C   
1380 O O   . SER A 188 ? 2.14982 2.56861 2.65090 0.33169  -0.54648 0.34327  182 SER A O   
1381 C CB  . SER A 188 ? 2.40486 2.72912 2.75995 0.37960  -0.62478 0.41137  182 SER A CB  
1382 O OG  . SER A 188 ? 2.33098 2.59831 2.68206 0.39821  -0.59338 0.43362  182 SER A OG  
1383 N N   . ALA A 189 ? 2.30184 2.60379 2.67104 0.33817  -0.51235 0.38700  183 ALA A N   
1384 C CA  . ALA A 189 ? 2.01012 2.32639 2.43567 0.32810  -0.44817 0.35855  183 ALA A CA  
1385 C C   . ALA A 189 ? 2.01231 2.33043 2.37977 0.29044  -0.41319 0.33023  183 ALA A C   
1386 O O   . ALA A 189 ? 2.01633 2.35442 2.42902 0.27898  -0.36566 0.30461  183 ALA A O   
1387 C CB  . ALA A 189 ? 1.83746 2.09517 2.24990 0.34398  -0.40918 0.37467  183 ALA A CB  
1388 N N   . ALA A 190 ? 2.04320 2.33970 2.31124 0.27133  -0.43555 0.33402  184 ALA A N   
1389 C CA  . ALA A 190 ? 1.96496 2.26287 2.18265 0.23711  -0.40640 0.30710  184 ALA A CA  
1390 C C   . ALA A 190 ? 2.01763 2.37856 2.28428 0.22111  -0.43120 0.28278  184 ALA A C   
1391 O O   . ALA A 190 ? 1.80547 2.18941 2.09502 0.19943  -0.39759 0.25552  184 ALA A O   
1392 C CB  . ALA A 190 ? 1.98754 2.22433 2.07180 0.22262  -0.40866 0.31969  184 ALA A CB  
1393 N N   . ALA A 191 ? 2.13237 2.52051 2.41566 0.23102  -0.49078 0.29254  185 ALA A N   
1394 C CA  . ALA A 191 ? 1.85839 2.31025 2.20133 0.21600  -0.51656 0.26767  185 ALA A CA  
1395 C C   . ALA A 191 ? 1.78365 2.29683 2.26629 0.22528  -0.50112 0.25166  185 ALA A C   
1396 O O   . ALA A 191 ? 1.59550 2.16067 2.13704 0.20745  -0.50396 0.22602  185 ALA A O   
1397 C CB  . ALA A 191 ? 1.46810 1.93262 1.78669 0.22338  -0.58873 0.28102  185 ALA A CB  
1398 N N   . ALA A 192 ? 1.81018 2.31686 2.34795 0.25147  -0.48223 0.26478  186 ALA A N   
1399 C CA  . ALA A 192 ? 1.35661 1.91659 2.02398 0.26012  -0.45836 0.24768  186 ALA A CA  
1400 C C   . ALA A 192 ? 1.29623 1.84682 1.96474 0.24263  -0.38867 0.22742  186 ALA A C   
1401 O O   . ALA A 192 ? 1.25513 1.83174 2.01121 0.25237  -0.35701 0.21691  186 ALA A O   
1402 C CB  . ALA A 192 ? 1.16751 1.72614 1.90014 0.29839  -0.47347 0.26867  186 ALA A CB  
1403 N N   . LEU A 193 ? 1.30532 1.81955 1.87881 0.21733  -0.36485 0.22093  187 LEU A N   
1404 C CA  . LEU A 193 ? 1.25785 1.75870 1.82106 0.20155  -0.30434 0.20445  187 LEU A CA  
1405 C C   . LEU A 193 ? 1.43087 1.97540 2.03279 0.17492  -0.29014 0.17815  187 LEU A C   
1406 O O   . LEU A 193 ? 1.38484 1.92531 1.93539 0.15378  -0.30619 0.17162  187 LEU A O   
1407 C CB  . LEU A 193 ? 1.02673 1.46362 1.47330 0.19080  -0.28602 0.21235  187 LEU A CB  
1408 C CG  . LEU A 193 ? 1.24709 1.65419 1.67048 0.18442  -0.22946 0.20396  187 LEU A CG  
1409 C CD1 . LEU A 193 ? 1.25416 1.60060 1.56861 0.17638  -0.22205 0.21374  187 LEU A CD1 
1410 C CD2 . LEU A 193 ? 0.97587 1.41312 1.42934 0.16183  -0.19514 0.17853  187 LEU A CD2 
1411 N N   . PRO A 194 ? 1.31016 1.89380 1.99957 0.17371  -0.25816 0.16212  188 PRO A N   
1412 C CA  . PRO A 194 ? 1.00659 1.61891 1.71794 0.14523  -0.23423 0.13985  188 PRO A CA  
1413 C C   . PRO A 194 ? 1.13554 1.70405 1.75914 0.12531  -0.19847 0.13585  188 PRO A C   
1414 O O   . PRO A 194 ? 1.36282 1.91305 1.97754 0.12739  -0.15689 0.13352  188 PRO A O   
1415 C CB  . PRO A 194 ? 0.83350 1.48874 1.64986 0.15139  -0.20187 0.12686  188 PRO A CB  
1416 C CG  . PRO A 194 ? 0.65954 1.32410 1.53155 0.18464  -0.22584 0.13991  188 PRO A CG  
1417 C CD  . PRO A 194 ? 0.78700 1.39124 1.56337 0.19786  -0.24306 0.16306  188 PRO A CD  
1418 N N   . VAL A 195 ? 1.07690 1.62897 1.63763 0.10639  -0.21555 0.13341  189 VAL A N   
1419 C CA  . VAL A 195 ? 0.94861 1.46065 1.43190 0.08854  -0.18645 0.12906  189 VAL A CA  
1420 C C   . VAL A 195 ? 0.97997 1.51662 1.49779 0.06501  -0.16082 0.11216  189 VAL A C   
1421 O O   . VAL A 195 ? 1.05948 1.59622 1.55757 0.04500  -0.17214 0.10381  189 VAL A O   
1422 C CB  . VAL A 195 ? 0.80631 1.28299 1.20318 0.08113  -0.21423 0.13405  189 VAL A CB  
1423 C CG1 . VAL A 195 ? 1.10372 1.53672 1.42744 0.06834  -0.18247 0.13041  189 VAL A CG1 
1424 C CG2 . VAL A 195 ? 1.00434 1.46108 1.37212 0.10344  -0.24622 0.15383  189 VAL A CG2 
1425 N N   . SER A 196 ? 0.85620 1.41061 1.42328 0.06652  -0.12434 0.10691  190 SER A N   
1426 C CA  . SER A 196 ? 0.74302 1.32560 1.35521 0.04557  -0.10006 0.09374  190 SER A CA  
1427 C C   . SER A 196 ? 0.82431 1.37215 1.37199 0.02706  -0.07102 0.09171  190 SER A C   
1428 O O   . SER A 196 ? 0.92264 1.43107 1.40467 0.03272  -0.06058 0.09761  190 SER A O   
1429 C CB  . SER A 196 ? 0.59530 1.21146 1.28506 0.05347  -0.07024 0.08794  190 SER A CB  
1430 O OG  . SER A 196 ? 0.85581 1.50547 1.61589 0.07378  -0.09735 0.08972  190 SER A OG  
1431 N N   . THR A 197 ? 0.71819 1.28137 1.29015 0.00469  -0.05862 0.08340  191 THR A N   
1432 C CA  . THR A 197 ? 0.68071 1.21617 1.20774 -0.01248 -0.02874 0.08324  191 THR A CA  
1433 C C   . THR A 197 ? 0.80056 1.36441 1.38449 -0.03247 -0.00605 0.07647  191 THR A C   
1434 O O   . THR A 197 ? 0.78136 1.37918 1.42588 -0.04064 -0.02321 0.06875  191 THR A O   
1435 C CB  . THR A 197 ? 0.80631 1.30645 1.26902 -0.02232 -0.04701 0.08377  191 THR A CB  
1436 O OG1 . THR A 197 ? 0.62684 1.10396 1.06046 -0.03830 -0.02044 0.08454  191 THR A OG1 
1437 C CG2 . THR A 197 ? 0.72570 1.24567 1.21697 -0.03299 -0.08057 0.07563  191 THR A CG2 
1438 N N   . ALA A 198 ? 0.84134 1.39102 1.40498 -0.04120 0.03250  0.07922  192 ALA A N   
1439 C CA  . ALA A 198 ? 0.70048 1.26962 1.30781 -0.06246 0.06033  0.07558  192 ALA A CA  
1440 C C   . ALA A 198 ? 0.84685 1.38902 1.42221 -0.08455 0.06063  0.07910  192 ALA A C   
1441 O O   . ALA A 198 ? 0.77737 1.33709 1.39991 -0.10471 0.07023  0.07477  192 ALA A O   
1442 C CB  . ALA A 198 ? 0.79047 1.35795 1.39006 -0.06210 0.10424  0.07730  192 ALA A CB  
1443 N N   . TYR A 199 ? 0.71459 1.21425 1.21691 -0.08141 0.05136  0.08584  193 TYR A N   
1444 C CA  . TYR A 199 ? 0.73929 1.20787 1.21126 -0.09951 0.05384  0.09001  193 TYR A CA  
1445 C C   . TYR A 199 ? 0.85200 1.29648 1.28556 -0.09487 0.02121  0.08606  193 TYR A C   
1446 O O   . TYR A 199 ? 1.03773 1.46595 1.42755 -0.07779 0.01101  0.08778  193 TYR A O   
1447 C CB  . TYR A 199 ? 0.57574 1.01240 0.99534 -0.10214 0.08340  0.10270  193 TYR A CB  
1448 C CG  . TYR A 199 ? 0.84193 1.29846 1.28538 -0.10728 0.11955  0.10540  193 TYR A CG  
1449 C CD1 . TYR A 199 ? 0.82872 1.30022 1.31722 -0.12896 0.14127  0.10585  193 TYR A CD1 
1450 C CD2 . TYR A 199 ? 0.73006 1.18942 1.15184 -0.09222 0.13491  0.10531  193 TYR A CD2 
1451 C CE1 . TYR A 199 ? 0.82117 1.30997 1.32916 -0.13577 0.17922  0.10663  193 TYR A CE1 
1452 C CE2 . TYR A 199 ? 0.70141 1.17815 1.14205 -0.09834 0.17129  0.10429  193 TYR A CE2 
1453 C CZ  . TYR A 199 ? 0.72803 1.21956 1.21026 -0.12026 0.19426  0.10518  193 TYR A CZ  
1454 O OH  . TYR A 199 ? 0.76708 1.27512 1.26616 -0.12855 0.23525  0.10266  193 TYR A OH  
1455 N N   . HIS A 200 ? 0.80166 1.24319 1.25280 -0.11162 0.00761  0.07885  194 HIS A N   
1456 C CA  . HIS A 200 ? 0.86900 1.28355 1.28187 -0.11226 -0.01730 0.07187  194 HIS A CA  
1457 C C   . HIS A 200 ? 0.88637 1.26591 1.28327 -0.12906 -0.00409 0.07481  194 HIS A C   
1458 O O   . HIS A 200 ? 0.80772 1.17901 1.21034 -0.13747 0.02295  0.08672  194 HIS A O   
1459 C CB  . HIS A 200 ? 0.87222 1.31345 1.31886 -0.11645 -0.05046 0.05647  194 HIS A CB  
1460 C CG  . HIS A 200 ? 0.79260 1.28394 1.30670 -0.11337 -0.05539 0.05355  194 HIS A CG  
1461 N ND1 . HIS A 200 ? 1.10244 1.62390 1.68663 -0.13220 -0.04770 0.04612  194 HIS A ND1 
1462 C CD2 . HIS A 200 ? 0.93252 1.44923 1.46121 -0.09329 -0.06702 0.05626  194 HIS A CD2 
1463 C CE1 . HIS A 200 ? 1.31518 1.88229 1.95797 -0.12340 -0.05464 0.04282  194 HIS A CE1 
1464 N NE2 . HIS A 200 ? 1.06597 1.63000 1.67631 -0.09873 -0.06736 0.04967  194 HIS A NE2 
1465 N N   . ILE A 201 ? 0.96645 1.32282 1.34166 -0.13399 -0.02277 0.06403  195 ILE A N   
1466 C CA  . ILE A 201 ? 0.83028 1.15213 1.20044 -0.14934 -0.01282 0.06477  195 ILE A CA  
1467 C C   . ILE A 201 ? 0.78172 1.11948 1.21176 -0.17235 -0.00384 0.06160  195 ILE A C   
1468 O O   . ILE A 201 ? 0.85017 1.16067 1.28440 -0.18565 0.01546  0.07094  195 ILE A O   
1469 C CB  . ILE A 201 ? 0.73004 1.02532 1.06930 -0.14973 -0.03272 0.04881  195 ILE A CB  
1470 C CG1 . ILE A 201 ? 0.77281 1.02661 1.10747 -0.16100 -0.02063 0.05060  195 ILE A CG1 
1471 C CG2 . ILE A 201 ? 0.79699 1.11737 1.16220 -0.15951 -0.05926 0.02755  195 ILE A CG2 
1472 C CD1 . ILE A 201 ? 0.77422 0.99956 1.08097 -0.16081 -0.03427 0.03225  195 ILE A CD1 
1473 N N   . LYS A 202 ? 0.90440 1.28592 1.38450 -0.17739 -0.01771 0.04922  196 LYS A N   
1474 C CA  . LYS A 202 ? 0.98580 1.38839 1.53335 -0.20092 -0.00802 0.04300  196 LYS A CA  
1475 C C   . LYS A 202 ? 0.98111 1.39089 1.54951 -0.20569 0.02908  0.06110  196 LYS A C   
1476 O O   . LYS A 202 ? 1.10435 1.50855 1.70908 -0.22804 0.05027  0.06365  196 LYS A O   
1477 C CB  . LYS A 202 ? 0.97656 1.42959 1.57787 -0.20346 -0.03664 0.02316  196 LYS A CB  
1478 C CG  . LYS A 202 ? 1.07326 1.51999 1.65757 -0.20719 -0.07283 0.00175  196 LYS A CG  
1479 C CD  . LYS A 202 ? 1.37252 1.87186 2.00421 -0.20633 -0.10654 -0.01467 196 LYS A CD  
1480 C CE  . LYS A 202 ? 1.47915 1.97071 2.07748 -0.20896 -0.14483 -0.03543 196 LYS A CE  
1481 N NZ  . LYS A 202 ? 1.42387 1.96730 2.06572 -0.20753 -0.18348 -0.04974 196 LYS A NZ  
1482 N N   . ASN A 203 ? 0.95350 1.37362 1.49836 -0.18672 0.03959  0.07269  197 ASN A N   
1483 C CA  . ASN A 203 ? 0.78961 1.21568 1.34403 -0.19099 0.07716  0.08764  197 ASN A CA  
1484 C C   . ASN A 203 ? 0.87002 1.27187 1.35575 -0.17128 0.08751  0.10299  197 ASN A C   
1485 O O   . ASN A 203 ? 0.94710 1.37224 1.43132 -0.15473 0.08945  0.10187  197 ASN A O   
1486 C CB  . ASN A 203 ? 0.84150 1.32416 1.46816 -0.19223 0.08287  0.07735  197 ASN A CB  
1487 C CG  . ASN A 203 ? 0.92609 1.43768 1.55508 -0.16728 0.05476  0.06885  197 ASN A CG  
1488 O OD1 . ASN A 203 ? 1.04627 1.54323 1.63797 -0.15566 0.02338  0.06448  197 ASN A OD1 
1489 N ND2 . ASN A 203 ? 0.97384 1.52406 1.64648 -0.15910 0.06812  0.06680  197 ASN A ND2 
1490 N N   . PRO A 204 ? 0.87568 1.23062 1.30728 -0.17221 0.09326  0.11653  198 PRO A N   
1491 C CA  . PRO A 204 ? 0.88089 1.21509 1.25076 -0.15568 0.10260  0.13006  198 PRO A CA  
1492 C C   . PRO A 204 ? 0.75207 1.09557 1.12043 -0.16159 0.13782  0.14203  198 PRO A C   
1493 O O   . PRO A 204 ? 0.86143 1.21476 1.26779 -0.18148 0.16050  0.14502  198 PRO A O   
1494 C CB  . PRO A 204 ? 0.92210 1.20631 1.24857 -0.15760 0.09717  0.14095  198 PRO A CB  
1495 C CG  . PRO A 204 ? 0.84015 1.11919 1.20216 -0.17068 0.08007  0.12769  198 PRO A CG  
1496 C CD  . PRO A 204 ? 0.80753 1.12616 1.23518 -0.18671 0.08782  0.11808  198 PRO A CD  
1497 N N   . ILE A 205 ? 0.83851 1.17845 1.16189 -0.14557 0.14441  0.14690  199 ILE A N   
1498 C CA  . ILE A 205 ? 0.85601 1.19967 1.16167 -0.15038 0.17862  0.15635  199 ILE A CA  
1499 C C   . ILE A 205 ? 0.96849 1.26624 1.20211 -0.15066 0.18334  0.17656  199 ILE A C   
1500 O O   . ILE A 205 ? 0.88676 1.16876 1.07565 -0.13359 0.16630  0.17691  199 ILE A O   
1501 C CB  . ILE A 205 ? 0.74546 1.11983 1.05603 -0.13342 0.18390  0.14424  199 ILE A CB  
1502 C CG1 . ILE A 205 ? 0.82702 1.20000 1.10735 -0.13923 0.22113  0.15109  199 ILE A CG1 
1503 C CG2 . ILE A 205 ? 0.70511 1.06820 0.97975 -0.11097 0.15627  0.13894  199 ILE A CG2 
1504 C CD1 . ILE A 205 ? 0.76061 1.15227 1.08551 -0.16160 0.25545  0.15214  199 ILE A CD1 
1505 N N   . GLY A 206 ? 1.04380 1.31910 1.26813 -0.17026 0.20531  0.19408  200 GLY A N   
1506 C CA  . GLY A 206 ? 0.85978 1.08854 1.01659 -0.17057 0.20621  0.21748  200 GLY A CA  
1507 C C   . GLY A 206 ? 1.06569 1.26467 1.20766 -0.15883 0.17221  0.21952  200 GLY A C   
1508 O O   . GLY A 206 ? 1.12844 1.29695 1.21637 -0.14890 0.16218  0.23330  200 GLY A O   
1509 N N   . GLY A 207 ? 1.01015 1.21902 1.20124 -0.16003 0.15393  0.20401  201 GLY A N   
1510 C CA  . GLY A 207 ? 0.75425 0.93745 0.93775 -0.15034 0.12551  0.20034  201 GLY A CA  
1511 C C   . GLY A 207 ? 0.88704 1.08463 1.05833 -0.12897 0.10327  0.18302  201 GLY A C   
1512 O O   . GLY A 207 ? 0.95425 1.12942 1.11365 -0.12002 0.08345  0.17918  201 GLY A O   
1513 N N   . VAL A 208 ? 0.97653 1.20895 1.15338 -0.12093 0.10809  0.17204  202 VAL A N   
1514 C CA  . VAL A 208 ? 0.83354 1.07658 0.99658 -0.10158 0.09112  0.15785  202 VAL A CA  
1515 C C   . VAL A 208 ? 0.88902 1.16721 1.09582 -0.10018 0.08363  0.14085  202 VAL A C   
1516 O O   . VAL A 208 ? 0.95283 1.25831 1.19760 -0.10930 0.09738  0.13947  202 VAL A O   
1517 C CB  . VAL A 208 ? 0.89569 1.14194 1.01862 -0.09037 0.10223  0.16186  202 VAL A CB  
1518 C CG1 . VAL A 208 ? 0.74377 0.99948 0.85830 -0.07232 0.08791  0.14661  202 VAL A CG1 
1519 C CG2 . VAL A 208 ? 0.79367 1.00604 0.86951 -0.09085 0.10349  0.17985  202 VAL A CG2 
1520 N N   . PHE A 209 ? 0.89013 1.16742 1.09220 -0.08893 0.06175  0.12822  203 PHE A N   
1521 C CA  . PHE A 209 ? 0.87035 1.17709 1.10339 -0.08448 0.04916  0.11504  203 PHE A CA  
1522 C C   . PHE A 209 ? 0.78128 1.07802 0.98411 -0.06858 0.03243  0.10663  203 PHE A C   
1523 O O   . PHE A 209 ? 0.87703 1.14562 1.04752 -0.06512 0.02798  0.10616  203 PHE A O   
1524 C CB  . PHE A 209 ? 0.88183 1.19799 1.15613 -0.09975 0.03721  0.10732  203 PHE A CB  
1525 C CG  . PHE A 209 ? 0.81429 1.10018 1.07192 -0.10476 0.02187  0.10099  203 PHE A CG  
1526 C CD1 . PHE A 209 ? 0.79787 1.05359 1.04958 -0.11542 0.03093  0.10964  203 PHE A CD1 
1527 C CD2 . PHE A 209 ? 0.90995 1.19514 1.15706 -0.09901 -0.00037 0.08642  203 PHE A CD2 
1528 C CE1 . PHE A 209 ? 0.72871 0.95591 0.97244 -0.11911 0.01880  0.10124  203 PHE A CE1 
1529 C CE2 . PHE A 209 ? 0.88940 1.14678 1.12209 -0.10479 -0.01043 0.07665  203 PHE A CE2 
1530 C CZ  . PHE A 209 ? 0.82899 1.05831 1.06425 -0.11434 -0.00049 0.08271  203 PHE A CZ  
1531 N N   . PHE A 210 ? 0.86701 1.18639 1.08381 -0.05892 0.02405  0.10043  204 PHE A N   
1532 C CA  . PHE A 210 ? 0.73170 1.04029 0.91932 -0.04515 0.01085  0.09444  204 PHE A CA  
1533 C C   . PHE A 210 ? 0.75880 1.06888 0.95145 -0.04903 -0.01341 0.08538  204 PHE A C   
1534 O O   . PHE A 210 ? 0.93739 1.27176 1.16826 -0.05646 -0.02371 0.08260  204 PHE A O   
1535 C CB  . PHE A 210 ? 0.69891 1.02414 0.89167 -0.03012 0.01723  0.09601  204 PHE A CB  
1536 C CG  . PHE A 210 ? 0.76913 1.09135 0.94816 -0.02610 0.04064  0.10029  204 PHE A CG  
1537 C CD1 . PHE A 210 ? 0.73175 1.02845 0.87004 -0.02212 0.04467  0.09970  204 PHE A CD1 
1538 C CD2 . PHE A 210 ? 0.84622 1.19281 1.05445 -0.02680 0.05867  0.10247  204 PHE A CD2 
1539 C CE1 . PHE A 210 ? 0.73873 1.03410 0.86073 -0.01927 0.06248  0.10171  204 PHE A CE1 
1540 C CE2 . PHE A 210 ? 0.82360 1.16641 1.01172 -0.02480 0.08071  0.10385  204 PHE A CE2 
1541 C CZ  . PHE A 210 ? 0.78986 1.10694 0.93227 -0.02113 0.08069  0.10370  204 PHE A CZ  
1542 N N   . THR A 211 ? 0.79548 1.08045 0.94946 -0.04510 -0.02197 0.07905  205 THR A N   
1543 C CA  . THR A 211 ? 0.77871 1.06124 0.92043 -0.04694 -0.04401 0.06992  205 THR A CA  
1544 C C   . THR A 211 ? 0.78705 1.06065 0.89582 -0.03181 -0.04717 0.07239  205 THR A C   
1545 O O   . THR A 211 ? 0.78579 1.04957 0.88016 -0.02198 -0.03095 0.07694  205 THR A O   
1546 C CB  . THR A 211 ? 0.80671 1.06298 0.92847 -0.05884 -0.04777 0.05777  205 THR A CB  
1547 O OG1 . THR A 211 ? 0.85180 1.08284 0.95125 -0.05444 -0.03137 0.05861  205 THR A OG1 
1548 C CG2 . THR A 211 ? 0.67090 0.93594 0.83050 -0.07551 -0.04994 0.05435  205 THR A CG2 
1549 N N   . ASP A 212 ? 0.71842 0.99382 0.81355 -0.03086 -0.06886 0.06946  206 ASP A N   
1550 C CA  . ASP A 212 ? 0.72666 0.99555 0.79683 -0.01592 -0.07403 0.07723  206 ASP A CA  
1551 C C   . ASP A 212 ? 0.75901 1.00316 0.77684 -0.01970 -0.08880 0.07104  206 ASP A C   
1552 O O   . ASP A 212 ? 0.87029 1.10811 0.87664 -0.03400 -0.09767 0.05797  206 ASP A O   
1553 C CB  . ASP A 212 ? 0.76829 1.06993 0.88072 -0.00601 -0.08766 0.08682  206 ASP A CB  
1554 C CG  . ASP A 212 ? 0.79190 1.11735 0.95347 -0.00403 -0.06750 0.09039  206 ASP A CG  
1555 O OD1 . ASP A 212 ? 0.98925 1.30346 1.14029 0.00370  -0.04525 0.09371  206 ASP A OD1 
1556 O OD2 . ASP A 212 ? 0.90513 1.25991 1.11445 -0.01208 -0.07223 0.08813  206 ASP A OD2 
1557 N N   . SER A 213 ? 0.79105 1.01864 0.77533 -0.00759 -0.08934 0.08019  207 SER A N   
1558 C CA  . SER A 213 ? 0.89096 1.08847 0.81347 -0.01077 -0.09737 0.07744  207 SER A CA  
1559 C C   . SER A 213 ? 0.85221 1.03704 0.75292 0.00555  -0.09978 0.09523  207 SER A C   
1560 O O   . SER A 213 ? 0.90511 1.09581 0.83439 0.01782  -0.08467 0.10386  207 SER A O   
1561 C CB  . SER A 213 ? 0.90371 1.07118 0.79460 -0.02012 -0.07288 0.06308  207 SER A CB  
1562 O OG  . SER A 213 ? 0.95252 1.08982 0.78179 -0.02629 -0.07492 0.05742  207 SER A OG  
1563 N N   . PRO A 214 ? 0.86577 1.03035 0.71369 0.00576  -0.11813 0.10137  208 PRO A N   
1564 C CA  . PRO A 214 ? 0.95804 1.11353 0.76135 -0.00908 -0.13800 0.09011  208 PRO A CA  
1565 C C   . PRO A 214 ? 0.96442 1.15624 0.80099 -0.01019 -0.17570 0.09050  208 PRO A C   
1566 O O   . PRO A 214 ? 1.06341 1.28956 0.96511 -0.00064 -0.18242 0.09782  208 PRO A O   
1567 C CB  . PRO A 214 ? 1.01507 1.13028 0.74294 -0.00540 -0.13810 0.10201  208 PRO A CB  
1568 C CG  . PRO A 214 ? 0.88755 1.00600 0.63927 0.01613  -0.14105 0.12660  208 PRO A CG  
1569 C CD  . PRO A 214 ? 0.86487 1.00787 0.68667 0.02147  -0.11811 0.12170  208 PRO A CD  
1570 N N   . GLU A 215 ? 1.00052 1.18694 0.79512 -0.02291 -0.20010 0.08024  209 GLU A N   
1571 C CA  . GLU A 215 ? 1.00456 1.22944 0.83747 -0.02714 -0.23724 0.07517  209 GLU A CA  
1572 C C   . GLU A 215 ? 1.15348 1.39756 1.00295 -0.00750 -0.27012 0.09830  209 GLU A C   
1573 O O   . GLU A 215 ? 1.29014 1.57834 1.20971 -0.00374 -0.29182 0.09799  209 GLU A O   
1574 C CB  . GLU A 215 ? 1.03785 1.25131 0.81868 -0.04769 -0.25544 0.05397  209 GLU A CB  
1575 C CG  . GLU A 215 ? 1.18210 1.43786 1.01277 -0.05745 -0.29006 0.04066  209 GLU A CG  
1576 C CD  . GLU A 215 ? 1.38649 1.63012 1.16861 -0.08072 -0.30430 0.01365  209 GLU A CD  
1577 O OE1 . GLU A 215 ? 1.39588 1.59802 1.09538 -0.08727 -0.29231 0.00826  209 GLU A OE1 
1578 O OE2 . GLU A 215 ? 1.68338 1.95868 1.51164 -0.09391 -0.32517 -0.00434 209 GLU A OE2 
1579 N N   . HIS A 216 ? 1.16952 1.38077 0.96058 0.00537  -0.27341 0.11873  210 HIS A N   
1580 C CA  . HIS A 216 ? 1.21707 1.44146 1.02277 0.02651  -0.30777 0.14340  210 HIS A CA  
1581 C C   . HIS A 216 ? 1.07420 1.31967 0.95820 0.04682  -0.29175 0.15686  210 HIS A C   
1582 O O   . HIS A 216 ? 1.19330 1.44669 1.09855 0.06779  -0.31528 0.17817  210 HIS A O   
1583 C CB  . HIS A 216 ? 1.34699 1.52218 1.05713 0.03280  -0.31725 0.16381  210 HIS A CB  
1584 C CG  . HIS A 216 ? 1.62292 1.75482 1.30224 0.03875  -0.27383 0.17472  210 HIS A CG  
1585 N ND1 . HIS A 216 ? 1.62516 1.74677 1.32636 0.06161  -0.26868 0.20011  210 HIS A ND1 
1586 C CD2 . HIS A 216 ? 1.62918 1.72629 1.26301 0.02437  -0.23352 0.16162  210 HIS A CD2 
1587 C CE1 . HIS A 216 ? 1.28932 1.37154 0.95809 0.05948  -0.22701 0.20158  210 HIS A CE1 
1588 N NE2 . HIS A 216 ? 1.39239 1.46101 1.02173 0.03732  -0.20564 0.17852  210 HIS A NE2 
1589 N N   . LEU A 217 ? 1.03919 1.29308 0.96571 0.04134  -0.25327 0.14451  211 LEU A N   
1590 C CA  . LEU A 217 ? 0.94768 1.22628 0.94997 0.05636  -0.23568 0.15103  211 LEU A CA  
1591 C C   . LEU A 217 ? 1.05928 1.38117 1.13464 0.04496  -0.22716 0.13340  211 LEU A C   
1592 O O   . LEU A 217 ? 1.00268 1.34144 1.13189 0.05144  -0.20219 0.13363  211 LEU A O   
1593 C CB  . LEU A 217 ? 1.04676 1.29119 1.02704 0.06162  -0.19403 0.15537  211 LEU A CB  
1594 C CG  . LEU A 217 ? 1.04342 1.23760 0.95201 0.06950  -0.18939 0.17169  211 LEU A CG  
1595 C CD1 . LEU A 217 ? 0.98971 1.16366 0.90671 0.07577  -0.14848 0.17266  211 LEU A CD1 
1596 C CD2 . LEU A 217 ? 1.04016 1.23273 0.94549 0.08856  -0.22554 0.19575  211 LEU A CD2 
1597 N N   . LEU A 218 ? 1.03234 1.37001 1.10820 0.02660  -0.24545 0.11741  212 LEU A N   
1598 C CA  . LEU A 218 ? 1.09882 1.47082 1.23963 0.01257  -0.23435 0.10148  212 LEU A CA  
1599 C C   . LEU A 218 ? 1.04442 1.46780 1.27336 0.02109  -0.25148 0.10392  212 LEU A C   
1600 O O   . LEU A 218 ? 1.01620 1.46590 1.30631 0.01384  -0.22964 0.09599  212 LEU A O   
1601 C CB  . LEU A 218 ? 1.07391 1.44332 1.19140 -0.01110 -0.24718 0.08150  212 LEU A CB  
1602 C CG  . LEU A 218 ? 0.89477 1.22477 0.95809 -0.02571 -0.21959 0.06965  212 LEU A CG  
1603 C CD1 . LEU A 218 ? 1.10826 1.43867 1.15736 -0.04779 -0.23688 0.04786  212 LEU A CD1 
1604 C CD2 . LEU A 218 ? 0.87088 1.20262 0.97150 -0.02756 -0.18179 0.06891  212 LEU A CD2 
1605 N N   . GLY A 219 ? 1.10398 1.54172 1.34182 0.03624  -0.28942 0.11503  213 GLY A N   
1606 C CA  . GLY A 219 ? 1.14367 1.63673 1.47289 0.04064  -0.31269 0.11138  213 GLY A CA  
1607 C C   . GLY A 219 ? 1.13648 1.65389 1.48428 0.01580  -0.33066 0.08950  213 GLY A C   
1608 O O   . GLY A 219 ? 1.01299 1.50517 1.29366 0.00140  -0.34468 0.08077  213 GLY A O   
1609 N N   . TYR A 220 ? 1.15654 1.72190 1.59760 0.00875  -0.32626 0.07824  214 TYR A N   
1610 C CA  . TYR A 220 ? 0.81301 1.40484 1.28624 -0.01605 -0.34221 0.05597  214 TYR A CA  
1611 C C   . TYR A 220 ? 0.80076 1.39640 1.31193 -0.03707 -0.29881 0.04352  214 TYR A C   
1612 O O   . TYR A 220 ? 0.81159 1.42477 1.35352 -0.05998 -0.30615 0.02456  214 TYR A O   
1613 C CB  . TYR A 220 ? 0.90766 1.55801 1.46538 -0.00982 -0.38464 0.05101  214 TYR A CB  
1614 C CG  . TYR A 220 ? 1.23636 1.88294 1.75483 0.01084  -0.43589 0.06545  214 TYR A CG  
1615 C CD1 . TYR A 220 ? 1.27652 1.89398 1.70544 0.00149  -0.46722 0.06154  214 TYR A CD1 
1616 C CD2 . TYR A 220 ? 1.24150 1.91120 1.81075 0.03966  -0.45242 0.08328  214 TYR A CD2 
1617 C CE1 . TYR A 220 ? 1.45590 2.06544 1.83826 0.01946  -0.51467 0.07778  214 TYR A CE1 
1618 C CE2 . TYR A 220 ? 1.38933 2.05100 1.91984 0.05993  -0.50170 0.10079  214 TYR A CE2 
1619 C CZ  . TYR A 220 ? 1.69474 2.32543 2.12758 0.04929  -0.53326 0.09935  214 TYR A CZ  
1620 O OH  . TYR A 220 ? 1.88001 2.49838 2.26385 0.06857  -0.58278 0.11970  214 TYR A OH  
1621 N N   . SER A 221 ? 0.84099 1.41842 1.34800 -0.03096 -0.25472 0.05362  215 SER A N   
1622 C CA  . SER A 221 ? 0.78942 1.36652 1.32464 -0.04976 -0.21433 0.04633  215 SER A CA  
1623 C C   . SER A 221 ? 0.91305 1.43820 1.37443 -0.05414 -0.18291 0.05129  215 SER A C   
1624 O O   . SER A 221 ? 0.99239 1.50672 1.45820 -0.07316 -0.16035 0.04458  215 SER A O   
1625 C CB  . SER A 221 ? 0.70238 1.31353 1.31385 -0.04215 -0.18694 0.05099  215 SER A CB  
1626 O OG  . SER A 221 ? 0.99049 1.58504 1.57613 -0.01874 -0.17249 0.06609  215 SER A OG  
1627 N N   . ARG A 222 ? 0.82912 1.32166 1.22702 -0.03717 -0.18111 0.06303  216 ARG A N   
1628 C CA  . ARG A 222 ? 0.89008 1.33870 1.22826 -0.03982 -0.15183 0.06621  216 ARG A CA  
1629 C C   . ARG A 222 ? 0.82587 1.24607 1.11738 -0.05689 -0.16043 0.05360  216 ARG A C   
1630 O O   . ARG A 222 ? 0.74722 1.17236 1.02695 -0.06290 -0.19189 0.04392  216 ARG A O   
1631 C CB  . ARG A 222 ? 0.77561 1.19900 1.06597 -0.01868 -0.14677 0.07943  216 ARG A CB  
1632 C CG  . ARG A 222 ? 0.76682 1.20943 1.09925 -0.00225 -0.12869 0.08931  216 ARG A CG  
1633 C CD  . ARG A 222 ? 0.95921 1.37138 1.24473 0.01620  -0.12032 0.10035  216 ARG A CD  
1634 N NE  . ARG A 222 ? 0.88121 1.30878 1.20757 0.03019  -0.09869 0.10575  216 ARG A NE  
1635 C CZ  . ARG A 222 ? 0.83290 1.23935 1.13646 0.04677  -0.08779 0.11373  216 ARG A CZ  
1636 N NH1 . ARG A 222 ? 0.84793 1.21652 1.08801 0.05133  -0.09496 0.11937  216 ARG A NH1 
1637 N NH2 . ARG A 222 ? 0.74646 1.16900 1.09323 0.05763  -0.06645 0.11436  216 ARG A NH2 
1638 N N   . ASP A 223 ? 0.80070 1.19077 1.06602 -0.06438 -0.13275 0.05267  217 ASP A N   
1639 C CA  . ASP A 223 ? 0.78914 1.14844 1.01561 -0.07896 -0.13460 0.03941  217 ASP A CA  
1640 C C   . ASP A 223 ? 0.83104 1.15461 0.98659 -0.06901 -0.13390 0.04072  217 ASP A C   
1641 O O   . ASP A 223 ? 0.95412 1.26409 1.09101 -0.05565 -0.11482 0.05201  217 ASP A O   
1642 C CB  . ASP A 223 ? 0.96124 1.30498 1.20236 -0.09090 -0.10674 0.03892  217 ASP A CB  
1643 C CG  . ASP A 223 ? 1.00213 1.37375 1.30870 -0.10636 -0.10352 0.03604  217 ASP A CG  
1644 O OD1 . ASP A 223 ? 1.03911 1.44112 1.38132 -0.11294 -0.12724 0.02636  217 ASP A OD1 
1645 O OD2 . ASP A 223 ? 0.82025 1.18264 1.14208 -0.11271 -0.07746 0.04361  217 ASP A OD2 
1646 N N   . LEU A 224 ? 0.85839 1.16663 0.97450 -0.07733 -0.15280 0.02717  218 LEU A N   
1647 C CA  . LEU A 224 ? 0.79294 1.06362 0.84059 -0.07276 -0.14607 0.02498  218 LEU A CA  
1648 C C   . LEU A 224 ? 0.82056 1.06343 0.86137 -0.07896 -0.11762 0.01763  218 LEU A C   
1649 O O   . LEU A 224 ? 0.85829 1.09650 0.91804 -0.09425 -0.11557 0.00380  218 LEU A O   
1650 C CB  . LEU A 224 ? 0.75641 1.01779 0.75920 -0.08244 -0.17207 0.01053  218 LEU A CB  
1651 C CG  . LEU A 224 ? 0.86028 1.08274 0.78612 -0.07932 -0.16421 0.00844  218 LEU A CG  
1652 C CD1 . LEU A 224 ? 0.90230 1.11938 0.81135 -0.05882 -0.15734 0.03142  218 LEU A CD1 
1653 C CD2 . LEU A 224 ? 0.85415 1.06938 0.72948 -0.09038 -0.19187 -0.00514 218 LEU A CD2 
1654 N N   . ASP A 225 ? 0.94936 1.17383 0.96775 -0.06673 -0.09682 0.02650  219 ASP A N   
1655 C CA  . ASP A 225 ? 0.75436 0.95577 0.77179 -0.06940 -0.07337 0.02084  219 ASP A CA  
1656 C C   . ASP A 225 ? 0.86934 1.04515 0.86169 -0.08278 -0.07326 -0.00115 219 ASP A C   
1657 O O   . ASP A 225 ? 0.93231 1.09471 0.94425 -0.08954 -0.06157 -0.00952 219 ASP A O   
1658 C CB  . ASP A 225 ? 0.74341 0.93150 0.73880 -0.05483 -0.05533 0.02977  219 ASP A CB  
1659 C CG  . ASP A 225 ? 0.95585 1.13202 0.96637 -0.05371 -0.03557 0.02904  219 ASP A CG  
1660 O OD1 . ASP A 225 ? 0.84265 1.02389 0.88511 -0.06095 -0.03485 0.03002  219 ASP A OD1 
1661 O OD2 . ASP A 225 ? 1.03447 1.19552 1.02584 -0.04578 -0.02164 0.02800  219 ASP A OD2 
1662 N N   . THR A 226 ? 0.86057 1.02733 0.80808 -0.08668 -0.08592 -0.01072 220 THR A N   
1663 C CA  . THR A 226 ? 0.75729 0.89906 0.67515 -0.10104 -0.08325 -0.03565 220 THR A CA  
1664 C C   . THR A 226 ? 0.85490 1.00310 0.81206 -0.11710 -0.09088 -0.05081 220 THR A C   
1665 O O   . THR A 226 ? 0.97453 1.10053 0.93934 -0.12554 -0.07655 -0.06811 220 THR A O   
1666 C CB  . THR A 226 ? 0.92132 1.05493 0.77757 -0.10444 -0.09922 -0.04113 220 THR A CB  
1667 O OG1 . THR A 226 ? 1.06929 1.19248 0.89128 -0.08996 -0.08978 -0.02435 220 THR A OG1 
1668 C CG2 . THR A 226 ? 0.81929 0.92449 0.63719 -0.12066 -0.09102 -0.07020 220 THR A CG2 
1669 N N   . ASP A 227 ? 0.92508 1.10348 0.91363 -0.12159 -0.11260 -0.04548 221 ASP A N   
1670 C CA  . ASP A 227 ? 0.90399 1.08882 0.93307 -0.13962 -0.11972 -0.06142 221 ASP A CA  
1671 C C   . ASP A 227 ? 1.00745 1.18658 1.08673 -0.13969 -0.09880 -0.05256 221 ASP A C   
1672 O O   . ASP A 227 ? 0.94406 1.10542 1.04475 -0.15291 -0.09181 -0.06784 221 ASP A O   
1673 C CB  . ASP A 227 ? 0.91498 1.13779 0.97077 -0.14498 -0.14895 -0.05949 221 ASP A CB  
1674 C CG  . ASP A 227 ? 1.08302 1.30894 1.08545 -0.14667 -0.17645 -0.06885 221 ASP A CG  
1675 O OD1 . ASP A 227 ? 1.13769 1.33356 1.08500 -0.15382 -0.17191 -0.08696 221 ASP A OD1 
1676 O OD2 . ASP A 227 ? 1.14122 1.39900 1.15634 -0.14071 -0.20257 -0.05807 221 ASP A OD2 
1677 N N   . VAL A 228 ? 0.88405 1.07526 0.98004 -0.12533 -0.08852 -0.02785 222 VAL A N   
1678 C CA  . VAL A 228 ? 0.87376 1.05769 1.00695 -0.12528 -0.07028 -0.01577 222 VAL A CA  
1679 C C   . VAL A 228 ? 0.83809 0.98576 0.95638 -0.12187 -0.05370 -0.02260 222 VAL A C   
1680 O O   . VAL A 228 ? 0.95093 1.08003 1.09700 -0.12933 -0.04551 -0.02521 222 VAL A O   
1681 C CB  . VAL A 228 ? 0.81451 1.01977 0.95995 -0.11150 -0.06277 0.00953  222 VAL A CB  
1682 C CG1 . VAL A 228 ? 0.62925 0.81947 0.79229 -0.10939 -0.04325 0.02381  222 VAL A CG1 
1683 C CG2 . VAL A 228 ? 0.73124 0.97380 0.91278 -0.11696 -0.07556 0.01405  222 VAL A CG2 
1684 N N   . VAL A 229 ? 0.85218 0.98855 0.93090 -0.11054 -0.04814 -0.02572 223 VAL A N   
1685 C CA  . VAL A 229 ? 0.83988 0.94678 0.91288 -0.10592 -0.03215 -0.03447 223 VAL A CA  
1686 C C   . VAL A 229 ? 0.95837 1.04253 1.03671 -0.12072 -0.03128 -0.06159 223 VAL A C   
1687 O O   . VAL A 229 ? 1.03484 1.09708 1.14129 -0.12142 -0.02116 -0.06610 223 VAL A O   
1688 C CB  . VAL A 229 ? 0.82220 0.92414 0.85549 -0.09380 -0.02418 -0.03570 223 VAL A CB  
1689 C CG1 . VAL A 229 ? 0.76345 0.83758 0.79475 -0.09267 -0.00819 -0.05401 223 VAL A CG1 
1690 C CG2 . VAL A 229 ? 0.76205 0.88002 0.79960 -0.07870 -0.02017 -0.01170 223 VAL A CG2 
1691 N N   . ILE A 230 ? 0.97786 1.06564 1.02887 -0.13251 -0.04288 -0.08050 224 ILE A N   
1692 C CA  . ILE A 230 ? 0.85729 0.92273 0.90698 -0.14839 -0.04047 -0.11174 224 ILE A CA  
1693 C C   . ILE A 230 ? 0.91856 0.98197 1.02074 -0.16133 -0.04419 -0.11456 224 ILE A C   
1694 O O   . ILE A 230 ? 1.03173 1.06767 1.15680 -0.16819 -0.03305 -0.13213 224 ILE A O   
1695 C CB  . ILE A 230 ? 0.89019 0.96039 0.88759 -0.15902 -0.05450 -0.13086 224 ILE A CB  
1696 C CG1 . ILE A 230 ? 0.88797 0.94656 0.83044 -0.14905 -0.04277 -0.13108 224 ILE A CG1 
1697 C CG2 . ILE A 230 ? 0.87367 0.92544 0.87164 -0.17949 -0.05488 -0.16622 224 ILE A CG2 
1698 C CD1 . ILE A 230 ? 0.89180 0.94719 0.76988 -0.15966 -0.05477 -0.14717 224 ILE A CD1 
1699 N N   . ASP A 231 ? 0.92853 1.01960 1.05519 -0.16518 -0.05768 -0.09797 225 ASP A N   
1700 C CA  . ASP A 231 ? 0.95413 1.04239 1.13352 -0.17953 -0.05756 -0.09875 225 ASP A CA  
1701 C C   . ASP A 231 ? 0.84809 0.90981 1.05776 -0.17148 -0.03884 -0.08200 225 ASP A C   
1702 O O   . ASP A 231 ? 0.98767 1.02353 1.23069 -0.18216 -0.03194 -0.09209 225 ASP A O   
1703 C CB  . ASP A 231 ? 1.00218 1.12845 1.20706 -0.18429 -0.07117 -0.08286 225 ASP A CB  
1704 C CG  . ASP A 231 ? 1.35046 1.50231 1.54115 -0.19596 -0.09616 -0.10272 225 ASP A CG  
1705 O OD1 . ASP A 231 ? 1.24582 1.38159 1.41479 -0.20825 -0.10200 -0.13256 225 ASP A OD1 
1706 O OD2 . ASP A 231 ? 1.57732 1.76567 1.77921 -0.19269 -0.11072 -0.08946 225 ASP A OD2 
1707 N N   . LYS A 232 ? 0.88331 0.94939 1.08150 -0.15255 -0.03187 -0.05638 226 LYS A N   
1708 C CA  . LYS A 232 ? 0.87342 0.91494 1.09357 -0.14304 -0.01915 -0.03831 226 LYS A CA  
1709 C C   . LYS A 232 ? 1.01897 1.02646 1.24269 -0.13923 -0.01058 -0.05875 226 LYS A C   
1710 O O   . LYS A 232 ? 1.04120 1.01986 1.29928 -0.14026 -0.00423 -0.05569 226 LYS A O   
1711 C CB  . LYS A 232 ? 0.76364 0.82015 0.96527 -0.12448 -0.01623 -0.01109 226 LYS A CB  
1712 C CG  . LYS A 232 ? 0.82427 0.91070 1.03251 -0.12747 -0.01897 0.01022  226 LYS A CG  
1713 C CD  . LYS A 232 ? 0.80252 0.87836 1.04915 -0.14140 -0.01343 0.02200  226 LYS A CD  
1714 C CE  . LYS A 232 ? 0.80417 0.91215 1.06323 -0.14698 -0.01160 0.03921  226 LYS A CE  
1715 N NZ  . LYS A 232 ? 0.96666 1.06260 1.26378 -0.16403 -0.00187 0.04983  226 LYS A NZ  
1716 N N   . LEU A 233 ? 0.90656 0.91513 1.09710 -0.13480 -0.00863 -0.07950 227 LEU A N   
1717 C CA  . LEU A 233 ? 0.90754 0.88656 1.10605 -0.13265 0.00343  -0.10430 227 LEU A CA  
1718 C C   . LEU A 233 ? 0.95725 0.91448 1.18055 -0.15155 0.00519  -0.13173 227 LEU A C   
1719 O O   . LEU A 233 ? 1.21958 1.14598 1.47619 -0.14944 0.01608  -0.14404 227 LEU A O   
1720 C CB  . LEU A 233 ? 0.84993 0.83474 1.00369 -0.12834 0.00954  -0.12266 227 LEU A CB  
1721 C CG  . LEU A 233 ? 0.88155 0.88038 1.01695 -0.10957 0.01299  -0.10303 227 LEU A CG  
1722 C CD1 . LEU A 233 ? 0.89429 0.89551 0.98240 -0.11050 0.02111  -0.12170 227 LEU A CD1 
1723 C CD2 . LEU A 233 ? 0.84366 0.82674 1.01660 -0.09428 0.02084  -0.09539 227 LEU A CD2 
1724 N N   . LYS A 234 ? 1.02774 1.00085 1.23975 -0.16982 -0.00639 -0.14312 228 LYS A N   
1725 C CA  . LYS A 234 ? 1.08997 1.04451 1.32635 -0.19064 -0.00595 -0.17257 228 LYS A CA  
1726 C C   . LYS A 234 ? 0.99000 0.92907 1.28309 -0.19677 -0.00403 -0.15603 228 LYS A C   
1727 O O   . LYS A 234 ? 1.10611 1.01669 1.43245 -0.20992 0.00270  -0.17864 228 LYS A O   
1728 C CB  . LYS A 234 ? 0.85418 0.83399 1.05942 -0.20889 -0.02318 -0.19212 228 LYS A CB  
1729 C CG  . LYS A 234 ? 1.06253 1.04473 1.20522 -0.20885 -0.02332 -0.21536 228 LYS A CG  
1730 C CD  . LYS A 234 ? 1.13996 1.14339 1.25032 -0.22762 -0.04545 -0.23486 228 LYS A CD  
1731 C CE  . LYS A 234 ? 1.33537 1.33259 1.37358 -0.23008 -0.04385 -0.25808 228 LYS A CE  
1732 N NZ  . LYS A 234 ? 1.40408 1.36391 1.44152 -0.23528 -0.01784 -0.29173 228 LYS A NZ  
1733 N N   . SER A 235 ? 1.02769 0.98199 1.33102 -0.18877 -0.00744 -0.11797 229 SER A N   
1734 C CA  . SER A 235 ? 0.99455 0.93114 1.34422 -0.19564 -0.00249 -0.09733 229 SER A CA  
1735 C C   . SER A 235 ? 1.08402 0.98577 1.45273 -0.17778 0.00772  -0.07484 229 SER A C   
1736 O O   . SER A 235 ? 1.05883 0.93636 1.46144 -0.18233 0.01301  -0.05433 229 SER A O   
1737 C CB  . SER A 235 ? 1.16753 1.13797 1.51735 -0.19918 -0.00848 -0.06882 229 SER A CB  
1738 O OG  . SER A 235 ? 1.12697 1.10996 1.45079 -0.17813 -0.00709 -0.03869 229 SER A OG  
1739 N N   . ALA A 236 ? 1.25769 1.01082 1.13078 -0.11359 -0.04460 0.00984  230 ALA A N   
1740 C CA  . ALA A 236 ? 1.15529 0.88216 1.00059 -0.09505 -0.04335 0.01278  230 ALA A CA  
1741 C C   . ALA A 236 ? 1.20391 0.85998 1.00802 -0.09473 -0.05852 0.01408  230 ALA A C   
1742 O O   . ALA A 236 ? 1.32141 0.94987 1.11507 -0.09165 -0.07043 0.00265  230 ALA A O   
1743 C CB  . ALA A 236 ? 1.17090 0.92189 1.02400 -0.06463 -0.04040 -0.00091 230 ALA A CB  
1744 N N   . LYS A 237 ? 1.35081 0.97300 1.12679 -0.09706 -0.05898 0.02792  231 LYS A N   
1745 C CA  . LYS A 237 ? 1.29076 0.83620 1.02266 -0.09647 -0.07518 0.03181  231 LYS A CA  
1746 C C   . LYS A 237 ? 1.27210 0.78729 0.97448 -0.06236 -0.08301 0.02872  231 LYS A C   
1747 O O   . LYS A 237 ? 1.37052 0.81931 1.03643 -0.05197 -0.09981 0.02678  231 LYS A O   
1748 C CB  . LYS A 237 ? 1.27028 0.78511 0.98531 -0.13291 -0.07320 0.05437  231 LYS A CB  
1749 C CG  . LYS A 237 ? 1.56738 1.11177 1.31543 -0.16924 -0.06839 0.05725  231 LYS A CG  
1750 C CD  . LYS A 237 ? 1.79641 1.31711 1.53134 -0.20789 -0.06284 0.08053  231 LYS A CD  
1751 C CE  . LYS A 237 ? 1.94247 1.50096 1.71877 -0.24507 -0.05910 0.08196  231 LYS A CE  
1752 N NZ  . LYS A 237 ? 1.97161 1.51115 1.73875 -0.28707 -0.05118 0.10506  231 LYS A NZ  
1753 N N   . THR A 238 ? 1.34790 0.90803 1.06522 -0.04365 -0.07379 0.02692  232 THR A N   
1754 C CA  . THR A 238 ? 1.32917 0.86562 1.02185 -0.01174 -0.08402 0.02429  232 THR A CA  
1755 C C   . THR A 238 ? 1.32613 0.91985 1.05156 0.01653  -0.07928 0.00607  232 THR A C   
1756 O O   . THR A 238 ? 1.33417 0.91980 1.05950 0.04438  -0.08860 -0.01046 232 THR A O   
1757 C CB  . THR A 238 ? 1.35766 0.87655 1.02129 -0.02069 -0.08176 0.04584  232 THR A CB  
1758 O OG1 . THR A 238 ? 1.38341 0.85008 1.01747 -0.05249 -0.08349 0.06502  232 THR A OG1 
1759 C CG2 . THR A 238 ? 1.30257 0.78895 0.93560 0.01404  -0.09840 0.04363  232 THR A CG2 
1760 N N   . SER A 239 ? 1.26784 0.91975 1.02222 0.00934  -0.06449 0.00796  233 SER A N   
1761 C CA  . SER A 239 ? 1.06492 0.76736 0.84834 0.03185  -0.06083 -0.00677 233 SER A CA  
1762 C C   . SER A 239 ? 1.18170 0.94032 1.00554 0.01798  -0.04531 -0.01200 233 SER A C   
1763 O O   . SER A 239 ? 1.13401 0.90394 0.96537 -0.00633 -0.03614 -0.00189 233 SER A O   
1764 C CB  . SER A 239 ? 1.23127 0.94095 1.00233 0.04353  -0.06368 -0.00076 233 SER A CB  
1765 O OG  . SER A 239 ? 1.45408 1.18584 1.22746 0.02135  -0.04998 0.01178  233 SER A OG  
1766 N N   . ILE A 240 ? 1.06408 0.85828 0.91464 0.03397  -0.04269 -0.02781 234 ILE A N   
1767 C CA  . ILE A 240 ? 0.94161 0.78531 0.82713 0.02498  -0.03013 -0.03248 234 ILE A CA  
1768 C C   . ILE A 240 ? 0.98118 0.86012 0.88729 0.04342  -0.02930 -0.04387 234 ILE A C   
1769 O O   . ILE A 240 ? 1.11426 0.99816 1.02709 0.06088  -0.03275 -0.05640 234 ILE A O   
1770 C CB  . ILE A 240 ? 1.08541 0.93210 0.98096 0.01778  -0.02708 -0.03905 234 ILE A CB  
1771 C CG1 . ILE A 240 ? 0.90754 0.72830 0.79079 -0.00483 -0.02952 -0.02869 234 ILE A CG1 
1772 C CG2 . ILE A 240 ? 0.89122 0.78368 0.81844 0.01410  -0.01666 -0.04417 234 ILE A CG2 
1773 C CD1 . ILE A 240 ? 0.92572 0.74264 0.81105 -0.01074 -0.03122 -0.03586 234 ILE A CD1 
1774 N N   . ASP A 241 ? 0.99047 0.89551 0.90776 0.03947  -0.02475 -0.04110 235 ASP A N   
1775 C CA  . ASP A 241 ? 0.97700 0.91720 0.91725 0.05184  -0.02523 -0.05244 235 ASP A CA  
1776 C C   . ASP A 241 ? 0.97057 0.94388 0.93948 0.03873  -0.01397 -0.05522 235 ASP A C   
1777 O O   . ASP A 241 ? 0.92247 0.89777 0.89079 0.02516  -0.00793 -0.04744 235 ASP A O   
1778 C CB  . ASP A 241 ? 1.00813 0.94512 0.93194 0.06040  -0.03319 -0.04942 235 ASP A CB  
1779 C CG  . ASP A 241 ? 1.12215 1.02179 1.01444 0.07702  -0.04814 -0.04615 235 ASP A CG  
1780 O OD1 . ASP A 241 ? 1.22776 1.11776 1.12348 0.09043  -0.05404 -0.05406 235 ASP A OD1 
1781 O OD2 . ASP A 241 ? 1.15155 1.02932 1.01258 0.07789  -0.05411 -0.03583 235 ASP A OD2 
1782 N N   . ILE A 242 ? 0.84072 0.83956 0.83471 0.04285  -0.01096 -0.06615 236 ILE A N   
1783 C CA  . ILE A 242 ? 0.83460 0.85665 0.85179 0.03065  -0.00218 -0.06785 236 ILE A CA  
1784 C C   . ILE A 242 ? 0.87380 0.92571 0.91597 0.03595  -0.00310 -0.07919 236 ILE A C   
1785 O O   . ILE A 242 ? 0.92899 0.99344 0.98096 0.04712  -0.00573 -0.08809 236 ILE A O   
1786 C CB  . ILE A 242 ? 0.87978 0.89696 0.89817 0.02237  0.00443  -0.06645 236 ILE A CB  
1787 C CG1 . ILE A 242 ? 0.89618 0.88739 0.89528 0.01318  0.00279  -0.05622 236 ILE A CG1 
1788 C CG2 . ILE A 242 ? 0.81461 0.85124 0.85338 0.01187  0.01145  -0.06754 236 ILE A CG2 
1789 C CD1 . ILE A 242 ? 0.78826 0.77144 0.78302 0.00578  0.00533  -0.05562 236 ILE A CD1 
1790 N N   . GLU A 243 ? 0.80846 0.87281 0.86301 0.02818  -0.00164 -0.08031 237 GLU A N   
1791 C CA  . GLU A 243 ? 0.77920 0.86943 0.86006 0.02679  -0.00288 -0.09094 237 GLU A CA  
1792 C C   . GLU A 243 ? 0.80395 0.89442 0.89611 0.01131  0.00474  -0.08792 237 GLU A C   
1793 O O   . GLU A 243 ? 0.89450 0.97913 0.98468 0.00799  0.00308  -0.08710 237 GLU A O   
1794 C CB  . GLU A 243 ? 0.74990 0.84631 0.82852 0.03482  -0.01399 -0.09762 237 GLU A CB  
1795 C CG  . GLU A 243 ? 0.64987 0.77288 0.75816 0.03115  -0.01855 -0.11045 237 GLU A CG  
1796 C CD  . GLU A 243 ? 0.83621 0.96364 0.93808 0.04054  -0.03329 -0.11916 237 GLU A CD  
1797 O OE1 . GLU A 243 ? 0.81247 0.92746 0.88851 0.05444  -0.04124 -0.11594 237 GLU A OE1 
1798 O OE2 . GLU A 243 ? 0.80060 0.93968 0.91926 0.03351  -0.03819 -0.12899 237 GLU A OE2 
1799 N N   . HIS A 244 ? 0.76890 0.86377 0.86946 0.00335  0.01297  -0.08640 238 HIS A N   
1800 C CA  . HIS A 244 ? 0.74420 0.83307 0.85013 -0.01122 0.01863  -0.08138 238 HIS A CA  
1801 C C   . HIS A 244 ? 0.72029 0.82927 0.84754 -0.02115 0.02515  -0.08662 238 HIS A C   
1802 O O   . HIS A 244 ? 0.88913 1.02350 1.03275 -0.01554 0.02533  -0.09595 238 HIS A O   
1803 C CB  . HIS A 244 ? 0.82897 0.89810 0.91578 -0.01501 0.02278  -0.07072 238 HIS A CB  
1804 C CG  . HIS A 244 ? 0.91730 0.97146 0.99438 -0.01370 0.01763  -0.06444 238 HIS A CG  
1805 N ND1 . HIS A 244 ? 0.83746 0.87953 0.91267 -0.02029 0.01666  -0.05754 238 HIS A ND1 
1806 C CD2 . HIS A 244 ? 0.80614 0.85825 0.87604 -0.00665 0.01374  -0.06399 238 HIS A CD2 
1807 C CE1 . HIS A 244 ? 0.90082 0.94048 0.97440 -0.01638 0.01286  -0.05506 238 HIS A CE1 
1808 N NE2 . HIS A 244 ? 0.83760 0.88337 0.90685 -0.00994 0.01281  -0.05821 238 HIS A NE2 
1809 N N   . LEU A 245 ? 0.73090 0.82896 0.85865 -0.03642 0.03024  -0.08013 239 LEU A N   
1810 C CA  . LEU A 245 ? 0.66709 0.78212 0.81298 -0.05170 0.03938  -0.08206 239 LEU A CA  
1811 C C   . LEU A 245 ? 0.85682 0.98220 0.99448 -0.05312 0.05367  -0.07922 239 LEU A C   
1812 O O   . LEU A 245 ? 0.80539 0.96294 0.96439 -0.05764 0.06350  -0.08640 239 LEU A O   
1813 C CB  . LEU A 245 ? 0.57305 0.66370 0.71598 -0.06869 0.03864  -0.07419 239 LEU A CB  
1814 C CG  . LEU A 245 ? 0.66944 0.77225 0.83083 -0.09083 0.04771  -0.07410 239 LEU A CG  
1815 C CD1 . LEU A 245 ? 0.48417 0.62389 0.68117 -0.09118 0.04355  -0.08979 239 LEU A CD1 
1816 C CD2 . LEU A 245 ? 0.70313 0.76826 0.85471 -0.10597 0.04273  -0.06503 239 LEU A CD2 
1817 N N   . ALA A 246 ? 0.81009 0.91142 0.91808 -0.04890 0.05486  -0.07054 240 ALA A N   
1818 C CA  . ALA A 246 ? 0.81977 0.92502 0.91152 -0.04847 0.06749  -0.06950 240 ALA A CA  
1819 C C   . ALA A 246 ? 0.89009 0.96698 0.95061 -0.03882 0.06053  -0.06425 240 ALA A C   
1820 O O   . ALA A 246 ? 1.03824 1.09211 1.08919 -0.04036 0.05000  -0.05639 240 ALA A O   
1821 C CB  . ALA A 246 ? 0.69155 0.79322 0.77517 -0.06899 0.08118  -0.06051 240 ALA A CB  
1822 N N   . ILE A 247 ? 0.97105 1.05131 1.01808 -0.02851 0.06585  -0.07032 241 ILE A N   
1823 C CA  . ILE A 247 ? 0.92305 0.97447 0.93906 -0.02199 0.05860  -0.06710 241 ILE A CA  
1824 C C   . ILE A 247 ? 0.86030 0.90594 0.84875 -0.02526 0.07046  -0.06723 241 ILE A C   
1825 O O   . ILE A 247 ? 1.21962 1.25260 1.18574 -0.01455 0.06911  -0.07365 241 ILE A O   
1826 C CB  . ILE A 247 ? 0.88074 0.92885 0.89690 -0.00467 0.04985  -0.07536 241 ILE A CB  
1827 C CG1 . ILE A 247 ? 0.94223 1.00319 0.98338 -0.00034 0.04198  -0.07716 241 ILE A CG1 
1828 C CG2 . ILE A 247 ? 1.12311 1.13788 1.11300 -0.00430 0.03845  -0.06956 241 ILE A CG2 
1829 C CD1 . ILE A 247 ? 0.91071 0.95596 0.95022 -0.00718 0.03253  -0.06759 241 ILE A CD1 
1830 N N   . VAL A 248 ? 1.04038 1.09160 1.02597 -0.04057 0.08219  -0.06027 242 VAL A N   
1831 C CA  . VAL A 248 ? 1.02749 1.07301 0.98016 -0.04548 0.09615  -0.05891 242 VAL A CA  
1832 C C   . VAL A 248 ? 1.03944 1.04458 0.95311 -0.05003 0.08309  -0.04730 242 VAL A C   
1833 O O   . VAL A 248 ? 1.14639 1.13550 1.06617 -0.05555 0.06868  -0.03706 242 VAL A O   
1834 C CB  . VAL A 248 ? 1.07361 1.14145 1.03598 -0.06321 0.11629  -0.05427 242 VAL A CB  
1835 C CG1 . VAL A 248 ? 1.15818 1.27471 1.16271 -0.05759 0.12910  -0.06914 242 VAL A CG1 
1836 C CG2 . VAL A 248 ? 0.93893 0.98972 0.90943 -0.08001 0.10785  -0.03957 242 VAL A CG2 
1837 N N   . PRO A 249 ? 1.05292 1.04178 0.92669 -0.04612 0.08594  -0.05029 243 PRO A N   
1838 C CA  . PRO A 249 ? 1.04254 0.99455 0.87829 -0.05085 0.07048  -0.03999 243 PRO A CA  
1839 C C   . PRO A 249 ? 1.03814 0.97564 0.84715 -0.06677 0.07633  -0.02426 243 PRO A C   
1840 O O   . PRO A 249 ? 1.23090 1.13696 1.00522 -0.06930 0.06119  -0.01511 243 PRO A O   
1841 C CB  . PRO A 249 ? 1.19347 1.13231 0.99362 -0.03966 0.07074  -0.05245 243 PRO A CB  
1842 C CG  . PRO A 249 ? 1.06802 1.03760 0.87492 -0.03381 0.09623  -0.06474 243 PRO A CG  
1843 C CD  . PRO A 249 ? 1.15161 1.15497 1.01342 -0.03398 0.10087  -0.06604 243 PRO A CD  
1844 N N   . THR A 250 ? 1.01479 0.97249 0.83810 -0.07852 0.09611  -0.02024 244 THR A N   
1845 C CA  . THR A 250 ? 1.09867 1.03737 0.89151 -0.09687 0.10406  -0.00305 244 THR A CA  
1846 C C   . THR A 250 ? 1.10874 1.05399 0.93773 -0.11035 0.10514  0.00566  244 THR A C   
1847 O O   . THR A 250 ? 1.35674 1.33818 1.22851 -0.11187 0.11697  -0.00399 244 THR A O   
1848 C CB  . THR A 250 ? 0.99157 0.94547 0.75504 -0.10381 0.13297  -0.00599 244 THR A CB  
1849 O OG1 . THR A 250 ? 1.34192 1.28810 1.07108 -0.08811 0.13114  -0.01853 244 THR A OG1 
1850 C CG2 . THR A 250 ? 0.98194 0.90717 0.70156 -0.12503 0.14064  0.01542  244 THR A CG2 
1851 N N   . THR A 251 ? 1.14940 1.05762 0.96051 -0.11878 0.09033  0.02262  245 THR A N   
1852 C CA  . THR A 251 ? 1.05615 0.95783 0.89176 -0.13247 0.08920  0.03155  245 THR A CA  
1853 C C   . THR A 251 ? 1.26397 1.12495 1.05341 -0.15141 0.09222  0.05333  245 THR A C   
1854 O O   . THR A 251 ? 1.44954 1.27997 1.18816 -0.14862 0.08469  0.06287  245 THR A O   
1855 C CB  . THR A 251 ? 1.02301 0.91364 0.88713 -0.11979 0.06367  0.02936  245 THR A CB  
1856 O OG1 . THR A 251 ? 1.37838 1.24149 1.21488 -0.10787 0.04242  0.03471  245 THR A OG1 
1857 C CG2 . THR A 251 ? 1.02218 0.95162 0.93147 -0.10652 0.06423  0.01075  245 THR A CG2 
1858 N N   . ARG A 252 ? 1.29844 1.15558 1.10287 -0.17172 0.10156  0.06160  246 ARG A N   
1859 C CA  . ARG A 252 ? 1.56259 1.37757 1.32156 -0.19472 0.10764  0.08475  246 ARG A CA  
1860 C C   . ARG A 252 ? 1.70457 1.47062 1.46426 -0.19439 0.08108  0.09649  246 ARG A C   
1861 O O   . ARG A 252 ? 1.71341 1.48373 1.51253 -0.20211 0.07938  0.09235  246 ARG A O   
1862 C CB  . ARG A 252 ? 1.47782 1.32189 1.25010 -0.22281 0.14017  0.08685  246 ARG A CB  
1863 C CG  . ARG A 252 ? 1.79660 1.60819 1.50682 -0.24742 0.15778  0.10996  246 ARG A CG  
1864 C CD  . ARG A 252 ? 1.87731 1.71441 1.60864 -0.28177 0.18826  0.11534  246 ARG A CD  
1865 N NE  . ARG A 252 ? 2.03617 1.84428 1.79406 -0.29804 0.17412  0.12333  246 ARG A NE  
1866 C CZ  . ARG A 252 ? 2.00717 1.82334 1.78372 -0.33290 0.19328  0.13113  246 ARG A CZ  
1867 N NH1 . ARG A 252 ? 2.02150 1.88112 1.79772 -0.35625 0.23026  0.13273  246 ARG A NH1 
1868 N NH2 . ARG A 252 ? 1.90845 1.68924 1.70551 -0.34514 0.17519  0.13630  246 ARG A NH2 
1869 N N   . VAL A 253 ? 1.89189 1.61126 1.60784 -0.18355 0.05845  0.10934  247 VAL A N   
1870 C CA  . VAL A 253 ? 1.96101 1.62696 1.66864 -0.18052 0.03213  0.12209  247 VAL A CA  
1871 C C   . VAL A 253 ? 2.07181 1.68562 1.72532 -0.20734 0.04012  0.14843  247 VAL A C   
1872 O O   . VAL A 253 ? 2.28602 1.88132 1.88177 -0.21349 0.04688  0.16210  247 VAL A O   
1873 C CB  . VAL A 253 ? 1.78730 1.43414 1.48177 -0.15242 0.00037  0.12125  247 VAL A CB  
1874 C CG1 . VAL A 253 ? 1.66007 1.25405 1.34963 -0.14456 -0.02774 0.13212  247 VAL A CG1 
1875 C CG2 . VAL A 253 ? 1.42501 1.12379 1.17025 -0.13111 -0.00375 0.09735  247 VAL A CG2 
1876 N N   . ASP A 254 ? 1.97405 1.56028 1.64221 -0.22415 0.03866  0.15569  248 ASP A N   
1877 C CA  . ASP A 254 ? 2.17717 1.71390 1.80118 -0.25714 0.04999  0.18130  248 ASP A CA  
1878 C C   . ASP A 254 ? 2.21643 1.77899 1.80666 -0.28112 0.08598  0.18982  248 ASP A C   
1879 O O   . ASP A 254 ? 2.07821 1.70082 1.70928 -0.29557 0.11501  0.17643  248 ASP A O   
1880 C CB  . ASP A 254 ? 2.34272 1.79575 1.90959 -0.24869 0.01852  0.20422  248 ASP A CB  
1881 C CG  . ASP A 254 ? 2.50382 1.95026 2.03168 -0.22196 0.00006  0.20607  248 ASP A CG  
1882 O OD1 . ASP A 254 ? 2.48746 1.92931 1.96045 -0.23341 0.01542  0.21854  248 ASP A OD1 
1883 O OD2 . ASP A 254 ? 2.52619 1.97401 2.07847 -0.19023 -0.02954 0.19411  248 ASP A OD2 
1884 N N   . GLY A 255 ? 2.25248 1.77243 1.76808 -0.28384 0.08410  0.21071  249 GLY A N   
1885 C CA  . GLY A 255 ? 2.25302 1.79080 1.72603 -0.30749 0.12011  0.22044  249 GLY A CA  
1886 C C   . GLY A 255 ? 2.13409 1.73023 1.61026 -0.28810 0.13396  0.19963  249 GLY A C   
1887 O O   . GLY A 255 ? 1.95802 1.61477 1.46179 -0.29953 0.16823  0.18656  249 GLY A O   
1888 N N   . ASN A 256 ? 2.10396 1.68259 1.55387 -0.25839 0.10634  0.19520  250 ASN A N   
1889 C CA  . ASN A 256 ? 2.14582 1.76387 1.58428 -0.24104 0.11526  0.17746  250 ASN A CA  
1890 C C   . ASN A 256 ? 1.83994 1.51334 1.35302 -0.21684 0.10764  0.14751  250 ASN A C   
1891 O O   . ASN A 256 ? 1.56124 1.23520 1.12484 -0.20719 0.08755  0.14148  250 ASN A O   
1892 C CB  . ASN A 256 ? 2.07091 1.63928 1.43795 -0.22491 0.08777  0.18827  250 ASN A CB  
1893 C CG  . ASN A 256 ? 2.26014 1.77086 1.54012 -0.24785 0.09632  0.21899  250 ASN A CG  
1894 O OD1 . ASN A 256 ? 2.36775 1.88545 1.59350 -0.25694 0.12128  0.22148  250 ASN A OD1 
1895 N ND2 . ASN A 256 ? 2.17883 1.62911 1.44126 -0.25688 0.07598  0.24255  250 ASN A ND2 
1896 N N   . SER A 257 ? 1.79800 1.51486 1.31296 -0.20653 0.12420  0.12863  251 SER A N   
1897 C CA  . SER A 257 ? 1.48552 1.25081 1.06181 -0.18496 0.11939  0.10170  251 SER A CA  
1898 C C   . SER A 257 ? 1.48816 1.23492 1.05246 -0.15947 0.08594  0.09482  251 SER A C   
1899 O O   . SER A 257 ? 1.46022 1.16686 0.96490 -0.15633 0.07031  0.10607  251 SER A O   
1900 C CB  . SER A 257 ? 1.32425 1.14309 0.91104 -0.18493 0.15264  0.08343  251 SER A CB  
1901 O OG  . SER A 257 ? 1.63274 1.48034 1.24220 -0.20949 0.18404  0.08767  251 SER A OG  
1902 N N   . TYR A 258 ? 1.27779 1.05525 0.89927 -0.14248 0.07458  0.07628  252 TYR A N   
1903 C CA  . TYR A 258 ? 1.21643 0.98411 0.84157 -0.12194 0.04353  0.06908  252 TYR A CA  
1904 C C   . TYR A 258 ? 1.32048 1.12767 0.97790 -0.10835 0.04925  0.04565  252 TYR A C   
1905 O O   . TYR A 258 ? 1.27005 1.11086 0.98076 -0.10606 0.05826  0.03488  252 TYR A O   
1906 C CB  . TYR A 258 ? 1.27979 1.03501 0.94234 -0.11563 0.01847  0.07438  252 TYR A CB  
1907 C CG  . TYR A 258 ? 1.47983 1.23368 1.15461 -0.09665 -0.01179 0.06712  252 TYR A CG  
1908 C CD1 . TYR A 258 ? 1.46584 1.18904 1.09352 -0.09118 -0.03393 0.07436  252 TYR A CD1 
1909 C CD2 . TYR A 258 ? 1.25060 1.03536 0.98371 -0.08564 -0.01844 0.05326  252 TYR A CD2 
1910 C CE1 . TYR A 258 ? 1.33389 1.06228 0.97981 -0.07645 -0.06222 0.06683  252 TYR A CE1 
1911 C CE2 . TYR A 258 ? 1.28049 1.06949 1.02888 -0.07211 -0.04323 0.04726  252 TYR A CE2 
1912 C CZ  . TYR A 258 ? 1.35866 1.12184 1.06711 -0.06818 -0.06526 0.05356  252 TYR A CZ  
1913 O OH  . TYR A 258 ? 1.48037 1.25390 1.21061 -0.05720 -0.09058 0.04670  252 TYR A OH  
1914 N N   . TYR A 259 ? 1.23201 1.03020 0.85359 -0.09911 0.04156  0.03783  253 TYR A N   
1915 C CA  . TYR A 259 ? 1.18856 1.01171 0.83028 -0.08598 0.04372  0.01635  253 TYR A CA  
1916 C C   . TYR A 259 ? 1.07890 0.89871 0.74955 -0.07532 0.01372  0.01175  253 TYR A C   
1917 O O   . TYR A 259 ? 1.20426 0.99828 0.85213 -0.07368 -0.01139 0.01924  253 TYR A O   
1918 C CB  . TYR A 259 ? 1.23443 1.04594 0.81851 -0.08254 0.05223  0.00796  253 TYR A CB  
1919 C CG  . TYR A 259 ? 1.30640 1.13599 0.90473 -0.06801 0.05546  -0.01539 253 TYR A CG  
1920 C CD1 . TYR A 259 ? 1.22069 1.08786 0.86104 -0.06313 0.07727  -0.02781 253 TYR A CD1 
1921 C CD2 . TYR A 259 ? 1.37691 1.18278 0.94539 -0.05896 0.03427  -0.02536 253 TYR A CD2 
1922 C CE1 . TYR A 259 ? 1.21132 1.08781 0.86108 -0.04728 0.07757  -0.04843 253 TYR A CE1 
1923 C CE2 . TYR A 259 ? 1.29372 1.10671 0.87119 -0.04615 0.03540  -0.04626 253 TYR A CE2 
1924 C CZ  . TYR A 259 ? 1.25980 1.10598 0.87640 -0.03920 0.05704  -0.05716 253 TYR A CZ  
1925 O OH  . TYR A 259 ? 1.31439 1.16080 0.93649 -0.02396 0.05556  -0.07720 253 TYR A OH  
1926 N N   . TRP A 260 ? 1.14069 0.98839 0.86161 -0.06857 0.01627  -0.00022 254 TRP A N   
1927 C CA  . TRP A 260 ? 1.00854 0.85981 0.76227 -0.06169 -0.00642 -0.00402 254 TRP A CA  
1928 C C   . TRP A 260 ? 0.99391 0.86791 0.77873 -0.05446 0.00178  -0.01914 254 TRP A C   
1929 O O   . TRP A 260 ? 1.14215 1.03889 0.96679 -0.05332 0.01065  -0.02067 254 TRP A O   
1930 C CB  . TRP A 260 ? 0.99080 0.84562 0.77868 -0.06337 -0.01617 0.00666  254 TRP A CB  
1931 C CG  . TRP A 260 ? 1.07080 0.93187 0.88883 -0.05715 -0.03903 0.00459  254 TRP A CG  
1932 C CD1 . TRP A 260 ? 1.08566 0.93238 0.89217 -0.05508 -0.06416 0.00936  254 TRP A CD1 
1933 C CD2 . TRP A 260 ? 1.08573 0.97285 0.95142 -0.05296 -0.03812 -0.00274 254 TRP A CD2 
1934 N NE1 . TRP A 260 ? 1.06095 0.92882 0.91091 -0.05095 -0.07690 0.00466  254 TRP A NE1 
1935 C CE2 . TRP A 260 ? 1.03280 0.92361 0.91608 -0.05022 -0.05990 -0.00196 254 TRP A CE2 
1936 C CE3 . TRP A 260 ? 1.08969 0.99838 0.98344 -0.05122 -0.02158 -0.00985 254 TRP A CE3 
1937 C CZ2 . TRP A 260 ? 0.93090 0.84682 0.85689 -0.04783 -0.06151 -0.00710 254 TRP A CZ2 
1938 C CZ3 . TRP A 260 ? 1.08020 1.00751 1.00999 -0.04738 -0.02599 -0.01424 254 TRP A CZ3 
1939 C CH2 . TRP A 260 ? 0.92895 0.86002 0.87365 -0.04668 -0.04379 -0.01241 254 TRP A CH2 
1940 N N   . PRO A 261 ? 1.02091 0.88489 0.78503 -0.04890 -0.00288 -0.03073 255 PRO A N   
1941 C CA  . PRO A 261 ? 1.06536 0.94249 0.85049 -0.04034 0.00493  -0.04435 255 PRO A CA  
1942 C C   . PRO A 261 ? 1.02632 0.90084 0.83656 -0.03984 -0.01321 -0.04612 255 PRO A C   
1943 O O   . PRO A 261 ? 1.13885 1.00852 0.95083 -0.03352 -0.01305 -0.05644 255 PRO A O   
1944 C CB  . PRO A 261 ? 1.14623 1.00702 0.88682 -0.03377 0.01158  -0.05697 255 PRO A CB  
1945 C CG  . PRO A 261 ? 1.07414 0.90595 0.77422 -0.04001 -0.00737 -0.05146 255 PRO A CG  
1946 C CD  . PRO A 261 ? 0.99843 0.83393 0.71039 -0.04922 -0.01374 -0.03317 255 PRO A CD  
1947 N N   . ASP A 262 ? 1.06569 0.94322 0.89534 -0.04627 -0.02843 -0.03613 256 ASP A N   
1948 C CA  . ASP A 262 ? 0.91148 0.79062 0.76427 -0.04952 -0.04426 -0.03709 256 ASP A CA  
1949 C C   . ASP A 262 ? 1.03385 0.92725 0.91538 -0.04580 -0.03429 -0.04088 256 ASP A C   
1950 O O   . ASP A 262 ? 1.12398 1.00520 1.00274 -0.04661 -0.03980 -0.04628 256 ASP A O   
1951 C CB  . ASP A 262 ? 1.06010 0.95075 0.93671 -0.05419 -0.05890 -0.02721 256 ASP A CB  
1952 C CG  . ASP A 262 ? 1.08893 0.96105 0.93399 -0.05627 -0.07506 -0.02264 256 ASP A CG  
1953 O OD1 . ASP A 262 ? 1.14320 0.99385 0.94375 -0.05530 -0.07059 -0.02576 256 ASP A OD1 
1954 O OD2 . ASP A 262 ? 1.24281 1.12267 1.10630 -0.05740 -0.09263 -0.01656 256 ASP A OD2 
1955 N N   . ILE A 263 ? 0.93239 0.84732 0.83817 -0.04226 -0.02140 -0.03783 257 ILE A N   
1956 C CA  . ILE A 263 ? 0.87113 0.79833 0.79883 -0.03722 -0.01385 -0.04135 257 ILE A CA  
1957 C C   . ILE A 263 ? 0.98364 0.90374 0.89456 -0.02724 -0.00414 -0.05168 257 ILE A C   
1958 O O   . ILE A 263 ? 1.05246 0.96387 0.96362 -0.02175 -0.00636 -0.05629 257 ILE A O   
1959 C CB  . ILE A 263 ? 0.87466 0.82582 0.83168 -0.03607 -0.00631 -0.03719 257 ILE A CB  
1960 C CG1 . ILE A 263 ? 0.94004 0.89858 0.91533 -0.04127 -0.01659 -0.02973 257 ILE A CG1 
1961 C CG2 . ILE A 263 ? 0.91510 0.87753 0.88846 -0.02973 -0.00033 -0.04133 257 ILE A CG2 
1962 C CD1 . ILE A 263 ? 0.89497 0.87105 0.89534 -0.03824 -0.01109 -0.02807 257 ILE A CD1 
1963 N N   . TYR A 264 ? 0.82012 0.74370 0.71565 -0.02422 0.00700  -0.05533 258 TYR A N   
1964 C CA  . TYR A 264 ? 0.94616 0.87053 0.82951 -0.01198 0.01805  -0.06786 258 TYR A CA  
1965 C C   . TYR A 264 ? 1.07729 0.97003 0.93344 -0.00579 0.00747  -0.07658 258 TYR A C   
1966 O O   . TYR A 264 ? 1.03427 0.92151 0.89058 0.00757  0.00869  -0.08619 258 TYR A O   
1967 C CB  . TYR A 264 ? 1.04350 0.97770 0.91030 -0.01373 0.03349  -0.06931 258 TYR A CB  
1968 C CG  . TYR A 264 ? 1.01094 0.95829 0.87184 -0.00005 0.04947  -0.08413 258 TYR A CG  
1969 C CD1 . TYR A 264 ? 0.99231 0.97450 0.88736 0.00609  0.06189  -0.08913 258 TYR A CD1 
1970 C CD2 . TYR A 264 ? 1.20274 1.13027 1.02506 0.00788  0.05148  -0.09505 258 TYR A CD2 
1971 C CE1 . TYR A 264 ? 1.11849 1.12101 1.01550 0.02070  0.07636  -0.10445 258 TYR A CE1 
1972 C CE2 . TYR A 264 ? 1.13237 1.07644 0.95179 0.02379  0.06765  -0.11117 258 TYR A CE2 
1973 C CZ  . TYR A 264 ? 1.14179 1.12623 1.00163 0.03057  0.08037  -0.11571 258 TYR A CZ  
1974 O OH  . TYR A 264 ? 1.27371 1.28262 1.13799 0.04847  0.09621  -0.13348 258 TYR A OH  
1975 N N   . ASN A 265 ? 1.00007 0.86880 0.83216 -0.01489 -0.00579 -0.07390 259 ASN A N   
1976 C CA  . ASN A 265 ? 1.00329 0.83631 0.80751 -0.01201 -0.01865 -0.08320 259 ASN A CA  
1977 C C   . ASN A 265 ? 1.00310 0.82422 0.82498 -0.01612 -0.03002 -0.07933 259 ASN A C   
1978 O O   . ASN A 265 ? 1.09811 0.89149 0.90446 -0.00768 -0.03491 -0.08793 259 ASN A O   
1979 C CB  . ASN A 265 ? 0.92903 0.74103 0.70399 -0.02270 -0.03303 -0.08197 259 ASN A CB  
1980 C CG  . ASN A 265 ? 1.17423 0.98465 0.91354 -0.01738 -0.02222 -0.08756 259 ASN A CG  
1981 O OD1 . ASN A 265 ? 1.20824 1.03038 0.94176 -0.00478 -0.00304 -0.09652 259 ASN A OD1 
1982 N ND2 . ASN A 265 ? 0.98899 0.78673 0.70360 -0.02690 -0.03453 -0.08236 259 ASN A ND2 
1983 N N   . SER A 266 ? 1.01262 0.85203 0.86417 -0.02878 -0.03405 -0.06642 260 SER A N   
1984 C CA  . SER A 266 ? 0.97251 0.80317 0.83819 -0.03632 -0.04164 -0.06066 260 SER A CA  
1985 C C   . SER A 266 ? 1.09372 0.92187 0.96256 -0.02238 -0.03397 -0.06350 260 SER A C   
1986 O O   . SER A 266 ? 1.25106 1.05331 1.11236 -0.02485 -0.04142 -0.06124 260 SER A O   
1987 C CB  . SER A 266 ? 1.00693 0.86714 0.90627 -0.04935 -0.04258 -0.04835 260 SER A CB  
1988 O OG  . SER A 266 ? 1.21421 1.07340 1.11297 -0.06186 -0.05586 -0.04598 260 SER A OG  
1989 N N   . ILE A 267 ? 1.06057 0.91408 0.93991 -0.00864 -0.02064 -0.06791 261 ILE A N   
1990 C CA  . ILE A 267 ? 0.94367 0.79866 0.82789 0.00758  -0.01662 -0.07258 261 ILE A CA  
1991 C C   . ILE A 267 ? 1.06091 0.88504 0.91726 0.02436  -0.02038 -0.08654 261 ILE A C   
1992 O O   . ILE A 267 ? 1.18806 0.98207 1.03226 0.03245  -0.02951 -0.08763 261 ILE A O   
1993 C CB  . ILE A 267 ? 1.03415 0.93125 0.94471 0.01469  -0.00312 -0.07434 261 ILE A CB  
1994 C CG1 . ILE A 267 ? 0.93960 0.85939 0.87436 0.00090  -0.00168 -0.06260 261 ILE A CG1 
1995 C CG2 . ILE A 267 ? 0.90416 0.80720 0.82208 0.03358  -0.00228 -0.08150 261 ILE A CG2 
1996 C CD1 . ILE A 267 ? 0.76676 0.72070 0.72415 0.00275  0.00931  -0.06424 261 ILE A CD1 
1997 N N   . ILE A 268 ? 1.00658 0.83462 0.84869 0.03068  -0.01343 -0.09751 262 ILE A N   
1998 C CA  . ILE A 268 ? 0.99446 0.79618 0.80932 0.05037  -0.01498 -0.11464 262 ILE A CA  
1999 C C   . ILE A 268 ? 1.13647 0.88166 0.92007 0.04447  -0.03405 -0.11549 262 ILE A C   
2000 O O   . ILE A 268 ? 1.21807 0.92776 0.98353 0.06083  -0.04243 -0.12480 262 ILE A O   
2001 C CB  . ILE A 268 ? 1.01349 0.83327 0.81500 0.05533  -0.00059 -0.12561 262 ILE A CB  
2002 C CG1 . ILE A 268 ? 1.12466 0.99813 0.95874 0.06173  0.01915  -0.12681 262 ILE A CG1 
2003 C CG2 . ILE A 268 ? 1.21721 1.00457 0.98330 0.07508  -0.00309 -0.14564 262 ILE A CG2 
2004 C CD1 . ILE A 268 ? 1.46672 1.36082 1.28716 0.06626  0.03785  -0.13725 262 ILE A CD1 
2005 N N   . GLU A 269 ? 1.17569 0.91051 0.95371 0.02100  -0.04301 -0.10624 263 GLU A N   
2006 C CA  . GLU A 269 ? 1.21582 0.90002 0.96996 0.00903  -0.06245 -0.10594 263 GLU A CA  
2007 C C   . GLU A 269 ? 1.23076 0.89141 0.99033 0.00745  -0.06972 -0.09684 263 GLU A C   
2008 O O   . GLU A 269 ? 1.23184 0.83901 0.96352 0.01028  -0.08350 -0.10198 263 GLU A O   
2009 C CB  . GLU A 269 ? 1.26866 0.96054 1.02988 -0.01766 -0.07121 -0.09585 263 GLU A CB  
2010 C CG  . GLU A 269 ? 1.53948 1.18520 1.28205 -0.03573 -0.09242 -0.09585 263 GLU A CG  
2011 C CD  . GLU A 269 ? 1.54197 1.20810 1.30471 -0.06200 -0.10193 -0.08536 263 GLU A CD  
2012 O OE1 . GLU A 269 ? 1.38220 1.09501 1.17898 -0.06645 -0.09210 -0.07404 263 GLU A OE1 
2013 O OE2 . GLU A 269 ? 1.82436 1.45993 1.57012 -0.07719 -0.12087 -0.08988 263 GLU A OE2 
2014 N N   . ALA A 270 ? 1.02839 0.72381 0.81893 0.00310  -0.06121 -0.08327 264 ALA A N   
2015 C CA  . ALA A 270 ? 1.12052 0.79405 0.91005 0.00142  -0.06659 -0.07260 264 ALA A CA  
2016 C C   . ALA A 270 ? 1.27303 0.91838 1.04318 0.03067  -0.07045 -0.08358 264 ALA A C   
2017 O O   . ALA A 270 ? 1.37305 0.96841 1.11988 0.03169  -0.08314 -0.07900 264 ALA A O   
2018 C CB  . ALA A 270 ? 1.00791 0.72736 0.83020 -0.00585 -0.05555 -0.05890 264 ALA A CB  
2019 N N   . ALA A 271 ? 1.22912 0.90590 1.00923 0.05464  -0.06006 -0.09795 265 ALA A N   
2020 C CA  . ALA A 271 ? 1.14500 0.80629 0.91551 0.08664  -0.06386 -0.11090 265 ALA A CA  
2021 C C   . ALA A 271 ? 1.25291 0.85971 0.98584 0.10063  -0.07508 -0.12751 265 ALA A C   
2022 O O   . ALA A 271 ? 1.43505 0.99078 1.14442 0.11595  -0.09003 -0.13023 265 ALA A O   
2023 C CB  . ALA A 271 ? 1.05544 0.77797 0.85701 0.10538  -0.04745 -0.12184 265 ALA A CB  
2024 N N   . ILE A 272 ? 1.22964 0.84160 0.95185 0.09655  -0.06950 -0.13906 266 ILE A N   
2025 C CA  . ILE A 272 ? 1.30127 0.86418 0.98487 0.11364  -0.07872 -0.15956 266 ILE A CA  
2026 C C   . ILE A 272 ? 1.32464 0.81727 0.97581 0.09282  -0.10079 -0.15301 266 ILE A C   
2027 O O   . ILE A 272 ? 1.54186 0.97240 1.16234 0.10774  -0.11679 -0.16161 266 ILE A O   
2028 C CB  . ILE A 272 ? 1.36315 0.95552 1.03966 0.11665  -0.06417 -0.17467 266 ILE A CB  
2029 C CG1 . ILE A 272 ? 1.23641 0.89916 0.94730 0.13269  -0.04046 -0.17976 266 ILE A CG1 
2030 C CG2 . ILE A 272 ? 1.20717 0.74787 0.83892 0.13670  -0.07308 -0.19903 266 ILE A CG2 
2031 C CD1 . ILE A 272 ? 1.14995 0.83952 0.84798 0.13749  -0.02266 -0.19448 266 ILE A CD1 
2032 N N   . ASN A 273 ? 1.34146 0.84220 1.00043 0.05796  -0.10319 -0.13825 267 ASN A N   
2033 C CA  . ASN A 273 ? 1.31277 0.75408 0.94606 0.03349  -0.12385 -0.13388 267 ASN A CA  
2034 C C   . ASN A 273 ? 1.50060 0.90741 1.13435 0.01949  -0.13370 -0.11457 267 ASN A C   
2035 O O   . ASN A 273 ? 1.61646 0.95475 1.21931 0.00906  -0.15256 -0.11459 267 ASN A O   
2036 C CB  . ASN A 273 ? 1.29842 0.76715 0.94509 0.00202  -0.12461 -0.12633 267 ASN A CB  
2037 C CG  . ASN A 273 ? 1.27345 0.75701 0.90311 0.01244  -0.12000 -0.14435 267 ASN A CG  
2038 O OD1 . ASN A 273 ? 1.46153 0.99037 1.10916 0.00026  -0.11231 -0.13820 267 ASN A OD1 
2039 N ND2 . ASN A 273 ? 1.38450 0.82749 0.97577 0.03667  -0.12468 -0.16697 267 ASN A ND2 
2040 N N   . ARG A 274 ? 1.32839 0.77729 0.99238 0.01772  -0.12168 -0.09791 268 ARG A N   
2041 C CA  . ARG A 274 ? 1.31203 0.73315 0.97287 0.00049  -0.12784 -0.07660 268 ARG A CA  
2042 C C   . ARG A 274 ? 1.39223 0.80658 1.04812 0.02822  -0.12700 -0.07348 268 ARG A C   
2043 O O   . ARG A 274 ? 1.58220 0.97051 1.22806 0.01588  -0.13159 -0.05427 268 ARG A O   
2044 C CB  . ARG A 274 ? 1.24858 0.72149 0.94506 -0.03191 -0.11658 -0.05705 268 ARG A CB  
2045 C CG  . ARG A 274 ? 1.19687 0.68517 0.90488 -0.05758 -0.11996 -0.05984 268 ARG A CG  
2046 C CD  . ARG A 274 ? 1.32925 0.85532 1.07039 -0.09097 -0.11360 -0.04019 268 ARG A CD  
2047 N NE  . ARG A 274 ? 1.22512 0.81179 0.99767 -0.08245 -0.09500 -0.03228 268 ARG A NE  
2048 C CZ  . ARG A 274 ? 1.15683 0.79983 0.95819 -0.07806 -0.08494 -0.03662 268 ARG A CZ  
2049 N NH1 . ARG A 274 ? 1.41823 1.06764 1.21941 -0.08038 -0.09088 -0.04732 268 ARG A NH1 
2050 N NH2 . ARG A 274 ? 1.28652 0.97583 1.11325 -0.07122 -0.07011 -0.02995 268 ARG A NH2 
2051 N N   . GLY A 275 ? 1.39861 0.83725 1.06098 0.06453  -0.12154 -0.09149 269 GLY A N   
2052 C CA  . GLY A 275 ? 1.23839 0.67134 0.89806 0.09406  -0.12543 -0.09128 269 GLY A CA  
2053 C C   . GLY A 275 ? 1.39490 0.87301 1.08000 0.08516  -0.11583 -0.07277 269 GLY A C   
2054 O O   . GLY A 275 ? 1.44136 0.89647 1.11249 0.09895  -0.12487 -0.06444 269 GLY A O   
2055 N N   . VAL A 276 ? 1.36039 0.89883 1.07893 0.06394  -0.09935 -0.06674 270 VAL A N   
2056 C CA  . VAL A 276 ? 1.24693 0.82899 0.98861 0.05677  -0.08968 -0.05246 270 VAL A CA  
2057 C C   . VAL A 276 ? 1.18908 0.81246 0.95173 0.08846  -0.08590 -0.06489 270 VAL A C   
2058 O O   . VAL A 276 ? 1.30746 0.96274 1.08840 0.10419  -0.07874 -0.08294 270 VAL A O   
2059 C CB  . VAL A 276 ? 1.21002 0.84097 0.98163 0.02818  -0.07513 -0.04522 270 VAL A CB  
2060 C CG1 . VAL A 276 ? 1.20888 0.88591 1.00391 0.02480  -0.06450 -0.03493 270 VAL A CG1 
2061 C CG2 . VAL A 276 ? 1.20654 0.80429 0.96475 -0.00421 -0.08043 -0.03324 270 VAL A CG2 
2062 N N   . LYS A 277 ? 1.31712 0.94137 1.07648 0.09687  -0.09079 -0.05538 271 LYS A N   
2063 C CA  . LYS A 277 ? 1.22171 0.89145 1.00653 0.12355  -0.08968 -0.06665 271 LYS A CA  
2064 C C   . LYS A 277 ? 1.14214 0.87919 0.96626 0.10801  -0.07204 -0.06586 271 LYS A C   
2065 O O   . LYS A 277 ? 1.22207 0.96672 1.04657 0.08571  -0.06644 -0.05071 271 LYS A O   
2066 C CB  . LYS A 277 ? 1.27979 0.92195 1.04168 0.13893  -0.10545 -0.05713 271 LYS A CB  
2067 C CG  . LYS A 277 ? 1.50935 1.19861 1.29947 0.16827  -0.10955 -0.07084 271 LYS A CG  
2068 C CD  . LYS A 277 ? 1.71399 1.36646 1.47372 0.18891  -0.13130 -0.06290 271 LYS A CD  
2069 C CE  . LYS A 277 ? 1.74481 1.44964 1.53827 0.21869  -0.13891 -0.07905 271 LYS A CE  
2070 N NZ  . LYS A 277 ? 1.65495 1.32139 1.41601 0.24382  -0.16509 -0.07279 271 LYS A NZ  
2071 N N   . ILE A 278 ? 1.21100 0.99563 1.06718 0.11949  -0.06259 -0.08238 272 ILE A N   
2072 C CA  . ILE A 278 ? 1.11994 0.95978 1.01035 0.10358  -0.04671 -0.08221 272 ILE A CA  
2073 C C   . ILE A 278 ? 1.12174 1.01068 1.04487 0.12167  -0.04505 -0.09443 272 ILE A C   
2074 O O   . ILE A 278 ? 1.13596 1.03470 1.06799 0.14558  -0.04797 -0.10998 272 ILE A O   
2075 C CB  . ILE A 278 ? 0.96387 0.81289 0.85978 0.09095  -0.03487 -0.08749 272 ILE A CB  
2076 C CG1 . ILE A 278 ? 1.07025 0.87300 0.93739 0.07196  -0.04033 -0.07701 272 ILE A CG1 
2077 C CG2 . ILE A 278 ? 0.96062 0.85822 0.88740 0.07521  -0.02081 -0.08530 272 ILE A CG2 
2078 C CD1 . ILE A 278 ? 1.07651 0.88420 0.94356 0.05953  -0.03320 -0.08152 272 ILE A CD1 
2079 N N   . ARG A 279 ? 1.01210 0.93337 0.95491 0.11053  -0.04087 -0.08904 273 ARG A N   
2080 C CA  . ARG A 279 ? 1.02680 0.99795 1.00513 0.12094  -0.03992 -0.10055 273 ARG A CA  
2081 C C   . ARG A 279 ? 1.02687 1.03401 1.03153 0.09875  -0.02468 -0.09910 273 ARG A C   
2082 O O   . ARG A 279 ? 0.90826 0.90809 0.90577 0.08159  -0.02242 -0.08766 273 ARG A O   
2083 C CB  . ARG A 279 ? 0.98121 0.94819 0.95160 0.13231  -0.05585 -0.09726 273 ARG A CB  
2084 C CG  . ARG A 279 ? 1.11209 1.03858 1.05351 0.15726  -0.07441 -0.09775 273 ARG A CG  
2085 C CD  . ARG A 279 ? 1.01149 0.93188 0.93896 0.16889  -0.09207 -0.09315 273 ARG A CD  
2086 N NE  . ARG A 279 ? 1.07552 0.97525 0.97568 0.14681  -0.08806 -0.07521 273 ARG A NE  
2087 C CZ  . ARG A 279 ? 1.16107 1.04944 1.03723 0.15136  -0.09995 -0.06784 273 ARG A CZ  
2088 N NH1 . ARG A 279 ? 1.15129 1.04386 1.02639 0.17754  -0.12057 -0.07596 273 ARG A NH1 
2089 N NH2 . ARG A 279 ? 1.13056 1.00517 0.98273 0.13021  -0.09119 -0.05279 273 ARG A NH2 
2090 N N   . LEU A 280 ? 0.88873 0.93365 0.92284 0.09939  -0.01382 -0.11062 274 LEU A N   
2091 C CA  . LEU A 280 ? 0.87421 0.94656 0.92983 0.07820  -0.00008 -0.10850 274 LEU A CA  
2092 C C   . LEU A 280 ? 1.01044 1.12843 1.10404 0.07999  -0.00053 -0.11857 274 LEU A C   
2093 O O   . LEU A 280 ? 0.94842 1.09675 1.06525 0.09402  0.00031  -0.13198 274 LEU A O   
2094 C CB  . LEU A 280 ? 0.77479 0.84911 0.82739 0.07127  0.01469  -0.11073 274 LEU A CB  
2095 C CG  . LEU A 280 ? 0.78923 0.81904 0.80509 0.06921  0.01245  -0.10400 274 LEU A CG  
2096 C CD1 . LEU A 280 ? 0.72694 0.76030 0.73543 0.06494  0.02583  -0.10886 274 LEU A CD1 
2097 C CD2 . LEU A 280 ? 0.77028 0.77816 0.77356 0.05130  0.00830  -0.08871 274 LEU A CD2 
2098 N N   . LEU A 281 ? 0.83661 0.96085 0.93831 0.06622  -0.00250 -0.11378 275 LEU A N   
2099 C CA  . LEU A 281 ? 0.77779 0.94087 0.91478 0.06247  -0.00486 -0.12338 275 LEU A CA  
2100 C C   . LEU A 281 ? 0.79723 0.96838 0.94715 0.03797  0.00889  -0.11888 275 LEU A C   
2101 O O   . LEU A 281 ? 0.86140 1.01327 0.99981 0.02677  0.00740  -0.11091 275 LEU A O   
2102 C CB  . LEU A 281 ? 0.77476 0.93103 0.90382 0.06877  -0.02182 -0.12368 275 LEU A CB  
2103 C CG  . LEU A 281 ? 0.77197 0.96383 0.93442 0.06450  -0.02939 -0.13546 275 LEU A CG  
2104 C CD1 . LEU A 281 ? 0.64281 0.87880 0.84365 0.07502  -0.03128 -0.15015 275 LEU A CD1 
2105 C CD2 . LEU A 281 ? 0.71415 0.89189 0.85632 0.07351  -0.04754 -0.13603 275 LEU A CD2 
2106 N N   . VAL A 282 ? 0.77736 0.97589 0.94942 0.03042  0.02266  -0.12388 276 VAL A N   
2107 C CA  . VAL A 282 ? 0.65672 0.85328 0.83106 0.00684  0.03674  -0.11621 276 VAL A CA  
2108 C C   . VAL A 282 ? 0.70673 0.94390 0.92145 -0.00734 0.04243  -0.12439 276 VAL A C   
2109 O O   . VAL A 282 ? 0.80755 1.08094 1.05278 0.00217  0.03595  -0.13770 276 VAL A O   
2110 C CB  . VAL A 282 ? 0.71837 0.90239 0.87080 0.00489  0.05138  -0.11068 276 VAL A CB  
2111 C CG1 . VAL A 282 ? 0.71896 0.86333 0.83510 0.01617  0.04329  -0.10397 276 VAL A CG1 
2112 C CG2 . VAL A 282 ? 0.68265 0.90378 0.85459 0.01463  0.06255  -0.12341 276 VAL A CG2 
2113 N N   . GLY A 283 ? 0.71104 0.94061 0.92580 -0.03118 0.05322  -0.11583 277 GLY A N   
2114 C CA  . GLY A 283 ? 0.53219 0.79490 0.78302 -0.05152 0.06072  -0.12076 277 GLY A CA  
2115 C C   . GLY A 283 ? 0.75776 1.06536 1.03154 -0.05193 0.07925  -0.12812 277 GLY A C   
2116 O O   . GLY A 283 ? 1.00383 1.30942 1.25842 -0.03737 0.08833  -0.12848 277 GLY A O   
2117 N N   . ASN A 284 ? 0.69674 1.04721 1.01375 -0.06957 0.08527  -0.13557 278 ASN A N   
2118 C CA  . ASN A 284 ? 0.87569 1.28249 1.22523 -0.07115 0.10523  -0.14522 278 ASN A CA  
2119 C C   . ASN A 284 ? 1.08639 1.48225 1.41041 -0.09086 0.13259  -0.13185 278 ASN A C   
2120 O O   . ASN A 284 ? 1.05689 1.41998 1.36249 -0.11734 0.13681  -0.11631 278 ASN A O   
2121 C CB  . ASN A 284 ? 0.88046 1.34177 1.28978 -0.08807 0.10284  -0.15732 278 ASN A CB  
2122 C CG  . ASN A 284 ? 1.10783 1.64170 1.56240 -0.08520 0.12237  -0.17141 278 ASN A CG  
2123 O OD1 . ASN A 284 ? 0.97905 1.52514 1.42434 -0.05795 0.12930  -0.17866 278 ASN A OD1 
2124 N ND2 . ASN A 284 ? 1.30195 1.88529 1.80743 -0.11355 0.13141  -0.17657 278 ASN A ND2 
2125 N N   . TRP A 285 ? 1.14335 1.56332 1.46223 -0.07616 0.15008  -0.13843 279 TRP A N   
2126 C CA  . TRP A 285 ? 1.14320 1.55611 1.43246 -0.09277 0.17757  -0.12754 279 TRP A CA  
2127 C C   . TRP A 285 ? 1.37203 1.83373 1.69971 -0.12570 0.20105  -0.12675 279 TRP A C   
2128 O O   . TRP A 285 ? 1.44013 1.95827 1.82696 -0.12923 0.19902  -0.14087 279 TRP A O   
2129 C CB  . TRP A 285 ? 1.07024 1.49413 1.33986 -0.06513 0.18938  -0.13827 279 TRP A CB  
2130 C CG  . TRP A 285 ? 1.35089 1.74229 1.60000 -0.03101 0.16497  -0.14482 279 TRP A CG  
2131 C CD1 . TRP A 285 ? 1.50462 1.91966 1.78427 -0.00412 0.14762  -0.16107 279 TRP A CD1 
2132 C CD2 . TRP A 285 ? 1.64663 1.97481 1.83935 -0.02189 0.15446  -0.13436 279 TRP A CD2 
2133 N NE1 . TRP A 285 ? 1.67831 2.04423 1.92041 0.01917  0.12861  -0.15948 279 TRP A NE1 
2134 C CE2 . TRP A 285 ? 1.52637 1.84166 1.71834 0.00758  0.13295  -0.14393 279 TRP A CE2 
2135 C CE3 . TRP A 285 ? 1.72454 2.00589 1.86781 -0.03637 0.15939  -0.11760 279 TRP A CE3 
2136 C CZ2 . TRP A 285 ? 1.29356 1.55322 1.44041 0.01918  0.11877  -0.13716 279 TRP A CZ2 
2137 C CZ3 . TRP A 285 ? 1.66053 1.89137 1.76281 -0.02226 0.14311  -0.11295 279 TRP A CZ3 
2138 C CH2 . TRP A 285 ? 1.50372 1.72526 1.60970 0.00341  0.12422  -0.12263 279 TRP A CH2 
2139 N N   . ASP A 286 ? 1.56665 2.00585 1.85915 -0.15140 0.22282  -0.10941 280 ASP A N   
2140 C CA  . ASP A 286 ? 1.93083 2.40626 2.24966 -0.18932 0.24823  -0.10330 280 ASP A CA  
2141 C C   . ASP A 286 ? 1.89356 2.39161 2.18705 -0.19360 0.28434  -0.10112 280 ASP A C   
2142 O O   . ASP A 286 ? 1.99980 2.46303 2.23939 -0.17336 0.28636  -0.09850 280 ASP A O   
2143 C CB  . ASP A 286 ? 2.02127 2.43905 2.31579 -0.22336 0.24034  -0.08039 280 ASP A CB  
2144 C CG  . ASP A 286 ? 2.01896 2.47200 2.35151 -0.26643 0.25964  -0.07515 280 ASP A CG  
2145 O OD1 . ASP A 286 ? 1.91491 2.42053 2.31223 -0.27164 0.25253  -0.09112 280 ASP A OD1 
2146 O OD2 . ASP A 286 ? 2.03278 2.45951 2.32912 -0.29644 0.28074  -0.05450 280 ASP A OD2 
2147 N N   . LYS A 287 ? 1.77691 2.33551 2.10976 -0.22153 0.31346  -0.10311 281 LYS A N   
2148 C CA  . LYS A 287 ? 1.88265 2.47336 2.19492 -0.22796 0.35321  -0.10264 281 LYS A CA  
2149 C C   . LYS A 287 ? 2.13498 2.67251 2.38467 -0.26493 0.37169  -0.07291 281 LYS A C   
2150 O O   . LYS A 287 ? 1.93918 2.47602 2.14214 -0.26403 0.39907  -0.06872 281 LYS A O   
2151 C CB  . LYS A 287 ? 1.73049 2.42409 2.12033 -0.23893 0.37972  -0.12103 281 LYS A CB  
2152 C CG  . LYS A 287 ? 1.62764 2.37710 2.08174 -0.20061 0.35915  -0.15091 281 LYS A CG  
2153 C CD  . LYS A 287 ? 1.39645 2.12046 1.81134 -0.15044 0.34833  -0.16397 281 LYS A CD  
2154 C CE  . LYS A 287 ? 1.34508 2.09566 1.80839 -0.11212 0.31687  -0.18718 281 LYS A CE  
2155 N NZ  . LYS A 287 ? 1.16876 1.87258 1.63496 -0.11906 0.27945  -0.17761 281 LYS A NZ  
2156 N N   . ASN A 288 ? 2.34352 2.83286 2.58693 -0.29585 0.35624  -0.05271 282 ASN A N   
2157 C CA  . ASN A 288 ? 2.21012 2.63532 2.38640 -0.32749 0.36756  -0.02224 282 ASN A CA  
2158 C C   . ASN A 288 ? 2.17828 2.53428 2.27548 -0.30100 0.35404  -0.01321 282 ASN A C   
2159 O O   . ASN A 288 ? 2.06242 2.37833 2.09402 -0.31693 0.36985  0.00723  282 ASN A O   
2160 C CB  . ASN A 288 ? 1.82216 2.20053 2.00744 -0.35934 0.34686  -0.00515 282 ASN A CB  
2161 C CG  . ASN A 288 ? 1.78261 2.22558 2.04534 -0.39131 0.35796  -0.01361 282 ASN A CG  
2162 O OD1 . ASN A 288 ? 1.75433 2.27100 2.05091 -0.40683 0.39277  -0.02087 282 ASN A OD1 
2163 N ND2 . ASN A 288 ? 1.74542 2.16343 2.03789 -0.40131 0.32820  -0.01431 282 ASN A ND2 
2164 N N   . ASP A 289 ? 2.10394 2.44467 2.20494 -0.26234 0.32416  -0.02755 283 ASP A N   
2165 C CA  . ASP A 289 ? 1.87994 2.16671 1.91735 -0.23508 0.30975  -0.02415 283 ASP A CA  
2166 C C   . ASP A 289 ? 1.83453 2.16650 1.88760 -0.19824 0.31537  -0.05087 283 ASP A C   
2167 O O   . ASP A 289 ? 1.67766 2.01468 1.75967 -0.17027 0.29108  -0.06638 283 ASP A O   
2168 C CB  . ASP A 289 ? 1.71628 1.94263 1.74336 -0.22376 0.27004  -0.01694 283 ASP A CB  
2169 C CG  . ASP A 289 ? 1.80548 1.98032 1.77289 -0.19962 0.25392  -0.01305 283 ASP A CG  
2170 O OD1 . ASP A 289 ? 1.74442 1.87560 1.65148 -0.21209 0.25930  0.00570  283 ASP A OD1 
2171 O OD2 . ASP A 289 ? 2.01290 2.18964 1.99250 -0.16941 0.23476  -0.02824 283 ASP A OD2 
2172 N N   . VAL A 290 ? 2.00939 2.37151 2.03963 -0.19800 0.34805  -0.05621 284 VAL A N   
2173 C CA  . VAL A 290 ? 1.91178 2.31474 1.95423 -0.16119 0.35504  -0.08370 284 VAL A CA  
2174 C C   . VAL A 290 ? 1.97157 2.31638 1.96952 -0.12875 0.32524  -0.08785 284 VAL A C   
2175 O O   . VAL A 290 ? 1.99245 2.35498 2.00964 -0.09492 0.31537  -0.11019 284 VAL A O   
2176 C CB  . VAL A 290 ? 1.75426 2.19793 1.77357 -0.16752 0.39858  -0.08913 284 VAL A CB  
2177 C CG1 . VAL A 290 ? 1.73985 2.25418 1.81633 -0.20076 0.42994  -0.08761 284 VAL A CG1 
2178 C CG2 . VAL A 290 ? 1.61173 1.99021 1.53906 -0.18128 0.40555  -0.06715 284 VAL A CG2 
2179 N N   . TYR A 291 ? 1.89657 2.17077 1.83623 -0.13879 0.30883  -0.06646 285 TYR A N   
2180 C CA  . TYR A 291 ? 1.57296 1.79454 1.47210 -0.11289 0.28082  -0.06946 285 TYR A CA  
2181 C C   . TYR A 291 ? 1.66686 1.88775 1.61017 -0.09202 0.25053  -0.07999 285 TYR A C   
2182 O O   . TYR A 291 ? 1.83020 2.02276 1.75301 -0.06760 0.23121  -0.08855 285 TYR A O   
2183 C CB  . TYR A 291 ? 1.75549 1.90910 1.59463 -0.12952 0.26636  -0.04399 285 TYR A CB  
2184 C CG  . TYR A 291 ? 1.93714 2.08267 1.72404 -0.15331 0.29446  -0.02882 285 TYR A CG  
2185 C CD1 . TYR A 291 ? 1.85309 1.98331 1.57740 -0.14205 0.30579  -0.03419 285 TYR A CD1 
2186 C CD2 . TYR A 291 ? 1.95578 2.10541 1.75162 -0.18820 0.30955  -0.00897 285 TYR A CD2 
2187 C CE1 . TYR A 291 ? 1.85623 1.97736 1.52506 -0.16402 0.33278  -0.01936 285 TYR A CE1 
2188 C CE2 . TYR A 291 ? 1.62513 1.76350 1.36751 -0.21260 0.33668  0.00780  285 TYR A CE2 
2189 C CZ  . TYR A 291 ? 1.83087 1.95614 1.50835 -0.19995 0.34897  0.00293  285 TYR A CZ  
2190 O OH  . TYR A 291 ? 1.82990 1.94207 1.44652 -0.22446 0.37712  0.02064  285 TYR A OH  
2191 N N   . SER A 292 ? 1.73720 1.98594 1.73721 -0.10270 0.24552  -0.07922 286 SER A N   
2192 C CA  . SER A 292 ? 1.58038 1.83512 1.62016 -0.08150 0.22020  -0.09114 286 SER A CA  
2193 C C   . SER A 292 ? 1.62670 1.92877 1.69692 -0.05324 0.22711  -0.11658 286 SER A C   
2194 O O   . SER A 292 ? 1.68819 1.97743 1.76467 -0.02744 0.20526  -0.12682 286 SER A O   
2195 C CB  . SER A 292 ? 1.48706 1.75541 1.57308 -0.10038 0.21129  -0.08476 286 SER A CB  
2196 O OG  . SER A 292 ? 1.47407 1.68890 1.53178 -0.11733 0.19678  -0.06416 286 SER A OG  
2197 N N   . MET A 293 ? 1.78163 2.13794 1.87015 -0.05714 0.25747  -0.12687 287 MET A N   
2198 C CA  . MET A 293 ? 1.89283 2.29759 2.01256 -0.02598 0.26425  -0.15352 287 MET A CA  
2199 C C   . MET A 293 ? 1.82312 2.18849 1.89104 0.00357  0.25805  -0.16388 287 MET A C   
2200 O O   . MET A 293 ? 1.80418 2.16869 1.88514 0.03557  0.24120  -0.18086 287 MET A O   
2201 C CB  . MET A 293 ? 1.92478 2.40319 2.07826 -0.03801 0.30168  -0.16296 287 MET A CB  
2202 C CG  . MET A 293 ? 1.85454 2.37255 2.06039 -0.07280 0.30913  -0.15298 287 MET A CG  
2203 S SD  . MET A 293 ? 2.26227 2.81745 2.54508 -0.05752 0.27941  -0.16776 287 MET A SD  
2204 C CE  . MET A 293 ? 1.50863 2.13404 1.83112 -0.01543 0.29079  -0.20155 287 MET A CE  
2205 N N   . ALA A 294 ? 1.66885 1.99712 1.67452 -0.00692 0.26949  -0.15390 288 ALA A N   
2206 C CA  . ALA A 294 ? 1.49841 1.78370 1.45059 0.01832  0.26097  -0.16457 288 ALA A CA  
2207 C C   . ALA A 294 ? 1.52234 1.75173 1.46380 0.02987  0.22287  -0.15969 288 ALA A C   
2208 O O   . ALA A 294 ? 1.69235 1.90216 1.62349 0.05830  0.20876  -0.17559 288 ALA A O   
2209 C CB  . ALA A 294 ? 1.44999 1.70335 1.33374 0.00171  0.27685  -0.15297 288 ALA A CB  
2210 N N   . THR A 295 ? 1.34963 1.55177 1.29263 0.00782  0.20647  -0.13797 289 THR A N   
2211 C CA  . THR A 295 ? 1.36391 1.52473 1.30622 0.01622  0.17403  -0.13314 289 THR A CA  
2212 C C   . THR A 295 ? 1.50235 1.68901 1.49192 0.03756  0.16272  -0.14711 289 THR A C   
2213 O O   . THR A 295 ? 1.53380 1.68761 1.51283 0.05549  0.14102  -0.15154 289 THR A O   
2214 C CB  . THR A 295 ? 1.40650 1.54482 1.34985 -0.00932 0.16225  -0.11005 289 THR A CB  
2215 O OG1 . THR A 295 ? 1.45612 1.56325 1.34987 -0.02559 0.16772  -0.09635 289 THR A OG1 
2216 C CG2 . THR A 295 ? 1.42938 1.53382 1.37593 -0.00157 0.13282  -0.10578 289 THR A CG2 
2217 N N   . ALA A 296 ? 1.63934 1.88363 1.67984 0.03504  0.17605  -0.15379 290 ALA A N   
2218 C CA  . ALA A 296 ? 1.65435 1.92657 1.73900 0.05802  0.16335  -0.16849 290 ALA A CA  
2219 C C   . ALA A 296 ? 1.51523 1.79390 1.59212 0.09238  0.16621  -0.19130 290 ALA A C   
2220 O O   . ALA A 296 ? 1.54745 1.80158 1.62256 0.11717  0.14383  -0.19884 290 ALA A O   
2221 C CB  . ALA A 296 ? 1.77026 2.10631 1.91454 0.04474  0.17474  -0.17120 290 ALA A CB  
2222 N N   . ARG A 297 ? 1.50010 1.80878 1.56891 0.09486  0.19398  -0.20261 291 ARG A N   
2223 C CA  . ARG A 297 ? 1.63373 1.94812 1.69306 0.13080  0.19813  -0.22765 291 ARG A CA  
2224 C C   . ARG A 297 ? 1.77022 2.00730 1.76971 0.14511  0.17704  -0.22775 291 ARG A C   
2225 O O   . ARG A 297 ? 1.90148 2.12219 1.89486 0.17845  0.16507  -0.24624 291 ARG A O   
2226 C CB  . ARG A 297 ? 1.48353 1.84558 1.53983 0.12838  0.23597  -0.23956 291 ARG A CB  
2227 C CG  . ARG A 297 ? 1.34082 1.79061 1.46627 0.11884  0.25859  -0.24582 291 ARG A CG  
2228 C CD  . ARG A 297 ? 1.50997 2.01524 1.63781 0.12686  0.29719  -0.26471 291 ARG A CD  
2229 N NE  . ARG A 297 ? 1.68615 2.17272 1.76092 0.09632  0.32246  -0.24874 291 ARG A NE  
2230 C CZ  . ARG A 297 ? 1.63271 2.16087 1.72524 0.05981  0.35011  -0.23468 291 ARG A CZ  
2231 N NH1 . ARG A 297 ? 1.48832 2.08334 1.65503 0.04670  0.35688  -0.23598 291 ARG A NH1 
2232 N NH2 . ARG A 297 ? 1.56879 2.06802 1.60107 0.03478  0.36987  -0.21853 291 ARG A NH2 
2233 N N   . SER A 298 ? 1.65532 1.84327 1.61145 0.12054  0.17039  -0.20793 292 SER A N   
2234 C CA  . SER A 298 ? 1.50271 1.61949 1.40992 0.12887  0.14644  -0.20656 292 SER A CA  
2235 C C   . SER A 298 ? 1.40088 1.49196 1.32674 0.13760  0.11725  -0.20141 292 SER A C   
2236 O O   . SER A 298 ? 1.55074 1.59956 1.45454 0.15907  0.09932  -0.21101 292 SER A O   
2237 C CB  . SER A 298 ? 1.61282 1.69156 1.47704 0.10020  0.14413  -0.18679 292 SER A CB  
2238 O OG  . SER A 298 ? 1.40777 1.49030 1.23309 0.09733  0.16622  -0.19313 292 SER A OG  
2239 N N   . LEU A 299 ? 1.43602 1.54822 1.39822 0.12065  0.11210  -0.18624 293 LEU A N   
2240 C CA  . LEU A 299 ? 1.50505 1.59677 1.48175 0.12863  0.08709  -0.18102 293 LEU A CA  
2241 C C   . LEU A 299 ? 1.61151 1.73167 1.62005 0.16011  0.08240  -0.19941 293 LEU A C   
2242 O O   . LEU A 299 ? 1.40815 1.49459 1.40968 0.17684  0.05963  -0.19975 293 LEU A O   
2243 C CB  . LEU A 299 ? 1.19987 1.30535 1.20162 0.10318  0.08339  -0.16202 293 LEU A CB  
2244 C CG  . LEU A 299 ? 1.32193 1.39545 1.29555 0.07615  0.08166  -0.14318 293 LEU A CG  
2245 C CD1 . LEU A 299 ? 1.42505 1.51756 1.42709 0.05522  0.08071  -0.12867 293 LEU A CD1 
2246 C CD2 . LEU A 299 ? 1.12615 1.14252 1.06524 0.07887  0.06097  -0.13790 293 LEU A CD2 
2247 N N   . ASP A 300 ? 1.87554 2.05802 1.91920 0.16835  0.10322  -0.21433 294 ASP A N   
2248 C CA  . ASP A 300 ? 1.95235 2.17082 2.03351 0.20130  0.09753  -0.23426 294 ASP A CA  
2249 C C   . ASP A 300 ? 1.96521 2.14155 2.01302 0.23670  0.08680  -0.25174 294 ASP A C   
2250 O O   . ASP A 300 ? 2.16975 2.32857 2.22400 0.26412  0.06395  -0.25865 294 ASP A O   
2251 C CB  . ASP A 300 ? 1.93065 2.23307 2.06159 0.19953  0.12527  -0.24759 294 ASP A CB  
2252 C CG  . ASP A 300 ? 2.04925 2.40322 2.23404 0.23088  0.11655  -0.26741 294 ASP A CG  
2253 O OD1 . ASP A 300 ? 2.32751 2.64886 2.50904 0.25141  0.08677  -0.26704 294 ASP A OD1 
2254 O OD2 . ASP A 300 ? 1.75399 2.18256 1.98452 0.23460  0.13926  -0.28303 294 ASP A OD2 
2255 N N   . GLU A 301 ? 1.65557 1.80963 1.66281 0.23715  0.10105  -0.25916 295 GLU A N   
2256 C CA  . GLU A 301 ? 1.49350 1.60623 1.46747 0.27222  0.09172  -0.27982 295 GLU A CA  
2257 C C   . GLU A 301 ? 1.62077 1.64678 1.55168 0.27296  0.05978  -0.26824 295 GLU A C   
2258 O O   . GLU A 301 ? 1.66674 1.65149 1.57864 0.30481  0.04219  -0.28265 295 GLU A O   
2259 C CB  . GLU A 301 ? 1.49391 1.60638 1.43162 0.27153  0.11613  -0.29259 295 GLU A CB  
2260 C CG  . GLU A 301 ? 2.10891 2.30795 2.08573 0.27372  0.15164  -0.30671 295 GLU A CG  
2261 C CD  . GLU A 301 ? 2.25882 2.45461 2.19306 0.28398  0.17532  -0.32529 295 GLU A CD  
2262 O OE1 . GLU A 301 ? 2.20754 2.33154 2.08399 0.29484  0.15980  -0.33114 295 GLU A OE1 
2263 O OE2 . GLU A 301 ? 2.10833 2.37251 2.06494 0.27974  0.20965  -0.33425 295 GLU A OE2 
2264 N N   . LEU A 302 ? 1.54093 1.53822 1.45689 0.23842  0.05195  -0.24267 296 LEU A N   
2265 C CA  . LEU A 302 ? 1.49759 1.42049 1.37871 0.23392  0.02438  -0.22978 296 LEU A CA  
2266 C C   . LEU A 302 ? 1.62279 1.53927 1.52473 0.24771  0.00343  -0.22373 296 LEU A C   
2267 O O   . LEU A 302 ? 1.62754 1.48271 1.50025 0.24292  -0.01819 -0.21109 296 LEU A O   
2268 C CB  . LEU A 302 ? 1.32811 1.23197 1.19283 0.19392  0.02411  -0.20598 296 LEU A CB  
2269 C CG  . LEU A 302 ? 1.41358 1.31462 1.24909 0.17878  0.03954  -0.20874 296 LEU A CG  
2270 C CD1 . LEU A 302 ? 1.21504 1.10503 1.04336 0.14246  0.03624  -0.18505 296 LEU A CD1 
2271 C CD2 . LEU A 302 ? 1.35206 1.19652 1.13877 0.19645  0.03000  -0.22582 296 LEU A CD2 
2272 N N   . CYS A 303 ? 1.86128 1.83894 1.81123 0.26332  0.00866  -0.23204 297 CYS A N   
2273 C CA  . CYS A 303 ? 1.78025 1.75507 1.74803 0.27846  -0.01326 -0.22728 297 CYS A CA  
2274 C C   . CYS A 303 ? 1.91901 1.87053 1.88011 0.32372  -0.03074 -0.24700 297 CYS A C   
2275 O O   . CYS A 303 ? 1.96514 1.90185 1.93083 0.34019  -0.05371 -0.24247 297 CYS A O   
2276 C CB  . CYS A 303 ? 1.70077 1.75399 1.72597 0.27074  -0.00345 -0.22656 297 CYS A CB  
2277 S SG  . CYS A 303 ? 1.87029 1.94425 1.90390 0.22126  0.01238  -0.20342 297 CYS A SG  
2278 N N   . VAL A 304 ? 1.86357 1.80854 1.81041 0.34602  -0.02168 -0.26922 298 VAL A N   
2279 C CA  . VAL A 304 ? 1.99285 1.92080 1.93812 0.39459  -0.03769 -0.29209 298 VAL A CA  
2280 C C   . VAL A 304 ? 2.16346 1.98542 2.04589 0.40467  -0.06408 -0.28796 298 VAL A C   
2281 O O   . VAL A 304 ? 2.38850 2.17444 2.26208 0.44137  -0.08839 -0.29698 298 VAL A O   
2282 C CB  . VAL A 304 ? 1.93559 1.91980 1.90322 0.41916  -0.01245 -0.32294 298 VAL A CB  
2283 C CG1 . VAL A 304 ? 1.73095 1.81936 1.76181 0.40311  0.01485  -0.32452 298 VAL A CG1 
2284 C CG2 . VAL A 304 ? 1.84469 1.78697 1.76164 0.40720  0.00143  -0.32823 298 VAL A CG2 
2285 N N   . GLN A 305 ? 2.02287 1.79222 1.86170 0.37251  -0.06187 -0.27437 299 GLN A N   
2286 C CA  . GLN A 305 ? 2.13263 1.80015 1.91355 0.37451  -0.08716 -0.26869 299 GLN A CA  
2287 C C   . GLN A 305 ? 1.99087 1.62058 1.75052 0.32858  -0.09413 -0.23634 299 GLN A C   
2288 O O   . GLN A 305 ? 1.99941 1.55615 1.72450 0.32516  -0.11777 -0.22219 299 GLN A O   
2289 C CB  . GLN A 305 ? 2.10915 1.73985 1.85244 0.38575  -0.08166 -0.29113 299 GLN A CB  
2290 C CG  . GLN A 305 ? 2.12930 1.77395 1.88107 0.43917  -0.08096 -0.32586 299 GLN A CG  
2291 C CD  . GLN A 305 ? 2.34943 1.94397 2.05322 0.45212  -0.07873 -0.34945 299 GLN A CD  
2292 O OE1 . GLN A 305 ? 2.21409 1.78021 1.88465 0.41849  -0.07329 -0.34116 299 GLN A OE1 
2293 N NE2 . GLN A 305 ? 2.40448 1.99242 2.10697 0.49746  -0.08407 -0.37640 299 GLN A NE2 
2294 N N   . ASN A 306 ? 1.90423 1.58208 1.68362 0.29330  -0.07349 -0.22441 300 ASN A N   
2295 C CA  . ASN A 306 ? 1.85367 1.51152 1.62429 0.25316  -0.07816 -0.19555 300 ASN A CA  
2296 C C   . ASN A 306 ? 1.67213 1.36775 1.47521 0.25089  -0.08082 -0.18078 300 ASN A C   
2297 O O   . ASN A 306 ? 1.49100 1.24401 1.33223 0.27234  -0.07497 -0.19228 300 ASN A O   
2298 C CB  . ASN A 306 ? 1.50577 1.19313 1.28105 0.21938  -0.05888 -0.18946 300 ASN A CB  
2299 C CG  . ASN A 306 ? 1.71508 1.37648 1.45849 0.22434  -0.05448 -0.20760 300 ASN A CG  
2300 O OD1 . ASN A 306 ? 1.79931 1.50515 1.55453 0.23807  -0.03541 -0.22555 300 ASN A OD1 
2301 N ND2 . ASN A 306 ? 1.81995 1.40920 1.52112 0.21166  -0.07180 -0.20334 300 ASN A ND2 
2302 N N   . ASP A 307 ? 1.48192 1.14655 1.26966 0.22400  -0.08979 -0.15610 301 ASP A N   
2303 C CA  . ASP A 307 ? 1.44934 1.13939 1.25657 0.22114  -0.09421 -0.14163 301 ASP A CA  
2304 C C   . ASP A 307 ? 1.47223 1.23159 1.31831 0.19645  -0.07378 -0.13552 301 ASP A C   
2305 O O   . ASP A 307 ? 1.38859 1.14968 1.23464 0.17024  -0.07202 -0.11660 301 ASP A O   
2306 C CB  . ASP A 307 ? 1.81422 1.43895 1.58276 0.20465  -0.11071 -0.11839 301 ASP A CB  
2307 C CG  . ASP A 307 ? 1.85823 1.46827 1.61897 0.22745  -0.12906 -0.11270 301 ASP A CG  
2308 O OD1 . ASP A 307 ? 1.75574 1.42435 1.55269 0.24451  -0.12671 -0.12143 301 ASP A OD1 
2309 O OD2 . ASP A 307 ? 2.02660 1.56467 1.74334 0.22714  -0.14712 -0.09901 301 ASP A OD2 
2310 N N   . LEU A 308 ? 1.22882 1.04489 1.10742 0.20556  -0.05744 -0.15251 302 LEU A N   
2311 C CA  . LEU A 308 ? 1.22787 1.10656 1.14310 0.18472  -0.03878 -0.14871 302 LEU A CA  
2312 C C   . LEU A 308 ? 1.32548 1.26259 1.28375 0.20341  -0.03767 -0.15962 302 LEU A C   
2313 O O   . LEU A 308 ? 1.52350 1.47118 1.49205 0.23506  -0.04300 -0.17747 302 LEU A O   
2314 C CB  . LEU A 308 ? 1.23652 1.13334 1.15220 0.17335  -0.01925 -0.15653 302 LEU A CB  
2315 C CG  . LEU A 308 ? 1.16615 1.11529 1.11107 0.14890  -0.00035 -0.15025 302 LEU A CG  
2316 C CD1 . LEU A 308 ? 1.00402 0.93920 0.94462 0.12174  -0.00522 -0.12912 302 LEU A CD1 
2317 C CD2 . LEU A 308 ? 1.32826 1.28477 1.26151 0.14118  0.01675  -0.15733 302 LEU A CD2 
2318 N N   . SER A 309 ? 1.20313 1.17833 1.18801 0.18477  -0.03246 -0.15042 303 SER A N   
2319 C CA  . SER A 309 ? 1.15626 1.18952 1.18535 0.19674  -0.03316 -0.16065 303 SER A CA  
2320 C C   . SER A 309 ? 1.05672 1.13464 1.11519 0.16787  -0.01656 -0.15504 303 SER A C   
2321 O O   . SER A 309 ? 1.14817 1.20514 1.19019 0.14330  -0.01397 -0.13907 303 SER A O   
2322 C CB  . SER A 309 ? 1.16437 1.17967 1.18548 0.21145  -0.05732 -0.15515 303 SER A CB  
2323 O OG  . SER A 309 ? 1.19453 1.15899 1.18340 0.23843  -0.07519 -0.15823 303 SER A OG  
2324 N N   . VAL A 310 ? 0.84566 0.98499 0.94893 0.17085  -0.00569 -0.16862 304 VAL A N   
2325 C CA  . VAL A 310 ? 0.86726 1.04527 0.99791 0.14252  0.01056  -0.16416 304 VAL A CA  
2326 C C   . VAL A 310 ? 0.92962 1.16456 1.10984 0.14700  0.00562  -0.17504 304 VAL A C   
2327 O O   . VAL A 310 ? 1.04779 1.32316 1.25919 0.16811  0.00598  -0.19250 304 VAL A O   
2328 C CB  . VAL A 310 ? 0.88922 1.08406 1.02106 0.13073  0.03565  -0.16781 304 VAL A CB  
2329 C CG1 . VAL A 310 ? 0.81285 1.04537 0.97328 0.10203  0.05086  -0.16256 304 VAL A CG1 
2330 C CG2 . VAL A 310 ? 0.94886 1.08746 1.03134 0.12296  0.03714  -0.15714 304 VAL A CG2 
2331 N N   . LYS A 311 ? 0.88474 1.12464 1.07399 0.12793  0.00016  -0.16662 305 LYS A N   
2332 C CA  . LYS A 311 ? 0.76178 1.05474 0.99857 0.12417  -0.00462 -0.17672 305 LYS A CA  
2333 C C   . LYS A 311 ? 0.70026 1.00604 0.95085 0.08968  0.01018  -0.16910 305 LYS A C   
2334 O O   . LYS A 311 ? 0.80348 1.06995 1.02225 0.07312  0.01586  -0.15422 305 LYS A O   
2335 C CB  . LYS A 311 ? 0.67269 0.95302 0.90238 0.13816  -0.03221 -0.17679 305 LYS A CB  
2336 C CG  . LYS A 311 ? 0.92297 1.19114 1.14156 0.17438  -0.05130 -0.18461 305 LYS A CG  
2337 C CD  . LYS A 311 ? 0.77948 1.04066 0.99127 0.18756  -0.07967 -0.18494 305 LYS A CD  
2338 C CE  . LYS A 311 ? 0.93694 1.18814 1.14102 0.22634  -0.10169 -0.19353 305 LYS A CE  
2339 N NZ  . LYS A 311 ? 0.94770 1.19804 1.14657 0.24110  -0.13185 -0.19533 305 LYS A NZ  
2340 N N   . VAL A 312 ? 0.66261 1.02314 0.96227 0.07875  0.01516  -0.17961 306 VAL A N   
2341 C CA  . VAL A 312 ? 0.78981 1.15957 1.10342 0.04474  0.02879  -0.17271 306 VAL A CA  
2342 C C   . VAL A 312 ? 0.81709 1.20835 1.16090 0.03568  0.01175  -0.17942 306 VAL A C   
2343 O O   . VAL A 312 ? 0.68074 1.10605 1.05362 0.05292  -0.00499 -0.19385 306 VAL A O   
2344 C CB  . VAL A 312 ? 0.67795 1.08998 1.01931 0.03013  0.05591  -0.17689 306 VAL A CB  
2345 C CG1 . VAL A 312 ? 0.76709 1.15076 1.06925 0.03737  0.07213  -0.17058 306 VAL A CG1 
2346 C CG2 . VAL A 312 ? 0.73661 1.21772 1.13378 0.04390  0.05504  -0.19737 306 VAL A CG2 
2347 N N   . PHE A 313 ? 0.72030 1.08908 1.05560 0.00987  0.01379  -0.17001 307 PHE A N   
2348 C CA  . PHE A 313 ? 0.67377 1.05744 1.03500 -0.00362 -0.00099 -0.17748 307 PHE A CA  
2349 C C   . PHE A 313 ? 0.62685 1.02363 1.01224 -0.03887 0.01540  -0.17385 307 PHE A C   
2350 O O   . PHE A 313 ? 0.80680 1.17946 1.17029 -0.05332 0.03470  -0.15995 307 PHE A O   
2351 C CB  . PHE A 313 ? 0.73857 1.07350 1.06099 0.00100  -0.01849 -0.17164 307 PHE A CB  
2352 C CG  . PHE A 313 ? 0.63444 0.92065 0.91883 -0.01106 -0.00670 -0.15485 307 PHE A CG  
2353 C CD1 . PHE A 313 ? 0.71730 0.99003 1.00628 -0.03663 -0.00114 -0.15024 307 PHE A CD1 
2354 C CD2 . PHE A 313 ? 0.72016 0.97267 0.96516 0.00344  -0.00363 -0.14413 307 PHE A CD2 
2355 C CE1 . PHE A 313 ? 0.61278 0.84219 0.86895 -0.04370 0.00644  -0.13582 307 PHE A CE1 
2356 C CE2 . PHE A 313 ? 0.69553 0.91004 0.91171 -0.00658 0.00469  -0.13028 307 PHE A CE2 
2357 C CZ  . PHE A 313 ? 0.63642 0.84067 0.85869 -0.02822 0.00918  -0.12644 307 PHE A CZ  
2358 N N   . THR A 314 ? 0.56404 0.99663 0.99279 -0.05367 0.00578  -0.18604 308 THR A N   
2359 C CA  . THR A 314 ? 0.56691 1.00650 1.01869 -0.09119 0.01793  -0.18231 308 THR A CA  
2360 C C   . THR A 314 ? 0.73445 1.13761 1.17646 -0.10587 -0.00086 -0.18330 308 THR A C   
2361 O O   . THR A 314 ? 0.76304 1.15396 1.21372 -0.13762 0.00661  -0.17771 308 THR A O   
2362 C CB  . THR A 314 ? 0.59265 1.10738 1.11000 -0.10433 0.02506  -0.19645 308 THR A CB  
2363 O OG1 . THR A 314 ? 0.64700 1.19543 1.19611 -0.08789 -0.00285 -0.21576 308 THR A OG1 
2364 C CG2 . THR A 314 ? 0.58762 1.13930 1.11414 -0.09091 0.04878  -0.19679 308 THR A CG2 
2365 N N   . ILE A 315 ? 0.69588 1.07825 1.11645 -0.08357 -0.02477 -0.19038 309 ILE A N   
2366 C CA  . ILE A 315 ? 0.65439 1.00065 1.06053 -0.09333 -0.04243 -0.19446 309 ILE A CA  
2367 C C   . ILE A 315 ? 0.69595 0.98282 1.06031 -0.10209 -0.03135 -0.17768 309 ILE A C   
2368 O O   . ILE A 315 ? 0.67100 0.93963 1.00800 -0.09305 -0.01616 -0.16328 309 ILE A O   
2369 C CB  . ILE A 315 ? 0.56800 0.90655 0.95317 -0.06517 -0.06801 -0.20560 309 ILE A CB  
2370 C CG1 . ILE A 315 ? 0.62475 0.93880 0.96646 -0.03752 -0.06212 -0.19387 309 ILE A CG1 
2371 C CG2 . ILE A 315 ? 0.52615 0.92050 0.95470 -0.05775 -0.08653 -0.22438 309 ILE A CG2 
2372 C CD1 . ILE A 315 ? 0.59869 0.89308 0.90651 -0.01343 -0.08313 -0.19942 309 ILE A CD1 
2373 N N   . GLN A 316 ? 0.58579 0.84104 0.94566 -0.11879 -0.04158 -0.18111 310 GLN A N   
2374 C CA  . GLN A 316 ? 0.54435 0.74090 0.86379 -0.11918 -0.03819 -0.16931 310 GLN A CA  
2375 C C   . GLN A 316 ? 0.59392 0.77187 0.87587 -0.08780 -0.04474 -0.16917 310 GLN A C   
2376 O O   . GLN A 316 ? 0.86296 1.04157 1.13750 -0.07405 -0.06251 -0.18294 310 GLN A O   
2377 C CB  . GLN A 316 ? 0.73004 0.89366 1.05169 -0.13873 -0.05171 -0.17714 310 GLN A CB  
2378 C CG  . GLN A 316 ? 0.59338 0.76170 0.94484 -0.17618 -0.04282 -0.17200 310 GLN A CG  
2379 C CD  . GLN A 316 ? 1.09418 1.22574 1.44826 -0.19602 -0.06069 -0.18233 310 GLN A CD  
2380 O OE1 . GLN A 316 ? 1.09275 1.22473 1.44832 -0.18595 -0.08283 -0.20200 310 GLN A OE1 
2381 N NE2 . GLN A 316 ? 1.30573 1.40006 1.65549 -0.22415 -0.05249 -0.16914 310 GLN A NE2 
2382 N N   . ASN A 317 ? 0.67892 0.84075 0.93569 -0.07788 -0.03061 -0.15366 311 ASN A N   
2383 C CA  . ASN A 317 ? 0.75082 0.90008 0.97568 -0.05232 -0.03360 -0.15136 311 ASN A CA  
2384 C C   . ASN A 317 ? 0.74078 0.85681 0.94004 -0.05127 -0.02234 -0.13592 311 ASN A C   
2385 O O   . ASN A 317 ? 0.77982 0.89733 0.97879 -0.05757 -0.00890 -0.12353 311 ASN A O   
2386 C CB  . ASN A 317 ? 0.57157 0.75141 0.79999 -0.03645 -0.03192 -0.15131 311 ASN A CB  
2387 C CG  . ASN A 317 ? 0.72298 0.88526 0.91578 -0.01450 -0.03444 -0.14630 311 ASN A CG  
2388 O OD1 . ASN A 317 ? 0.94243 1.08219 1.11280 -0.00873 -0.04011 -0.14824 311 ASN A OD1 
2389 N ND2 . ASN A 317 ? 0.65351 0.82527 0.84013 -0.00267 -0.02947 -0.14030 311 ASN A ND2 
2390 N N   . ASN A 318 ? 0.79516 0.88376 0.97325 -0.04211 -0.02840 -0.13815 312 ASN A N   
2391 C CA  . ASN A 318 ? 0.72232 0.78473 0.88121 -0.03794 -0.02102 -0.12598 312 ASN A CA  
2392 C C   . ASN A 318 ? 0.72353 0.79161 0.86317 -0.02066 -0.01638 -0.12008 312 ASN A C   
2393 O O   . ASN A 318 ? 0.83827 0.89151 0.96625 -0.01641 -0.01159 -0.11151 312 ASN A O   
2394 C CB  . ASN A 318 ? 0.67687 0.70860 0.82802 -0.03621 -0.02928 -0.13317 312 ASN A CB  
2395 C CG  . ASN A 318 ? 0.69174 0.70373 0.85673 -0.05697 -0.03398 -0.13479 312 ASN A CG  
2396 O OD1 . ASN A 318 ? 1.02527 1.04300 1.20204 -0.07487 -0.02604 -0.12459 312 ASN A OD1 
2397 N ND2 . ASN A 318 ? 0.89892 0.88515 1.05989 -0.05547 -0.04626 -0.14781 312 ASN A ND2 
2398 N N   . THR A 319 ? 0.76991 0.85798 0.90650 -0.01131 -0.01910 -0.12408 313 THR A N   
2399 C CA  . THR A 319 ? 0.69440 0.78164 0.80877 0.00213  -0.01562 -0.11743 313 THR A CA  
2400 C C   . THR A 319 ? 0.80447 0.88570 0.91494 -0.00144 -0.00520 -0.10281 313 THR A C   
2401 O O   . THR A 319 ? 0.80381 0.89158 0.92407 -0.00840 -0.00072 -0.09892 313 THR A O   
2402 C CB  . THR A 319 ? 0.69954 0.80245 0.80891 0.01213  -0.02276 -0.12212 313 THR A CB  
2403 O OG1 . THR A 319 ? 0.78074 0.89077 0.89441 0.01465  -0.03594 -0.13717 313 THR A OG1 
2404 C CG2 . THR A 319 ? 0.80711 0.90046 0.88682 0.02347  -0.02021 -0.11388 313 THR A CG2 
2405 N N   . LYS A 320 ? 0.79797 0.86914 0.89459 0.00304  -0.00123 -0.09603 314 LYS A N   
2406 C CA  . LYS A 320 ? 0.79321 0.85857 0.88409 0.00007  0.00514  -0.08345 314 LYS A CA  
2407 C C   . LYS A 320 ? 0.86438 0.93016 0.93800 0.00687  0.00720  -0.07890 314 LYS A C   
2408 O O   . LYS A 320 ? 0.88780 0.95473 0.95845 0.00936  0.01016  -0.07837 314 LYS A O   
2409 C CB  . LYS A 320 ? 0.73240 0.78638 0.82924 -0.00495 0.00616  -0.07862 314 LYS A CB  
2410 C CG  . LYS A 320 ? 0.66992 0.71471 0.77736 -0.01450 0.00411  -0.08023 314 LYS A CG  
2411 C CD  . LYS A 320 ? 0.89047 0.93970 0.99868 -0.02377 0.00952  -0.07494 314 LYS A CD  
2412 C CE  . LYS A 320 ? 0.77818 0.81633 0.89306 -0.03791 0.01079  -0.07242 314 LYS A CE  
2413 N NZ  . LYS A 320 ? 0.77970 0.81870 0.90908 -0.04209 0.00503  -0.08331 314 LYS A NZ  
2414 N N   . LEU A 321 ? 0.77184 0.83631 0.83401 0.00985  0.00611  -0.07576 315 LEU A N   
2415 C CA  . LEU A 321 ? 0.75530 0.81330 0.79541 0.01420  0.00677  -0.06997 315 LEU A CA  
2416 C C   . LEU A 321 ? 0.87628 0.92060 0.90612 0.01099  0.00752  -0.06057 315 LEU A C   
2417 O O   . LEU A 321 ? 0.90484 0.94704 0.93812 0.01341  0.00490  -0.06308 315 LEU A O   
2418 C CB  . LEU A 321 ? 0.80717 0.86671 0.83396 0.02457  -0.00090 -0.07661 315 LEU A CB  
2419 C CG  . LEU A 321 ? 0.83255 0.87763 0.82736 0.02898  -0.00165 -0.06818 315 LEU A CG  
2420 C CD1 . LEU A 321 ? 0.88092 0.92859 0.86452 0.02430  0.00837  -0.06380 315 LEU A CD1 
2421 C CD2 . LEU A 321 ? 0.72729 0.77073 0.70732 0.04198  -0.01428 -0.07477 315 LEU A CD2 
2422 N N   . LEU A 322 ? 0.82558 0.86167 0.84347 0.00506  0.01152  -0.05103 316 LEU A N   
2423 C CA  . LEU A 322 ? 0.72513 0.74150 0.72899 -0.00000 0.01003  -0.04243 316 LEU A CA  
2424 C C   . LEU A 322 ? 0.78833 0.79185 0.76837 -0.00338 0.01191  -0.03312 316 LEU A C   
2425 O O   . LEU A 322 ? 0.97234 0.98940 0.95476 -0.00919 0.01992  -0.03004 316 LEU A O   
2426 C CB  . LEU A 322 ? 0.83136 0.84873 0.84786 -0.01102 0.01190  -0.03838 316 LEU A CB  
2427 C CG  . LEU A 322 ? 0.82822 0.82610 0.83150 -0.02134 0.00975  -0.02946 316 LEU A CG  
2428 C CD1 . LEU A 322 ? 0.76023 0.73095 0.74266 -0.01505 0.00316  -0.03091 316 LEU A CD1 
2429 C CD2 . LEU A 322 ? 0.90317 0.90789 0.92218 -0.03122 0.00826  -0.02766 316 LEU A CD2 
2430 N N   . ILE A 323 ? 0.83290 0.80942 0.78853 0.00078  0.00511  -0.02871 317 ILE A N   
2431 C CA  . ILE A 323 ? 0.90393 0.85767 0.82880 -0.00458 0.00575  -0.01659 317 ILE A CA  
2432 C C   . ILE A 323 ? 0.90830 0.82705 0.81744 -0.01152 -0.00028 -0.00907 317 ILE A C   
2433 O O   . ILE A 323 ? 1.04505 0.94873 0.95176 0.00002  -0.00936 -0.01588 317 ILE A O   
2434 C CB  . ILE A 323 ? 0.86738 0.81116 0.76692 0.01073  -0.00161 -0.01809 317 ILE A CB  
2435 C CG1 . ILE A 323 ? 0.94172 0.91745 0.85651 0.01812  0.00115  -0.02939 317 ILE A CG1 
2436 C CG2 . ILE A 323 ? 0.84521 0.76091 0.70527 0.00278  0.00056  -0.00225 317 ILE A CG2 
2437 C CD1 . ILE A 323 ? 0.89880 0.86835 0.79160 0.03448  -0.01046 -0.03425 317 ILE A CD1 
2438 N N   . VAL A 324 ? 1.02999 0.93683 0.92938 -0.03073 0.00509  0.00363  318 VAL A N   
2439 C CA  . VAL A 324 ? 0.95007 0.82035 0.83515 -0.04220 -0.00180 0.01045  318 VAL A CA  
2440 C C   . VAL A 324 ? 1.19344 1.02771 1.04144 -0.05333 -0.00170 0.02684  318 VAL A C   
2441 O O   . VAL A 324 ? 1.22685 1.07763 1.07538 -0.07030 0.01129  0.03701  318 VAL A O   
2442 C CB  . VAL A 324 ? 0.96308 0.85188 0.87582 -0.06106 0.00200  0.01067  318 VAL A CB  
2443 C CG1 . VAL A 324 ? 0.94250 0.79051 0.83708 -0.07778 -0.00618 0.01844  318 VAL A CG1 
2444 C CG2 . VAL A 324 ? 0.92871 0.83927 0.86645 -0.05017 -0.00082 -0.00291 318 VAL A CG2 
2445 N N   . ASP A 325 ? 1.14587 0.93038 0.96041 -0.04322 -0.01559 0.02943  319 ASP A N   
2446 C CA  . ASP A 325 ? 1.18643 0.91958 0.95791 -0.05545 -0.01954 0.04728  319 ASP A CA  
2447 C C   . ASP A 325 ? 1.24199 0.98221 0.99026 -0.05926 -0.00938 0.05977  319 ASP A C   
2448 O O   . ASP A 325 ? 1.53246 1.23939 1.24738 -0.07888 -0.00555 0.07871  319 ASP A O   
2449 C CB  . ASP A 325 ? 1.06083 0.77774 0.83628 -0.08688 -0.01663 0.05699  319 ASP A CB  
2450 C CG  . ASP A 325 ? 1.28179 0.96845 1.05901 -0.08273 -0.03163 0.04660  319 ASP A CG  
2451 O OD1 . ASP A 325 ? 1.49684 1.17667 1.27173 -0.05469 -0.04150 0.03239  319 ASP A OD1 
2452 O OD2 . ASP A 325 ? 1.34281 1.01461 1.12418 -0.10778 -0.03341 0.05145  319 ASP A OD2 
2453 N N   . ASP A 326 ? 1.18067 0.96089 0.94232 -0.04218 -0.00492 0.04960  320 ASP A N   
2454 C CA  . ASP A 326 ? 1.36486 1.15603 1.10252 -0.04377 0.00538  0.05783  320 ASP A CA  
2455 C C   . ASP A 326 ? 1.18485 0.99659 0.92815 -0.07411 0.02748  0.07063  320 ASP A C   
2456 O O   . ASP A 326 ? 1.35651 1.15381 1.06204 -0.08551 0.03729  0.08635  320 ASP A O   
2457 C CB  . ASP A 326 ? 1.39118 1.12805 1.07091 -0.03201 -0.00891 0.06963  320 ASP A CB  
2458 C CG  . ASP A 326 ? 1.62172 1.34699 1.30258 0.00081  -0.03154 0.05486  320 ASP A CG  
2459 O OD1 . ASP A 326 ? 1.55378 1.31318 1.27923 0.01094  -0.03302 0.03662  320 ASP A OD1 
2460 O OD2 . ASP A 326 ? 1.51933 1.20253 1.15667 0.01648  -0.04790 0.06176  320 ASP A OD2 
2461 N N   . GLU A 327 ? 1.21322 1.06038 1.00359 -0.08733 0.03533  0.06406  321 GLU A N   
2462 C CA  . GLU A 327 ? 1.10568 0.98766 0.91675 -0.11372 0.05598  0.07181  321 GLU A CA  
2463 C C   . GLU A 327 ? 1.11323 1.05675 0.97935 -0.10892 0.06433  0.05558  321 GLU A C   
2464 O O   . GLU A 327 ? 1.16238 1.14626 1.05194 -0.12464 0.08223  0.05815  321 GLU A O   
2465 C CB  . GLU A 327 ? 1.24625 1.10065 1.05786 -0.14271 0.05360  0.08488  321 GLU A CB  
2466 C CG  . GLU A 327 ? 1.58255 1.36740 1.33671 -0.15232 0.04549  0.10395  321 GLU A CG  
2467 C CD  . GLU A 327 ? 1.61274 1.36739 1.36921 -0.18409 0.04177  0.11538  321 GLU A CD  
2468 O OE1 . GLU A 327 ? 1.47583 1.26619 1.28019 -0.19607 0.04291  0.10650  321 GLU A OE1 
2469 O OE2 . GLU A 327 ? 1.85560 1.54768 1.56431 -0.19732 0.03559  0.13321  321 GLU A OE2 
2470 N N   . TYR A 328 ? 0.93859 0.89039 0.82589 -0.08783 0.05221  0.03936  322 TYR A N   
2471 C CA  . TYR A 328 ? 0.89106 0.88961 0.82518 -0.08225 0.05613  0.02542  322 TYR A CA  
2472 C C   . TYR A 328 ? 1.01655 1.01894 0.95348 -0.05678 0.04757  0.01049  322 TYR A C   
2473 O O   . TYR A 328 ? 1.01761 0.99142 0.93920 -0.04553 0.03400  0.00782  322 TYR A O   
2474 C CB  . TYR A 328 ? 0.83871 0.83841 0.80166 -0.09387 0.04784  0.02429  322 TYR A CB  
2475 C CG  . TYR A 328 ? 0.90150 0.93768 0.90556 -0.08450 0.04594  0.01097  322 TYR A CG  
2476 C CD1 . TYR A 328 ? 0.84133 0.92333 0.87958 -0.08942 0.05704  0.00811  322 TYR A CD1 
2477 C CD2 . TYR A 328 ? 0.94567 0.96970 0.95327 -0.07041 0.03318  0.00163  322 TYR A CD2 
2478 C CE1 . TYR A 328 ? 0.90984 1.01779 0.98182 -0.07856 0.05200  -0.00309 322 TYR A CE1 
2479 C CE2 . TYR A 328 ? 0.92399 0.97327 0.96209 -0.06339 0.03052  -0.00758 322 TYR A CE2 
2480 C CZ  . TYR A 328 ? 0.97710 1.06480 1.04587 -0.06660 0.03817  -0.00956 322 TYR A CZ  
2481 O OH  . TYR A 328 ? 1.01984 1.12570 1.11532 -0.05726 0.03236  -0.01788 322 TYR A OH  
2482 N N   . VAL A 329 ? 0.96586 1.00422 0.92404 -0.04789 0.05541  -0.00021 323 VAL A N   
2483 C CA  . VAL A 329 ? 0.84257 0.88604 0.80751 -0.02814 0.04756  -0.01480 323 VAL A CA  
2484 C C   . VAL A 329 ? 0.78306 0.85539 0.78803 -0.02562 0.04890  -0.02478 323 VAL A C   
2485 O O   . VAL A 329 ? 0.81139 0.91152 0.83608 -0.03088 0.05945  -0.02506 323 VAL A O   
2486 C CB  . VAL A 329 ? 0.83997 0.88594 0.77917 -0.01658 0.05126  -0.01962 323 VAL A CB  
2487 C CG1 . VAL A 329 ? 0.93337 1.00863 0.87578 -0.02166 0.06978  -0.01973 323 VAL A CG1 
2488 C CG2 . VAL A 329 ? 0.82028 0.87151 0.77066 0.00031  0.04081  -0.03589 323 VAL A CG2 
2489 N N   . HIS A 330 ? 0.93093 0.99688 0.94778 -0.01729 0.03820  -0.03267 324 HIS A N   
2490 C CA  . HIS A 330 ? 0.71600 0.79768 0.76346 -0.01473 0.03591  -0.03970 324 HIS A CA  
2491 C C   . HIS A 330 ? 0.84591 0.92551 0.89574 -0.00245 0.03052  -0.05149 324 HIS A C   
2492 O O   . HIS A 330 ? 1.08733 1.15317 1.13188 -0.00047 0.02328  -0.05312 324 HIS A O   
2493 C CB  . HIS A 330 ? 0.81914 0.88960 0.87493 -0.02287 0.02819  -0.03443 324 HIS A CB  
2494 C CG  . HIS A 330 ? 0.85597 0.93320 0.93360 -0.01924 0.02265  -0.03948 324 HIS A CG  
2495 N ND1 . HIS A 330 ? 0.77877 0.87391 0.87946 -0.02170 0.02175  -0.03864 324 HIS A ND1 
2496 C CD2 . HIS A 330 ? 0.87904 0.94604 0.95768 -0.01400 0.01701  -0.04433 324 HIS A CD2 
2497 C CE1 . HIS A 330 ? 0.75020 0.83981 0.86021 -0.01622 0.01378  -0.04194 324 HIS A CE1 
2498 N NE2 . HIS A 330 ? 0.90823 0.97979 1.00382 -0.01345 0.01222  -0.04454 324 HIS A NE2 
2499 N N   . ILE A 331 ? 0.68903 0.78331 0.74820 0.00543  0.03419  -0.06091 325 ILE A N   
2500 C CA  . ILE A 331 ? 0.67368 0.76321 0.73627 0.01448  0.02773  -0.07333 325 ILE A CA  
2501 C C   . ILE A 331 ? 0.76474 0.85701 0.85132 0.01708  0.02479  -0.07772 325 ILE A C   
2502 O O   . ILE A 331 ? 0.84546 0.95378 0.94465 0.02127  0.03010  -0.07945 325 ILE A O   
2503 C CB  . ILE A 331 ? 0.72238 0.81697 0.76744 0.02384  0.03093  -0.08324 325 ILE A CB  
2504 C CG1 . ILE A 331 ? 0.70649 0.79230 0.72174 0.02270  0.03042  -0.07678 325 ILE A CG1 
2505 C CG2 . ILE A 331 ? 0.65187 0.73933 0.70291 0.03096  0.02162  -0.09798 325 ILE A CG2 
2506 C CD1 . ILE A 331 ? 0.79145 0.87974 0.77982 0.03145  0.03319  -0.08435 325 ILE A CD1 
2507 N N   . THR A 332 ? 0.74693 0.82408 0.83981 0.01486  0.01641  -0.07921 326 THR A N   
2508 C CA  . THR A 332 ? 0.73190 0.80148 0.84054 0.01612  0.01090  -0.07939 326 THR A CA  
2509 C C   . THR A 332 ? 0.84232 0.89273 0.95149 0.01470  0.00373  -0.08587 326 THR A C   
2510 O O   . THR A 332 ? 0.93413 0.98400 1.03712 0.01262  0.00287  -0.09187 326 THR A O   
2511 C CB  . THR A 332 ? 0.83976 0.90559 0.95142 0.00760  0.00839  -0.06679 326 THR A CB  
2512 O OG1 . THR A 332 ? 0.88838 0.94416 1.01088 0.01093  0.00036  -0.06579 326 THR A OG1 
2513 C CG2 . THR A 332 ? 0.73685 0.79026 0.83640 -0.00153 0.00763  -0.06182 326 THR A CG2 
2514 N N   . SER A 333 ? 0.76416 0.79787 0.88109 0.01507  -0.00298 -0.08424 327 SER A N   
2515 C CA  . SER A 333 ? 0.71346 0.72294 0.82958 0.00807  -0.00949 -0.08631 327 SER A CA  
2516 C C   . SER A 333 ? 0.69193 0.68760 0.80297 -0.00524 -0.01020 -0.07250 327 SER A C   
2517 O O   . SER A 333 ? 0.89236 0.87109 1.00153 -0.01650 -0.01185 -0.07135 327 SER A O   
2518 C CB  . SER A 333 ? 0.66841 0.65740 0.78931 0.01848  -0.01812 -0.09487 327 SER A CB  
2519 O OG  . SER A 333 ? 0.98799 0.96679 1.11266 0.02365  -0.02398 -0.08626 327 SER A OG  
2520 N N   . ALA A 334 ? 0.74857 0.75083 0.85579 -0.00574 -0.00871 -0.06242 328 ALA A N   
2521 C CA  . ALA A 334 ? 0.75481 0.74309 0.84990 -0.01680 -0.00908 -0.05030 328 ALA A CA  
2522 C C   . ALA A 334 ? 0.89561 0.89755 0.98412 -0.02457 0.00019  -0.04924 328 ALA A C   
2523 O O   . ALA A 334 ? 0.91124 0.93133 1.00284 -0.01976 0.00408  -0.05468 328 ALA A O   
2524 C CB  . ALA A 334 ? 0.77738 0.76324 0.86966 -0.01224 -0.01611 -0.04210 328 ALA A CB  
2525 N N   . ASN A 335 ? 0.84949 0.84084 0.92632 -0.03558 0.00381  -0.04214 329 ASN A N   
2526 C CA  . ASN A 335 ? 0.79449 0.79915 0.86524 -0.04012 0.01314  -0.04272 329 ASN A CA  
2527 C C   . ASN A 335 ? 0.89661 0.89468 0.94861 -0.03944 0.01205  -0.03555 329 ASN A C   
2528 O O   . ASN A 335 ? 0.92058 0.90148 0.96150 -0.04075 0.00465  -0.02749 329 ASN A O   
2529 C CB  . ASN A 335 ? 0.77741 0.78116 0.84843 -0.05351 0.02139  -0.04166 329 ASN A CB  
2530 C CG  . ASN A 335 ? 0.87431 0.90001 0.94561 -0.05438 0.03240  -0.04618 329 ASN A CG  
2531 O OD1 . ASN A 335 ? 0.94196 0.98915 1.02870 -0.04735 0.03293  -0.05625 329 ASN A OD1 
2532 N ND2 . ASN A 335 ? 0.94503 0.96464 0.99700 -0.06105 0.04047  -0.03961 329 ASN A ND2 
2533 N N   . PHE A 336 ? 0.82371 0.83269 0.87079 -0.03621 0.01684  -0.03944 330 PHE A N   
2534 C CA  . PHE A 336 ? 0.83359 0.83305 0.86116 -0.03569 0.01405  -0.03560 330 PHE A CA  
2535 C C   . PHE A 336 ? 0.81427 0.80140 0.81902 -0.04296 0.01926  -0.03097 330 PHE A C   
2536 O O   . PHE A 336 ? 0.92435 0.91674 0.91855 -0.04239 0.02865  -0.03569 330 PHE A O   
2537 C CB  . PHE A 336 ? 0.78976 0.79633 0.81533 -0.02903 0.01613  -0.04192 330 PHE A CB  
2538 C CG  . PHE A 336 ? 0.89370 0.90583 0.93001 -0.02464 0.01107  -0.04245 330 PHE A CG  
2539 C CD1 . PHE A 336 ? 0.80966 0.82405 0.85667 -0.02608 0.00545  -0.03842 330 PHE A CD1 
2540 C CD2 . PHE A 336 ? 0.87901 0.89430 0.91317 -0.01826 0.01230  -0.04682 330 PHE A CD2 
2541 C CE1 . PHE A 336 ? 0.74368 0.76823 0.79998 -0.02350 0.00500  -0.03898 330 PHE A CE1 
2542 C CE2 . PHE A 336 ? 0.78272 0.80066 0.82004 -0.01668 0.00990  -0.04500 330 PHE A CE2 
2543 C CZ  . PHE A 336 ? 0.90156 0.92654 0.95039 -0.02046 0.00817  -0.04118 330 PHE A CZ  
2544 N N   . ASP A 337 ? 0.82834 0.79775 0.82254 -0.04840 0.01296  -0.02175 331 ASP A N   
2545 C CA  . ASP A 337 ? 0.94498 0.89726 0.90819 -0.05645 0.01729  -0.01452 331 ASP A CA  
2546 C C   . ASP A 337 ? 0.93257 0.86000 0.87852 -0.05671 0.00092  -0.00399 331 ASP A C   
2547 O O   . ASP A 337 ? 0.98248 0.91115 0.94770 -0.05012 -0.01223 -0.00364 331 ASP A O   
2548 C CB  . ASP A 337 ? 1.02788 0.98386 0.99353 -0.06747 0.03175  -0.01244 331 ASP A CB  
2549 C CG  . ASP A 337 ? 1.00079 0.94677 0.98345 -0.07148 0.02518  -0.00814 331 ASP A CG  
2550 O OD1 . ASP A 337 ? 1.24761 1.18699 1.24064 -0.06230 0.01066  -0.00816 331 ASP A OD1 
2551 O OD2 . ASP A 337 ? 1.09965 1.04492 1.08643 -0.08410 0.03475  -0.00577 331 ASP A OD2 
2552 N N   . GLY A 338 ? 1.17058 1.07689 1.07898 -0.06319 0.00181  0.00408  332 GLY A N   
2553 C CA  . GLY A 338 ? 1.03891 0.91973 0.92477 -0.06129 -0.01772 0.01380  332 GLY A CA  
2554 C C   . GLY A 338 ? 0.95059 0.81255 0.84277 -0.06108 -0.02794 0.02348  332 GLY A C   
2555 O O   . GLY A 338 ? 1.12447 0.97917 1.02438 -0.05160 -0.04846 0.02603  332 GLY A O   
2556 N N   . THR A 339 ? 1.01855 0.87219 0.90915 -0.07134 -0.01486 0.02813  333 THR A N   
2557 C CA  . THR A 339 ? 1.01218 0.83816 0.90453 -0.07180 -0.02568 0.03707  333 THR A CA  
2558 C C   . THR A 339 ? 1.04775 0.88852 0.98173 -0.05648 -0.03792 0.02713  333 THR A C   
2559 O O   . THR A 339 ? 1.02696 0.84857 0.96266 -0.04555 -0.05719 0.03122  333 THR A O   
2560 C CB  . THR A 339 ? 1.06312 0.88102 0.95285 -0.08954 -0.00806 0.04152  333 THR A CB  
2561 O OG1 . THR A 339 ? 1.31868 1.12844 1.16940 -0.10437 0.00728  0.05067  333 THR A OG1 
2562 C CG2 . THR A 339 ? 0.94769 0.72579 0.83329 -0.09128 -0.02144 0.05129  333 THR A CG2 
2563 N N   . HIS A 340 ? 1.03096 0.90627 0.99707 -0.05379 -0.02706 0.01351  334 HIS A N   
2564 C CA  . HIS A 340 ? 0.92156 0.81372 0.92269 -0.04002 -0.03452 0.00330  334 HIS A CA  
2565 C C   . HIS A 340 ? 0.96044 0.86603 0.97095 -0.02783 -0.04842 0.00177  334 HIS A C   
2566 O O   . HIS A 340 ? 0.93256 0.83287 0.95556 -0.01554 -0.06371 0.00184  334 HIS A O   
2567 C CB  . HIS A 340 ? 0.77120 0.69408 0.79580 -0.04096 -0.02004 -0.00924 334 HIS A CB  
2568 C CG  . HIS A 340 ? 0.83279 0.74981 0.86330 -0.05030 -0.01159 -0.01204 334 HIS A CG  
2569 N ND1 . HIS A 340 ? 0.96435 0.88450 1.01670 -0.04413 -0.01472 -0.02203 334 HIS A ND1 
2570 C CD2 . HIS A 340 ? 0.89323 0.80369 0.91198 -0.06676 -0.00007 -0.00724 334 HIS A CD2 
2571 C CE1 . HIS A 340 ? 0.95964 0.87296 1.01418 -0.05734 -0.00825 -0.02345 334 HIS A CE1 
2572 N NE2 . HIS A 340 ? 1.05099 0.96118 1.08817 -0.07219 0.00173  -0.01401 334 HIS A NE2 
2573 N N   . TYR A 341 ? 0.92061 0.84417 0.92733 -0.03096 -0.04422 -0.00063 335 TYR A N   
2574 C CA  . TYR A 341 ? 0.99631 0.94001 1.02062 -0.02385 -0.05529 -0.00408 335 TYR A CA  
2575 C C   . TYR A 341 ? 0.93063 0.85884 0.94104 -0.02018 -0.07639 0.00356  335 TYR A C   
2576 O O   . TYR A 341 ? 1.18384 1.13198 1.21101 -0.01713 -0.08739 0.00046  335 TYR A O   
2577 C CB  . TYR A 341 ? 0.78446 0.74461 0.80675 -0.03031 -0.04601 -0.00901 335 TYR A CB  
2578 C CG  . TYR A 341 ? 0.84744 0.83246 0.89583 -0.02758 -0.03447 -0.01743 335 TYR A CG  
2579 C CD1 . TYR A 341 ? 0.83147 0.81707 0.88049 -0.02831 -0.02143 -0.02154 335 TYR A CD1 
2580 C CD2 . TYR A 341 ? 0.88155 0.89052 0.95337 -0.02528 -0.03708 -0.02094 335 TYR A CD2 
2581 C CE1 . TYR A 341 ? 0.81773 0.82271 0.88419 -0.02449 -0.01362 -0.02899 335 TYR A CE1 
2582 C CE2 . TYR A 341 ? 0.96069 0.98878 1.04822 -0.02337 -0.02568 -0.02682 335 TYR A CE2 
2583 C CZ  . TYR A 341 ? 0.88178 0.90558 0.96374 -0.02174 -0.01517 -0.03085 335 TYR A CZ  
2584 O OH  . TYR A 341 ? 0.98775 1.02738 1.07897 -0.01864 -0.00639 -0.03653 335 TYR A OH  
2585 N N   . GLN A 342 ? 0.98803 0.88123 0.96824 -0.02134 -0.08359 0.01392  336 GLN A N   
2586 C CA  . GLN A 342 ? 0.88621 0.76014 0.84908 -0.01498 -0.10777 0.02204  336 GLN A CA  
2587 C C   . GLN A 342 ? 0.91972 0.76456 0.87974 -0.00421 -0.12191 0.02913  336 GLN A C   
2588 O O   . GLN A 342 ? 1.03891 0.86764 0.98797 0.00571  -0.14639 0.03551  336 GLN A O   
2589 C CB  . GLN A 342 ? 0.90824 0.75583 0.81911 -0.02620 -0.10819 0.03073  336 GLN A CB  
2590 C CG  . GLN A 342 ? 1.08530 0.95258 0.99412 -0.03160 -0.10679 0.02287  336 GLN A CG  
2591 C CD  . GLN A 342 ? 1.28181 1.12073 1.13754 -0.03688 -0.11673 0.02923  336 GLN A CD  
2592 O OE1 . GLN A 342 ? 1.38623 1.19255 1.19945 -0.04120 -0.11332 0.04037  336 GLN A OE1 
2593 N NE2 . GLN A 342 ? 1.41706 1.26622 1.27199 -0.03803 -0.12928 0.02225  336 GLN A NE2 
2594 N N   . ASN A 343 ? 0.95811 0.79299 0.92690 -0.00494 -0.11018 0.02748  337 ASN A N   
2595 C CA  . ASN A 343 ? 1.15929 0.95497 1.11898 0.00426  -0.12480 0.03450  337 ASN A CA  
2596 C C   . ASN A 343 ? 0.93886 0.74555 0.93611 0.01572  -0.12090 0.02161  337 ASN A C   
2597 O O   . ASN A 343 ? 1.10753 0.89727 1.11526 0.03436  -0.13900 0.01980  337 ASN A O   
2598 C CB  . ASN A 343 ? 1.05547 0.80387 0.96672 -0.01405 -0.11712 0.05037  337 ASN A CB  
2599 C CG  . ASN A 343 ? 1.17541 0.90908 1.04055 -0.02404 -0.11974 0.06259  337 ASN A CG  
2600 O OD1 . ASN A 343 ? 1.34345 1.06652 1.19441 -0.01293 -0.14347 0.06769  337 ASN A OD1 
2601 N ND2 . ASN A 343 ? 1.39140 1.12697 1.23343 -0.04376 -0.09595 0.06555  337 ASN A ND2 
2602 N N   . HIS A 344 ? 0.94180 0.77510 0.95711 0.00701  -0.09909 0.01142  338 HIS A N   
2603 C CA  . HIS A 344 ? 1.13420 0.96953 1.17322 0.01427  -0.09400 -0.00076 338 HIS A CA  
2604 C C   . HIS A 344 ? 0.95117 0.82741 1.03054 0.03472  -0.09696 -0.01625 338 HIS A C   
2605 O O   . HIS A 344 ? 0.99066 0.90619 1.08634 0.03513  -0.09342 -0.01914 338 HIS A O   
2606 C CB  . HIS A 344 ? 1.00030 0.84687 1.03925 -0.00338 -0.07194 -0.00537 338 HIS A CB  
2607 C CG  . HIS A 344 ? 1.00602 0.81739 1.01374 -0.02420 -0.06582 0.00733  338 HIS A CG  
2608 N ND1 . HIS A 344 ? 0.99436 0.75641 0.97160 -0.02716 -0.07901 0.02243  338 HIS A ND1 
2609 C CD2 . HIS A 344 ? 0.99651 0.81687 0.99935 -0.04367 -0.04731 0.00761  338 HIS A CD2 
2610 C CE1 . HIS A 344 ? 1.05439 0.79658 1.00772 -0.05065 -0.06615 0.03261  338 HIS A CE1 
2611 N NE2 . HIS A 344 ? 1.11271 0.89371 1.08482 -0.06050 -0.04652 0.02270  338 HIS A NE2 
2612 N N   . GLY A 345 ? 0.83295 0.69839 0.92726 0.05086  -0.10280 -0.02671 339 GLY A N   
2613 C CA  . GLY A 345 ? 0.79530 0.70037 0.92703 0.07227  -0.10284 -0.04323 339 GLY A CA  
2614 C C   . GLY A 345 ? 0.84997 0.77932 0.99408 0.06996  -0.08344 -0.05782 339 GLY A C   
2615 O O   . GLY A 345 ? 0.87390 0.77601 1.00941 0.07001  -0.08226 -0.06469 339 GLY A O   
2616 N N   . PHE A 346 ? 0.80358 0.78103 0.96504 0.06682  -0.06970 -0.06224 340 PHE A N   
2617 C CA  . PHE A 346 ? 0.81002 0.81030 0.97657 0.06446  -0.05200 -0.07393 340 PHE A CA  
2618 C C   . PHE A 346 ? 0.83753 0.89007 1.02915 0.06997  -0.04188 -0.07948 340 PHE A C   
2619 O O   . PHE A 346 ? 0.89439 0.96775 1.10247 0.07153  -0.04838 -0.07405 340 PHE A O   
2620 C CB  . PHE A 346 ? 0.79862 0.78967 0.94352 0.04247  -0.04158 -0.06701 340 PHE A CB  
2621 C CG  . PHE A 346 ? 0.81971 0.81851 0.95572 0.02830  -0.04002 -0.05354 340 PHE A CG  
2622 C CD1 . PHE A 346 ? 0.82705 0.79598 0.94291 0.01956  -0.04894 -0.04070 340 PHE A CD1 
2623 C CD2 . PHE A 346 ? 0.79385 0.82535 0.93695 0.02329  -0.02986 -0.05378 340 PHE A CD2 
2624 C CE1 . PHE A 346 ? 0.81211 0.78589 0.91531 0.00831  -0.04796 -0.03113 340 PHE A CE1 
2625 C CE2 . PHE A 346 ? 0.79449 0.82705 0.92694 0.01107  -0.03045 -0.04369 340 PHE A CE2 
2626 C CZ  . PHE A 346 ? 0.80119 0.80595 0.91376 0.00466  -0.03959 -0.03375 340 PHE A CZ  
2627 N N   . VAL A 347 ? 0.80292 0.87647 0.99619 0.07143  -0.02636 -0.09015 341 VAL A N   
2628 C CA  . VAL A 347 ? 0.85121 0.97225 1.06155 0.07111  -0.01190 -0.09313 341 VAL A CA  
2629 C C   . VAL A 347 ? 0.84068 0.96295 1.02890 0.05550  0.00192  -0.08980 341 VAL A C   
2630 O O   . VAL A 347 ? 0.71631 0.81822 0.88600 0.05576  0.00346  -0.09589 341 VAL A O   
2631 C CB  . VAL A 347 ? 0.85898 1.00791 1.09085 0.09344  -0.00550 -0.11077 341 VAL A CB  
2632 C CG1 . VAL A 347 ? 0.76430 0.88423 0.97740 0.10435  -0.00573 -0.12496 341 VAL A CG1 
2633 C CG2 . VAL A 347 ? 0.69745 0.89620 0.94148 0.08802  0.01492  -0.11225 341 VAL A CG2 
2634 N N   . SER A 348 ? 0.81961 0.96328 1.00965 0.04193  0.00942  -0.08032 342 SER A N   
2635 C CA  . SER A 348 ? 0.70232 0.84089 0.86870 0.02824  0.01881  -0.07465 342 SER A CA  
2636 C C   . SER A 348 ? 0.81429 0.98390 0.98185 0.02731  0.03547  -0.07710 342 SER A C   
2637 O O   . SER A 348 ? 0.89324 1.09515 1.08420 0.02539  0.04122  -0.07553 342 SER A O   
2638 C CB  . SER A 348 ? 0.83005 0.95678 0.98827 0.01222  0.01328  -0.06096 342 SER A CB  
2639 O OG  . SER A 348 ? 0.97849 1.07565 1.12713 0.01124  0.00184  -0.05786 342 SER A OG  
2640 N N   . PHE A 349 ? 0.79422 0.95520 0.93608 0.02760  0.04288  -0.08053 343 PHE A N   
2641 C CA  . PHE A 349 ? 0.62705 0.80963 0.75738 0.02461  0.05953  -0.07994 343 PHE A CA  
2642 C C   . PHE A 349 ? 0.83249 1.00921 0.94931 0.00530  0.06237  -0.06346 343 PHE A C   
2643 O O   . PHE A 349 ? 0.83397 0.98185 0.93208 -0.00005 0.05341  -0.05753 343 PHE A O   
2644 C CB  . PHE A 349 ? 0.80803 0.97802 0.90937 0.03414  0.06234  -0.09031 343 PHE A CB  
2645 C CG  . PHE A 349 ? 0.85573 1.03846 0.93118 0.02979  0.07845  -0.08669 343 PHE A CG  
2646 C CD1 . PHE A 349 ? 0.81205 1.02531 0.89053 0.03822  0.09509  -0.09591 343 PHE A CD1 
2647 C CD2 . PHE A 349 ? 0.79069 0.95307 0.83569 0.01844  0.07717  -0.07410 343 PHE A CD2 
2648 C CE1 . PHE A 349 ? 0.88156 1.10466 0.92959 0.03208  0.11217  -0.09055 343 PHE A CE1 
2649 C CE2 . PHE A 349 ? 0.72968 0.89623 0.74350 0.01354  0.09073  -0.06791 343 PHE A CE2 
2650 C CZ  . PHE A 349 ? 0.87053 1.06732 0.88393 0.01873  0.10926  -0.07513 343 PHE A CZ  
2651 N N   . ASN A 350 ? 0.82940 1.03362 0.95680 -0.00528 0.07501  -0.05688 344 ASN A N   
2652 C CA  . ASN A 350 ? 0.80830 1.00220 0.92045 -0.02590 0.07789  -0.04096 344 ASN A CA  
2653 C C   . ASN A 350 ? 0.84987 1.06097 0.94464 -0.03384 0.09818  -0.03596 344 ASN A C   
2654 O O   . ASN A 350 ? 0.91050 1.16149 1.02547 -0.02971 0.11322  -0.04294 344 ASN A O   
2655 C CB  . ASN A 350 ? 0.69237 0.89869 0.83499 -0.03954 0.07115  -0.03418 344 ASN A CB  
2656 C CG  . ASN A 350 ? 0.82876 1.01196 0.97728 -0.03402 0.05151  -0.03618 344 ASN A CG  
2657 O OD1 . ASN A 350 ? 1.40681 1.55851 1.53181 -0.02810 0.04434  -0.03734 344 ASN A OD1 
2658 N ND2 . ASN A 350 ? 0.90245 1.10336 1.08222 -0.03619 0.04275  -0.03660 344 ASN A ND2 
2659 N N   . SER A 351 ? 0.85465 1.03489 0.90997 -0.04422 0.09886  -0.02386 345 SER A N   
2660 C CA  . SER A 351 ? 0.87932 1.06660 0.90756 -0.05518 0.11782  -0.01465 345 SER A CA  
2661 C C   . SER A 351 ? 1.04912 1.19853 1.04737 -0.07536 0.11350  0.00465  345 SER A C   
2662 O O   . SER A 351 ? 1.05349 1.16357 1.03536 -0.07096 0.09545  0.00665  345 SER A O   
2663 C CB  . SER A 351 ? 0.84513 1.02463 0.83678 -0.03791 0.12262  -0.02331 345 SER A CB  
2664 O OG  . SER A 351 ? 1.06419 1.24646 1.02076 -0.04933 0.14164  -0.01228 345 SER A OG  
2665 N N   . ILE A 352 ? 1.01028 1.17163 1.00190 -0.09762 0.13073  0.01833  346 ILE A N   
2666 C CA  . ILE A 352 ? 1.09468 1.21301 1.05036 -0.11899 0.12802  0.03849  346 ILE A CA  
2667 C C   . ILE A 352 ? 1.07995 1.18549 0.98397 -0.12508 0.14484  0.05059  346 ILE A C   
2668 O O   . ILE A 352 ? 1.09785 1.17101 0.96997 -0.14745 0.14806  0.07052  346 ILE A O   
2669 C CB  . ILE A 352 ? 0.95077 1.08273 0.93962 -0.14774 0.13011  0.04814  346 ILE A CB  
2670 C CG1 . ILE A 352 ? 0.98059 1.17404 1.00080 -0.16299 0.15684  0.04903  346 ILE A CG1 
2671 C CG2 . ILE A 352 ? 0.96403 1.10145 0.99349 -0.14022 0.11026  0.03677  346 ILE A CG2 
2672 C CD1 . ILE A 352 ? 0.84503 1.05789 0.90139 -0.19557 0.15922  0.05887  346 ILE A CD1 
2673 N N   . ASP A 353 ? 0.97903 1.10558 0.87020 -0.10574 0.15477  0.03881  347 ASP A N   
2674 C CA  . ASP A 353 ? 1.10436 1.21584 0.93735 -0.10816 0.16919  0.04893  347 ASP A CA  
2675 C C   . ASP A 353 ? 1.29682 1.34303 1.07508 -0.09884 0.14661  0.05760  347 ASP A C   
2676 O O   . ASP A 353 ? 1.18055 1.21374 0.96225 -0.07495 0.12574  0.04337  347 ASP A O   
2677 C CB  . ASP A 353 ? 0.95939 1.10877 0.79140 -0.08676 0.18286  0.02983  347 ASP A CB  
2678 C CG  . ASP A 353 ? 1.14249 1.27808 0.90821 -0.08879 0.19912  0.03929  347 ASP A CG  
2679 O OD1 . ASP A 353 ? 1.27058 1.41768 1.02168 -0.11440 0.22351  0.05682  347 ASP A OD1 
2680 O OD2 . ASP A 353 ? 1.28031 1.39379 1.00729 -0.06617 0.18729  0.02945  347 ASP A OD2 
2681 N N   . LYS A 354 ? 1.50984 1.51540 1.23875 -0.11802 0.15038  0.08116  348 LYS A N   
2682 C CA  . LYS A 354 ? 1.40005 1.33942 1.07755 -0.10791 0.12599  0.09076  348 LYS A CA  
2683 C C   . LYS A 354 ? 1.31395 1.24708 0.95937 -0.07750 0.11450  0.07738  348 LYS A C   
2684 O O   . LYS A 354 ? 1.28319 1.18950 0.92511 -0.05681 0.08808  0.06948  348 LYS A O   
2685 C CB  . LYS A 354 ? 1.67378 1.56676 1.29550 -0.13390 0.13367  0.11997  348 LYS A CB  
2686 C CG  . LYS A 354 ? 1.85877 1.73668 1.50480 -0.16427 0.13403  0.13398  348 LYS A CG  
2687 C CD  . LYS A 354 ? 1.63521 1.46262 1.28234 -0.15158 0.10208  0.13102  348 LYS A CD  
2688 C CE  . LYS A 354 ? 1.73614 1.52800 1.38540 -0.18281 0.09908  0.14772  348 LYS A CE  
2689 N NZ  . LYS A 354 ? 1.83231 1.56237 1.46537 -0.16770 0.06824  0.14588  348 LYS A NZ  
2690 N N   . GLN A 355 ? 1.33678 1.29715 0.95985 -0.07430 0.13390  0.07301  349 GLN A N   
2691 C CA  . GLN A 355 ? 1.36487 1.31650 0.95180 -0.04709 0.12106  0.05947  349 GLN A CA  
2692 C C   . GLN A 355 ? 1.33669 1.31514 0.97522 -0.02419 0.10509  0.03178  349 GLN A C   
2693 O O   . GLN A 355 ? 1.28766 1.24631 0.91182 -0.00327 0.08074  0.02163  349 GLN A O   
2694 C CB  . GLN A 355 ? 1.36289 1.33760 0.91094 -0.04919 0.14730  0.05900  349 GLN A CB  
2695 C CG  . GLN A 355 ? 1.80115 1.72603 1.26081 -0.04913 0.14319  0.07771  349 GLN A CG  
2696 C CD  . GLN A 355 ? 1.88112 1.77130 1.31204 -0.01973 0.10719  0.06697  349 GLN A CD  
2697 O OE1 . GLN A 355 ? 1.68450 1.60024 1.15096 0.00135  0.09403  0.04070  349 GLN A OE1 
2698 N NE2 . GLN A 355 ? 1.76718 1.59823 1.13467 -0.01864 0.08967  0.08740  349 GLN A NE2 
2699 N N   . LEU A 356 ? 1.34353 1.36670 1.04271 -0.02854 0.11740  0.01980  350 LEU A N   
2700 C CA  . LEU A 356 ? 1.15366 1.19638 0.89839 -0.00992 0.10302  -0.00376 350 LEU A CA  
2701 C C   . LEU A 356 ? 1.07281 1.09069 0.83931 -0.00718 0.07923  -0.00218 350 LEU A C   
2702 O O   . LEU A 356 ? 1.11891 1.13338 0.89619 0.00994  0.06049  -0.01685 350 LEU A O   
2703 C CB  . LEU A 356 ? 1.20363 1.29521 1.00214 -0.01356 0.12072  -0.01520 350 LEU A CB  
2704 C CG  . LEU A 356 ? 1.11327 1.22158 0.95496 0.00397  0.10816  -0.03814 350 LEU A CG  
2705 C CD1 . LEU A 356 ? 0.93335 1.02917 0.74603 0.02411  0.09517  -0.05446 350 LEU A CD1 
2706 C CD2 . LEU A 356 ? 1.26086 1.41408 1.14548 0.00411  0.12587  -0.04872 350 LEU A CD2 
2707 N N   . VAL A 357 ? 1.10260 1.10393 0.87586 -0.02466 0.08020  0.01441  351 VAL A N   
2708 C CA  . VAL A 357 ? 0.99133 0.96571 0.77731 -0.02044 0.05912  0.01525  351 VAL A CA  
2709 C C   . VAL A 357 ? 1.10983 1.04675 0.85336 -0.00370 0.03872  0.01675  351 VAL A C   
2710 O O   . VAL A 357 ? 1.09284 1.02432 0.85328 0.01139  0.01996  0.00613  351 VAL A O   
2711 C CB  . VAL A 357 ? 1.09752 1.05494 0.89029 -0.04284 0.06316  0.03187  351 VAL A CB  
2712 C CG1 . VAL A 357 ? 1.08393 1.00776 0.87987 -0.03551 0.04173  0.03133  351 VAL A CG1 
2713 C CG2 . VAL A 357 ? 1.11306 1.11332 0.95602 -0.05655 0.07797  0.02746  351 VAL A CG2 
2714 N N   . SER A 358 ? 1.28244 1.19494 0.97008 -0.00576 0.04202  0.02999  352 SER A N   
2715 C CA  . SER A 358 ? 1.20259 1.07775 0.84537 0.01269  0.01926  0.03208  352 SER A CA  
2716 C C   . SER A 358 ? 1.22702 1.12616 0.88575 0.03570  0.00460  0.00855  352 SER A C   
2717 O O   . SER A 358 ? 1.12609 1.01383 0.79059 0.05302  -0.01915 0.00085  352 SER A O   
2718 C CB  . SER A 358 ? 1.23188 1.07661 0.80518 0.00519  0.02709  0.05152  352 SER A CB  
2719 O OG  . SER A 358 ? 1.54584 1.35385 1.07216 0.02621  0.00155  0.05296  352 SER A OG  
2720 N N   . GLU A 359 ? 1.22040 1.15392 0.88837 0.03614  0.01812  -0.00445 353 GLU A N   
2721 C CA  . GLU A 359 ? 1.11474 1.06775 0.79792 0.05448  0.00345  -0.02789 353 GLU A CA  
2722 C C   . GLU A 359 ? 1.08397 1.05492 0.82781 0.05800  -0.00702 -0.04107 353 GLU A C   
2723 O O   . GLU A 359 ? 1.10470 1.08073 0.86136 0.07197  -0.02704 -0.05547 353 GLU A O   
2724 C CB  . GLU A 359 ? 1.03169 1.01319 0.71304 0.05405  0.02106  -0.04061 353 GLU A CB  
2725 C CG  . GLU A 359 ? 1.13403 1.10232 0.74987 0.05247  0.03333  -0.03075 353 GLU A CG  
2726 C CD  . GLU A 359 ? 1.43188 1.37633 0.99690 0.07078  0.00926  -0.03664 353 GLU A CD  
2727 O OE1 . GLU A 359 ? 1.39860 1.34444 0.98800 0.08466  -0.01677 -0.05131 353 GLU A OE1 
2728 O OE2 . GLU A 359 ? 1.56800 1.49402 1.06823 0.07058  0.01628  -0.02653 353 GLU A OE2 
2729 N N   . ALA A 360 ? 0.96650 0.94878 0.74769 0.04429  0.00625  -0.03627 354 ALA A N   
2730 C CA  . ALA A 360 ? 0.90985 0.90558 0.74077 0.04593  -0.00150 -0.04618 354 ALA A CA  
2731 C C   . ALA A 360 ? 1.01616 0.98987 0.84373 0.05393  -0.01887 -0.04195 354 ALA A C   
2732 O O   . ALA A 360 ? 1.01629 1.00310 0.87314 0.06313  -0.03109 -0.05482 354 ALA A O   
2733 C CB  . ALA A 360 ? 0.78654 0.79682 0.65105 0.03055  0.01478  -0.04161 354 ALA A CB  
2734 N N   . LYS A 361 ? 1.08812 1.02818 0.88100 0.05031  -0.01967 -0.02444 355 LYS A N   
2735 C CA  . LYS A 361 ? 1.01049 0.92389 0.79482 0.06279  -0.03822 -0.02187 355 LYS A CA  
2736 C C   . LYS A 361 ? 1.04168 0.95757 0.81514 0.08496  -0.06000 -0.03328 355 LYS A C   
2737 O O   . LYS A 361 ? 1.12879 1.05089 0.92560 0.09955  -0.07543 -0.04332 355 LYS A O   
2738 C CB  . LYS A 361 ? 0.98641 0.85327 0.72647 0.05461  -0.03724 -0.00011 355 LYS A CB  
2739 C CG  . LYS A 361 ? 1.18720 1.01939 0.91946 0.06796  -0.05569 0.00219  355 LYS A CG  
2740 C CD  . LYS A 361 ? 1.19607 1.03416 0.96555 0.05957  -0.04934 -0.00172 355 LYS A CD  
2741 C CE  . LYS A 361 ? 1.44862 1.24615 1.20350 0.07368  -0.06603 -0.00020 355 LYS A CE  
2742 N NZ  . LYS A 361 ? 1.53302 1.32791 1.31192 0.06327  -0.05910 -0.00277 355 LYS A NZ  
2743 N N   . LYS A 362 ? 1.08167 0.99606 0.82057 0.08819  -0.06165 -0.03330 356 LYS A N   
2744 C CA  . LYS A 362 ? 1.07319 0.99291 0.80205 0.10859  -0.08537 -0.04628 356 LYS A CA  
2745 C C   . LYS A 362 ? 1.09310 1.05642 0.88033 0.11200  -0.09064 -0.06935 356 LYS A C   
2746 O O   . LYS A 362 ? 1.09162 1.06729 0.89659 0.12778  -0.11222 -0.08162 356 LYS A O   
2747 C CB  . LYS A 362 ? 1.09957 1.00916 0.77561 0.10927  -0.08387 -0.04321 356 LYS A CB  
2748 C CG  . LYS A 362 ? 1.46422 1.37461 1.12032 0.13037  -0.11213 -0.05622 356 LYS A CG  
2749 C CD  . LYS A 362 ? 1.62372 1.52190 1.22001 0.13019  -0.10816 -0.05382 356 LYS A CD  
2750 C CE  . LYS A 362 ? 1.45901 1.35731 1.03267 0.15132  -0.13999 -0.06865 356 LYS A CE  
2751 N NZ  . LYS A 362 ? 1.49229 1.37594 0.99943 0.15211  -0.13592 -0.06757 356 LYS A NZ  
2752 N N   . ILE A 363 ? 1.07617 1.06326 0.89510 0.09683  -0.07171 -0.07513 357 ILE A N   
2753 C CA  . ILE A 363 ? 0.87616 0.89752 0.74722 0.09554  -0.07507 -0.09400 357 ILE A CA  
2754 C C   . ILE A 363 ? 1.08940 1.12107 0.99890 0.09788  -0.07898 -0.09573 357 ILE A C   
2755 O O   . ILE A 363 ? 1.04359 1.09948 0.98446 0.10557  -0.09271 -0.11006 357 ILE A O   
2756 C CB  . ILE A 363 ? 0.89375 0.92881 0.78429 0.08037  -0.05517 -0.09726 357 ILE A CB  
2757 C CG1 . ILE A 363 ? 0.82464 0.85623 0.68087 0.08223  -0.05147 -0.10187 357 ILE A CG1 
2758 C CG2 . ILE A 363 ? 0.90349 0.96422 0.84482 0.07540  -0.05784 -0.11224 357 ILE A CG2 
2759 C CD1 . ILE A 363 ? 1.16820 1.20805 1.02044 0.09294  -0.07190 -0.12088 357 ILE A CD1 
2760 N N   . PHE A 364 ? 0.90766 0.92345 0.81601 0.09071  -0.06654 -0.08244 358 PHE A N   
2761 C CA  . PHE A 364 ? 0.96129 0.98565 0.90110 0.09388  -0.06769 -0.08570 358 PHE A CA  
2762 C C   . PHE A 364 ? 1.09997 1.12050 1.03466 0.11611  -0.08881 -0.09083 358 PHE A C   
2763 O O   . PHE A 364 ? 0.91059 0.95984 0.88407 0.12373  -0.09419 -0.10385 358 PHE A O   
2764 C CB  . PHE A 364 ? 0.82959 0.83133 0.76098 0.08309  -0.05372 -0.07172 358 PHE A CB  
2765 C CG  . PHE A 364 ? 0.90487 0.91530 0.86455 0.08563  -0.05192 -0.07707 358 PHE A CG  
2766 C CD1 . PHE A 364 ? 0.88468 0.91969 0.87860 0.07319  -0.03958 -0.08267 358 PHE A CD1 
2767 C CD2 . PHE A 364 ? 0.99346 0.98517 0.94190 0.10196  -0.06278 -0.07704 358 PHE A CD2 
2768 C CE1 . PHE A 364 ? 0.85624 0.89988 0.87024 0.07507  -0.03547 -0.08757 358 PHE A CE1 
2769 C CE2 . PHE A 364 ? 0.94266 0.94470 0.91494 0.10643  -0.05901 -0.08463 358 PHE A CE2 
2770 C CZ  . PHE A 364 ? 0.91046 0.94007 0.91444 0.09205  -0.04405 -0.08969 358 PHE A CZ  
2771 N N   . GLU A 365 ? 1.07269 1.05846 0.95966 0.12717  -0.10084 -0.08043 359 GLU A N   
2772 C CA  . GLU A 365 ? 0.94115 0.91908 0.81997 0.15261  -0.12536 -0.08524 359 GLU A CA  
2773 C C   . GLU A 365 ? 1.01451 1.03590 0.92730 0.16318  -0.14182 -0.10548 359 GLU A C   
2774 O O   . GLU A 365 ? 0.99831 1.04489 0.94529 0.17964  -0.15495 -0.11833 359 GLU A O   
2775 C CB  . GLU A 365 ? 0.91433 0.84108 0.72717 0.16087  -0.13709 -0.06823 359 GLU A CB  
2776 C CG  . GLU A 365 ? 0.99913 0.87901 0.77874 0.14917  -0.12441 -0.04767 359 GLU A CG  
2777 C CD  . GLU A 365 ? 1.16304 1.02712 0.95650 0.16182  -0.13077 -0.04993 359 GLU A CD  
2778 O OE1 . GLU A 365 ? 1.12173 1.01014 0.94554 0.18431  -0.14623 -0.06632 359 GLU A OE1 
2779 O OE2 . GLU A 365 ? 1.14635 0.97508 0.92131 0.14937  -0.12042 -0.03671 359 GLU A OE2 
2780 N N   . ARG A 366 ? 0.90785 0.94054 0.81374 0.15378  -0.14145 -0.11024 360 ARG A N   
2781 C CA  . ARG A 366 ? 0.93232 1.00514 0.87221 0.15876  -0.15787 -0.13085 360 ARG A CA  
2782 C C   . ARG A 366 ? 0.92328 1.04099 0.93060 0.14895  -0.14807 -0.14400 360 ARG A C   
2783 O O   . ARG A 366 ? 0.95155 1.10453 0.99842 0.16046  -0.16267 -0.15843 360 ARG A O   
2784 C CB  . ARG A 366 ? 0.89401 0.96474 0.81192 0.14763  -0.15572 -0.13480 360 ARG A CB  
2785 C CG  . ARG A 366 ? 0.71041 0.81825 0.66308 0.14793  -0.17332 -0.15755 360 ARG A CG  
2786 C CD  . ARG A 366 ? 0.87397 0.97832 0.81422 0.13291  -0.16430 -0.16380 360 ARG A CD  
2787 N NE  . ARG A 366 ? 0.88573 0.99205 0.84958 0.11308  -0.13650 -0.15842 360 ARG A NE  
2788 C CZ  . ARG A 366 ? 0.92319 1.02125 0.87633 0.10173  -0.12365 -0.16091 360 ARG A CZ  
2789 N NH1 . ARG A 366 ? 1.02921 1.11647 0.94632 0.10716  -0.13289 -0.16969 360 ARG A NH1 
2790 N NH2 . ARG A 366 ? 0.79716 0.89684 0.77411 0.08668  -0.10207 -0.15549 360 ARG A NH2 
2791 N N   . ASP A 367 ? 0.95022 1.06852 0.97110 0.12738  -0.12308 -0.13877 361 ASP A N   
2792 C CA  . ASP A 367 ? 0.89052 1.04547 0.96664 0.11452  -0.11138 -0.14810 361 ASP A CA  
2793 C C   . ASP A 367 ? 0.92089 1.09033 1.02029 0.12716  -0.11072 -0.15012 361 ASP A C   
2794 O O   . ASP A 367 ? 0.97738 1.19015 1.12611 0.12504  -0.10948 -0.16323 361 ASP A O   
2795 C CB  . ASP A 367 ? 0.77632 0.91916 0.85179 0.09239  -0.08735 -0.13894 361 ASP A CB  
2796 C CG  . ASP A 367 ? 0.95797 1.09158 1.01766 0.08252  -0.08696 -0.14123 361 ASP A CG  
2797 O OD1 . ASP A 367 ? 0.94066 1.07789 0.98924 0.09068  -0.10471 -0.15115 361 ASP A OD1 
2798 O OD2 . ASP A 367 ? 0.80263 0.92507 0.86003 0.06851  -0.07027 -0.13451 361 ASP A OD2 
2799 N N   . TRP A 368 ? 0.99025 1.12364 1.05443 0.13998  -0.11101 -0.13806 362 TRP A N   
2800 C CA  . TRP A 368 ? 0.91356 1.05374 0.99429 0.15482  -0.10993 -0.14172 362 TRP A CA  
2801 C C   . TRP A 368 ? 0.82661 1.00242 0.93771 0.17904  -0.13192 -0.15866 362 TRP A C   
2802 O O   . TRP A 368 ? 1.01039 1.22470 1.16479 0.18597  -0.12664 -0.17110 362 TRP A O   
2803 C CB  . TRP A 368 ? 0.99711 1.08159 1.02821 0.16325  -0.10997 -0.12582 362 TRP A CB  
2804 C CG  . TRP A 368 ? 0.99398 1.07569 1.03498 0.17898  -0.10807 -0.13071 362 TRP A CG  
2805 C CD1 . TRP A 368 ? 1.05641 1.12039 1.08436 0.20858  -0.12724 -0.13463 362 TRP A CD1 
2806 C CD2 . TRP A 368 ? 0.92394 1.01827 0.98608 0.16829  -0.08673 -0.13356 362 TRP A CD2 
2807 N NE1 . TRP A 368 ? 1.06870 1.13464 1.11035 0.21800  -0.11809 -0.14179 362 TRP A NE1 
2808 C CE2 . TRP A 368 ? 0.94072 1.02587 1.00159 0.19278  -0.09258 -0.14111 362 TRP A CE2 
2809 C CE3 . TRP A 368 ? 0.94171 1.05093 1.01971 0.14202  -0.06463 -0.13062 362 TRP A CE3 
2810 C CZ2 . TRP A 368 ? 0.97192 1.06445 1.04503 0.19099  -0.07516 -0.14703 362 TRP A CZ2 
2811 C CZ3 . TRP A 368 ? 1.01214 1.12706 1.10034 0.13926  -0.04878 -0.13407 362 TRP A CZ3 
2812 C CH2 . TRP A 368 ? 0.99028 1.09798 1.07518 0.16316  -0.05313 -0.14280 362 TRP A CH2 
2813 N N   . VAL A 369 ? 0.86493 1.03158 0.95425 0.19284  -0.15679 -0.16021 363 VAL A N   
2814 C CA  . VAL A 369 ? 0.94455 1.14492 1.06173 0.21875  -0.18345 -0.17665 363 VAL A CA  
2815 C C   . VAL A 369 ? 0.85339 1.10623 1.01497 0.20704  -0.19227 -0.19337 363 VAL A C   
2816 O O   . VAL A 369 ? 0.90569 1.18940 1.09018 0.22616  -0.21915 -0.20797 363 VAL A O   
2817 C CB  . VAL A 369 ? 0.78370 0.93635 0.84439 0.24526  -0.21117 -0.16788 363 VAL A CB  
2818 C CG1 . VAL A 369 ? 1.59503 1.77168 1.68274 0.28087  -0.23661 -0.18249 363 VAL A CG1 
2819 C CG2 . VAL A 369 ? 1.20546 1.29073 1.20691 0.24147  -0.19869 -0.14516 363 VAL A CG2 
2820 N N   . SER A 370 ? 0.84551 1.10710 1.01995 0.17631  -0.17261 -0.19219 364 SER A N   
2821 C CA  . SER A 370 ? 0.70450 1.00978 0.92117 0.16132  -0.18071 -0.20838 364 SER A CA  
2822 C C   . SER A 370 ? 0.79227 1.16457 1.08221 0.16251  -0.17981 -0.22566 364 SER A C   
2823 O O   . SER A 370 ? 0.80996 1.19549 1.11877 0.16839  -0.16296 -0.22439 364 SER A O   
2824 C CB  . SER A 370 ? 0.79731 1.08947 1.00992 0.12927  -0.15913 -0.20253 364 SER A CB  
2825 O OG  . SER A 370 ? 0.80238 1.13182 1.05749 0.11180  -0.16653 -0.21851 364 SER A OG  
2826 N N   . SER A 371 ? 0.57729 0.99442 0.90930 0.15633  -0.19808 -0.24334 365 SER A N   
2827 C CA  . SER A 371 ? 0.59997 1.09034 1.01002 0.15038  -0.19400 -0.26039 365 SER A CA  
2828 C C   . SER A 371 ? 0.58868 1.09251 1.02575 0.11610  -0.15820 -0.25500 365 SER A C   
2829 O O   . SER A 371 ? 0.89225 1.45105 1.38490 0.11066  -0.14345 -0.26373 365 SER A O   
2830 C CB  . SER A 371 ? 0.55017 1.08519 1.00071 0.14676  -0.22371 -0.28066 365 SER A CB  
2831 O OG  . SER A 371 ? 0.82324 1.34248 1.26737 0.11432  -0.22017 -0.28061 365 SER A OG  
2832 N N   . HIS A 372 ? 0.76786 1.22328 1.16554 0.09408  -0.14393 -0.24084 366 HIS A N   
2833 C CA  . HIS A 372 ? 0.69052 1.14612 1.10223 0.06294  -0.11305 -0.23260 366 HIS A CA  
2834 C C   . HIS A 372 ? 0.69545 1.12732 1.08196 0.06937  -0.08813 -0.21793 366 HIS A C   
2835 O O   . HIS A 372 ? 0.78224 1.20690 1.17006 0.04594  -0.06330 -0.20871 366 HIS A O   
2836 C CB  . HIS A 372 ? 0.61157 1.02416 0.99293 0.04042  -0.11250 -0.22578 366 HIS A CB  
2837 C CG  . HIS A 372 ? 0.70508 1.13019 1.10081 0.03454  -0.13901 -0.24161 366 HIS A CG  
2838 N ND1 . HIS A 372 ? 0.81104 1.29239 1.26932 0.01917  -0.14758 -0.25847 366 HIS A ND1 
2839 C CD2 . HIS A 372 ? 0.77672 1.16618 1.13139 0.04123  -0.15902 -0.24438 366 HIS A CD2 
2840 C CE1 . HIS A 372 ? 0.76590 1.24263 1.22073 0.01657  -0.17470 -0.27158 366 HIS A CE1 
2841 N NE2 . HIS A 372 ? 0.71355 1.13375 1.10311 0.03105  -0.18163 -0.26369 366 HIS A NE2 
2842 N N   . SER A 373 ? 0.82957 1.24436 1.18959 0.10021  -0.09628 -0.21551 367 SER A N   
2843 C CA  . SER A 373 ? 0.64032 1.02856 0.97376 0.10829  -0.07691 -0.20418 367 SER A CA  
2844 C C   . SER A 373 ? 0.81151 1.24003 1.17681 0.13413  -0.07856 -0.21752 367 SER A C   
2845 O O   . SER A 373 ? 0.85976 1.28390 1.21647 0.16472  -0.10240 -0.22362 367 SER A O   
2846 C CB  . SER A 373 ? 0.56334 0.88533 0.83145 0.12029  -0.08435 -0.18862 367 SER A CB  
2847 O OG  . SER A 373 ? 0.86244 1.15358 1.10500 0.09894  -0.08022 -0.17840 367 SER A OG  
2848 N N   . LYS A 374 ? 0.75614 1.22253 1.15556 0.12321  -0.05335 -0.22221 368 LYS A N   
2849 C CA  . LYS A 374 ? 0.72513 1.23711 1.15920 0.14770  -0.04910 -0.23761 368 LYS A CA  
2850 C C   . LYS A 374 ? 0.80444 1.28015 1.20059 0.15688  -0.02945 -0.22992 368 LYS A C   
2851 O O   . LYS A 374 ? 0.84205 1.28606 1.20949 0.13281  -0.00944 -0.21540 368 LYS A O   
2852 C CB  . LYS A 374 ? 0.53183 1.12403 1.03690 0.12826  -0.03260 -0.25173 368 LYS A CB  
2853 C CG  . LYS A 374 ? 0.71898 1.35292 1.26910 0.11859  -0.05509 -0.26312 368 LYS A CG  
2854 C CD  . LYS A 374 ? 0.96290 1.68732 1.59321 0.10483  -0.04131 -0.28052 368 LYS A CD  
2855 C CE  . LYS A 374 ? 0.99720 1.76447 1.67539 0.09640  -0.06905 -0.29444 368 LYS A CE  
2856 N NZ  . LYS A 374 ? 1.07660 1.93938 1.84094 0.07969  -0.05609 -0.31206 368 LYS A NZ  
2857 N N   . SER A 375 ? 0.93840 1.41602 1.33300 0.19323  -0.03795 -0.24073 369 SER A N   
2858 C CA  . SER A 375 ? 0.95483 1.39544 1.31218 0.20496  -0.02266 -0.23728 369 SER A CA  
2859 C C   . SER A 375 ? 1.02871 1.51187 1.41160 0.18642  0.01250  -0.24250 369 SER A C   
2860 O O   . SER A 375 ? 0.87465 1.43174 1.31693 0.18182  0.02347  -0.25710 369 SER A O   
2861 C CB  . SER A 375 ? 1.04273 1.47593 1.39566 0.25070  -0.04153 -0.25100 369 SER A CB  
2862 O OG  . SER A 375 ? 1.24872 1.62402 1.55939 0.26593  -0.07217 -0.24065 369 SER A OG  
2863 N N   . LEU A 376 ? 1.07371 1.51066 1.41041 0.17436  0.03004  -0.23014 370 LEU A N   
2864 C CA  . LEU A 376 ? 0.99973 1.46593 1.34572 0.15527  0.06362  -0.23176 370 LEU A CA  
2865 C C   . LEU A 376 ? 1.01031 1.52735 1.38651 0.18385  0.07611  -0.25512 370 LEU A C   
2866 O O   . LEU A 376 ? 1.29815 1.78571 1.64961 0.21839  0.06533  -0.26421 370 LEU A O   
2867 C CB  . LEU A 376 ? 1.10337 1.50393 1.38734 0.14148  0.07369  -0.21483 370 LEU A CB  
2868 C CG  . LEU A 376 ? 1.19868 1.61759 1.47602 0.12610  0.10661  -0.21576 370 LEU A CG  
2869 C CD1 . LEU A 376 ? 1.11245 1.57732 1.42597 0.09019  0.12514  -0.20967 370 LEU A CD1 
2870 C CD2 . LEU A 376 ? 1.00152 1.35173 1.21441 0.11788  0.10922  -0.20112 370 LEU A CD2 
2871 N N   . LYS A 377 ? 1.01446 1.60788 1.44481 0.16916  0.09927  -0.26543 371 LYS A N   
2872 C CA  . LYS A 377 ? 1.21917 1.87478 1.68507 0.19292  0.11848  -0.28911 371 LYS A CA  
2873 C C   . LYS A 377 ? 1.25977 1.94758 1.72795 0.16074  0.15996  -0.28501 371 LYS A C   
2874 O O   . LYS A 377 ? 1.16099 1.86852 1.64838 0.12048  0.17107  -0.27201 371 LYS A O   
2875 C CB  . LYS A 377 ? 1.08489 1.82109 1.62843 0.21046  0.10529  -0.30980 371 LYS A CB  
2876 C CG  . LYS A 377 ? 1.30708 2.01132 1.84468 0.24439  0.06192  -0.31353 371 LYS A CG  
2877 C CD  . LYS A 377 ? 1.46606 2.11261 1.95443 0.28661  0.05051  -0.31979 371 LYS A CD  
2878 C CE  . LYS A 377 ? 1.46834 2.06841 1.93768 0.31575  0.00705  -0.31754 371 LYS A CE  
2879 N NZ  . LYS A 377 ? 1.44839 1.98067 1.86465 0.35351  -0.00594 -0.32122 371 LYS A NZ  
2880 N N   . ILE A 378 ? 1.32410 2.01157 1.76724 0.17832  0.18198  -0.29577 372 ILE A N   
2881 C CA  . ILE A 378 ? 1.45759 2.17082 1.89100 0.15037  0.22306  -0.29163 372 ILE A CA  
2882 C C   . ILE A 378 ? 1.60701 2.39687 2.07865 0.17624  0.24984  -0.31996 372 ILE A C   
2883 O O   . ILE A 378 ? 1.57143 2.35401 2.03683 0.22201  0.23850  -0.34058 372 ILE A O   
2884 C CB  . ILE A 378 ? 1.40054 2.02867 1.74876 0.14046  0.22756  -0.27415 372 ILE A CB  
2885 C CG1 . ILE A 378 ? 1.38957 1.94939 1.70674 0.11813  0.20129  -0.24839 372 ILE A CG1 
2886 C CG2 . ILE A 378 ? 1.43483 2.08482 1.76482 0.11086  0.26838  -0.26762 372 ILE A CG2 
2887 C CD1 . ILE A 378 ? 1.49939 1.97735 1.73998 0.11333  0.19782  -0.23334 372 ILE A CD1 
2888 O OXT . ILE A 378 ? 1.60315 2.46383 2.11262 0.15226  0.28411  -0.32332 372 ILE A OXT 
# 
